data_7HOV
# 
_entry.id   7HOV 
# 
_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   7HOV         pdb_00007hov 10.2210/pdb7hov/pdb 
WWPDB D_1001407745 ?            ?                   
# 
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                        7HOV 
_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    4  ?                           ?    ? ? 
4 non-polymer syn 
'3-chloro-5-[({2-[(dimethylamino)methyl]-1,3-thiazol-4-yl}methyl)amino]-N-(1-hydroxy-2-methylpropan-2-yl)benzamide' 396.935   1  ? 
?    ? ? 
5 non-polymer syn 'SULFATE ION' 96.063    1  ?                           ?    ? ? 
6 water       nat water 18.015    96 ?                           ?    ? ? 
# 
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 '3-chloro-5-[({2-[(dimethylamino)methyl]-1,3-thiazol-4-yl}methyl)amino]-N-(1-hydroxy-2-methylpropan-2-yl)benzamide' A1BGM 
5 'SULFATE ION'                                                                                                       SO4   
6 water                                                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BGM non-polymer         . 
'3-chloro-5-[({2-[(dimethylamino)methyl]-1,3-thiazol-4-yl}methyl)amino]-N-(1-hydroxy-2-methylpropan-2-yl)benzamide' ? 
'C18 H25 Cl N4 O2 S' 396.935 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'          78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ? 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'         105.093 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'            96.063  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BGM 1  204 301 A1BGM LIG B . 
G 3 DMS   1  205 302 DMS   DMS B . 
H 5 SO4   1  206 303 SO4   SO4 B . 
I 6 HOH   1  101 127 HOH   HOH A . 
I 6 HOH   2  102 34  HOH   HOH A . 
I 6 HOH   3  103 48  HOH   HOH A . 
I 6 HOH   4  104 65  HOH   HOH A . 
I 6 HOH   5  105 98  HOH   HOH A . 
I 6 HOH   6  106 105 HOH   HOH A . 
I 6 HOH   7  107 50  HOH   HOH A . 
I 6 HOH   8  108 20  HOH   HOH A . 
I 6 HOH   9  109 121 HOH   HOH A . 
I 6 HOH   10 110 36  HOH   HOH A . 
I 6 HOH   11 111 110 HOH   HOH A . 
I 6 HOH   12 112 125 HOH   HOH A . 
I 6 HOH   13 113 28  HOH   HOH A . 
I 6 HOH   14 114 118 HOH   HOH A . 
I 6 HOH   15 115 49  HOH   HOH A . 
I 6 HOH   16 116 119 HOH   HOH A . 
I 6 HOH   17 117 40  HOH   HOH A . 
I 6 HOH   18 118 77  HOH   HOH A . 
I 6 HOH   19 119 29  HOH   HOH A . 
I 6 HOH   20 120 120 HOH   HOH A . 
I 6 HOH   21 121 27  HOH   HOH A . 
I 6 HOH   22 122 70  HOH   HOH A . 
J 6 HOH   1  301 57  HOH   HOH B . 
J 6 HOH   2  302 51  HOH   HOH B . 
J 6 HOH   3  303 66  HOH   HOH B . 
J 6 HOH   4  304 11  HOH   HOH B . 
J 6 HOH   5  305 89  HOH   HOH B . 
J 6 HOH   6  306 81  HOH   HOH B . 
J 6 HOH   7  307 5   HOH   HOH B . 
J 6 HOH   8  308 92  HOH   HOH B . 
J 6 HOH   9  309 4   HOH   HOH B . 
J 6 HOH   10 310 42  HOH   HOH B . 
J 6 HOH   11 311 60  HOH   HOH B . 
J 6 HOH   12 312 90  HOH   HOH B . 
J 6 HOH   13 313 46  HOH   HOH B . 
J 6 HOH   14 314 9   HOH   HOH B . 
J 6 HOH   15 315 58  HOH   HOH B . 
J 6 HOH   16 316 1   HOH   HOH B . 
J 6 HOH   17 317 68  HOH   HOH B . 
J 6 HOH   18 318 14  HOH   HOH B . 
J 6 HOH   19 319 24  HOH   HOH B . 
J 6 HOH   20 320 117 HOH   HOH B . 
J 6 HOH   21 321 32  HOH   HOH B . 
J 6 HOH   22 322 126 HOH   HOH B . 
J 6 HOH   23 323 31  HOH   HOH B . 
J 6 HOH   24 324 56  HOH   HOH B . 
J 6 HOH   25 325 23  HOH   HOH B . 
J 6 HOH   26 326 30  HOH   HOH B . 
J 6 HOH   27 327 35  HOH   HOH B . 
J 6 HOH   28 328 107 HOH   HOH B . 
J 6 HOH   29 329 39  HOH   HOH B . 
J 6 HOH   30 330 43  HOH   HOH B . 
J 6 HOH   31 331 16  HOH   HOH B . 
J 6 HOH   32 332 21  HOH   HOH B . 
J 6 HOH   33 333 83  HOH   HOH B . 
J 6 HOH   34 334 115 HOH   HOH B . 
J 6 HOH   35 335 102 HOH   HOH B . 
J 6 HOH   36 336 116 HOH   HOH B . 
J 6 HOH   37 337 63  HOH   HOH B . 
J 6 HOH   38 338 106 HOH   HOH B . 
J 6 HOH   39 339 62  HOH   HOH B . 
J 6 HOH   40 340 2   HOH   HOH B . 
J 6 HOH   41 341 10  HOH   HOH B . 
J 6 HOH   42 342 13  HOH   HOH B . 
J 6 HOH   43 343 82  HOH   HOH B . 
J 6 HOH   44 344 3   HOH   HOH B . 
J 6 HOH   45 345 128 HOH   HOH B . 
J 6 HOH   46 346 108 HOH   HOH B . 
J 6 HOH   47 347 103 HOH   HOH B . 
J 6 HOH   48 348 72  HOH   HOH B . 
J 6 HOH   49 349 61  HOH   HOH B . 
J 6 HOH   50 350 54  HOH   HOH B . 
J 6 HOH   51 351 69  HOH   HOH B . 
J 6 HOH   52 352 67  HOH   HOH B . 
J 6 HOH   53 353 124 HOH   HOH B . 
J 6 HOH   54 354 12  HOH   HOH B . 
J 6 HOH   55 355 73  HOH   HOH B . 
J 6 HOH   56 356 18  HOH   HOH B . 
J 6 HOH   57 357 122 HOH   HOH B . 
J 6 HOH   58 358 79  HOH   HOH B . 
J 6 HOH   59 359 64  HOH   HOH B . 
J 6 HOH   60 360 80  HOH   HOH B . 
J 6 HOH   61 361 94  HOH   HOH B . 
J 6 HOH   62 362 112 HOH   HOH B . 
J 6 HOH   63 363 87  HOH   HOH B . 
J 6 HOH   64 364 17  HOH   HOH B . 
J 6 HOH   65 365 26  HOH   HOH B . 
J 6 HOH   66 366 123 HOH   HOH B . 
J 6 HOH   67 367 100 HOH   HOH B . 
J 6 HOH   68 368 129 HOH   HOH B . 
J 6 HOH   69 369 75  HOH   HOH B . 
J 6 HOH   70 370 59  HOH   HOH B . 
J 6 HOH   71 371 45  HOH   HOH B . 
J 6 HOH   72 372 85  HOH   HOH B . 
J 6 HOH   73 373 109 HOH   HOH B . 
J 6 HOH   74 374 44  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HOV 
_cell.length_a           42.508 
_cell.length_b           42.508 
_cell.length_c           216.455 
_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                         7HOV 
_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          7HOV 
_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   41.67 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-09-19 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HOV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.46 
_reflns.d_resolution_high            1.69 
_reflns.number_obs                   23551 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.233 
_reflns.pdbx_netI_over_sigmaI        6.4 
_reflns.pdbx_redundancy              25.5 
_reflns.pdbx_Rrim_I_all              0.237 
_reflns.pdbx_Rpim_I_all              0.047 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     600934 
_reflns.pdbx_chi_squared             0.20 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.69 
_reflns_shell.d_res_low                   1.72 
_reflns_shell.number_measured_all         32383 
_reflns_shell.number_unique_obs           1229 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.06 
_reflns_shell.pdbx_redundancy             26.3 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             16.365 
_reflns_shell.pdbx_Rpim_I_all             3.176 
_reflns_shell.pdbx_CC_half                0.508 
_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                                 7HOV 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     18908 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.11 
_refine.ls_d_res_high                            1.69 
_refine.ls_percent_reflns_obs                    84.89 
_refine.ls_R_factor_obs                          0.23125 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22889 
_refine.ls_R_factor_R_free                       0.27565 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  997 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.B_iso_mean                               53.248 
_refine.aniso_B[1][1]                            2.52 
_refine.aniso_B[2][2]                            2.52 
_refine.aniso_B[3][3]                            -5.04 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.178 
_refine.pdbx_overall_ESU_R_Free                  0.163 
_refine.overall_SU_ML                            0.254 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             19.676 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         47 
_refine_hist.number_atoms_solvent             96 
_refine_hist.number_atoms_total               1619 
_refine_hist.d_res_high                       1.69 
_refine_hist.d_res_low                        54.11 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.011  0.014  ? 2199 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.015  ? 1827 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.629  1.637  ? 2672 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.238  1.583  ? 4206 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.302  5.000  ? 256  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.737 21.839 ? 87   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.481 15.000 ? 301  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       18.912 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.066  0.200  ? 241  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2289 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 443  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.603  2.528  ? 1077 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.617  2.464  ? 1053 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.910  3.651  ? 1236 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.911  3.656  ? 1237 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.726  2.763  ? 1122 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.728  2.719  ? 1110 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              3.073  3.942  ? 1425 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.584  29.082 ? 2136 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         8.485  28.499 ? 2112 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.690 
_refine_ls_shell.d_res_low                        1.734 
_refine_ls_shell.number_reflns_R_work             151 
_refine_ls_shell.R_factor_R_work                  0.606 
_refine_ls_shell.percent_reflns_obs               9.28 
_refine_ls_shell.R_factor_R_free                  0.856 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             4 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HOV 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014707-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOV 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HOV A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOV 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 7HOV SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOV MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOV MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOV 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)' 4780  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  10670 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'crystal symmetry operation' 
_pdbx_struct_oper_list.name                 8_554 
_pdbx_struct_oper_list.symmetry_operation   -y,-x,-z-1/4 
_pdbx_struct_oper_list.matrix[1][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         -1.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         -1.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         0.0000000000 
_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]            -54.1137500000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.767 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N 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 PHE B 37  ? N PHE B 46  O TYR B 70  ? O TYR B 79  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HOV 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B LEU 30 ? ? O  B HOH 301 ? ? 2.11 
2 1 OD2 B ASP 90 ? ? OG B SER 93  ? ? 2.18 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ALA 
_pdbx_validate_rmsd_bond.auth_seq_id_1             65 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            ALA 
_pdbx_validate_rmsd_bond.auth_seq_id_2             65 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.435 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.206 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP B 20  ? ? -46.07  153.08 
2 1 ASP B 71  ? ? -161.01 112.25 
3 1 CYS B 80  ? A 90.44   -25.29 
4 1 CYS B 80  ? B 90.44   -25.29 
5 1 LEU B 92  ? ? -125.91 -58.62 
6 1 LYS B 157 ? C -52.84  -6.05  
7 1 LYS B 157 ? D -52.83  -5.97  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ALA 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              65 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.98 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 329 ? J HOH . 
2 1 B HOH 371 ? J HOH . 
3 1 B HOH 374 ? J HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.2991 -2.1421 -19.2648 0.2942 0.4015 0.1396 0.1909 0.1194 0.1422 2.2503 2.5794 1.2936 -0.4767 
-0.7560 0.2384  0.6413 0.2891 0.3749 -0.3812 -0.6082 -0.3319 -0.2663 0.3208 -0.0331 
'X-RAY DIFFRACTION' 2 ? refined -18.2830 0.5266  -15.8858 0.3173 0.3015 0.3682 0.1895 0.1004 0.0013 0.6137 0.4532 1.0704 -0.4869 
0.5209  -0.5036 0.3249 0.2116 0.1163 -0.2508 -0.2609 0.0204  0.1835  0.1943 -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 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 303 ? ? ? ? 
# 
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 
A1BGM N1   N  N N 1   
A1BGM N3   N  N N 2   
A1BGM C4   C  Y N 3   
A1BGM C5   C  Y N 4   
A1BGM C6   C  N N 5   
A1BGM C7   C  Y N 6   
A1BGM C8   C  Y N 7   
A1BGM C10  C  Y N 8   
A1BGM C13  C  N N 9   
A1BGM C15  C  N N 10  
A1BGM C17  C  Y N 11  
A1BGM C1   C  N N 12  
A1BGM C2   C  N N 13  
A1BGM C3   C  N N 14  
A1BGM N2   N  Y N 15  
A1BGM C9   C  Y N 16  
A1BGM CL1  CL N N 17  
A1BGM C11  C  Y N 18  
A1BGM C12  C  N N 19  
A1BGM O1   O  N N 20  
A1BGM N4   N  N N 21  
A1BGM C14  C  N N 22  
A1BGM C16  C  N N 23  
A1BGM O2   O  N N 24  
A1BGM C18  C  Y N 25  
A1BGM S1   S  Y N 26  
A1BGM H2   H  N N 27  
A1BGM H3   H  N N 28  
A1BGM H4   H  N N 29  
A1BGM H5   H  N N 30  
A1BGM H6   H  N N 31  
A1BGM H7   H  N N 32  
A1BGM H8   H  N N 33  
A1BGM H9   H  N N 34  
A1BGM H10  H  N N 35  
A1BGM H11  H  N N 36  
A1BGM H12  H  N N 37  
A1BGM H13  H  N N 38  
A1BGM H14  H  N N 39  
A1BGM H15  H  N N 40  
A1BGM H16  H  N N 41  
A1BGM H17  H  N N 42  
A1BGM H18  H  N N 43  
A1BGM H19  H  N N 44  
A1BGM H20  H  N N 45  
A1BGM H21  H  N N 46  
A1BGM H22  H  N N 47  
A1BGM H23  H  N N 48  
A1BGM H24  H  N N 49  
A1BGM H25  H  N N 50  
A1BGM H26  H  N N 51  
ALA   N    N  N N 52  
ALA   CA   C  N S 53  
ALA   C    C  N N 54  
ALA   O    O  N N 55  
ALA   CB   C  N N 56  
ALA   OXT  O  N N 57  
ALA   H    H  N N 58  
ALA   H2   H  N N 59  
ALA   HA   H  N N 60  
ALA   HB1  H  N N 61  
ALA   HB2  H  N N 62  
ALA   HB3  H  N N 63  
ALA   HXT  H  N N 64  
ARG   N    N  N N 65  
ARG   CA   C  N S 66  
ARG   C    C  N N 67  
ARG   O    O  N N 68  
ARG   CB   C  N N 69  
ARG   CG   C  N N 70  
ARG   CD   C  N N 71  
ARG   NE   N  N N 72  
ARG   CZ   C  N N 73  
ARG   NH1  N  N N 74  
ARG   NH2  N  N N 75  
ARG   OXT  O  N N 76  
ARG   H    H  N N 77  
ARG   H2   H  N N 78  
ARG   HA   H  N N 79  
ARG   HB2  H  N N 80  
ARG   HB3  H  N N 81  
ARG   HG2  H  N N 82  
ARG   HG3  H  N N 83  
ARG   HD2  H  N N 84  
ARG   HD3  H  N N 85  
ARG   HE   H  N N 86  
ARG   HH11 H  N N 87  
ARG   HH12 H  N N 88  
ARG   HH21 H  N N 89  
ARG   HH22 H  N N 90  
ARG   HXT  H  N N 91  
ASN   N    N  N N 92  
ASN   CA   C  N S 93  
ASN   C    C  N N 94  
ASN   O    O  N N 95  
ASN   CB   C  N N 96  
ASN   CG   C  N N 97  
ASN   OD1  O  N N 98  
ASN   ND2  N  N N 99  
ASN   OXT  O  N N 100 
ASN   H    H  N N 101 
ASN   H2   H  N N 102 
ASN   HA   H  N N 103 
ASN   HB2  H  N N 104 
ASN   HB3  H  N N 105 
ASN   HD21 H  N N 106 
ASN   HD22 H  N N 107 
ASN   HXT  H  N N 108 
ASP   N    N  N N 109 
ASP   CA   C  N S 110 
ASP   C    C  N N 111 
ASP   O    O  N N 112 
ASP   CB   C  N N 113 
ASP   CG   C  N N 114 
ASP   OD1  O  N N 115 
ASP   OD2  O  N N 116 
ASP   OXT  O  N N 117 
ASP   H    H  N N 118 
ASP   H2   H  N N 119 
ASP   HA   H  N N 120 
ASP   HB2  H  N N 121 
ASP   HB3  H  N N 122 
ASP   HD2  H  N N 123 
ASP   HXT  H  N N 124 
CYS   N    N  N N 125 
CYS   CA   C  N R 126 
CYS   C    C  N N 127 
CYS   O    O  N N 128 
CYS   CB   C  N N 129 
CYS   SG   S  N N 130 
CYS   OXT  O  N N 131 
CYS   H    H  N N 132 
CYS   H2   H  N N 133 
CYS   HA   H  N N 134 
CYS   HB2  H  N N 135 
CYS   HB3  H  N N 136 
CYS   HG   H  N N 137 
CYS   HXT  H  N N 138 
DMS   S    S  N N 139 
DMS   O    O  N N 140 
DMS   C1   C  N N 141 
DMS   C2   C  N N 142 
DMS   H11  H  N N 143 
DMS   H12  H  N N 144 
DMS   H13  H  N N 145 
DMS   H21  H  N N 146 
DMS   H22  H  N N 147 
DMS   H23  H  N N 148 
GLN   N    N  N N 149 
GLN   CA   C  N S 150 
GLN   C    C  N N 151 
GLN   O    O  N N 152 
GLN   CB   C  N N 153 
GLN   CG   C  N N 154 
GLN   CD   C  N N 155 
GLN   OE1  O  N N 156 
GLN   NE2  N  N N 157 
GLN   OXT  O  N N 158 
GLN   H    H  N N 159 
GLN   H2   H  N N 160 
GLN   HA   H  N N 161 
GLN   HB2  H  N N 162 
GLN   HB3  H  N N 163 
GLN   HG2  H  N N 164 
GLN   HG3  H  N N 165 
GLN   HE21 H  N N 166 
GLN   HE22 H  N N 167 
GLN   HXT  H  N N 168 
GLU   N    N  N N 169 
GLU   CA   C  N S 170 
GLU   C    C  N N 171 
GLU   O    O  N N 172 
GLU   CB   C  N N 173 
GLU   CG   C  N N 174 
GLU   CD   C  N N 175 
GLU   OE1  O  N N 176 
GLU   OE2  O  N N 177 
GLU   OXT  O  N N 178 
GLU   H    H  N N 179 
GLU   H2   H  N N 180 
GLU   HA   H  N N 181 
GLU   HB2  H  N N 182 
GLU   HB3  H  N N 183 
GLU   HG2  H  N N 184 
GLU   HG3  H  N N 185 
GLU   HE2  H  N N 186 
GLU   HXT  H  N N 187 
GLY   N    N  N N 188 
GLY   CA   C  N N 189 
GLY   C    C  N N 190 
GLY   O    O  N N 191 
GLY   OXT  O  N N 192 
GLY   H    H  N N 193 
GLY   H2   H  N N 194 
GLY   HA2  H  N N 195 
GLY   HA3  H  N N 196 
GLY   HXT  H  N N 197 
HIS   N    N  N N 198 
HIS   CA   C  N S 199 
HIS   C    C  N N 200 
HIS   O    O  N N 201 
HIS   CB   C  N N 202 
HIS   CG   C  Y N 203 
HIS   ND1  N  Y N 204 
HIS   CD2  C  Y N 205 
HIS   CE1  C  Y N 206 
HIS   NE2  N  Y N 207 
HIS   OXT  O  N N 208 
HIS   H    H  N N 209 
HIS   H2   H  N N 210 
HIS   HA   H  N N 211 
HIS   HB2  H  N N 212 
HIS   HB3  H  N N 213 
HIS   HD1  H  N N 214 
HIS   HD2  H  N N 215 
HIS   HE1  H  N N 216 
HIS   HE2  H  N N 217 
HIS   HXT  H  N N 218 
HOH   O    O  N N 219 
HOH   H1   H  N N 220 
HOH   H2   H  N N 221 
ILE   N    N  N N 222 
ILE   CA   C  N S 223 
ILE   C    C  N N 224 
ILE   O    O  N N 225 
ILE   CB   C  N S 226 
ILE   CG1  C  N N 227 
ILE   CG2  C  N N 228 
ILE   CD1  C  N N 229 
ILE   OXT  O  N N 230 
ILE   H    H  N N 231 
ILE   H2   H  N N 232 
ILE   HA   H  N N 233 
ILE   HB   H  N N 234 
ILE   HG12 H  N N 235 
ILE   HG13 H  N N 236 
ILE   HG21 H  N N 237 
ILE   HG22 H  N N 238 
ILE   HG23 H  N N 239 
ILE   HD11 H  N N 240 
ILE   HD12 H  N N 241 
ILE   HD13 H  N N 242 
ILE   HXT  H  N N 243 
LEU   N    N  N N 244 
LEU   CA   C  N S 245 
LEU   C    C  N N 246 
LEU   O    O  N N 247 
LEU   CB   C  N N 248 
LEU   CG   C  N N 249 
LEU   CD1  C  N N 250 
LEU   CD2  C  N N 251 
LEU   OXT  O  N N 252 
LEU   H    H  N N 253 
LEU   H2   H  N N 254 
LEU   HA   H  N N 255 
LEU   HB2  H  N N 256 
LEU   HB3  H  N N 257 
LEU   HG   H  N N 258 
LEU   HD11 H  N N 259 
LEU   HD12 H  N N 260 
LEU   HD13 H  N N 261 
LEU   HD21 H  N N 262 
LEU   HD22 H  N N 263 
LEU   HD23 H  N N 264 
LEU   HXT  H  N N 265 
LYS   N    N  N N 266 
LYS   CA   C  N S 267 
LYS   C    C  N N 268 
LYS   O    O  N N 269 
LYS   CB   C  N N 270 
LYS   CG   C  N N 271 
LYS   CD   C  N N 272 
LYS   CE   C  N N 273 
LYS   NZ   N  N N 274 
LYS   OXT  O  N N 275 
LYS   H    H  N N 276 
LYS   H2   H  N N 277 
LYS   HA   H  N N 278 
LYS   HB2  H  N N 279 
LYS   HB3  H  N N 280 
LYS   HG2  H  N N 281 
LYS   HG3  H  N N 282 
LYS   HD2  H  N N 283 
LYS   HD3  H  N N 284 
LYS   HE2  H  N N 285 
LYS   HE3  H  N N 286 
LYS   HZ1  H  N N 287 
LYS   HZ2  H  N N 288 
LYS   HZ3  H  N N 289 
LYS   HXT  H  N N 290 
MET   N    N  N N 291 
MET   CA   C  N S 292 
MET   C    C  N N 293 
MET   O    O  N N 294 
MET   CB   C  N N 295 
MET   CG   C  N N 296 
MET   SD   S  N N 297 
MET   CE   C  N N 298 
MET   OXT  O  N N 299 
MET   H    H  N N 300 
MET   H2   H  N N 301 
MET   HA   H  N N 302 
MET   HB2  H  N N 303 
MET   HB3  H  N N 304 
MET   HG2  H  N N 305 
MET   HG3  H  N N 306 
MET   HE1  H  N N 307 
MET   HE2  H  N N 308 
MET   HE3  H  N N 309 
MET   HXT  H  N N 310 
PHE   N    N  N N 311 
PHE   CA   C  N S 312 
PHE   C    C  N N 313 
PHE   O    O  N N 314 
PHE   CB   C  N N 315 
PHE   CG   C  Y N 316 
PHE   CD1  C  Y N 317 
PHE   CD2  C  Y N 318 
PHE   CE1  C  Y N 319 
PHE   CE2  C  Y N 320 
PHE   CZ   C  Y N 321 
PHE   OXT  O  N N 322 
PHE   H    H  N N 323 
PHE   H2   H  N N 324 
PHE   HA   H  N N 325 
PHE   HB2  H  N N 326 
PHE   HB3  H  N N 327 
PHE   HD1  H  N N 328 
PHE   HD2  H  N N 329 
PHE   HE1  H  N N 330 
PHE   HE2  H  N N 331 
PHE   HZ   H  N N 332 
PHE   HXT  H  N N 333 
PRO   N    N  N N 334 
PRO   CA   C  N S 335 
PRO   C    C  N N 336 
PRO   O    O  N N 337 
PRO   CB   C  N N 338 
PRO   CG   C  N N 339 
PRO   CD   C  N N 340 
PRO   OXT  O  N N 341 
PRO   H    H  N N 342 
PRO   HA   H  N N 343 
PRO   HB2  H  N N 344 
PRO   HB3  H  N N 345 
PRO   HG2  H  N N 346 
PRO   HG3  H  N N 347 
PRO   HD2  H  N N 348 
PRO   HD3  H  N N 349 
PRO   HXT  H  N N 350 
SER   N    N  N N 351 
SER   CA   C  N S 352 
SER   C    C  N N 353 
SER   O    O  N N 354 
SER   CB   C  N N 355 
SER   OG   O  N N 356 
SER   OXT  O  N N 357 
SER   H    H  N N 358 
SER   H2   H  N N 359 
SER   HA   H  N N 360 
SER   HB2  H  N N 361 
SER   HB3  H  N N 362 
SER   HG   H  N N 363 
SER   HXT  H  N N 364 
SO4   S    S  N N 365 
SO4   O1   O  N N 366 
SO4   O2   O  N N 367 
SO4   O3   O  N N 368 
SO4   O4   O  N N 369 
THR   N    N  N N 370 
THR   CA   C  N S 371 
THR   C    C  N N 372 
THR   O    O  N N 373 
THR   CB   C  N R 374 
THR   OG1  O  N N 375 
THR   CG2  C  N N 376 
THR   OXT  O  N N 377 
THR   H    H  N N 378 
THR   H2   H  N N 379 
THR   HA   H  N N 380 
THR   HB   H  N N 381 
THR   HG1  H  N N 382 
THR   HG21 H  N N 383 
THR   HG22 H  N N 384 
THR   HG23 H  N N 385 
THR   HXT  H  N N 386 
TRP   N    N  N N 387 
TRP   CA   C  N S 388 
TRP   C    C  N N 389 
TRP   O    O  N N 390 
TRP   CB   C  N N 391 
TRP   CG   C  Y N 392 
TRP   CD1  C  Y N 393 
TRP   CD2  C  Y N 394 
TRP   NE1  N  Y N 395 
TRP   CE2  C  Y N 396 
TRP   CE3  C  Y N 397 
TRP   CZ2  C  Y N 398 
TRP   CZ3  C  Y N 399 
TRP   CH2  C  Y N 400 
TRP   OXT  O  N N 401 
TRP   H    H  N N 402 
TRP   H2   H  N N 403 
TRP   HA   H  N N 404 
TRP   HB2  H  N N 405 
TRP   HB3  H  N N 406 
TRP   HD1  H  N N 407 
TRP   HE1  H  N N 408 
TRP   HE3  H  N N 409 
TRP   HZ2  H  N N 410 
TRP   HZ3  H  N N 411 
TRP   HH2  H  N N 412 
TRP   HXT  H  N N 413 
TYR   N    N  N N 414 
TYR   CA   C  N S 415 
TYR   C    C  N N 416 
TYR   O    O  N N 417 
TYR   CB   C  N N 418 
TYR   CG   C  Y N 419 
TYR   CD1  C  Y N 420 
TYR   CD2  C  Y N 421 
TYR   CE1  C  Y N 422 
TYR   CE2  C  Y N 423 
TYR   CZ   C  Y N 424 
TYR   OH   O  N N 425 
TYR   OXT  O  N N 426 
TYR   H    H  N N 427 
TYR   H2   H  N N 428 
TYR   HA   H  N N 429 
TYR   HB2  H  N N 430 
TYR   HB3  H  N N 431 
TYR   HD1  H  N N 432 
TYR   HD2  H  N N 433 
TYR   HE1  H  N N 434 
TYR   HE2  H  N N 435 
TYR   HH   H  N N 436 
TYR   HXT  H  N N 437 
VAL   N    N  N N 438 
VAL   CA   C  N S 439 
VAL   C    C  N N 440 
VAL   O    O  N N 441 
VAL   CB   C  N N 442 
VAL   CG1  C  N N 443 
VAL   CG2  C  N N 444 
VAL   OXT  O  N N 445 
VAL   H    H  N N 446 
VAL   H2   H  N N 447 
VAL   HA   H  N N 448 
VAL   HB   H  N N 449 
VAL   HG11 H  N N 450 
VAL   HG12 H  N N 451 
VAL   HG13 H  N N 452 
VAL   HG21 H  N N 453 
VAL   HG22 H  N N 454 
VAL   HG23 H  N N 455 
VAL   HXT  H  N N 456 
# 
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 
A1BGM C14 C13  sing N N 1   
A1BGM O2  C16  sing N N 2   
A1BGM C13 C16  sing N N 3   
A1BGM C13 C15  sing N N 4   
A1BGM C13 N4   sing N N 5   
A1BGM N4  C12  sing N N 6   
A1BGM CL1 C9   sing N N 7   
A1BGM C12 O1   doub N N 8   
A1BGM C12 C11  sing N N 9   
A1BGM C10 C11  doub Y N 10  
A1BGM C10 C9   sing Y N 11  
A1BGM C11 C17  sing Y N 12  
A1BGM C9  C8   doub Y N 13  
A1BGM C17 C7   doub Y N 14  
A1BGM C8  C7   sing Y N 15  
A1BGM C7  N3   sing N N 16  
A1BGM N3  C6   sing N N 17  
A1BGM C6  C5   sing N N 18  
A1BGM C5  C18  doub Y N 19  
A1BGM C5  N2   sing Y N 20  
A1BGM C18 S1   sing Y N 21  
A1BGM N2  C4   doub Y N 22  
A1BGM S1  C4   sing Y N 23  
A1BGM C4  C3   sing N N 24  
A1BGM C2  N1   sing N N 25  
A1BGM N1  C3   sing N N 26  
A1BGM N1  C1   sing N N 27  
A1BGM N3  H2   sing N N 28  
A1BGM C6  H3   sing N N 29  
A1BGM C6  H4   sing N N 30  
A1BGM C8  H5   sing N N 31  
A1BGM C10 H6   sing N N 32  
A1BGM C15 H7   sing N N 33  
A1BGM C15 H8   sing N N 34  
A1BGM C15 H9   sing N N 35  
A1BGM C17 H10  sing N N 36  
A1BGM C1  H11  sing N N 37  
A1BGM C1  H12  sing N N 38  
A1BGM C1  H13  sing N N 39  
A1BGM C2  H14  sing N N 40  
A1BGM C2  H15  sing N N 41  
A1BGM C2  H16  sing N N 42  
A1BGM C3  H17  sing N N 43  
A1BGM C3  H18  sing N N 44  
A1BGM N4  H19  sing N N 45  
A1BGM C14 H20  sing N N 46  
A1BGM C14 H21  sing N N 47  
A1BGM C14 H22  sing N N 48  
A1BGM C16 H23  sing N N 49  
A1BGM C16 H24  sing N N 50  
A1BGM O2  H25  sing N N 51  
A1BGM C18 H26  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
DMS   S   O    doub N N 135 
DMS   S   C1   sing N N 136 
DMS   S   C2   sing N N 137 
DMS   C1  H11  sing N N 138 
DMS   C1  H12  sing N N 139 
DMS   C1  H13  sing N N 140 
DMS   C2  H21  sing N N 141 
DMS   C2  H22  sing N N 142 
DMS   C2  H23  sing N N 143 
GLN   N   CA   sing N N 144 
GLN   N   H    sing N N 145 
GLN   N   H2   sing N N 146 
GLN   CA  C    sing N N 147 
GLN   CA  CB   sing N N 148 
GLN   CA  HA   sing N N 149 
GLN   C   O    doub N N 150 
GLN   C   OXT  sing N N 151 
GLN   CB  CG   sing N N 152 
GLN   CB  HB2  sing N N 153 
GLN   CB  HB3  sing N N 154 
GLN   CG  CD   sing N N 155 
GLN   CG  HG2  sing N N 156 
GLN   CG  HG3  sing N N 157 
GLN   CD  OE1  doub N N 158 
GLN   CD  NE2  sing N N 159 
GLN   NE2 HE21 sing N N 160 
GLN   NE2 HE22 sing N N 161 
GLN   OXT HXT  sing N N 162 
GLU   N   CA   sing N N 163 
GLU   N   H    sing N N 164 
GLU   N   H2   sing N N 165 
GLU   CA  C    sing N N 166 
GLU   CA  CB   sing N N 167 
GLU   CA  HA   sing N N 168 
GLU   C   O    doub N N 169 
GLU   C   OXT  sing N N 170 
GLU   CB  CG   sing N N 171 
GLU   CB  HB2  sing N N 172 
GLU   CB  HB3  sing N N 173 
GLU   CG  CD   sing N N 174 
GLU   CG  HG2  sing N N 175 
GLU   CG  HG3  sing N N 176 
GLU   CD  OE1  doub N N 177 
GLU   CD  OE2  sing N N 178 
GLU   OE2 HE2  sing N N 179 
GLU   OXT HXT  sing N N 180 
GLY   N   CA   sing N N 181 
GLY   N   H    sing N N 182 
GLY   N   H2   sing N N 183 
GLY   CA  C    sing N N 184 
GLY   CA  HA2  sing N N 185 
GLY   CA  HA3  sing N N 186 
GLY   C   O    doub N N 187 
GLY   C   OXT  sing N N 188 
GLY   OXT HXT  sing N N 189 
HIS   N   CA   sing N N 190 
HIS   N   H    sing N N 191 
HIS   N   H2   sing N N 192 
HIS   CA  C    sing N N 193 
HIS   CA  CB   sing N N 194 
HIS   CA  HA   sing N N 195 
HIS   C   O    doub N N 196 
HIS   C   OXT  sing N N 197 
HIS   CB  CG   sing N N 198 
HIS   CB  HB2  sing N N 199 
HIS   CB  HB3  sing N N 200 
HIS   CG  ND1  sing Y N 201 
HIS   CG  CD2  doub Y N 202 
HIS   ND1 CE1  doub Y N 203 
HIS   ND1 HD1  sing N N 204 
HIS   CD2 NE2  sing Y N 205 
HIS   CD2 HD2  sing N N 206 
HIS   CE1 NE2  sing Y N 207 
HIS   CE1 HE1  sing N N 208 
HIS   NE2 HE2  sing N N 209 
HIS   OXT HXT  sing N N 210 
HOH   O   H1   sing N N 211 
HOH   O   H2   sing N N 212 
ILE   N   CA   sing N N 213 
ILE   N   H    sing N N 214 
ILE   N   H2   sing N N 215 
ILE   CA  C    sing N N 216 
ILE   CA  CB   sing N N 217 
ILE   CA  HA   sing N N 218 
ILE   C   O    doub N N 219 
ILE   C   OXT  sing N N 220 
ILE   CB  CG1  sing N N 221 
ILE   CB  CG2  sing N N 222 
ILE   CB  HB   sing N N 223 
ILE   CG1 CD1  sing N N 224 
ILE   CG1 HG12 sing N N 225 
ILE   CG1 HG13 sing N N 226 
ILE   CG2 HG21 sing N N 227 
ILE   CG2 HG22 sing N N 228 
ILE   CG2 HG23 sing N N 229 
ILE   CD1 HD11 sing N N 230 
ILE   CD1 HD12 sing N N 231 
ILE   CD1 HD13 sing N N 232 
ILE   OXT HXT  sing N N 233 
LEU   N   CA   sing N N 234 
LEU   N   H    sing N N 235 
LEU   N   H2   sing N N 236 
LEU   CA  C    sing N N 237 
LEU   CA  CB   sing N N 238 
LEU   CA  HA   sing N N 239 
LEU   C   O    doub N N 240 
LEU   C   OXT  sing N N 241 
LEU   CB  CG   sing N N 242 
LEU   CB  HB2  sing N N 243 
LEU   CB  HB3  sing N N 244 
LEU   CG  CD1  sing N N 245 
LEU   CG  CD2  sing N N 246 
LEU   CG  HG   sing N N 247 
LEU   CD1 HD11 sing N N 248 
LEU   CD1 HD12 sing N N 249 
LEU   CD1 HD13 sing N N 250 
LEU   CD2 HD21 sing N N 251 
LEU   CD2 HD22 sing N N 252 
LEU   CD2 HD23 sing N N 253 
LEU   OXT HXT  sing N N 254 
LYS   N   CA   sing N N 255 
LYS   N   H    sing N N 256 
LYS   N   H2   sing N N 257 
LYS   CA  C    sing N N 258 
LYS   CA  CB   sing N N 259 
LYS   CA  HA   sing N N 260 
LYS   C   O    doub N N 261 
LYS   C   OXT  sing N N 262 
LYS   CB  CG   sing N N 263 
LYS   CB  HB2  sing N N 264 
LYS   CB  HB3  sing N N 265 
LYS   CG  CD   sing N N 266 
LYS   CG  HG2  sing N N 267 
LYS   CG  HG3  sing N N 268 
LYS   CD  CE   sing N N 269 
LYS   CD  HD2  sing N N 270 
LYS   CD  HD3  sing N N 271 
LYS   CE  NZ   sing N N 272 
LYS   CE  HE2  sing N N 273 
LYS   CE  HE3  sing N N 274 
LYS   NZ  HZ1  sing N N 275 
LYS   NZ  HZ2  sing N N 276 
LYS   NZ  HZ3  sing N N 277 
LYS   OXT HXT  sing N N 278 
MET   N   CA   sing N N 279 
MET   N   H    sing N N 280 
MET   N   H2   sing N N 281 
MET   CA  C    sing N N 282 
MET   CA  CB   sing N N 283 
MET   CA  HA   sing N N 284 
MET   C   O    doub N N 285 
MET   C   OXT  sing N N 286 
MET   CB  CG   sing N N 287 
MET   CB  HB2  sing N N 288 
MET   CB  HB3  sing N N 289 
MET   CG  SD   sing N N 290 
MET   CG  HG2  sing N N 291 
MET   CG  HG3  sing N N 292 
MET   SD  CE   sing N N 293 
MET   CE  HE1  sing N N 294 
MET   CE  HE2  sing N N 295 
MET   CE  HE3  sing N N 296 
MET   OXT HXT  sing N N 297 
PHE   N   CA   sing N N 298 
PHE   N   H    sing N N 299 
PHE   N   H2   sing N N 300 
PHE   CA  C    sing N N 301 
PHE   CA  CB   sing N N 302 
PHE   CA  HA   sing N N 303 
PHE   C   O    doub N N 304 
PHE   C   OXT  sing N N 305 
PHE   CB  CG   sing N N 306 
PHE   CB  HB2  sing N N 307 
PHE   CB  HB3  sing N N 308 
PHE   CG  CD1  doub Y N 309 
PHE   CG  CD2  sing Y N 310 
PHE   CD1 CE1  sing Y N 311 
PHE   CD1 HD1  sing N N 312 
PHE   CD2 CE2  doub Y N 313 
PHE   CD2 HD2  sing N N 314 
PHE   CE1 CZ   doub Y N 315 
PHE   CE1 HE1  sing N N 316 
PHE   CE2 CZ   sing Y N 317 
PHE   CE2 HE2  sing N N 318 
PHE   CZ  HZ   sing N N 319 
PHE   OXT HXT  sing N N 320 
PRO   N   CA   sing N N 321 
PRO   N   CD   sing N N 322 
PRO   N   H    sing N N 323 
PRO   CA  C    sing N N 324 
PRO   CA  CB   sing N N 325 
PRO   CA  HA   sing N N 326 
PRO   C   O    doub N N 327 
PRO   C   OXT  sing N N 328 
PRO   CB  CG   sing N N 329 
PRO   CB  HB2  sing N N 330 
PRO   CB  HB3  sing N N 331 
PRO   CG  CD   sing N N 332 
PRO   CG  HG2  sing N N 333 
PRO   CG  HG3  sing N N 334 
PRO   CD  HD2  sing N N 335 
PRO   CD  HD3  sing N N 336 
PRO   OXT HXT  sing N N 337 
SER   N   CA   sing N N 338 
SER   N   H    sing N N 339 
SER   N   H2   sing N N 340 
SER   CA  C    sing N N 341 
SER   CA  CB   sing N N 342 
SER   CA  HA   sing N N 343 
SER   C   O    doub N N 344 
SER   C   OXT  sing N N 345 
SER   CB  OG   sing N N 346 
SER   CB  HB2  sing N N 347 
SER   CB  HB3  sing N N 348 
SER   OG  HG   sing N N 349 
SER   OXT HXT  sing N N 350 
SO4   S   O1   doub N N 351 
SO4   S   O2   doub N N 352 
SO4   S   O3   sing N N 353 
SO4   S   O4   sing N N 354 
THR   N   CA   sing N N 355 
THR   N   H    sing N N 356 
THR   N   H2   sing N N 357 
THR   CA  C    sing N N 358 
THR   CA  CB   sing N N 359 
THR   CA  HA   sing N N 360 
THR   C   O    doub N N 361 
THR   C   OXT  sing N N 362 
THR   CB  OG1  sing N N 363 
THR   CB  CG2  sing N N 364 
THR   CB  HB   sing N N 365 
THR   OG1 HG1  sing N N 366 
THR   CG2 HG21 sing N N 367 
THR   CG2 HG22 sing N N 368 
THR   CG2 HG23 sing N N 369 
THR   OXT HXT  sing N N 370 
TRP   N   CA   sing N N 371 
TRP   N   H    sing N N 372 
TRP   N   H2   sing N N 373 
TRP   CA  C    sing N N 374 
TRP   CA  CB   sing N N 375 
TRP   CA  HA   sing N N 376 
TRP   C   O    doub N N 377 
TRP   C   OXT  sing N N 378 
TRP   CB  CG   sing N N 379 
TRP   CB  HB2  sing N N 380 
TRP   CB  HB3  sing N N 381 
TRP   CG  CD1  doub Y N 382 
TRP   CG  CD2  sing Y N 383 
TRP   CD1 NE1  sing Y N 384 
TRP   CD1 HD1  sing N N 385 
TRP   CD2 CE2  doub Y N 386 
TRP   CD2 CE3  sing Y N 387 
TRP   NE1 CE2  sing Y N 388 
TRP   NE1 HE1  sing N N 389 
TRP   CE2 CZ2  sing Y N 390 
TRP   CE3 CZ3  doub Y N 391 
TRP   CE3 HE3  sing N N 392 
TRP   CZ2 CH2  doub Y N 393 
TRP   CZ2 HZ2  sing N N 394 
TRP   CZ3 CH2  sing Y N 395 
TRP   CZ3 HZ3  sing N N 396 
TRP   CH2 HH2  sing N N 397 
TRP   OXT HXT  sing N N 398 
TYR   N   CA   sing N N 399 
TYR   N   H    sing N N 400 
TYR   N   H2   sing N N 401 
TYR   CA  C    sing N N 402 
TYR   CA  CB   sing N N 403 
TYR   CA  HA   sing N N 404 
TYR   C   O    doub N N 405 
TYR   C   OXT  sing N N 406 
TYR   CB  CG   sing N N 407 
TYR   CB  HB2  sing N N 408 
TYR   CB  HB3  sing N N 409 
TYR   CG  CD1  doub Y N 410 
TYR   CG  CD2  sing Y N 411 
TYR   CD1 CE1  sing Y N 412 
TYR   CD1 HD1  sing N N 413 
TYR   CD2 CE2  doub Y N 414 
TYR   CD2 HD2  sing N N 415 
TYR   CE1 CZ   doub Y N 416 
TYR   CE1 HE1  sing N N 417 
TYR   CE2 CZ   sing Y N 418 
TYR   CE2 HE2  sing N N 419 
TYR   CZ  OH   sing N N 420 
TYR   OH  HH   sing N N 421 
TYR   OXT HXT  sing N N 422 
VAL   N   CA   sing N N 423 
VAL   N   H    sing N N 424 
VAL   N   H2   sing N N 425 
VAL   CA  C    sing N N 426 
VAL   CA  CB   sing N N 427 
VAL   CA  HA   sing N N 428 
VAL   C   O    doub N N 429 
VAL   C   OXT  sing N N 430 
VAL   CB  CG1  sing N N 431 
VAL   CB  CG2  sing N N 432 
VAL   CB  HB   sing N N 433 
VAL   CG1 HG11 sing N N 434 
VAL   CG1 HG12 sing N N 435 
VAL   CG1 HG13 sing N N 436 
VAL   CG2 HG21 sing N N 437 
VAL   CG2 HG22 sing N N 438 
VAL   CG2 HG23 sing N N 439 
VAL   OXT HXT  sing N N 440 
# 
_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                    7HOV 
_atom_sites.fract_transf_matrix[1][1]   0.023525 
_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]   0.023525 
_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]   0.004620 
_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   ? -20.485 18.872  -7.761  1.00 73.93  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -21.811 18.171  -7.669  1.00 71.00  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.116 17.527  -9.028  1.00 67.65  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -21.843 18.155  -10.106 1.00 70.48  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -22.904 19.125  -7.204  1.00 73.75  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.278 18.501  -7.058  1.00 74.37  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -24.626 18.048  -5.919  1.00 75.80  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -25.015 18.513  -8.072  1.00 75.84  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.613 16.303  -8.975  1.00 59.96  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.460 15.352  -10.089 1.00 57.53  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.835 15.058  -10.674 1.00 52.16  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.766 14.882  -9.888  1.00 50.59  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.776 14.063  -9.613  1.00 57.83  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.274 14.194  -9.556  1.00 60.79  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.476 12.605  -9.171  1.00 62.04  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.761 13.126  -9.069  1.00 63.85  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.921 14.966  -12.008 1.00 49.99  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.197 14.686  -12.723 1.00 48.40  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.941 13.694  -13.851 1.00 46.77  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.840 13.546  -14.333 1.00 46.27  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.868 15.995  -13.180 1.00 49.24  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.080 16.825  -14.139 1.00 49.40  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.060 17.650  -13.700 1.00 50.41  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.318 16.748  -15.500 1.00 49.40  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.309 18.394  -14.599 1.00 52.03  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.565 17.472  -16.409 1.00 51.39  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.568 18.317  -15.957 1.00 52.36  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.826 19.008  -16.867 1.00 54.89  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -25.997 13.015  -14.264 1.00 46.62  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.947 12.039  -15.379 1.00 47.06  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.715 12.540  -16.613 1.00 48.66  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.763 13.221  -16.465 1.00 50.63  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.417 10.657  -14.890 1.00 45.37  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.835 10.633  -14.341 1.00 46.05  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.446 10.139  -13.865 1.00 45.82  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.369 9.226   -14.148 1.00 44.92  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.189 12.216  -17.783 1.00 49.76  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -26.810 12.454  -19.114 1.00 52.19  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -26.838 11.128  -19.888 1.00 52.07  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.766 10.464  -19.995 1.00 49.12  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.009 13.473  -19.910 1.00 54.23  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.127 14.888  -19.412 1.00 57.07  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.242 15.832  -20.214 1.00 60.73  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.323 15.359  -20.911 1.00 60.29  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.480 17.036  -20.162 1.00 64.76  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -27.995 10.763  -20.445 1.00 53.69  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.101 9.546   -21.294 1.00 54.94  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.169 9.672   -22.502 1.00 54.85  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.079 10.766  -23.083 1.00 56.56  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.547 9.301   -21.708 1.00 56.82  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -29.847 7.847   -22.035 1.00 58.07  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.337 7.543   -22.090 1.00 59.65  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.575 6.140   -22.353 1.00 61.06  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.369 5.564   -23.539 1.00 62.66  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -30.939 6.281   -24.561 1.00 67.91  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.555 4.269   -23.711 1.00 60.72  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.462 8.597   -22.864 1.00 53.93  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.537 8.571   -24.020 1.00 54.75  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -25.979 7.523   -25.051 1.00 53.61  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.401 7.532   -26.127 1.00 55.12  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.102 8.335   -23.562 1.00 54.75  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -26.924 6.639   -24.741 1.00 52.12  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.352 5.626   -25.723 1.00 53.18  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -27.998 4.389   -25.112 1.00 53.06  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.130 4.339   -23.859 1.00 51.84  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.361 3.425   -25.986 1.00 54.72  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -28.970 2.110   -25.664 1.00 55.46  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.828 1.109   -25.450 1.00 56.28  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.744 1.306   -26.014 1.00 56.85  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -29.857 1.564   -26.782 1.00 56.93  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.169 2.292   -26.944 1.00 61.23  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.388 3.260   -26.213 1.00 59.83  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -31.952 1.896   -27.815 1.00 65.48  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.056 0.079   -24.653 1.00 56.31  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.033 -0.986  -24.506 1.00 57.67  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.397 -2.145  -25.445 1.00 58.54  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.270 -2.970  -25.105 1.00 60.29  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.907 -1.374  -23.048 1.00 55.14  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.416 -0.161  -22.257 1.00 53.60  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -25.988 -2.593  -22.923 1.00 56.52  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.431 -0.364  -20.791 1.00 52.83  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.738 -2.175  -26.603 0.25 59.73  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.735 -2.216  -26.602 0.25 59.78  ? 60  THR   A N   1 
ATOM   84   N  N   C THR   A 1 17  ? -26.738 -2.175  -26.603 0.25 59.73  ? 60  THR   A N   1 
ATOM   85   N  N   D THR   A 1 17  ? -26.735 -2.216  -26.602 0.25 59.78  ? 60  THR   A N   1 
ATOM   86   C  CA  A THR   A 1 17  ? -26.972 -3.144  -27.701 0.25 61.15  ? 60  THR   A CA  1 
ATOM   87   C  CA  B THR   A 1 17  ? -27.055 -3.167  -27.701 0.25 61.31  ? 60  THR   A CA  1 
ATOM   88   C  CA  C THR   A 1 17  ? -26.972 -3.144  -27.701 0.25 61.15  ? 60  THR   A CA  1 
ATOM   89   C  CA  D THR   A 1 17  ? -27.055 -3.167  -27.701 0.25 61.31  ? 60  THR   A CA  1 
ATOM   90   C  C   A THR   A 1 17  ? -25.639 -3.717  -28.184 0.25 61.57  ? 60  THR   A C   1 
ATOM   91   C  C   B THR   A 1 17  ? -25.758 -3.666  -28.357 0.25 62.51  ? 60  THR   A C   1 
ATOM   92   C  C   C THR   A 1 17  ? -25.639 -3.717  -28.184 0.25 61.57  ? 60  THR   A C   1 
ATOM   93   C  C   D THR   A 1 17  ? -25.758 -3.666  -28.357 0.25 62.51  ? 60  THR   A C   1 
ATOM   94   O  O   A THR   A 1 17  ? -24.619 -3.004  -28.146 0.25 60.60  ? 60  THR   A O   1 
ATOM   95   O  O   B THR   A 1 17  ? -24.874 -2.830  -28.638 0.25 63.39  ? 60  THR   A O   1 
ATOM   96   O  O   C THR   A 1 17  ? -24.619 -3.004  -28.146 0.25 60.60  ? 60  THR   A O   1 
ATOM   97   O  O   D THR   A 1 17  ? -24.874 -2.830  -28.638 0.25 63.39  ? 60  THR   A O   1 
ATOM   98   C  CB  A THR   A 1 17  ? -27.722 -2.489  -28.863 0.25 62.86  ? 60  THR   A CB  1 
ATOM   99   C  CB  B THR   A 1 17  ? -28.035 -2.509  -28.680 0.25 62.58  ? 60  THR   A CB  1 
ATOM   100  C  CB  C THR   A 1 17  ? -27.722 -2.489  -28.863 0.25 62.86  ? 60  THR   A CB  1 
ATOM   101  C  CB  D THR   A 1 17  ? -28.035 -2.509  -28.680 0.25 62.58  ? 60  THR   A CB  1 
ATOM   102  O  OG1 A THR   A 1 17  ? -26.936 -1.385  -29.309 0.25 63.27  ? 60  THR   A OG1 1 
ATOM   103  O  OG1 B THR   A 1 17  ? -29.167 -2.112  -27.904 0.25 61.61  ? 60  THR   A OG1 1 
ATOM   104  O  OG1 C THR   A 1 17  ? -26.936 -1.385  -29.309 0.25 63.27  ? 60  THR   A OG1 1 
ATOM   105  O  OG1 D THR   A 1 17  ? -29.167 -2.112  -27.904 0.25 61.61  ? 60  THR   A OG1 1 
ATOM   106  C  CG2 A THR   A 1 17  ? -29.105 -2.033  -28.463 0.25 63.50  ? 60  THR   A CG2 1 
ATOM   107  C  CG2 B THR   A 1 17  ? -28.478 -3.414  -29.808 0.25 63.92  ? 60  THR   A CG2 1 
ATOM   108  C  CG2 C THR   A 1 17  ? -29.105 -2.033  -28.463 0.25 63.50  ? 60  THR   A CG2 1 
ATOM   109  C  CG2 D THR   A 1 17  ? -28.478 -3.414  -29.808 0.25 63.92  ? 60  THR   A CG2 1 
ATOM   110  N  N   . TRP   A 1 18  ? -25.660 -4.979  -28.597 1.00 62.32  ? 61  TRP   A N   1 
ATOM   111  C  CA  . TRP   A 1 18  ? -24.587 -5.556  -29.431 1.00 66.66  ? 61  TRP   A CA  1 
ATOM   112  C  C   . TRP   A 1 18  ? -24.823 -5.038  -30.856 1.00 73.47  ? 61  TRP   A C   1 
ATOM   113  O  O   . TRP   A 1 18  ? -25.986 -5.046  -31.291 1.00 78.62  ? 61  TRP   A O   1 
ATOM   114  C  CB  . TRP   A 1 18  ? -24.628 -7.074  -29.360 1.00 67.20  ? 61  TRP   A CB  1 
ATOM   115  C  CG  . TRP   A 1 18  ? -23.529 -7.685  -30.167 1.00 69.59  ? 61  TRP   A CG  1 
ATOM   116  C  CD1 . TRP   A 1 18  ? -23.548 -7.923  -31.505 1.00 71.30  ? 61  TRP   A CD1 1 
ATOM   117  C  CD2 . TRP   A 1 18  ? -22.244 -8.122  -29.694 1.00 69.35  ? 61  TRP   A CD2 1 
ATOM   118  N  NE1 . TRP   A 1 18  ? -22.363 -8.470  -31.896 1.00 73.45  ? 61  TRP   A NE1 1 
ATOM   119  C  CE2 . TRP   A 1 18  ? -21.546 -8.621  -30.813 1.00 72.27  ? 61  TRP   A CE2 1 
ATOM   120  C  CE3 . TRP   A 1 18  ? -21.620 -8.163  -28.445 1.00 67.09  ? 61  TRP   A CE3 1 
ATOM   121  C  CZ2 . TRP   A 1 18  ? -20.262 -9.162  -30.714 1.00 71.59  ? 61  TRP   A CZ2 1 
ATOM   122  C  CZ3 . TRP   A 1 18  ? -20.346 -8.678  -28.349 1.00 68.03  ? 61  TRP   A CZ3 1 
ATOM   123  C  CH2 . TRP   A 1 18  ? -19.684 -9.181  -29.461 1.00 66.05  ? 61  TRP   A CH2 1 
ATOM   124  N  N   . GLU   A 1 19  ? -23.793 -4.519  -31.521 1.00 77.56  ? 62  GLU   A N   1 
ATOM   125  C  CA  . GLU   A 1 19  ? -23.909 -3.938  -32.879 1.00 82.91  ? 62  GLU   A CA  1 
ATOM   126  C  C   . GLU   A 1 19  ? -23.121 -4.798  -33.856 1.00 86.11  ? 62  GLU   A C   1 
ATOM   127  O  O   . GLU   A 1 19  ? -21.874 -4.830  -33.732 1.00 84.93  ? 62  GLU   A O   1 
ATOM   128  C  CB  . GLU   A 1 19  ? -23.423 -2.492  -32.890 1.00 88.42  ? 62  GLU   A CB  1 
ATOM   129  C  CG  . GLU   A 1 19  ? -24.318 -1.574  -32.049 1.00 94.45  ? 62  GLU   A CG  1 
ATOM   130  C  CD  . GLU   A 1 19  ? -25.774 -1.415  -32.490 1.00 96.41  ? 62  GLU   A CD  1 
ATOM   131  O  OE1 . GLU   A 1 19  ? -26.001 -0.913  -33.611 1.00 101.32 ? 62  GLU   A OE1 1 
ATOM   132  O  OE2 . GLU   A 1 19  ? -26.680 -1.783  -31.708 1.00 95.81  ? 62  GLU   A OE2 1 
ATOM   133  N  N   . LYS   A 1 20  ? -23.835 -5.483  -34.759 1.00 89.60  ? 63  LYS   A N   1 
ATOM   134  C  CA  . LYS   A 1 20  ? -23.241 -6.272  -35.870 1.00 92.06  ? 63  LYS   A CA  1 
ATOM   135  C  C   . LYS   A 1 20  ? -22.288 -5.348  -36.621 1.00 90.18  ? 63  LYS   A C   1 
ATOM   136  O  O   . LYS   A 1 20  ? -22.650 -4.196  -36.805 1.00 96.76  ? 63  LYS   A O   1 
ATOM   137  C  CB  . LYS   A 1 20  ? -24.339 -6.812  -36.787 1.00 97.60  ? 63  LYS   A CB  1 
ATOM   138  C  CG  . LYS   A 1 20  ? -24.678 -8.282  -36.595 1.00 100.47 ? 63  LYS   A CG  1 
ATOM   139  C  CD  . LYS   A 1 20  ? -24.898 -9.014  -37.922 1.00 108.39 ? 63  LYS   A CD  1 
ATOM   140  C  CE  . LYS   A 1 20  ? -24.003 -10.226 -38.093 1.00 109.13 ? 63  LYS   A CE  1 
ATOM   141  N  NZ  . LYS   A 1 20  ? -24.160 -11.176 -36.965 1.00 108.37 ? 63  LYS   A NZ  1 
ATOM   142  N  N   . ASP   A 1 21  ? -21.091 -5.807  -36.962 1.00 90.10  ? 64  ASP   A N   1 
ATOM   143  C  CA  . ASP   A 1 21  ? -20.090 -4.992  -37.704 1.00 94.49  ? 64  ASP   A CA  1 
ATOM   144  C  C   . ASP   A 1 21  ? -19.721 -3.717  -36.913 1.00 90.33  ? 64  ASP   A C   1 
ATOM   145  O  O   . ASP   A 1 21  ? -19.789 -2.615  -37.503 1.00 89.79  ? 64  ASP   A O   1 
ATOM   146  C  CB  . ASP   A 1 21  ? -20.597 -4.625  -39.115 1.00 105.07 ? 64  ASP   A CB  1 
ATOM   147  C  CG  . ASP   A 1 21  ? -20.656 -5.753  -40.152 1.00 108.64 ? 64  ASP   A CG  1 
ATOM   148  O  OD1 . ASP   A 1 21  ? -19.571 -6.233  -40.577 1.00 107.20 ? 64  ASP   A OD1 1 
ATOM   149  O  OD2 . ASP   A 1 21  ? -21.790 -6.118  -40.564 1.00 112.84 ? 64  ASP   A OD2 1 
ATOM   150  N  N   . ALA   A 1 22  ? -19.327 -3.851  -35.639 1.00 87.84  ? 65  ALA   A N   1 
ATOM   151  C  CA  . ALA   A 1 22  ? -18.515 -2.855  -34.890 1.00 83.39  ? 65  ALA   A CA  1 
ATOM   152  C  C   . ALA   A 1 22  ? -17.001 -3.061  -35.208 1.00 83.39  ? 65  ALA   A C   1 
ATOM   153  O  O   . ALA   A 1 22  ? -16.636 -4.184  -36.024 1.00 84.82  ? 65  ALA   A O   1 
ATOM   154  C  CB  . ALA   A 1 22  ? -18.778 -3.009  -33.380 1.00 82.84  ? 65  ALA   A CB  1 
ATOM   155  N  N   . GLU   A 1 23  ? -16.209 -1.986  -35.041 1.00 83.53  ? 66  GLU   A N   1 
ATOM   156  C  CA  . GLU   A 1 23  ? -14.717 -1.895  -35.209 1.00 84.88  ? 66  GLU   A CA  1 
ATOM   157  C  C   . GLU   A 1 23  ? -14.034 -2.936  -34.287 1.00 81.16  ? 66  GLU   A C   1 
ATOM   158  O  O   . GLU   A 1 23  ? -14.110 -2.784  -33.052 1.00 72.51  ? 66  GLU   A O   1 
ATOM   159  C  CB  . GLU   A 1 23  ? -14.309 -0.448  -34.889 1.00 90.84  ? 66  GLU   A CB  1 
ATOM   160  C  CG  . GLU   A 1 23  ? -12.814 -0.168  -34.856 1.00 97.78  ? 66  GLU   A CG  1 
ATOM   161  C  CD  . GLU   A 1 23  ? -12.461 1.248   -34.406 1.00 106.29 ? 66  GLU   A CD  1 
ATOM   162  O  OE1 . GLU   A 1 23  ? -13.179 2.219   -34.801 1.00 108.19 ? 66  GLU   A OE1 1 
ATOM   163  O  OE2 . GLU   A 1 23  ? -11.458 1.383   -33.661 1.00 109.87 ? 66  GLU   A OE2 1 
ATOM   164  N  N   . VAL   A 1 24  ? -13.387 -3.964  -34.858 1.00 80.61  ? 67  VAL   A N   1 
ATOM   165  C  CA  . VAL   A 1 24  ? -12.809 -5.122  -34.101 1.00 78.89  ? 67  VAL   A CA  1 
ATOM   166  C  C   . VAL   A 1 24  ? -11.313 -4.876  -33.901 1.00 78.03  ? 67  VAL   A C   1 
ATOM   167  O  O   . VAL   A 1 24  ? -10.618 -4.703  -34.900 1.00 81.47  ? 67  VAL   A O   1 
ATOM   168  C  CB  . VAL   A 1 24  ? -13.073 -6.457  -34.821 1.00 79.72  ? 67  VAL   A CB  1 
ATOM   169  C  CG1 . VAL   A 1 24  ? -12.562 -7.638  -34.016 1.00 77.18  ? 67  VAL   A CG1 1 
ATOM   170  C  CG2 . VAL   A 1 24  ? -14.551 -6.621  -35.169 1.00 80.66  ? 67  VAL   A CG2 1 
ATOM   171  N  N   . THR   A 1 25  ? -10.844 -4.841  -32.654 1.00 75.30  ? 68  THR   A N   1 
ATOM   172  C  CA  . THR   A 1 25  ? -9.493  -4.339  -32.301 1.00 74.15  ? 68  THR   A CA  1 
ATOM   173  C  C   . THR   A 1 25  ? -9.137  -4.769  -30.876 1.00 71.56  ? 68  THR   A C   1 
ATOM   174  O  O   . THR   A 1 25  ? -10.010 -5.282  -30.171 1.00 70.12  ? 68  THR   A O   1 
ATOM   175  C  CB  . THR   A 1 25  ? -9.427  -2.819  -32.498 1.00 77.25  ? 68  THR   A CB  1 
ATOM   176  O  OG1 . THR   A 1 25  ? -8.045  -2.487  -32.524 1.00 78.19  ? 68  THR   A OG1 1 
ATOM   177  C  CG2 . THR   A 1 25  ? -10.133 -2.009  -31.429 1.00 76.68  ? 68  THR   A CG2 1 
ATOM   178  N  N   . GLY   A 1 26  ? -7.864  -4.595  -30.519 1.00 71.51  ? 69  GLY   A N   1 
ATOM   179  C  CA  . GLY   A 1 26  ? -7.263  -4.958  -29.234 1.00 68.55  ? 69  GLY   A CA  1 
ATOM   180  C  C   . GLY   A 1 26  ? -6.681  -6.368  -29.260 1.00 69.02  ? 69  GLY   A C   1 
ATOM   181  O  O   . GLY   A 1 26  ? -7.197  -7.222  -30.002 1.00 71.57  ? 69  GLY   A O   1 
ATOM   182  N  N   . ASN   A 1 27  ? -5.668  -6.586  -28.412 1.00 70.55  ? 70  ASN   A N   1 
ATOM   183  C  CA  . ASN   A 1 27  ? -4.975  -7.880  -28.172 1.00 69.88  ? 70  ASN   A CA  1 
ATOM   184  C  C   . ASN   A 1 27  ? -5.619  -8.540  -26.933 1.00 66.43  ? 70  ASN   A C   1 
ATOM   185  O  O   . ASN   A 1 27  ? -6.646  -7.964  -26.450 1.00 65.40  ? 70  ASN   A O   1 
ATOM   186  C  CB  . ASN   A 1 27  ? -3.470  -7.609  -28.131 1.00 72.23  ? 70  ASN   A CB  1 
ATOM   187  C  CG  . ASN   A 1 27  ? -3.044  -6.990  -26.817 1.00 73.17  ? 70  ASN   A CG  1 
ATOM   188  O  OD1 . ASN   A 1 27  ? -3.476  -5.889  -26.474 1.00 69.09  ? 70  ASN   A OD1 1 
ATOM   189  N  ND2 . ASN   A 1 27  ? -2.233  -7.713  -26.052 1.00 76.45  ? 70  ASN   A ND2 1 
ATOM   190  N  N   . SER   A 1 28  ? -5.121  -9.712  -26.477 1.00 64.25  ? 71  SER   A N   1 
ATOM   191  C  CA  . SER   A 1 28  ? -5.677  -10.527 -25.354 1.00 65.59  ? 71  SER   A CA  1 
ATOM   192  C  C   . SER   A 1 28  ? -4.585  -10.915 -24.366 1.00 66.62  ? 71  SER   A C   1 
ATOM   193  O  O   . SER   A 1 28  ? -4.291  -12.099 -24.277 1.00 68.18  ? 71  SER   A O   1 
ATOM   194  C  CB  . SER   A 1 28  ? -6.305  -11.811 -25.836 1.00 66.09  ? 71  SER   A CB  1 
ATOM   195  O  OG  . SER   A 1 28  ? -7.415  -11.597 -26.672 1.00 68.97  ? 71  SER   A OG  1 
ATOM   196  N  N   . PRO   A 1 29  ? -3.959  -10.003 -23.588 1.00 68.00  ? 72  PRO   A N   1 
ATOM   197  C  CA  . PRO   A 1 29  ? -2.796  -10.379 -22.784 1.00 69.96  ? 72  PRO   A CA  1 
ATOM   198  C  C   . PRO   A 1 29  ? -3.222  -11.264 -21.611 1.00 66.42  ? 72  PRO   A C   1 
ATOM   199  O  O   . PRO   A 1 29  ? -4.290  -11.039 -21.068 1.00 62.86  ? 72  PRO   A O   1 
ATOM   200  C  CB  . PRO   A 1 29  ? -2.201  -9.029  -22.343 1.00 71.81  ? 72  PRO   A CB  1 
ATOM   201  C  CG  . PRO   A 1 29  ? -3.411  -8.105  -22.282 1.00 69.40  ? 72  PRO   A CG  1 
ATOM   202  C  CD  . PRO   A 1 29  ? -4.316  -8.589  -23.402 1.00 68.89  ? 72  PRO   A CD  1 
ATOM   203  N  N   . ARG   A 1 30  ? -2.416  -12.279 -21.301 1.00 67.63  ? 73  ARG   A N   1 
ATOM   204  C  CA  . ARG   A 1 30  ? -2.540  -13.064 -20.047 1.00 70.50  ? 73  ARG   A CA  1 
ATOM   205  C  C   . ARG   A 1 30  ? -1.580  -12.442 -19.031 1.00 69.07  ? 73  ARG   A C   1 
ATOM   206  O  O   . ARG   A 1 30  ? -0.374  -12.504 -19.269 1.00 67.24  ? 73  ARG   A O   1 
ATOM   207  C  CB  . ARG   A 1 30  ? -2.273  -14.550 -20.294 1.00 77.20  ? 73  ARG   A CB  1 
ATOM   208  C  CG  . ARG   A 1 30  ? -3.348  -15.215 -21.144 1.00 81.79  ? 73  ARG   A CG  1 
ATOM   209  C  CD  . ARG   A 1 30  ? -3.001  -16.641 -21.546 1.00 87.90  ? 73  ARG   A CD  1 
ATOM   210  N  NE  . ARG   A 1 30  ? -3.943  -17.206 -22.519 1.00 91.01  ? 73  ARG   A NE  1 
ATOM   211  C  CZ  . ARG   A 1 30  ? -5.112  -17.786 -22.221 1.00 88.97  ? 73  ARG   A CZ  1 
ATOM   212  N  NH1 . ARG   A 1 30  ? -5.515  -17.874 -20.960 1.00 91.20  ? 73  ARG   A NH1 1 
ATOM   213  N  NH2 . ARG   A 1 30  ? -5.874  -18.274 -23.189 1.00 82.69  ? 73  ARG   A NH2 1 
ATOM   214  N  N   . LEU   A 1 31  ? -2.091  -11.783 -17.982 1.00 64.85  ? 74  LEU   A N   1 
ATOM   215  C  CA  . LEU   A 1 31  ? -1.207  -10.999 -17.080 1.00 64.37  ? 74  LEU   A CA  1 
ATOM   216  C  C   . LEU   A 1 31  ? -1.330  -11.539 -15.657 1.00 60.55  ? 74  LEU   A C   1 
ATOM   217  O  O   . LEU   A 1 31  ? -2.413  -11.957 -15.271 1.00 58.94  ? 74  LEU   A O   1 
ATOM   218  C  CB  . LEU   A 1 31  ? -1.548  -9.507  -17.170 1.00 62.96  ? 74  LEU   A CB  1 
ATOM   219  C  CG  . LEU   A 1 31  ? -1.312  -8.861  -18.530 1.00 64.94  ? 74  LEU   A CG  1 
ATOM   220  C  CD1 . LEU   A 1 31  ? -1.937  -7.472  -18.573 1.00 64.49  ? 74  LEU   A CD1 1 
ATOM   221  C  CD2 . LEU   A 1 31  ? 0.190   -8.801  -18.863 1.00 66.40  ? 74  LEU   A CD2 1 
ATOM   222  N  N   . ASP   A 1 32  ? -0.229  -11.525 -14.923 1.00 59.93  ? 75  ASP   A N   1 
ATOM   223  C  CA  . ASP   A 1 32  ? -0.209  -11.858 -13.483 1.00 61.65  ? 75  ASP   A CA  1 
ATOM   224  C  C   . ASP   A 1 32  ? -0.385  -10.578 -12.677 1.00 58.90  ? 75  ASP   A C   1 
ATOM   225  O  O   . ASP   A 1 32  ? 0.551   -9.710  -12.702 1.00 58.50  ? 75  ASP   A O   1 
ATOM   226  C  CB  . ASP   A 1 32  ? 1.089   -12.572 -13.099 1.00 66.27  ? 75  ASP   A CB  1 
ATOM   227  C  CG  . ASP   A 1 32  ? 1.036   -14.065 -13.360 1.00 68.23  ? 75  ASP   A CG  1 
ATOM   228  O  OD1 . ASP   A 1 32  ? -0.050  -14.656 -13.194 1.00 66.10  ? 75  ASP   A OD1 1 
ATOM   229  O  OD2 . ASP   A 1 32  ? 2.082   -14.622 -13.713 1.00 75.13  ? 75  ASP   A OD2 1 
ATOM   230  N  N   . VAL   A 1 33  ? -1.522  -10.474 -11.982 1.00 55.37  ? 76  VAL   A N   1 
ATOM   231  C  CA  . VAL   A 1 33  ? -1.881  -9.227  -11.248 1.00 55.60  ? 76  VAL   A CA  1 
ATOM   232  C  C   . VAL   A 1 33  ? -2.167  -9.550  -9.775  1.00 54.66  ? 76  VAL   A C   1 
ATOM   233  O  O   . VAL   A 1 33  ? -2.721  -10.659 -9.460  1.00 55.25  ? 76  VAL   A O   1 
ATOM   234  C  CB  . VAL   A 1 33  ? -3.028  -8.467  -11.950 1.00 52.41  ? 76  VAL   A CB  1 
ATOM   235  C  CG1 . VAL   A 1 33  ? -2.851  -8.387  -13.447 1.00 52.44  ? 76  VAL   A CG1 1 
ATOM   236  C  CG2 . VAL   A 1 33  ? -4.388  -9.044  -11.642 1.00 51.34  ? 76  VAL   A CG2 1 
ATOM   237  N  N   . ALA   A 1 34  ? -1.829  -8.605  -8.894  1.00 54.30  ? 77  ALA   A N   1 
ATOM   238  C  CA  . ALA   A 1 34  ? -2.303  -8.523  -7.494  1.00 52.86  ? 77  ALA   A CA  1 
ATOM   239  C  C   . ALA   A 1 34  ? -3.370  -7.414  -7.358  1.00 51.39  ? 77  ALA   A C   1 
ATOM   240  O  O   . ALA   A 1 34  ? -3.367  -6.481  -8.158  1.00 51.14  ? 77  ALA   A O   1 
ATOM   241  C  CB  . ALA   A 1 34  ? -1.132  -8.302  -6.580  1.00 55.49  ? 77  ALA   A CB  1 
ATOM   242  N  N   . LEU   A 1 35  ? -4.297  -7.587  -6.417  1.00 51.19  ? 78  LEU   A N   1 
ATOM   243  C  CA  . LEU   A 1 35  ? -5.385  -6.635  -6.043  1.00 50.47  ? 78  LEU   A CA  1 
ATOM   244  C  C   . LEU   A 1 35  ? -5.231  -6.270  -4.556  1.00 51.03  ? 78  LEU   A C   1 
ATOM   245  O  O   . LEU   A 1 35  ? -5.385  -7.182  -3.677  1.00 51.85  ? 78  LEU   A O   1 
ATOM   246  C  CB  . LEU   A 1 35  ? -6.754  -7.279  -6.321  1.00 49.27  ? 78  LEU   A CB  1 
ATOM   247  C  CG  . LEU   A 1 35  ? -7.996  -6.385  -6.082  1.00 48.95  ? 78  LEU   A CG  1 
ATOM   248  C  CD1 . LEU   A 1 35  ? -7.907  -5.055  -6.820  1.00 47.94  ? 78  LEU   A CD1 1 
ATOM   249  C  CD2 . LEU   A 1 35  ? -9.289  -7.097  -6.482  1.00 46.91  ? 78  LEU   A CD2 1 
ATOM   250  N  N   . ASP   A 1 36  ? -4.856  -5.020  -4.250  1.00 50.55  ? 79  ASP   A N   1 
ATOM   251  C  CA  . ASP   A 1 36  ? -4.734  -4.529  -2.853  1.00 51.29  ? 79  ASP   A CA  1 
ATOM   252  C  C   . ASP   A 1 36  ? -6.134  -4.172  -2.272  1.00 49.94  ? 79  ASP   A C   1 
ATOM   253  O  O   . ASP   A 1 36  ? -7.158  -4.180  -3.028  1.00 46.71  ? 79  ASP   A O   1 
ATOM   254  C  CB  . ASP   A 1 36  ? -3.670  -3.420  -2.757  1.00 54.05  ? 79  ASP   A CB  1 
ATOM   255  C  CG  . ASP   A 1 36  ? -4.095  -2.067  -3.312  1.00 53.61  ? 79  ASP   A CG  1 
ATOM   256  O  OD1 . ASP   A 1 36  ? -5.301  -1.889  -3.621  1.00 52.13  ? 79  ASP   A OD1 1 
ATOM   257  O  OD2 . ASP   A 1 36  ? -3.227  -1.214  -3.439  1.00 55.04  ? 79  ASP   A OD2 1 
ATOM   258  N  N   . GLU   A 1 37  ? -6.147  -3.853  -0.971  1.00 51.74  ? 80  GLU   A N   1 
ATOM   259  C  CA  . GLU   A 1 37  ? -7.338  -3.483  -0.174  1.00 52.63  ? 80  GLU   A CA  1 
ATOM   260  C  C   . GLU   A 1 37  ? -8.017  -2.237  -0.758  1.00 51.11  ? 80  GLU   A C   1 
ATOM   261  O  O   . GLU   A 1 37  ? -9.242  -2.148  -0.604  1.00 49.77  ? 80  GLU   A O   1 
ATOM   262  C  CB  . GLU   A 1 37  ? -6.928  -3.265  1.282   1.00 56.51  ? 80  GLU   A CB  1 
ATOM   263  C  CG  . GLU   A 1 37  ? -8.075  -3.380  2.264   1.00 57.22  ? 80  GLU   A CG  1 
ATOM   264  C  CD  . GLU   A 1 37  ? -7.655  -3.236  3.722   1.00 60.45  ? 80  GLU   A CD  1 
ATOM   265  O  OE1 . GLU   A 1 37  ? -7.196  -2.147  4.124   1.00 61.53  ? 80  GLU   A OE1 1 
ATOM   266  O  OE2 . GLU   A 1 37  ? -7.773  -4.222  4.451   1.00 64.60  ? 80  GLU   A OE2 1 
ATOM   267  N  N   . SER   A 1 38  ? -7.258  -1.319  -1.368  1.00 51.73  ? 81  SER   A N   1 
ATOM   268  C  CA  . SER   A 1 38  ? -7.743  -0.052  -1.969  1.00 51.30  ? 81  SER   A CA  1 
ATOM   269  C  C   . SER   A 1 38  ? -8.284  -0.244  -3.368  1.00 49.51  ? 81  SER   A C   1 
ATOM   270  O  O   . SER   A 1 38  ? -8.571  0.787   -3.989  1.00 50.88  ? 81  SER   A O   1 
ATOM   271  C  CB  . SER   A 1 38  ? -6.668  0.955   -2.009  1.00 53.84  ? 81  SER   A CB  1 
ATOM   272  O  OG  . SER   A 1 38  ? -6.140  1.108   -0.721  1.00 56.43  ? 81  SER   A OG  1 
ATOM   273  N  N   . GLY   A 1 39  ? -8.391  -1.472  -3.883  1.00 48.84  ? 82  GLY   A N   1 
ATOM   274  C  CA  . GLY   A 1 39  ? -8.921  -1.745  -5.241  1.00 47.39  ? 82  GLY   A CA  1 
ATOM   275  C  C   . GLY   A 1 39  ? -7.938  -1.459  -6.382  1.00 48.63  ? 82  GLY   A C   1 
ATOM   276  O  O   . GLY   A 1 39  ? -8.381  -1.452  -7.536  1.00 47.75  ? 82  GLY   A O   1 
ATOM   277  N  N   . ASP   A 1 40  ? -6.639  -1.254  -6.096  1.00 50.72  ? 83  ASP   A N   1 
ATOM   278  C  CA  . ASP   A 1 40  ? -5.579  -1.054  -7.118  1.00 52.41  ? 83  ASP   A CA  1 
ATOM   279  C  C   . ASP   A 1 40  ? -5.042  -2.409  -7.597  1.00 51.19  ? 83  ASP   A C   1 
ATOM   280  O  O   . ASP   A 1 40  ? -4.504  -3.141  -6.771  1.00 50.82  ? 83  ASP   A O   1 
ATOM   281  C  CB  . ASP   A 1 40  ? -4.402  -0.229  -6.588  1.00 55.28  ? 83  ASP   A CB  1 
ATOM   282  C  CG  . ASP   A 1 40  ? -4.830  1.068   -5.943  1.00 55.95  ? 83  ASP   A CG  1 
ATOM   283  O  OD1 . ASP   A 1 40  ? -5.339  1.909   -6.668  1.00 54.88  ? 83  ASP   A OD1 1 
ATOM   284  O  OD2 . ASP   A 1 40  ? -4.657  1.196   -4.713  1.00 58.56  ? 83  ASP   A OD2 1 
ATOM   285  N  N   . PHE   A 1 41  ? -5.158  -2.683  -8.897  1.00 51.20  ? 84  PHE   A N   1 
ATOM   286  C  CA  . PHE   A 1 41  ? -4.466  -3.788  -9.601  1.00 51.53  ? 84  PHE   A CA  1 
ATOM   287  C  C   . PHE   A 1 41  ? -3.003  -3.404  -9.837  1.00 54.91  ? 84  PHE   A C   1 
ATOM   288  O  O   . PHE   A 1 41  ? -2.709  -2.216  -10.011 1.00 56.48  ? 84  PHE   A O   1 
ATOM   289  C  CB  . PHE   A 1 41  ? -5.176  -4.111  -10.903 1.00 49.89  ? 84  PHE   A CB  1 
ATOM   290  C  CG  . PHE   A 1 41  ? -6.448  -4.900  -10.747 1.00 49.04  ? 84  PHE   A CG  1 
ATOM   291  C  CD1 . PHE   A 1 41  ? -6.415  -6.216  -10.315 1.00 48.14  ? 84  PHE   A CD1 1 
ATOM   292  C  CD2 . PHE   A 1 41  ? -7.680  -4.340  -11.068 1.00 48.92  ? 84  PHE   A CD2 1 
ATOM   293  C  CE1 . PHE   A 1 41  ? -7.590  -6.946  -10.212 1.00 48.99  ? 84  PHE   A CE1 1 
ATOM   294  C  CE2 . PHE   A 1 41  ? -8.854  -5.067  -10.924 1.00 46.68  ? 84  PHE   A CE2 1 
ATOM   295  C  CZ  . PHE   A 1 41  ? -8.804  -6.376  -10.550 1.00 46.09  ? 84  PHE   A CZ  1 
ATOM   296  N  N   . SER   A 1 42  ? -2.110  -4.391  -9.813  1.00 56.29  ? 85  SER   A N   1 
ATOM   297  C  CA  . SER   A 1 42  ? -0.676  -4.225  -10.146 1.00 58.20  ? 85  SER   A CA  1 
ATOM   298  C  C   . SER   A 1 42  ? -0.117  -5.506  -10.779 1.00 59.33  ? 85  SER   A C   1 
ATOM   299  O  O   . SER   A 1 42  ? -0.653  -6.598  -10.503 1.00 55.69  ? 85  SER   A O   1 
ATOM   300  C  CB  . SER   A 1 42  ? 0.084   -3.852  -8.926  1.00 59.99  ? 85  SER   A CB  1 
ATOM   301  O  OG  . SER   A 1 42  ? -0.091  -4.822  -7.915  1.00 59.82  ? 85  SER   A OG  1 
ATOM   302  N  N   . LEU   A 1 43  ? 0.918   -5.358  -11.616 1.00 63.06  ? 86  LEU   A N   1 
ATOM   303  C  CA  . LEU   A 1 43  ? 1.603   -6.489  -12.289 1.00 63.83  ? 86  LEU   A CA  1 
ATOM   304  C  C   . LEU   A 1 43  ? 2.575   -7.129  -11.299 1.00 65.18  ? 86  LEU   A C   1 
ATOM   305  O  O   . LEU   A 1 43  ? 3.459   -6.430  -10.771 1.00 64.94  ? 86  LEU   A O   1 
ATOM   306  C  CB  . LEU   A 1 43  ? 2.339   -5.987  -13.531 1.00 66.12  ? 86  LEU   A CB  1 
ATOM   307  C  CG  . LEU   A 1 43  ? 1.471   -5.372  -14.619 1.00 66.77  ? 86  LEU   A CG  1 
ATOM   308  C  CD1 . LEU   A 1 43  ? 2.303   -4.968  -15.815 1.00 69.86  ? 86  LEU   A CD1 1 
ATOM   309  C  CD2 . LEU   A 1 43  ? 0.380   -6.332  -15.055 1.00 67.18  ? 86  LEU   A CD2 1 
ATOM   310  N  N   . VAL   A 1 44  ? 2.404   -8.423  -11.069 1.00 67.22  ? 87  VAL   A N   1 
ATOM   311  C  CA  . VAL   A 1 44  ? 3.424   -9.332  -10.454 1.00 72.12  ? 87  VAL   A CA  1 
ATOM   312  C  C   . VAL   A 1 44  ? 4.406   -9.779  -11.559 1.00 75.64  ? 87  VAL   A C   1 
ATOM   313  O  O   . VAL   A 1 44  ? 3.999   -9.746  -12.739 1.00 79.58  ? 87  VAL   A O   1 
ATOM   314  C  CB  . VAL   A 1 44  ? 2.646   -10.501 -9.825  1.00 69.86  ? 87  VAL   A CB  1 
ATOM   315  C  CG1 . VAL   A 1 44  ? 3.558   -11.543 -9.196  1.00 71.49  ? 87  VAL   A CG1 1 
ATOM   316  C  CG2 . VAL   A 1 44  ? 1.603   -9.980  -8.839  1.00 67.05  ? 87  VAL   A CG2 1 
ATOM   317  N  N   . GLU   A 1 45  ? 5.657   -10.137 -11.258 1.00 82.70  ? 88  GLU   A N   1 
ATOM   318  C  CA  . GLU   A 1 45  ? 6.542   -10.886 -12.225 1.00 84.80  ? 88  GLU   A CA  1 
ATOM   319  C  C   . GLU   A 1 45  ? 7.466   -11.832 -11.445 1.00 85.30  ? 88  GLU   A C   1 
ATOM   320  O  O   . GLU   A 1 45  ? 7.033   -12.481 -10.482 1.00 81.27  ? 88  GLU   A O   1 
ATOM   321  C  CB  . GLU   A 1 45  ? 7.389   -9.994  -13.150 1.00 86.93  ? 88  GLU   A CB  1 
ATOM   322  C  CG  . GLU   A 1 45  ? 6.694   -8.750  -13.718 1.00 87.74  ? 88  GLU   A CG  1 
ATOM   323  C  CD  . GLU   A 1 45  ? 6.073   -8.831  -15.108 1.00 85.44  ? 88  GLU   A CD  1 
ATOM   324  O  OE1 . GLU   A 1 45  ? 4.985   -9.395  -15.216 1.00 86.53  ? 88  GLU   A OE1 1 
ATOM   325  O  OE2 . GLU   A 1 45  ? 6.652   -8.289  -16.074 1.00 89.18  ? 88  GLU   A OE2 1 
ATOM   326  N  N   . GLY   B 2 7   ? -36.801 12.078  -12.075 1.00 79.45  ? 16  GLY   B N   1 
ATOM   327  C  CA  . GLY   B 2 7   ? -35.521 11.842  -12.831 1.00 78.11  ? 16  GLY   B CA  1 
ATOM   328  C  C   . GLY   B 2 7   ? -35.665 10.832  -13.972 1.00 77.51  ? 16  GLY   B C   1 
ATOM   329  O  O   . GLY   B 2 7   ? -36.632 10.017  -13.951 1.00 82.87  ? 16  GLY   B O   1 
ATOM   330  N  N   . GLU   B 2 8   ? -34.727 10.859  -14.927 1.00 70.35  ? 17  GLU   B N   1 
ATOM   331  C  CA  . GLU   B 2 8   ? -34.626 9.880   -16.055 1.00 69.00  ? 17  GLU   B CA  1 
ATOM   332  C  C   . GLU   B 2 8   ? -34.208 8.492   -15.526 1.00 64.21  ? 17  GLU   B C   1 
ATOM   333  O  O   . GLU   B 2 8   ? -33.071 8.317   -15.063 1.00 63.52  ? 17  GLU   B O   1 
ATOM   334  C  CB  . GLU   B 2 8   ? -33.635 10.347  -17.131 1.00 70.94  ? 17  GLU   B CB  1 
ATOM   335  C  CG  . GLU   B 2 8   ? -33.683 9.500   -18.394 1.00 72.22  ? 17  GLU   B CG  1 
ATOM   336  C  CD  . GLU   B 2 8   ? -32.984 10.092  -19.610 1.00 76.21  ? 17  GLU   B CD  1 
ATOM   337  O  OE1 . GLU   B 2 8   ? -32.067 10.949  -19.447 1.00 72.54  ? 17  GLU   B OE1 1 
ATOM   338  O  OE2 . GLU   B 2 8   ? -33.376 9.705   -20.738 1.00 82.92  ? 17  GLU   B OE2 1 
ATOM   339  N  N   A THR   B 2 9   ? -35.120 7.521   -15.596 0.25 63.40  ? 18  THR   B N   1 
ATOM   340  N  N   B THR   B 2 9   ? -35.122 7.528   -15.624 0.25 63.14  ? 18  THR   B N   1 
ATOM   341  N  N   C THR   B 2 9   ? -35.130 7.529   -15.602 0.25 63.49  ? 18  THR   B N   1 
ATOM   342  N  N   D THR   B 2 9   ? -35.133 7.534   -15.622 0.25 63.02  ? 18  THR   B N   1 
ATOM   343  C  CA  A THR   B 2 9   ? -34.912 6.134   -15.106 0.25 61.78  ? 18  THR   B CA  1 
ATOM   344  C  CA  B THR   B 2 9   ? -34.966 6.145   -15.109 0.25 61.38  ? 18  THR   B CA  1 
ATOM   345  C  CA  C THR   B 2 9   ? -34.961 6.137   -15.110 0.25 61.92  ? 18  THR   B CA  1 
ATOM   346  C  CA  D THR   B 2 9   ? -35.007 6.145   -15.113 0.25 61.17  ? 18  THR   B CA  1 
ATOM   347  C  C   A THR   B 2 9   ? -34.783 5.167   -16.283 0.25 60.42  ? 18  THR   B C   1 
ATOM   348  C  C   B THR   B 2 9   ? -34.835 5.169   -16.281 0.25 60.21  ? 18  THR   B C   1 
ATOM   349  C  C   C THR   B 2 9   ? -34.751 5.175   -16.280 0.25 60.48  ? 18  THR   B C   1 
ATOM   350  C  C   D THR   B 2 9   ? -34.797 5.175   -16.278 0.25 60.07  ? 18  THR   B C   1 
ATOM   351  O  O   A THR   B 2 9   ? -34.695 3.945   -16.026 0.25 60.16  ? 18  THR   B O   1 
ATOM   352  O  O   B THR   B 2 9   ? -34.785 3.945   -16.020 0.25 60.02  ? 18  THR   B O   1 
ATOM   353  O  O   C THR   B 2 9   ? -34.578 3.965   -16.014 0.25 60.19  ? 18  THR   B O   1 
ATOM   354  O  O   D THR   B 2 9   ? -34.661 3.961   -16.009 0.25 59.84  ? 18  THR   B O   1 
ATOM   355  C  CB  A THR   B 2 9   ? -36.061 5.695   -14.196 0.25 61.98  ? 18  THR   B CB  1 
ATOM   356  C  CB  B THR   B 2 9   ? -36.145 5.812   -14.190 0.25 61.28  ? 18  THR   B CB  1 
ATOM   357  C  CB  C THR   B 2 9   ? -36.187 5.679   -14.316 0.25 62.23  ? 18  THR   B CB  1 
ATOM   358  C  CB  D THR   B 2 9   ? -36.259 5.771   -14.314 0.25 60.96  ? 18  THR   B CB  1 
ATOM   359  O  OG1 A THR   B 2 9   ? -36.338 6.784   -13.315 0.25 61.91  ? 18  THR   B OG1 1 
ATOM   360  O  OG1 B THR   B 2 9   ? -37.339 6.215   -14.864 0.25 61.01  ? 18  THR   B OG1 1 
ATOM   361  O  OG1 C THR   B 2 9   ? -36.646 6.793   -13.548 0.25 62.19  ? 18  THR   B OG1 1 
ATOM   362  O  OG1 D THR   B 2 9   ? -37.392 6.030   -15.145 0.25 60.33  ? 18  THR   B OG1 1 
ATOM   363  C  CG2 A THR   B 2 9   ? -35.731 4.435   -13.425 0.25 61.85  ? 18  THR   B CG2 1 
ATOM   364  C  CG2 B THR   B 2 9   ? -36.038 6.507   -12.851 0.25 61.10  ? 18  THR   B CG2 1 
ATOM   365  C  CG2 C THR   B 2 9   ? -35.881 4.485   -13.436 0.25 62.29  ? 18  THR   B CG2 1 
ATOM   366  C  CG2 D THR   B 2 9   ? -36.370 6.543   -13.018 0.25 60.89  ? 18  THR   B CG2 1 
ATOM   367  N  N   . THR   B 2 10  ? -34.777 5.689   -17.513 1.00 58.95  ? 19  THR   B N   1 
ATOM   368  C  CA  . THR   B 2 10  ? -34.689 4.871   -18.740 1.00 56.43  ? 19  THR   B CA  1 
ATOM   369  C  C   . THR   B 2 10  ? -33.429 3.997   -18.693 1.00 51.63  ? 19  THR   B C   1 
ATOM   370  O  O   . THR   B 2 10  ? -32.333 4.555   -18.476 1.00 47.82  ? 19  THR   B O   1 
ATOM   371  C  CB  . THR   B 2 10  ? -34.679 5.773   -19.980 1.00 57.98  ? 19  THR   B CB  1 
ATOM   372  O  OG1 . THR   B 2 10  ? -35.771 6.697   -19.918 1.00 62.88  ? 19  THR   B OG1 1 
ATOM   373  C  CG2 . THR   B 2 10  ? -34.786 4.968   -21.252 1.00 59.14  ? 19  THR   B CG2 1 
ATOM   374  N  N   . ASP   B 2 11  ? -33.577 2.695   -18.953 1.00 49.56  ? 20  ASP   B N   1 
ATOM   375  C  CA  . ASP   B 2 11  ? -32.439 1.776   -19.181 1.00 49.33  ? 20  ASP   B CA  1 
ATOM   376  C  C   . ASP   B 2 11  ? -31.434 2.428   -20.153 1.00 49.05  ? 20  ASP   B C   1 
ATOM   377  O  O   . ASP   B 2 11  ? -31.859 3.267   -20.983 1.00 49.85  ? 20  ASP   B O   1 
ATOM   378  C  CB  . ASP   B 2 11  ? -32.943 0.417   -19.676 1.00 51.37  ? 20  ASP   B CB  1 
ATOM   379  C  CG  . ASP   B 2 11  ? -33.512 -0.457  -18.568 1.00 52.78  ? 20  ASP   B CG  1 
ATOM   380  O  OD1 . ASP   B 2 11  ? -33.816 0.090   -17.490 1.00 50.53  ? 20  ASP   B OD1 1 
ATOM   381  O  OD2 . ASP   B 2 11  ? -33.609 -1.688  -18.797 1.00 55.89  ? 20  ASP   B OD2 1 
ATOM   382  N  N   . GLY   B 2 12  ? -30.143 2.063   -20.077 1.00 46.59  ? 21  GLY   B N   1 
ATOM   383  C  CA  . GLY   B 2 12  ? -29.110 2.519   -21.019 1.00 44.76  ? 21  GLY   B CA  1 
ATOM   384  C  C   . GLY   B 2 12  ? -27.851 3.001   -20.346 1.00 43.28  ? 21  GLY   B C   1 
ATOM   385  O  O   . GLY   B 2 12  ? -27.712 2.882   -19.097 1.00 41.50  ? 21  GLY   B O   1 
ATOM   386  N  N   . VAL   B 2 13  ? -26.952 3.554   -21.160 1.00 43.09  ? 22  VAL   B N   1 
ATOM   387  C  CA  . VAL   B 2 13  ? -25.613 4.016   -20.714 1.00 42.50  ? 22  VAL   B CA  1 
ATOM   388  C  C   . VAL   B 2 13  ? -25.704 5.533   -20.548 1.00 43.21  ? 22  VAL   B C   1 
ATOM   389  O  O   . VAL   B 2 13  ? -26.465 6.180   -21.311 1.00 45.59  ? 22  VAL   B O   1 
ATOM   390  C  CB  . VAL   B 2 13  ? -24.532 3.506   -21.664 1.00 43.32  ? 22  VAL   B CB  1 
ATOM   391  C  CG1 . VAL   B 2 13  ? -24.674 4.088   -23.090 1.00 43.41  ? 22  VAL   B CG1 1 
ATOM   392  C  CG2 . VAL   B 2 13  ? -23.142 3.686   -21.069 1.00 43.03  ? 22  VAL   B CG2 1 
ATOM   393  N  N   . TYR   B 2 14  ? -25.080 6.053   -19.496 1.00 41.80  ? 23  TYR   B N   1 
ATOM   394  C  CA  . TYR   B 2 14  ? -25.117 7.477   -19.111 1.00 41.45  ? 23  TYR   B CA  1 
ATOM   395  C  C   . TYR   B 2 14  ? -23.698 7.978   -18.894 1.00 41.51  ? 23  TYR   B C   1 
ATOM   396  O  O   . TYR   B 2 14  ? -22.779 7.200   -18.561 1.00 41.29  ? 23  TYR   B O   1 
ATOM   397  C  CB  . TYR   B 2 14  ? -25.959 7.662   -17.853 1.00 41.17  ? 23  TYR   B CB  1 
ATOM   398  C  CG  . TYR   B 2 14  ? -27.445 7.482   -18.008 1.00 40.13  ? 23  TYR   B CG  1 
ATOM   399  C  CD1 . TYR   B 2 14  ? -27.997 6.256   -18.293 1.00 40.19  ? 23  TYR   B CD1 1 
ATOM   400  C  CD2 . TYR   B 2 14  ? -28.283 8.572   -17.915 1.00 40.70  ? 23  TYR   B CD2 1 
ATOM   401  C  CE1 . TYR   B 2 14  ? -29.357 6.091   -18.447 1.00 40.44  ? 23  TYR   B CE1 1 
ATOM   402  C  CE2 . TYR   B 2 14  ? -29.660 8.443   -18.070 1.00 41.30  ? 23  TYR   B CE2 1 
ATOM   403  C  CZ  . TYR   B 2 14  ? -30.195 7.193   -18.331 1.00 41.79  ? 23  TYR   B CZ  1 
ATOM   404  O  OH  . TYR   B 2 14  ? -31.550 7.037   -18.447 1.00 43.28  ? 23  TYR   B OH  1 
ATOM   405  N  N   . ARG   B 2 15  ? -23.506 9.259   -19.170 1.00 42.00  ? 24  ARG   B N   1 
ATOM   406  C  CA  . ARG   B 2 15  ? -22.286 9.979   -18.754 1.00 42.57  ? 24  ARG   B CA  1 
ATOM   407  C  C   . ARG   B 2 15  ? -22.462 10.470  -17.328 1.00 41.80  ? 24  ARG   B C   1 
ATOM   408  O  O   . ARG   B 2 15  ? -23.535 10.933  -16.987 1.00 39.75  ? 24  ARG   B O   1 
ATOM   409  C  CB  . ARG   B 2 15  ? -21.987 11.210  -19.605 1.00 43.65  ? 24  ARG   B CB  1 
ATOM   410  C  CG  . ARG   B 2 15  ? -21.939 10.950  -21.100 1.00 45.11  ? 24  ARG   B CG  1 
ATOM   411  C  CD  . ARG   B 2 15  ? -21.709 12.245  -21.863 1.00 46.07  ? 24  ARG   B CD  1 
ATOM   412  N  NE  . ARG   B 2 15  ? -21.867 11.998  -23.283 1.00 46.83  ? 24  ARG   B NE  1 
ATOM   413  C  CZ  . ARG   B 2 15  ? -20.916 11.688  -24.139 1.00 48.63  ? 24  ARG   B CZ  1 
ATOM   414  N  NH1 . ARG   B 2 15  ? -19.641 11.579  -23.779 1.00 49.38  ? 24  ARG   B NH1 1 
ATOM   415  N  NH2 . ARG   B 2 15  ? -21.259 11.435  -25.391 1.00 50.73  ? 24  ARG   B NH2 1 
ATOM   416  N  N   . VAL   B 2 16  ? -21.377 10.443  -16.566 1.00 42.36  ? 25  VAL   B N   1 
ATOM   417  C  CA  . VAL   B 2 16  ? -21.298 11.090  -15.235 1.00 43.23  ? 25  VAL   B CA  1 
ATOM   418  C  C   . VAL   B 2 16  ? -20.458 12.356  -15.369 1.00 42.80  ? 25  VAL   B C   1 
ATOM   419  O  O   . VAL   B 2 16  ? -19.280 12.247  -15.712 1.00 42.27  ? 25  VAL   B O   1 
ATOM   420  C  CB  . VAL   B 2 16  ? -20.751 10.101  -14.187 1.00 43.94  ? 25  VAL   B CB  1 
ATOM   421  C  CG1 . VAL   B 2 16  ? -20.803 10.675  -12.766 1.00 44.17  ? 25  VAL   B CG1 1 
ATOM   422  C  CG2 . VAL   B 2 16  ? -21.487 8.758   -14.271 1.00 43.47  ? 25  VAL   B CG2 1 
ATOM   423  N  N   . MET   B 2 17  ? -21.062 13.483  -15.022 1.00 43.28  ? 26  MET   B N   1 
ATOM   424  C  CA  . MET   B 2 17  ? -20.543 14.852  -15.246 1.00 45.76  ? 26  MET   B CA  1 
ATOM   425  C  C   . MET   B 2 17  ? -20.386 15.581  -13.910 1.00 45.83  ? 26  MET   B C   1 
ATOM   426  O  O   . MET   B 2 17  ? -21.235 15.418  -13.057 1.00 43.68  ? 26  MET   B O   1 
ATOM   427  C  CB  . MET   B 2 17  ? -21.520 15.668  -16.097 1.00 47.05  ? 26  MET   B CB  1 
ATOM   428  C  CG  . MET   B 2 17  ? -21.854 15.038  -17.479 1.00 48.30  ? 26  MET   B CG  1 
ATOM   429  S  SD  . MET   B 2 17  ? -20.505 14.717  -18.658 1.00 48.36  ? 26  MET   B SD  1 
ATOM   430  C  CE  . MET   B 2 17  ? -19.832 16.367  -18.898 1.00 50.85  ? 26  MET   B CE  1 
ATOM   431  N  N   . THR   B 2 18  ? -19.345 16.402  -13.788 1.00 48.22  ? 27  THR   B N   1 
ATOM   432  C  CA  . THR   B 2 18  ? -19.196 17.391  -12.701 1.00 51.89  ? 27  THR   B CA  1 
ATOM   433  C  C   . THR   B 2 18  ? -19.037 18.810  -13.276 1.00 54.25  ? 27  THR   B C   1 
ATOM   434  O  O   . THR   B 2 18  ? -18.386 18.975  -14.323 1.00 50.28  ? 27  THR   B O   1 
ATOM   435  C  CB  . THR   B 2 18  ? -18.021 17.030  -11.788 1.00 52.52  ? 27  THR   B CB  1 
ATOM   436  O  OG1 . THR   B 2 18  ? -18.220 17.921  -10.687 1.00 54.85  ? 27  THR   B OG1 1 
ATOM   437  C  CG2 . THR   B 2 18  ? -16.650 17.183  -12.424 1.00 52.48  ? 27  THR   B CG2 1 
ATOM   438  N  N   . ARG   B 2 19  ? -19.550 19.800  -12.549 1.00 59.15  ? 28  ARG   B N   1 
ATOM   439  C  CA  . ARG   B 2 19  ? -19.281 21.249  -12.793 1.00 68.61  ? 28  ARG   B CA  1 
ATOM   440  C  C   . ARG   B 2 19  ? -18.187 21.792  -11.843 1.00 72.40  ? 28  ARG   B C   1 
ATOM   441  O  O   . ARG   B 2 19  ? -17.699 22.893  -12.112 1.00 74.15  ? 28  ARG   B O   1 
ATOM   442  C  CB  . ARG   B 2 19  ? -20.619 21.990  -12.740 1.00 70.38  ? 28  ARG   B CB  1 
ATOM   443  C  CG  . ARG   B 2 19  ? -21.604 21.464  -13.775 1.00 74.47  ? 28  ARG   B CG  1 
ATOM   444  C  CD  . ARG   B 2 19  ? -21.977 22.483  -14.840 1.00 79.41  ? 28  ARG   B CD  1 
ATOM   445  N  NE  . ARG   B 2 19  ? -23.170 22.147  -15.624 1.00 83.07  ? 28  ARG   B NE  1 
ATOM   446  C  CZ  . ARG   B 2 19  ? -24.428 22.115  -15.161 1.00 86.33  ? 28  ARG   B CZ  1 
ATOM   447  N  NH1 . ARG   B 2 19  ? -24.697 22.351  -13.884 1.00 88.81  ? 28  ARG   B NH1 1 
ATOM   448  N  NH2 . ARG   B 2 19  ? -25.423 21.804  -15.977 1.00 86.98  ? 28  ARG   B NH2 1 
ATOM   449  N  N   . ARG   B 2 20  ? -17.712 21.004  -10.866 1.00 79.92  ? 29  ARG   B N   1 
ATOM   450  C  CA  . ARG   B 2 20  ? -16.765 21.441  -9.793  1.00 84.48  ? 29  ARG   B CA  1 
ATOM   451  C  C   . ARG   B 2 20  ? -15.432 21.926  -10.397 1.00 83.68  ? 29  ARG   B C   1 
ATOM   452  O  O   . ARG   B 2 20  ? -14.823 22.814  -9.788  1.00 84.72  ? 29  ARG   B O   1 
ATOM   453  C  CB  . ARG   B 2 20  ? -16.547 20.336  -8.750  1.00 88.09  ? 29  ARG   B CB  1 
ATOM   454  C  CG  . ARG   B 2 20  ? -16.485 20.856  -7.318  1.00 93.88  ? 29  ARG   B CG  1 
ATOM   455  C  CD  . ARG   B 2 20  ? -16.508 19.768  -6.256  1.00 101.55 ? 29  ARG   B CD  1 
ATOM   456  N  NE  . ARG   B 2 20  ? -15.571 18.653  -6.466  1.00 109.16 ? 29  ARG   B NE  1 
ATOM   457  C  CZ  . ARG   B 2 20  ? -14.343 18.545  -5.944  1.00 112.20 ? 29  ARG   B CZ  1 
ATOM   458  N  NH1 . ARG   B 2 20  ? -13.836 19.502  -5.184  1.00 115.07 ? 29  ARG   B NH1 1 
ATOM   459  N  NH2 . ARG   B 2 20  ? -13.613 17.470  -6.188  1.00 113.24 ? 29  ARG   B NH2 1 
ATOM   460  N  N   . LEU   B 2 21  ? -14.997 21.385  -11.543 1.00 79.95  ? 30  LEU   B N   1 
ATOM   461  C  CA  . LEU   B 2 21  ? -13.776 21.832  -12.279 1.00 75.85  ? 30  LEU   B CA  1 
ATOM   462  C  C   . LEU   B 2 21  ? -14.163 22.888  -13.326 1.00 72.43  ? 30  LEU   B C   1 
ATOM   463  O  O   . LEU   B 2 21  ? -15.262 23.429  -13.233 1.00 69.42  ? 30  LEU   B O   1 
ATOM   464  C  CB  . LEU   B 2 21  ? -13.121 20.607  -12.914 1.00 74.99  ? 30  LEU   B CB  1 
ATOM   465  C  CG  . LEU   B 2 21  ? -12.323 19.731  -11.956 1.00 78.03  ? 30  LEU   B CG  1 
ATOM   466  C  CD1 . LEU   B 2 21  ? -12.909 19.752  -10.553 1.00 77.51  ? 30  LEU   B CD1 1 
ATOM   467  C  CD2 . LEU   B 2 21  ? -12.223 18.297  -12.480 1.00 79.50  ? 30  LEU   B CD2 1 
ATOM   468  N  N   . LEU   B 2 22  ? -13.275 23.189  -14.279 1.00 72.17  ? 31  LEU   B N   1 
ATOM   469  C  CA  . LEU   B 2 22  ? -13.549 24.130  -15.396 1.00 69.06  ? 31  LEU   B CA  1 
ATOM   470  C  C   . LEU   B 2 22  ? -14.665 23.569  -16.279 1.00 66.63  ? 31  LEU   B C   1 
ATOM   471  O  O   . LEU   B 2 22  ? -14.700 22.325  -16.442 1.00 66.29  ? 31  LEU   B O   1 
ATOM   472  C  CB  . LEU   B 2 22  ? -12.274 24.314  -16.209 1.00 69.14  ? 31  LEU   B CB  1 
ATOM   473  C  CG  . LEU   B 2 22  ? -12.376 25.396  -17.274 1.00 69.47  ? 31  LEU   B CG  1 
ATOM   474  C  CD1 . LEU   B 2 22  ? -12.360 26.778  -16.644 1.00 68.57  ? 31  LEU   B CD1 1 
ATOM   475  C  CD2 . LEU   B 2 22  ? -11.255 25.236  -18.286 1.00 70.98  ? 31  LEU   B CD2 1 
ATOM   476  N  N   . GLY   B 2 23  ? -15.525 24.436  -16.839 1.00 63.80  ? 32  GLY   B N   1 
ATOM   477  C  CA  . GLY   B 2 23  ? -16.732 24.014  -17.587 1.00 60.53  ? 32  GLY   B CA  1 
ATOM   478  C  C   . GLY   B 2 23  ? -17.429 22.801  -16.952 1.00 56.85  ? 32  GLY   B C   1 
ATOM   479  O  O   . GLY   B 2 23  ? -17.513 22.730  -15.699 1.00 54.37  ? 32  GLY   B O   1 
ATOM   480  N  N   . SER   B 2 24  ? -17.966 21.907  -17.790 1.00 55.19  ? 33  SER   B N   1 
ATOM   481  C  CA  . SER   B 2 24  ? -18.592 20.611  -17.411 1.00 53.82  ? 33  SER   B CA  1 
ATOM   482  C  C   . SER   B 2 24  ? -17.631 19.506  -17.807 1.00 51.39  ? 33  SER   B C   1 
ATOM   483  O  O   . SER   B 2 24  ? -17.328 19.443  -19.001 1.00 50.05  ? 33  SER   B O   1 
ATOM   484  C  CB  . SER   B 2 24  ? -19.897 20.379  -18.098 1.00 53.77  ? 33  SER   B CB  1 
ATOM   485  O  OG  . SER   B 2 24  ? -20.844 21.328  -17.698 1.00 56.89  ? 33  SER   B OG  1 
ATOM   486  N  N   . THR   B 2 25  ? -17.190 18.687  -16.856 1.00 50.54  ? 34  THR   B N   1 
ATOM   487  C  CA  . THR   B 2 25  ? -16.145 17.659  -17.085 1.00 51.06  ? 34  THR   B CA  1 
ATOM   488  C  C   . THR   B 2 25  ? -16.744 16.275  -16.879 1.00 50.25  ? 34  THR   B C   1 
ATOM   489  O  O   . THR   B 2 25  ? -17.419 16.065  -15.837 1.00 50.55  ? 34  THR   B O   1 
ATOM   490  C  CB  . THR   B 2 25  ? -14.941 17.852  -16.167 1.00 52.33  ? 34  THR   B CB  1 
ATOM   491  O  OG1 . THR   B 2 25  ? -14.609 19.241  -16.234 1.00 53.44  ? 34  THR   B OG1 1 
ATOM   492  C  CG2 . THR   B 2 25  ? -13.770 16.974  -16.572 1.00 52.64  ? 34  THR   B CG2 1 
ATOM   493  N  N   . GLN   B 2 26  ? -16.506 15.377  -17.824 1.00 50.36  ? 35  GLN   B N   1 
ATOM   494  C  CA  . GLN   B 2 26  ? -16.972 13.981  -17.713 1.00 50.67  ? 35  GLN   B CA  1 
ATOM   495  C  C   . GLN   B 2 26  ? -15.981 13.211  -16.821 1.00 51.60  ? 35  GLN   B C   1 
ATOM   496  O  O   . GLN   B 2 26  ? -14.827 12.974  -17.253 1.00 51.49  ? 35  GLN   B O   1 
ATOM   497  C  CB  . GLN   B 2 26  ? -17.082 13.322  -19.082 1.00 51.41  ? 35  GLN   B CB  1 
ATOM   498  C  CG  . GLN   B 2 26  ? -17.719 11.939  -18.993 1.00 51.46  ? 35  GLN   B CG  1 
ATOM   499  C  CD  . GLN   B 2 26  ? -17.975 11.277  -20.324 1.00 51.02  ? 35  GLN   B CD  1 
ATOM   500  O  OE1 . GLN   B 2 26  ? -18.685 11.793  -21.169 1.00 53.03  ? 35  GLN   B OE1 1 
ATOM   501  N  NE2 . GLN   B 2 26  ? -17.459 10.088  -20.503 1.00 51.47  ? 35  GLN   B NE2 1 
ATOM   502  N  N   . VAL   B 2 27  ? -16.416 12.827  -15.621 1.00 50.18  ? 36  VAL   B N   1 
ATOM   503  C  CA  . VAL   B 2 27  ? -15.563 12.077  -14.647 1.00 49.14  ? 36  VAL   B CA  1 
ATOM   504  C  C   . VAL   B 2 27  ? -15.717 10.560  -14.885 1.00 46.48  ? 36  VAL   B C   1 
ATOM   505  O  O   . VAL   B 2 27  ? -14.763 9.834   -14.624 1.00 46.92  ? 36  VAL   B O   1 
ATOM   506  C  CB  . VAL   B 2 27  ? -15.885 12.528  -13.209 1.00 50.28  ? 36  VAL   B CB  1 
ATOM   507  C  CG1 . VAL   B 2 27  ? -15.627 14.017  -13.054 1.00 53.21  ? 36  VAL   B CG1 1 
ATOM   508  C  CG2 . VAL   B 2 27  ? -17.308 12.220  -12.794 1.00 48.78  ? 36  VAL   B CG2 1 
ATOM   509  N  N   . GLY   B 2 28  ? -16.797 10.109  -15.520 1.00 44.80  ? 37  GLY   B N   1 
ATOM   510  C  CA  . GLY   B 2 28  ? -16.956 8.711   -15.986 1.00 43.32  ? 37  GLY   B CA  1 
ATOM   511  C  C   . GLY   B 2 28  ? -18.308 8.438   -16.631 1.00 42.65  ? 37  GLY   B C   1 
ATOM   512  O  O   . GLY   B 2 28  ? -18.973 9.412   -17.077 1.00 42.98  ? 37  GLY   B O   1 
ATOM   513  N  N   . VAL   B 2 29  ? -18.744 7.165   -16.559 1.00 41.32  ? 38  VAL   B N   1 
ATOM   514  C  CA  . VAL   B 2 29  ? -19.893 6.520   -17.261 1.00 40.22  ? 38  VAL   B CA  1 
ATOM   515  C  C   . VAL   B 2 29  ? -20.559 5.516   -16.313 1.00 39.59  ? 38  VAL   B C   1 
ATOM   516  O  O   . VAL   B 2 29  ? -19.889 4.963   -15.414 1.00 39.05  ? 38  VAL   B O   1 
ATOM   517  C  CB  . VAL   B 2 29  ? -19.405 5.792   -18.522 1.00 41.46  ? 38  VAL   B CB  1 
ATOM   518  C  CG1 . VAL   B 2 29  ? -20.544 5.191   -19.349 1.00 41.83  ? 38  VAL   B CG1 1 
ATOM   519  C  CG2 . VAL   B 2 29  ? -18.474 6.644   -19.371 1.00 41.46  ? 38  VAL   B CG2 1 
ATOM   520  N  N   . GLY   B 2 30  ? -21.857 5.289   -16.463 1.00 39.07  ? 39  GLY   B N   1 
ATOM   521  C  CA  . GLY   B 2 30  ? -22.553 4.186   -15.795 1.00 38.48  ? 39  GLY   B CA  1 
ATOM   522  C  C   . GLY   B 2 30  ? -23.695 3.645   -16.615 1.00 38.45  ? 39  GLY   B C   1 
ATOM   523  O  O   . GLY   B 2 30  ? -23.903 4.160   -17.746 1.00 39.05  ? 39  GLY   B O   1 
ATOM   524  N  N   . VAL   B 2 31  ? -24.375 2.640   -16.050 1.00 37.74  ? 40  VAL   B N   1 
ATOM   525  C  CA  . VAL   B 2 31  ? -25.448 1.801   -16.655 1.00 37.70  ? 40  VAL   B CA  1 
ATOM   526  C  C   . VAL   B 2 31  ? -26.692 1.880   -15.770 1.00 37.61  ? 40  VAL   B C   1 
ATOM   527  O  O   . VAL   B 2 31  ? -26.600 1.574   -14.513 1.00 36.47  ? 40  VAL   B O   1 
ATOM   528  C  CB  . VAL   B 2 31  ? -25.059 0.318   -16.771 1.00 38.01  ? 40  VAL   B CB  1 
ATOM   529  C  CG1 . VAL   B 2 31  ? -26.229 -0.527  -17.219 1.00 38.47  ? 40  VAL   B CG1 1 
ATOM   530  C  CG2 . VAL   B 2 31  ? -23.870 0.082   -17.653 1.00 38.64  ? 40  VAL   B CG2 1 
ATOM   531  N  N   . MET   B 2 32  ? -27.810 2.328   -16.350 1.00 38.24  ? 41  MET   B N   1 
ATOM   532  C  CA  . MET   B 2 32  ? -29.120 2.319   -15.675 1.00 39.05  ? 41  MET   B CA  1 
ATOM   533  C  C   . MET   B 2 32  ? -29.808 1.019   -16.065 1.00 39.56  ? 41  MET   B C   1 
ATOM   534  O  O   . MET   B 2 32  ? -29.923 0.769   -17.271 1.00 39.61  ? 41  MET   B O   1 
ATOM   535  C  CB  . MET   B 2 32  ? -29.998 3.496   -16.119 1.00 40.49  ? 41  MET   B CB  1 
ATOM   536  C  CG  . MET   B 2 32  ? -31.233 3.673   -15.257 1.00 42.08  ? 41  MET   B CG  1 
ATOM   537  S  SD  . MET   B 2 32  ? -30.898 4.295   -13.580 1.00 44.31  ? 41  MET   B SD  1 
ATOM   538  C  CE  . MET   B 2 32  ? -30.409 5.990   -13.907 1.00 43.81  ? 41  MET   B CE  1 
ATOM   539  N  N   . GLN   B 2 33  ? -30.227 0.210   -15.101 1.00 41.09  ? 42  GLN   B N   1 
ATOM   540  C  CA  . GLN   B 2 33  ? -30.942 -1.059  -15.404 1.00 43.01  ? 42  GLN   B CA  1 
ATOM   541  C  C   . GLN   B 2 33  ? -31.868 -1.369  -14.246 1.00 43.21  ? 42  GLN   B C   1 
ATOM   542  O  O   . GLN   B 2 33  ? -31.433 -1.266  -13.069 1.00 41.73  ? 42  GLN   B O   1 
ATOM   543  C  CB  . GLN   B 2 33  ? -29.987 -2.235  -15.659 1.00 44.46  ? 42  GLN   B CB  1 
ATOM   544  C  CG  . GLN   B 2 33  ? -30.737 -3.437  -16.204 1.00 46.98  ? 42  GLN   B CG  1 
ATOM   545  C  CD  . GLN   B 2 33  ? -29.835 -4.576  -16.625 1.00 49.87  ? 42  GLN   B CD  1 
ATOM   546  O  OE1 . GLN   B 2 33  ? -29.925 -5.694  -16.120 1.00 52.94  ? 42  GLN   B OE1 1 
ATOM   547  N  NE2 . GLN   B 2 33  ? -28.959 -4.315  -17.574 1.00 50.99  ? 42  GLN   B NE2 1 
ATOM   548  N  N   . GLU   B 2 34  ? -33.112 -1.691  -14.565 1.00 45.23  ? 43  GLU   B N   1 
ATOM   549  C  CA  . GLU   B 2 34  ? -34.133 -2.029  -13.551 1.00 46.60  ? 43  GLU   B CA  1 
ATOM   550  C  C   . GLU   B 2 34  ? -34.189 -0.903  -12.501 1.00 45.37  ? 43  GLU   B C   1 
ATOM   551  O  O   . GLU   B 2 34  ? -34.348 -1.224  -11.339 1.00 44.28  ? 43  GLU   B O   1 
ATOM   552  C  CB  . GLU   B 2 34  ? -33.807 -3.412  -12.954 1.00 49.64  ? 43  GLU   B CB  1 
ATOM   553  C  CG  . GLU   B 2 34  ? -33.908 -4.585  -13.949 1.00 52.53  ? 43  GLU   B CG  1 
ATOM   554  C  CD  . GLU   B 2 34  ? -33.380 -5.937  -13.473 1.00 55.94  ? 43  GLU   B CD  1 
ATOM   555  O  OE1 . GLU   B 2 34  ? -33.926 -6.456  -12.499 1.00 60.61  ? 43  GLU   B OE1 1 
ATOM   556  O  OE2 . GLU   B 2 34  ? -32.403 -6.475  -14.055 1.00 56.95  ? 43  GLU   B OE2 1 
ATOM   557  N  N   . GLY   B 2 35  ? -34.068 0.374   -12.882 1.00 43.53  ? 44  GLY   B N   1 
ATOM   558  C  CA  . GLY   B 2 35  ? -34.265 1.497   -11.943 1.00 42.51  ? 44  GLY   B CA  1 
ATOM   559  C  C   . GLY   B 2 35  ? -33.068 1.758   -11.046 1.00 41.65  ? 44  GLY   B C   1 
ATOM   560  O  O   . GLY   B 2 35  ? -33.175 2.649   -10.161 1.00 41.32  ? 44  GLY   B O   1 
ATOM   561  N  N   . VAL   B 2 36  ? -31.946 1.065   -11.279 1.00 39.68  ? 45  VAL   B N   1 
ATOM   562  C  CA  . VAL   B 2 36  ? -30.688 1.157   -10.486 1.00 38.06  ? 45  VAL   B CA  1 
ATOM   563  C  C   . VAL   B 2 36  ? -29.564 1.675   -11.398 1.00 36.89  ? 45  VAL   B C   1 
ATOM   564  O  O   . VAL   B 2 36  ? -29.444 1.193   -12.571 1.00 37.20  ? 45  VAL   B O   1 
ATOM   565  C  CB  . VAL   B 2 36  ? -30.340 -0.219  -9.873  1.00 39.22  ? 45  VAL   B CB  1 
ATOM   566  C  CG1 . VAL   B 2 36  ? -28.903 -0.313  -9.361  1.00 38.94  ? 45  VAL   B CG1 1 
ATOM   567  C  CG2 . VAL   B 2 36  ? -31.323 -0.573  -8.750  1.00 39.84  ? 45  VAL   B CG2 1 
ATOM   568  N  N   . PHE   B 2 37  ? -28.790 2.636   -10.897 1.00 35.08  ? 46  PHE   B N   1 
ATOM   569  C  CA  . PHE   B 2 37  ? -27.645 3.205   -11.628 1.00 34.67  ? 46  PHE   B CA  1 
ATOM   570  C  C   . PHE   B 2 37  ? -26.387 2.517   -11.099 1.00 33.94  ? 46  PHE   B C   1 
ATOM   571  O  O   . PHE   B 2 37  ? -26.201 2.512   -9.899  1.00 33.90  ? 46  PHE   B O   1 
ATOM   572  C  CB  . PHE   B 2 37  ? -27.555 4.721   -11.468 1.00 34.02  ? 46  PHE   B CB  1 
ATOM   573  C  CG  . PHE   B 2 37  ? -26.525 5.298   -12.395 1.00 33.89  ? 46  PHE   B CG  1 
ATOM   574  C  CD1 . PHE   B 2 37  ? -26.690 5.195   -13.743 1.00 34.19  ? 46  PHE   B CD1 1 
ATOM   575  C  CD2 . PHE   B 2 37  ? -25.390 5.903   -11.910 1.00 33.88  ? 46  PHE   B CD2 1 
ATOM   576  C  CE1 . PHE   B 2 37  ? -25.752 5.706   -14.617 1.00 35.08  ? 46  PHE   B CE1 1 
ATOM   577  C  CE2 . PHE   B 2 37  ? -24.442 6.408   -12.773 1.00 34.14  ? 46  PHE   B CE2 1 
ATOM   578  C  CZ  . PHE   B 2 37  ? -24.631 6.321   -14.120 1.00 34.97  ? 46  PHE   B CZ  1 
ATOM   579  N  N   . HIS   B 2 38  ? -25.569 2.020   -11.992 1.00 34.71  ? 47  HIS   B N   1 
ATOM   580  C  CA  . HIS   B 2 38  ? -24.366 1.196   -11.716 1.00 34.38  ? 47  HIS   B CA  1 
ATOM   581  C  C   . HIS   B 2 38  ? -23.150 1.925   -12.266 1.00 34.65  ? 47  HIS   B C   1 
ATOM   582  O  O   . HIS   B 2 38  ? -23.149 2.278   -13.469 1.00 34.40  ? 47  HIS   B O   1 
ATOM   583  C  CB  . HIS   B 2 38  ? -24.465 -0.142  -12.390 1.00 34.69  ? 47  HIS   B CB  1 
ATOM   584  C  CG  . HIS   B 2 38  ? -25.661 -0.947  -12.078 1.00 35.64  ? 47  HIS   B CG  1 
ATOM   585  N  ND1 . HIS   B 2 38  ? -26.913 -0.641  -12.554 1.00 36.96  ? 47  HIS   B ND1 1 
ATOM   586  C  CD2 . HIS   B 2 38  ? -25.798 -2.113  -11.406 1.00 36.34  ? 47  HIS   B CD2 1 
ATOM   587  C  CE1 . HIS   B 2 38  ? -27.781 -1.546  -12.151 1.00 37.09  ? 47  HIS   B CE1 1 
ATOM   588  N  NE2 . HIS   B 2 38  ? -27.131 -2.428  -11.393 1.00 37.08  ? 47  HIS   B NE2 1 
ATOM   589  N  N   . THR   B 2 39  ? -22.153 2.187   -11.437 1.00 35.04  ? 48  THR   B N   1 
ATOM   590  C  CA  . THR   B 2 39  ? -20.915 2.828   -11.945 1.00 36.29  ? 48  THR   B CA  1 
ATOM   591  C  C   . THR   B 2 39  ? -19.742 2.255   -11.160 1.00 37.25  ? 48  THR   B C   1 
ATOM   592  O  O   . THR   B 2 39  ? -19.975 1.303   -10.352 1.00 36.98  ? 48  THR   B O   1 
ATOM   593  C  CB  . THR   B 2 39  ? -21.094 4.352   -12.002 1.00 36.43  ? 48  THR   B CB  1 
ATOM   594  O  OG1 . THR   B 2 39  ? -19.990 4.937   -12.686 1.00 36.99  ? 48  THR   B OG1 1 
ATOM   595  C  CG2 . THR   B 2 39  ? -21.192 4.981   -10.646 1.00 37.02  ? 48  THR   B CG2 1 
ATOM   596  N  N   . MET   B 2 40  ? -18.546 2.796   -11.375 1.00 38.79  ? 49  MET   B N   1 
ATOM   597  C  CA  . MET   B 2 40  ? -17.362 2.477   -10.551 1.00 39.76  ? 49  MET   B CA  1 
ATOM   598  C  C   . MET   B 2 40  ? -17.206 3.471   -9.392  1.00 40.17  ? 49  MET   B C   1 
ATOM   599  O  O   . MET   B 2 40  ? -17.481 4.692   -9.565  1.00 40.45  ? 49  MET   B O   1 
ATOM   600  C  CB  . MET   B 2 40  ? -16.139 2.466   -11.466 1.00 40.30  ? 49  MET   B CB  1 
ATOM   601  C  CG  . MET   B 2 40  ? -16.371 1.551   -12.672 1.00 42.11  ? 49  MET   B CG  1 
ATOM   602  S  SD  . MET   B 2 40  ? -14.888 0.845   -13.380 1.00 46.58  ? 49  MET   B SD  1 
ATOM   603  C  CE  . MET   B 2 40  ? -14.759 -0.672  -12.437 1.00 44.83  ? 49  MET   B CE  1 
ATOM   604  N  N   A TRP   B 2 41  ? -16.778 2.979   -8.218  0.25 40.11  ? 50  TRP   B N   1 
ATOM   605  N  N   B TRP   B 2 41  ? -16.757 2.965   -8.244  0.25 39.80  ? 50  TRP   B N   1 
ATOM   606  N  N   C TRP   B 2 41  ? -16.778 2.979   -8.218  0.25 40.11  ? 50  TRP   B N   1 
ATOM   607  N  N   D TRP   B 2 41  ? -16.757 2.965   -8.244  0.25 39.80  ? 50  TRP   B N   1 
ATOM   608  C  CA  A TRP   B 2 41  ? -16.609 3.784   -6.972  0.25 40.31  ? 50  TRP   B CA  1 
ATOM   609  C  CA  B TRP   B 2 41  ? -16.614 3.750   -6.993  0.25 39.76  ? 50  TRP   B CA  1 
ATOM   610  C  CA  C TRP   B 2 41  ? -16.609 3.784   -6.972  0.25 40.31  ? 50  TRP   B CA  1 
ATOM   611  C  CA  D TRP   B 2 41  ? -16.614 3.750   -6.993  0.25 39.76  ? 50  TRP   B CA  1 
ATOM   612  C  C   A TRP   B 2 41  ? -15.697 4.985   -7.246  0.25 40.58  ? 50  TRP   B C   1 
ATOM   613  C  C   B TRP   B 2 41  ? -15.688 4.956   -7.220  0.25 40.25  ? 50  TRP   B C   1 
ATOM   614  C  C   C TRP   B 2 41  ? -15.697 4.985   -7.246  0.25 40.58  ? 50  TRP   B C   1 
ATOM   615  C  C   D TRP   B 2 41  ? -15.688 4.956   -7.220  0.25 40.25  ? 50  TRP   B C   1 
ATOM   616  O  O   A TRP   B 2 41  ? -16.029 6.091   -6.792  0.25 40.58  ? 50  TRP   B O   1 
ATOM   617  O  O   B TRP   B 2 41  ? -16.012 6.045   -6.717  0.25 40.23  ? 50  TRP   B O   1 
ATOM   618  O  O   C TRP   B 2 41  ? -16.029 6.091   -6.792  0.25 40.58  ? 50  TRP   B O   1 
ATOM   619  O  O   D TRP   B 2 41  ? -16.012 6.045   -6.717  0.25 40.23  ? 50  TRP   B O   1 
ATOM   620  C  CB  A TRP   B 2 41  ? -16.057 2.958   -5.794  0.25 40.41  ? 50  TRP   B CB  1 
ATOM   621  C  CB  B TRP   B 2 41  ? -16.120 2.876   -5.832  0.25 39.45  ? 50  TRP   B CB  1 
ATOM   622  C  CB  C TRP   B 2 41  ? -16.057 2.958   -5.794  0.25 40.41  ? 50  TRP   B CB  1 
ATOM   623  C  CB  D TRP   B 2 41  ? -16.120 2.876   -5.832  0.25 39.45  ? 50  TRP   B CB  1 
ATOM   624  C  CG  A TRP   B 2 41  ? -16.111 3.671   -4.469  0.25 40.67  ? 50  TRP   B CG  1 
ATOM   625  C  CG  B TRP   B 2 41  ? -16.011 3.682   -4.578  0.25 39.35  ? 50  TRP   B CG  1 
ATOM   626  C  CG  C TRP   B 2 41  ? -16.111 3.671   -4.469  0.25 40.67  ? 50  TRP   B CG  1 
ATOM   627  C  CG  D TRP   B 2 41  ? -16.011 3.682   -4.578  0.25 39.35  ? 50  TRP   B CG  1 
ATOM   628  C  CD1 A TRP   B 2 41  ? -17.117 3.595   -3.552  0.25 40.69  ? 50  TRP   B CD1 1 
ATOM   629  C  CD1 B TRP   B 2 41  ? -14.945 4.436   -4.186  0.25 39.54  ? 50  TRP   B CD1 1 
ATOM   630  C  CD1 C TRP   B 2 41  ? -17.117 3.595   -3.552  0.25 40.69  ? 50  TRP   B CD1 1 
ATOM   631  C  CD1 D TRP   B 2 41  ? -14.945 4.436   -4.186  0.25 39.54  ? 50  TRP   B CD1 1 
ATOM   632  C  CD2 A TRP   B 2 41  ? -15.139 4.580   -3.907  0.25 41.13  ? 50  TRP   B CD2 1 
ATOM   633  C  CD2 B TRP   B 2 41  ? -17.051 3.919   -3.616  0.25 39.19  ? 50  TRP   B CD2 1 
ATOM   634  C  CD2 C TRP   B 2 41  ? -15.139 4.580   -3.907  0.25 41.13  ? 50  TRP   B CD2 1 
ATOM   635  C  CD2 D TRP   B 2 41  ? -17.051 3.919   -3.616  0.25 39.19  ? 50  TRP   B CD2 1 
ATOM   636  N  NE1 A TRP   B 2 41  ? -16.844 4.387   -2.466  0.25 40.88  ? 50  TRP   B NE1 1 
ATOM   637  N  NE1 B TRP   B 2 41  ? -15.228 5.086   -3.020  0.25 39.59  ? 50  TRP   B NE1 1 
ATOM   638  N  NE1 C TRP   B 2 41  ? -16.844 4.387   -2.466  0.25 40.88  ? 50  TRP   B NE1 1 
ATOM   639  N  NE1 D TRP   B 2 41  ? -15.228 5.086   -3.020  0.25 39.59  ? 50  TRP   B NE1 1 
ATOM   640  C  CE2 A TRP   B 2 41  ? -15.634 5.000   -2.653  0.25 41.44  ? 50  TRP   B CE2 1 
ATOM   641  C  CE2 B TRP   B 2 41  ? -16.517 4.796   -2.648  0.25 39.28  ? 50  TRP   B CE2 1 
ATOM   642  C  CE2 C TRP   B 2 41  ? -15.634 5.000   -2.653  0.25 41.44  ? 50  TRP   B CE2 1 
ATOM   643  C  CE2 D TRP   B 2 41  ? -16.517 4.796   -2.648  0.25 39.28  ? 50  TRP   B CE2 1 
ATOM   644  C  CE3 A TRP   B 2 41  ? -13.902 5.081   -4.328  0.25 42.01  ? 50  TRP   B CE3 1 
ATOM   645  C  CE3 B TRP   B 2 41  ? -18.366 3.458   -3.459  0.25 39.15  ? 50  TRP   B CE3 1 
ATOM   646  C  CE3 C TRP   B 2 41  ? -13.902 5.081   -4.328  0.25 42.01  ? 50  TRP   B CE3 1 
ATOM   647  C  CE3 D TRP   B 2 41  ? -18.366 3.458   -3.459  0.25 39.15  ? 50  TRP   B CE3 1 
ATOM   648  C  CZ2 A TRP   B 2 41  ? -14.933 5.884   -1.827  0.25 41.71  ? 50  TRP   B CZ2 1 
ATOM   649  C  CZ2 B TRP   B 2 41  ? -17.251 5.209   -1.539  0.25 39.07  ? 50  TRP   B CZ2 1 
ATOM   650  C  CZ2 C TRP   B 2 41  ? -14.933 5.884   -1.827  0.25 41.71  ? 50  TRP   B CZ2 1 
ATOM   651  C  CZ2 D TRP   B 2 41  ? -17.251 5.209   -1.539  0.25 39.07  ? 50  TRP   B CZ2 1 
ATOM   652  C  CZ3 A TRP   B 2 41  ? -13.213 5.956   -3.515  0.25 42.10  ? 50  TRP   B CZ3 1 
ATOM   653  C  CZ3 B TRP   B 2 41  ? -19.092 3.873   -2.364  0.25 38.59  ? 50  TRP   B CZ3 1 
ATOM   654  C  CZ3 C TRP   B 2 41  ? -13.213 5.956   -3.515  0.25 42.10  ? 50  TRP   B CZ3 1 
ATOM   655  C  CZ3 D TRP   B 2 41  ? -19.092 3.873   -2.364  0.25 38.59  ? 50  TRP   B CZ3 1 
ATOM   656  C  CH2 A TRP   B 2 41  ? -13.718 6.346   -2.279  0.25 41.92  ? 50  TRP   B CH2 1 
ATOM   657  C  CH2 B TRP   B 2 41  ? -18.538 4.735   -1.418  0.25 38.84  ? 50  TRP   B CH2 1 
ATOM   658  C  CH2 C TRP   B 2 41  ? -13.718 6.346   -2.279  0.25 41.92  ? 50  TRP   B CH2 1 
ATOM   659  C  CH2 D TRP   B 2 41  ? -18.538 4.735   -1.418  0.25 38.84  ? 50  TRP   B CH2 1 
ATOM   660  N  N   . HIS   B 2 42  ? -14.573 4.776   -7.929  1.00 40.45  ? 51  HIS   B N   1 
ATOM   661  C  CA  . HIS   B 2 42  ? -13.601 5.878   -8.147  1.00 41.83  ? 51  HIS   B CA  1 
ATOM   662  C  C   . HIS   B 2 42  ? -14.227 7.028   -8.980  1.00 43.28  ? 51  HIS   B C   1 
ATOM   663  O  O   . HIS   B 2 42  ? -13.704 8.132   -8.889  1.00 42.94  ? 51  HIS   B O   1 
ATOM   664  C  CB  . HIS   B 2 42  ? -12.283 5.368   -8.686  1.00 40.79  ? 51  HIS   B CB  1 
ATOM   665  C  CG  . HIS   B 2 42  ? -12.302 5.104   -10.137 1.00 41.23  ? 51  HIS   B CG  1 
ATOM   666  N  ND1 . HIS   B 2 42  ? -12.410 3.827   -10.656 1.00 40.27  ? 51  HIS   B ND1 1 
ATOM   667  C  CD2 . HIS   B 2 42  ? -12.158 5.954   -11.190 1.00 41.86  ? 51  HIS   B CD2 1 
ATOM   668  C  CE1 . HIS   B 2 42  ? -12.369 3.904   -11.970 1.00 41.07  ? 51  HIS   B CE1 1 
ATOM   669  N  NE2 . HIS   B 2 42  ? -12.229 5.219   -12.330 1.00 41.30  ? 51  HIS   B NE2 1 
ATOM   670  N  N   . VAL   B 2 43  ? -15.325 6.801   -9.703  1.00 42.38  ? 52  VAL   B N   1 
ATOM   671  C  CA  . VAL   B 2 43  ? -15.960 7.859   -10.521 1.00 42.45  ? 52  VAL   B CA  1 
ATOM   672  C  C   . VAL   B 2 43  ? -16.665 8.830   -9.575  1.00 41.90  ? 52  VAL   B C   1 
ATOM   673  O  O   . VAL   B 2 43  ? -16.404 10.047  -9.703  1.00 42.74  ? 52  VAL   B O   1 
ATOM   674  C  CB  . VAL   B 2 43  ? -16.886 7.250   -11.593 1.00 41.77  ? 52  VAL   B CB  1 
ATOM   675  C  CG1 . VAL   B 2 43  ? -17.802 8.291   -12.247 1.00 42.04  ? 52  VAL   B CG1 1 
ATOM   676  C  CG2 . VAL   B 2 43  ? -16.088 6.539   -12.642 1.00 41.97  ? 52  VAL   B CG2 1 
ATOM   677  N  N   . THR   B 2 44  ? -17.496 8.342   -8.644  1.00 40.85  ? 53  THR   B N   1 
ATOM   678  C  CA  . THR   B 2 44  ? -18.366 9.219   -7.802  1.00 40.25  ? 53  THR   B CA  1 
ATOM   679  C  C   . THR   B 2 44  ? -17.807 9.396   -6.380  1.00 41.06  ? 53  THR   B C   1 
ATOM   680  O  O   . THR   B 2 44  ? -18.244 10.365  -5.711  1.00 41.11  ? 53  THR   B O   1 
ATOM   681  C  CB  . THR   B 2 44  ? -19.805 8.697   -7.810  1.00 39.10  ? 53  THR   B CB  1 
ATOM   682  O  OG1 . THR   B 2 44  ? -19.842 7.478   -7.058  1.00 37.67  ? 53  THR   B OG1 1 
ATOM   683  C  CG2 . THR   B 2 44  ? -20.278 8.430   -9.224  1.00 38.68  ? 53  THR   B CG2 1 
ATOM   684  N  N   . LYS   B 2 45  ? -16.892 8.527   -5.941  1.00 42.41  ? 54  LYS   B N   1 
ATOM   685  C  CA  . LYS   B 2 45  ? -16.424 8.409   -4.526  1.00 45.93  ? 54  LYS   B CA  1 
ATOM   686  C  C   . LYS   B 2 45  ? -17.606 8.209   -3.576  1.00 43.85  ? 54  LYS   B C   1 
ATOM   687  O  O   . LYS   B 2 45  ? -17.486 8.618   -2.413  1.00 45.41  ? 54  LYS   B O   1 
ATOM   688  C  CB  . LYS   B 2 45  ? -15.667 9.655   -4.060  1.00 51.09  ? 54  LYS   B CB  1 
ATOM   689  C  CG  . LYS   B 2 45  ? -14.522 10.063  -4.958  1.00 56.98  ? 54  LYS   B CG  1 
ATOM   690  C  CD  . LYS   B 2 45  ? -13.274 9.315   -4.640  1.00 63.66  ? 54  LYS   B CD  1 
ATOM   691  C  CE  . LYS   B 2 45  ? -12.073 10.001  -5.257  1.00 69.61  ? 54  LYS   B CE  1 
ATOM   692  N  NZ  . LYS   B 2 45  ? -11.766 9.389   -6.578  1.00 74.54  ? 54  LYS   B NZ  1 
ATOM   693  N  N   . GLY   B 2 46  ? -18.725 7.666   -4.070  1.00 43.21  ? 55  GLY   B N   1 
ATOM   694  C  CA  . GLY   B 2 46  ? -19.928 7.386   -3.266  1.00 42.75  ? 55  GLY   B CA  1 
ATOM   695  C  C   . GLY   B 2 46  ? -20.838 8.591   -3.121  1.00 43.14  ? 55  GLY   B C   1 
ATOM   696  O  O   . GLY   B 2 46  ? -21.832 8.455   -2.401  1.00 45.35  ? 55  GLY   B O   1 
ATOM   697  N  N   . ALA   B 2 47  ? -20.571 9.718   -3.789  1.00 42.08  ? 56  ALA   B N   1 
ATOM   698  C  CA  . ALA   B 2 47  ? -21.410 10.939  -3.661  1.00 42.29  ? 56  ALA   B CA  1 
ATOM   699  C  C   . ALA   B 2 47  ? -22.792 10.713  -4.298  1.00 42.23  ? 56  ALA   B C   1 
ATOM   700  O  O   . ALA   B 2 47  ? -22.880 9.985   -5.315  1.00 40.55  ? 56  ALA   B O   1 
ATOM   701  C  CB  . ALA   B 2 47  ? -20.727 12.104  -4.342  1.00 42.64  ? 56  ALA   B CB  1 
ATOM   702  N  N   . ALA   B 2 48  ? -23.785 11.492  -3.873  1.00 42.39  ? 57  ALA   B N   1 
ATOM   703  C  CA  . ALA   B 2 48  ? -25.090 11.589  -4.547  1.00 44.18  ? 57  ALA   B CA  1 
ATOM   704  C  C   . ALA   B 2 48  ? -24.921 12.129  -5.968  1.00 45.31  ? 57  ALA   B C   1 
ATOM   705  O  O   . ALA   B 2 48  ? -23.883 12.770  -6.283  1.00 46.28  ? 57  ALA   B O   1 
ATOM   706  C  CB  . ALA   B 2 48  ? -26.074 12.419  -3.752  1.00 45.00  ? 57  ALA   B CB  1 
ATOM   707  N  N   . LEU   B 2 49  ? -25.925 11.845  -6.796  1.00 45.49  ? 58  LEU   B N   1 
ATOM   708  C  CA  . LEU   B 2 49  ? -26.011 12.262  -8.220  1.00 46.48  ? 58  LEU   B CA  1 
ATOM   709  C  C   . LEU   B 2 49  ? -27.376 12.894  -8.488  1.00 49.08  ? 58  LEU   B C   1 
ATOM   710  O  O   . LEU   B 2 49  ? -28.375 12.538  -7.805  1.00 47.67  ? 58  LEU   B O   1 
ATOM   711  C  CB  . LEU   B 2 49  ? -25.864 11.039  -9.120  1.00 46.30  ? 58  LEU   B CB  1 
ATOM   712  C  CG  . LEU   B 2 49  ? -24.581 10.234  -8.989  1.00 44.49  ? 58  LEU   B CG  1 
ATOM   713  C  CD1 . LEU   B 2 49  ? -24.737 8.982   -9.804  1.00 44.60  ? 58  LEU   B CD1 1 
ATOM   714  C  CD2 . LEU   B 2 49  ? -23.362 11.028  -9.430  1.00 44.97  ? 58  LEU   B CD2 1 
ATOM   715  N  N   . ARG   B 2 50  ? -27.408 13.751  -9.501  1.00 52.42  ? 59  ARG   B N   1 
ATOM   716  C  CA  . ARG   B 2 50  ? -28.627 14.413  -10.021 1.00 53.72  ? 59  ARG   B CA  1 
ATOM   717  C  C   . ARG   B 2 50  ? -28.933 13.815  -11.405 1.00 52.31  ? 59  ARG   B C   1 
ATOM   718  O  O   . ARG   B 2 50  ? -27.991 13.584  -12.197 1.00 49.84  ? 59  ARG   B O   1 
ATOM   719  C  CB  . ARG   B 2 50  ? -28.328 15.912  -10.003 1.00 56.87  ? 59  ARG   B CB  1 
ATOM   720  C  CG  . ARG   B 2 50  ? -29.361 16.787  -10.687 1.00 62.99  ? 59  ARG   B CG  1 
ATOM   721  C  CD  . ARG   B 2 50  ? -29.099 18.273  -10.395 1.00 66.19  ? 59  ARG   B CD  1 
ATOM   722  N  NE  . ARG   B 2 50  ? -27.701 18.689  -10.577 1.00 67.05  ? 59  ARG   B NE  1 
ATOM   723  C  CZ  . ARG   B 2 50  ? -27.147 19.076  -11.731 1.00 71.75  ? 59  ARG   B CZ  1 
ATOM   724  N  NH1 . ARG   B 2 50  ? -27.859 19.068  -12.850 1.00 72.14  ? 59  ARG   B NH1 1 
ATOM   725  N  NH2 . ARG   B 2 50  ? -25.869 19.452  -11.763 1.00 73.45  ? 59  ARG   B NH2 1 
ATOM   726  N  N   . SER   B 2 51  ? -30.189 13.463  -11.632 1.00 53.10  ? 60  SER   B N   1 
ATOM   727  C  CA  . SER   B 2 51  ? -30.794 13.242  -12.971 1.00 56.16  ? 60  SER   B CA  1 
ATOM   728  C  C   . SER   B 2 51  ? -31.899 14.292  -13.221 1.00 59.32  ? 60  SER   B C   1 
ATOM   729  O  O   . SER   B 2 51  ? -33.078 14.071  -12.819 1.00 54.89  ? 60  SER   B O   1 
ATOM   730  C  CB  . SER   B 2 51  ? -31.363 11.868  -13.080 1.00 55.19  ? 60  SER   B CB  1 
ATOM   731  O  OG  . SER   B 2 51  ? -32.003 11.736  -14.338 1.00 57.76  ? 60  SER   B OG  1 
ATOM   732  N  N   . GLY   B 2 52  ? -31.569 15.413  -13.859 1.00 64.25  ? 61  GLY   B N   1 
ATOM   733  C  CA  . GLY   B 2 52  ? -32.559 16.504  -13.993 1.00 67.64  ? 61  GLY   B CA  1 
ATOM   734  C  C   . GLY   B 2 52  ? -32.752 17.161  -12.646 1.00 70.50  ? 61  GLY   B C   1 
ATOM   735  O  O   . GLY   B 2 52  ? -31.752 17.676  -12.113 1.00 73.41  ? 61  GLY   B O   1 
ATOM   736  N  N   . GLU   B 2 53  ? -33.947 17.091  -12.062 1.00 75.19  ? 62  GLU   B N   1 
ATOM   737  C  CA  . GLU   B 2 53  ? -34.138 17.582  -10.669 1.00 79.41  ? 62  GLU   B CA  1 
ATOM   738  C  C   . GLU   B 2 53  ? -34.491 16.424  -9.720  1.00 74.46  ? 62  GLU   B C   1 
ATOM   739  O  O   . GLU   B 2 53  ? -34.647 16.692  -8.519  1.00 72.61  ? 62  GLU   B O   1 
ATOM   740  C  CB  . GLU   B 2 53  ? -35.079 18.790  -10.698 1.00 86.92  ? 62  GLU   B CB  1 
ATOM   741  C  CG  . GLU   B 2 53  ? -34.401 19.965  -11.404 1.00 95.75  ? 62  GLU   B CG  1 
ATOM   742  C  CD  . GLU   B 2 53  ? -34.539 21.340  -10.764 1.00 100.44 ? 62  GLU   B CD  1 
ATOM   743  O  OE1 . GLU   B 2 53  ? -35.656 21.672  -10.317 1.00 109.89 ? 62  GLU   B OE1 1 
ATOM   744  O  OE2 . GLU   B 2 53  ? -33.522 22.084  -10.715 1.00 100.42 ? 62  GLU   B OE2 1 
ATOM   745  N  N   . GLY   B 2 54  ? -34.486 15.177  -10.203 1.00 68.81  ? 63  GLY   B N   1 
ATOM   746  C  CA  . GLY   B 2 54  ? -34.407 13.981  -9.342  1.00 66.70  ? 63  GLY   B CA  1 
ATOM   747  C  C   . GLY   B 2 54  ? -33.021 13.846  -8.715  1.00 63.55  ? 63  GLY   B C   1 
ATOM   748  O  O   . GLY   B 2 54  ? -32.055 14.378  -9.314  1.00 60.41  ? 63  GLY   B O   1 
ATOM   749  N  N   . ARG   B 2 55  ? -32.934 13.165  -7.562  1.00 59.11  ? 64  ARG   B N   1 
ATOM   750  C  CA  . ARG   B 2 55  ? -31.673 12.818  -6.837  1.00 58.42  ? 64  ARG   B CA  1 
ATOM   751  C  C   . ARG   B 2 55  ? -31.516 11.290  -6.772  1.00 54.67  ? 64  ARG   B C   1 
ATOM   752  O  O   . ARG   B 2 55  ? -32.467 10.611  -6.362  1.00 54.68  ? 64  ARG   B O   1 
ATOM   753  C  CB  . ARG   B 2 55  ? -31.689 13.376  -5.408  1.00 59.05  ? 64  ARG   B CB  1 
ATOM   754  C  CG  . ARG   B 2 55  ? -30.369 13.322  -4.648  1.00 61.62  ? 64  ARG   B CG  1 
ATOM   755  C  CD  . ARG   B 2 55  ? -30.645 13.425  -3.150  1.00 67.01  ? 64  ARG   B CD  1 
ATOM   756  N  NE  . ARG   B 2 55  ? -29.547 13.047  -2.252  1.00 71.25  ? 64  ARG   B NE  1 
ATOM   757  C  CZ  . ARG   B 2 55  ? -28.785 13.880  -1.517  1.00 74.14  ? 64  ARG   B CZ  1 
ATOM   758  N  NH1 . ARG   B 2 55  ? -28.969 15.189  -1.568  1.00 72.61  ? 64  ARG   B NH1 1 
ATOM   759  N  NH2 . ARG   B 2 55  ? -27.832 13.393  -0.725  1.00 75.16  ? 64  ARG   B NH2 1 
ATOM   760  N  N   . LEU   B 2 56  ? -30.319 10.790  -7.053  1.00 50.65  ? 65  LEU   B N   1 
ATOM   761  C  CA  . LEU   B 2 56  ? -29.946 9.368   -6.872  1.00 48.33  ? 65  LEU   B CA  1 
ATOM   762  C  C   . LEU   B 2 56  ? -29.084 9.246   -5.618  1.00 45.86  ? 65  LEU   B C   1 
ATOM   763  O  O   . LEU   B 2 56  ? -27.974 9.857   -5.591  1.00 46.20  ? 65  LEU   B O   1 
ATOM   764  C  CB  . LEU   B 2 56  ? -29.146 8.928   -8.093  1.00 49.08  ? 65  LEU   B CB  1 
ATOM   765  C  CG  . LEU   B 2 56  ? -29.839 8.902   -9.451  1.00 52.02  ? 65  LEU   B CG  1 
ATOM   766  C  CD1 . LEU   B 2 56  ? -29.333 7.718   -10.290 1.00 51.12  ? 65  LEU   B CD1 1 
ATOM   767  C  CD2 . LEU   B 2 56  ? -31.342 8.807   -9.319  1.00 53.38  ? 65  LEU   B CD2 1 
ATOM   768  N  N   . ASP   B 2 57  ? -29.489 8.441   -4.638  1.00 44.43  ? 66  ASP   B N   1 
ATOM   769  C  CA  . ASP   B 2 57  ? -28.597 8.183   -3.472  1.00 44.49  ? 66  ASP   B CA  1 
ATOM   770  C  C   . ASP   B 2 57  ? -27.932 6.814   -3.577  1.00 43.41  ? 66  ASP   B C   1 
ATOM   771  O  O   . ASP   B 2 57  ? -28.540 5.823   -4.025  1.00 42.59  ? 66  ASP   B O   1 
ATOM   772  C  CB  . ASP   B 2 57  ? -29.327 8.328   -2.152  1.00 48.07  ? 66  ASP   B CB  1 
ATOM   773  C  CG  . ASP   B 2 57  ? -29.517 9.807   -1.817  1.00 51.49  ? 66  ASP   B CG  1 
ATOM   774  O  OD1 . ASP   B 2 57  ? -28.495 10.502  -1.608  1.00 58.42  ? 66  ASP   B OD1 1 
ATOM   775  O  OD2 . ASP   B 2 57  ? -30.639 10.255  -1.827  1.00 51.53  ? 66  ASP   B OD2 1 
ATOM   776  N  N   . PRO   B 2 58  ? -26.654 6.754   -3.141  1.00 41.50  ? 67  PRO   B N   1 
ATOM   777  C  CA  . PRO   B 2 58  ? -25.894 5.509   -3.151  1.00 40.00  ? 67  PRO   B CA  1 
ATOM   778  C  C   . PRO   B 2 58  ? -26.654 4.457   -2.323  1.00 38.99  ? 67  PRO   B C   1 
ATOM   779  O  O   . PRO   B 2 58  ? -27.240 4.796   -1.343  1.00 40.26  ? 67  PRO   B O   1 
ATOM   780  C  CB  . PRO   B 2 58  ? -24.541 5.868   -2.515  1.00 40.35  ? 67  PRO   B CB  1 
ATOM   781  C  CG  . PRO   B 2 58  ? -24.674 7.261   -1.941  1.00 41.89  ? 67  PRO   B CG  1 
ATOM   782  C  CD  . PRO   B 2 58  ? -25.957 7.865   -2.458  1.00 41.98  ? 67  PRO   B CD  1 
ATOM   783  N  N   . TYR   B 2 59  ? -26.643 3.185   -2.710  1.00 36.91  ? 68  TYR   B N   1 
ATOM   784  C  CA  . TYR   B 2 59  ? -27.345 2.115   -1.968  1.00 35.42  ? 68  TYR   B CA  1 
ATOM   785  C  C   . TYR   B 2 59  ? -26.323 1.061   -1.533  1.00 33.53  ? 68  TYR   B C   1 
ATOM   786  O  O   . TYR   B 2 59  ? -26.385 0.561   -0.404  1.00 32.78  ? 68  TYR   B O   1 
ATOM   787  C  CB  . TYR   B 2 59  ? -28.470 1.561   -2.833  1.00 36.22  ? 68  TYR   B CB  1 
ATOM   788  C  CG  . TYR   B 2 59  ? -29.220 0.390   -2.252  1.00 36.71  ? 68  TYR   B CG  1 
ATOM   789  C  CD1 . TYR   B 2 59  ? -28.655 -0.883  -2.245  1.00 36.67  ? 68  TYR   B CD1 1 
ATOM   790  C  CD2 . TYR   B 2 59  ? -30.536 0.533   -1.825  1.00 37.22  ? 68  TYR   B CD2 1 
ATOM   791  C  CE1 . TYR   B 2 59  ? -29.364 -1.974  -1.751  1.00 37.73  ? 68  TYR   B CE1 1 
ATOM   792  C  CE2 . TYR   B 2 59  ? -31.260 -0.544  -1.339  1.00 37.71  ? 68  TYR   B CE2 1 
ATOM   793  C  CZ  . TYR   B 2 59  ? -30.679 -1.812  -1.316  1.00 38.54  ? 68  TYR   B CZ  1 
ATOM   794  O  OH  . TYR   B 2 59  ? -31.361 -2.896  -0.798  1.00 39.15  ? 68  TYR   B OH  1 
ATOM   795  N  N   . TRP   B 2 60  ? -25.374 0.787   -2.365  1.00 32.16  ? 69  TRP   B N   1 
ATOM   796  C  CA  . TRP   B 2 60  ? -24.351 -0.261  -2.094  1.00 31.96  ? 69  TRP   B CA  1 
ATOM   797  C  C   . TRP   B 2 60  ? -23.047 0.220   -2.671  1.00 31.74  ? 69  TRP   B C   1 
ATOM   798  O  O   . TRP   B 2 60  ? -23.028 0.703   -3.825  1.00 32.11  ? 69  TRP   B O   1 
ATOM   799  C  CB  . TRP   B 2 60  ? -24.711 -1.650  -2.628  1.00 31.44  ? 69  TRP   B CB  1 
ATOM   800  C  CG  . TRP   B 2 60  ? -23.551 -2.598  -2.564  1.00 31.51  ? 69  TRP   B CG  1 
ATOM   801  C  CD1 . TRP   B 2 60  ? -23.126 -3.289  -1.471  1.00 31.72  ? 69  TRP   B CD1 1 
ATOM   802  C  CD2 . TRP   B 2 60  ? -22.666 -3.003  -3.636  1.00 31.93  ? 69  TRP   B CD2 1 
ATOM   803  N  NE1 . TRP   B 2 60  ? -22.031 -4.060  -1.781  1.00 31.46  ? 69  TRP   B NE1 1 
ATOM   804  C  CE2 . TRP   B 2 60  ? -21.729 -3.910  -3.101  1.00 31.64  ? 69  TRP   B CE2 1 
ATOM   805  C  CE3 . TRP   B 2 60  ? -22.555 -2.663  -4.987  1.00 31.98  ? 69  TRP   B CE3 1 
ATOM   806  C  CZ2 . TRP   B 2 60  ? -20.691 -4.445  -3.861  1.00 32.05  ? 69  TRP   B CZ2 1 
ATOM   807  C  CZ3 . TRP   B 2 60  ? -21.539 -3.191  -5.738  1.00 32.68  ? 69  TRP   B CZ3 1 
ATOM   808  C  CH2 . TRP   B 2 60  ? -20.633 -4.092  -5.191  1.00 32.60  ? 69  TRP   B CH2 1 
ATOM   809  N  N   . GLY   B 2 61  ? -21.960 -0.077  -1.996  1.00 32.88  ? 70  GLY   B N   1 
ATOM   810  C  CA  . GLY   B 2 61  ? -20.671 0.017   -2.717  1.00 33.34  ? 70  GLY   B CA  1 
ATOM   811  C  C   . GLY   B 2 61  ? -19.540 -0.630  -1.991  1.00 33.07  ? 70  GLY   B C   1 
ATOM   812  O  O   . GLY   B 2 61  ? -19.703 -0.873  -0.787  1.00 32.50  ? 70  GLY   B O   1 
ATOM   813  N  N   . ASP   B 2 62  ? -18.400 -0.736  -2.653  1.00 34.64  ? 71  ASP   B N   1 
ATOM   814  C  CA  . ASP   B 2 62  ? -17.213 -1.512  -2.188  1.00 36.05  ? 71  ASP   B CA  1 
ATOM   815  C  C   . ASP   B 2 62  ? -16.010 -1.007  -2.954  1.00 35.56  ? 71  ASP   B C   1 
ATOM   816  O  O   . ASP   B 2 62  ? -16.007 -1.128  -4.214  1.00 35.71  ? 71  ASP   B O   1 
ATOM   817  C  CB  . ASP   B 2 62  ? -17.466 -3.001  -2.320  1.00 38.35  ? 71  ASP   B CB  1 
ATOM   818  C  CG  . ASP   B 2 62  ? -16.365 -3.874  -1.767  1.00 40.94  ? 71  ASP   B CG  1 
ATOM   819  O  OD1 . ASP   B 2 62  ? -15.304 -3.786  -2.256  1.00 44.96  ? 71  ASP   B OD1 1 
ATOM   820  O  OD2 . ASP   B 2 62  ? -16.629 -4.674  -0.861  1.00 47.32  ? 71  ASP   B OD2 1 
ATOM   821  N  N   . VAL   B 2 63  ? -15.096 -0.351  -2.240  1.00 36.34  ? 72  VAL   B N   1 
ATOM   822  C  CA  . VAL   B 2 63  ? -13.840 0.279   -2.773  1.00 37.33  ? 72  VAL   B CA  1 
ATOM   823  C  C   . VAL   B 2 63  ? -12.931 -0.812  -3.335  1.00 38.44  ? 72  VAL   B C   1 
ATOM   824  O  O   . VAL   B 2 63  ? -12.185 -0.554  -4.342  1.00 38.52  ? 72  VAL   B O   1 
ATOM   825  C  CB  . VAL   B 2 63  ? -13.124 1.118   -1.693  1.00 37.48  ? 72  VAL   B CB  1 
ATOM   826  C  CG1 . VAL   B 2 63  ? -11.628 1.207   -1.901  1.00 37.64  ? 72  VAL   B CG1 1 
ATOM   827  C  CG2 . VAL   B 2 63  ? -13.725 2.526   -1.586  1.00 38.26  ? 72  VAL   B CG2 1 
ATOM   828  N  N   . LYS   B 2 64  ? -12.991 -2.034  -2.803  1.00 40.28  ? 73  LYS   B N   1 
ATOM   829  C  CA  . LYS   B 2 64  ? -12.043 -3.079  -3.311  1.00 39.98  ? 73  LYS   B CA  1 
ATOM   830  C  C   . LYS   B 2 64  ? -12.491 -3.617  -4.685  1.00 40.69  ? 73  LYS   B C   1 
ATOM   831  O  O   . LYS   B 2 64  ? -11.601 -3.888  -5.519  1.00 40.17  ? 73  LYS   B O   1 
ATOM   832  C  CB  . LYS   B 2 64  ? -11.904 -4.262  -2.363  1.00 40.31  ? 73  LYS   B CB  1 
ATOM   833  C  CG  . LYS   B 2 64  ? -10.920 -5.282  -2.913  1.00 41.62  ? 73  LYS   B CG  1 
ATOM   834  C  CD  . LYS   B 2 64  ? -10.383 -6.187  -1.880  1.00 41.98  ? 73  LYS   B CD  1 
ATOM   835  C  CE  . LYS   B 2 64  ? -9.326  -7.098  -2.472  1.00 44.10  ? 73  LYS   B CE  1 
ATOM   836  N  NZ  . LYS   B 2 64  ? -9.061  -8.175  -1.505  1.00 44.54  ? 73  LYS   B NZ  1 
ATOM   837  N  N   . GLN   B 2 65  ? -13.816 -3.838  -4.873  1.00 40.84  ? 74  GLN   B N   1 
ATOM   838  C  CA  . GLN   B 2 65  ? -14.439 -4.234  -6.164  1.00 41.11  ? 74  GLN   B CA  1 
ATOM   839  C  C   . GLN   B 2 65  ? -14.445 -3.033  -7.133  1.00 39.48  ? 74  GLN   B C   1 
ATOM   840  O  O   . GLN   B 2 65  ? -14.556 -3.246  -8.319  1.00 39.53  ? 74  GLN   B O   1 
ATOM   841  C  CB  . GLN   B 2 65  ? -15.862 -4.740  -5.955  1.00 43.07  ? 74  GLN   B CB  1 
ATOM   842  C  CG  . GLN   B 2 65  ? -15.953 -6.110  -5.274  1.00 46.07  ? 74  GLN   B CG  1 
ATOM   843  C  CD  . GLN   B 2 65  ? -17.422 -6.479  -5.072  1.00 47.94  ? 74  GLN   B CD  1 
ATOM   844  O  OE1 . GLN   B 2 65  ? -18.211 -6.610  -6.007  1.00 50.76  ? 74  GLN   B OE1 1 
ATOM   845  N  NE2 . GLN   B 2 65  ? -17.832 -6.635  -3.838  1.00 49.08  ? 74  GLN   B NE2 1 
ATOM   846  N  N   . ASP   B 2 66  ? -14.395 -1.829  -6.570  1.00 37.83  ? 75  ASP   B N   1 
ATOM   847  C  CA  . ASP   B 2 66  ? -14.429 -0.486  -7.203  1.00 36.78  ? 75  ASP   B CA  1 
ATOM   848  C  C   . ASP   B 2 66  ? -15.765 -0.323  -7.901  1.00 35.55  ? 75  ASP   B C   1 
ATOM   849  O  O   . ASP   B 2 66  ? -15.735 0.060   -9.072  1.00 35.32  ? 75  ASP   B O   1 
ATOM   850  C  CB  . ASP   B 2 66  ? -13.266 -0.264  -8.160  1.00 36.84  ? 75  ASP   B CB  1 
ATOM   851  C  CG  . ASP   B 2 66  ? -13.208 1.153   -8.709  1.00 36.84  ? 75  ASP   B CG  1 
ATOM   852  O  OD1 . ASP   B 2 66  ? -13.435 2.075   -7.954  1.00 36.21  ? 75  ASP   B OD1 1 
ATOM   853  O  OD2 . ASP   B 2 66  ? -12.915 1.282   -9.929  1.00 38.09  ? 75  ASP   B OD2 1 
ATOM   854  N  N   . LEU   B 2 67  ? -16.850 -0.696  -7.206  1.00 34.85  ? 76  LEU   B N   1 
ATOM   855  C  CA  . LEU   B 2 67  ? -18.239 -0.647  -7.744  1.00 34.36  ? 76  LEU   B CA  1 
ATOM   856  C  C   . LEU   B 2 67  ? -19.186 0.086   -6.820  1.00 33.99  ? 76  LEU   B C   1 
ATOM   857  O  O   . LEU   B 2 67  ? -18.961 0.123   -5.574  1.00 33.40  ? 76  LEU   B O   1 
ATOM   858  C  CB  . LEU   B 2 67  ? -18.677 -2.085  -7.974  1.00 34.71  ? 76  LEU   B CB  1 
ATOM   859  C  CG  . LEU   B 2 67  ? -18.028 -2.817  -9.153  1.00 34.64  ? 76  LEU   B CG  1 
ATOM   860  C  CD1 . LEU   B 2 67  ? -18.688 -4.172  -9.254  1.00 35.02  ? 76  LEU   B CD1 1 
ATOM   861  C  CD2 . LEU   B 2 67  ? -18.205 -2.065  -10.496 1.00 34.95  ? 76  LEU   B CD2 1 
ATOM   862  N  N   . VAL   B 2 68  ? -20.249 0.651   -7.390  1.00 34.39  ? 77  VAL   B N   1 
ATOM   863  C  CA  . VAL   B 2 68  ? -21.294 1.382   -6.602  1.00 33.85  ? 77  VAL   B CA  1 
ATOM   864  C  C   . VAL   B 2 68  ? -22.634 1.328   -7.327  1.00 32.65  ? 77  VAL   B C   1 
ATOM   865  O  O   . VAL   B 2 68  ? -22.639 1.456   -8.549  1.00 32.80  ? 77  VAL   B O   1 
ATOM   866  C  CB  . VAL   B 2 68  ? -20.852 2.815   -6.251  1.00 34.13  ? 77  VAL   B CB  1 
ATOM   867  C  CG1 . VAL   B 2 68  ? -20.474 3.599   -7.490  1.00 34.94  ? 77  VAL   B CG1 1 
ATOM   868  C  CG2 . VAL   B 2 68  ? -21.890 3.523   -5.414  1.00 34.36  ? 77  VAL   B CG2 1 
ATOM   869  N  N   . SER   B 2 69  ? -23.704 1.087   -6.590  1.00 32.16  ? 78  SER   B N   1 
ATOM   870  C  CA  . SER   B 2 69  ? -25.083 1.045   -7.109  1.00 32.81  ? 78  SER   B CA  1 
ATOM   871  C  C   . SER   B 2 69  ? -25.876 2.170   -6.460  1.00 32.48  ? 78  SER   B C   1 
ATOM   872  O  O   . SER   B 2 69  ? -25.681 2.441   -5.233  1.00 31.86  ? 78  SER   B O   1 
ATOM   873  C  CB  . SER   B 2 69  ? -25.778 -0.319  -6.895  1.00 33.01  ? 78  SER   B CB  1 
ATOM   874  O  OG  . SER   B 2 69  ? -26.211 -0.471  -5.546  1.00 33.31  ? 78  SER   B OG  1 
ATOM   875  N  N   A TYR   B 2 70  ? -26.759 2.814   -7.226  0.25 32.83  ? 79  TYR   B N   1 
ATOM   876  N  N   B TYR   B 2 70  ? -26.759 2.814   -7.226  0.25 32.83  ? 79  TYR   B N   1 
ATOM   877  N  N   C TYR   B 2 70  ? -26.796 2.753   -7.230  0.25 32.87  ? 79  TYR   B N   1 
ATOM   878  N  N   D TYR   B 2 70  ? -26.796 2.753   -7.230  0.25 32.87  ? 79  TYR   B N   1 
ATOM   879  C  CA  A TYR   B 2 70  ? -27.661 3.895   -6.743  0.25 32.84  ? 79  TYR   B CA  1 
ATOM   880  C  CA  B TYR   B 2 70  ? -27.661 3.895   -6.743  0.25 32.84  ? 79  TYR   B CA  1 
ATOM   881  C  CA  C TYR   B 2 70  ? -27.656 3.898   -6.833  0.25 32.93  ? 79  TYR   B CA  1 
ATOM   882  C  CA  D TYR   B 2 70  ? -27.656 3.898   -6.833  0.25 32.93  ? 79  TYR   B CA  1 
ATOM   883  C  C   A TYR   B 2 70  ? -29.126 3.484   -6.920  0.25 33.05  ? 79  TYR   B C   1 
ATOM   884  C  C   B TYR   B 2 70  ? -29.126 3.484   -6.920  0.25 33.05  ? 79  TYR   B C   1 
ATOM   885  C  C   C TYR   B 2 70  ? -29.138 3.513   -6.927  0.25 33.26  ? 79  TYR   B C   1 
ATOM   886  C  C   D TYR   B 2 70  ? -29.138 3.513   -6.927  0.25 33.26  ? 79  TYR   B C   1 
ATOM   887  O  O   A TYR   B 2 70  ? -29.472 2.946   -7.980  0.25 33.29  ? 79  TYR   B O   1 
ATOM   888  O  O   B TYR   B 2 70  ? -29.472 2.946   -7.980  0.25 33.29  ? 79  TYR   B O   1 
ATOM   889  O  O   C TYR   B 2 70  ? -29.565 3.058   -7.998  0.25 33.53  ? 79  TYR   B O   1 
ATOM   890  O  O   D TYR   B 2 70  ? -29.565 3.058   -7.998  0.25 33.53  ? 79  TYR   B O   1 
ATOM   891  C  CB  A TYR   B 2 70  ? -27.387 5.200   -7.486  0.25 33.12  ? 79  TYR   B CB  1 
ATOM   892  C  CB  B TYR   B 2 70  ? -27.387 5.200   -7.486  0.25 33.12  ? 79  TYR   B CB  1 
ATOM   893  C  CB  C TYR   B 2 70  ? -27.352 5.089   -7.738  0.25 33.13  ? 79  TYR   B CB  1 
ATOM   894  C  CB  D TYR   B 2 70  ? -27.352 5.089   -7.738  0.25 33.13  ? 79  TYR   B CB  1 
ATOM   895  C  CG  A TYR   B 2 70  ? -26.094 5.871   -7.104  0.25 33.06  ? 79  TYR   B CG  1 
ATOM   896  C  CG  B TYR   B 2 70  ? -26.094 5.871   -7.104  0.25 33.06  ? 79  TYR   B CG  1 
ATOM   897  C  CG  C TYR   B 2 70  ? -26.009 5.729   -7.499  0.25 33.01  ? 79  TYR   B CG  1 
ATOM   898  C  CG  D TYR   B 2 70  ? -26.009 5.729   -7.499  0.25 33.01  ? 79  TYR   B CG  1 
ATOM   899  C  CD1 A TYR   B 2 70  ? -24.885 5.382   -7.548  0.25 33.14  ? 79  TYR   B CD1 1 
ATOM   900  C  CD1 B TYR   B 2 70  ? -24.885 5.382   -7.548  0.25 33.14  ? 79  TYR   B CD1 1 
ATOM   901  C  CD1 C TYR   B 2 70  ? -24.829 5.118   -7.883  0.25 33.12  ? 79  TYR   B CD1 1 
ATOM   902  C  CD1 D TYR   B 2 70  ? -24.829 5.118   -7.883  0.25 33.12  ? 79  TYR   B CD1 1 
ATOM   903  C  CD2 A TYR   B 2 70  ? -26.078 6.995   -6.292  0.25 33.29  ? 79  TYR   B CD2 1 
ATOM   904  C  CD2 B TYR   B 2 70  ? -26.078 6.995   -6.292  0.25 33.29  ? 79  TYR   B CD2 1 
ATOM   905  C  CD2 C TYR   B 2 70  ? -25.926 6.964   -6.890  0.25 33.23  ? 79  TYR   B CD2 1 
ATOM   906  C  CD2 D TYR   B 2 70  ? -25.926 6.964   -6.890  0.25 33.23  ? 79  TYR   B CD2 1 
ATOM   907  C  CE1 A TYR   B 2 70  ? -23.691 5.995   -7.209  0.25 33.14  ? 79  TYR   B CE1 1 
ATOM   908  C  CE1 B TYR   B 2 70  ? -23.691 5.995   -7.209  0.25 33.14  ? 79  TYR   B CE1 1 
ATOM   909  C  CE1 C TYR   B 2 70  ? -23.601 5.723   -7.664  0.25 33.13  ? 79  TYR   B CE1 1 
ATOM   910  C  CE1 D TYR   B 2 70  ? -23.601 5.723   -7.664  0.25 33.13  ? 79  TYR   B CE1 1 
ATOM   911  C  CE2 A TYR   B 2 70  ? -24.891 7.613   -5.931  0.25 33.14  ? 79  TYR   B CE2 1 
ATOM   912  C  CE2 B TYR   B 2 70  ? -24.891 7.613   -5.931  0.25 33.14  ? 79  TYR   B CE2 1 
ATOM   913  C  CE2 C TYR   B 2 70  ? -24.711 7.573   -6.643  0.25 33.12  ? 79  TYR   B CE2 1 
ATOM   914  C  CE2 D TYR   B 2 70  ? -24.711 7.573   -6.643  0.25 33.12  ? 79  TYR   B CE2 1 
ATOM   915  C  CZ  A TYR   B 2 70  ? -23.692 7.105   -6.390  0.25 32.97  ? 79  TYR   B CZ  1 
ATOM   916  C  CZ  B TYR   B 2 70  ? -23.692 7.105   -6.390  0.25 32.97  ? 79  TYR   B CZ  1 
ATOM   917  C  CZ  C TYR   B 2 70  ? -23.546 6.951   -7.027  0.25 33.02  ? 79  TYR   B CZ  1 
ATOM   918  C  CZ  D TYR   B 2 70  ? -23.546 6.951   -7.027  0.25 33.02  ? 79  TYR   B CZ  1 
ATOM   919  O  OH  A TYR   B 2 70  ? -22.508 7.693   -6.052  0.25 32.99  ? 79  TYR   B OH  1 
ATOM   920  O  OH  B TYR   B 2 70  ? -22.508 7.693   -6.052  0.25 32.99  ? 79  TYR   B OH  1 
ATOM   921  O  OH  C TYR   B 2 70  ? -22.360 7.570   -6.781  0.25 33.11  ? 79  TYR   B OH  1 
ATOM   922  O  OH  D TYR   B 2 70  ? -22.360 7.570   -6.781  0.25 33.11  ? 79  TYR   B OH  1 
ATOM   923  N  N   A CYS   B 2 71  ? -29.947 3.741   -5.896  0.25 33.03  ? 80  CYS   B N   1 
ATOM   924  N  N   B CYS   B 2 71  ? -29.947 3.741   -5.896  0.25 33.03  ? 80  CYS   B N   1 
ATOM   925  N  N   C CYS   B 2 71  ? -29.884 3.693   -5.829  0.25 33.38  ? 80  CYS   B N   1 
ATOM   926  N  N   D CYS   B 2 71  ? -29.884 3.693   -5.829  0.25 33.38  ? 80  CYS   B N   1 
ATOM   927  C  CA  A CYS   B 2 71  ? -31.427 3.566   -5.900  0.25 33.32  ? 80  CYS   B CA  1 
ATOM   928  C  CA  B CYS   B 2 71  ? -31.427 3.566   -5.900  0.25 33.32  ? 80  CYS   B CA  1 
ATOM   929  C  CA  C CYS   B 2 71  ? -31.371 3.581   -5.742  0.25 33.77  ? 80  CYS   B CA  1 
ATOM   930  C  CA  D CYS   B 2 71  ? -31.371 3.581   -5.742  0.25 33.77  ? 80  CYS   B CA  1 
ATOM   931  C  C   A CYS   B 2 71  ? -31.801 2.153   -5.424  0.25 33.39  ? 80  CYS   B C   1 
ATOM   932  C  C   B CYS   B 2 71  ? -31.801 2.153   -5.424  0.25 33.39  ? 80  CYS   B C   1 
ATOM   933  C  C   C CYS   B 2 71  ? -31.831 2.122   -5.698  0.25 33.72  ? 80  CYS   B C   1 
ATOM   934  C  C   D CYS   B 2 71  ? -31.831 2.122   -5.698  0.25 33.72  ? 80  CYS   B C   1 
ATOM   935  O  O   A CYS   B 2 71  ? -32.912 1.985   -4.882  0.25 33.60  ? 80  CYS   B O   1 
ATOM   936  O  O   B CYS   B 2 71  ? -32.912 1.985   -4.882  0.25 33.60  ? 80  CYS   B O   1 
ATOM   937  O  O   C CYS   B 2 71  ? -33.039 1.888   -5.860  0.25 34.01  ? 80  CYS   B O   1 
ATOM   938  O  O   D CYS   B 2 71  ? -33.039 1.888   -5.860  0.25 34.01  ? 80  CYS   B O   1 
ATOM   939  C  CB  A CYS   B 2 71  ? -32.005 3.822   -7.293  0.25 33.73  ? 80  CYS   B CB  1 
ATOM   940  C  CB  B CYS   B 2 71  ? -32.005 3.822   -7.293  0.25 33.73  ? 80  CYS   B CB  1 
ATOM   941  C  CB  C CYS   B 2 71  ? -32.050 4.231   -6.940  0.25 34.47  ? 80  CYS   B CB  1 
ATOM   942  C  CB  D CYS   B 2 71  ? -32.050 4.231   -6.940  0.25 34.47  ? 80  CYS   B CB  1 
ATOM   943  S  SG  A CYS   B 2 71  ? -31.580 5.440   -8.010  0.25 33.71  ? 80  CYS   B SG  1 
ATOM   944  S  SG  B CYS   B 2 71  ? -31.580 5.440   -8.010  0.25 33.71  ? 80  CYS   B SG  1 
ATOM   945  S  SG  C CYS   B 2 71  ? -31.852 6.030   -6.992  0.25 34.99  ? 80  CYS   B SG  1 
ATOM   946  S  SG  D CYS   B 2 71  ? -31.852 6.030   -6.992  0.25 34.99  ? 80  CYS   B SG  1 
ATOM   947  N  N   . GLY   B 2 72  ? -30.900 1.175   -5.578  1.00 33.28  ? 81  GLY   B N   1 
ATOM   948  C  CA  . GLY   B 2 72  ? -31.243 -0.228  -5.327  1.00 33.36  ? 81  GLY   B CA  1 
ATOM   949  C  C   . GLY   B 2 72  ? -29.969 -1.042  -5.365  1.00 33.10  ? 81  GLY   B C   1 
ATOM   950  O  O   . GLY   B 2 72  ? -28.882 -0.506  -5.636  1.00 33.16  ? 81  GLY   B O   1 
ATOM   951  N  N   . PRO   B 2 73  ? -30.084 -2.348  -5.102  1.00 33.88  ? 82  PRO   B N   1 
ATOM   952  C  CA  . PRO   B 2 73  ? -28.918 -3.231  -5.125  1.00 34.50  ? 82  PRO   B CA  1 
ATOM   953  C  C   . PRO   B 2 73  ? -28.414 -3.462  -6.556  1.00 36.09  ? 82  PRO   B C   1 
ATOM   954  O  O   . PRO   B 2 73  ? -29.190 -3.315  -7.523  1.00 37.92  ? 82  PRO   B O   1 
ATOM   955  C  CB  . PRO   B 2 73  ? -29.447 -4.552  -4.543  1.00 34.23  ? 82  PRO   B CB  1 
ATOM   956  C  CG  . PRO   B 2 73  ? -30.952 -4.507  -4.771  1.00 34.77  ? 82  PRO   B CG  1 
ATOM   957  C  CD  . PRO   B 2 73  ? -31.335 -3.033  -4.728  1.00 34.55  ? 82  PRO   B CD  1 
ATOM   958  N  N   . TRP   B 2 74  ? -27.185 -3.956  -6.676  1.00 36.65  ? 83  TRP   B N   1 
ATOM   959  C  CA  . TRP   B 2 74  ? -26.530 -4.308  -7.948  1.00 37.87  ? 83  TRP   B CA  1 
ATOM   960  C  C   . TRP   B 2 74  ? -27.426 -5.310  -8.717  1.00 39.95  ? 83  TRP   B C   1 
ATOM   961  O  O   . TRP   B 2 74  ? -27.785 -6.323  -8.140  1.00 39.78  ? 83  TRP   B O   1 
ATOM   962  C  CB  . TRP   B 2 74  ? -25.096 -4.838  -7.670  1.00 36.91  ? 83  TRP   B CB  1 
ATOM   963  C  CG  . TRP   B 2 74  ? -24.261 -4.976  -8.905  1.00 36.31  ? 83  TRP   B CG  1 
ATOM   964  C  CD1 . TRP   B 2 74  ? -24.179 -6.082  -9.696  1.00 36.56  ? 83  TRP   B CD1 1 
ATOM   965  C  CD2 . TRP   B 2 74  ? -23.400 -3.992  -9.516  1.00 36.06  ? 83  TRP   B CD2 1 
ATOM   966  N  NE1 . TRP   B 2 74  ? -23.328 -5.856  -10.746 1.00 37.01  ? 83  TRP   B NE1 1 
ATOM   967  C  CE2 . TRP   B 2 74  ? -22.865 -4.576  -10.681 1.00 36.27  ? 83  TRP   B CE2 1 
ATOM   968  C  CE3 . TRP   B 2 74  ? -23.085 -2.645  -9.237  1.00 35.49  ? 83  TRP   B CE3 1 
ATOM   969  C  CZ2 . TRP   B 2 74  ? -22.013 -3.898  -11.542 1.00 36.33  ? 83  TRP   B CZ2 1 
ATOM   970  C  CZ3 . TRP   B 2 74  ? -22.253 -1.975  -10.099 1.00 35.07  ? 83  TRP   B CZ3 1 
ATOM   971  C  CH2 . TRP   B 2 74  ? -21.740 -2.585  -11.244 1.00 35.82  ? 83  TRP   B CH2 1 
ATOM   972  N  N   . LYS   B 2 75  ? -27.701 -5.057  -10.014 1.00 41.87  ? 84  LYS   B N   1 
ATOM   973  C  CA  . LYS   B 2 75  ? -28.653 -5.831  -10.854 1.00 43.46  ? 84  LYS   B CA  1 
ATOM   974  C  C   . LYS   B 2 75  ? -27.924 -6.693  -11.895 1.00 44.79  ? 84  LYS   B C   1 
ATOM   975  O  O   . LYS   B 2 75  ? -28.574 -7.595  -12.422 1.00 47.43  ? 84  LYS   B O   1 
ATOM   976  C  CB  . LYS   B 2 75  ? -29.566 -4.861  -11.592 1.00 44.49  ? 84  LYS   B CB  1 
ATOM   977  C  CG  . LYS   B 2 75  ? -30.434 -4.003  -10.693 1.00 44.34  ? 84  LYS   B CG  1 
ATOM   978  C  CD  . LYS   B 2 75  ? -31.517 -4.840  -10.055 1.00 44.83  ? 84  LYS   B CD  1 
ATOM   979  C  CE  . LYS   B 2 75  ? -31.923 -4.335  -8.690  1.00 44.82  ? 84  LYS   B CE  1 
ATOM   980  N  NZ  . LYS   B 2 75  ? -33.380 -4.251  -8.618  1.00 45.52  ? 84  LYS   B NZ  1 
ATOM   981  N  N   . LEU   B 2 76  ? -26.669 -6.393  -12.238 1.00 45.06  ? 85  LEU   B N   1 
ATOM   982  C  CA  . LEU   B 2 76  ? -25.957 -6.938  -13.431 1.00 45.70  ? 85  LEU   B CA  1 
ATOM   983  C  C   . LEU   B 2 76  ? -25.253 -8.239  -13.023 1.00 46.91  ? 85  LEU   B C   1 
ATOM   984  O  O   . LEU   B 2 76  ? -24.291 -8.160  -12.238 1.00 44.53  ? 85  LEU   B O   1 
ATOM   985  C  CB  . LEU   B 2 76  ? -24.967 -5.890  -13.953 1.00 45.13  ? 85  LEU   B CB  1 
ATOM   986  C  CG  . LEU   B 2 76  ? -25.547 -4.477  -14.112 1.00 45.27  ? 85  LEU   B CG  1 
ATOM   987  C  CD1 . LEU   B 2 76  ? -24.507 -3.472  -14.601 1.00 45.16  ? 85  LEU   B CD1 1 
ATOM   988  C  CD2 . LEU   B 2 76  ? -26.751 -4.475  -15.042 1.00 46.02  ? 85  LEU   B CD2 1 
ATOM   989  N  N   . ASP   B 2 77  ? -25.728 -9.387  -13.503 1.00 49.97  ? 86  ASP   B N   1 
ATOM   990  C  CA  . ASP   B 2 77  ? -25.155 -10.702 -13.088 1.00 53.55  ? 86  ASP   B CA  1 
ATOM   991  C  C   . ASP   B 2 77  ? -24.564 -11.477 -14.281 1.00 52.82  ? 86  ASP   B C   1 
ATOM   992  O  O   . ASP   B 2 77  ? -24.086 -12.565 -14.046 1.00 53.30  ? 86  ASP   B O   1 
ATOM   993  C  CB  . ASP   B 2 77  ? -26.162 -11.564 -12.302 1.00 57.41  ? 86  ASP   B CB  1 
ATOM   994  C  CG  . ASP   B 2 77  ? -27.522 -11.778 -12.950 1.00 63.08  ? 86  ASP   B CG  1 
ATOM   995  O  OD1 . ASP   B 2 77  ? -27.751 -11.252 -14.056 1.00 67.04  ? 86  ASP   B OD1 1 
ATOM   996  O  OD2 . ASP   B 2 77  ? -28.362 -12.455 -12.328 1.00 70.07  ? 86  ASP   B OD2 1 
ATOM   997  N  N   . ALA   B 2 78  ? -24.535 -10.954 -15.508 1.00 51.27  ? 87  ALA   B N   1 
ATOM   998  C  CA  . ALA   B 2 78  ? -23.998 -11.711 -16.651 1.00 50.13  ? 87  ALA   B CA  1 
ATOM   999  C  C   . ALA   B 2 78  ? -22.476 -11.755 -16.519 1.00 48.95  ? 87  ALA   B C   1 
ATOM   1000 O  O   . ALA   B 2 78  ? -21.892 -10.886 -15.811 1.00 46.17  ? 87  ALA   B O   1 
ATOM   1001 C  CB  . ALA   B 2 78  ? -24.476 -11.133 -17.953 1.00 51.65  ? 87  ALA   B CB  1 
ATOM   1002 N  N   . ALA   B 2 79  ? -21.886 -12.795 -17.109 1.00 47.62  ? 88  ALA   B N   1 
ATOM   1003 C  CA  . ALA   B 2 79  ? -20.482 -13.229 -16.965 1.00 47.54  ? 88  ALA   B CA  1 
ATOM   1004 C  C   . ALA   B 2 79  ? -19.851 -13.477 -18.346 1.00 47.08  ? 88  ALA   B C   1 
ATOM   1005 O  O   . ALA   B 2 79  ? -20.530 -14.005 -19.190 1.00 46.07  ? 88  ALA   B O   1 
ATOM   1006 C  CB  . ALA   B 2 79  ? -20.474 -14.493 -16.133 1.00 47.71  ? 88  ALA   B CB  1 
ATOM   1007 N  N   . TRP   B 2 80  ? -18.604 -13.060 -18.580 1.00 48.05  ? 89  TRP   B N   1 
ATOM   1008 C  CA  . TRP   B 2 80  ? -17.805 -13.495 -19.758 1.00 50.53  ? 89  TRP   B CA  1 
ATOM   1009 C  C   . TRP   B 2 80  ? -17.763 -15.021 -19.705 1.00 52.53  ? 89  TRP   B C   1 
ATOM   1010 O  O   . TRP   B 2 80  ? -17.689 -15.574 -18.564 1.00 51.82  ? 89  TRP   B O   1 
ATOM   1011 C  CB  . TRP   B 2 80  ? -16.403 -12.875 -19.777 1.00 49.88  ? 89  TRP   B CB  1 
ATOM   1012 C  CG  . TRP   B 2 80  ? -15.592 -13.216 -20.992 1.00 51.25  ? 89  TRP   B CG  1 
ATOM   1013 C  CD1 . TRP   B 2 80  ? -16.027 -13.279 -22.286 1.00 51.47  ? 89  TRP   B CD1 1 
ATOM   1014 C  CD2 . TRP   B 2 80  ? -14.200 -13.611 -21.017 1.00 51.24  ? 89  TRP   B CD2 1 
ATOM   1015 N  NE1 . TRP   B 2 80  ? -14.998 -13.627 -23.108 1.00 52.67  ? 89  TRP   B NE1 1 
ATOM   1016 C  CE2 . TRP   B 2 80  ? -13.859 -13.822 -22.364 1.00 51.91  ? 89  TRP   B CE2 1 
ATOM   1017 C  CE3 . TRP   B 2 80  ? -13.209 -13.754 -20.040 1.00 50.66  ? 89  TRP   B CE3 1 
ATOM   1018 C  CZ2 . TRP   B 2 80  ? -12.583 -14.215 -22.766 1.00 52.60  ? 89  TRP   B CZ2 1 
ATOM   1019 C  CZ3 . TRP   B 2 80  ? -11.932 -14.101 -20.439 1.00 51.28  ? 89  TRP   B CZ3 1 
ATOM   1020 C  CH2 . TRP   B 2 80  ? -11.631 -14.331 -21.784 1.00 52.15  ? 89  TRP   B CH2 1 
ATOM   1021 N  N   . ASP   B 2 81  ? -17.909 -15.673 -20.854 1.00 55.86  ? 90  ASP   B N   1 
ATOM   1022 C  CA  . ASP   B 2 81  ? -17.901 -17.163 -20.914 1.00 57.69  ? 90  ASP   B CA  1 
ATOM   1023 C  C   . ASP   B 2 81  ? -16.469 -17.669 -21.043 1.00 59.15  ? 90  ASP   B C   1 
ATOM   1024 O  O   . ASP   B 2 81  ? -16.326 -18.886 -21.119 1.00 60.87  ? 90  ASP   B O   1 
ATOM   1025 C  CB  . ASP   B 2 81  ? -18.732 -17.709 -22.075 1.00 59.23  ? 90  ASP   B CB  1 
ATOM   1026 C  CG  . ASP   B 2 81  ? -18.250 -17.239 -23.506 1.00 61.22  ? 90  ASP   B CG  1 
ATOM   1027 O  OD1 . ASP   B 2 81  ? -17.167 -16.752 -23.634 1.00 62.75  ? 90  ASP   B OD1 1 
ATOM   1028 O  OD2 . ASP   B 2 81  ? -18.989 -17.533 -24.444 1.00 65.80  ? 90  ASP   B OD2 1 
ATOM   1029 N  N   . GLY   B 2 82  ? -15.478 -16.769 -21.109 1.00 59.31  ? 91  GLY   B N   1 
ATOM   1030 C  CA  . GLY   B 2 82  ? -14.042 -17.095 -21.212 1.00 59.08  ? 91  GLY   B CA  1 
ATOM   1031 C  C   . GLY   B 2 82  ? -13.596 -17.506 -22.607 1.00 60.62  ? 91  GLY   B C   1 
ATOM   1032 O  O   . GLY   B 2 82  ? -12.411 -17.948 -22.721 1.00 62.19  ? 91  GLY   B O   1 
ATOM   1033 N  N   . LEU   B 2 83  ? -14.477 -17.429 -23.610 1.00 60.50  ? 92  LEU   B N   1 
ATOM   1034 C  CA  . LEU   B 2 83  ? -14.250 -17.895 -25.004 1.00 62.67  ? 92  LEU   B CA  1 
ATOM   1035 C  C   . LEU   B 2 83  ? -14.526 -16.777 -26.005 1.00 64.04  ? 92  LEU   B C   1 
ATOM   1036 O  O   . LEU   B 2 83  ? -13.643 -16.481 -26.816 1.00 63.50  ? 92  LEU   B O   1 
ATOM   1037 C  CB  . LEU   B 2 83  ? -15.196 -19.053 -25.311 1.00 64.55  ? 92  LEU   B CB  1 
ATOM   1038 C  CG  . LEU   B 2 83  ? -14.756 -20.451 -24.860 1.00 65.94  ? 92  LEU   B CG  1 
ATOM   1039 C  CD1 . LEU   B 2 83  ? -15.579 -21.505 -25.588 1.00 67.87  ? 92  LEU   B CD1 1 
ATOM   1040 C  CD2 . LEU   B 2 83  ? -13.276 -20.694 -25.124 1.00 66.47  ? 92  LEU   B CD2 1 
ATOM   1041 N  N   . SER   B 2 84  ? -15.746 -16.238 -26.005 1.00 64.01  ? 93  SER   B N   1 
ATOM   1042 C  CA  . SER   B 2 84  ? -16.286 -15.416 -27.112 1.00 63.89  ? 93  SER   B CA  1 
ATOM   1043 C  C   . SER   B 2 84  ? -15.755 -13.987 -26.979 1.00 62.86  ? 93  SER   B C   1 
ATOM   1044 O  O   . SER   B 2 84  ? -15.378 -13.588 -25.843 1.00 61.32  ? 93  SER   B O   1 
ATOM   1045 C  CB  . SER   B 2 84  ? -17.790 -15.430 -27.102 1.00 65.59  ? 93  SER   B CB  1 
ATOM   1046 O  OG  . SER   B 2 84  ? -18.280 -16.369 -26.147 1.00 66.60  ? 93  SER   B OG  1 
ATOM   1047 N  N   . GLU   B 2 85  ? -15.737 -13.274 -28.109 1.00 61.33  ? 94  GLU   B N   1 
ATOM   1048 C  CA  . GLU   B 2 85  ? -15.481 -11.814 -28.201 1.00 59.55  ? 94  GLU   B CA  1 
ATOM   1049 C  C   . GLU   B 2 85  ? -16.612 -11.080 -27.471 1.00 55.61  ? 94  GLU   B C   1 
ATOM   1050 O  O   . GLU   B 2 85  ? -17.707 -11.661 -27.188 1.00 53.47  ? 94  GLU   B O   1 
ATOM   1051 C  CB  . GLU   B 2 85  ? -15.318 -11.348 -29.662 1.00 61.30  ? 94  GLU   B CB  1 
ATOM   1052 C  CG  . GLU   B 2 85  ? -13.978 -11.775 -30.299 1.00 62.37  ? 94  GLU   B CG  1 
ATOM   1053 C  CD  . GLU   B 2 85  ? -13.604 -11.318 -31.711 1.00 64.03  ? 94  GLU   B CD  1 
ATOM   1054 O  OE1 . GLU   B 2 85  ? -14.129 -10.289 -32.207 1.00 62.86  ? 94  GLU   B OE1 1 
ATOM   1055 O  OE2 . GLU   B 2 85  ? -12.752 -11.996 -32.323 1.00 65.24  ? 94  GLU   B OE2 1 
ATOM   1056 N  N   . VAL   B 2 86  ? -16.303 -9.845  -27.125 1.00 53.48  ? 95  VAL   B N   1 
ATOM   1057 C  CA  . VAL   B 2 86  ? -17.231 -8.947  -26.379 1.00 51.57  ? 95  VAL   B CA  1 
ATOM   1058 C  C   . VAL   B 2 86  ? -17.173 -7.576  -27.042 1.00 51.01  ? 95  VAL   B C   1 
ATOM   1059 O  O   . VAL   B 2 86  ? -16.238 -7.330  -27.825 1.00 52.44  ? 95  VAL   B O   1 
ATOM   1060 C  CB  . VAL   B 2 86  ? -16.859 -8.865  -24.879 1.00 49.44  ? 95  VAL   B CB  1 
ATOM   1061 C  CG1 . VAL   B 2 86  ? -16.724 -10.245 -24.274 1.00 49.22  ? 95  VAL   B CG1 1 
ATOM   1062 C  CG2 . VAL   B 2 86  ? -15.579 -8.073  -24.633 1.00 49.27  ? 95  VAL   B CG2 1 
ATOM   1063 N  N   . GLN   B 2 87  ? -18.090 -6.685  -26.675 1.00 50.33  ? 96  GLN   B N   1 
ATOM   1064 C  CA  . GLN   B 2 87  ? -17.991 -5.271  -27.101 1.00 50.49  ? 96  GLN   B CA  1 
ATOM   1065 C  C   . GLN   B 2 87  ? -17.872 -4.374  -25.868 1.00 47.95  ? 96  GLN   B C   1 
ATOM   1066 O  O   . GLN   B 2 87  ? -18.736 -4.441  -25.008 1.00 49.98  ? 96  GLN   B O   1 
ATOM   1067 C  CB  . GLN   B 2 87  ? -19.166 -4.896  -28.021 1.00 51.70  ? 96  GLN   B CB  1 
ATOM   1068 C  CG  . GLN   B 2 87  ? -18.960 -5.390  -29.444 1.00 53.34  ? 96  GLN   B CG  1 
ATOM   1069 C  CD  . GLN   B 2 87  ? -20.129 -5.143  -30.375 1.00 54.19  ? 96  GLN   B CD  1 
ATOM   1070 O  OE1 . GLN   B 2 87  ? -21.068 -4.381  -30.108 1.00 52.58  ? 96  GLN   B OE1 1 
ATOM   1071 N  NE2 . GLN   B 2 87  ? -20.074 -5.829  -31.499 1.00 55.85  ? 96  GLN   B NE2 1 
ATOM   1072 N  N   . LEU   B 2 88  ? -16.850 -3.530  -25.835 1.00 46.30  ? 97  LEU   B N   1 
ATOM   1073 C  CA  . LEU   B 2 88  ? -16.835 -2.320  -24.998 1.00 45.17  ? 97  LEU   B CA  1 
ATOM   1074 C  C   . LEU   B 2 88  ? -17.748 -1.265  -25.661 1.00 44.81  ? 97  LEU   B C   1 
ATOM   1075 O  O   . LEU   B 2 88  ? -17.429 -0.798  -26.749 1.00 45.77  ? 97  LEU   B O   1 
ATOM   1076 C  CB  . LEU   B 2 88  ? -15.397 -1.796  -24.914 1.00 45.52  ? 97  LEU   B CB  1 
ATOM   1077 C  CG  . LEU   B 2 88  ? -15.262 -0.508  -24.102 1.00 45.41  ? 97  LEU   B CG  1 
ATOM   1078 C  CD1 . LEU   B 2 88  ? -15.769 -0.723  -22.675 1.00 45.01  ? 97  LEU   B CD1 1 
ATOM   1079 C  CD2 . LEU   B 2 88  ? -13.836 0.011   -24.077 1.00 45.83  ? 97  LEU   B CD2 1 
ATOM   1080 N  N   A LEU   B 2 89  ? -18.875 -0.941  -25.033 0.25 43.97  ? 98  LEU   B N   1 
ATOM   1081 N  N   B LEU   B 2 89  ? -18.875 -0.941  -25.033 0.25 43.97  ? 98  LEU   B N   1 
ATOM   1082 N  N   C LEU   B 2 89  ? -18.870 -0.932  -25.030 0.25 43.86  ? 98  LEU   B N   1 
ATOM   1083 N  N   D LEU   B 2 89  ? -18.870 -0.932  -25.030 0.25 43.86  ? 98  LEU   B N   1 
ATOM   1084 C  CA  A LEU   B 2 89  ? -19.679 0.249   -25.408 0.25 43.89  ? 98  LEU   B CA  1 
ATOM   1085 C  CA  B LEU   B 2 89  ? -19.679 0.249   -25.408 0.25 43.89  ? 98  LEU   B CA  1 
ATOM   1086 C  CA  C LEU   B 2 89  ? -19.683 0.254   -25.407 0.25 43.71  ? 98  LEU   B CA  1 
ATOM   1087 C  CA  D LEU   B 2 89  ? -19.683 0.254   -25.407 0.25 43.71  ? 98  LEU   B CA  1 
ATOM   1088 C  C   A LEU   B 2 89  ? -18.982 1.461   -24.792 0.25 43.60  ? 98  LEU   B C   1 
ATOM   1089 C  C   B LEU   B 2 89  ? -18.982 1.461   -24.792 0.25 43.60  ? 98  LEU   B C   1 
ATOM   1090 C  C   C LEU   B 2 89  ? -18.990 1.471   -24.796 0.25 43.50  ? 98  LEU   B C   1 
ATOM   1091 C  C   D LEU   B 2 89  ? -18.990 1.471   -24.796 0.25 43.50  ? 98  LEU   B C   1 
ATOM   1092 O  O   A LEU   B 2 89  ? -19.360 1.851   -23.682 0.25 43.59  ? 98  LEU   B O   1 
ATOM   1093 O  O   B LEU   B 2 89  ? -19.360 1.851   -23.682 0.25 43.59  ? 98  LEU   B O   1 
ATOM   1094 O  O   C LEU   B 2 89  ? -19.377 1.872   -23.692 0.25 43.50  ? 98  LEU   B O   1 
ATOM   1095 O  O   D LEU   B 2 89  ? -19.377 1.872   -23.692 0.25 43.50  ? 98  LEU   B O   1 
ATOM   1096 C  CB  A LEU   B 2 89  ? -21.117 0.078   -24.913 0.25 43.27  ? 98  LEU   B CB  1 
ATOM   1097 C  CB  B LEU   B 2 89  ? -21.117 0.078   -24.913 0.25 43.27  ? 98  LEU   B CB  1 
ATOM   1098 C  CB  C LEU   B 2 89  ? -21.118 0.055   -24.911 0.25 42.95  ? 98  LEU   B CB  1 
ATOM   1099 C  CB  D LEU   B 2 89  ? -21.118 0.055   -24.911 0.25 42.95  ? 98  LEU   B CB  1 
ATOM   1100 C  CG  A LEU   B 2 89  ? -22.102 1.171   -25.351 0.25 43.32  ? 98  LEU   B CG  1 
ATOM   1101 C  CG  B LEU   B 2 89  ? -22.102 1.171   -25.351 0.25 43.32  ? 98  LEU   B CG  1 
ATOM   1102 C  CG  C LEU   B 2 89  ? -22.093 1.228   -25.097 0.25 42.74  ? 98  LEU   B CG  1 
ATOM   1103 C  CG  D LEU   B 2 89  ? -22.093 1.228   -25.097 0.25 42.74  ? 98  LEU   B CG  1 
ATOM   1104 C  CD1 A LEU   B 2 89  ? -22.124 1.315   -26.864 0.25 44.17  ? 98  LEU   B CD1 1 
ATOM   1105 C  CD1 B LEU   B 2 89  ? -22.124 1.315   -26.864 0.25 44.17  ? 98  LEU   B CD1 1 
ATOM   1106 C  CD1 C LEU   B 2 89  ? -21.532 2.321   -25.993 0.25 43.11  ? 98  LEU   B CD1 1 
ATOM   1107 C  CD1 D LEU   B 2 89  ? -21.532 2.321   -25.993 0.25 43.11  ? 98  LEU   B CD1 1 
ATOM   1108 C  CD2 A LEU   B 2 89  ? -23.505 0.890   -24.826 0.25 42.96  ? 98  LEU   B CD2 1 
ATOM   1109 C  CD2 B LEU   B 2 89  ? -23.505 0.890   -24.826 0.25 42.96  ? 98  LEU   B CD2 1 
ATOM   1110 C  CD2 C LEU   B 2 89  ? -23.431 0.735   -25.631 0.25 42.87  ? 98  LEU   B CD2 1 
ATOM   1111 C  CD2 D LEU   B 2 89  ? -23.431 0.735   -25.631 0.25 42.87  ? 98  LEU   B CD2 1 
ATOM   1112 N  N   . ALA   B 2 90  ? -17.946 1.973   -25.459 1.00 44.36  ? 99  ALA   B N   1 
ATOM   1113 C  CA  . ALA   B 2 90  ? -17.117 3.083   -24.938 1.00 44.88  ? 99  ALA   B CA  1 
ATOM   1114 C  C   . ALA   B 2 90  ? -17.899 4.389   -25.031 1.00 45.95  ? 99  ALA   B C   1 
ATOM   1115 O  O   . ALA   B 2 90  ? -18.492 4.643   -26.107 1.00 47.81  ? 99  ALA   B O   1 
ATOM   1116 C  CB  . ALA   B 2 90  ? -15.844 3.209   -25.713 1.00 45.58  ? 99  ALA   B CB  1 
ATOM   1117 N  N   . VAL   B 2 91  ? -17.894 5.193   -23.966 1.00 45.64  ? 100 VAL   B N   1 
ATOM   1118 C  CA  . VAL   B 2 91  ? -18.502 6.546   -24.003 1.00 45.41  ? 100 VAL   B CA  1 
ATOM   1119 C  C   . VAL   B 2 91  ? -17.464 7.588   -23.600 1.00 45.75  ? 100 VAL   B C   1 
ATOM   1120 O  O   . VAL   B 2 91  ? -17.461 8.053   -22.458 1.00 44.83  ? 100 VAL   B O   1 
ATOM   1121 C  CB  . VAL   B 2 91  ? -19.769 6.560   -23.157 1.00 44.72  ? 100 VAL   B CB  1 
ATOM   1122 C  CG1 . VAL   B 2 91  ? -20.379 7.949   -23.150 1.00 44.82  ? 100 VAL   B CG1 1 
ATOM   1123 C  CG2 . VAL   B 2 91  ? -20.737 5.497   -23.654 1.00 45.01  ? 100 VAL   B CG2 1 
ATOM   1124 N  N   . PRO   B 2 92  ? -16.577 7.998   -24.548 1.00 48.04  ? 101 PRO   B N   1 
ATOM   1125 C  CA  . PRO   B 2 92  ? -15.445 8.875   -24.250 1.00 48.98  ? 101 PRO   B CA  1 
ATOM   1126 C  C   . PRO   B 2 92  ? -15.944 10.298  -24.005 1.00 50.20  ? 101 PRO   B C   1 
ATOM   1127 O  O   . PRO   B 2 92  ? -17.046 10.646  -24.416 1.00 50.38  ? 101 PRO   B O   1 
ATOM   1128 C  CB  . PRO   B 2 92  ? -14.525 8.759   -25.470 1.00 50.40  ? 101 PRO   B CB  1 
ATOM   1129 C  CG  . PRO   B 2 92  ? -15.143 7.663   -26.333 1.00 50.62  ? 101 PRO   B CG  1 
ATOM   1130 C  CD  . PRO   B 2 92  ? -16.616 7.658   -25.973 1.00 49.04  ? 101 PRO   B CD  1 
ATOM   1131 N  N   . PRO   B 2 93  ? -15.195 11.136  -23.256 1.00 51.45  ? 102 PRO   B N   1 
ATOM   1132 C  CA  . PRO   B 2 93  ? -15.580 12.539  -23.060 1.00 52.94  ? 102 PRO   B CA  1 
ATOM   1133 C  C   . PRO   B 2 93  ? -15.756 13.324  -24.375 1.00 53.29  ? 102 PRO   B C   1 
ATOM   1134 O  O   . PRO   B 2 93  ? -14.909 13.229  -25.265 1.00 53.77  ? 102 PRO   B O   1 
ATOM   1135 C  CB  . PRO   B 2 93  ? -14.432 13.091  -22.182 1.00 53.08  ? 102 PRO   B CB  1 
ATOM   1136 C  CG  . PRO   B 2 93  ? -13.967 11.856  -21.412 1.00 52.17  ? 102 PRO   B CG  1 
ATOM   1137 C  CD  . PRO   B 2 93  ? -14.006 10.775  -22.470 1.00 52.39  ? 102 PRO   B CD  1 
ATOM   1138 N  N   . GLY   B 2 94  ? -16.887 14.041  -24.472 1.00 52.89  ? 103 GLY   B N   1 
ATOM   1139 C  CA  . GLY   B 2 94  ? -17.292 14.860  -25.626 1.00 52.98  ? 103 GLY   B CA  1 
ATOM   1140 C  C   . GLY   B 2 94  ? -17.462 14.084  -26.928 1.00 53.89  ? 103 GLY   B C   1 
ATOM   1141 O  O   . GLY   B 2 94  ? -17.577 14.720  -27.944 1.00 57.46  ? 103 GLY   B O   1 
ATOM   1142 N  N   . GLU   B 2 95  ? -17.470 12.752  -26.935 1.00 54.26  ? 104 GLU   B N   1 
ATOM   1143 C  CA  . GLU   B 2 95  ? -17.533 11.915  -28.170 1.00 53.38  ? 104 GLU   B CA  1 
ATOM   1144 C  C   . GLU   B 2 95  ? -18.770 11.005  -28.064 1.00 52.74  ? 104 GLU   B C   1 
ATOM   1145 O  O   . GLU   B 2 95  ? -19.206 10.748  -26.937 1.00 51.89  ? 104 GLU   B O   1 
ATOM   1146 C  CB  . GLU   B 2 95  ? -16.202 11.143  -28.337 1.00 54.08  ? 104 GLU   B CB  1 
ATOM   1147 C  CG  . GLU   B 2 95  ? -14.972 12.050  -28.565 1.00 54.83  ? 104 GLU   B CG  1 
ATOM   1148 C  CD  . GLU   B 2 95  ? -13.606 11.350  -28.610 1.00 56.98  ? 104 GLU   B CD  1 
ATOM   1149 O  OE1 . GLU   B 2 95  ? -13.558 10.118  -28.323 1.00 55.79  ? 104 GLU   B OE1 1 
ATOM   1150 O  OE2 . GLU   B 2 95  ? -12.560 12.033  -28.926 1.00 59.00  ? 104 GLU   B OE2 1 
ATOM   1151 N  N   . ARG   B 2 96  ? -19.312 10.527  -29.179 1.00 55.14  ? 105 ARG   B N   1 
ATOM   1152 C  CA  . ARG   B 2 96  ? -20.501 9.642   -29.227 1.00 56.98  ? 105 ARG   B CA  1 
ATOM   1153 C  C   . ARG   B 2 96  ? -20.156 8.255   -28.699 1.00 55.45  ? 105 ARG   B C   1 
ATOM   1154 O  O   . ARG   B 2 96  ? -18.999 7.816   -28.868 1.00 54.14  ? 105 ARG   B O   1 
ATOM   1155 C  CB  . ARG   B 2 96  ? -21.022 9.473   -30.658 1.00 62.93  ? 105 ARG   B CB  1 
ATOM   1156 C  CG  . ARG   B 2 96  ? -22.501 9.092   -30.734 1.00 67.41  ? 105 ARG   B CG  1 
ATOM   1157 C  CD  . ARG   B 2 96  ? -23.237 9.677   -31.950 1.00 71.67  ? 105 ARG   B CD  1 
ATOM   1158 N  NE  . ARG   B 2 96  ? -22.484 9.483   -33.178 1.00 75.55  ? 105 ARG   B NE  1 
ATOM   1159 C  CZ  . ARG   B 2 96  ? -21.940 10.440  -33.942 1.00 81.01  ? 105 ARG   B CZ  1 
ATOM   1160 N  NH1 . ARG   B 2 96  ? -22.090 11.731  -33.662 1.00 80.40  ? 105 ARG   B NH1 1 
ATOM   1161 N  NH2 . ARG   B 2 96  ? -21.251 10.077  -35.019 1.00 83.05  ? 105 ARG   B NH2 1 
ATOM   1162 N  N   . ALA   B 2 97  ? -21.161 7.615   -28.098 1.00 53.54  ? 106 ALA   B N   1 
ATOM   1163 C  CA  . ALA   B 2 97  ? -21.161 6.196   -27.741 1.00 52.97  ? 106 ALA   B CA  1 
ATOM   1164 C  C   . ALA   B 2 97  ? -20.665 5.423   -28.959 1.00 54.00  ? 106 ALA   B C   1 
ATOM   1165 O  O   . ALA   B 2 97  ? -21.305 5.524   -29.994 1.00 54.27  ? 106 ALA   B O   1 
ATOM   1166 C  CB  . ALA   B 2 97  ? -22.544 5.805   -27.312 1.00 51.24  ? 106 ALA   B CB  1 
ATOM   1167 N  N   . LYS   B 2 98  ? -19.576 4.659   -28.820 1.00 55.47  ? 107 LYS   B N   1 
ATOM   1168 C  CA  . LYS   B 2 98  ? -19.012 3.786   -29.878 1.00 58.86  ? 107 LYS   B CA  1 
ATOM   1169 C  C   . LYS   B 2 98  ? -18.796 2.359   -29.352 1.00 57.01  ? 107 LYS   B C   1 
ATOM   1170 O  O   . LYS   B 2 98  ? -18.181 2.249   -28.290 1.00 56.96  ? 107 LYS   B O   1 
ATOM   1171 C  CB  . LYS   B 2 98  ? -17.656 4.368   -30.282 1.00 63.63  ? 107 LYS   B CB  1 
ATOM   1172 C  CG  . LYS   B 2 98  ? -17.131 3.957   -31.647 1.00 68.52  ? 107 LYS   B CG  1 
ATOM   1173 C  CD  . LYS   B 2 98  ? -15.717 4.482   -31.921 1.00 73.74  ? 107 LYS   B CD  1 
ATOM   1174 C  CE  . LYS   B 2 98  ? -14.920 4.714   -30.643 1.00 75.35  ? 107 LYS   B CE  1 
ATOM   1175 N  NZ  . LYS   B 2 98  ? -13.462 4.500   -30.831 1.00 78.93  ? 107 LYS   B NZ  1 
ATOM   1176 N  N   . ASN   B 2 99  ? -19.276 1.319   -30.045 1.00 55.35  ? 108 ASN   B N   1 
ATOM   1177 C  CA  . ASN   B 2 99  ? -18.932 -0.104  -29.758 1.00 54.66  ? 108 ASN   B CA  1 
ATOM   1178 C  C   . ASN   B 2 99  ? -17.531 -0.434  -30.289 1.00 55.53  ? 108 ASN   B C   1 
ATOM   1179 O  O   . ASN   B 2 99  ? -17.237 -0.126  -31.448 1.00 58.84  ? 108 ASN   B O   1 
ATOM   1180 C  CB  . ASN   B 2 99  ? -19.935 -1.118  -30.313 1.00 54.04  ? 108 ASN   B CB  1 
ATOM   1181 C  CG  . ASN   B 2 99  ? -21.290 -0.917  -29.694 1.00 53.83  ? 108 ASN   B CG  1 
ATOM   1182 O  OD1 . ASN   B 2 99  ? -21.770 0.222   -29.687 1.00 55.17  ? 108 ASN   B OD1 1 
ATOM   1183 N  ND2 . ASN   B 2 99  ? -21.925 -1.975  -29.214 1.00 52.48  ? 108 ASN   B ND2 1 
ATOM   1184 N  N   . ILE   B 2 100 ? -16.712 -1.118  -29.506 1.00 53.76  ? 109 ILE   B N   1 
ATOM   1185 C  CA  . ILE   B 2 100 ? -15.356 -1.559  -29.951 1.00 54.36  ? 109 ILE   B CA  1 
ATOM   1186 C  C   . ILE   B 2 100 ? -15.296 -3.027  -29.616 1.00 53.87  ? 109 ILE   B C   1 
ATOM   1187 O  O   . ILE   B 2 100 ? -15.432 -3.355  -28.444 1.00 54.90  ? 109 ILE   B O   1 
ATOM   1188 C  CB  . ILE   B 2 100 ? -14.240 -0.764  -29.252 1.00 54.26  ? 109 ILE   B CB  1 
ATOM   1189 C  CG1 . ILE   B 2 100 ? -14.512 0.745   -29.306 1.00 54.77  ? 109 ILE   B CG1 1 
ATOM   1190 C  CG2 . ILE   B 2 100 ? -12.867 -1.130  -29.780 1.00 55.27  ? 109 ILE   B CG2 1 
ATOM   1191 C  CD1 . ILE   B 2 100 ? -14.254 1.370   -30.671 1.00 55.51  ? 109 ILE   B CD1 1 
ATOM   1192 N  N   . GLN   B 2 101 ? -15.214 -3.885  -30.604 1.00 55.73  ? 110 GLN   B N   1 
ATOM   1193 C  CA  . GLN   B 2 101 ? -15.259 -5.338  -30.359 1.00 57.09  ? 110 GLN   B CA  1 
ATOM   1194 C  C   . GLN   B 2 101 ? -13.844 -5.861  -30.112 1.00 58.36  ? 110 GLN   B C   1 
ATOM   1195 O  O   . GLN   B 2 101 ? -12.912 -5.379  -30.816 1.00 58.61  ? 110 GLN   B O   1 
ATOM   1196 C  CB  . GLN   B 2 101 ? -15.879 -6.058  -31.534 1.00 58.69  ? 110 GLN   B CB  1 
ATOM   1197 C  CG  . GLN   B 2 101 ? -16.026 -7.535  -31.286 1.00 59.25  ? 110 GLN   B CG  1 
ATOM   1198 C  CD  . GLN   B 2 101 ? -17.034 -8.113  -32.237 1.00 60.19  ? 110 GLN   B CD  1 
ATOM   1199 O  OE1 . GLN   B 2 101 ? -18.050 -7.489  -32.562 1.00 60.99  ? 110 GLN   B OE1 1 
ATOM   1200 N  NE2 . GLN   B 2 101 ? -16.722 -9.294  -32.725 1.00 60.34  ? 110 GLN   B NE2 1 
ATOM   1201 N  N   . THR   B 2 102 ? -13.709 -6.809  -29.162 1.00 58.19  ? 111 THR   B N   1 
ATOM   1202 C  CA  . THR   B 2 102 ? -12.408 -7.399  -28.749 1.00 57.86  ? 111 THR   B CA  1 
ATOM   1203 C  C   . THR   B 2 102 ? -12.630 -8.766  -28.092 1.00 57.04  ? 111 THR   B C   1 
ATOM   1204 O  O   . THR   B 2 102 ? -13.746 -9.034  -27.588 1.00 58.65  ? 111 THR   B O   1 
ATOM   1205 C  CB  . THR   B 2 102 ? -11.659 -6.368  -27.885 1.00 58.03  ? 111 THR   B CB  1 
ATOM   1206 O  OG1 . THR   B 2 102 ? -10.304 -6.812  -27.758 1.00 58.22  ? 111 THR   B OG1 1 
ATOM   1207 C  CG2 . THR   B 2 102 ? -12.308 -6.083  -26.545 1.00 56.52  ? 111 THR   B CG2 1 
ATOM   1208 N  N   . LEU   B 2 103 ? -11.599 -9.615  -28.146 1.00 55.92  ? 112 LEU   B N   1 
ATOM   1209 C  CA  . LEU   B 2 103 ? -11.477 -10.883 -27.383 1.00 55.29  ? 112 LEU   B CA  1 
ATOM   1210 C  C   . LEU   B 2 103 ? -10.658 -10.610 -26.111 1.00 53.72  ? 112 LEU   B C   1 
ATOM   1211 O  O   . LEU   B 2 103 ? -9.430  -10.236 -26.172 1.00 53.40  ? 112 LEU   B O   1 
ATOM   1212 C  CB  . LEU   B 2 103 ? -10.751 -11.953 -28.196 1.00 56.94  ? 112 LEU   B CB  1 
ATOM   1213 C  CG  . LEU   B 2 103 ? -10.542 -13.228 -27.392 1.00 56.80  ? 112 LEU   B CG  1 
ATOM   1214 C  CD1 . LEU   B 2 103 ? -11.850 -13.984 -27.288 1.00 56.81  ? 112 LEU   B CD1 1 
ATOM   1215 C  CD2 . LEU   B 2 103 ? -9.441  -14.083 -27.971 1.00 58.68  ? 112 LEU   B CD2 1 
ATOM   1216 N  N   . PRO   B 2 104 ? -11.288 -10.753 -24.923 1.00 52.64  ? 113 PRO   B N   1 
ATOM   1217 C  CA  . PRO   B 2 104 ? -10.619 -10.421 -23.674 1.00 52.19  ? 113 PRO   B CA  1 
ATOM   1218 C  C   . PRO   B 2 104 ? -9.402  -11.303 -23.382 1.00 53.49  ? 113 PRO   B C   1 
ATOM   1219 O  O   . PRO   B 2 104 ? -9.364  -12.458 -23.817 1.00 54.40  ? 113 PRO   B O   1 
ATOM   1220 C  CB  . PRO   B 2 104 ? -11.684 -10.654 -22.602 1.00 51.03  ? 113 PRO   B CB  1 
ATOM   1221 C  CG  . PRO   B 2 104 ? -12.983 -10.473 -23.339 1.00 50.78  ? 113 PRO   B CG  1 
ATOM   1222 C  CD  . PRO   B 2 104 ? -12.718 -11.057 -24.716 1.00 52.68  ? 113 PRO   B CD  1 
ATOM   1223 N  N   . GLY   B 2 105 ? -8.425  -10.680 -22.721 1.00 54.40  ? 114 GLY   B N   1 
ATOM   1224 C  CA  . GLY   B 2 105 ? -7.274  -11.329 -22.080 1.00 55.69  ? 114 GLY   B CA  1 
ATOM   1225 C  C   . GLY   B 2 105 ? -7.668  -11.746 -20.670 1.00 55.32  ? 114 GLY   B C   1 
ATOM   1226 O  O   . GLY   B 2 105 ? -8.890  -11.850 -20.404 1.00 52.58  ? 114 GLY   B O   1 
ATOM   1227 N  N   . ILE   B 2 106 ? -6.675  -11.975 -19.808 1.00 55.83  ? 115 ILE   B N   1 
ATOM   1228 C  CA  . ILE   B 2 106 ? -6.881  -12.592 -18.465 1.00 55.31  ? 115 ILE   B CA  1 
ATOM   1229 C  C   . ILE   B 2 106 ? -6.032  -11.869 -17.432 1.00 54.07  ? 115 ILE   B C   1 
ATOM   1230 O  O   . ILE   B 2 106 ? -4.863  -11.674 -17.664 1.00 55.39  ? 115 ILE   B O   1 
ATOM   1231 C  CB  . ILE   B 2 106 ? -6.520  -14.078 -18.510 1.00 57.87  ? 115 ILE   B CB  1 
ATOM   1232 C  CG1 . ILE   B 2 106 ? -7.413  -14.850 -19.473 1.00 59.82  ? 115 ILE   B CG1 1 
ATOM   1233 C  CG2 . ILE   B 2 106 ? -6.574  -14.671 -17.124 1.00 59.32  ? 115 ILE   B CG2 1 
ATOM   1234 C  CD1 . ILE   B 2 106 ? -8.770  -15.123 -18.949 1.00 58.90  ? 115 ILE   B CD1 1 
ATOM   1235 N  N   . PHE   B 2 107 ? -6.625  -11.497 -16.315 1.00 53.74  ? 116 PHE   B N   1 
ATOM   1236 C  CA  . PHE   B 2 107 ? -5.908  -11.182 -15.069 1.00 52.78  ? 116 PHE   B CA  1 
ATOM   1237 C  C   . PHE   B 2 107 ? -5.856  -12.480 -14.279 1.00 54.48  ? 116 PHE   B C   1 
ATOM   1238 O  O   . PHE   B 2 107 ? -6.939  -12.968 -13.896 1.00 54.04  ? 116 PHE   B O   1 
ATOM   1239 C  CB  . PHE   B 2 107 ? -6.660  -10.127 -14.287 1.00 51.25  ? 116 PHE   B CB  1 
ATOM   1240 C  CG  . PHE   B 2 107 ? -6.445  -8.718  -14.749 1.00 50.59  ? 116 PHE   B CG  1 
ATOM   1241 C  CD1 . PHE   B 2 107 ? -5.645  -8.429  -15.841 1.00 51.56  ? 116 PHE   B CD1 1 
ATOM   1242 C  CD2 . PHE   B 2 107 ? -7.042  -7.683  -14.061 1.00 49.27  ? 116 PHE   B CD2 1 
ATOM   1243 C  CE1 . PHE   B 2 107 ? -5.445  -7.125  -16.239 1.00 51.90  ? 116 PHE   B CE1 1 
ATOM   1244 C  CE2 . PHE   B 2 107 ? -6.824  -6.380  -14.456 1.00 50.23  ? 116 PHE   B CE2 1 
ATOM   1245 C  CZ  . PHE   B 2 107 ? -6.032  -6.103  -15.541 1.00 50.07  ? 116 PHE   B CZ  1 
ATOM   1246 N  N   . LYS   B 2 108 ? -4.665  -13.038 -14.101 1.00 55.12  ? 117 LYS   B N   1 
ATOM   1247 C  CA  . LYS   B 2 108 ? -4.442  -14.207 -13.213 1.00 58.35  ? 117 LYS   B CA  1 
ATOM   1248 C  C   . LYS   B 2 108 ? -4.120  -13.685 -11.800 1.00 55.61  ? 117 LYS   B C   1 
ATOM   1249 O  O   . LYS   B 2 108 ? -3.147  -12.916 -11.664 1.00 55.24  ? 117 LYS   B O   1 
ATOM   1250 C  CB  . LYS   B 2 108 ? -3.342  -15.105 -13.804 1.00 63.30  ? 117 LYS   B CB  1 
ATOM   1251 C  CG  . LYS   B 2 108 ? -3.836  -16.111 -14.836 1.00 69.39  ? 117 LYS   B CG  1 
ATOM   1252 C  CD  . LYS   B 2 108 ? -2.872  -16.379 -15.996 1.00 76.11  ? 117 LYS   B CD  1 
ATOM   1253 C  CE  . LYS   B 2 108 ? -3.549  -16.811 -17.299 1.00 82.40  ? 117 LYS   B CE  1 
ATOM   1254 N  NZ  . LYS   B 2 108 ? -2.636  -17.536 -18.245 1.00 88.04  ? 117 LYS   B NZ  1 
ATOM   1255 N  N   . THR   B 2 109 ? -4.941  -14.026 -10.805 1.00 54.39  ? 118 THR   B N   1 
ATOM   1256 C  CA  . THR   B 2 109 ? -4.783  -13.553 -9.394  1.00 54.80  ? 118 THR   B CA  1 
ATOM   1257 C  C   . THR   B 2 109 ? -4.778  -14.767 -8.460  1.00 57.71  ? 118 THR   B C   1 
ATOM   1258 O  O   . THR   B 2 109 ? -5.285  -15.833 -8.859  1.00 56.75  ? 118 THR   B O   1 
ATOM   1259 C  CB  . THR   B 2 109 ? -5.828  -12.507 -8.967  1.00 53.31  ? 118 THR   B CB  1 
ATOM   1260 O  OG1 . THR   B 2 109 ? -7.014  -13.134 -8.472  1.00 51.76  ? 118 THR   B OG1 1 
ATOM   1261 C  CG2 . THR   B 2 109 ? -6.173  -11.528 -10.066 1.00 52.72  ? 118 THR   B CG2 1 
ATOM   1262 N  N   . LYS   B 2 110 ? -4.233  -14.599 -7.251  1.00 62.32  ? 119 LYS   B N   1 
ATOM   1263 C  CA  . LYS   B 2 110 ? -4.173  -15.641 -6.183  1.00 63.34  ? 119 LYS   B CA  1 
ATOM   1264 C  C   . LYS   B 2 110 ? -5.598  -16.157 -5.908  1.00 62.74  ? 119 LYS   B C   1 
ATOM   1265 O  O   . LYS   B 2 110 ? -5.727  -17.355 -5.596  1.00 65.00  ? 119 LYS   B O   1 
ATOM   1266 C  CB  . LYS   B 2 110 ? -3.485  -15.067 -4.936  1.00 63.90  ? 119 LYS   B CB  1 
ATOM   1267 C  CG  . LYS   B 2 110 ? -4.349  -14.208 -4.018  1.00 66.49  ? 119 LYS   B CG  1 
ATOM   1268 C  CD  . LYS   B 2 110 ? -3.570  -13.285 -3.075  1.00 67.25  ? 119 LYS   B CD  1 
ATOM   1269 C  CE  . LYS   B 2 110 ? -4.128  -13.237 -1.665  1.00 69.04  ? 119 LYS   B CE  1 
ATOM   1270 N  NZ  . LYS   B 2 110 ? -5.465  -12.597 -1.622  1.00 71.37  ? 119 LYS   B NZ  1 
ATOM   1271 N  N   . ASP   B 2 111 ? -6.620  -15.307 -6.073  1.00 59.31  ? 120 ASP   B N   1 
ATOM   1272 C  CA  . ASP   B 2 111 ? -8.049  -15.625 -5.811  1.00 58.30  ? 120 ASP   B CA  1 
ATOM   1273 C  C   . ASP   B 2 111 ? -8.799  -16.055 -7.074  1.00 57.97  ? 120 ASP   B C   1 
ATOM   1274 O  O   . ASP   B 2 111 ? -10.016 -16.264 -6.947  1.00 58.35  ? 120 ASP   B O   1 
ATOM   1275 C  CB  . ASP   B 2 111 ? -8.787  -14.414 -5.243  1.00 58.87  ? 120 ASP   B CB  1 
ATOM   1276 C  CG  . ASP   B 2 111 ? -8.263  -13.968 -3.897  1.00 60.08  ? 120 ASP   B CG  1 
ATOM   1277 O  OD1 . ASP   B 2 111 ? -7.473  -14.680 -3.326  1.00 60.71  ? 120 ASP   B OD1 1 
ATOM   1278 O  OD2 . ASP   B 2 111 ? -8.684  -12.920 -3.425  1.00 67.34  ? 120 ASP   B OD2 1 
ATOM   1279 N  N   . GLY   B 2 112 ? -8.157  -16.139 -8.245  1.00 57.23  ? 121 GLY   B N   1 
ATOM   1280 C  CA  . GLY   B 2 112 ? -8.836  -16.541 -9.492  1.00 57.46  ? 121 GLY   B CA  1 
ATOM   1281 C  C   . GLY   B 2 112 ? -8.578  -15.635 -10.697 1.00 57.08  ? 121 GLY   B C   1 
ATOM   1282 O  O   . GLY   B 2 112 ? -8.070  -14.535 -10.523 1.00 56.15  ? 121 GLY   B O   1 
ATOM   1283 N  N   . ASP   B 2 113 ? -8.970  -16.107 -11.888 1.00 57.36  ? 122 ASP   B N   1 
ATOM   1284 C  CA  . ASP   B 2 113 ? -8.811  -15.439 -13.206 1.00 57.08  ? 122 ASP   B CA  1 
ATOM   1285 C  C   . ASP   B 2 113 ? -10.008 -14.529 -13.473 1.00 56.36  ? 122 ASP   B C   1 
ATOM   1286 O  O   . ASP   B 2 113 ? -11.149 -14.965 -13.206 1.00 54.44  ? 122 ASP   B O   1 
ATOM   1287 C  CB  . ASP   B 2 113 ? -8.785  -16.445 -14.347 1.00 58.80  ? 122 ASP   B CB  1 
ATOM   1288 C  CG  . ASP   B 2 113 ? -7.601  -17.385 -14.326 1.00 62.48  ? 122 ASP   B CG  1 
ATOM   1289 O  OD1 . ASP   B 2 113 ? -6.783  -17.275 -13.389 1.00 64.03  ? 122 ASP   B OD1 1 
ATOM   1290 O  OD2 . ASP   B 2 113 ? -7.513  -18.223 -15.259 1.00 66.18  ? 122 ASP   B OD2 1 
ATOM   1291 N  N   . ILE   B 2 114 ? -9.742  -13.332 -13.998 1.00 56.18  ? 123 ILE   B N   1 
ATOM   1292 C  CA  . ILE   B 2 114 ? -10.758 -12.351 -14.469 1.00 54.75  ? 123 ILE   B CA  1 
ATOM   1293 C  C   . ILE   B 2 114 ? -10.468 -12.048 -15.935 1.00 52.25  ? 123 ILE   B C   1 
ATOM   1294 O  O   . ILE   B 2 114 ? -9.284  -11.874 -16.296 1.00 51.25  ? 123 ILE   B O   1 
ATOM   1295 C  CB  . ILE   B 2 114 ? -10.718 -11.045 -13.658 1.00 55.89  ? 123 ILE   B CB  1 
ATOM   1296 C  CG1 . ILE   B 2 114 ? -10.051 -11.193 -12.296 1.00 58.90  ? 123 ILE   B CG1 1 
ATOM   1297 C  CG2 . ILE   B 2 114 ? -12.102 -10.474 -13.517 1.00 56.15  ? 123 ILE   B CG2 1 
ATOM   1298 C  CD1 . ILE   B 2 114 ? -9.739  -9.854  -11.644 1.00 60.09  ? 123 ILE   B CD1 1 
ATOM   1299 N  N   . GLY   B 2 115 ? -11.510 -11.924 -16.741 1.00 50.47  ? 124 GLY   B N   1 
ATOM   1300 C  CA  . GLY   B 2 115 ? -11.391 -11.306 -18.077 1.00 50.28  ? 124 GLY   B CA  1 
ATOM   1301 C  C   . GLY   B 2 115 ? -10.793 -9.908  -17.968 1.00 49.38  ? 124 GLY   B C   1 
ATOM   1302 O  O   . GLY   B 2 115 ? -10.920 -9.236  -16.916 1.00 47.70  ? 124 GLY   B O   1 
ATOM   1303 N  N   . ALA   B 2 116 ? -10.051 -9.533  -18.987 1.00 51.85  ? 125 ALA   B N   1 
ATOM   1304 C  CA  . ALA   B 2 116 ? -9.403  -8.214  -19.118 1.00 52.66  ? 125 ALA   B CA  1 
ATOM   1305 C  C   . ALA   B 2 116 ? -9.581  -7.778  -20.578 1.00 52.79  ? 125 ALA   B C   1 
ATOM   1306 O  O   . ALA   B 2 116 ? -9.500  -8.632  -21.494 1.00 53.54  ? 125 ALA   B O   1 
ATOM   1307 C  CB  . ALA   B 2 116 ? -7.948  -8.295  -18.706 1.00 53.84  ? 125 ALA   B CB  1 
ATOM   1308 N  N   A VAL   B 2 117 ? -9.836  -6.487  -20.800 0.25 52.29  ? 126 VAL   B N   1 
ATOM   1309 N  N   B VAL   B 2 117 ? -9.810  -6.476  -20.783 0.25 52.30  ? 126 VAL   B N   1 
ATOM   1310 N  N   C VAL   B 2 117 ? -9.836  -6.487  -20.800 0.25 52.29  ? 126 VAL   B N   1 
ATOM   1311 N  N   D VAL   B 2 117 ? -9.810  -6.476  -20.783 0.25 52.30  ? 126 VAL   B N   1 
ATOM   1312 C  CA  A VAL   B 2 117 ? -9.977  -5.907  -22.167 0.25 53.32  ? 126 VAL   B CA  1 
ATOM   1313 C  CA  B VAL   B 2 117 ? -10.003 -5.840  -22.119 0.25 53.29  ? 126 VAL   B CA  1 
ATOM   1314 C  CA  C VAL   B 2 117 ? -9.977  -5.907  -22.167 0.25 53.32  ? 126 VAL   B CA  1 
ATOM   1315 C  CA  D VAL   B 2 117 ? -10.003 -5.840  -22.119 0.25 53.29  ? 126 VAL   B CA  1 
ATOM   1316 C  C   A VAL   B 2 117 ? -8.868  -4.866  -22.366 0.25 53.75  ? 126 VAL   B C   1 
ATOM   1317 C  C   B VAL   B 2 117 ? -8.857  -4.845  -22.356 0.25 53.75  ? 126 VAL   B C   1 
ATOM   1318 C  C   C VAL   B 2 117 ? -8.868  -4.866  -22.366 0.25 53.75  ? 126 VAL   B C   1 
ATOM   1319 C  C   D VAL   B 2 117 ? -8.857  -4.845  -22.356 0.25 53.75  ? 126 VAL   B C   1 
ATOM   1320 O  O   A VAL   B 2 117 ? -8.711  -3.989  -21.496 0.25 53.52  ? 126 VAL   B O   1 
ATOM   1321 O  O   B VAL   B 2 117 ? -8.662  -3.963  -21.497 0.25 53.52  ? 126 VAL   B O   1 
ATOM   1322 O  O   C VAL   B 2 117 ? -8.711  -3.989  -21.496 0.25 53.52  ? 126 VAL   B O   1 
ATOM   1323 O  O   D VAL   B 2 117 ? -8.662  -3.963  -21.497 0.25 53.52  ? 126 VAL   B O   1 
ATOM   1324 C  CB  A VAL   B 2 117 ? -11.390 -5.336  -22.371 0.25 53.04  ? 126 VAL   B CB  1 
ATOM   1325 C  CB  B VAL   B 2 117 ? -11.396 -5.186  -22.188 0.25 52.90  ? 126 VAL   B CB  1 
ATOM   1326 C  CB  C VAL   B 2 117 ? -11.390 -5.336  -22.371 0.25 53.04  ? 126 VAL   B CB  1 
ATOM   1327 C  CB  D VAL   B 2 117 ? -11.396 -5.186  -22.188 0.25 52.90  ? 126 VAL   B CB  1 
ATOM   1328 C  CG1 A VAL   B 2 117 ? -12.428 -6.225  -21.704 0.25 52.43  ? 126 VAL   B CG1 1 
ATOM   1329 C  CG1 B VAL   B 2 117 ? -11.443 -4.000  -23.141 0.25 53.02  ? 126 VAL   B CG1 1 
ATOM   1330 C  CG1 C VAL   B 2 117 ? -12.428 -6.225  -21.704 0.25 52.43  ? 126 VAL   B CG1 1 
ATOM   1331 C  CG1 D VAL   B 2 117 ? -11.443 -4.000  -23.141 0.25 53.02  ? 126 VAL   B CG1 1 
ATOM   1332 C  CG2 A VAL   B 2 117 ? -11.503 -3.901  -21.884 0.25 52.24  ? 126 VAL   B CG2 1 
ATOM   1333 C  CG2 B VAL   B 2 117 ? -12.458 -6.215  -22.545 0.25 53.24  ? 126 VAL   B CG2 1 
ATOM   1334 C  CG2 C VAL   B 2 117 ? -11.503 -3.901  -21.884 0.25 52.24  ? 126 VAL   B CG2 1 
ATOM   1335 C  CG2 D VAL   B 2 117 ? -12.458 -6.215  -22.545 0.25 53.24  ? 126 VAL   B CG2 1 
ATOM   1336 N  N   . ALA   B 2 118 ? -8.102  -5.002  -23.451 1.00 55.22  ? 127 ALA   B N   1 
ATOM   1337 C  CA  . ALA   B 2 118 ? -6.903  -4.160  -23.748 1.00 55.96  ? 127 ALA   B CA  1 
ATOM   1338 C  C   . ALA   B 2 118 ? -7.273  -3.044  -24.739 1.00 56.52  ? 127 ALA   B C   1 
ATOM   1339 O  O   . ALA   B 2 118 ? -7.146  -3.287  -25.938 1.00 55.49  ? 127 ALA   B O   1 
ATOM   1340 C  CB  . ALA   B 2 118 ? -5.764  -5.023  -24.259 1.00 57.13  ? 127 ALA   B CB  1 
ATOM   1341 N  N   . LEU   B 2 119 ? -7.829  -1.920  -24.247 1.00 55.60  ? 128 LEU   B N   1 
ATOM   1342 C  CA  . LEU   B 2 119 ? -8.260  -0.771  -25.088 1.00 57.02  ? 128 LEU   B CA  1 
ATOM   1343 C  C   . LEU   B 2 119 ? -7.906  0.529   -24.353 1.00 58.77  ? 128 LEU   B C   1 
ATOM   1344 O  O   . LEU   B 2 119 ? -8.069  0.578   -23.116 1.00 59.80  ? 128 LEU   B O   1 
ATOM   1345 C  CB  . LEU   B 2 119 ? -9.761  -0.911  -25.339 1.00 55.77  ? 128 LEU   B CB  1 
ATOM   1346 C  CG  . LEU   B 2 119 ? -10.193 -2.133  -26.151 1.00 55.20  ? 128 LEU   B CG  1 
ATOM   1347 C  CD1 . LEU   B 2 119 ? -11.721 -2.295  -26.149 1.00 53.51  ? 128 LEU   B CD1 1 
ATOM   1348 C  CD2 . LEU   B 2 119 ? -9.682  -2.022  -27.573 1.00 57.08  ? 128 LEU   B CD2 1 
ATOM   1349 N  N   . ASP   B 2 120 ? -7.342  1.501   -25.059 1.00 61.35  ? 129 ASP   B N   1 
ATOM   1350 C  CA  . ASP   B 2 120 ? -6.864  2.776   -24.472 1.00 63.34  ? 129 ASP   B CA  1 
ATOM   1351 C  C   . ASP   B 2 120 ? -7.965  3.811   -24.632 1.00 62.76  ? 129 ASP   B C   1 
ATOM   1352 O  O   . ASP   B 2 120 ? -8.329  4.055   -25.779 1.00 66.76  ? 129 ASP   B O   1 
ATOM   1353 C  CB  . ASP   B 2 120 ? -5.641  3.344   -25.187 1.00 66.32  ? 129 ASP   B CB  1 
ATOM   1354 C  CG  . ASP   B 2 120 ? -4.330  2.664   -24.849 1.00 69.81  ? 129 ASP   B CG  1 
ATOM   1355 O  OD1 . ASP   B 2 120 ? -4.341  1.725   -24.025 1.00 69.88  ? 129 ASP   B OD1 1 
ATOM   1356 O  OD2 . ASP   B 2 120 ? -3.309  3.058   -25.469 1.00 73.93  ? 129 ASP   B OD2 1 
ATOM   1357 N  N   . TYR   B 2 121 ? -8.426  4.410   -23.543 1.00 59.55  ? 130 TYR   B N   1 
ATOM   1358 C  CA  . TYR   B 2 121 ? -9.327  5.584   -23.562 1.00 60.04  ? 130 TYR   B CA  1 
ATOM   1359 C  C   . TYR   B 2 121 ? -8.974  6.490   -22.390 1.00 58.94  ? 130 TYR   B C   1 
ATOM   1360 O  O   . TYR   B 2 121 ? -8.355  6.073   -21.412 1.00 57.84  ? 130 TYR   B O   1 
ATOM   1361 C  CB  . TYR   B 2 121 ? -10.801 5.167   -23.526 1.00 62.20  ? 130 TYR   B CB  1 
ATOM   1362 C  CG  . TYR   B 2 121 ? -11.309 4.584   -24.820 1.00 65.59  ? 130 TYR   B CG  1 
ATOM   1363 C  CD1 . TYR   B 2 121 ? -11.670 5.404   -25.878 1.00 66.84  ? 130 TYR   B CD1 1 
ATOM   1364 C  CD2 . TYR   B 2 121 ? -11.390 3.210   -25.003 1.00 67.75  ? 130 TYR   B CD2 1 
ATOM   1365 C  CE1 . TYR   B 2 121 ? -12.116 4.871   -27.078 1.00 69.61  ? 130 TYR   B CE1 1 
ATOM   1366 C  CE2 . TYR   B 2 121 ? -11.836 2.659   -26.196 1.00 70.11  ? 130 TYR   B CE2 1 
ATOM   1367 C  CZ  . TYR   B 2 121 ? -12.200 3.497   -27.236 1.00 71.56  ? 130 TYR   B CZ  1 
ATOM   1368 O  OH  . TYR   B 2 121 ? -12.625 2.972   -28.418 1.00 76.31  ? 130 TYR   B OH  1 
ATOM   1369 N  N   . PRO   B 2 122 ? -9.376  7.771   -22.450 1.00 57.91  ? 131 PRO   B N   1 
ATOM   1370 C  CA  . PRO   B 2 122 ? -9.136  8.676   -21.339 1.00 57.45  ? 131 PRO   B CA  1 
ATOM   1371 C  C   . PRO   B 2 122 ? -9.797  8.127   -20.071 1.00 54.93  ? 131 PRO   B C   1 
ATOM   1372 O  O   . PRO   B 2 122 ? -10.778 7.389   -20.145 1.00 53.85  ? 131 PRO   B O   1 
ATOM   1373 C  CB  . PRO   B 2 122 ? -9.813  9.988   -21.741 1.00 58.63  ? 131 PRO   B CB  1 
ATOM   1374 C  CG  . PRO   B 2 122 ? -10.178 9.856   -23.215 1.00 59.76  ? 131 PRO   B CG  1 
ATOM   1375 C  CD  . PRO   B 2 122 ? -10.146 8.377   -23.543 1.00 59.93  ? 131 PRO   B CD  1 
ATOM   1376 N  N   . ALA   B 2 123 ? -9.292  8.548   -18.925 1.00 53.90  ? 132 ALA   B N   1 
ATOM   1377 C  CA  . ALA   B 2 123 ? -9.776  8.079   -17.610 1.00 51.32  ? 132 ALA   B CA  1 
ATOM   1378 C  C   . ALA   B 2 123 ? -11.282 8.337   -17.458 1.00 49.19  ? 132 ALA   B C   1 
ATOM   1379 O  O   . ALA   B 2 123 ? -11.958 7.516   -16.756 1.00 46.71  ? 132 ALA   B O   1 
ATOM   1380 C  CB  . ALA   B 2 123 ? -8.975  8.736   -16.524 1.00 51.96  ? 132 ALA   B CB  1 
ATOM   1381 N  N   . GLY   B 2 124 ? -11.807 9.386   -18.116 1.00 48.15  ? 133 GLY   B N   1 
ATOM   1382 C  CA  . GLY   B 2 124 ? -13.240 9.747   -18.082 1.00 45.78  ? 133 GLY   B CA  1 
ATOM   1383 C  C   . GLY   B 2 124 ? -14.164 8.690   -18.714 1.00 44.35  ? 133 GLY   B C   1 
ATOM   1384 O  O   . GLY   B 2 124 ? -15.401 8.856   -18.608 1.00 42.78  ? 133 GLY   B O   1 
ATOM   1385 N  N   . THR   B 2 125 ? -13.647 7.653   -19.352 1.00 43.92  ? 134 THR   B N   1 
ATOM   1386 C  CA  . THR   B 2 125 ? -14.446 6.561   -19.978 1.00 44.81  ? 134 THR   B CA  1 
ATOM   1387 C  C   . THR   B 2 125 ? -14.730 5.458   -18.942 1.00 43.64  ? 134 THR   B C   1 
ATOM   1388 O  O   . THR   B 2 125 ? -15.510 4.548   -19.282 1.00 43.37  ? 134 THR   B O   1 
ATOM   1389 C  CB  . THR   B 2 125 ? -13.749 5.994   -21.231 1.00 46.59  ? 134 THR   B CB  1 
ATOM   1390 O  OG1 . THR   B 2 125 ? -13.263 7.094   -21.989 1.00 48.39  ? 134 THR   B OG1 1 
ATOM   1391 C  CG2 . THR   B 2 125 ? -14.637 5.190   -22.161 1.00 46.64  ? 134 THR   B CG2 1 
ATOM   1392 N  N   . SER   B 2 126 ? -14.146 5.541   -17.731 1.00 42.32  ? 135 SER   B N   1 
ATOM   1393 C  CA  . SER   B 2 126 ? -14.376 4.597   -16.605 1.00 40.87  ? 135 SER   B CA  1 
ATOM   1394 C  C   . SER   B 2 126 ? -15.879 4.412   -16.403 1.00 39.68  ? 135 SER   B C   1 
ATOM   1395 O  O   . SER   B 2 126 ? -16.610 5.470   -16.237 1.00 39.70  ? 135 SER   B O   1 
ATOM   1396 C  CB  . SER   B 2 126 ? -13.728 5.045   -15.332 1.00 40.73  ? 135 SER   B CB  1 
ATOM   1397 O  OG  . SER   B 2 126 ? -12.305 5.065   -15.430 1.00 42.13  ? 135 SER   B OG  1 
ATOM   1398 N  N   . GLY   B 2 127 ? -16.330 3.155   -16.381 1.00 38.71  ? 136 GLY   B N   1 
ATOM   1399 C  CA  . GLY   B 2 127 ? -17.740 2.848   -16.077 1.00 39.08  ? 136 GLY   B CA  1 
ATOM   1400 C  C   . GLY   B 2 127 ? -18.469 2.377   -17.304 1.00 39.56  ? 136 GLY   B C   1 
ATOM   1401 O  O   . GLY   B 2 127 ? -19.581 1.856   -17.136 1.00 39.86  ? 136 GLY   B O   1 
ATOM   1402 N  N   . SER   B 2 128 ? -17.830 2.518   -18.481 1.00 40.60  ? 137 SER   B N   1 
ATOM   1403 C  CA  . SER   B 2 128 ? -18.379 2.088   -19.780 1.00 40.34  ? 137 SER   B CA  1 
ATOM   1404 C  C   . SER   B 2 128 ? -18.627 0.589   -19.701 1.00 39.99  ? 137 SER   B C   1 
ATOM   1405 O  O   . SER   B 2 128 ? -17.742 -0.175  -19.315 1.00 39.04  ? 137 SER   B O   1 
ATOM   1406 C  CB  . SER   B 2 128 ? -17.458 2.453   -20.897 1.00 41.98  ? 137 SER   B CB  1 
ATOM   1407 O  OG  . SER   B 2 128 ? -17.481 3.844   -21.132 1.00 42.59  ? 137 SER   B OG  1 
ATOM   1408 N  N   . PRO   B 2 129 ? -19.827 0.131   -20.088 1.00 39.40  ? 138 PRO   B N   1 
ATOM   1409 C  CA  . PRO   B 2 129 ? -20.153 -1.282  -20.027 1.00 39.55  ? 138 PRO   B CA  1 
ATOM   1410 C  C   . PRO   B 2 129 ? -19.507 -2.139  -21.102 1.00 41.37  ? 138 PRO   B C   1 
ATOM   1411 O  O   . PRO   B 2 129 ? -19.346 -1.722  -22.278 1.00 42.14  ? 138 PRO   B O   1 
ATOM   1412 C  CB  . PRO   B 2 129 ? -21.682 -1.322  -20.195 1.00 39.43  ? 138 PRO   B CB  1 
ATOM   1413 C  CG  . PRO   B 2 129 ? -22.024 -0.049  -20.942 1.00 39.25  ? 138 PRO   B CG  1 
ATOM   1414 C  CD  . PRO   B 2 129 ? -20.956 0.959   -20.569 1.00 39.22  ? 138 PRO   B CD  1 
ATOM   1415 N  N   . ILE   B 2 130 ? -19.277 -3.378  -20.709 1.00 41.69  ? 139 ILE   B N   1 
ATOM   1416 C  CA  . ILE   B 2 130 ? -18.777 -4.482  -21.562 1.00 43.56  ? 139 ILE   B CA  1 
ATOM   1417 C  C   . ILE   B 2 130 ? -19.950 -5.457  -21.760 1.00 44.28  ? 139 ILE   B C   1 
ATOM   1418 O  O   . ILE   B 2 130 ? -20.605 -5.801  -20.770 1.00 42.25  ? 139 ILE   B O   1 
ATOM   1419 C  CB  . ILE   B 2 130 ? -17.551 -5.142  -20.912 1.00 43.81  ? 139 ILE   B CB  1 
ATOM   1420 C  CG1 . ILE   B 2 130 ? -16.397 -4.169  -20.732 1.00 44.70  ? 139 ILE   B CG1 1 
ATOM   1421 C  CG2 . ILE   B 2 130 ? -17.085 -6.340  -21.721 1.00 44.99  ? 139 ILE   B CG2 1 
ATOM   1422 C  CD1 . ILE   B 2 130 ? -15.544 -4.500  -19.548 1.00 45.09  ? 139 ILE   B CD1 1 
ATOM   1423 N  N   . LEU   B 2 131 ? -20.211 -5.821  -23.016 1.00 46.96  ? 140 LEU   B N   1 
ATOM   1424 C  CA  . LEU   B 2 131 ? -21.405 -6.588  -23.453 1.00 50.03  ? 140 LEU   B CA  1 
ATOM   1425 C  C   . LEU   B 2 131 ? -21.027 -7.959  -24.017 1.00 50.89  ? 140 LEU   B C   1 
ATOM   1426 O  O   . LEU   B 2 131 ? -20.015 -8.049  -24.740 1.00 53.85  ? 140 LEU   B O   1 
ATOM   1427 C  CB  . LEU   B 2 131 ? -22.100 -5.802  -24.563 1.00 51.72  ? 140 LEU   B CB  1 
ATOM   1428 C  CG  . LEU   B 2 131 ? -22.275 -4.322  -24.275 1.00 51.83  ? 140 LEU   B CG  1 
ATOM   1429 C  CD1 . LEU   B 2 131 ? -23.052 -3.657  -25.402 1.00 51.95  ? 140 LEU   B CD1 1 
ATOM   1430 C  CD2 . LEU   B 2 131 ? -22.939 -4.148  -22.922 1.00 51.83  ? 140 LEU   B CD2 1 
ATOM   1431 N  N   . ASP   B 2 132 ? -21.899 -8.939  -23.805 1.00 51.69  ? 141 ASP   B N   1 
ATOM   1432 C  CA  . ASP   B 2 132 ? -21.903 -10.248 -24.516 1.00 54.31  ? 141 ASP   B CA  1 
ATOM   1433 C  C   . ASP   B 2 132 ? -22.816 -10.121 -25.745 1.00 57.66  ? 141 ASP   B C   1 
ATOM   1434 O  O   . ASP   B 2 132 ? -23.435 -9.044  -25.932 1.00 56.09  ? 141 ASP   B O   1 
ATOM   1435 C  CB  . ASP   B 2 132 ? -22.331 -11.420 -23.629 1.00 52.54  ? 141 ASP   B CB  1 
ATOM   1436 C  CG  . ASP   B 2 132 ? -23.782 -11.389 -23.188 1.00 52.86  ? 141 ASP   B CG  1 
ATOM   1437 O  OD1 . ASP   B 2 132 ? -24.572 -10.581 -23.717 1.00 51.96  ? 141 ASP   B OD1 1 
ATOM   1438 O  OD2 . ASP   B 2 132 ? -24.118 -12.170 -22.270 1.00 55.01  ? 141 ASP   B OD2 1 
ATOM   1439 N  N   . LYS   B 2 133 ? -22.925 -11.199 -26.521 1.00 60.42  ? 142 LYS   B N   1 
ATOM   1440 C  CA  . LYS   B 2 133 ? -23.533 -11.188 -27.885 1.00 64.51  ? 142 LYS   B CA  1 
ATOM   1441 C  C   . LYS   B 2 133 ? -25.029 -10.903 -27.744 1.00 63.02  ? 142 LYS   B C   1 
ATOM   1442 O  O   . LYS   B 2 133 ? -25.594 -10.428 -28.694 1.00 61.10  ? 142 LYS   B O   1 
ATOM   1443 C  CB  . LYS   B 2 133 ? -23.193 -12.494 -28.629 1.00 67.71  ? 142 LYS   B CB  1 
ATOM   1444 C  CG  . LYS   B 2 133 ? -21.751 -12.553 -29.144 1.00 70.74  ? 142 LYS   B CG  1 
ATOM   1445 C  CD  . LYS   B 2 133 ? -21.136 -13.950 -29.363 1.00 74.80  ? 142 LYS   B CD  1 
ATOM   1446 C  CE  . LYS   B 2 133 ? -19.741 -13.903 -29.980 1.00 76.62  ? 142 LYS   B CE  1 
ATOM   1447 N  NZ  . LYS   B 2 133 ? -19.175 -15.246 -30.286 1.00 79.38  ? 142 LYS   B NZ  1 
ATOM   1448 N  N   . CYS   B 2 134 ? -25.609 -11.127 -26.563 1.00 62.49  ? 143 CYS   B N   1 
ATOM   1449 C  CA  . CYS   B 2 134 ? -27.052 -10.938 -26.311 1.00 61.15  ? 143 CYS   B CA  1 
ATOM   1450 C  C   . CYS   B 2 134 ? -27.315 -9.535  -25.772 1.00 58.66  ? 143 CYS   B C   1 
ATOM   1451 O  O   . CYS   B 2 134 ? -28.450 -9.282  -25.352 1.00 59.63  ? 143 CYS   B O   1 
ATOM   1452 C  CB  . CYS   B 2 134 ? -27.544 -11.982 -25.332 1.00 63.73  ? 143 CYS   B CB  1 
ATOM   1453 S  SG  . CYS   B 2 134 ? -27.545 -13.652 -26.030 1.00 67.36  ? 143 CYS   B SG  1 
ATOM   1454 N  N   . GLY   B 2 135 ? -26.335 -8.632  -25.835 1.00 56.90  ? 144 GLY   B N   1 
ATOM   1455 C  CA  . GLY   B 2 135 ? -26.462 -7.271  -25.264 1.00 55.37  ? 144 GLY   B CA  1 
ATOM   1456 C  C   . GLY   B 2 135 ? -26.444 -7.192  -23.725 1.00 52.78  ? 144 GLY   B C   1 
ATOM   1457 O  O   . GLY   B 2 135 ? -26.659 -6.081  -23.210 1.00 50.34  ? 144 GLY   B O   1 
ATOM   1458 N  N   . ARG   B 2 136 ? -26.135 -8.265  -22.980 1.00 53.03  ? 145 ARG   B N   1 
ATOM   1459 C  CA  . ARG   B 2 136 ? -26.117 -8.228  -21.479 1.00 51.67  ? 145 ARG   B CA  1 
ATOM   1460 C  C   . ARG   B 2 136 ? -24.791 -7.655  -20.944 1.00 49.03  ? 145 ARG   B C   1 
ATOM   1461 O  O   . ARG   B 2 136 ? -23.717 -7.947  -21.550 1.00 49.00  ? 145 ARG   B O   1 
ATOM   1462 C  CB  . ARG   B 2 136 ? -26.428 -9.612  -20.937 1.00 54.35  ? 145 ARG   B CB  1 
ATOM   1463 C  CG  . ARG   B 2 136 ? -27.911 -9.932  -21.021 1.00 57.91  ? 145 ARG   B CG  1 
ATOM   1464 C  CD  . ARG   B 2 136 ? -28.144 -11.316 -20.467 1.00 61.55  ? 145 ARG   B CD  1 
ATOM   1465 N  NE  . ARG   B 2 136 ? -27.387 -12.211 -21.338 1.00 65.80  ? 145 ARG   B NE  1 
ATOM   1466 C  CZ  . ARG   B 2 136 ? -26.783 -13.339 -20.998 1.00 69.73  ? 145 ARG   B CZ  1 
ATOM   1467 N  NH1 . ARG   B 2 136 ? -26.804 -13.784 -19.745 1.00 73.69  ? 145 ARG   B NH1 1 
ATOM   1468 N  NH2 . ARG   B 2 136 ? -26.141 -14.019 -21.936 1.00 71.78  ? 145 ARG   B NH2 1 
ATOM   1469 N  N   . VAL   B 2 137 ? -24.836 -6.843  -19.876 1.00 46.22  ? 146 VAL   B N   1 
ATOM   1470 C  CA  . VAL   B 2 137 ? -23.596 -6.230  -19.310 1.00 44.65  ? 146 VAL   B CA  1 
ATOM   1471 C  C   . VAL   B 2 137 ? -22.874 -7.294  -18.458 1.00 44.03  ? 146 VAL   B C   1 
ATOM   1472 O  O   . VAL   B 2 137 ? -23.426 -7.759  -17.440 1.00 43.43  ? 146 VAL   B O   1 
ATOM   1473 C  CB  . VAL   B 2 137 ? -23.851 -4.947  -18.520 1.00 43.65  ? 146 VAL   B CB  1 
ATOM   1474 C  CG1 . VAL   B 2 137 ? -22.545 -4.358  -18.009 1.00 43.27  ? 146 VAL   B CG1 1 
ATOM   1475 C  CG2 . VAL   B 2 137 ? -24.622 -3.919  -19.345 1.00 44.96  ? 146 VAL   B CG2 1 
ATOM   1476 N  N   . ILE   B 2 138 ? -21.670 -7.661  -18.855 1.00 43.51  ? 147 ILE   B N   1 
ATOM   1477 C  CA  . ILE   B 2 138 ? -20.855 -8.696  -18.148 1.00 43.16  ? 147 ILE   B CA  1 
ATOM   1478 C  C   . ILE   B 2 138 ? -19.829 -7.992  -17.239 1.00 42.65  ? 147 ILE   B C   1 
ATOM   1479 O  O   . ILE   B 2 138 ? -19.036 -8.703  -16.559 1.00 41.66  ? 147 ILE   B O   1 
ATOM   1480 C  CB  . ILE   B 2 138 ? -20.185 -9.610  -19.183 1.00 43.75  ? 147 ILE   B CB  1 
ATOM   1481 C  CG1 . ILE   B 2 138 ? -19.286 -8.801  -20.115 1.00 44.04  ? 147 ILE   B CG1 1 
ATOM   1482 C  CG2 . ILE   B 2 138 ? -21.231 -10.412 -19.936 1.00 44.26  ? 147 ILE   B CG2 1 
ATOM   1483 C  CD1 . ILE   B 2 138 ? -18.360 -9.634  -20.943 1.00 45.87  ? 147 ILE   B CD1 1 
ATOM   1484 N  N   . GLY   B 2 139 ? -19.818 -6.649  -17.220 1.00 40.92  ? 148 GLY   B N   1 
ATOM   1485 C  CA  . GLY   B 2 139 ? -18.971 -5.900  -16.273 1.00 40.55  ? 148 GLY   B CA  1 
ATOM   1486 C  C   . GLY   B 2 139 ? -18.682 -4.500  -16.761 1.00 40.60  ? 148 GLY   B C   1 
ATOM   1487 O  O   . GLY   B 2 139 ? -19.152 -4.157  -17.853 1.00 40.54  ? 148 GLY   B O   1 
ATOM   1488 N  N   . LEU   B 2 140 ? -17.930 -3.715  -15.998 1.00 41.38  ? 149 LEU   B N   1 
ATOM   1489 C  CA  . LEU   B 2 140 ? -17.614 -2.309  -16.336 1.00 41.30  ? 149 LEU   B CA  1 
ATOM   1490 C  C   . LEU   B 2 140 ? -16.116 -2.187  -16.544 1.00 42.42  ? 149 LEU   B C   1 
ATOM   1491 O  O   . LEU   B 2 140 ? -15.327 -2.959  -15.906 1.00 42.32  ? 149 LEU   B O   1 
ATOM   1492 C  CB  . LEU   B 2 140 ? -18.087 -1.367  -15.231 1.00 41.24  ? 149 LEU   B CB  1 
ATOM   1493 C  CG  . LEU   B 2 140 ? -19.584 -1.392  -14.877 1.00 41.09  ? 149 LEU   B CG  1 
ATOM   1494 C  CD1 . LEU   B 2 140 ? -19.908 -0.305  -13.867 1.00 40.44  ? 149 LEU   B CD1 1 
ATOM   1495 C  CD2 . LEU   B 2 140 ? -20.453 -1.277  -16.106 1.00 41.45  ? 149 LEU   B CD2 1 
ATOM   1496 N  N   . TYR   B 2 141 ? -15.764 -1.280  -17.445 1.00 42.09  ? 150 TYR   B N   1 
ATOM   1497 C  CA  . TYR   B 2 141 ? -14.392 -1.007  -17.908 1.00 43.53  ? 150 TYR   B CA  1 
ATOM   1498 C  C   . TYR   B 2 141 ? -13.899 0.184   -17.112 1.00 43.50  ? 150 TYR   B C   1 
ATOM   1499 O  O   . TYR   B 2 141 ? -14.633 1.107   -16.933 1.00 42.80  ? 150 TYR   B O   1 
ATOM   1500 C  CB  . TYR   B 2 141 ? -14.391 -0.785  -19.429 1.00 45.40  ? 150 TYR   B CB  1 
ATOM   1501 C  CG  . TYR   B 2 141 ? -13.202 -0.081  -20.054 1.00 45.57  ? 150 TYR   B CG  1 
ATOM   1502 C  CD1 . TYR   B 2 141 ? -13.212 1.296   -20.244 1.00 45.97  ? 150 TYR   B CD1 1 
ATOM   1503 C  CD2 . TYR   B 2 141 ? -12.101 -0.780  -20.525 1.00 46.26  ? 150 TYR   B CD2 1 
ATOM   1504 C  CE1 . TYR   B 2 141 ? -12.153 1.953   -20.866 1.00 47.13  ? 150 TYR   B CE1 1 
ATOM   1505 C  CE2 . TYR   B 2 141 ? -11.038 -0.143  -21.158 1.00 46.92  ? 150 TYR   B CE2 1 
ATOM   1506 C  CZ  . TYR   B 2 141 ? -11.045 1.235   -21.321 1.00 47.90  ? 150 TYR   B CZ  1 
ATOM   1507 O  OH  . TYR   B 2 141 ? -10.012 1.899   -21.948 1.00 48.58  ? 150 TYR   B OH  1 
ATOM   1508 N  N   . GLY   B 2 142 ? -12.642 0.177   -16.703 1.00 44.76  ? 151 GLY   B N   1 
ATOM   1509 C  CA  . GLY   B 2 142 ? -12.061 1.382   -16.087 1.00 45.48  ? 151 GLY   B CA  1 
ATOM   1510 C  C   . GLY   B 2 142 ? -11.307 1.126   -14.792 1.00 45.41  ? 151 GLY   B C   1 
ATOM   1511 O  O   . GLY   B 2 142 ? -10.868 2.138   -14.211 1.00 45.11  ? 151 GLY   B O   1 
ATOM   1512 N  N   . ASN   B 2 143 ? -11.173 -0.137  -14.332 1.00 44.48  ? 152 ASN   B N   1 
ATOM   1513 C  CA  . ASN   B 2 143 ? -10.230 -0.476  -13.239 1.00 44.09  ? 152 ASN   B CA  1 
ATOM   1514 C  C   . ASN   B 2 143 ? -9.268  -1.541  -13.759 1.00 44.33  ? 152 ASN   B C   1 
ATOM   1515 O  O   . ASN   B 2 143 ? -9.691  -2.624  -14.096 1.00 44.21  ? 152 ASN   B O   1 
ATOM   1516 C  CB  . ASN   B 2 143 ? -10.897 -0.952  -11.949 1.00 43.30  ? 152 ASN   B CB  1 
ATOM   1517 C  CG  . ASN   B 2 143 ? -9.927  -1.021  -10.776 1.00 43.39  ? 152 ASN   B CG  1 
ATOM   1518 O  OD1 . ASN   B 2 143 ? -8.950  -0.255  -10.708 1.00 44.09  ? 152 ASN   B OD1 1 
ATOM   1519 N  ND2 . ASN   B 2 143 ? -10.191 -1.919  -9.837  1.00 42.38  ? 152 ASN   B ND2 1 
ATOM   1520 N  N   . GLY   B 2 144 ? -8.000  -1.222  -13.785 1.00 46.10  ? 153 GLY   B N   1 
ATOM   1521 C  CA  . GLY   B 2 144 ? -6.999  -2.168  -14.250 1.00 49.27  ? 153 GLY   B CA  1 
ATOM   1522 C  C   . GLY   B 2 144 ? -5.614  -1.609  -14.104 1.00 51.34  ? 153 GLY   B C   1 
ATOM   1523 O  O   . GLY   B 2 144 ? -5.307  -0.943  -13.080 1.00 49.00  ? 153 GLY   B O   1 
ATOM   1524 N  N   A VAL   B 2 145 ? -4.798  -1.840  -15.137 0.12 53.11  ? 154 VAL   B N   1 
ATOM   1525 N  N   B VAL   B 2 145 ? -4.797  -1.840  -15.137 0.16 53.11  ? 154 VAL   B N   1 
ATOM   1526 N  N   C VAL   B 2 145 ? -4.781  -1.839  -15.117 0.34 53.90  ? 154 VAL   B N   1 
ATOM   1527 N  N   D VAL   B 2 145 ? -4.781  -1.839  -15.117 0.38 53.90  ? 154 VAL   B N   1 
ATOM   1528 C  CA  A VAL   B 2 145 ? -3.309  -1.731  -15.120 0.12 54.98  ? 154 VAL   B CA  1 
ATOM   1529 C  CA  B VAL   B 2 145 ? -3.309  -1.732  -15.120 0.16 54.95  ? 154 VAL   B CA  1 
ATOM   1530 C  CA  C VAL   B 2 145 ? -3.304  -1.689  -15.007 0.34 56.22  ? 154 VAL   B CA  1 
ATOM   1531 C  CA  D VAL   B 2 145 ? -3.305  -1.689  -15.007 0.38 56.20  ? 154 VAL   B CA  1 
ATOM   1532 C  C   A VAL   B 2 145 ? -2.848  -0.948  -16.356 0.12 57.37  ? 154 VAL   B C   1 
ATOM   1533 C  C   B VAL   B 2 145 ? -2.848  -0.948  -16.355 0.16 57.36  ? 154 VAL   B C   1 
ATOM   1534 C  C   C VAL   B 2 145 ? -2.748  -1.099  -16.306 0.34 60.28  ? 154 VAL   B C   1 
ATOM   1535 C  C   D VAL   B 2 145 ? -2.748  -1.098  -16.306 0.38 60.30  ? 154 VAL   B C   1 
ATOM   1536 O  O   A VAL   B 2 145 ? -3.600  -0.920  -17.348 0.12 57.43  ? 154 VAL   B O   1 
ATOM   1537 O  O   B VAL   B 2 145 ? -3.599  -0.921  -17.348 0.16 57.40  ? 154 VAL   B O   1 
ATOM   1538 O  O   C VAL   B 2 145 ? -3.430  -1.194  -17.345 0.34 60.39  ? 154 VAL   B O   1 
ATOM   1539 O  O   D VAL   B 2 145 ? -3.429  -1.193  -17.345 0.38 60.38  ? 154 VAL   B O   1 
ATOM   1540 C  CB  A VAL   B 2 145 ? -2.695  -3.144  -15.080 0.12 55.19  ? 154 VAL   B CB  1 
ATOM   1541 C  CB  B VAL   B 2 145 ? -2.696  -3.145  -15.081 0.16 55.15  ? 154 VAL   B CB  1 
ATOM   1542 C  CB  C VAL   B 2 145 ? -2.695  -3.059  -14.655 0.34 55.93  ? 154 VAL   B CB  1 
ATOM   1543 C  CB  D VAL   B 2 145 ? -2.696  -3.059  -14.655 0.38 55.90  ? 154 VAL   B CB  1 
ATOM   1544 C  CG1 A VAL   B 2 145 ? -1.181  -3.114  -15.166 0.12 56.17  ? 154 VAL   B CG1 1 
ATOM   1545 C  CG1 B VAL   B 2 145 ? -1.183  -3.115  -15.167 0.16 56.16  ? 154 VAL   B CG1 1 
ATOM   1546 C  CG1 C VAL   B 2 145 ? -2.395  -3.900  -15.886 0.34 56.07  ? 154 VAL   B CG1 1 
ATOM   1547 C  CG1 D VAL   B 2 145 ? -2.396  -3.900  -15.886 0.38 56.00  ? 154 VAL   B CG1 1 
ATOM   1548 C  CG2 A VAL   B 2 145 ? -3.146  -3.920  -13.850 0.12 54.24  ? 154 VAL   B CG2 1 
ATOM   1549 C  CG2 B VAL   B 2 145 ? -3.147  -3.921  -13.851 0.16 54.21  ? 154 VAL   B CG2 1 
ATOM   1550 C  CG2 C VAL   B 2 145 ? -1.479  -2.907  -13.760 0.34 56.27  ? 154 VAL   B CG2 1 
ATOM   1551 C  CG2 D VAL   B 2 145 ? -1.481  -2.906  -13.759 0.38 56.27  ? 154 VAL   B CG2 1 
ATOM   1552 N  N   A VAL   B 2 146 ? -1.653  -0.347  -16.293 0.12 59.89  ? 155 VAL   B N   1 
ATOM   1553 N  N   B VAL   B 2 146 ? -1.653  -0.346  -16.292 0.16 59.91  ? 155 VAL   B N   1 
ATOM   1554 N  N   C VAL   B 2 146 ? -1.548  -0.515  -16.234 0.34 64.49  ? 155 VAL   B N   1 
ATOM   1555 N  N   D VAL   B 2 146 ? -1.547  -0.515  -16.234 0.38 64.54  ? 155 VAL   B N   1 
ATOM   1556 C  CA  A VAL   B 2 146 ? -0.945  0.284   -17.448 0.12 62.40  ? 155 VAL   B CA  1 
ATOM   1557 C  CA  B VAL   B 2 146 ? -0.945  0.284   -17.448 0.16 62.39  ? 155 VAL   B CA  1 
ATOM   1558 C  CA  C VAL   B 2 146 ? -0.736  -0.075  -17.404 0.34 67.79  ? 155 VAL   B CA  1 
ATOM   1559 C  CA  D VAL   B 2 146 ? -0.736  -0.075  -17.404 0.38 67.79  ? 155 VAL   B CA  1 
ATOM   1560 C  C   A VAL   B 2 146 ? 0.322   -0.532  -17.734 0.12 64.93  ? 155 VAL   B C   1 
ATOM   1561 C  C   B VAL   B 2 146 ? 0.322   -0.531  -17.735 0.16 64.91  ? 155 VAL   B C   1 
ATOM   1562 C  C   C VAL   B 2 146 ? 0.387   -1.099  -17.593 0.34 71.68  ? 155 VAL   B C   1 
ATOM   1563 C  C   D VAL   B 2 146 ? 0.387   -1.099  -17.593 0.38 71.71  ? 155 VAL   B C   1 
ATOM   1564 O  O   A VAL   B 2 146 ? 1.326   -0.310  -17.036 0.12 65.34  ? 155 VAL   B O   1 
ATOM   1565 O  O   B VAL   B 2 146 ? 1.324   -0.308  -17.037 0.16 65.34  ? 155 VAL   B O   1 
ATOM   1566 O  O   C VAL   B 2 146 ? 0.995   -1.494  -16.575 0.34 72.89  ? 155 VAL   B O   1 
ATOM   1567 O  O   D VAL   B 2 146 ? 0.994   -1.496  -16.575 0.38 72.98  ? 155 VAL   B O   1 
ATOM   1568 C  CB  A VAL   B 2 146 ? -0.623  1.766   -17.172 0.12 62.42  ? 155 VAL   B CB  1 
ATOM   1569 C  CB  B VAL   B 2 146 ? -0.624  1.766   -17.172 0.16 62.40  ? 155 VAL   B CB  1 
ATOM   1570 C  CB  C VAL   B 2 146 ? -0.216  1.361   -17.206 0.34 68.22  ? 155 VAL   B CB  1 
ATOM   1571 C  CB  D VAL   B 2 146 ? -0.216  1.361   -17.205 0.38 68.22  ? 155 VAL   B CB  1 
ATOM   1572 C  CG1 A VAL   B 2 146 ? 0.199   2.386   -18.292 0.12 63.63  ? 155 VAL   B CG1 1 
ATOM   1573 C  CG1 B VAL   B 2 146 ? 0.197   2.386   -18.292 0.16 63.61  ? 155 VAL   B CG1 1 
ATOM   1574 C  CG1 C VAL   B 2 146 ? 0.590   1.836   -18.401 0.34 70.02  ? 155 VAL   B CG1 1 
ATOM   1575 C  CG1 D VAL   B 2 146 ? 0.589   1.837   -18.400 0.38 70.05  ? 155 VAL   B CG1 1 
ATOM   1576 C  CG2 A VAL   B 2 146 ? -1.887  2.578   -16.930 0.12 61.49  ? 155 VAL   B CG2 1 
ATOM   1577 C  CG2 B VAL   B 2 146 ? -1.889  2.578   -16.931 0.16 61.45  ? 155 VAL   B CG2 1 
ATOM   1578 C  CG2 C VAL   B 2 146 ? -1.359  2.330   -16.934 0.34 67.66  ? 155 VAL   B CG2 1 
ATOM   1579 C  CG2 D VAL   B 2 146 ? -1.360  2.329   -16.934 0.38 67.67  ? 155 VAL   B CG2 1 
ATOM   1580 N  N   A ILE   B 2 147 ? 0.275   -1.416  -18.739 0.12 67.74  ? 156 ILE   B N   1 
ATOM   1581 N  N   B ILE   B 2 147 ? 0.276   -1.414  -18.741 0.16 67.73  ? 156 ILE   B N   1 
ATOM   1582 N  N   C ILE   B 2 147 ? 0.618   -1.556  -18.832 0.34 75.39  ? 156 ILE   B N   1 
ATOM   1583 N  N   D ILE   B 2 147 ? 0.619   -1.554  -18.832 0.38 75.40  ? 156 ILE   B N   1 
ATOM   1584 C  CA  A ILE   B 2 147 ? 1.285   -2.498  -18.973 0.12 70.28  ? 156 ILE   B CA  1 
ATOM   1585 C  CA  B ILE   B 2 147 ? 1.286   -2.496  -18.973 0.16 70.26  ? 156 ILE   B CA  1 
ATOM   1586 C  CA  C ILE   B 2 147 ? 1.491   -2.737  -19.124 0.34 77.96  ? 156 ILE   B CA  1 
ATOM   1587 C  CA  D ILE   B 2 147 ? 1.491   -2.736  -19.124 0.38 77.94  ? 156 ILE   B CA  1 
ATOM   1588 C  C   A ILE   B 2 147 ? 2.590   -1.893  -19.509 0.12 72.87  ? 156 ILE   B C   1 
ATOM   1589 C  C   B ILE   B 2 147 ? 2.591   -1.893  -19.509 0.16 72.85  ? 156 ILE   B C   1 
ATOM   1590 C  C   C ILE   B 2 147 ? 2.842   -2.249  -19.659 0.34 80.88  ? 156 ILE   B C   1 
ATOM   1591 C  C   D ILE   B 2 147 ? 2.842   -2.249  -19.659 0.38 80.87  ? 156 ILE   B C   1 
ATOM   1592 O  O   A ILE   B 2 147 ? 2.596   -0.692  -19.844 0.12 72.94  ? 156 ILE   B O   1 
ATOM   1593 O  O   B ILE   B 2 147 ? 2.598   -0.692  -19.845 0.16 72.89  ? 156 ILE   B O   1 
ATOM   1594 O  O   C ILE   B 2 147 ? 2.981   -1.029  -19.887 0.34 79.75  ? 156 ILE   B O   1 
ATOM   1595 O  O   D ILE   B 2 147 ? 2.982   -1.029  -19.888 0.38 79.67  ? 156 ILE   B O   1 
ATOM   1596 C  CB  A ILE   B 2 147 ? 0.737   -3.607  -19.900 0.12 71.14  ? 156 ILE   B CB  1 
ATOM   1597 C  CB  B ILE   B 2 147 ? 0.737   -3.606  -19.899 0.16 71.15  ? 156 ILE   B CB  1 
ATOM   1598 C  CB  C ILE   B 2 147 ? 0.811   -3.740  -20.082 0.34 79.66  ? 156 ILE   B CB  1 
ATOM   1599 C  CB  D ILE   B 2 147 ? 0.811   -3.741  -20.080 0.38 79.68  ? 156 ILE   B CB  1 
ATOM   1600 C  CG1 A ILE   B 2 147 ? 0.156   -3.060  -21.209 0.12 72.34  ? 156 ILE   B CG1 1 
ATOM   1601 C  CG1 B ILE   B 2 147 ? 0.157   -3.061  -21.209 0.16 72.43  ? 156 ILE   B CG1 1 
ATOM   1602 C  CG1 C ILE   B 2 147 ? 0.246   -3.077  -21.343 0.34 81.76  ? 156 ILE   B CG1 1 
ATOM   1603 C  CG1 D ILE   B 2 147 ? 0.247   -3.080  -21.342 0.38 81.85  ? 156 ILE   B CG1 1 
ATOM   1604 C  CG2 A ILE   B 2 147 ? -0.272  -4.468  -19.157 0.12 70.21  ? 156 ILE   B CG2 1 
ATOM   1605 C  CG2 B ILE   B 2 147 ? -0.272  -4.468  -19.156 0.16 70.25  ? 156 ILE   B CG2 1 
ATOM   1606 C  CG2 C ILE   B 2 147 ? -0.251  -4.544  -19.348 0.34 78.77  ? 156 ILE   B CG2 1 
ATOM   1607 C  CG2 D ILE   B 2 147 ? -0.251  -4.544  -19.346 0.38 78.81  ? 156 ILE   B CG2 1 
ATOM   1608 C  CD1 A ILE   B 2 147 ? -0.088  -4.121  -22.264 0.12 73.21  ? 156 ILE   B CD1 1 
ATOM   1609 C  CD1 B ILE   B 2 147 ? -0.087  -4.125  -22.262 0.16 73.30  ? 156 ILE   B CD1 1 
ATOM   1610 C  CD1 C ILE   B 2 147 ? 0.122   -4.021  -22.526 0.34 82.64  ? 156 ILE   B CD1 1 
ATOM   1611 C  CD1 D ILE   B 2 147 ? 0.123   -4.030  -22.523 0.38 82.70  ? 156 ILE   B CD1 1 
ATOM   1612 N  N   A LYS   B 2 148 ? 3.646   -2.716  -19.571 0.12 75.76  ? 157 LYS   B N   1 
ATOM   1613 N  N   B LYS   B 2 148 ? 3.646   -2.717  -19.572 0.16 75.79  ? 157 LYS   B N   1 
ATOM   1614 N  N   C LYS   B 2 148 ? 3.786   -3.180  -19.861 0.34 84.14  ? 157 LYS   B N   1 
ATOM   1615 N  N   D LYS   B 2 148 ? 3.785   -3.182  -19.860 0.38 84.15  ? 157 LYS   B N   1 
ATOM   1616 C  CA  A LYS   B 2 148 ? 5.031   -2.343  -19.978 0.12 78.38  ? 157 LYS   B CA  1 
ATOM   1617 C  CA  B LYS   B 2 148 ? 5.031   -2.344  -19.978 0.16 78.39  ? 157 LYS   B CA  1 
ATOM   1618 C  CA  C LYS   B 2 148 ? 5.200   -2.900  -20.230 0.34 87.38  ? 157 LYS   B CA  1 
ATOM   1619 C  CA  D LYS   B 2 148 ? 5.200   -2.901  -20.229 0.38 87.41  ? 157 LYS   B CA  1 
ATOM   1620 C  C   A LYS   B 2 148 ? 4.984   -1.246  -21.046 0.12 80.15  ? 157 LYS   B C   1 
ATOM   1621 C  C   B LYS   B 2 148 ? 4.984   -1.245  -21.044 0.16 80.16  ? 157 LYS   B C   1 
ATOM   1622 C  C   C LYS   B 2 148 ? 5.291   -1.991  -21.464 0.34 88.33  ? 157 LYS   B C   1 
ATOM   1623 C  C   D LYS   B 2 148 ? 5.291   -1.993  -21.462 0.38 88.33  ? 157 LYS   B C   1 
ATOM   1624 O  O   A LYS   B 2 148 ? 5.518   -0.146  -20.792 0.12 80.07  ? 157 LYS   B O   1 
ATOM   1625 O  O   B LYS   B 2 148 ? 5.511   -0.143  -20.786 0.16 80.01  ? 157 LYS   B O   1 
ATOM   1626 O  O   C LYS   B 2 148 ? 6.426   -1.615  -21.787 0.34 89.65  ? 157 LYS   B O   1 
ATOM   1627 O  O   D LYS   B 2 148 ? 6.427   -1.621  -21.784 0.38 89.64  ? 157 LYS   B O   1 
ATOM   1628 C  CB  A LYS   B 2 148 ? 5.781   -3.561  -20.531 0.12 80.04  ? 157 LYS   B CB  1 
ATOM   1629 C  CB  B LYS   B 2 148 ? 5.781   -3.561  -20.531 0.16 80.09  ? 157 LYS   B CB  1 
ATOM   1630 C  CB  C LYS   B 2 148 ? 5.978   -4.196  -20.497 0.34 90.10  ? 157 LYS   B CB  1 
ATOM   1631 C  CB  D LYS   B 2 148 ? 5.977   -4.197  -20.496 0.38 90.17  ? 157 LYS   B CB  1 
ATOM   1632 C  CG  A LYS   B 2 148 ? 5.984   -4.712  -19.554 0.12 79.77  ? 157 LYS   B CG  1 
ATOM   1633 C  CG  B LYS   B 2 148 ? 5.984   -4.713  -19.554 0.16 79.80  ? 157 LYS   B CG  1 
ATOM   1634 C  CG  C LYS   B 2 148 ? 5.356   -5.153  -21.511 0.34 91.58  ? 157 LYS   B CG  1 
ATOM   1635 C  CG  D LYS   B 2 148 ? 5.356   -5.153  -21.510 0.38 91.67  ? 157 LYS   B CG  1 
ATOM   1636 C  CD  A LYS   B 2 148 ? 6.783   -5.859  -20.137 0.12 81.12  ? 157 LYS   B CD  1 
ATOM   1637 C  CD  B LYS   B 2 148 ? 6.783   -5.859  -20.136 0.16 81.14  ? 157 LYS   B CD  1 
ATOM   1638 C  CD  C LYS   B 2 148 ? 6.368   -5.929  -22.356 0.34 93.37  ? 157 LYS   B CD  1 
ATOM   1639 C  CD  D LYS   B 2 148 ? 6.368   -5.930  -22.356 0.38 93.42  ? 157 LYS   B CD  1 
ATOM   1640 C  CE  A LYS   B 2 148 ? 6.797   -7.078  -19.240 0.12 80.84  ? 157 LYS   B CE  1 
ATOM   1641 C  CE  B LYS   B 2 148 ? 6.795   -7.079  -19.240 0.16 80.87  ? 157 LYS   B CE  1 
ATOM   1642 C  CE  C LYS   B 2 148 ? 6.351   -5.577  -23.833 0.34 94.92  ? 157 LYS   B CE  1 
ATOM   1643 C  CE  D LYS   B 2 148 ? 6.350   -5.579  -23.833 0.38 94.96  ? 157 LYS   B CE  1 
ATOM   1644 N  NZ  A LYS   B 2 148 ? 8.009   -7.900  -19.459 0.12 82.29  ? 157 LYS   B NZ  1 
ATOM   1645 N  NZ  B LYS   B 2 148 ? 8.007   -7.901  -19.459 0.16 82.35  ? 157 LYS   B NZ  1 
ATOM   1646 N  NZ  C LYS   B 2 148 ? 6.794   -4.187  -24.095 0.34 95.93  ? 157 LYS   B NZ  1 
ATOM   1647 N  NZ  D LYS   B 2 148 ? 6.793   -4.188  -24.096 0.38 95.99  ? 157 LYS   B NZ  1 
ATOM   1648 N  N   A ASN   B 2 149 ? 4.327   -1.540  -22.173 0.12 81.84  ? 158 ASN   B N   1 
ATOM   1649 N  N   B ASN   B 2 149 ? 4.328   -1.539  -22.172 0.16 81.87  ? 158 ASN   B N   1 
ATOM   1650 N  N   C ASN   B 2 149 ? 4.163   -1.668  -22.121 0.34 88.65  ? 158 ASN   B N   1 
ATOM   1651 N  N   D ASN   B 2 149 ? 4.164   -1.668  -22.120 0.38 88.70  ? 158 ASN   B N   1 
ATOM   1652 C  CA  A ASN   B 2 149 ? 4.313   -0.713  -23.412 0.12 83.68  ? 158 ASN   B CA  1 
ATOM   1653 C  CA  B ASN   B 2 149 ? 4.314   -0.712  -23.411 0.16 83.70  ? 158 ASN   B CA  1 
ATOM   1654 C  CA  C ASN   B 2 149 ? 4.086   -0.882  -23.390 0.34 89.25  ? 158 ASN   B CA  1 
ATOM   1655 C  CA  D ASN   B 2 149 ? 4.088   -0.882  -23.389 0.38 89.29  ? 158 ASN   B CA  1 
ATOM   1656 C  C   A ASN   B 2 149 ? 3.469   0.559   -23.225 0.12 83.20  ? 158 ASN   B C   1 
ATOM   1657 C  C   B ASN   B 2 149 ? 3.469   0.559   -23.225 0.16 83.20  ? 158 ASN   B C   1 
ATOM   1658 C  C   C ASN   B 2 149 ? 3.652   0.575   -23.144 0.34 86.45  ? 158 ASN   B C   1 
ATOM   1659 C  C   D ASN   B 2 149 ? 3.652   0.575   -23.143 0.38 86.45  ? 158 ASN   B C   1 
ATOM   1660 O  O   A ASN   B 2 149 ? 3.219   1.237   -24.242 0.12 83.75  ? 158 ASN   B O   1 
ATOM   1661 O  O   B ASN   B 2 149 ? 3.217   1.236   -24.242 0.16 83.70  ? 158 ASN   B O   1 
ATOM   1662 O  O   C ASN   B 2 149 ? 3.899   1.407   -24.035 0.34 87.21  ? 158 ASN   B O   1 
ATOM   1663 O  O   D ASN   B 2 149 ? 3.898   1.407   -24.034 0.38 87.20  ? 158 ASN   B O   1 
ATOM   1664 C  CB  A ASN   B 2 149 ? 3.822   -1.517  -24.624 0.12 84.72  ? 158 ASN   B CB  1 
ATOM   1665 C  CB  B ASN   B 2 149 ? 3.825   -1.517  -24.624 0.16 84.76  ? 158 ASN   B CB  1 
ATOM   1666 C  CB  C ASN   B 2 149 ? 3.103   -1.501  -24.395 0.34 90.92  ? 158 ASN   B CB  1 
ATOM   1667 C  CB  D ASN   B 2 149 ? 3.106   -1.501  -24.395 0.38 91.00  ? 158 ASN   B CB  1 
ATOM   1668 C  CG  A ASN   B 2 149 ? 2.522   -2.256  -24.373 0.12 83.98  ? 158 ASN   B CG  1 
ATOM   1669 C  CG  B ASN   B 2 149 ? 2.525   -2.256  -24.375 0.16 84.03  ? 158 ASN   B CG  1 
ATOM   1670 C  CG  C ASN   B 2 149 ? 3.315   -2.980  -24.653 0.34 92.13  ? 158 ASN   B CG  1 
ATOM   1671 C  CG  D ASN   B 2 149 ? 3.317   -2.980  -24.653 0.38 92.19  ? 158 ASN   B CG  1 
ATOM   1672 O  OD1 A ASN   B 2 149 ? 2.486   -3.203  -23.591 0.12 84.05  ? 158 ASN   B OD1 1 
ATOM   1673 O  OD1 B ASN   B 2 149 ? 2.486   -3.202  -23.591 0.16 84.16  ? 158 ASN   B OD1 1 
ATOM   1674 O  OD1 C ASN   B 2 149 ? 4.037   -3.654  -23.921 0.34 93.35  ? 158 ASN   B OD1 1 
ATOM   1675 O  OD1 D ASN   B 2 149 ? 4.038   -3.656  -23.921 0.38 93.45  ? 158 ASN   B OD1 1 
ATOM   1676 N  ND2 A ASN   B 2 149 ? 1.452   -1.843  -25.033 0.12 83.69  ? 158 ASN   B ND2 1 
ATOM   1677 N  ND2 B ASN   B 2 149 ? 1.457   -1.845  -25.039 0.16 83.71  ? 158 ASN   B ND2 1 
ATOM   1678 N  ND2 C ASN   B 2 149 ? 2.671   -3.500  -25.686 0.34 92.95  ? 158 ASN   B ND2 1 
ATOM   1679 N  ND2 D ASN   B 2 149 ? 2.671   -3.500  -25.686 0.38 93.02  ? 158 ASN   B ND2 1 
ATOM   1680 N  N   . GLY   B 2 150 ? 3.017   0.868   -22.002 1.00 83.96  ? 159 GLY   B N   1 
ATOM   1681 C  CA  . GLY   B 2 150 ? 2.368   2.178   -21.709 1.00 78.48  ? 159 GLY   B CA  1 
ATOM   1682 C  C   . GLY   B 2 150 ? 0.862   2.180   -21.967 1.00 75.20  ? 159 GLY   B C   1 
ATOM   1683 O  O   . GLY   B 2 150 ? 0.142   3.174   -21.594 1.00 71.67  ? 159 GLY   B O   1 
ATOM   1684 N  N   A SER   B 2 151 ? 0.363   1.105   -22.585 0.12 74.38  ? 160 SER   B N   1 
ATOM   1685 N  N   B SER   B 2 151 ? 0.368   1.100   -22.580 0.16 74.13  ? 160 SER   B N   1 
ATOM   1686 N  N   C SER   B 2 151 ? 0.364   1.105   -22.588 0.34 74.68  ? 160 SER   B N   1 
ATOM   1687 N  N   D SER   B 2 151 ? 0.370   1.100   -22.582 0.38 74.38  ? 160 SER   B N   1 
ATOM   1688 C  CA  A SER   B 2 151 ? -1.072  0.908   -22.916 0.12 72.86  ? 160 SER   B CA  1 
ATOM   1689 C  CA  B SER   B 2 151 ? -1.062  0.877   -22.913 0.16 72.44  ? 160 SER   B CA  1 
ATOM   1690 C  CA  C SER   B 2 151 ? -1.072  0.909   -22.914 0.34 73.14  ? 160 SER   B CA  1 
ATOM   1691 C  CA  D SER   B 2 151 ? -1.061  0.876   -22.912 0.38 72.64  ? 160 SER   B CA  1 
ATOM   1692 C  C   A SER   B 2 151 ? -1.841  0.490   -21.656 0.12 69.97  ? 160 SER   B C   1 
ATOM   1693 C  C   B SER   B 2 151 ? -1.839  0.493   -21.647 0.16 69.71  ? 160 SER   B C   1 
ATOM   1694 C  C   C SER   B 2 151 ? -1.841  0.492   -21.653 0.34 70.10  ? 160 SER   B C   1 
ATOM   1695 C  C   D SER   B 2 151 ? -1.839  0.496   -21.644 0.38 69.80  ? 160 SER   B C   1 
ATOM   1696 O  O   A SER   B 2 151 ? -1.205  -0.017  -20.709 0.12 69.52  ? 160 SER   B O   1 
ATOM   1697 O  O   B SER   B 2 151 ? -1.208  0.015   -20.682 0.16 69.18  ? 160 SER   B O   1 
ATOM   1698 O  O   C SER   B 2 151 ? -1.208  -0.015  -20.703 0.34 69.44  ? 160 SER   B O   1 
ATOM   1699 O  O   D SER   B 2 151 ? -1.210  0.019   -20.676 0.38 69.06  ? 160 SER   B O   1 
ATOM   1700 C  CB  A SER   B 2 151 ? -1.239  -0.100  -24.022 0.12 74.08  ? 160 SER   B CB  1 
ATOM   1701 C  CB  B SER   B 2 151 ? -1.190  -0.179  -23.979 0.16 73.35  ? 160 SER   B CB  1 
ATOM   1702 C  CB  C SER   B 2 151 ? -1.242  -0.099  -24.021 0.34 74.51  ? 160 SER   B CB  1 
ATOM   1703 C  CB  D SER   B 2 151 ? -1.187  -0.183  -23.977 0.38 73.60  ? 160 SER   B CB  1 
ATOM   1704 O  OG  A SER   B 2 151 ? -2.581  -0.119  -24.487 0.12 74.15  ? 160 SER   B OG  1 
ATOM   1705 O  OG  B SER   B 2 151 ? -0.336  -1.276  -23.697 0.16 73.72  ? 160 SER   B OG  1 
ATOM   1706 O  OG  C SER   B 2 151 ? -2.585  -0.111  -24.484 0.34 74.77  ? 160 SER   B OG  1 
ATOM   1707 O  OG  D SER   B 2 151 ? -0.312  -1.268  -23.705 0.38 73.86  ? 160 SER   B OG  1 
ATOM   1708 N  N   . TYR   B 2 152 ? -3.160  0.694   -21.667 1.00 67.83  ? 161 TYR   B N   1 
ATOM   1709 C  CA  . TYR   B 2 152 ? -4.067  0.358   -20.550 1.00 63.11  ? 161 TYR   B CA  1 
ATOM   1710 C  C   . TYR   B 2 152 ? -4.702  -1.018  -20.752 1.00 57.80  ? 161 TYR   B C   1 
ATOM   1711 O  O   . TYR   B 2 152 ? -5.160  -1.310  -21.812 1.00 55.56  ? 161 TYR   B O   1 
ATOM   1712 C  CB  . TYR   B 2 152 ? -5.194  1.382   -20.508 1.00 62.26  ? 161 TYR   B CB  1 
ATOM   1713 C  CG  . TYR   B 2 152 ? -6.102  1.234   -19.322 1.00 60.28  ? 161 TYR   B CG  1 
ATOM   1714 C  CD1 . TYR   B 2 152 ? -5.602  1.401   -18.044 1.00 60.50  ? 161 TYR   B CD1 1 
ATOM   1715 C  CD2 . TYR   B 2 152 ? -7.445  0.921   -19.469 1.00 60.38  ? 161 TYR   B CD2 1 
ATOM   1716 C  CE1 . TYR   B 2 152 ? -6.409  1.282   -16.930 1.00 59.00  ? 161 TYR   B CE1 1 
ATOM   1717 C  CE2 . TYR   B 2 152 ? -8.283  0.842   -18.367 1.00 60.00  ? 161 TYR   B CE2 1 
ATOM   1718 C  CZ  . TYR   B 2 152 ? -7.754  1.005   -17.092 1.00 59.83  ? 161 TYR   B CZ  1 
ATOM   1719 O  OH  . TYR   B 2 152 ? -8.538  0.927   -15.978 1.00 59.80  ? 161 TYR   B OH  1 
ATOM   1720 N  N   . VAL   B 2 153 ? -4.827  -1.788  -19.686 1.00 55.41  ? 162 VAL   B N   1 
ATOM   1721 C  CA  . VAL   B 2 153 ? -5.621  -3.049  -19.649 1.00 53.86  ? 162 VAL   B CA  1 
ATOM   1722 C  C   . VAL   B 2 153 ? -6.563  -3.006  -18.434 1.00 50.55  ? 162 VAL   B C   1 
ATOM   1723 O  O   . VAL   B 2 153 ? -6.069  -2.929  -17.312 1.00 48.38  ? 162 VAL   B O   1 
ATOM   1724 C  CB  . VAL   B 2 153 ? -4.708  -4.290  -19.580 1.00 54.10  ? 162 VAL   B CB  1 
ATOM   1725 C  CG1 . VAL   B 2 153 ? -5.490  -5.550  -19.892 1.00 54.01  ? 162 VAL   B CG1 1 
ATOM   1726 C  CG2 . VAL   B 2 153 ? -3.491  -4.162  -20.475 1.00 56.69  ? 162 VAL   B CG2 1 
ATOM   1727 N  N   . SER   B 2 154 ? -7.866  -3.121  -18.671 1.00 48.80  ? 163 SER   B N   1 
ATOM   1728 C  CA  . SER   B 2 154 ? -8.938  -3.085  -17.661 1.00 46.46  ? 163 SER   B CA  1 
ATOM   1729 C  C   . SER   B 2 154 ? -9.436  -4.500  -17.363 1.00 45.42  ? 163 SER   B C   1 
ATOM   1730 O  O   . SER   B 2 154 ? -9.675  -5.218  -18.318 1.00 44.76  ? 163 SER   B O   1 
ATOM   1731 C  CB  . SER   B 2 154 ? -10.096 -2.238  -18.140 1.00 46.24  ? 163 SER   B CB  1 
ATOM   1732 O  OG  . SER   B 2 154 ? -11.229 -2.406  -17.303 1.00 44.05  ? 163 SER   B OG  1 
ATOM   1733 N  N   . ALA   B 2 155 ? -9.724  -4.793  -16.098 1.00 43.48  ? 164 ALA   B N   1 
ATOM   1734 C  CA  . ALA   B 2 155 ? -10.542 -5.940  -15.684 1.00 43.47  ? 164 ALA   B CA  1 
ATOM   1735 C  C   . ALA   B 2 155 ? -11.915 -5.744  -16.298 1.00 44.52  ? 164 ALA   B C   1 
ATOM   1736 O  O   . ALA   B 2 155 ? -12.365 -4.575  -16.493 1.00 44.79  ? 164 ALA   B O   1 
ATOM   1737 C  CB  . ALA   B 2 155 ? -10.645 -6.049  -14.177 1.00 42.94  ? 164 ALA   B CB  1 
ATOM   1738 N  N   . ILE   B 2 156 ? -12.554 -6.858  -16.600 1.00 44.70  ? 165 ILE   B N   1 
ATOM   1739 C  CA  . ILE   B 2 156 ? -14.025 -6.919  -16.678 1.00 44.26  ? 165 ILE   B CA  1 
ATOM   1740 C  C   . ILE   B 2 156 ? -14.537 -6.989  -15.240 1.00 43.05  ? 165 ILE   B C   1 
ATOM   1741 O  O   . ILE   B 2 156 ? -14.674 -8.106  -14.716 1.00 41.63  ? 165 ILE   B O   1 
ATOM   1742 C  CB  . ILE   B 2 156 ? -14.490 -8.128  -17.492 1.00 44.71  ? 165 ILE   B CB  1 
ATOM   1743 C  CG1 . ILE   B 2 156 ? -13.761 -8.199  -18.833 1.00 45.79  ? 165 ILE   B CG1 1 
ATOM   1744 C  CG2 . ILE   B 2 156 ? -16.010 -8.048  -17.634 1.00 44.75  ? 165 ILE   B CG2 1 
ATOM   1745 C  CD1 . ILE   B 2 156 ? -14.057 -9.436  -19.643 1.00 46.59  ? 165 ILE   B CD1 1 
ATOM   1746 N  N   . THR   B 2 157 ? -14.879 -5.838  -14.648 1.00 42.85  ? 166 THR   B N   1 
ATOM   1747 C  CA  . THR   B 2 157 ? -15.332 -5.744  -13.237 1.00 41.94  ? 166 THR   B CA  1 
ATOM   1748 C  C   . THR   B 2 157 ? -16.853 -5.945  -13.149 1.00 42.12  ? 166 THR   B C   1 
ATOM   1749 O  O   . THR   B 2 157 ? -17.571 -5.066  -13.637 1.00 42.42  ? 166 THR   B O   1 
ATOM   1750 C  CB  . THR   B 2 157 ? -14.934 -4.409  -12.622 1.00 41.86  ? 166 THR   B CB  1 
ATOM   1751 O  OG1 . THR   B 2 157 ? -13.517 -4.307  -12.736 1.00 41.06  ? 166 THR   B OG1 1 
ATOM   1752 C  CG2 . THR   B 2 157 ? -15.385 -4.291  -11.185 1.00 41.24  ? 166 THR   B CG2 1 
ATOM   1753 N  N   . GLN   B 2 158 ? -17.300 -7.052  -12.537 1.00 41.32  ? 167 GLN   B N   1 
ATOM   1754 C  CA  . GLN   B 2 158 ? -18.726 -7.393  -12.322 1.00 41.28  ? 167 GLN   B CA  1 
ATOM   1755 C  C   . GLN   B 2 158 ? -19.023 -7.480  -10.817 1.00 42.39  ? 167 GLN   B C   1 
ATOM   1756 O  O   . GLN   B 2 158 ? -18.178 -7.989  -10.049 1.00 40.53  ? 167 GLN   B O   1 
ATOM   1757 C  CB  . GLN   B 2 158 ? -19.067 -8.696  -13.036 1.00 40.70  ? 167 GLN   B CB  1 
ATOM   1758 C  CG  . GLN   B 2 158 ? -20.545 -9.039  -13.098 1.00 40.24  ? 167 GLN   B CG  1 
ATOM   1759 C  CD  . GLN   B 2 158 ? -21.437 -7.905  -13.583 1.00 40.00  ? 167 GLN   B CD  1 
ATOM   1760 O  OE1 . GLN   B 2 158 ? -21.467 -6.820  -13.004 1.00 38.01  ? 167 GLN   B OE1 1 
ATOM   1761 N  NE2 . GLN   B 2 158 ? -22.216 -8.179  -14.623 1.00 40.07  ? 167 GLN   B NE2 1 
ATOM   1762 N  N   . GLY   B 2 159 ? -20.205 -7.006  -10.426 1.00 44.42  ? 168 GLY   B N   1 
ATOM   1763 C  CA  . GLY   B 2 159 ? -20.739 -7.111  -9.065  1.00 49.02  ? 168 GLY   B CA  1 
ATOM   1764 C  C   . GLY   B 2 159 ? -21.450 -8.439  -8.869  1.00 54.55  ? 168 GLY   B C   1 
ATOM   1765 O  O   . GLY   B 2 159 ? -21.441 -9.255  -9.797  1.00 56.41  ? 168 GLY   B O   1 
ATOM   1766 N  N   . LYS   B 2 160 ? -21.949 -8.681  -7.658  1.00 62.25  ? 169 LYS   B N   1 
ATOM   1767 C  CA  . LYS   B 2 160 ? -22.787 -9.854  -7.273  1.00 67.87  ? 169 LYS   B CA  1 
ATOM   1768 C  C   . LYS   B 2 160 ? -24.226 -9.342  -7.067  1.00 71.07  ? 169 LYS   B C   1 
ATOM   1769 O  O   . LYS   B 2 160 ? -24.398 -8.179  -6.598  1.00 66.84  ? 169 LYS   B O   1 
ATOM   1770 C  CB  . LYS   B 2 160 ? -22.201 -10.546 -6.032  1.00 71.65  ? 169 LYS   B CB  1 
ATOM   1771 C  CG  . LYS   B 2 160 ? -22.470 -12.044 -5.965  1.00 77.06  ? 169 LYS   B CG  1 
ATOM   1772 C  CD  . LYS   B 2 160 ? -22.338 -12.646 -4.584  1.00 79.35  ? 169 LYS   B CD  1 
ATOM   1773 C  CE  . LYS   B 2 160 ? -23.554 -13.443 -4.165  1.00 81.65  ? 169 LYS   B CE  1 
ATOM   1774 N  NZ  . LYS   B 2 160 ? -23.755 -13.344 -2.702  1.00 85.32  ? 169 LYS   B NZ  1 
ATOM   1775 N  N   . ARG   B 2 161 ? -25.221 -10.136 -7.486  1.00 75.30  ? 170 ARG   B N   1 
ATOM   1776 C  CA  . ARG   B 2 161 ? -26.681 -9.928  -7.244  1.00 76.62  ? 170 ARG   B CA  1 
ATOM   1777 C  C   . ARG   B 2 161 ? -27.065 -10.773 -6.004  1.00 83.58  ? 170 ARG   B C   1 
ATOM   1778 O  O   . ARG   B 2 161 ? -26.323 -11.750 -5.711  1.00 89.23  ? 170 ARG   B O   1 
ATOM   1779 C  CB  . ARG   B 2 161 ? -27.419 -10.257 -8.554  1.00 74.36  ? 170 ARG   B CB  1 
ATOM   1780 C  CG  . ARG   B 2 161 ? -28.810 -9.655  -8.725  1.00 71.70  ? 170 ARG   B CG  1 
ATOM   1781 C  CD  . ARG   B 2 161 ? -29.491 -10.048 -10.032 1.00 72.59  ? 170 ARG   B CD  1 
ATOM   1782 N  NE  . ARG   B 2 161 ? -30.950 -9.887  -9.989  1.00 73.91  ? 170 ARG   B NE  1 
ATOM   1783 C  CZ  . ARG   B 2 161 ? -31.691 -9.070  -10.750 1.00 73.38  ? 170 ARG   B CZ  1 
ATOM   1784 N  NH1 . ARG   B 2 161 ? -31.144 -8.294  -11.670 1.00 71.18  ? 170 ARG   B NH1 1 
ATOM   1785 N  NH2 . ARG   B 2 161 ? -33.003 -9.043  -10.587 1.00 75.01  ? 170 ARG   B NH2 1 
ATOM   1786 N  N   . GLU   B 2 162 ? -28.116 -10.388 -5.255  1.00 90.22  ? 171 GLU   B N   1 
ATOM   1787 C  CA  . GLU   B 2 162 ? -28.632 -11.111 -4.049  1.00 93.74  ? 171 GLU   B CA  1 
ATOM   1788 C  C   . GLU   B 2 162 ? -30.149 -11.304 -4.189  1.00 90.96  ? 171 GLU   B C   1 
ATOM   1789 O  O   . GLU   B 2 162 ? -30.700 -12.388 -3.952  1.00 93.68  ? 171 GLU   B O   1 
ATOM   1790 C  CB  . GLU   B 2 162 ? -28.298 -10.354 -2.754  1.00 99.69  ? 171 GLU   B CB  1 
ATOM   1791 C  CG  . GLU   B 2 162 ? -26.808 -10.101 -2.514  1.00 104.05 ? 171 GLU   B CG  1 
ATOM   1792 C  CD  . GLU   B 2 162 ? -26.041 -11.174 -1.742  1.00 112.22 ? 171 GLU   B CD  1 
ATOM   1793 O  OE1 . GLU   B 2 162 ? -25.008 -10.832 -1.117  1.00 112.08 ? 171 GLU   B OE1 1 
ATOM   1794 O  OE2 . GLU   B 2 162 ? -26.460 -12.355 -1.771  1.00 117.31 ? 171 GLU   B OE2 1 
HETATM 1795 S  S   A DMS   C 3 .   ? -8.688  4.688   -18.001 0.12 56.98  ? 201 DMS   B S   1 
HETATM 1796 S  S   B DMS   C 3 .   ? -8.688  4.688   -18.000 0.16 56.99  ? 201 DMS   B S   1 
HETATM 1797 O  O   A DMS   C 3 .   ? -7.551  3.897   -18.576 0.12 57.60  ? 201 DMS   B O   1 
HETATM 1798 O  O   B DMS   C 3 .   ? -7.551  3.897   -18.577 0.16 57.59  ? 201 DMS   B O   1 
HETATM 1799 C  C1  A DMS   C 3 .   ? -8.783  4.257   -16.284 0.12 55.96  ? 201 DMS   B C1  1 
HETATM 1800 C  C1  B DMS   C 3 .   ? -8.782  4.256   -16.284 0.16 55.95  ? 201 DMS   B C1  1 
HETATM 1801 C  C2  A DMS   C 3 .   ? -10.180 3.887   -18.534 0.12 56.48  ? 201 DMS   B C2  1 
HETATM 1802 C  C2  B DMS   C 3 .   ? -10.180 3.887   -18.532 0.16 56.48  ? 201 DMS   B C2  1 
HETATM 1803 S  S   . DMS   D 3 .   ? -18.745 11.532  -0.112  1.00 81.83  ? 202 DMS   B S   1 
HETATM 1804 O  O   . DMS   D 3 .   ? -19.182 10.120  -0.385  1.00 79.49  ? 202 DMS   B O   1 
HETATM 1805 C  C1  . DMS   D 3 .   ? -20.013 12.575  -0.758  1.00 81.81  ? 202 DMS   B C1  1 
HETATM 1806 C  C2  . DMS   D 3 .   ? -17.480 11.925  -1.295  1.00 78.28  ? 202 DMS   B C2  1 
HETATM 1807 S  S   A DMS   E 3 .   ? -7.256  2.360   -13.502 0.12 45.89  ? 203 DMS   B S   1 
HETATM 1808 S  S   B DMS   E 3 .   ? -7.256  2.356   -13.503 0.16 45.89  ? 203 DMS   B S   1 
HETATM 1809 O  O   A DMS   E 3 .   ? -7.439  0.921   -13.815 0.12 45.50  ? 203 DMS   B O   1 
HETATM 1810 O  O   B DMS   E 3 .   ? -7.444  0.920   -13.815 0.16 45.44  ? 203 DMS   B O   1 
HETATM 1811 C  C1  A DMS   E 3 .   ? -8.053  2.631   -11.943 0.12 45.05  ? 203 DMS   B C1  1 
HETATM 1812 C  C1  B DMS   E 3 .   ? -8.051  2.629   -11.944 0.16 45.08  ? 203 DMS   B C1  1 
HETATM 1813 C  C2  A DMS   E 3 .   ? -5.577  2.552   -12.949 0.12 46.48  ? 203 DMS   B C2  1 
HETATM 1814 C  C2  B DMS   E 3 .   ? -5.576  2.549   -12.949 0.16 46.50  ? 203 DMS   B C2  1 
HETATM 1815 N  N1  C A1BGM F 4 .   ? -8.844  2.305   -8.735  0.34 63.84  ? 204 A1BGM B N1  1 
HETATM 1816 N  N1  D A1BGM F 4 .   ? -8.843  2.306   -8.735  0.38 63.91  ? 204 A1BGM B N1  1 
HETATM 1817 N  N3  C A1BGM F 4 .   ? -8.646  5.197   -14.566 0.34 59.49  ? 204 A1BGM B N3  1 
HETATM 1818 N  N3  D A1BGM F 4 .   ? -8.647  5.197   -14.566 0.38 59.49  ? 204 A1BGM B N3  1 
HETATM 1819 C  C4  C A1BGM F 4 .   ? -8.627  4.416   -9.985  0.34 61.27  ? 204 A1BGM B C4  1 
HETATM 1820 C  C4  D A1BGM F 4 .   ? -8.626  4.416   -9.985  0.38 61.25  ? 204 A1BGM B C4  1 
HETATM 1821 C  C5  C A1BGM F 4 .   ? -8.360  4.717   -12.176 0.34 60.03  ? 204 A1BGM B C5  1 
HETATM 1822 C  C5  D A1BGM F 4 .   ? -8.361  4.718   -12.175 0.38 59.99  ? 204 A1BGM B C5  1 
HETATM 1823 C  C6  C A1BGM F 4 .   ? -8.289  4.201   -13.578 0.34 59.90  ? 204 A1BGM B C6  1 
HETATM 1824 C  C6  D A1BGM F 4 .   ? -8.291  4.202   -13.578 0.38 59.89  ? 204 A1BGM B C6  1 
HETATM 1825 C  C7  C A1BGM F 4 .   ? -8.550  4.968   -15.933 0.34 59.15  ? 204 A1BGM B C7  1 
HETATM 1826 C  C7  D A1BGM F 4 .   ? -8.550  4.968   -15.933 0.38 59.15  ? 204 A1BGM B C7  1 
HETATM 1827 C  C8  C A1BGM F 4 .   ? -9.610  4.365   -16.597 0.34 58.14  ? 204 A1BGM B C8  1 
HETATM 1828 C  C8  D A1BGM F 4 .   ? -9.610  4.364   -16.598 0.38 58.12  ? 204 A1BGM B C8  1 
HETATM 1829 C  C10 C A1BGM F 4 .   ? -8.392  4.511   -18.666 0.34 59.64  ? 204 A1BGM B C10 1 
HETATM 1830 C  C10 D A1BGM F 4 .   ? -8.392  4.511   -18.666 0.38 59.64  ? 204 A1BGM B C10 1 
HETATM 1831 C  C13 C A1BGM F 4 .   ? -4.838  5.690   -20.947 0.34 61.96  ? 204 A1BGM B C13 1 
HETATM 1832 C  C13 D A1BGM F 4 .   ? -4.837  5.690   -20.948 0.38 61.96  ? 204 A1BGM B C13 1 
HETATM 1833 C  C15 C A1BGM F 4 .   ? -3.591  4.869   -20.613 0.34 61.97  ? 204 A1BGM B C15 1 
HETATM 1834 C  C15 D A1BGM F 4 .   ? -3.591  4.868   -20.614 0.38 61.94  ? 204 A1BGM B C15 1 
HETATM 1835 C  C17 C A1BGM F 4 .   ? -7.406  5.337   -16.642 0.34 59.46  ? 204 A1BGM B C17 1 
HETATM 1836 C  C17 D A1BGM F 4 .   ? -7.406  5.338   -16.643 0.38 59.45  ? 204 A1BGM B C17 1 
HETATM 1837 C  C1  C A1BGM F 4 .   ? -9.471  1.667   -7.576  0.34 64.05  ? 204 A1BGM B C1  1 
HETATM 1838 C  C1  D A1BGM F 4 .   ? -9.470  1.668   -7.576  0.38 64.16  ? 204 A1BGM B C1  1 
HETATM 1839 C  C2  C A1BGM F 4 .   ? -7.421  1.984   -8.806  0.34 64.88  ? 204 A1BGM B C2  1 
HETATM 1840 C  C2  D A1BGM F 4 .   ? -7.420  1.986   -8.806  0.38 64.97  ? 204 A1BGM B C2  1 
HETATM 1841 C  C3  C A1BGM F 4 .   ? -9.055  3.754   -8.712  0.34 62.54  ? 204 A1BGM B C3  1 
HETATM 1842 C  C3  D A1BGM F 4 .   ? -9.054  3.754   -8.711  0.38 62.58  ? 204 A1BGM B C3  1 
HETATM 1843 N  N2  C A1BGM F 4 .   ? -8.567  3.814   -11.139 0.34 60.53  ? 204 A1BGM B N2  1 
HETATM 1844 N  N2  D A1BGM F 4 .   ? -8.567  3.815   -11.138 0.38 60.51  ? 204 A1BGM B N2  1 
HETATM 1845 C  C9  C A1BGM F 4 .   ? -9.515  4.156   -17.957 0.34 58.51  ? 204 A1BGM B C9  1 
HETATM 1846 C  C9  D A1BGM F 4 .   ? -9.516  4.155   -17.957 0.38 58.49  ? 204 A1BGM B C9  1 
HETATM 1847 CL CL1 C A1BGM F 4 .   ? -10.860 3.414   -18.776 0.34 58.01  ? 204 A1BGM B CL1 1 
HETATM 1848 CL CL1 D A1BGM F 4 .   ? -10.860 3.413   -18.776 0.38 57.98  ? 204 A1BGM B CL1 1 
HETATM 1849 C  C11 C A1BGM F 4 .   ? -7.321  5.117   -18.017 0.34 59.76  ? 204 A1BGM B C11 1 
HETATM 1850 C  C11 D A1BGM F 4 .   ? -7.321  5.118   -18.017 0.38 59.73  ? 204 A1BGM B C11 1 
HETATM 1851 C  C12 C A1BGM F 4 .   ? -6.056  5.526   -18.726 0.34 60.77  ? 204 A1BGM B C12 1 
HETATM 1852 C  C12 D A1BGM F 4 .   ? -6.056  5.526   -18.727 0.38 60.76  ? 204 A1BGM B C12 1 
HETATM 1853 O  O1  C A1BGM F 4 .   ? -5.139  6.042   -18.090 0.34 62.04  ? 204 A1BGM B O1  1 
HETATM 1854 O  O1  D A1BGM F 4 .   ? -5.140  6.041   -18.090 0.38 62.09  ? 204 A1BGM B O1  1 
HETATM 1855 N  N4  C A1BGM F 4 .   ? -5.966  5.294   -20.043 0.34 61.22  ? 204 A1BGM B N4  1 
HETATM 1856 N  N4  D A1BGM F 4 .   ? -5.965  5.294   -20.044 0.38 61.22  ? 204 A1BGM B N4  1 
HETATM 1857 C  C14 C A1BGM F 4 .   ? -5.258  5.436   -22.397 0.34 62.71  ? 204 A1BGM B C14 1 
HETATM 1858 C  C14 D A1BGM F 4 .   ? -5.258  5.438   -22.398 0.38 62.72  ? 204 A1BGM B C14 1 
HETATM 1859 C  C16 C A1BGM F 4 .   ? -4.511  7.179   -20.815 0.34 61.63  ? 204 A1BGM B C16 1 
HETATM 1860 C  C16 D A1BGM F 4 .   ? -4.510  7.179   -20.815 0.38 61.59  ? 204 A1BGM B C16 1 
HETATM 1861 O  O2  C A1BGM F 4 .   ? -5.612  8.015   -21.124 0.34 61.60  ? 204 A1BGM B O2  1 
HETATM 1862 O  O2  D A1BGM F 4 .   ? -5.611  8.014   -21.126 0.38 61.58  ? 204 A1BGM B O2  1 
HETATM 1863 C  C18 C A1BGM F 4 .   ? -8.212  6.001   -11.769 0.34 60.82  ? 204 A1BGM B C18 1 
HETATM 1864 C  C18 D A1BGM F 4 .   ? -8.213  6.002   -11.768 0.38 60.79  ? 204 A1BGM B C18 1 
HETATM 1865 S  S1  C A1BGM F 4 .   ? -8.216  6.093   -10.053 0.34 62.06  ? 204 A1BGM B S1  1 
HETATM 1866 S  S1  D A1BGM F 4 .   ? -8.216  6.094   -10.053 0.38 62.12  ? 204 A1BGM B S1  1 
HETATM 1867 S  S   C DMS   G 3 .   ? -8.523  -16.136 -23.699 0.50 93.08  ? 205 DMS   B S   1 
HETATM 1868 S  S   D DMS   G 3 .   ? -8.523  -16.136 -23.699 0.50 93.08  ? 205 DMS   B S   1 
HETATM 1869 O  O   C DMS   G 3 .   ? -9.787  -15.633 -24.369 0.50 90.08  ? 205 DMS   B O   1 
HETATM 1870 O  O   D DMS   G 3 .   ? -9.787  -15.633 -24.369 0.50 90.08  ? 205 DMS   B O   1 
HETATM 1871 C  C1  C DMS   G 3 .   ? -7.650  -14.699 -23.134 0.50 91.74  ? 205 DMS   B C1  1 
HETATM 1872 C  C1  D DMS   G 3 .   ? -7.650  -14.699 -23.134 0.50 91.74  ? 205 DMS   B C1  1 
HETATM 1873 C  C2  C DMS   G 3 .   ? -7.385  -16.553 -25.011 0.50 93.43  ? 205 DMS   B C2  1 
HETATM 1874 C  C2  D DMS   G 3 .   ? -7.385  -16.553 -25.011 0.50 93.43  ? 205 DMS   B C2  1 
HETATM 1875 S  S   C SO4   H 5 .   ? -0.746  6.079   -26.265 0.34 107.34 ? 206 SO4   B S   1 
HETATM 1876 S  S   D SO4   H 5 .   ? -0.747  6.078   -26.266 0.38 107.41 ? 206 SO4   B S   1 
HETATM 1877 O  O1  C SO4   H 5 .   ? -1.159  7.445   -26.471 0.34 106.58 ? 206 SO4   B O1  1 
HETATM 1878 O  O1  D SO4   H 5 .   ? -1.157  7.445   -26.471 0.38 106.58 ? 206 SO4   B O1  1 
HETATM 1879 O  O2  C SO4   H 5 .   ? 0.494   6.055   -25.536 0.34 104.28 ? 206 SO4   B O2  1 
HETATM 1880 O  O2  D SO4   H 5 .   ? 0.494   6.052   -25.538 0.38 104.12 ? 206 SO4   B O2  1 
HETATM 1881 O  O3  C SO4   H 5 .   ? -1.764  5.382   -25.521 0.34 105.18 ? 206 SO4   B O3  1 
HETATM 1882 O  O3  D SO4   H 5 .   ? -1.767  5.383   -25.521 0.38 105.18 ? 206 SO4   B O3  1 
HETATM 1883 O  O4  C SO4   H 5 .   ? -0.552  5.435   -27.537 0.34 109.41 ? 206 SO4   B O4  1 
HETATM 1884 O  O4  D SO4   H 5 .   ? -0.555  5.434   -27.538 0.38 109.53 ? 206 SO4   B O4  1 
HETATM 1885 O  O   C HOH   I 6 .   ? -25.816 15.981  -6.308  0.50 55.49  ? 101 HOH   A O   1 
HETATM 1886 O  O   D HOH   I 6 .   ? -25.816 15.981  -6.308  0.50 55.49  ? 101 HOH   A O   1 
HETATM 1887 O  O   . HOH   I 6 .   ? -1.829  -4.216  -6.222  1.00 48.59  ? 102 HOH   A O   1 
HETATM 1888 O  O   . HOH   I 6 .   ? -7.973  0.233   3.613   1.00 51.42  ? 103 HOH   A O   1 
HETATM 1889 O  O   . HOH   I 6 .   ? -23.860 8.889   -27.649 1.00 45.33  ? 104 HOH   A O   1 
HETATM 1890 O  O   . HOH   I 6 .   ? -23.157 18.915  -19.408 1.00 58.19  ? 105 HOH   A O   1 
HETATM 1891 O  O   . HOH   I 6 .   ? -27.906 -6.147  -28.182 1.00 53.03  ? 106 HOH   A O   1 
HETATM 1892 O  O   . HOH   I 6 .   ? -30.280 0.156   -23.209 1.00 61.80  ? 107 HOH   A O   1 
HETATM 1893 O  O   . HOH   I 6 .   ? -7.011  -9.213  -3.011  1.00 44.00  ? 108 HOH   A O   1 
HETATM 1894 O  O   . HOH   I 6 .   ? -30.796 0.135   -29.525 1.00 66.86  ? 109 HOH   A O   1 
HETATM 1895 O  O   . HOH   I 6 .   ? -30.269 12.141  -16.569 1.00 63.82  ? 110 HOH   A O   1 
HETATM 1896 O  O   . HOH   I 6 .   ? -3.798  -3.694  0.489   1.00 63.34  ? 111 HOH   A O   1 
HETATM 1897 O  O   C HOH   I 6 .   ? -26.982 1.489   -29.546 0.50 64.74  ? 112 HOH   A O   1 
HETATM 1898 O  O   D HOH   I 6 .   ? -26.982 1.489   -29.546 0.50 64.74  ? 112 HOH   A O   1 
HETATM 1899 O  O   . HOH   I 6 .   ? -2.861  -12.003 -6.844  1.00 42.98  ? 113 HOH   A O   1 
HETATM 1900 O  O   . HOH   I 6 .   ? -4.048  -14.868 -25.275 1.00 44.47  ? 114 HOH   A O   1 
HETATM 1901 O  O   . HOH   I 6 .   ? -8.114  -1.960  6.945   1.00 54.19  ? 115 HOH   A O   1 
HETATM 1902 O  O   . HOH   I 6 .   ? -4.041  -0.955  -0.058  1.00 50.52  ? 116 HOH   A O   1 
HETATM 1903 O  O   A HOH   I 6 .   ? -4.735  1.289   -9.655  0.12 29.34  ? 117 HOH   A O   1 
HETATM 1904 O  O   B HOH   I 6 .   ? -4.740  1.286   -9.659  0.16 29.32  ? 117 HOH   A O   1 
HETATM 1905 O  O   A HOH   I 6 .   ? -9.309  1.545   -7.321  0.12 0.56   ? 118 HOH   A O   1 
HETATM 1906 O  O   B HOH   I 6 .   ? -9.327  1.817   -8.597  0.16 0.83   ? 118 HOH   A O   1 
HETATM 1907 O  O   . HOH   I 6 .   ? -4.550  -10.568 -5.388  1.00 43.85  ? 119 HOH   A O   1 
HETATM 1908 O  O   . HOH   I 6 .   ? -21.695 -9.222  -35.044 1.00 67.27  ? 120 HOH   A O   1 
HETATM 1909 O  O   . HOH   I 6 .   ? -2.862  -9.371  -3.087  1.00 66.42  ? 121 HOH   A O   1 
HETATM 1910 O  O   . HOH   I 6 .   ? -27.183 -5.144  -35.226 1.00 71.01  ? 122 HOH   A O   1 
HETATM 1911 O  O   . HOH   J 6 .   ? -16.459 25.091  -13.720 1.00 67.21  ? 301 HOH   B O   1 
HETATM 1912 O  O   . HOH   J 6 .   ? -30.342 12.427  -19.512 1.00 51.40  ? 302 HOH   B O   1 
HETATM 1913 O  O   . HOH   J 6 .   ? -21.826 9.411   -26.286 1.00 104.09 ? 303 HOH   B O   1 
HETATM 1914 O  O   . HOH   J 6 .   ? -33.684 1.385   -15.573 1.00 48.38  ? 304 HOH   B O   1 
HETATM 1915 O  O   . HOH   J 6 .   ? -28.478 -4.895  -22.308 1.00 53.40  ? 305 HOH   B O   1 
HETATM 1916 O  O   . HOH   J 6 .   ? -35.018 -5.622  -10.564 1.00 55.78  ? 306 HOH   B O   1 
HETATM 1917 O  O   . HOH   J 6 .   ? -25.613 -8.412  -16.727 1.00 41.32  ? 307 HOH   B O   1 
HETATM 1918 O  O   A HOH   J 6 .   ? -15.539 -10.360 -15.136 0.50 58.82  ? 308 HOH   B O   1 
HETATM 1919 O  O   B HOH   J 6 .   ? -15.539 -10.360 -15.136 0.50 58.82  ? 308 HOH   B O   1 
HETATM 1920 O  O   . HOH   J 6 .   ? -17.811 -10.889 -16.380 1.00 48.30  ? 309 HOH   B O   1 
HETATM 1921 O  O   . HOH   J 6 .   ? -20.443 -7.681  -5.524  1.00 51.32  ? 310 HOH   B O   1 
HETATM 1922 O  O   A HOH   J 6 .   ? -21.313 5.150   -32.499 0.50 76.01  ? 311 HOH   B O   1 
HETATM 1923 O  O   B HOH   J 6 .   ? -21.313 5.150   -32.499 0.50 76.01  ? 311 HOH   B O   1 
HETATM 1924 O  O   . HOH   J 6 .   ? -19.347 -12.354 -25.385 1.00 53.23  ? 312 HOH   B O   1 
HETATM 1925 O  O   . HOH   J 6 .   ? -16.304 20.450  -14.262 1.00 55.72  ? 313 HOH   B O   1 
HETATM 1926 O  O   . HOH   J 6 .   ? -15.399 -4.947  1.408   1.00 45.77  ? 314 HOH   B O   1 
HETATM 1927 O  O   . HOH   J 6 .   ? -17.011 12.644  -5.362  1.00 47.05  ? 315 HOH   B O   1 
HETATM 1928 O  O   . HOH   J 6 .   ? -12.804 -2.644  -14.647 1.00 38.10  ? 316 HOH   B O   1 
HETATM 1929 O  O   . HOH   J 6 .   ? -21.510 -14.009 -21.639 1.00 53.24  ? 317 HOH   B O   1 
HETATM 1930 O  O   . HOH   J 6 .   ? -6.220  -0.597  -10.610 1.00 40.38  ? 318 HOH   B O   1 
HETATM 1931 O  O   . HOH   J 6 .   ? -16.551 -7.265  -8.056  1.00 56.47  ? 319 HOH   B O   1 
HETATM 1932 O  O   A HOH   J 6 .   ? -9.138  -6.830  -25.114 0.50 65.37  ? 320 HOH   B O   1 
HETATM 1933 O  O   B HOH   J 6 .   ? -9.138  -6.830  -25.114 0.50 65.37  ? 320 HOH   B O   1 
HETATM 1934 O  O   . HOH   J 6 .   ? -12.332 -3.542  -9.962  1.00 43.83  ? 321 HOH   B O   1 
HETATM 1935 O  O   C HOH   J 6 .   ? -22.186 14.869  -6.298  0.50 53.25  ? 322 HOH   B O   1 
HETATM 1936 O  O   D HOH   J 6 .   ? -22.186 14.869  -6.298  0.50 53.25  ? 322 HOH   B O   1 
HETATM 1937 O  O   . HOH   J 6 .   ? -12.390 2.017   -5.450  1.00 47.10  ? 323 HOH   B O   1 
HETATM 1938 O  O   . HOH   J 6 .   ? -15.903 -14.835 -16.637 1.00 48.96  ? 324 HOH   B O   1 
HETATM 1939 O  O   A HOH   J 6 .   ? -31.847 7.056   -4.751  0.50 61.30  ? 325 HOH   B O   1 
HETATM 1940 O  O   B HOH   J 6 .   ? -31.847 7.056   -4.751  0.50 61.30  ? 325 HOH   B O   1 
HETATM 1941 O  O   . HOH   J 6 .   ? -10.605 11.686  -19.039 1.00 42.94  ? 326 HOH   B O   1 
HETATM 1942 O  O   . HOH   J 6 .   ? -15.634 -14.370 -30.695 1.00 64.55  ? 327 HOH   B O   1 
HETATM 1943 O  O   . HOH   J 6 .   ? -8.363  -11.012 -7.180  1.00 58.45  ? 328 HOH   B O   1 
HETATM 1944 O  O   . HOH   J 6 .   ? -21.254 7.072   0.000   0.50 41.88  ? 329 HOH   B O   1 
HETATM 1945 O  O   . HOH   J 6 .   ? -19.008 24.796  -14.468 1.00 56.90  ? 330 HOH   B O   1 
HETATM 1946 O  O   . HOH   J 6 .   ? -28.942 15.760  -14.864 1.00 72.84  ? 331 HOH   B O   1 
HETATM 1947 O  O   . HOH   J 6 .   ? -14.745 16.020  -19.957 1.00 52.66  ? 332 HOH   B O   1 
HETATM 1948 O  O   . HOH   J 6 .   ? -10.105 7.113   -6.213  1.00 67.32  ? 333 HOH   B O   1 
HETATM 1949 O  O   . HOH   J 6 .   ? -15.285 9.000   -0.646  1.00 47.35  ? 334 HOH   B O   1 
HETATM 1950 O  O   . HOH   J 6 .   ? -30.590 4.438   -2.610  1.00 54.70  ? 335 HOH   B O   1 
HETATM 1951 O  O   . HOH   J 6 .   ? -14.290 -12.421 -16.329 1.00 51.21  ? 336 HOH   B O   1 
HETATM 1952 O  O   . HOH   J 6 .   ? -27.522 -7.152  -5.411  1.00 54.60  ? 337 HOH   B O   1 
HETATM 1953 O  O   . HOH   J 6 .   ? -18.106 18.558  -21.623 1.00 65.37  ? 338 HOH   B O   1 
HETATM 1954 O  O   . HOH   J 6 .   ? -14.475 -6.501  -1.434  1.00 59.93  ? 339 HOH   B O   1 
HETATM 1955 O  O   . HOH   J 6 .   ? -27.557 -6.613  -18.642 1.00 49.60  ? 340 HOH   B O   1 
HETATM 1956 O  O   . HOH   J 6 .   ? -18.479 14.574  -22.100 1.00 47.27  ? 341 HOH   B O   1 
HETATM 1957 O  O   . HOH   J 6 .   ? -29.461 -1.573  -19.037 1.00 57.92  ? 342 HOH   B O   1 
HETATM 1958 O  O   . HOH   J 6 .   ? -11.436 -5.287  -8.157  1.00 45.14  ? 343 HOH   B O   1 
HETATM 1959 O  O   . HOH   J 6 .   ? -25.950 -4.650  -4.042  1.00 46.99  ? 344 HOH   B O   1 
HETATM 1960 O  O   C HOH   J 6 .   ? -6.658  9.983   -18.935 0.34 49.62  ? 345 HOH   B O   1 
HETATM 1961 O  O   D HOH   J 6 .   ? -6.659  9.988   -18.936 0.38 49.55  ? 345 HOH   B O   1 
HETATM 1962 O  O   A HOH   J 6 .   ? -21.221 -12.412 -13.058 0.50 59.41  ? 346 HOH   B O   1 
HETATM 1963 O  O   B HOH   J 6 .   ? -21.221 -12.412 -13.058 0.50 59.41  ? 346 HOH   B O   1 
HETATM 1964 O  O   A HOH   J 6 .   ? -20.615 2.175   -32.635 0.50 47.77  ? 347 HOH   B O   1 
HETATM 1965 O  O   B HOH   J 6 .   ? -20.615 2.175   -32.635 0.50 47.77  ? 347 HOH   B O   1 
HETATM 1966 O  O   . HOH   J 6 .   ? -16.692 14.457  -30.845 1.00 56.77  ? 348 HOH   B O   1 
HETATM 1967 O  O   . HOH   J 6 .   ? -29.812 -5.525  -0.987  1.00 59.07  ? 349 HOH   B O   1 
HETATM 1968 O  O   . HOH   J 6 .   ? 8.838   -5.288  -18.044 1.00 75.93  ? 350 HOH   B O   1 
HETATM 1969 O  O   . HOH   J 6 .   ? -6.984  -11.097 -5.243  1.00 46.13  ? 351 HOH   B O   1 
HETATM 1970 O  O   . HOH   J 6 .   ? -23.768 -15.139 -17.900 1.00 62.04  ? 352 HOH   B O   1 
HETATM 1971 O  O   C HOH   J 6 .   ? -29.609 11.021  1.256   0.50 70.20  ? 353 HOH   B O   1 
HETATM 1972 O  O   D HOH   J 6 .   ? -29.609 11.021  1.256   0.50 70.20  ? 353 HOH   B O   1 
HETATM 1973 O  O   A HOH   J 6 .   ? -7.618  -6.612  0.831   0.50 69.42  ? 354 HOH   B O   1 
HETATM 1974 O  O   B HOH   J 6 .   ? -7.618  -6.612  0.831   0.50 69.42  ? 354 HOH   B O   1 
HETATM 1975 O  O   . HOH   J 6 .   ? -10.303 7.712   -13.476 1.00 55.98  ? 355 HOH   B O   1 
HETATM 1976 O  O   A HOH   J 6 .   ? -19.262 -13.637 -22.961 0.50 54.22  ? 356 HOH   B O   1 
HETATM 1977 O  O   B HOH   J 6 .   ? -19.262 -13.637 -22.961 0.50 54.22  ? 356 HOH   B O   1 
HETATM 1978 O  O   . HOH   J 6 .   ? -20.180 24.328  -16.589 1.00 59.92  ? 357 HOH   B O   1 
HETATM 1979 O  O   . HOH   J 6 .   ? -23.037 -7.149  -1.838  1.00 65.13  ? 358 HOH   B O   1 
HETATM 1980 O  O   . HOH   J 6 .   ? -19.584 -6.045  -0.857  1.00 45.12  ? 359 HOH   B O   1 
HETATM 1981 O  O   . HOH   J 6 .   ? -32.353 -6.938  -6.960  1.00 52.71  ? 360 HOH   B O   1 
HETATM 1982 O  O   . HOH   J 6 .   ? -10.354 -19.195 -11.776 1.00 62.58  ? 361 HOH   B O   1 
HETATM 1983 O  O   . HOH   J 6 .   ? -30.112 -7.669  -5.604  1.00 64.00  ? 362 HOH   B O   1 
HETATM 1984 O  O   . HOH   J 6 .   ? -1.008  -14.651 -9.653  1.00 65.61  ? 363 HOH   B O   1 
HETATM 1985 O  O   A HOH   J 6 .   ? -0.288  0.014   -13.129 0.12 27.91  ? 364 HOH   B O   1 
HETATM 1986 O  O   B HOH   J 6 .   ? -0.288  0.013   -13.125 0.16 27.89  ? 364 HOH   B O   1 
HETATM 1987 O  O   . HOH   J 6 .   ? -16.732 16.322  -21.776 1.00 59.00  ? 365 HOH   B O   1 
HETATM 1988 O  O   C HOH   J 6 .   ? -4.522  2.454   -13.707 0.34 50.78  ? 366 HOH   B O   1 
HETATM 1989 O  O   D HOH   J 6 .   ? -4.524  2.455   -13.705 0.38 50.77  ? 366 HOH   B O   1 
HETATM 1990 O  O   A HOH   J 6 .   ? -37.449 3.557   -12.137 0.50 82.98  ? 367 HOH   B O   1 
HETATM 1991 O  O   B HOH   J 6 .   ? -37.449 3.557   -12.137 0.50 82.98  ? 367 HOH   B O   1 
HETATM 1992 O  O   C HOH   J 6 .   ? -8.025  12.117  -18.573 0.34 55.61  ? 368 HOH   B O   1 
HETATM 1993 O  O   D HOH   J 6 .   ? -8.025  12.116  -18.574 0.38 55.57  ? 368 HOH   B O   1 
HETATM 1994 O  O   . HOH   J 6 .   ? -11.631 12.150  -14.707 1.00 66.06  ? 369 HOH   B O   1 
HETATM 1995 O  O   A HOH   J 6 .   ? -18.952 -12.142 -13.565 0.50 59.57  ? 370 HOH   B O   1 
HETATM 1996 O  O   B HOH   J 6 .   ? -18.952 -12.142 -13.565 0.50 59.57  ? 370 HOH   B O   1 
HETATM 1997 O  O   . HOH   J 6 .   ? -29.745 -12.763 -27.057 0.50 65.03  ? 371 HOH   B O   1 
HETATM 1998 O  O   A HOH   J 6 .   ? -8.880  5.728   -9.095  0.12 30.41  ? 372 HOH   B O   1 
HETATM 1999 O  O   B HOH   J 6 .   ? -8.879  5.723   -9.099  0.16 30.38  ? 372 HOH   B O   1 
HETATM 2000 O  O   . HOH   J 6 .   ? -11.367 -7.431  2.289   1.00 54.56  ? 373 HOH   B O   1 
HETATM 2001 O  O   . HOH   J 6 .   ? -21.254 4.294   0.000   0.50 68.22  ? 374 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   ? 1.0196 0.7183 1.0711 -0.1271 0.3728  -0.0218 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.9874 0.6891 1.0210 -0.1098 0.3605  -0.0291 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.9439 0.6579 0.9683 -0.0708 0.3511  -0.0046 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.9809 0.6824 1.0143 -0.0506 0.3652  0.0175  50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.0302 0.6985 1.0734 -0.1123 0.3790  -0.0444 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.0409 0.7122 1.0724 -0.0966 0.3690  -0.0535 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.0606 0.7380 1.0813 -0.1175 0.3613  -0.0763 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.0603 0.7270 1.0943 -0.0635 0.3699  -0.0380 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.8447 0.5823 0.8509 -0.0610 0.3285  -0.0084 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.8107 0.5710 0.8042 -0.0322 0.3128  0.0114  51  MET   A CA  
11   C  C   . MET   A 8   ? 0.7459 0.5026 0.7331 -0.0022 0.3066  0.0125  51  MET   A C   
12   O  O   . MET   A 8   ? 0.7272 0.4806 0.7143 -0.0104 0.3030  -0.0067 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.8080 0.6014 0.7877 -0.0451 0.2899  0.0068  51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.8390 0.6441 0.8266 -0.0626 0.2924  0.0149  51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.8463 0.6918 0.8188 -0.0711 0.2642  0.0138  51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.8595 0.7149 0.8515 -0.0933 0.2722  0.0218  51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.7194 0.4785 0.7011 0.0313  0.3048  0.0341  52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.7012 0.4600 0.6776 0.0634  0.2963  0.0365  52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.6788 0.4611 0.6369 0.0908  0.2784  0.0528  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.6717 0.4628 0.6233 0.0916  0.2796  0.0678  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.7178 0.4451 0.7080 0.0793  0.3173  0.0442  52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.7244 0.4366 0.7160 0.0927  0.3345  0.0696  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.7376 0.4350 0.7424 0.0674  0.3543  0.0714  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.7282 0.4419 0.7068 0.1307  0.3309  0.0918  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7618 0.4448 0.7700 0.0794  0.3724  0.0959  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7589 0.4579 0.7356 0.1442  0.3484  0.1173  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.7713 0.4538 0.7644 0.1182  0.3707  0.1199  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.8082 0.4757 0.8013 0.1313  0.3900  0.1459  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.6757 0.4684 0.6271 0.1134  0.2622  0.0483  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.6803 0.4944 0.6130 0.1421  0.2435  0.0604  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.7056 0.5093 0.6337 0.1803  0.2452  0.0750  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.7312 0.5191 0.6733 0.1869  0.2515  0.0686  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.6526 0.4911 0.5800 0.1367  0.2199  0.0426  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.6581 0.4925 0.5988 0.1365  0.2157  0.0232  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.6549 0.5046 0.5812 0.1038  0.2176  0.0346  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.6374 0.4956 0.5736 0.1380  0.1928  0.0091  53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.7232 0.5358 0.6316 0.2050  0.2400  0.0943  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.7600 0.5682 0.6547 0.2457  0.2364  0.1102  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.7568 0.5926 0.6290 0.2664  0.2112  0.1098  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.7189 0.5685 0.5790 0.2589  0.2084  0.1153  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.7952 0.5828 0.6825 0.2578  0.2591  0.1373  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.8343 0.5903 0.7437 0.2451  0.2851  0.1401  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.8897 0.6247 0.7929 0.2559  0.3094  0.1683  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.8864 0.6334 0.7709 0.2644  0.3080  0.1833  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 0.9456 0.6514 0.8635 0.2566  0.3309  0.1758  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.7758 0.6199 0.6440 0.2923  0.1935  0.1034  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.7907 0.6596 0.6369 0.3149  0.1690  0.1017  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.8001 0.6668 0.6170 0.3379  0.1754  0.1272  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.8306 0.6762 0.6420 0.3533  0.1930  0.1473  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8102 0.6875 0.6611 0.3390  0.1496  0.0898  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8201 0.7253 0.6610 0.3482  0.1219  0.0751  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8309 0.7471 0.6884 0.3621  0.1026  0.0564  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8423 0.7840 0.6935 0.3678  0.0773  0.0407  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.8681 0.8219 0.6907 0.3956  0.0623  0.0474  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.9470 0.8899 0.7430 0.4209  0.0705  0.0709  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.8375 0.8129 0.6567 0.3982  0.0405  0.0309  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.7880 0.6743 0.5866 0.3403  0.1637  0.1274  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.8083 0.6946 0.5771 0.3624  0.1702  0.1503  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.7964 0.7022 0.5381 0.3932  0.1454  0.1458  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.8258 0.7304 0.5381 0.4169  0.1499  0.1642  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.8056 0.6964 0.5781 0.3371  0.1829  0.1564  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.7688 0.6915 0.5198 0.3924  0.1212  0.1218  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.7839 0.7253 0.5110 0.4207  0.0967  0.1146  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.7699 0.7321 0.5139 0.4079  0.0732  0.0860  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.7450 0.7063 0.5182 0.3764  0.0771  0.0728  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.7917 0.7709 0.5163 0.4318  0.0506  0.0768  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.7900 0.7895 0.5275 0.4252  0.0267  0.0498  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8002 0.8084 0.5295 0.4104  0.0281  0.0495  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.8170 0.8204 0.5227 0.4181  0.0411  0.0691  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.8096 0.8231 0.5303 0.4588  0.0014  0.0391  58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.8598 0.8715 0.5951 0.4741  -0.0068 0.0339  58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8394 0.8367 0.5971 0.4595  0.0092  0.0396  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.9126 0.9378 0.6372 0.5012  -0.0296 0.0239  58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.7899 0.8099 0.5395 0.3902  0.0166  0.0289  59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8065 0.8357 0.5489 0.3794  0.0155  0.0281  59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8179 0.8622 0.5439 0.4030  -0.0070 0.0140  59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8305 0.8847 0.5754 0.3977  -0.0244 -0.0091 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.7644 0.7947 0.5357 0.3429  0.0192  0.0177  59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.7464 0.7614 0.5284 0.3217  0.0418  0.0319  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.7800 0.8214 0.5460 0.3348  0.0146  0.0156  59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.7286 0.7428 0.5357 0.2869  0.0455  0.0211  59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.8443 0.8891 0.5360 0.4283  -0.0053 0.0274  60  THR   A N   
83   N  N   B THR   A 17  ? 0.8447 0.8899 0.5364 0.4282  -0.0057 0.0269  60  THR   A N   
84   N  N   C THR   A 17  ? 0.8443 0.8891 0.5360 0.4283  -0.0053 0.0274  60  THR   A N   
85   N  N   D THR   A 17  ? 0.8447 0.8899 0.5364 0.4282  -0.0057 0.0269  60  THR   A N   
86   C  CA  A THR   A 17  ? 0.8664 0.9233 0.5337 0.4554  -0.0250 0.0158  60  THR   A CA  
87   C  CA  B THR   A 17  ? 0.8678 0.9253 0.5361 0.4557  -0.0264 0.0144  60  THR   A CA  
88   C  CA  C THR   A 17  ? 0.8664 0.9233 0.5337 0.4554  -0.0250 0.0158  60  THR   A CA  
89   C  CA  D THR   A 17  ? 0.8678 0.9253 0.5361 0.4557  -0.0264 0.0144  60  THR   A CA  
90   C  C   A THR   A 17  ? 0.8790 0.9379 0.5223 0.4602  -0.0160 0.0276  60  THR   A C   
91   C  C   B THR   A 17  ? 0.8922 0.9511 0.5316 0.4651  -0.0178 0.0273  60  THR   A C   
92   C  C   C THR   A 17  ? 0.8790 0.9379 0.5223 0.4602  -0.0160 0.0276  60  THR   A C   
93   C  C   D THR   A 17  ? 0.8922 0.9511 0.5316 0.4651  -0.0178 0.0273  60  THR   A C   
94   O  O   A THR   A 17  ? 0.8723 0.9220 0.5079 0.4551  0.0062  0.0509  60  THR   A O   
95   O  O   B THR   A 17  ? 0.9121 0.9608 0.5357 0.4689  0.0031  0.0521  60  THR   A O   
96   O  O   C THR   A 17  ? 0.8723 0.9220 0.5079 0.4551  0.0062  0.0509  60  THR   A O   
97   O  O   D THR   A 17  ? 0.9121 0.9608 0.5357 0.4689  0.0031  0.0521  60  THR   A O   
98   C  CB  A THR   A 17  ? 0.8970 0.9521 0.5392 0.4898  -0.0338 0.0198  60  THR   A CB  
99   C  CB  B THR   A 17  ? 0.8901 0.9466 0.5411 0.4867  -0.0374 0.0145  60  THR   A CB  
100  C  CB  C THR   A 17  ? 0.8970 0.9521 0.5392 0.4898  -0.0338 0.0198  60  THR   A CB  
101  C  CB  D THR   A 17  ? 0.8901 0.9466 0.5411 0.4867  -0.0374 0.0145  60  THR   A CB  
102  O  OG1 A THR   A 17  ? 0.9147 0.9550 0.5342 0.4995  -0.0113 0.0490  60  THR   A OG1 
103  O  OG1 B THR   A 17  ? 0.8662 0.9226 0.5519 0.4739  -0.0434 0.0017  60  THR   A OG1 
104  O  OG1 C THR   A 17  ? 0.9147 0.9550 0.5342 0.4995  -0.0113 0.0490  60  THR   A OG1 
105  O  OG1 D THR   A 17  ? 0.8662 0.9226 0.5519 0.4739  -0.0434 0.0017  60  THR   A OG1 
106  C  CG2 A THR   A 17  ? 0.8955 0.9520 0.5649 0.4880  -0.0453 0.0061  60  THR   A CG2 
107  C  CG2 B THR   A 17  ? 0.9108 0.9808 0.5370 0.5155  -0.0613 -0.0011 60  THR   A CG2 
108  C  CG2 C THR   A 17  ? 0.8955 0.9520 0.5649 0.4880  -0.0453 0.0061  60  THR   A CG2 
109  C  CG2 D THR   A 17  ? 0.9108 0.9808 0.5370 0.5155  -0.0613 -0.0011 60  THR   A CG2 
110  N  N   . TRP   A 18  ? 0.8874 0.9579 0.5226 0.4688  -0.0322 0.0108  61  TRP   A N   
111  C  CA  . TRP   A 18  ? 0.9516 1.0247 0.5565 0.4843  -0.0266 0.0196  61  TRP   A CA  
112  C  C   . TRP   A 18  ? 1.0530 1.1229 0.6154 0.5217  -0.0296 0.0280  61  TRP   A C   
113  O  O   . TRP   A 18  ? 1.1180 1.1926 0.6764 0.5379  -0.0498 0.0126  61  TRP   A O   
114  C  CB  . TRP   A 18  ? 0.9521 1.0366 0.5645 0.4809  -0.0429 -0.0032 61  TRP   A CB  
115  C  CG  . TRP   A 18  ? 0.9911 1.0777 0.5749 0.4963  -0.0359 0.0046  61  TRP   A CG  
116  C  CD1 . TRP   A 18  ? 1.0256 1.1138 0.5695 0.5290  -0.0427 0.0022  61  TRP   A CD1 
117  C  CD2 . TRP   A 18  ? 0.9848 1.0725 0.5775 0.4805  -0.0202 0.0160  61  TRP   A CD2 
118  N  NE1 . TRP   A 18  ? 1.0581 1.1470 0.5855 0.5343  -0.0303 0.0113  61  TRP   A NE1 
119  C  CE2 . TRP   A 18  ? 1.0324 1.1221 0.5913 0.5053  -0.0169 0.0199  61  TRP   A CE2 
120  C  CE3 . TRP   A 18  ? 0.9451 1.0335 0.5704 0.4487  -0.0096 0.0228  61  TRP   A CE3 
121  C  CZ2 . TRP   A 18  ? 1.0220 1.1147 0.5831 0.4992  -0.0025 0.0303  61  TRP   A CZ2 
122  C  CZ3 . TRP   A 18  ? 0.9552 1.0477 0.5818 0.4431  0.0025  0.0337  61  TRP   A CZ3 
123  C  CH2 . TRP   A 18  ? 0.9391 1.0341 0.5364 0.4679  0.0062  0.0373  61  TRP   A CH2 
124  N  N   . GLU   A 19  ? 1.1172 1.1793 0.6505 0.5348  -0.0095 0.0527  62  GLU   A N   
125  C  CA  . GLU   A 19  ? 1.2022 1.2583 0.6896 0.5714  -0.0083 0.0654  62  GLU   A CA  
126  C  C   . GLU   A 19  ? 1.2533 1.3140 0.7045 0.5917  -0.0073 0.0653  62  GLU   A C   
127  O  O   . GLU   A 19  ? 1.2393 1.2970 0.6904 0.5826  0.0147  0.0819  62  GLU   A O   
128  C  CB  . GLU   A 19  ? 1.2794 1.3188 0.7613 0.5715  0.0181  0.0964  62  GLU   A CB  
129  C  CG  . GLU   A 19  ? 1.3473 1.3800 0.8612 0.5558  0.0168  0.0952  62  GLU   A CG  
130  C  CD  . GLU   A 19  ? 1.3726 1.4091 0.8812 0.5763  -0.0071 0.0806  62  GLU   A CD  
131  O  OE1 . GLU   A 19  ? 1.4493 1.4805 0.9196 0.6092  -0.0089 0.0923  62  GLU   A OE1 
132  O  OE2 . GLU   A 19  ? 1.3506 1.3958 0.8938 0.5599  -0.0237 0.0581  62  GLU   A OE2 
133  N  N   . LYS   A 20  ? 1.3039 1.3724 0.7279 0.6173  -0.0308 0.0456  63  LYS   A N   
134  C  CA  . LYS   A 20  ? 1.3482 1.4198 0.7297 0.6423  -0.0318 0.0426  63  LYS   A CA  
135  C  C   . LYS   A 20  ? 1.3413 1.3995 0.6856 0.6600  -0.0037 0.0761  63  LYS   A C   
136  O  O   . LYS   A 20  ? 1.4312 1.4792 0.7660 0.6690  0.0029  0.0934  63  LYS   A O   
137  C  CB  . LYS   A 20  ? 1.4245 1.5049 0.7788 0.6699  -0.0625 0.0176  63  LYS   A CB  
138  C  CG  . LYS   A 20  ? 1.4505 1.5441 0.8227 0.6619  -0.0847 -0.0166 63  LYS   A CG  
139  C  CD  . LYS   A 20  ? 1.5648 1.6640 0.8892 0.6954  -0.1025 -0.0342 63  LYS   A CD  
140  C  CE  . LYS   A 20  ? 1.5759 1.6767 0.8938 0.6934  -0.0969 -0.0446 63  LYS   A CE  
141  N  NZ  . LYS   A 20  ? 1.5461 1.6535 0.9179 0.6619  -0.1049 -0.0652 63  LYS   A NZ  
142  N  N   . ASP   A 21  ? 1.3457 1.4031 0.6746 0.6628  0.0143  0.0858  64  ASP   A N   
143  C  CA  . ASP   A 21  ? 1.4167 1.4614 0.7119 0.6792  0.0447  0.1183  64  ASP   A CA  
144  C  C   . ASP   A 21  ? 1.3576 1.3912 0.6831 0.6574  0.0686  0.1444  64  ASP   A C   
145  O  O   . ASP   A 21  ? 1.3641 1.3834 0.6637 0.6751  0.0823  0.1671  64  ASP   A O   
146  C  CB  . ASP   A 21  ? 1.5735 1.6113 0.8072 0.7208  0.0384  0.1234  64  ASP   A CB  
147  C  CG  . ASP   A 21  ? 1.6305 1.6760 0.8212 0.7474  0.0222  0.1027  64  ASP   A CG  
148  O  OD1 . ASP   A 21  ? 1.6187 1.6629 0.7913 0.7531  0.0410  0.1101  64  ASP   A OD1 
149  O  OD2 . ASP   A 21  ? 1.6863 1.7393 0.8617 0.7632  -0.0087 0.0789  64  ASP   A OD2 
150  N  N   . ALA   A 22  ? 1.3072 1.3461 0.6841 0.6211  0.0738  0.1417  65  ALA   A N   
151  C  CA  . ALA   A 22  ? 1.2437 1.2742 0.6504 0.5972  0.1016  0.1662  65  ALA   A CA  
152  C  C   . ALA   A 22  ? 1.2450 1.2771 0.6463 0.5974  0.1283  0.1843  65  ALA   A C   
153  O  O   . ALA   A 22  ? 1.2700 1.3104 0.6422 0.6175  0.1228  0.1741  65  ALA   A O   
154  C  CB  . ALA   A 22  ? 1.2161 1.2538 0.6773 0.5588  0.0925  0.1523  65  ALA   A CB  
155  N  N   . GLU   A 23  ? 1.2463 1.2680 0.6592 0.5878  0.1575  0.2115  66  GLU   A N   
156  C  CA  . GLU   A 23  ? 1.2609 1.2839 0.6798 0.5834  0.1880  0.2329  66  GLU   A CA  
157  C  C   . GLU   A 23  ? 1.1940 1.2364 0.6532 0.5569  0.1820  0.2191  66  GLU   A C   
158  O  O   . GLU   A 23  ? 1.0682 1.1156 0.5710 0.5250  0.1764  0.2131  66  GLU   A O   
159  C  CB  . GLU   A 23  ? 1.3352 1.3434 0.7729 0.5701  0.2151  0.2590  66  GLU   A CB  
160  C  CG  . GLU   A 23  ? 1.4157 1.4262 0.8729 0.5590  0.2476  0.2810  66  GLU   A CG  
161  C  CD  . GLU   A 23  ? 1.5197 1.5156 1.0033 0.5413  0.2729  0.3031  66  GLU   A CD  
162  O  OE1 . GLU   A 23  ? 1.5573 1.5331 1.0201 0.5550  0.2773  0.3136  66  GLU   A OE1 
163  O  OE2 . GLU   A 23  ? 1.5477 1.5527 1.0742 0.5138  0.2881  0.3095  66  GLU   A OE2 
164  N  N   . VAL   A 24  ? 1.1887 1.2410 0.6328 0.5703  0.1833  0.2144  67  VAL   A N   
165  C  CA  . VAL   A 24  ? 1.1496 1.2200 0.6278 0.5506  0.1748  0.2002  67  VAL   A CA  
166  C  C   . VAL   A 24  ? 1.1276 1.2050 0.6320 0.5380  0.2036  0.2218  67  VAL   A C   
167  O  O   . VAL   A 24  ? 1.1814 1.2545 0.6594 0.5596  0.2258  0.2382  67  VAL   A O   
168  C  CB  . VAL   A 24  ? 1.1677 1.2442 0.6171 0.5730  0.1575  0.1792  67  VAL   A CB  
169  C  CG1 . VAL   A 24  ? 1.1181 1.2106 0.6037 0.5536  0.1485  0.1653  67  VAL   A CG1 
170  C  CG2 . VAL   A 24  ? 1.1904 1.2611 0.6129 0.5881  0.1295  0.1579  67  VAL   A CG2 
171  N  N   . THR   A 25  ? 1.0725 1.1610 0.6273 0.5045  0.2033  0.2219  68  THR   A N   
172  C  CA  . THR   A 25  ? 1.0440 1.1405 0.6326 0.4875  0.2297  0.2430  68  THR   A CA  
173  C  C   . THR   A 25  ? 0.9883 1.1021 0.6284 0.4528  0.2178  0.2340  68  THR   A C   
174  O  O   . THR   A 25  ? 0.9675 1.0827 0.6139 0.4418  0.1922  0.2140  68  THR   A O   
175  C  CB  . THR   A 25  ? 1.0894 1.1697 0.6758 0.4859  0.2527  0.2650  68  THR   A CB  
176  O  OG1 . THR   A 25  ? 1.0899 1.1784 0.7022 0.4777  0.2811  0.2853  68  THR   A OG1 
177  C  CG2 . THR   A 25  ? 1.0758 1.1494 0.6880 0.4596  0.2430  0.2601  68  THR   A CG2 
178  N  N   . GLY   A 26  ? 0.9716 1.0988 0.6465 0.4376  0.2364  0.2489  69  GLY   A N   
179  C  CA  . GLY   A 26  ? 0.9113 1.0580 0.6353 0.4063  0.2280  0.2445  69  GLY   A CA  
180  C  C   . GLY   A 26  ? 0.9086 1.0730 0.6408 0.4127  0.2195  0.2366  69  GLY   A C   
181  O  O   . GLY   A 26  ? 0.9537 1.1127 0.6528 0.4367  0.2097  0.2246  69  GLY   A O   
182  N  N   . ASN   A 27  ? 0.9060 1.0912 0.6831 0.3908  0.2219  0.2420  70  ASN   A N   
183  C  CA  . ASN   A 27  ? 0.8844 1.0893 0.6812 0.3917  0.2138  0.2367  70  ASN   A CA  
184  C  C   . ASN   A 27  ? 0.8339 1.0432 0.6468 0.3705  0.1846  0.2191  70  ASN   A C   
185  O  O   . ASN   A 27  ? 0.8284 1.0242 0.6321 0.3589  0.1732  0.2105  70  ASN   A O   
186  C  CB  . ASN   A 27  ? 0.8948 1.1198 0.7297 0.3842  0.2362  0.2560  70  ASN   A CB  
187  C  CG  . ASN   A 27  ? 0.8867 1.1257 0.7676 0.3489  0.2317  0.2600  70  ASN   A CG  
188  O  OD1 . ASN   A 27  ? 0.8387 1.0663 0.7201 0.3341  0.2347  0.2623  70  ASN   A OD1 
189  N  ND2 . ASN   A 27  ? 0.9074 1.1709 0.8262 0.3354  0.2230  0.2598  70  ASN   A ND2 
190  N  N   . SER   A 28  ? 0.7939 1.0193 0.6277 0.3676  0.1736  0.2138  71  SER   A N   
191  C  CA  . SER   A 28  ? 0.8055 1.0341 0.6522 0.3506  0.1473  0.1984  71  SER   A CA  
192  C  C   . SER   A 28  ? 0.7956 1.0487 0.6868 0.3311  0.1443  0.2066  71  SER   A C   
193  O  O   . SER   A 28  ? 0.8098 1.0712 0.7092 0.3383  0.1357  0.2022  71  SER   A O   
194  C  CB  . SER   A 28  ? 0.8223 1.0428 0.6459 0.3707  0.1337  0.1817  71  SER   A CB  
195  O  OG  . SER   A 28  ? 0.8789 1.0792 0.6622 0.3886  0.1308  0.1706  71  SER   A OG  
196  N  N   . PRO   A 29  ? 0.7987 1.0643 0.7205 0.3066  0.1498  0.2177  72  PRO   A N   
197  C  CA  . PRO   A 29  ? 0.8001 1.0929 0.7649 0.2914  0.1469  0.2265  72  PRO   A CA  
198  C  C   . PRO   A 29  ? 0.7516 1.0479 0.7241 0.2766  0.1206  0.2152  72  PRO   A C   
199  O  O   . PRO   A 29  ? 0.7176 0.9980 0.6729 0.2653  0.1079  0.2034  72  PRO   A O   
200  C  CB  . PRO   A 29  ? 0.8118 1.1137 0.8027 0.2691  0.1591  0.2380  72  PRO   A CB  
201  C  CG  . PRO   A 29  ? 0.7993 1.0755 0.7620 0.2623  0.1572  0.2295  72  PRO   A CG  
202  C  CD  . PRO   A 29  ? 0.8145 1.0695 0.7336 0.2919  0.1580  0.2215  72  PRO   A CD  
203  N  N   . ARG   A 30  ? 0.7525 1.0679 0.7492 0.2792  0.1144  0.2194  73  ARG   A N   
204  C  CA  . ARG   A 30  ? 0.7818 1.1045 0.7923 0.2629  0.0913  0.2142  73  ARG   A CA  
205  C  C   . ARG   A 30  ? 0.7425 1.0907 0.7911 0.2373  0.0886  0.2254  73  ARG   A C   
206  O  O   . ARG   A 30  ? 0.7012 1.0730 0.7806 0.2417  0.0985  0.2383  73  ARG   A O   
207  C  CB  . ARG   A 30  ? 0.8642 1.1907 0.8782 0.2818  0.0853  0.2125  73  ARG   A CB  
208  C  CG  . ARG   A 30  ? 0.9434 1.2439 0.9201 0.3036  0.0837  0.1970  73  ARG   A CG  
209  C  CD  . ARG   A 30  ? 1.0187 1.3211 1.0000 0.3242  0.0817  0.1947  73  ARG   A CD  
210  N  NE  . ARG   A 30  ? 1.0776 1.3563 1.0237 0.3463  0.0820  0.1783  73  ARG   A NE  
211  C  CZ  . ARG   A 30  ? 1.0641 1.3237 0.9924 0.3442  0.0662  0.1612  73  ARG   A CZ  
212  N  NH1 . ARG   A 30  ? 1.0889 1.3480 1.0280 0.3213  0.0504  0.1594  73  ARG   A NH1 
213  N  NH2 . ARG   A 30  ? 1.0003 1.2415 0.8998 0.3650  0.0666  0.1454  73  ARG   A NH2 
214  N  N   . LEU   A 31  ? 0.6908 1.0349 0.7379 0.2115  0.0771  0.2198  74  LEU   A N   
215  C  CA  . LEU   A 31  ? 0.6656 1.0333 0.7467 0.1859  0.0753  0.2280  74  LEU   A CA  
216  C  C   . LEU   A 31  ? 0.6127 0.9883 0.6996 0.1663  0.0507  0.2237  74  LEU   A C   
217  O  O   . LEU   A 31  ? 0.6084 0.9631 0.6677 0.1647  0.0391  0.2123  74  LEU   A O   
218  C  CB  . LEU   A 31  ? 0.6538 1.0096 0.7288 0.1719  0.0879  0.2261  74  LEU   A CB  
219  C  CG  . LEU   A 31  ? 0.6828 1.0313 0.7529 0.1903  0.1142  0.2340  74  LEU   A CG  
220  C  CD1 . LEU   A 31  ? 0.6879 1.0170 0.7452 0.1782  0.1248  0.2307  74  LEU   A CD1 
221  C  CD2 . LEU   A 31  ? 0.6780 1.0558 0.7890 0.1931  0.1283  0.2498  74  LEU   A CD2 
222  N  N   . ASP   A 32  ? 0.5829 0.9887 0.7054 0.1525  0.0435  0.2331  75  ASP   A N   
223  C  CA  . ASP   A 32  ? 0.5993 1.0158 0.7273 0.1318  0.0198  0.2311  75  ASP   A CA  
224  C  C   . ASP   A 32  ? 0.5644 0.9804 0.6931 0.1026  0.0176  0.2248  75  ASP   A C   
225  O  O   . ASP   A 32  ? 0.5417 0.9789 0.7021 0.0914  0.0258  0.2311  75  ASP   A O   
226  C  CB  . ASP   A 32  ? 0.6334 1.0850 0.7995 0.1338  0.0104  0.2443  75  ASP   A CB  
227  C  CG  . ASP   A 32  ? 0.6613 1.1092 0.8218 0.1570  0.0043  0.2476  75  ASP   A CG  
228  O  OD1 . ASP   A 32  ? 0.6541 1.0754 0.7818 0.1610  -0.0030 0.2381  75  ASP   A OD1 
229  O  OD2 . ASP   A 32  ? 0.7306 1.2020 0.9220 0.1704  0.0076  0.2594  75  ASP   A OD2 
230  N  N   . VAL   A 33  ? 0.5379 0.9306 0.6353 0.0905  0.0078  0.2123  76  VAL   A N   
231  C  CA  . VAL   A 33  ? 0.5448 0.9307 0.6371 0.0636  0.0075  0.2034  76  VAL   A CA  
232  C  C   . VAL   A 33  ? 0.5359 0.9239 0.6169 0.0431  -0.0148 0.1973  76  VAL   A C   
233  O  O   . VAL   A 33  ? 0.5533 0.9312 0.6146 0.0518  -0.0264 0.1960  76  VAL   A O   
234  C  CB  . VAL   A 33  ? 0.5245 0.8775 0.5892 0.0685  0.0231  0.1936  76  VAL   A CB  
235  C  CG1 . VAL   A 33  ? 0.5260 0.8740 0.5925 0.0938  0.0435  0.2006  76  VAL   A CG1 
236  C  CG2 . VAL   A 33  ? 0.5318 0.8580 0.5609 0.0716  0.0141  0.1815  76  VAL   A CG2 
237  N  N   . ALA   A 34  ? 0.5242 0.9231 0.6158 0.0165  -0.0198 0.1930  77  ALA   A N   
238  C  CA  . ALA   A 34  ? 0.5142 0.9082 0.5861 -0.0066 -0.0372 0.1834  77  ALA   A CA  
239  C  C   . ALA   A 34  ? 0.5130 0.8778 0.5617 -0.0211 -0.0267 0.1681  77  ALA   A C   
240  O  O   . ALA   A 34  ? 0.5091 0.8665 0.5674 -0.0191 -0.0083 0.1671  77  ALA   A O   
241  C  CB  . ALA   A 34  ? 0.5266 0.9552 0.6263 -0.0256 -0.0522 0.1879  77  ALA   A CB  
242  N  N   . LEU   A 35  ? 0.5266 0.8735 0.5448 -0.0328 -0.0366 0.1575  78  LEU   A N   
243  C  CA  . LEU   A 35  ? 0.5346 0.8536 0.5293 -0.0483 -0.0288 0.1416  78  LEU   A CA  
244  C  C   . LEU   A 35  ? 0.5420 0.8684 0.5285 -0.0770 -0.0435 0.1334  78  LEU   A C   
245  O  O   . LEU   A 35  ? 0.5577 0.8864 0.5258 -0.0795 -0.0600 0.1347  78  LEU   A O   
246  C  CB  . LEU   A 35  ? 0.5396 0.8286 0.5038 -0.0339 -0.0257 0.1351  78  LEU   A CB  
247  C  CG  . LEU   A 35  ? 0.5527 0.8119 0.4950 -0.0453 -0.0158 0.1190  78  LEU   A CG  
248  C  CD1 . LEU   A 35  ? 0.5374 0.7904 0.4936 -0.0473 0.0022  0.1168  78  LEU   A CD1 
249  C  CD2 . LEU   A 35  ? 0.5428 0.7769 0.4624 -0.0288 -0.0131 0.1131  78  LEU   A CD2 
250  N  N   . ASP   A 36  ? 0.5297 0.8610 0.5298 -0.0981 -0.0384 0.1258  79  ASP   A N   
251  C  CA  . ASP   A 36  ? 0.5406 0.8775 0.5306 -0.1270 -0.0516 0.1145  79  ASP   A CA  
252  C  C   . ASP   A 36  ? 0.5478 0.8496 0.5000 -0.1371 -0.0459 0.0982  79  ASP   A C   
253  O  O   . ASP   A 36  ? 0.5197 0.7949 0.4599 -0.1222 -0.0312 0.0956  79  ASP   A O   
254  C  CB  . ASP   A 36  ? 0.5568 0.9156 0.5812 -0.1458 -0.0495 0.1118  79  ASP   A CB  
255  C  CG  . ASP   A 36  ? 0.5562 0.8928 0.5878 -0.1530 -0.0263 0.1021  79  ASP   A CG  
256  O  OD1 . ASP   A 36  ? 0.5569 0.8606 0.5632 -0.1458 -0.0137 0.0954  79  ASP   A OD1 
257  O  OD2 . ASP   A 36  ? 0.5582 0.9106 0.6224 -0.1653 -0.0208 0.1016  79  ASP   A OD2 
258  N  N   . GLU   A 37  ? 0.5757 0.8790 0.5109 -0.1615 -0.0575 0.0872  80  GLU   A N   
259  C  CA  . GLU   A 37  ? 0.6089 0.8823 0.5083 -0.1753 -0.0531 0.0706  80  GLU   A CA  
260  C  C   . GLU   A 37  ? 0.5962 0.8445 0.5011 -0.1792 -0.0303 0.0587  80  GLU   A C   
261  O  O   . GLU   A 37  ? 0.5972 0.8164 0.4772 -0.1787 -0.0212 0.0486  80  GLU   A O   
262  C  CB  . GLU   A 37  ? 0.6594 0.9447 0.5429 -0.2015 -0.0701 0.0615  80  GLU   A CB  
263  C  CG  . GLU   A 37  ? 0.6921 0.9503 0.5317 -0.2117 -0.0697 0.0489  80  GLU   A CG  
264  C  CD  . GLU   A 37  ? 0.7365 1.0064 0.5538 -0.2360 -0.0875 0.0404  80  GLU   A CD  
265  O  OE1 . GLU   A 37  ? 0.7448 1.0213 0.5715 -0.2576 -0.0876 0.0270  80  GLU   A OE1 
266  O  OE2 . GLU   A 37  ? 0.7975 1.0694 0.5874 -0.2331 -0.1013 0.0472  80  GLU   A OE2 
267  N  N   . SER   A 38  ? 0.5897 0.8485 0.5272 -0.1830 -0.0209 0.0602  81  SER   A N   
268  C  CA  . SER   A 38  ? 0.5888 0.8245 0.5358 -0.1862 0.0018  0.0516  81  SER   A CA  
269  C  C   . SER   A 38  ? 0.5694 0.7906 0.5211 -0.1578 0.0175  0.0618  81  SER   A C   
270  O  O   . SER   A 38  ? 0.5891 0.7931 0.5509 -0.1572 0.0366  0.0585  81  SER   A O   
271  C  CB  . SER   A 38  ? 0.6041 0.8566 0.5848 -0.2023 0.0060  0.0503  81  SER   A CB  
272  O  OG  . SER   A 38  ? 0.6331 0.9015 0.6092 -0.2283 -0.0110 0.0394  81  SER   A OG  
273  N  N   . GLY   A 39  ? 0.5610 0.7884 0.5061 -0.1349 0.0103  0.0736  82  GLY   A N   
274  C  CA  . GLY   A 39  ? 0.5466 0.7612 0.4927 -0.1064 0.0231  0.0818  82  GLY   A CA  
275  C  C   . GLY   A 39  ? 0.5472 0.7772 0.5234 -0.0931 0.0333  0.0961  82  GLY   A C   
276  O  O   . GLY   A 39  ? 0.5410 0.7580 0.5153 -0.0706 0.0461  0.1018  82  GLY   A O   
277  N  N   . ASP   A 40  ? 0.5553 0.8131 0.5586 -0.1056 0.0279  0.1020  83  ASP   A N   
278  C  CA  . ASP   A 40  ? 0.5597 0.8357 0.5959 -0.0940 0.0385  0.1167  83  ASP   A CA  
279  C  C   . ASP   A 40  ? 0.5357 0.8326 0.5766 -0.0720 0.0282  0.1310  83  ASP   A C   
280  O  O   . ASP   A 40  ? 0.5228 0.8413 0.5666 -0.0798 0.0088  0.1327  83  ASP   A O   
281  C  CB  . ASP   A 40  ? 0.5771 0.8762 0.6470 -0.1183 0.0376  0.1155  83  ASP   A CB  
282  C  CG  . ASP   A 40  ? 0.5930 0.8727 0.6600 -0.1434 0.0458  0.0990  83  ASP   A CG  
283  O  OD1 . ASP   A 40  ? 0.5874 0.8429 0.6547 -0.1375 0.0670  0.0985  83  ASP   A OD1 
284  O  OD2 . ASP   A 40  ? 0.6245 0.9132 0.6873 -0.1679 0.0307  0.0869  83  ASP   A OD2 
285  N  N   . PHE   A 41  ? 0.5379 0.8281 0.5792 -0.0452 0.0414  0.1411  84  PHE   A N   
286  C  CA  . PHE   A 41  ? 0.5318 0.8417 0.5841 -0.0224 0.0376  0.1555  84  PHE   A CA  
287  C  C   . PHE   A 41  ? 0.5508 0.8907 0.6446 -0.0276 0.0433  0.1668  84  PHE   A C   
288  O  O   . PHE   A 41  ? 0.5658 0.9028 0.6773 -0.0396 0.0584  0.1658  84  PHE   A O   
289  C  CB  . PHE   A 41  ? 0.5237 0.8135 0.5580 0.0070  0.0506  0.1594  84  PHE   A CB  
290  C  CG  . PHE   A 41  ? 0.5312 0.8000 0.5321 0.0164  0.0411  0.1498  84  PHE   A CG  
291  C  CD1 . PHE   A 41  ? 0.5187 0.7969 0.5132 0.0221  0.0241  0.1512  84  PHE   A CD1 
292  C  CD2 . PHE   A 41  ? 0.5469 0.7863 0.5253 0.0204  0.0501  0.1400  84  PHE   A CD2 
293  C  CE1 . PHE   A 41  ? 0.5452 0.8033 0.5127 0.0303  0.0174  0.1422  84  PHE   A CE1 
294  C  CE2 . PHE   A 41  ? 0.5329 0.7550 0.4857 0.0282  0.0417  0.1303  84  PHE   A CE2 
295  C  CZ  . PHE   A 41  ? 0.5241 0.7551 0.4720 0.0335  0.0263  0.1314  84  PHE   A CZ  
296  N  N   . SER   A 42  ? 0.5531 0.9210 0.6646 -0.0191 0.0320  0.1772  85  SER   A N   
297  C  CA  . SER   A 42  ? 0.5517 0.9520 0.7075 -0.0197 0.0374  0.1895  85  SER   A CA  
298  C  C   . SER   A 42  ? 0.5574 0.9750 0.7219 0.0060  0.0340  0.2029  85  SER   A C   
299  O  O   . SER   A 42  ? 0.5213 0.9326 0.6620 0.0164  0.0194  0.2013  85  SER   A O   
300  C  CB  . SER   A 42  ? 0.5577 0.9839 0.7376 -0.0485 0.0213  0.1845  85  SER   A CB  
301  O  OG  . SER   A 42  ? 0.5586 0.9929 0.7212 -0.0524 -0.0042 0.1815  85  SER   A OG  
302  N  N   . LEU   A 43  ? 0.5866 1.0238 0.7853 0.0161  0.0490  0.2155  86  LEU   A N   
303  C  CA  . LEU   A 43  ? 0.5855 1.0412 0.7984 0.0410  0.0494  0.2286  86  LEU   A CA  
304  C  C   . LEU   A 43  ? 0.5802 1.0728 0.8232 0.0300  0.0266  0.2330  86  LEU   A C   
305  O  O   . LEU   A 43  ? 0.5564 1.0750 0.8359 0.0093  0.0237  0.2336  86  LEU   A O   
306  C  CB  . LEU   A 43  ? 0.6040 1.0659 0.8423 0.0547  0.0768  0.2404  86  LEU   A CB  
307  C  CG  . LEU   A 43  ? 0.6342 1.0610 0.8417 0.0694  0.0999  0.2392  86  LEU   A CG  
308  C  CD1 . LEU   A 43  ? 0.6628 1.0971 0.8942 0.0842  0.1277  0.2533  86  LEU   A CD1 
309  C  CD2 . LEU   A 43  ? 0.6625 1.0644 0.8255 0.0924  0.0939  0.2341  86  LEU   A CD2 
310  N  N   . VAL   A 44  ? 0.6102 1.1048 0.8391 0.0442  0.0107  0.2359  87  VAL   A N   
311  C  CA  . VAL   A 44  ? 0.6502 1.1807 0.9091 0.0452  -0.0083 0.2455  87  VAL   A CA  
312  C  C   . VAL   A 44  ? 0.6769 1.2271 0.9698 0.0687  0.0076  0.2598  87  VAL   A C   
313  O  O   . VAL   A 44  ? 0.7394 1.2677 1.0163 0.0884  0.0295  0.2609  87  VAL   A O   
314  C  CB  . VAL   A 44  ? 0.6382 1.1537 0.8622 0.0523  -0.0279 0.2427  87  VAL   A CB  
315  C  CG1 . VAL   A 44  ? 0.6401 1.1873 0.8887 0.0569  -0.0481 0.2541  87  VAL   A CG1 
316  C  CG2 . VAL   A 44  ? 0.6221 1.1148 0.8104 0.0300  -0.0386 0.2282  87  VAL   A CG2 
317  N  N   . GLU   A 45  ? 0.7377 1.3280 1.0763 0.0677  -0.0011 0.2703  88  GLU   A N   
318  C  CA  . GLU   A 45  ? 0.7480 1.3568 1.1171 0.0940  0.0119  0.2844  88  GLU   A CA  
319  C  C   . GLU   A 45  ? 0.7311 1.3767 1.1331 0.0955  -0.0113 0.2939  88  GLU   A C   
320  O  O   . GLU   A 45  ? 0.6889 1.3303 1.0686 0.0907  -0.0356 0.2913  88  GLU   A O   
321  C  CB  . GLU   A 45  ? 0.7573 1.3808 1.1647 0.0950  0.0392  0.2910  88  GLU   A CB  
322  C  CG  . GLU   A 45  ? 0.7851 1.3785 1.1698 0.0870  0.0612  0.2836  88  GLU   A CG  
323  C  CD  . GLU   A 45  ? 0.7774 1.3388 1.1299 0.1135  0.0871  0.2856  88  GLU   A CD  
324  O  OE1 . GLU   A 45  ? 0.8167 1.3484 1.1227 0.1250  0.0808  0.2782  88  GLU   A OE1 
325  O  OE2 . GLU   A 45  ? 0.8166 1.3821 1.1896 0.1219  0.1139  0.2940  88  GLU   A OE2 
326  N  N   . GLY   B 7   ? 0.9449 0.9606 1.1131 0.1417  0.1139  -0.0065 16  GLY   B N   
327  C  CA  . GLY   B 7   ? 0.9334 0.9390 1.0952 0.1432  0.1145  -0.0063 16  GLY   B CA  
328  C  C   . GLY   B 7   ? 0.9288 0.9323 1.0840 0.1465  0.1072  -0.0050 16  GLY   B C   
329  O  O   . GLY   B 7   ? 0.9942 1.0036 1.1506 0.1444  0.0997  -0.0047 16  GLY   B O   
330  N  N   . GLU   B 8   ? 0.8431 0.8386 0.9912 0.1515  0.1087  -0.0039 17  GLU   B N   
331  C  CA  . GLU   B 8   ? 0.8305 0.8217 0.9693 0.1563  0.1016  -0.0033 17  GLU   B CA  
332  C  C   . GLU   B 8   ? 0.7708 0.7614 0.9072 0.1505  0.0946  -0.0056 17  GLU   B C   
333  O  O   . GLU   B 8   ? 0.7631 0.7514 0.8988 0.1478  0.0976  -0.0065 17  GLU   B O   
334  C  CB  . GLU   B 8   ? 0.8598 0.8442 0.9915 0.1642  0.1064  -0.0009 17  GLU   B CB  
335  C  CG  . GLU   B 8   ? 0.8813 0.8610 1.0017 0.1718  0.0994  -0.0004 17  GLU   B CG  
336  C  CD  . GLU   B 8   ? 0.9356 0.9111 1.0489 0.1819  0.1044  0.0030  17  GLU   B CD  
337  O  OE1 . GLU   B 8   ? 0.8879 0.8634 1.0047 0.1817  0.1130  0.0056  17  GLU   B OE1 
338  O  OE2 . GLU   B 8   ? 1.0247 0.9970 1.1290 0.1900  0.0992  0.0036  17  GLU   B OE2 
339  N  N   A THR   B 9   ? 0.7602 0.7528 0.8957 0.1483  0.0849  -0.0061 18  THR   B N   
340  N  N   B THR   B 9   ? 0.7571 0.7495 0.8923 0.1485  0.0849  -0.0061 18  THR   B N   
341  N  N   C THR   B 9   ? 0.7614 0.7540 0.8968 0.1484  0.0849  -0.0061 18  THR   B N   
342  N  N   D THR   B 9   ? 0.7555 0.7480 0.8908 0.1485  0.0849  -0.0061 18  THR   B N   
343  C  CA  A THR   B 9   ? 0.7411 0.7322 0.8741 0.1424  0.0763  -0.0079 18  THR   B CA  
344  C  CA  B THR   B 9   ? 0.7359 0.7272 0.8691 0.1424  0.0762  -0.0079 18  THR   B CA  
345  C  CA  C THR   B 9   ? 0.7427 0.7340 0.8758 0.1424  0.0762  -0.0079 18  THR   B CA  
346  C  CA  D THR   B 9   ? 0.7331 0.7246 0.8664 0.1423  0.0761  -0.0078 18  THR   B CA  
347  C  C   A THR   B 9   ? 0.7312 0.7129 0.8514 0.1486  0.0672  -0.0084 18  THR   B C   
348  C  C   B THR   B 9   ? 0.7284 0.7102 0.8488 0.1485  0.0670  -0.0084 18  THR   B C   
349  C  C   C THR   B 9   ? 0.7320 0.7136 0.8522 0.1487  0.0674  -0.0084 18  THR   B C   
350  C  C   D THR   B 9   ? 0.7267 0.7085 0.8470 0.1486  0.0672  -0.0084 18  THR   B C   
351  O  O   A THR   B 9   ? 0.7305 0.7085 0.8467 0.1446  0.0582  -0.0100 18  THR   B O   
352  O  O   B THR   B 9   ? 0.7284 0.7068 0.8450 0.1444  0.0578  -0.0099 18  THR   B O   
353  O  O   C THR   B 9   ? 0.7311 0.7088 0.8470 0.1448  0.0588  -0.0101 18  THR   B O   
354  O  O   D THR   B 9   ? 0.7263 0.7043 0.8426 0.1446  0.0585  -0.0100 18  THR   B O   
355  C  CB  A THR   B 9   ? 0.7374 0.7377 0.8795 0.1341  0.0709  -0.0073 18  THR   B CB  
356  C  CB  B THR   B 9   ? 0.7281 0.7292 0.8709 0.1343  0.0715  -0.0072 18  THR   B CB  
357  C  CB  C THR   B 9   ? 0.7408 0.7411 0.8825 0.1346  0.0701  -0.0071 18  THR   B CB  
358  C  CB  D THR   B 9   ? 0.7242 0.7252 0.8665 0.1348  0.0706  -0.0070 18  THR   B CB  
359  O  OG1 A THR   B 9   ? 0.7304 0.7393 0.8824 0.1316  0.0798  -0.0068 18  THR   B OG1 
360  O  OG1 B THR   B 9   ? 0.7228 0.7279 0.8674 0.1381  0.0692  -0.0049 18  THR   B OG1 
361  O  OG1 C THR   B 9   ? 0.7339 0.7434 0.8856 0.1327  0.0785  -0.0062 18  THR   B OG1 
362  O  OG1 D THR   B 9   ? 0.7155 0.7188 0.8578 0.1392  0.0670  -0.0048 18  THR   B OG1 
363  C  CG2 A THR   B 9   ? 0.7362 0.7357 0.8779 0.1264  0.0639  -0.0087 18  THR   B CG2 
364  C  CG2 B THR   B 9   ? 0.7197 0.7290 0.8727 0.1284  0.0797  -0.0076 18  THR   B CG2 
365  C  CG2 C THR   B 9   ? 0.7412 0.7416 0.8837 0.1264  0.0638  -0.0084 18  THR   B CG2 
366  C  CG2 D THR   B 9   ? 0.7166 0.7270 0.8699 0.1292  0.0786  -0.0070 18  THR   B CG2 
367  N  N   . THR   B 10  ? 0.7164 0.6937 0.8296 0.1585  0.0690  -0.0071 19  THR   B N   
368  C  CA  . THR   B 10  ? 0.6923 0.6601 0.7915 0.1667  0.0603  -0.0078 19  THR   B CA  
369  C  C   . THR   B 10  ? 0.6371 0.5976 0.7268 0.1681  0.0583  -0.0098 19  THR   B C   
370  O  O   . THR   B 10  ? 0.5879 0.5500 0.6787 0.1695  0.0679  -0.0089 19  THR   B O   
371  C  CB  . THR   B 10  ? 0.7144 0.6801 0.8081 0.1778  0.0655  -0.0056 19  THR   B CB  
372  O  OG1 . THR   B 10  ? 0.7711 0.7440 0.8741 0.1766  0.0687  -0.0038 19  THR   B OG1 
373  C  CG2 . THR   B 10  ? 0.7373 0.6936 0.8159 0.1872  0.0558  -0.0066 19  THR   B CG2 
374  N  N   . ASP   B 11  ? 0.6167 0.5692 0.6969 0.1684  0.0459  -0.0121 20  ASP   B N   
375  C  CA  . ASP   B 11  ? 0.6211 0.5646 0.6883 0.1731  0.0423  -0.0142 20  ASP   B CA  
376  C  C   . ASP   B 11  ? 0.6209 0.5629 0.6796 0.1855  0.0509  -0.0124 20  ASP   B C   
377  O  O   . ASP   B 11  ? 0.6304 0.5743 0.6891 0.1920  0.0547  -0.0101 20  ASP   B O   
378  C  CB  . ASP   B 11  ? 0.6549 0.5867 0.7100 0.1748  0.0261  -0.0168 20  ASP   B CB  
379  C  CG  . ASP   B 11  ? 0.6700 0.6028 0.7326 0.1618  0.0176  -0.0178 20  ASP   B CG  
380  O  OD1 . ASP   B 11  ? 0.6324 0.5768 0.7105 0.1521  0.0242  -0.0161 20  ASP   B OD1 
381  O  OD2 . ASP   B 11  ? 0.7167 0.6380 0.7686 0.1620  0.0041  -0.0200 20  ASP   B OD2 
382  N  N   . GLY   B 12  ? 0.5926 0.5326 0.6446 0.1890  0.0539  -0.0127 21  GLY   B N   
383  C  CA  . GLY   B 12  ? 0.5724 0.5126 0.6157 0.2013  0.0612  -0.0098 21  GLY   B CA  
384  C  C   . GLY   B 12  ? 0.5489 0.4966 0.5989 0.1984  0.0721  -0.0073 21  GLY   B C   
385  O  O   . GLY   B 12  ? 0.5218 0.4731 0.5818 0.1870  0.0734  -0.0088 21  GLY   B O   
386  N  N   . VAL   B 13  ? 0.5471 0.4979 0.5920 0.2085  0.0797  -0.0030 22  VAL   B N   
387  C  CA  . VAL   B 13  ? 0.5351 0.4939 0.5856 0.2072  0.0898  0.0008  22  VAL   B CA  
388  C  C   . VAL   B 13  ? 0.5367 0.5033 0.6018 0.2027  0.1006  0.0055  22  VAL   B C   
389  O  O   . VAL   B 13  ? 0.5672 0.5328 0.6320 0.2073  0.1014  0.0071  22  VAL   B O   
390  C  CB  . VAL   B 13  ? 0.5508 0.5090 0.5860 0.2212  0.0902  0.0034  22  VAL   B CB  
391  C  CG1 . VAL   B 13  ? 0.5544 0.5131 0.5819 0.2345  0.0929  0.0077  22  VAL   B CG1 
392  C  CG2 . VAL   B 13  ? 0.5424 0.5095 0.5831 0.2187  0.0984  0.0073  22  VAL   B CG2 
393  N  N   . TYR   B 14  ? 0.5127 0.4853 0.5900 0.1931  0.1073  0.0069  23  TYR   B N   
394  C  CA  . TYR   B 14  ? 0.5019 0.4797 0.5933 0.1871  0.1164  0.0105  23  TYR   B CA  
395  C  C   . TYR   B 14  ? 0.4987 0.4833 0.5951 0.1860  0.1246  0.0161  23  TYR   B C   
396  O  O   . TYR   B 14  ? 0.4964 0.4832 0.5891 0.1859  0.1235  0.0158  23  TYR   B O   
397  C  CB  . TYR   B 14  ? 0.4948 0.4722 0.5972 0.1747  0.1148  0.0060  23  TYR   B CB  
398  C  CG  . TYR   B 14  ? 0.4831 0.4569 0.5846 0.1743  0.1083  0.0024  23  TYR   B CG  
399  C  CD1 . TYR   B 14  ? 0.4886 0.4575 0.5807 0.1768  0.0980  -0.0012 23  TYR   B CD1 
400  C  CD2 . TYR   B 14  ? 0.4870 0.4623 0.5968 0.1720  0.1121  0.0033  23  TYR   B CD2 
401  C  CE1 . TYR   B 14  ? 0.4924 0.4592 0.5848 0.1758  0.0915  -0.0035 23  TYR   B CE1 
402  C  CE2 . TYR   B 14  ? 0.4951 0.4692 0.6049 0.1720  0.1065  0.0009  23  TYR   B CE2 
403  C  CZ  . TYR   B 14  ? 0.5051 0.4757 0.6069 0.1734  0.0961  -0.0021 23  TYR   B CZ  
404  O  OH  . TYR   B 14  ? 0.5235 0.4941 0.6266 0.1724  0.0899  -0.0036 23  TYR   B OH  
405  N  N   . ARG   B 15  ? 0.5012 0.4892 0.6054 0.1860  0.1324  0.0220  24  ARG   B N   
406  C  CA  . ARG   B 15  ? 0.5031 0.4979 0.6164 0.1814  0.1400  0.0281  24  ARG   B CA  
407  C  C   . ARG   B 15  ? 0.4896 0.4832 0.6154 0.1678  0.1410  0.0244  24  ARG   B C   
408  O  O   . ARG   B 15  ? 0.4637 0.4528 0.5935 0.1639  0.1397  0.0207  24  ARG   B O   
409  C  CB  . ARG   B 15  ? 0.5142 0.5124 0.6316 0.1859  0.1473  0.0367  24  ARG   B CB  
410  C  CG  . ARG   B 15  ? 0.5362 0.5360 0.6415 0.2006  0.1473  0.0411  24  ARG   B CG  
411  C  CD  . ARG   B 15  ? 0.5453 0.5489 0.6562 0.2040  0.1547  0.0504  24  ARG   B CD  
412  N  NE  . ARG   B 15  ? 0.5586 0.5634 0.6571 0.2187  0.1542  0.0537  24  ARG   B NE  
413  C  CZ  . ARG   B 15  ? 0.5812 0.5940 0.6723 0.2293  0.1570  0.0606  24  ARG   B CZ  
414  N  NH1 . ARG   B 15  ? 0.5862 0.6083 0.6816 0.2270  0.1610  0.0660  24  ARG   B NH1 
415  N  NH2 . ARG   B 15  ? 0.6123 0.6244 0.6906 0.2433  0.1555  0.0620  24  ARG   B NH2 
416  N  N   . VAL   B 16  ? 0.4932 0.4915 0.6247 0.1616  0.1437  0.0262  25  VAL   B N   
417  C  CA  . VAL   B 16  ? 0.5006 0.4979 0.6440 0.1492  0.1455  0.0239  25  VAL   B CA  
418  C  C   . VAL   B 16  ? 0.4911 0.4914 0.6435 0.1467  0.1523  0.0321  25  VAL   B C   
419  O  O   . VAL   B 16  ? 0.4818 0.4895 0.6346 0.1489  0.1553  0.0387  25  VAL   B O   
420  C  CB  . VAL   B 16  ? 0.5088 0.5085 0.6522 0.1431  0.1424  0.0195  25  VAL   B CB  
421  C  CG1 . VAL   B 16  ? 0.5086 0.5067 0.6627 0.1311  0.1433  0.0159  25  VAL   B CG1 
422  C  CG2 . VAL   B 16  ? 0.5073 0.5036 0.6405 0.1467  0.1348  0.0130  25  VAL   B CG2 
423  N  N   . MET   B 17  ? 0.4967 0.4914 0.6563 0.1418  0.1540  0.0315  26  MET   B N   
424  C  CA  . MET   B 17  ? 0.5257 0.5196 0.6934 0.1394  0.1592  0.0392  26  MET   B CA  
425  C  C   . MET   B 17  ? 0.5249 0.5139 0.7022 0.1277  0.1591  0.0363  26  MET   B C   
426  O  O   . MET   B 17  ? 0.4995 0.4836 0.6765 0.1241  0.1560  0.0281  26  MET   B O   
427  C  CB  . MET   B 17  ? 0.5445 0.5328 0.7103 0.1453  0.1604  0.0408  26  MET   B CB  
428  C  CG  . MET   B 17  ? 0.5628 0.5544 0.7180 0.1578  0.1598  0.0430  26  MET   B CG  
429  S  SD  . MET   B 17  ? 0.5613 0.5639 0.7123 0.1668  0.1638  0.0539  26  MET   B SD  
430  C  CE  . MET   B 17  ? 0.5885 0.5921 0.7515 0.1626  0.1704  0.0653  26  MET   B CE  
431  N  N   . THR   B 18  ? 0.5521 0.5425 0.7375 0.1225  0.1622  0.0436  27  THR   B N   
432  C  CA  . THR   B 18  ? 0.5982 0.5810 0.7922 0.1123  0.1616  0.0420  27  THR   B CA  
433  C  C   . THR   B 18  ? 0.6282 0.6054 0.8277 0.1117  0.1643  0.0502  27  THR   B C   
434  O  O   . THR   B 18  ? 0.5752 0.5593 0.7759 0.1162  0.1677  0.0602  27  THR   B O   
435  C  CB  . THR   B 18  ? 0.6026 0.5908 0.8022 0.1041  0.1609  0.0427  27  THR   B CB  
436  O  OG1 . THR   B 18  ? 0.6336 0.6116 0.8388 0.0955  0.1589  0.0384  27  THR   B OG1 
437  C  CG2 . THR   B 18  ? 0.5969 0.5951 0.8018 0.1040  0.1642  0.0545  27  THR   B CG2 
438  N  N   . ARG   B 19  ? 0.6931 0.6583 0.8959 0.1064  0.1626  0.0463  28  ARG   B N   
439  C  CA  . ARG   B 19  ? 0.8138 0.7702 1.0226 0.1032  0.1637  0.0534  28  ARG   B CA  
440  C  C   . ARG   B 19  ? 0.8598 0.8132 1.0776 0.0917  0.1617  0.0561  28  ARG   B C   
441  O  O   . ARG   B 19  ? 0.8819 0.8295 1.1059 0.0878  0.1618  0.0642  28  ARG   B O   
442  C  CB  . ARG   B 19  ? 0.8419 0.7857 1.0463 0.1067  0.1625  0.0475  28  ARG   B CB  
443  C  CG  . ARG   B 19  ? 0.8948 0.8430 1.0914 0.1177  0.1642  0.0463  28  ARG   B CG  
444  C  CD  . ARG   B 19  ? 0.9595 0.9022 1.1555 0.1233  0.1666  0.0530  28  ARG   B CD  
445  N  NE  . ARG   B 19  ? 1.0081 0.9520 1.1962 0.1334  0.1672  0.0498  28  ARG   B NE  
446  C  CZ  . ARG   B 19  ? 1.0525 0.9912 1.2362 0.1357  0.1649  0.0409  28  ARG   B CZ  
447  N  NH1 . ARG   B 19  ? 1.0856 1.0177 1.2709 0.1296  0.1623  0.0336  28  ARG   B NH1 
448  N  NH2 . ARG   B 19  ? 1.0620 1.0033 1.2395 0.1445  0.1651  0.0395  28  ARG   B NH2 
449  N  N   . ARG   B 20  ? 0.9531 0.9113 1.1720 0.0863  0.1596  0.0509  29  ARG   B N   
450  C  CA  . ARG   B 20  ? 1.0094 0.9640 1.2361 0.0751  0.1567  0.0515  29  ARG   B CA  
451  C  C   . ARG   B 20  ? 0.9937 0.9556 1.2299 0.0707  0.1584  0.0656  29  ARG   B C   
452  O  O   . ARG   B 20  ? 1.0070 0.9611 1.2507 0.0613  0.1552  0.0686  29  ARG   B O   
453  C  CB  . ARG   B 20  ? 1.0536 1.0144 1.2787 0.0718  0.1547  0.0435  29  ARG   B CB  
454  C  CG  . ARG   B 20  ? 1.1298 1.0796 1.3574 0.0629  0.1501  0.0366  29  ARG   B CG  
455  C  CD  . ARG   B 20  ? 1.2261 1.1813 1.4508 0.0608  0.1483  0.0276  29  ARG   B CD  
456  N  NE  . ARG   B 20  ? 1.3168 1.2875 1.5432 0.0607  0.1501  0.0316  29  ARG   B NE  
457  C  CZ  . ARG   B 20  ? 1.3511 1.3276 1.5842 0.0533  0.1490  0.0355  29  ARG   B CZ  
458  N  NH1 . ARG   B 20  ? 1.3882 1.3559 1.6278 0.0443  0.1456  0.0363  29  ARG   B NH1 
459  N  NH2 . ARG   B 20  ? 1.3596 1.3505 1.5925 0.0551  0.1509  0.0387  29  ARG   B NH2 
460  N  N   . LEU   B 21  ? 0.9418 0.9180 1.1776 0.0775  0.1629  0.0742  30  LEU   B N   
461  C  CA  . LEU   B 21  ? 0.8833 0.8700 1.1283 0.0751  0.1656  0.0897  30  LEU   B CA  
462  C  C   . LEU   B 21  ? 0.8417 0.8224 1.0877 0.0790  0.1676  0.0978  30  LEU   B C   
463  O  O   . LEU   B 21  ? 0.8102 0.7763 1.0511 0.0812  0.1660  0.0907  30  LEU   B O   
464  C  CB  . LEU   B 21  ? 0.8669 0.8732 1.1091 0.0821  0.1694  0.0942  30  LEU   B CB  
465  C  CG  . LEU   B 21  ? 0.9019 0.9164 1.1463 0.0766  0.1677  0.0907  30  LEU   B CG  
466  C  CD1 . LEU   B 21  ? 0.9005 0.9013 1.1433 0.0694  0.1626  0.0773  30  LEU   B CD1 
467  C  CD2 . LEU   B 21  ? 0.9190 0.9472 1.1543 0.0868  0.1702  0.0891  30  LEU   B CD2 
468  N  N   . LEU   B 22  ? 0.8322 0.8248 1.0849 0.0801  0.1712  0.1127  31  LEU   B N   
469  C  CA  . LEU   B 22  ? 0.7934 0.7829 1.0474 0.0846  0.1739  0.1224  31  LEU   B CA  
470  C  C   . LEU   B 22  ? 0.7666 0.7567 1.0080 0.0985  0.1769  0.1167  31  LEU   B C   
471  O  O   . LEU   B 22  ? 0.7612 0.7622 0.9953 0.1057  0.1785  0.1121  31  LEU   B O   
472  C  CB  . LEU   B 22  ? 0.7854 0.7925 1.0491 0.0838  0.1777  0.1404  31  LEU   B CB  
473  C  CG  . LEU   B 22  ? 0.7891 0.7937 1.0566 0.0864  0.1801  0.1526  31  LEU   B CG  
474  C  CD1 . LEU   B 22  ? 0.7812 0.7669 1.0571 0.0741  0.1745  0.1545  31  LEU   B CD1 
475  C  CD2 . LEU   B 22  ? 0.7983 0.8259 1.0725 0.0901  0.1856  0.1703  31  LEU   B CD2 
476  N  N   . GLY   B 23  ? 0.7355 0.7142 0.9743 0.1024  0.1773  0.1172  32  GLY   B N   
477  C  CA  . GLY   B 23  ? 0.6986 0.6755 0.9256 0.1148  0.1791  0.1108  32  GLY   B CA  
478  C  C   . GLY   B 23  ? 0.6550 0.6322 0.8729 0.1179  0.1769  0.0963  32  GLY   B C   
479  O  O   . GLY   B 23  ? 0.6253 0.5953 0.8450 0.1098  0.1730  0.0875  32  GLY   B O   
480  N  N   . SER   B 24  ? 0.6347 0.6192 0.8429 0.1294  0.1787  0.0940  33  SER   B N   
481  C  CA  . SER   B 24  ? 0.6198 0.6063 0.8189 0.1334  0.1762  0.0821  33  SER   B CA  
482  C  C   . SER   B 24  ? 0.5847 0.5866 0.7812 0.1377  0.1779  0.0865  33  SER   B C   
483  O  O   . SER   B 24  ? 0.5659 0.5765 0.7593 0.1469  0.1814  0.0952  33  SER   B O   
484  C  CB  . SER   B 24  ? 0.6238 0.6060 0.8131 0.1432  0.1756  0.0765  33  SER   B CB  
485  O  OG  . SER   B 24  ? 0.6673 0.6362 0.8579 0.1404  0.1741  0.0719  33  SER   B OG  
486  N  N   . THR   B 25  ? 0.5726 0.5778 0.7697 0.1323  0.1754  0.0808  34  THR   B N   
487  C  CA  . THR   B 25  ? 0.5751 0.5948 0.7700 0.1359  0.1768  0.0850  34  THR   B CA  
488  C  C   . THR   B 25  ? 0.5687 0.5880 0.7523 0.1411  0.1731  0.0741  34  THR   B C   
489  O  O   . THR   B 25  ? 0.5753 0.5862 0.7589 0.1348  0.1691  0.0636  34  THR   B O   
490  C  CB  . THR   B 25  ? 0.5858 0.6107 0.7916 0.1248  0.1768  0.0892  34  THR   B CB  
491  O  OG1 . THR   B 25  ? 0.5976 0.6187 0.8142 0.1181  0.1783  0.0981  34  THR   B OG1 
492  C  CG2 . THR   B 25  ? 0.5845 0.6266 0.7889 0.1297  0.1793  0.0964  34  THR   B CG2 
493  N  N   . GLN   B 26  ? 0.5704 0.5983 0.7444 0.1525  0.1739  0.0767  35  GLN   B N   
494  C  CA  . GLN   B 26  ? 0.5787 0.6055 0.7409 0.1579  0.1693  0.0672  35  GLN   B CA  
495  C  C   . GLN   B 26  ? 0.5875 0.6209 0.7519 0.1524  0.1682  0.0659  35  GLN   B C   
496  O  O   . GLN   B 26  ? 0.5820 0.6277 0.7466 0.1566  0.1715  0.0744  35  GLN   B O   
497  C  CB  . GLN   B 26  ? 0.5910 0.6222 0.7401 0.1732  0.1696  0.0700  35  GLN   B CB  
498  C  CG  . GLN   B 26  ? 0.5976 0.6239 0.7337 0.1783  0.1630  0.0596  35  GLN   B CG  
499  C  CD  . GLN   B 26  ? 0.5965 0.6240 0.7177 0.1938  0.1615  0.0607  35  GLN   B CD  
500  O  OE1 . GLN   B 26  ? 0.6242 0.6482 0.7425 0.1998  0.1623  0.0623  35  GLN   B OE1 
501  N  NE2 . GLN   B 26  ? 0.6048 0.6357 0.7151 0.2011  0.1586  0.0590  35  GLN   B NE2 
502  N  N   . VAL   B 27  ? 0.5713 0.5979 0.7372 0.1440  0.1640  0.0561  36  VAL   B N   
503  C  CA  . VAL   B 27  ? 0.5557 0.5876 0.7236 0.1381  0.1625  0.0537  36  VAL   B CA  
504  C  C   . VAL   B 27  ? 0.5263 0.5590 0.6805 0.1464  0.1583  0.0479  36  VAL   B C   
505  O  O   . VAL   B 27  ? 0.5300 0.5702 0.6824 0.1470  0.1583  0.0494  36  VAL   B O   
506  C  CB  . VAL   B 27  ? 0.5698 0.5941 0.7465 0.1249  0.1603  0.0469  36  VAL   B CB  
507  C  CG1 . VAL   B 27  ? 0.6039 0.6256 0.7923 0.1177  0.1635  0.0530  36  VAL   B CG1 
508  C  CG2 . VAL   B 27  ? 0.5558 0.5699 0.7276 0.1243  0.1559  0.0363  36  VAL   B CG2 
509  N  N   . GLY   B 28  ? 0.5107 0.5364 0.6547 0.1538  0.1547  0.0429  37  GLY   B N   
510  C  CA  . GLY   B 28  ? 0.4975 0.5219 0.6266 0.1633  0.1495  0.0384  37  GLY   B CA  
511  C  C   . GLY   B 28  ? 0.4951 0.5101 0.6152 0.1694  0.1446  0.0330  37  GLY   B C   
512  O  O   . GLY   B 28  ? 0.4988 0.5110 0.6231 0.1697  0.1471  0.0351  37  GLY   B O   
513  N  N   . VAL   B 29  ? 0.4836 0.4933 0.5928 0.1727  0.1372  0.0259  38  VAL   B N   
514  C  CA  . VAL   B 29  ? 0.4766 0.4774 0.5741 0.1798  0.1302  0.0207  38  VAL   B CA  
515  C  C   . VAL   B 29  ? 0.4715 0.4655 0.5670 0.1729  0.1221  0.0120  38  VAL   B C   
516  O  O   . VAL   B 29  ? 0.4633 0.4596 0.5607 0.1673  0.1214  0.0102  38  VAL   B O   
517  C  CB  . VAL   B 29  ? 0.4972 0.4989 0.5788 0.1953  0.1284  0.0236  38  VAL   B CB  
518  C  CG1 . VAL   B 29  ? 0.5096 0.5012 0.5785 0.2033  0.1204  0.0187  38  VAL   B CG1 
519  C  CG2 . VAL   B 29  ? 0.4931 0.5051 0.5769 0.2024  0.1371  0.0340  38  VAL   B CG2 
520  N  N   . GLY   B 30  ? 0.4684 0.4550 0.5610 0.1726  0.1160  0.0072  39  GLY   B N   
521  C  CA  . GLY   B 30  ? 0.4643 0.4446 0.5532 0.1677  0.1068  0.0002  39  GLY   B CA  
522  C  C   . GLY   B 30  ? 0.4697 0.4420 0.5491 0.1736  0.0984  -0.0026 39  GLY   B C   
523  O  O   . GLY   B 30  ? 0.4790 0.4507 0.5537 0.1827  0.1003  0.0005  39  GLY   B O   
524  N  N   . VAL   B 31  ? 0.4635 0.4301 0.5402 0.1685  0.0891  -0.0079 40  VAL   B N   
525  C  CA  . VAL   B 31  ? 0.4693 0.4267 0.5363 0.1721  0.0779  -0.0112 40  VAL   B CA  
526  C  C   . VAL   B 31  ? 0.4640 0.4226 0.5421 0.1606  0.0743  -0.0136 40  VAL   B C   
527  O  O   . VAL   B 31  ? 0.4459 0.4077 0.5319 0.1503  0.0741  -0.0155 40  VAL   B O   
528  C  CB  . VAL   B 31  ? 0.4810 0.4297 0.5334 0.1763  0.0679  -0.0145 40  VAL   B CB  
529  C  CG1 . VAL   B 31  ? 0.4930 0.4312 0.5373 0.1773  0.0548  -0.0179 40  VAL   B CG1 
530  C  CG2 . VAL   B 31  ? 0.4937 0.4416 0.5328 0.1894  0.0704  -0.0123 40  VAL   B CG2 
531  N  N   . MET   B 32  ? 0.4718 0.4296 0.5515 0.1624  0.0723  -0.0131 41  MET   B N   
532  C  CA  . MET   B 32  ? 0.4780 0.4383 0.5671 0.1533  0.0679  -0.0145 41  MET   B CA  
533  C  C   . MET   B 32  ? 0.4907 0.4422 0.5700 0.1542  0.0537  -0.0169 41  MET   B C   
534  O  O   . MET   B 32  ? 0.4979 0.4419 0.5652 0.1642  0.0488  -0.0169 41  MET   B O   
535  C  CB  . MET   B 32  ? 0.4926 0.4572 0.5885 0.1551  0.0728  -0.0122 41  MET   B CB  
536  C  CG  . MET   B 32  ? 0.5067 0.4775 0.6143 0.1458  0.0708  -0.0127 41  MET   B CG  
537  S  SD  . MET   B 32  ? 0.5272 0.5071 0.6492 0.1348  0.0793  -0.0132 41  MET   B SD  
538  C  CE  . MET   B 32  ? 0.5184 0.5007 0.6451 0.1395  0.0922  -0.0106 41  MET   B CE  
539  N  N   . GLN   B 33  ? 0.5086 0.4603 0.5923 0.1445  0.0469  -0.0185 42  GLN   B N   
540  C  CA  . GLN   B 33  ? 0.5387 0.4811 0.6142 0.1437  0.0318  -0.0202 42  GLN   B CA  
541  C  C   . GLN   B 33  ? 0.5346 0.4839 0.6230 0.1305  0.0276  -0.0194 42  GLN   B C   
542  O  O   . GLN   B 33  ? 0.5106 0.4670 0.6077 0.1230  0.0334  -0.0195 42  GLN   B O   
543  C  CB  . GLN   B 33  ? 0.5662 0.4968 0.6261 0.1488  0.0247  -0.0229 42  GLN   B CB  
544  C  CG  . GLN   B 33  ? 0.6061 0.5238 0.6551 0.1498  0.0080  -0.0246 42  GLN   B CG  
545  C  CD  . GLN   B 33  ? 0.6537 0.5570 0.6840 0.1575  0.0000  -0.0278 42  GLN   B CD  
546  O  OE1 . GLN   B 33  ? 0.6965 0.5918 0.7229 0.1519  -0.0106 -0.0295 42  GLN   B OE1 
547  N  NE2 . GLN   B 33  ? 0.6732 0.5730 0.6911 0.1710  0.0048  -0.0283 42  GLN   B NE2 
548  N  N   . GLU   B 34  ? 0.5599 0.5084 0.6499 0.1281  0.0182  -0.0181 43  GLU   B N   
549  C  CA  . GLU   B 34  ? 0.5702 0.5273 0.6729 0.1158  0.0132  -0.0157 43  GLU   B CA  
550  C  C   . GLU   B 34  ? 0.5443 0.5170 0.6625 0.1105  0.0266  -0.0141 43  GLU   B C   
551  O  O   . GLU   B 34  ? 0.5251 0.5051 0.6521 0.1013  0.0262  -0.0132 43  GLU   B O   
552  C  CB  . GLU   B 34  ? 0.6127 0.5623 0.7108 0.1096  0.0029  -0.0169 43  GLU   B CB  
553  C  CG  . GLU   B 34  ? 0.6606 0.5926 0.7424 0.1145  -0.0127 -0.0187 43  GLU   B CG  
554  C  CD  . GLU   B 34  ? 0.7101 0.6311 0.7839 0.1105  -0.0229 -0.0205 43  GLU   B CD  
555  O  OE1 . GLU   B 34  ? 0.7642 0.6907 0.8479 0.0989  -0.0279 -0.0179 43  GLU   B OE1 
556  O  OE2 . GLU   B 34  ? 0.7331 0.6404 0.7903 0.1195  -0.0257 -0.0242 43  GLU   B OE2 
557  N  N   . GLY   B 35  ? 0.5186 0.4957 0.6395 0.1165  0.0375  -0.0138 44  GLY   B N   
558  C  CA  . GLY   B 35  ? 0.4970 0.4869 0.6312 0.1123  0.0487  -0.0126 44  GLY   B CA  
559  C  C   . GLY   B 35  ? 0.4850 0.4762 0.6212 0.1098  0.0573  -0.0146 44  GLY   B C   
560  O  O   . GLY   B 35  ? 0.4744 0.4748 0.6206 0.1062  0.0657  -0.0142 44  GLY   B O   
561  N  N   . VAL   B 36  ? 0.4663 0.4485 0.5927 0.1124  0.0552  -0.0166 45  VAL   B N   
562  C  CA  . VAL   B 36  ? 0.4451 0.4283 0.5726 0.1101  0.0621  -0.0182 45  VAL   B CA  
563  C  C   . VAL   B 36  ? 0.4348 0.4125 0.5543 0.1194  0.0684  -0.0183 45  VAL   B C   
564  O  O   . VAL   B 36  ? 0.4454 0.4148 0.5530 0.1277  0.0631  -0.0183 45  VAL   B O   
565  C  CB  . VAL   B 36  ? 0.4625 0.4417 0.5859 0.1048  0.0539  -0.0197 45  VAL   B CB  
566  C  CG1 . VAL   B 36  ? 0.4602 0.4382 0.5810 0.1048  0.0594  -0.0215 45  VAL   B CG1 
567  C  CG2 . VAL   B 36  ? 0.4639 0.4518 0.5980 0.0944  0.0500  -0.0184 45  VAL   B CG2 
568  N  N   . PHE   B 37  ? 0.4082 0.3906 0.5337 0.1183  0.0788  -0.0179 46  PHE   B N   
569  C  CA  . PHE   B 37  ? 0.4056 0.3855 0.5261 0.1257  0.0856  -0.0163 46  PHE   B CA  
570  C  C   . PHE   B 37  ? 0.3977 0.3769 0.5148 0.1239  0.0859  -0.0174 46  PHE   B C   
571  O  O   . PHE   B 37  ? 0.3932 0.3768 0.5178 0.1158  0.0879  -0.0187 46  PHE   B O   
572  C  CB  . PHE   B 37  ? 0.3928 0.3775 0.5224 0.1252  0.0959  -0.0144 46  PHE   B CB  
573  C  CG  . PHE   B 37  ? 0.3932 0.3761 0.5182 0.1329  0.1018  -0.0111 46  PHE   B CG  
574  C  CD1 . PHE   B 37  ? 0.4014 0.3802 0.5173 0.1426  0.0996  -0.0092 46  PHE   B CD1 
575  C  CD2 . PHE   B 37  ? 0.3904 0.3765 0.5204 0.1304  0.1092  -0.0094 46  PHE   B CD2 
576  C  CE1 . PHE   B 37  ? 0.4141 0.3930 0.5259 0.1504  0.1053  -0.0052 46  PHE   B CE1 
577  C  CE2 . PHE   B 37  ? 0.3946 0.3809 0.5214 0.1371  0.1144  -0.0049 46  PHE   B CE2 
578  C  CZ  . PHE   B 37  ? 0.4091 0.3925 0.5270 0.1472  0.1129  -0.0025 46  PHE   B CZ  
579  N  N   . HIS   B 38  ? 0.4130 0.3871 0.5187 0.1323  0.0844  -0.0165 47  HIS   B N   
580  C  CA  . HIS   B 38  ? 0.4113 0.3841 0.5106 0.1333  0.0834  -0.0173 47  HIS   B CA  
581  C  C   . HIS   B 38  ? 0.4138 0.3906 0.5121 0.1398  0.0922  -0.0133 47  HIS   B C   
582  O  O   . HIS   B 38  ? 0.4133 0.3884 0.5054 0.1494  0.0936  -0.0106 47  HIS   B O   
583  C  CB  . HIS   B 38  ? 0.4234 0.3866 0.5078 0.1396  0.0726  -0.0193 47  HIS   B CB  
584  C  CG  . HIS   B 38  ? 0.4371 0.3954 0.5214 0.1339  0.0621  -0.0219 47  HIS   B CG  
585  N  ND1 . HIS   B 38  ? 0.4533 0.4107 0.5400 0.1339  0.0586  -0.0214 47  HIS   B ND1 
586  C  CD2 . HIS   B 38  ? 0.4485 0.4023 0.5299 0.1283  0.0534  -0.0243 47  HIS   B CD2 
587  C  CE1 . HIS   B 38  ? 0.4562 0.4101 0.5430 0.1278  0.0484  -0.0228 47  HIS   B CE1 
588  N  NE2 . HIS   B 38  ? 0.4575 0.4092 0.5418 0.1237  0.0452  -0.0245 47  HIS   B NE2 
589  N  N   . THR   B 39  ? 0.4146 0.3974 0.5194 0.1348  0.0981  -0.0124 48  THR   B N   
590  C  CA  . THR   B 39  ? 0.4285 0.4167 0.5333 0.1403  0.1060  -0.0072 48  THR   B CA  
591  C  C   . THR   B 39  ? 0.4393 0.4316 0.5443 0.1371  0.1070  -0.0074 48  THR   B C   
592  O  O   . THR   B 39  ? 0.4375 0.4267 0.5406 0.1319  0.1010  -0.0120 48  THR   B O   
593  C  CB  . THR   B 39  ? 0.4252 0.4175 0.5413 0.1376  0.1140  -0.0037 48  THR   B CB  
594  O  OG1 . THR   B 39  ? 0.4305 0.4282 0.5465 0.1434  0.1207  0.0026  48  THR   B OG1 
595  C  CG2 . THR   B 39  ? 0.4273 0.4228 0.5564 0.1258  0.1172  -0.0057 48  THR   B CG2 
596  N  N   . MET   B 40  ? 0.4556 0.4552 0.5631 0.1398  0.1141  -0.0021 49  MET   B N   
597  C  CA  . MET   B 40  ? 0.4648 0.4706 0.5751 0.1358  0.1164  -0.0014 49  MET   B CA  
598  C  C   . MET   B 40  ? 0.4631 0.4738 0.5891 0.1237  0.1217  -0.0012 49  MET   B C   
599  O  O   . MET   B 40  ? 0.4636 0.4754 0.5980 0.1215  0.1265  0.0015  49  MET   B O   
600  C  CB  . MET   B 40  ? 0.4713 0.4841 0.5757 0.1460  0.1207  0.0052  49  MET   B CB  
601  C  CG  . MET   B 40  ? 0.5022 0.5086 0.5891 0.1597  0.1150  0.0044  49  MET   B CG  
602  S  SD  . MET   B 40  ? 0.5604 0.5742 0.6350 0.1730  0.1168  0.0096  49  MET   B SD  
603  C  CE  . MET   B 40  ? 0.5435 0.5502 0.6095 0.1702  0.1082  0.0022  49  MET   B CE  
604  N  N   A TRP   B 41  ? 0.4606 0.4734 0.5899 0.1163  0.1204  -0.0043 50  TRP   B N   
605  N  N   B TRP   B 41  ? 0.4567 0.4695 0.5857 0.1166  0.1204  -0.0042 50  TRP   B N   
606  N  N   C TRP   B 41  ? 0.4606 0.4734 0.5899 0.1163  0.1204  -0.0043 50  TRP   B N   
607  N  N   D TRP   B 41  ? 0.4567 0.4695 0.5857 0.1166  0.1204  -0.0042 50  TRP   B N   
608  C  CA  A TRP   B 41  ? 0.4576 0.4739 0.6001 0.1050  0.1241  -0.0053 50  TRP   B CA  
609  C  CA  B TRP   B 41  ? 0.4508 0.4670 0.5929 0.1052  0.1239  -0.0053 50  TRP   B CA  
610  C  CA  C TRP   B 41  ? 0.4576 0.4739 0.6001 0.1050  0.1241  -0.0053 50  TRP   B CA  
611  C  CA  D TRP   B 41  ? 0.4508 0.4670 0.5929 0.1052  0.1239  -0.0053 50  TRP   B CA  
612  C  C   A TRP   B 41  ? 0.4561 0.4786 0.6069 0.1043  0.1313  0.0014  50  TRP   B C   
613  C  C   B TRP   B 41  ? 0.4520 0.4746 0.6028 0.1042  0.1312  0.0013  50  TRP   B C   
614  C  C   C TRP   B 41  ? 0.4561 0.4786 0.6069 0.1043  0.1313  0.0014  50  TRP   B C   
615  C  C   D TRP   B 41  ? 0.4520 0.4746 0.6028 0.1042  0.1312  0.0013  50  TRP   B C   
616  O  O   A TRP   B 41  ? 0.4534 0.4745 0.6138 0.0979  0.1341  0.0014  50  TRP   B O   
617  O  O   B TRP   B 41  ? 0.4489 0.4701 0.6093 0.0975  0.1339  0.0011  50  TRP   B O   
618  O  O   C TRP   B 41  ? 0.4534 0.4745 0.6138 0.0979  0.1341  0.0014  50  TRP   B O   
619  O  O   D TRP   B 41  ? 0.4489 0.4701 0.6093 0.0975  0.1339  0.0011  50  TRP   B O   
620  C  CB  A TRP   B 41  ? 0.4579 0.4765 0.6009 0.0990  0.1217  -0.0088 50  TRP   B CB  
621  C  CB  B TRP   B 41  ? 0.4461 0.4643 0.5883 0.0994  0.1212  -0.0091 50  TRP   B CB  
622  C  CB  C TRP   B 41  ? 0.4579 0.4765 0.6009 0.0990  0.1217  -0.0088 50  TRP   B CB  
623  C  CB  D TRP   B 41  ? 0.4461 0.4643 0.5883 0.0994  0.1212  -0.0091 50  TRP   B CB  
624  C  CG  A TRP   B 41  ? 0.4567 0.4772 0.6112 0.0880  0.1239  -0.0113 50  TRP   B CG  
625  C  CG  B TRP   B 41  ? 0.4400 0.4609 0.5942 0.0888  0.1242  -0.0107 50  TRP   B CG  
626  C  CG  C TRP   B 41  ? 0.4567 0.4772 0.6112 0.0880  0.1239  -0.0113 50  TRP   B CG  
627  C  CG  D TRP   B 41  ? 0.4400 0.4609 0.5942 0.0888  0.1242  -0.0107 50  TRP   B CG  
628  C  CD1 A TRP   B 41  ? 0.4570 0.4743 0.6146 0.0819  0.1210  -0.0168 50  TRP   B CD1 
629  C  CD1 B TRP   B 41  ? 0.4377 0.4645 0.5999 0.0846  0.1291  -0.0070 50  TRP   B CD1 
630  C  CD1 C TRP   B 41  ? 0.4570 0.4743 0.6146 0.0819  0.1210  -0.0168 50  TRP   B CD1 
631  C  CD1 D TRP   B 41  ? 0.4377 0.4645 0.5999 0.0846  0.1291  -0.0070 50  TRP   B CD1 
632  C  CD2 A TRP   B 41  ? 0.4575 0.4834 0.6216 0.0824  0.1289  -0.0083 50  TRP   B CD2 
633  C  CD2 B TRP   B 41  ? 0.4373 0.4549 0.5966 0.0817  0.1224  -0.0159 50  TRP   B CD2 
634  C  CD2 C TRP   B 41  ? 0.4575 0.4834 0.6216 0.0824  0.1289  -0.0083 50  TRP   B CD2 
635  C  CD2 D TRP   B 41  ? 0.4373 0.4549 0.5966 0.0817  0.1224  -0.0159 50  TRP   B CD2 
636  N  NE1 A TRP   B 41  ? 0.4556 0.4752 0.6225 0.0739  0.1241  -0.0180 50  TRP   B NE1 
637  N  NE1 B TRP   B 41  ? 0.4359 0.4616 0.6067 0.0755  0.1297  -0.0106 50  TRP   B NE1 
638  N  NE1 C TRP   B 41  ? 0.4556 0.4752 0.6225 0.0739  0.1241  -0.0180 50  TRP   B NE1 
639  N  NE1 D TRP   B 41  ? 0.4359 0.4616 0.6067 0.0755  0.1297  -0.0106 50  TRP   B NE1 
640  C  CE2 A TRP   B 41  ? 0.4598 0.4838 0.6309 0.0736  0.1284  -0.0132 50  TRP   B CE2 
641  C  CE2 B TRP   B 41  ? 0.4343 0.4548 0.6032 0.0742  0.1261  -0.0160 50  TRP   B CE2 
642  C  CE2 C TRP   B 41  ? 0.4598 0.4838 0.6309 0.0736  0.1284  -0.0132 50  TRP   B CE2 
643  C  CE2 D TRP   B 41  ? 0.4343 0.4548 0.6032 0.0742  0.1261  -0.0160 50  TRP   B CE2 
644  C  CE3 A TRP   B 41  ? 0.4653 0.4979 0.6330 0.0838  0.1334  -0.0015 50  TRP   B CE3 
645  C  CE3 B TRP   B 41  ? 0.4391 0.4524 0.5958 0.0811  0.1177  -0.0200 50  TRP   B CE3 
646  C  CE3 C TRP   B 41  ? 0.4653 0.4979 0.6330 0.0838  0.1334  -0.0015 50  TRP   B CE3 
647  C  CE3 D TRP   B 41  ? 0.4391 0.4524 0.5958 0.0811  0.1177  -0.0200 50  TRP   B CE3 
648  C  CZ2 A TRP   B 41  ? 0.4594 0.4857 0.6395 0.0665  0.1314  -0.0124 50  TRP   B CZ2 
649  C  CZ2 B TRP   B 41  ? 0.4304 0.4492 0.6047 0.0676  0.1255  -0.0207 50  TRP   B CZ2 
650  C  CZ2 C TRP   B 41  ? 0.4594 0.4857 0.6395 0.0665  0.1314  -0.0124 50  TRP   B CZ2 
651  C  CZ2 D TRP   B 41  ? 0.4304 0.4492 0.6047 0.0676  0.1255  -0.0207 50  TRP   B CZ2 
652  C  CZ3 A TRP   B 41  ? 0.4617 0.4977 0.6400 0.0756  0.1363  0.0001  50  TRP   B CZ3 
653  C  CZ3 B TRP   B 41  ? 0.4296 0.4434 0.5931 0.0742  0.1178  -0.0237 50  TRP   B CZ3 
654  C  CZ3 C TRP   B 41  ? 0.4617 0.4977 0.6400 0.0756  0.1363  0.0001  50  TRP   B CZ3 
655  C  CZ3 D TRP   B 41  ? 0.4296 0.4434 0.5931 0.0742  0.1178  -0.0237 50  TRP   B CZ3 
656  C  CH2 A TRP   B 41  ? 0.4590 0.4908 0.6429 0.0671  0.1349  -0.0057 50  TRP   B CH2 
657  C  CH2 B TRP   B 41  ? 0.4294 0.4455 0.6008 0.0681  0.1218  -0.0243 50  TRP   B CH2 
658  C  CH2 C TRP   B 41  ? 0.4590 0.4908 0.6429 0.0671  0.1349  -0.0057 50  TRP   B CH2 
659  C  CH2 D TRP   B 41  ? 0.4294 0.4455 0.6008 0.0681  0.1218  -0.0243 50  TRP   B CH2 
660  N  N   . HIS   B 42  ? 0.4533 0.4827 0.6007 0.1107  0.1339  0.0075  51  HIS   B N   
661  C  CA  . HIS   B 42  ? 0.4650 0.5023 0.6218 0.1089  0.1404  0.0156  51  HIS   B CA  
662  C  C   . HIS   B 42  ? 0.4833 0.5174 0.6437 0.1111  0.1434  0.0194  51  HIS   B C   
663  O  O   . HIS   B 42  ? 0.4744 0.5118 0.6450 0.1062  0.1477  0.0249  51  HIS   B O   
664  C  CB  . HIS   B 42  ? 0.4496 0.4975 0.6024 0.1158  0.1427  0.0224  51  HIS   B CB  
665  C  CG  . HIS   B 42  ? 0.4582 0.5076 0.6006 0.1292  0.1435  0.0269  51  HIS   B CG  
666  N  ND1 . HIS   B 42  ? 0.4522 0.4985 0.5792 0.1394  0.1388  0.0236  51  HIS   B ND1 
667  C  CD2 . HIS   B 42  ? 0.4640 0.5176 0.6085 0.1347  0.1482  0.0348  51  HIS   B CD2 
668  C  CE1 . HIS   B 42  ? 0.4642 0.5125 0.5835 0.1512  0.1405  0.0287  51  HIS   B CE1 
669  N  NE2 . HIS   B 42  ? 0.4617 0.5153 0.5921 0.1485  0.1467  0.0360  51  HIS   B NE2 
670  N  N   . VAL   B 43  ? 0.4768 0.5038 0.6294 0.1174  0.1407  0.0164  52  VAL   B N   
671  C  CA  . VAL   B 43  ? 0.4779 0.5018 0.6331 0.1202  0.1435  0.0198  52  VAL   B CA  
672  C  C   . VAL   B 43  ? 0.4696 0.4876 0.6347 0.1102  0.1439  0.0159  52  VAL   B C   
673  O  O   . VAL   B 43  ? 0.4775 0.4956 0.6507 0.1074  0.1479  0.0210  52  VAL   B O   
674  C  CB  . VAL   B 43  ? 0.4751 0.4937 0.6183 0.1306  0.1399  0.0177  52  VAL   B CB  
675  C  CG1 . VAL   B 43  ? 0.4790 0.4930 0.6250 0.1324  0.1419  0.0193  52  VAL   B CG1 
676  C  CG2 . VAL   B 43  ? 0.4792 0.5032 0.6119 0.1422  0.1403  0.0226  52  VAL   B CG2 
677  N  N   . THR   B 44  ? 0.4581 0.4713 0.6225 0.1053  0.1396  0.0078  53  THR   B N   
678  C  CA  . THR   B 44  ? 0.4500 0.4576 0.6215 0.0983  0.1397  0.0035  53  THR   B CA  
679  C  C   . THR   B 44  ? 0.4575 0.4662 0.6361 0.0884  0.1398  0.0006  53  THR   B C   
680  O  O   . THR   B 44  ? 0.4578 0.4618 0.6424 0.0833  0.1406  -0.0015 53  THR   B O   
681  C  CB  . THR   B 44  ? 0.4388 0.4418 0.6051 0.1004  0.1352  -0.0022 53  THR   B CB  
682  O  OG1 . THR   B 44  ? 0.4212 0.4258 0.5841 0.0976  0.1306  -0.0070 53  THR   B OG1 
683  C  CG2 . THR   B 44  ? 0.4365 0.4381 0.5948 0.1103  0.1342  0.0003  53  THR   B CG2 
684  N  N   . LYS   B 45  ? 0.4732 0.4875 0.6505 0.0867  0.1387  0.0005  54  LYS   B N   
685  C  CA  . LYS   B 45  ? 0.5156 0.5314 0.6980 0.0779  0.1377  -0.0032 54  LYS   B CA  
686  C  C   . LYS   B 45  ? 0.4908 0.5022 0.6728 0.0742  0.1345  -0.0109 54  LYS   B C   
687  O  O   . LYS   B 45  ? 0.5090 0.5198 0.6964 0.0673  0.1345  -0.0142 54  LYS   B O   
688  C  CB  . LYS   B 45  ? 0.5778 0.5933 0.7699 0.0713  0.1408  0.0000  54  LYS   B CB  
689  C  CG  . LYS   B 45  ? 0.6494 0.6709 0.8446 0.0737  0.1444  0.0095  54  LYS   B CG  
690  C  CD  . LYS   B 45  ? 0.7307 0.7615 0.9265 0.0722  0.1445  0.0121  54  LYS   B CD  
691  C  CE  . LYS   B 45  ? 0.8012 0.8397 1.0037 0.0720  0.1483  0.0227  54  LYS   B CE  
692  N  NZ  . LYS   B 45  ? 0.8637 0.9095 1.0590 0.0829  0.1504  0.0288  54  LYS   B NZ  
693  N  N   . GLY   B 46  ? 0.4854 0.4945 0.6616 0.0790  0.1317  -0.0132 55  GLY   B N   
694  C  CA  . GLY   B 46  ? 0.4801 0.4877 0.6564 0.0761  0.1285  -0.0191 55  GLY   B CA  
695  C  C   . GLY   B 46  ? 0.4850 0.4886 0.6655 0.0757  0.1305  -0.0202 55  GLY   B C   
696  O  O   . GLY   B 46  ? 0.5125 0.5167 0.6937 0.0738  0.1285  -0.0243 55  GLY   B O   
697  N  N   . ALA   B 47  ? 0.4719 0.4720 0.6550 0.0777  0.1342  -0.0163 56  ALA   B N   
698  C  CA  . ALA   B 47  ? 0.4754 0.4700 0.6614 0.0780  0.1359  -0.0175 56  ALA   B CA  
699  C  C   . ALA   B 47  ? 0.4759 0.4703 0.6581 0.0837  0.1342  -0.0185 56  ALA   B C   
700  O  O   . ALA   B 47  ? 0.4558 0.4518 0.6330 0.0887  0.1325  -0.0161 56  ALA   B O   
701  C  CB  . ALA   B 47  ? 0.4801 0.4704 0.6694 0.0789  0.1395  -0.0121 56  ALA   B CB  
702  N  N   . ALA   B 48  ? 0.4782 0.4700 0.6622 0.0840  0.1347  -0.0212 57  ALA   B N   
703  C  CA  . ALA   B 48  ? 0.5017 0.4936 0.6833 0.0896  0.1339  -0.0210 57  ALA   B CA  
704  C  C   . ALA   B 48  ? 0.5180 0.5059 0.6975 0.0955  0.1360  -0.0159 57  ALA   B C   
705  O  O   . ALA   B 48  ? 0.5307 0.5153 0.7121 0.0948  0.1391  -0.0122 57  ALA   B O   
706  C  CB  . ALA   B 48  ? 0.5117 0.5024 0.6955 0.0896  0.1347  -0.0245 57  ALA   B CB  
707  N  N   . LEU   B 49  ? 0.5211 0.5101 0.6971 0.1011  0.1342  -0.0153 58  LEU   B N   
708  C  CA  . LEU   B 49  ? 0.5357 0.5218 0.7085 0.1082  0.1358  -0.0107 58  LEU   B CA  
709  C  C   . LEU   B 49  ? 0.5691 0.5539 0.7418 0.1124  0.1358  -0.0115 58  LEU   B C   
710  O  O   . LEU   B 49  ? 0.5494 0.5385 0.7232 0.1109  0.1331  -0.0150 58  LEU   B O   
711  C  CB  . LEU   B 49  ? 0.5347 0.5234 0.7010 0.1123  0.1321  -0.0091 58  LEU   B CB  
712  C  CG  . LEU   B 49  ? 0.5116 0.5025 0.6761 0.1101  0.1316  -0.0081 58  LEU   B CG  
713  C  CD1 . LEU   B 49  ? 0.5156 0.5072 0.6716 0.1154  0.1265  -0.0080 58  LEU   B CD1 
714  C  CD2 . LEU   B 49  ? 0.5172 0.5071 0.6840 0.1109  0.1368  -0.0027 58  LEU   B CD2 
715  N  N   . ARG   B 50  ? 0.6132 0.5936 0.7847 0.1178  0.1387  -0.0076 59  ARG   B N   
716  C  CA  . ARG   B 50  ? 0.6305 0.6094 0.8010 0.1234  0.1391  -0.0074 59  ARG   B CA  
717  C  C   . ARG   B 50  ? 0.6140 0.5944 0.7789 0.1304  0.1370  -0.0044 59  ARG   B C   
718  O  O   . ARG   B 50  ? 0.5841 0.5635 0.7459 0.1329  0.1380  -0.0006 59  ARG   B O   
719  C  CB  . ARG   B 50  ? 0.6722 0.6432 0.8454 0.1239  0.1438  -0.0055 59  ARG   B CB  
720  C  CG  . ARG   B 50  ? 0.7513 0.7191 0.9229 0.1307  0.1452  -0.0042 59  ARG   B CG  
721  C  CD  . ARG   B 50  ? 0.7944 0.7522 0.9681 0.1301  0.1486  -0.0033 59  ARG   B CD  
722  N  NE  . ARG   B 50  ? 0.8061 0.7590 0.9824 0.1264  0.1508  0.0010  59  ARG   B NE  
723  C  CZ  . ARG   B 50  ? 0.8664 0.8173 1.0423 0.1297  0.1532  0.0079  59  ARG   B CZ  
724  N  NH1 . ARG   B 50  ? 0.8722 0.8245 1.0441 0.1375  0.1537  0.0103  59  ARG   B NH1 
725  N  NH2 . ARG   B 50  ? 0.8875 0.8358 1.0672 0.1253  0.1550  0.0128  59  ARG   B NH2 
726  N  N   . SER   B 51  ? 0.6234 0.6073 0.7867 0.1334  0.1334  -0.0059 60  SER   B N   
727  C  CA  . SER   B 51  ? 0.6641 0.6477 0.8219 0.1411  0.1312  -0.0033 60  SER   B CA  
728  C  C   . SER   B 51  ? 0.7038 0.6867 0.8632 0.1455  0.1334  -0.0028 60  SER   B C   
729  O  O   . SER   B 51  ? 0.6453 0.6337 0.8065 0.1451  0.1303  -0.0049 60  SER   B O   
730  C  CB  . SER   B 51  ? 0.6515 0.6396 0.8059 0.1406  0.1238  -0.0052 60  SER   B CB  
731  O  OG  . SER   B 51  ? 0.6862 0.6731 0.8350 0.1482  0.1209  -0.0032 60  SER   B OG  
732  N  N   . GLY   B 52  ? 0.7683 0.7453 0.9273 0.1497  0.1384  0.0005  61  GLY   B N   
733  C  CA  . GLY   B 52  ? 0.8117 0.7866 0.9717 0.1541  0.1407  0.0008  61  GLY   B CA  
734  C  C   . GLY   B 52  ? 0.8467 0.8206 1.0114 0.1494  0.1426  -0.0027 61  GLY   B C   
735  O  O   . GLY   B 52  ? 0.8848 0.8528 1.0516 0.1451  0.1453  -0.0026 61  GLY   B O   
736  N  N   . GLU   B 53  ? 0.9035 0.8836 1.0697 0.1500  0.1407  -0.0056 62  GLU   B N   
737  C  CA  . GLU   B 53  ? 0.9558 0.9362 1.1251 0.1465  0.1421  -0.0094 62  GLU   B CA  
738  C  C   . GLU   B 53  ? 0.8885 0.8797 1.0606 0.1411  0.1382  -0.0122 62  GLU   B C   
739  O  O   . GLU   B 53  ? 0.8637 0.8570 1.0380 0.1386  0.1391  -0.0154 62  GLU   B O   
740  C  CB  . GLU   B 53  ? 1.0522 1.0296 1.2204 0.1531  0.1447  -0.0096 62  GLU   B CB  
741  C  CG  . GLU   B 53  ? 1.1693 1.1335 1.3352 0.1561  0.1485  -0.0068 62  GLU   B CG  
742  C  CD  . GLU   B 53  ? 1.2324 1.1865 1.3971 0.1584  0.1511  -0.0088 62  GLU   B CD  
743  O  OE1 . GLU   B 53  ? 1.3513 1.3094 1.5147 0.1631  0.1511  -0.0112 62  GLU   B OE1 
744  O  OE2 . GLU   B 53  ? 1.2361 1.1783 1.4008 0.1555  0.1528  -0.0076 62  GLU   B OE2 
745  N  N   . GLY   B 54  ? 0.8154 0.8121 0.9869 0.1393  0.1336  -0.0111 63  GLY   B N   
746  C  CA  . GLY   B 54  ? 0.7853 0.7896 0.9593 0.1325  0.1295  -0.0130 63  GLY   B CA  
747  C  C   . GLY   B 54  ? 0.7471 0.7462 0.9214 0.1268  0.1312  -0.0147 63  GLY   B C   
748  O  O   . GLY   B 54  ? 0.7107 0.7014 0.8830 0.1281  0.1342  -0.0129 63  GLY   B O   
749  N  N   . ARG   B 55  ? 0.6879 0.6927 0.8650 0.1206  0.1292  -0.0172 64  ARG   B N   
750  C  CA  . ARG   B 55  ? 0.6799 0.6819 0.8577 0.1144  0.1299  -0.0191 64  ARG   B CA  
751  C  C   . ARG   B 55  ? 0.6309 0.6383 0.8079 0.1102  0.1243  -0.0191 64  ARG   B C   
752  O  O   . ARG   B 55  ? 0.6274 0.6433 0.8066 0.1085  0.1203  -0.0192 64  ARG   B O   
753  C  CB  . ARG   B 55  ? 0.6864 0.6897 0.8674 0.1112  0.1323  -0.0226 64  ARG   B CB  
754  C  CG  . ARG   B 55  ? 0.7201 0.7190 0.9019 0.1053  0.1335  -0.0246 64  ARG   B CG  
755  C  CD  . ARG   B 55  ? 0.7861 0.7896 0.9702 0.1022  0.1337  -0.0286 64  ARG   B CD  
756  N  NE  . ARG   B 55  ? 0.8399 0.8422 1.0251 0.0957  0.1335  -0.0308 64  ARG   B NE  
757  C  CZ  . ARG   B 55  ? 0.8788 0.8739 1.0642 0.0936  0.1357  -0.0334 64  ARG   B CZ  
758  N  NH1 . ARG   B 55  ? 0.8627 0.8492 1.0467 0.0974  0.1381  -0.0342 64  ARG   B NH1 
759  N  NH2 . ARG   B 55  ? 0.8911 0.8868 1.0778 0.0876  0.1349  -0.0352 64  ARG   B NH2 
760  N  N   . LEU   B 56  ? 0.5824 0.5854 0.7567 0.1084  0.1239  -0.0186 65  LEU   B N   
761  C  CA  . LEU   B 56  ? 0.5527 0.5585 0.7250 0.1044  0.1186  -0.0192 65  LEU   B CA  
762  C  C   . LEU   B 56  ? 0.5200 0.5269 0.6953 0.0979  0.1203  -0.0217 65  LEU   B C   
763  O  O   . LEU   B 56  ? 0.5259 0.5278 0.7015 0.0973  0.1245  -0.0215 65  LEU   B O   
764  C  CB  . LEU   B 56  ? 0.5662 0.5664 0.7320 0.1087  0.1174  -0.0168 65  LEU   B CB  
765  C  CG  . LEU   B 56  ? 0.6058 0.6038 0.7666 0.1159  0.1149  -0.0144 65  LEU   B CG  
766  C  CD1 . LEU   B 56  ? 0.5983 0.5930 0.7508 0.1189  0.1093  -0.0136 65  LEU   B CD1 
767  C  CD2 . LEU   B 56  ? 0.6203 0.6238 0.7840 0.1159  0.1112  -0.0147 65  LEU   B CD2 
768  N  N   . ASP   B 57  ? 0.4989 0.5126 0.6766 0.0929  0.1169  -0.0235 66  ASP   B N   
769  C  CA  . ASP   B 57  ? 0.4985 0.5134 0.6783 0.0869  0.1180  -0.0260 66  ASP   B CA  
770  C  C   . ASP   B 57  ? 0.4862 0.5008 0.6622 0.0842  0.1131  -0.0258 66  ASP   B C   
771  O  O   . ASP   B 57  ? 0.4763 0.4924 0.6496 0.0846  0.1070  -0.0246 66  ASP   B O   
772  C  CB  . ASP   B 57  ? 0.5398 0.5622 0.7243 0.0836  0.1185  -0.0282 66  ASP   B CB  
773  C  CG  . ASP   B 57  ? 0.5835 0.6030 0.7698 0.0865  0.1240  -0.0297 66  ASP   B CG  
774  O  OD1 . ASP   B 57  ? 0.6737 0.6861 0.8597 0.0854  0.1273  -0.0310 66  ASP   B OD1 
775  O  OD2 . ASP   B 57  ? 0.5821 0.6058 0.7697 0.0900  0.1244  -0.0292 66  ASP   B OD2 
776  N  N   . PRO   B 58  ? 0.4628 0.4752 0.6385 0.0813  0.1153  -0.0268 67  PRO   B N   
777  C  CA  . PRO   B 58  ? 0.4455 0.4574 0.6169 0.0794  0.1112  -0.0269 67  PRO   B CA  
778  C  C   . PRO   B 58  ? 0.4303 0.4479 0.6031 0.0746  0.1056  -0.0280 67  PRO   B C   
779  O  O   . PRO   B 58  ? 0.4425 0.4661 0.6208 0.0713  0.1070  -0.0292 67  PRO   B O   
780  C  CB  . PRO   B 58  ? 0.4496 0.4607 0.6229 0.0762  0.1155  -0.0278 67  PRO   B CB  
781  C  CG  . PRO   B 58  ? 0.4673 0.4779 0.6463 0.0750  0.1208  -0.0289 67  PRO   B CG  
782  C  CD  . PRO   B 58  ? 0.4683 0.4788 0.6479 0.0793  0.1211  -0.0282 67  PRO   B CD  
783  N  N   . TYR   B 59  ? 0.4064 0.4221 0.5738 0.0744  0.0988  -0.0273 68  TYR   B N   
784  C  CA  . TYR   B 59  ? 0.3853 0.4059 0.5543 0.0691  0.0924  -0.0273 68  TYR   B CA  
785  C  C   . TYR   B 59  ? 0.3637 0.3817 0.5284 0.0660  0.0893  -0.0285 68  TYR   B C   
786  O  O   . TYR   B 59  ? 0.3512 0.3746 0.5196 0.0601  0.0879  -0.0292 68  TYR   B O   
787  C  CB  . TYR   B 59  ? 0.3967 0.4161 0.5634 0.0711  0.0852  -0.0249 68  TYR   B CB  
788  C  CG  . TYR   B 59  ? 0.4008 0.4245 0.5693 0.0652  0.0770  -0.0233 68  TYR   B CG  
789  C  CD1 . TYR   B 59  ? 0.4044 0.4222 0.5665 0.0631  0.0701  -0.0238 68  TYR   B CD1 
790  C  CD2 . TYR   B 59  ? 0.4014 0.4350 0.5776 0.0623  0.0756  -0.0207 68  TYR   B CD2 
791  C  CE1 . TYR   B 59  ? 0.4162 0.4369 0.5802 0.0570  0.0615  -0.0216 68  TYR   B CE1 
792  C  CE2 . TYR   B 59  ? 0.4049 0.4437 0.5840 0.0562  0.0675  -0.0178 68  TYR   B CE2 
793  C  CZ  . TYR   B 59  ? 0.4199 0.4514 0.5929 0.0531  0.0601  -0.0181 68  TYR   B CZ  
794  O  OH  . TYR   B 59  ? 0.4251 0.4608 0.6013 0.0462  0.0514  -0.0146 68  TYR   B OH  
795  N  N   . TRP   B 60  ? 0.3512 0.3621 0.5083 0.0706  0.0889  -0.0285 69  TRP   B N   
796  C  CA  . TRP   B 60  ? 0.3517 0.3596 0.5030 0.0695  0.0857  -0.0295 69  TRP   B CA  
797  C  C   . TRP   B 60  ? 0.3510 0.3562 0.4985 0.0746  0.0912  -0.0292 69  TRP   B C   
798  O  O   . TRP   B 60  ? 0.3582 0.3598 0.5021 0.0813  0.0928  -0.0274 69  TRP   B O   
799  C  CB  . TRP   B 60  ? 0.3502 0.3514 0.4928 0.0707  0.0753  -0.0291 69  TRP   B CB  
800  C  CG  . TRP   B 60  ? 0.3556 0.3518 0.4898 0.0721  0.0726  -0.0303 69  TRP   B CG  
801  C  CD1 . TRP   B 60  ? 0.3569 0.3556 0.4924 0.0663  0.0711  -0.0315 69  TRP   B CD1 
802  C  CD2 . TRP   B 60  ? 0.3674 0.3559 0.4898 0.0808  0.0711  -0.0301 69  TRP   B CD2 
803  N  NE1 . TRP   B 60  ? 0.3589 0.3517 0.4845 0.0706  0.0688  -0.0323 69  TRP   B NE1 
804  C  CE2 . TRP   B 60  ? 0.3661 0.3528 0.4832 0.0798  0.0687  -0.0314 69  TRP   B CE2 
805  C  CE3 . TRP   B 60  ? 0.3720 0.3556 0.4874 0.0900  0.0718  -0.0289 69  TRP   B CE3 
806  C  CZ2 . TRP   B 60  ? 0.3772 0.3581 0.4824 0.0882  0.0675  -0.0314 69  TRP   B CZ2 
807  C  CZ3 . TRP   B 60  ? 0.3865 0.3647 0.4902 0.0983  0.0706  -0.0286 69  TRP   B CZ3 
808  C  CH2 . TRP   B 60  ? 0.3877 0.3646 0.4860 0.0977  0.0683  -0.0299 69  TRP   B CH2 
809  N  N   . GLY   B 61  ? 0.3651 0.3720 0.5123 0.0721  0.0930  -0.0301 70  GLY   B N   
810  C  CA  . GLY   B 61  ? 0.3733 0.3783 0.5151 0.0780  0.0962  -0.0285 70  GLY   B CA  
811  C  C   . GLY   B 61  ? 0.3697 0.3769 0.5098 0.0756  0.0963  -0.0294 70  GLY   B C   
812  O  O   . GLY   B 61  ? 0.3596 0.3703 0.5047 0.0684  0.0955  -0.0316 70  GLY   B O   
813  N  N   . ASP   B 62  ? 0.3915 0.3985 0.5259 0.0816  0.0984  -0.0272 71  ASP   B N   
814  C  CA  . ASP   B 62  ? 0.4100 0.4192 0.5403 0.0816  0.0979  -0.0274 71  ASP   B CA  
815  C  C   . ASP   B 62  ? 0.4030 0.4163 0.5318 0.0880  0.1036  -0.0231 71  ASP   B C   
816  O  O   . ASP   B 62  ? 0.4088 0.4187 0.5293 0.0973  0.1026  -0.0207 71  ASP   B O   
817  C  CB  . ASP   B 62  ? 0.4453 0.4473 0.5643 0.0843  0.0889  -0.0294 71  ASP   B CB  
818  C  CG  . ASP   B 62  ? 0.4793 0.4827 0.5932 0.0845  0.0876  -0.0301 71  ASP   B CG  
819  O  OD1 . ASP   B 62  ? 0.5305 0.5370 0.6407 0.0905  0.0911  -0.0277 71  ASP   B OD1 
820  O  OD2 . ASP   B 62  ? 0.5608 0.5626 0.6745 0.0789  0.0829  -0.0327 71  ASP   B OD2 
821  N  N   . VAL   B 63  ? 0.4074 0.4283 0.5448 0.0831  0.1093  -0.0217 72  VAL   B N   
822  C  CA  . VAL   B 63  ? 0.4168 0.4448 0.5564 0.0869  0.1154  -0.0161 72  VAL   B CA  
823  C  C   . VAL   B 63  ? 0.4343 0.4637 0.5623 0.0956  0.1132  -0.0142 72  VAL   B C   
824  O  O   . VAL   B 63  ? 0.4348 0.4690 0.5596 0.1038  0.1168  -0.0085 72  VAL   B O   
825  C  CB  . VAL   B 63  ? 0.4123 0.4473 0.5642 0.0779  0.1201  -0.0154 72  VAL   B CB  
826  C  CG1 . VAL   B 63  ? 0.4108 0.4550 0.5640 0.0803  0.1241  -0.0097 72  VAL   B CG1 
827  C  CG2 . VAL   B 63  ? 0.4194 0.4529 0.5812 0.0730  0.1237  -0.0150 72  VAL   B CG2 
828  N  N   . LYS   B 64  ? 0.4615 0.4868 0.5820 0.0952  0.1073  -0.0183 73  LYS   B N   
829  C  CA  . LYS   B 64  ? 0.4618 0.4876 0.5696 0.1047  0.1050  -0.0168 73  LYS   B CA  
830  C  C   . LYS   B 64  ? 0.4784 0.4957 0.5719 0.1167  0.1005  -0.0164 73  LYS   B C   
831  O  O   . LYS   B 64  ? 0.4735 0.4945 0.5581 0.1275  0.1020  -0.0126 73  LYS   B O   
832  C  CB  . LYS   B 64  ? 0.4687 0.4912 0.5714 0.1015  0.0994  -0.0211 73  LYS   B CB  
833  C  CG  . LYS   B 64  ? 0.4902 0.5126 0.5786 0.1124  0.0970  -0.0197 73  LYS   B CG  
834  C  CD  . LYS   B 64  ? 0.4953 0.5182 0.5814 0.1088  0.0940  -0.0224 73  LYS   B CD  
835  C  CE  . LYS   B 64  ? 0.5268 0.5505 0.5982 0.1212  0.0924  -0.0205 73  LYS   B CE  
836  N  NZ  . LYS   B 64  ? 0.5353 0.5554 0.6017 0.1181  0.0873  -0.0242 73  LYS   B NZ  
837  N  N   . GLN   B 65  ? 0.4846 0.4915 0.5754 0.1152  0.0945  -0.0201 74  GLN   B N   
838  C  CA  . GLN   B 65  ? 0.4955 0.4929 0.5736 0.1254  0.0893  -0.0203 74  GLN   B CA  
839  C  C   . GLN   B 65  ? 0.4715 0.4742 0.5543 0.1301  0.0962  -0.0154 74  GLN   B C   
840  O  O   . GLN   B 65  ? 0.4773 0.4755 0.5490 0.1411  0.0940  -0.0141 74  GLN   B O   
841  C  CB  . GLN   B 65  ? 0.5244 0.5109 0.6010 0.1204  0.0807  -0.0248 74  GLN   B CB  
842  C  CG  . GLN   B 65  ? 0.5676 0.5462 0.6364 0.1177  0.0717  -0.0288 74  GLN   B CG  
843  C  CD  . GLN   B 65  ? 0.5937 0.5639 0.6639 0.1113  0.0635  -0.0316 74  GLN   B CD  
844  O  OE1 . GLN   B 65  ? 0.6343 0.5963 0.6979 0.1162  0.0581  -0.0318 74  GLN   B OE1 
845  N  NE2 . GLN   B 65  ? 0.6041 0.5771 0.6836 0.1001  0.0624  -0.0331 74  GLN   B NE2 
846  N  N   . ASP   B 66  ? 0.4426 0.4534 0.5410 0.1215  0.1035  -0.0133 75  ASP   B N   
847  C  CA  . ASP   B 66  ? 0.4248 0.4408 0.5315 0.1224  0.1106  -0.0084 75  ASP   B CA  
848  C  C   . ASP   B 66  ? 0.4132 0.4205 0.5167 0.1248  0.1069  -0.0104 75  ASP   B C   
849  O  O   . ASP   B 66  ? 0.4118 0.4194 0.5108 0.1337  0.1090  -0.0066 75  ASP   B O   
850  C  CB  . ASP   B 66  ? 0.4243 0.4485 0.5269 0.1325  0.1158  -0.0014 75  ASP   B CB  
851  C  CG  . ASP   B 66  ? 0.4188 0.4491 0.5315 0.1319  0.1231  0.0047  75  ASP   B CG  
852  O  OD1 . ASP   B 66  ? 0.4060 0.4378 0.5318 0.1216  0.1263  0.0043  75  ASP   B OD1 
853  O  OD2 . ASP   B 66  ? 0.4361 0.4691 0.5420 0.1429  0.1253  0.0099  75  ASP   B OD2 
854  N  N   . LEU   B 67  ? 0.4058 0.4069 0.5113 0.1176  0.1013  -0.0157 76  LEU   B N   
855  C  CA  . LEU   B 67  ? 0.4027 0.3964 0.5061 0.1186  0.0966  -0.0176 76  LEU   B CA  
856  C  C   . LEU   B 67  ? 0.3931 0.3887 0.5095 0.1081  0.0983  -0.0196 76  LEU   B C   
857  O  O   . LEU   B 67  ? 0.3816 0.3815 0.5057 0.0993  0.0998  -0.0215 76  LEU   B O   
858  C  CB  . LEU   B 67  ? 0.4149 0.3987 0.5051 0.1223  0.0860  -0.0212 76  LEU   B CB  
859  C  CG  . LEU   B 67  ? 0.4212 0.3999 0.4948 0.1360  0.0826  -0.0199 76  LEU   B CG  
860  C  CD1 . LEU   B 67  ? 0.4346 0.4004 0.4957 0.1377  0.0703  -0.0243 76  LEU   B CD1 
861  C  CD2 . LEU   B 67  ? 0.4262 0.4051 0.4965 0.1455  0.0860  -0.0164 76  LEU   B CD2 
862  N  N   . VAL   B 68  ? 0.3985 0.3915 0.5167 0.1094  0.0978  -0.0193 77  VAL   B N   
863  C  CA  . VAL   B 68  ? 0.3871 0.3824 0.5164 0.1012  0.0993  -0.0210 77  VAL   B CA  
864  C  C   . VAL   B 68  ? 0.3743 0.3651 0.5010 0.1041  0.0944  -0.0214 77  VAL   B C   
865  O  O   . VAL   B 68  ? 0.3797 0.3669 0.4995 0.1126  0.0941  -0.0193 77  VAL   B O   
866  C  CB  . VAL   B 68  ? 0.3853 0.3860 0.5252 0.0980  0.1083  -0.0189 77  VAL   B CB  
867  C  CG1 . VAL   B 68  ? 0.3964 0.3968 0.5343 0.1058  0.1129  -0.0143 77  VAL   B CG1 
868  C  CG2 . VAL   B 68  ? 0.3847 0.3870 0.5338 0.0913  0.1094  -0.0212 77  VAL   B CG2 
869  N  N   . SER   B 69  ? 0.3662 0.3580 0.4978 0.0975  0.0903  -0.0235 78  SER   B N   
870  C  CA  . SER   B 69  ? 0.3752 0.3649 0.5065 0.0987  0.0853  -0.0234 78  SER   B CA  
871  C  C   . SER   B 69  ? 0.3650 0.3613 0.5079 0.0939  0.0907  -0.0232 78  SER   B C   
872  O  O   . SER   B 69  ? 0.3527 0.3545 0.5031 0.0872  0.0942  -0.0246 78  SER   B O   
873  C  CB  . SER   B 69  ? 0.3805 0.3664 0.5073 0.0955  0.0744  -0.0247 78  SER   B CB  
874  O  OG  . SER   B 69  ? 0.3790 0.3717 0.5149 0.0860  0.0740  -0.0256 78  SER   B OG  
875  N  N   A TYR   B 70  ? 0.3692 0.3650 0.5130 0.0979  0.0912  -0.0218 79  TYR   B N   
876  N  N   B TYR   B 70  ? 0.3692 0.3650 0.5130 0.0979  0.0912  -0.0218 79  TYR   B N   
877  N  N   C TYR   B 70  ? 0.3699 0.3656 0.5134 0.0978  0.0907  -0.0218 79  TYR   B N   
878  N  N   D TYR   B 70  ? 0.3699 0.3656 0.5134 0.0978  0.0907  -0.0218 79  TYR   B N   
879  C  CA  A TYR   B 70  ? 0.3643 0.3658 0.5174 0.0953  0.0957  -0.0215 79  TYR   B CA  
880  C  CA  B TYR   B 70  ? 0.3643 0.3658 0.5174 0.0953  0.0957  -0.0215 79  TYR   B CA  
881  C  CA  C TYR   B 70  ? 0.3657 0.3668 0.5184 0.0958  0.0957  -0.0214 79  TYR   B CA  
882  C  CA  D TYR   B 70  ? 0.3657 0.3668 0.5184 0.0958  0.0957  -0.0214 79  TYR   B CA  
883  C  C   A TYR   B 70  ? 0.3657 0.3697 0.5201 0.0946  0.0892  -0.0208 79  TYR   B C   
884  C  C   B TYR   B 70  ? 0.3657 0.3697 0.5201 0.0946  0.0892  -0.0208 79  TYR   B C   
885  C  C   C TYR   B 70  ? 0.3684 0.3724 0.5228 0.0946  0.0893  -0.0207 79  TYR   B C   
886  C  C   D TYR   B 70  ? 0.3684 0.3724 0.5228 0.0946  0.0893  -0.0207 79  TYR   B C   
887  O  O   A TYR   B 70  ? 0.3728 0.3716 0.5202 0.0993  0.0832  -0.0197 79  TYR   B O   
888  O  O   B TYR   B 70  ? 0.3728 0.3716 0.5202 0.0993  0.0832  -0.0197 79  TYR   B O   
889  O  O   C TYR   B 70  ? 0.3755 0.3747 0.5235 0.0995  0.0836  -0.0196 79  TYR   B O   
890  O  O   D TYR   B 70  ? 0.3755 0.3747 0.5235 0.0995  0.0836  -0.0196 79  TYR   B O   
891  C  CB  A TYR   B 70  ? 0.3684 0.3678 0.5222 0.1009  0.1030  -0.0197 79  TYR   B CB  
892  C  CB  B TYR   B 70  ? 0.3684 0.3678 0.5222 0.1009  0.1030  -0.0197 79  TYR   B CB  
893  C  CB  C TYR   B 70  ? 0.3694 0.3678 0.5215 0.1022  0.1023  -0.0194 79  TYR   B CB  
894  C  CB  D TYR   B 70  ? 0.3694 0.3678 0.5215 0.1022  0.1023  -0.0194 79  TYR   B CB  
895  C  CG  A TYR   B 70  ? 0.3668 0.3660 0.5232 0.0996  0.1099  -0.0194 79  TYR   B CG  
896  C  CG  B TYR   B 70  ? 0.3668 0.3660 0.5232 0.0996  0.1099  -0.0194 79  TYR   B CG  
897  C  CG  C TYR   B 70  ? 0.3675 0.3653 0.5213 0.1017  0.1092  -0.0188 79  TYR   B CG  
898  C  CG  D TYR   B 70  ? 0.3675 0.3653 0.5213 0.1017  0.1092  -0.0188 79  TYR   B CG  
899  C  CD1 A TYR   B 70  ? 0.3705 0.3674 0.5212 0.1022  0.1101  -0.0181 79  TYR   B CD1 
900  C  CD1 B TYR   B 70  ? 0.3705 0.3674 0.5212 0.1022  0.1101  -0.0181 79  TYR   B CD1 
901  C  CD1 C TYR   B 70  ? 0.3717 0.3674 0.5193 0.1043  0.1088  -0.0177 79  TYR   B CD1 
902  C  CD1 D TYR   B 70  ? 0.3717 0.3674 0.5193 0.1043  0.1088  -0.0177 79  TYR   B CD1 
903  C  CD2 A TYR   B 70  ? 0.3665 0.3677 0.5305 0.0959  0.1158  -0.0202 79  TYR   B CD2 
904  C  CD2 B TYR   B 70  ? 0.3665 0.3677 0.5305 0.0959  0.1158  -0.0202 79  TYR   B CD2 
905  C  CD2 C TYR   B 70  ? 0.3672 0.3666 0.5285 0.0990  0.1157  -0.0189 79  TYR   B CD2 
906  C  CD2 D TYR   B 70  ? 0.3672 0.3666 0.5285 0.0990  0.1157  -0.0189 79  TYR   B CD2 
907  C  CE1 A TYR   B 70  ? 0.3689 0.3671 0.5230 0.1004  0.1161  -0.0168 79  TYR   B CE1 
908  C  CE1 B TYR   B 70  ? 0.3689 0.3671 0.5230 0.1004  0.1161  -0.0168 79  TYR   B CE1 
909  C  CE1 C TYR   B 70  ? 0.3703 0.3674 0.5208 0.1033  0.1149  -0.0160 79  TYR   B CE1 
910  C  CE1 D TYR   B 70  ? 0.3703 0.3674 0.5208 0.1033  0.1149  -0.0160 79  TYR   B CE1 
911  C  CE2 A TYR   B 70  ? 0.3639 0.3642 0.5307 0.0937  0.1209  -0.0195 79  TYR   B CE2 
912  C  CE2 B TYR   B 70  ? 0.3639 0.3642 0.5307 0.0937  0.1209  -0.0195 79  TYR   B CE2 
913  C  CE2 C TYR   B 70  ? 0.3653 0.3640 0.5291 0.0974  0.1209  -0.0177 79  TYR   B CE2 
914  C  CE2 D TYR   B 70  ? 0.3653 0.3640 0.5291 0.0974  0.1209  -0.0177 79  TYR   B CE2 
915  C  CZ  A TYR   B 70  ? 0.3635 0.3631 0.5261 0.0955  0.1211  -0.0174 79  TYR   B CZ  
916  C  CZ  B TYR   B 70  ? 0.3635 0.3631 0.5261 0.0955  0.1211  -0.0174 79  TYR   B CZ  
917  C  CZ  C TYR   B 70  ? 0.3656 0.3641 0.5248 0.0991  0.1207  -0.0158 79  TYR   B CZ  
918  C  CZ  D TYR   B 70  ? 0.3656 0.3641 0.5248 0.0991  0.1207  -0.0158 79  TYR   B CZ  
919  O  OH  A TYR   B 70  ? 0.3623 0.3625 0.5287 0.0929  0.1258  -0.0157 79  TYR   B OH  
920  O  OH  B TYR   B 70  ? 0.3623 0.3625 0.5287 0.0929  0.1258  -0.0157 79  TYR   B OH  
921  O  OH  C TYR   B 70  ? 0.3651 0.3646 0.5281 0.0970  0.1257  -0.0136 79  TYR   B OH  
922  O  OH  D TYR   B 70  ? 0.3651 0.3646 0.5281 0.0970  0.1257  -0.0136 79  TYR   B OH  
923  N  N   A CYS   B 71  ? 0.3599 0.3722 0.5228 0.0891  0.0901  -0.0209 80  CYS   B N   
924  N  N   B CYS   B 71  ? 0.3599 0.3722 0.5228 0.0891  0.0901  -0.0209 80  CYS   B N   
925  N  N   C CYS   B 71  ? 0.3643 0.3767 0.5273 0.0887  0.0901  -0.0211 80  CYS   B N   
926  N  N   D CYS   B 71  ? 0.3643 0.3767 0.5273 0.0887  0.0901  -0.0211 80  CYS   B N   
927  C  CA  A CYS   B 71  ? 0.3599 0.3786 0.5271 0.0877  0.0853  -0.0189 80  CYS   B CA  
928  C  CA  B CYS   B 71  ? 0.3599 0.3786 0.5271 0.0877  0.0853  -0.0189 80  CYS   B CA  
929  C  CA  C CYS   B 71  ? 0.3653 0.3846 0.5331 0.0871  0.0858  -0.0191 80  CYS   B CA  
930  C  CA  D CYS   B 71  ? 0.3653 0.3846 0.5331 0.0871  0.0858  -0.0191 80  CYS   B CA  
931  C  C   A CYS   B 71  ? 0.3601 0.3811 0.5273 0.0815  0.0759  -0.0180 80  CYS   B C   
932  C  C   B CYS   B 71  ? 0.3601 0.3811 0.5273 0.0815  0.0759  -0.0180 80  CYS   B C   
933  C  C   C CYS   B 71  ? 0.3653 0.3847 0.5311 0.0827  0.0751  -0.0178 80  CYS   B C   
934  C  C   D CYS   B 71  ? 0.3653 0.3847 0.5311 0.0827  0.0751  -0.0178 80  CYS   B C   
935  O  O   A CYS   B 71  ? 0.3572 0.3877 0.5314 0.0773  0.0729  -0.0155 80  CYS   B O   
936  O  O   B CYS   B 71  ? 0.3572 0.3877 0.5314 0.0773  0.0729  -0.0155 80  CYS   B O   
937  O  O   C CYS   B 71  ? 0.3660 0.3906 0.5353 0.0814  0.0698  -0.0151 80  CYS   B O   
938  O  O   D CYS   B 71  ? 0.3660 0.3906 0.5353 0.0814  0.0698  -0.0151 80  CYS   B O   
939  C  CB  A CYS   B 71  ? 0.3682 0.3823 0.5308 0.0948  0.0830  -0.0172 80  CYS   B CB  
940  C  CB  B CYS   B 71  ? 0.3682 0.3823 0.5308 0.0948  0.0830  -0.0172 80  CYS   B CB  
941  C  CB  C CYS   B 71  ? 0.3756 0.3925 0.5413 0.0940  0.0862  -0.0174 80  CYS   B CB  
942  C  CB  D CYS   B 71  ? 0.3756 0.3925 0.5413 0.0940  0.0862  -0.0174 80  CYS   B CB  
943  S  SG  A CYS   B 71  ? 0.3695 0.3799 0.5315 0.1024  0.0932  -0.0171 80  CYS   B SG  
944  S  SG  B CYS   B 71  ? 0.3695 0.3799 0.5315 0.1024  0.0932  -0.0171 80  CYS   B SG  
945  S  SG  C CYS   B 71  ? 0.3811 0.3980 0.5503 0.0988  0.0975  -0.0179 80  CYS   B SG  
946  S  SG  D CYS   B 71  ? 0.3811 0.3980 0.5503 0.0988  0.0975  -0.0179 80  CYS   B SG  
947  N  N   . GLY   B 72  ? 0.3639 0.3769 0.5236 0.0809  0.0714  -0.0194 81  GLY   B N   
948  C  CA  . GLY   B 72  ? 0.3659 0.3777 0.5237 0.0756  0.0607  -0.0183 81  GLY   B CA  
949  C  C   . GLY   B 72  ? 0.3688 0.3713 0.5175 0.0765  0.0585  -0.0208 81  GLY   B C   
950  O  O   . GLY   B 72  ? 0.3720 0.3709 0.5168 0.0812  0.0653  -0.0226 81  GLY   B O   
951  N  N   . PRO   B 73  ? 0.3811 0.3799 0.5263 0.0720  0.0487  -0.0203 82  PRO   B N   
952  C  CA  . PRO   B 73  ? 0.3953 0.3847 0.5306 0.0734  0.0456  -0.0227 82  PRO   B CA  
953  C  C   . PRO   B 73  ? 0.4244 0.4010 0.5458 0.0835  0.0421  -0.0240 82  PRO   B C   
954  O  O   . PRO   B 73  ? 0.4496 0.4228 0.5683 0.0877  0.0381  -0.0228 82  PRO   B O   
955  C  CB  . PRO   B 73  ? 0.3924 0.3802 0.5278 0.0659  0.0343  -0.0211 82  PRO   B CB  
956  C  CG  . PRO   B 73  ? 0.3952 0.3884 0.5375 0.0626  0.0286  -0.0172 82  PRO   B CG  
957  C  CD  . PRO   B 73  ? 0.3858 0.3898 0.5370 0.0650  0.0399  -0.0168 82  PRO   B CD  
958  N  N   . TRP   B 74  ? 0.4369 0.4067 0.5488 0.0876  0.0424  -0.0261 83  TRP   B N   
959  C  CA  . TRP   B 74  ? 0.4612 0.4195 0.5579 0.0986  0.0392  -0.0273 83  TRP   B CA  
960  C  C   . TRP   B 74  ? 0.4944 0.4413 0.5819 0.1003  0.0249  -0.0273 83  TRP   B C   
961  O  O   . TRP   B 74  ? 0.4937 0.4368 0.5807 0.0936  0.0156  -0.0273 83  TRP   B O   
962  C  CB  . TRP   B 74  ? 0.4527 0.4079 0.5418 0.1015  0.0411  -0.0291 83  TRP   B CB  
963  C  CG  . TRP   B 74  ? 0.4527 0.3998 0.5270 0.1144  0.0409  -0.0296 83  TRP   B CG  
964  C  CD1 . TRP   B 74  ? 0.4659 0.3993 0.5236 0.1218  0.0301  -0.0313 83  TRP   B CD1 
965  C  CD2 . TRP   B 74  ? 0.4479 0.4002 0.5218 0.1222  0.0515  -0.0279 83  TRP   B CD2 
966  N  NE1 . TRP   B 74  ? 0.4763 0.4070 0.5228 0.1346  0.0338  -0.0310 83  TRP   B NE1 
967  C  CE2 . TRP   B 74  ? 0.4593 0.4022 0.5163 0.1347  0.0470  -0.0284 83  TRP   B CE2 
968  C  CE3 . TRP   B 74  ? 0.4329 0.3963 0.5190 0.1200  0.0638  -0.0257 83  TRP   B CE3 
969  C  CZ2 . TRP   B 74  ? 0.4603 0.4069 0.5130 0.1450  0.0550  -0.0259 83  TRP   B CZ2 
970  C  CZ3 . TRP   B 74  ? 0.4281 0.3937 0.5104 0.1290  0.0709  -0.0232 83  TRP   B CZ3 
971  C  CH2 . TRP   B 74  ? 0.4454 0.4038 0.5118 0.1413  0.0669  -0.0228 83  TRP   B CH2 
972  N  N   . LYS   B 75  ? 0.5235 0.4641 0.6029 0.1095  0.0228  -0.0273 84  LYS   B N   
973  C  CA  . LYS   B 75  ? 0.5502 0.4797 0.6212 0.1116  0.0090  -0.0273 84  LYS   B CA  
974  C  C   . LYS   B 75  ? 0.5795 0.4926 0.6296 0.1233  0.0012  -0.0301 84  LYS   B C   
975  O  O   . LYS   B 75  ? 0.6202 0.5208 0.6610 0.1242  -0.0127 -0.0310 84  LYS   B O   
976  C  CB  . LYS   B 75  ? 0.5599 0.4943 0.6362 0.1144  0.0121  -0.0253 84  LYS   B CB  
977  C  CG  . LYS   B 75  ? 0.5465 0.4964 0.6415 0.1048  0.0188  -0.0225 84  LYS   B CG  
978  C  CD  . LYS   B 75  ? 0.5501 0.5016 0.6515 0.0944  0.0079  -0.0203 84  LYS   B CD  
979  C  CE  . LYS   B 75  ? 0.5389 0.5066 0.6573 0.0843  0.0150  -0.0179 84  LYS   B CE  
980  N  NZ  . LYS   B 75  ? 0.5416 0.5177 0.6700 0.0787  0.0100  -0.0137 84  LYS   B NZ  
981  N  N   . LEU   B 76  ? 0.5854 0.4988 0.6280 0.1325  0.0095  -0.0312 85  LEU   B N   
982  C  CA  . LEU   B 76  ? 0.6046 0.5051 0.6265 0.1473  0.0047  -0.0332 85  LEU   B CA  
983  C  C   . LEU   B 76  ? 0.6275 0.5174 0.6374 0.1480  -0.0036 -0.0360 85  LEU   B C   
984  O  O   . LEU   B 76  ? 0.5934 0.4907 0.6075 0.1457  0.0041  -0.0358 85  LEU   B O   
985  C  CB  . LEU   B 76  ? 0.5943 0.5039 0.6162 0.1566  0.0188  -0.0313 85  LEU   B CB  
986  C  CG  . LEU   B 76  ? 0.5874 0.5087 0.6236 0.1542  0.0288  -0.0282 85  LEU   B CG  
987  C  CD1 . LEU   B 76  ? 0.5831 0.5128 0.6197 0.1625  0.0419  -0.0254 85  LEU   B CD1 
988  C  CD2 . LEU   B 76  ? 0.6006 0.5152 0.6327 0.1574  0.0208  -0.0283 85  LEU   B CD2 
989  N  N   . ASP   B 77  ? 0.6767 0.5493 0.6724 0.1506  -0.0195 -0.0384 86  ASP   B N   
990  C  CA  . ASP   B 77  ? 0.7304 0.5903 0.7137 0.1509  -0.0294 -0.0412 86  ASP   B CA  
991  C  C   . ASP   B 77  ? 0.7359 0.5778 0.6930 0.1679  -0.0381 -0.0447 86  ASP   B C   
992  O  O   . ASP   B 77  ? 0.7504 0.5799 0.6948 0.1700  -0.0469 -0.0473 86  ASP   B O   
993  C  CB  . ASP   B 77  ? 0.7794 0.6330 0.7688 0.1369  -0.0423 -0.0407 86  ASP   B CB  
994  C  CG  . ASP   B 77  ? 0.8542 0.6995 0.8430 0.1342  -0.0548 -0.0399 86  ASP   B CG  
995  O  OD1 . ASP   B 77  ? 0.9070 0.7503 0.8898 0.1437  -0.0538 -0.0403 86  ASP   B OD1 
996  O  OD2 . ASP   B 77  ? 0.9417 0.7835 0.9369 0.1222  -0.0655 -0.0381 86  ASP   B OD2 
997  N  N   . ALA   B 78  ? 0.7197 0.5603 0.6679 0.1808  -0.0356 -0.0447 87  ALA   B N   
998  C  CA  . ALA   B 78  ? 0.7198 0.5433 0.6414 0.1986  -0.0444 -0.0482 87  ALA   B CA  
999  C  C   . ALA   B 78  ? 0.7053 0.5349 0.6195 0.2082  -0.0348 -0.0481 87  ALA   B C   
1000 O  O   . ALA   B 78  ? 0.6581 0.5069 0.5890 0.2023  -0.0196 -0.0446 87  ALA   B O   
1001 C  CB  . ALA   B 78  ? 0.7419 0.5634 0.6569 0.2093  -0.0445 -0.0478 87  ALA   B CB  
1002 N  N   . ALA   B 79  ? 0.7023 0.5150 0.5918 0.2221  -0.0447 -0.0518 88  ALA   B N   
1003 C  CA  . ALA   B 79  ? 0.7048 0.5190 0.5824 0.2324  -0.0401 -0.0524 88  ALA   B CA  
1004 C  C   . ALA   B 79  ? 0.7103 0.5161 0.5624 0.2557  -0.0425 -0.0539 88  ALA   B C   
1005 O  O   . ALA   B 79  ? 0.7089 0.4964 0.5451 0.2628  -0.0558 -0.0574 88  ALA   B O   
1006 C  CB  . ALA   B 79  ? 0.7140 0.5135 0.5850 0.2257  -0.0526 -0.0559 88  ALA   B CB  
1007 N  N   . TRP   B 80  ? 0.7189 0.5389 0.5677 0.2674  -0.0296 -0.0507 89  TRP   B N   
1008 C  CA  . TRP   B 80  ? 0.7616 0.5745 0.5835 0.2914  -0.0320 -0.0518 89  TRP   B CA  
1009 C  C   . TRP   B 80  ? 0.8035 0.5907 0.6017 0.2974  -0.0498 -0.0585 89  TRP   B C   
1010 O  O   . TRP   B 80  ? 0.7929 0.5775 0.5983 0.2846  -0.0530 -0.0599 89  TRP   B O   
1011 C  CB  . TRP   B 80  ? 0.7448 0.5802 0.5700 0.3006  -0.0150 -0.0459 89  TRP   B CB  
1012 C  CG  . TRP   B 80  ? 0.7720 0.6042 0.5710 0.3261  -0.0157 -0.0456 89  TRP   B CG  
1013 C  CD1 . TRP   B 80  ? 0.7844 0.6057 0.5654 0.3414  -0.0222 -0.0474 89  TRP   B CD1 
1014 C  CD2 . TRP   B 80  ? 0.7734 0.6136 0.5599 0.3404  -0.0102 -0.0434 89  TRP   B CD2 
1015 N  NE1 . TRP   B 80  ? 0.8066 0.6294 0.5651 0.3646  -0.0203 -0.0463 89  TRP   B NE1 
1016 C  CE2 . TRP   B 80  ? 0.7918 0.6270 0.5535 0.3646  -0.0126 -0.0435 89  TRP   B CE2 
1017 C  CE3 . TRP   B 80  ? 0.7592 0.6119 0.5538 0.3354  -0.0029 -0.0410 89  TRP   B CE3 
1018 C  CZ2 . TRP   B 80  ? 0.8041 0.6464 0.5481 0.3846  -0.0083 -0.0410 89  TRP   B CZ2 
1019 C  CZ3 . TRP   B 80  ? 0.7699 0.6303 0.5482 0.3543  0.0017  -0.0383 89  TRP   B CZ3 
1020 C  CH2 . TRP   B 80  ? 0.7907 0.6465 0.5441 0.3788  -0.0008 -0.0381 89  TRP   B CH2 
1021 N  N   . ASP   B 81  ? 0.8611 0.6288 0.6323 0.3151  -0.0620 -0.0628 90  ASP   B N   
1022 C  CA  . ASP   B 81  ? 0.9025 0.6417 0.6477 0.3225  -0.0813 -0.0698 90  ASP   B CA  
1023 C  C   . ASP   B 81  ? 0.9266 0.6680 0.6528 0.3407  -0.0770 -0.0700 90  ASP   B C   
1024 O  O   . ASP   B 81  ? 0.9642 0.6819 0.6666 0.3492  -0.0922 -0.0759 90  ASP   B O   
1025 C  CB  . ASP   B 81  ? 0.9380 0.6518 0.6605 0.3336  -0.0986 -0.0751 90  ASP   B CB  
1026 C  CG  . ASP   B 81  ? 0.9675 0.6861 0.6721 0.3580  -0.0927 -0.0740 90  ASP   B CG  
1027 O  OD1 . ASP   B 81  ? 0.9803 0.7184 0.6853 0.3686  -0.0778 -0.0695 90  ASP   B OD1 
1028 O  OD2 . ASP   B 81  ? 1.0372 0.7372 0.7256 0.3662  -0.1057 -0.0781 90  ASP   B OD2 
1029 N  N   . GLY   B 82  ? 0.9163 0.6849 0.6521 0.3470  -0.0579 -0.0635 91  GLY   B N   
1030 C  CA  . GLY   B 82  ? 0.9154 0.6925 0.6366 0.3642  -0.0511 -0.0616 91  GLY   B CA  
1031 C  C   . GLY   B 82  ? 0.9488 0.7162 0.6381 0.3927  -0.0561 -0.0635 91  GLY   B C   
1032 O  O   . GLY   B 82  ? 0.9723 0.7448 0.6457 0.4093  -0.0524 -0.0624 91  GLY   B O   
1033 N  N   . LEU   B 83  ? 0.9554 0.7090 0.6341 0.3992  -0.0647 -0.0664 92  LEU   B N   
1034 C  CA  . LEU   B 83  ? 0.9986 0.7385 0.6440 0.4269  -0.0724 -0.0695 92  LEU   B CA  
1035 C  C   . LEU   B 83  ? 1.0087 0.7640 0.6604 0.4336  -0.0624 -0.0643 92  LEU   B C   
1036 O  O   . LEU   B 83  ? 1.0012 0.7705 0.6409 0.4545  -0.0529 -0.0597 92  LEU   B O   
1037 C  CB  . LEU   B 83  ? 1.0428 0.7446 0.6652 0.4287  -0.0972 -0.0795 92  LEU   B CB  
1038 C  CG  . LEU   B 83  ? 1.0757 0.7539 0.6756 0.4344  -0.1117 -0.0861 92  LEU   B CG  
1039 C  CD1 . LEU   B 83  ? 1.1228 0.7623 0.6935 0.4434  -0.1366 -0.0954 92  LEU   B CD1 
1040 C  CD2 . LEU   B 83  ? 1.0847 0.7743 0.6665 0.4574  -0.1028 -0.0838 92  LEU   B CD2 
1041 N  N   . SER   B 84  ? 1.0041 0.7558 0.6722 0.4178  -0.0655 -0.0649 93  SER   B N   
1042 C  CA  . SER   B 84  ? 1.0008 0.7578 0.6686 0.4256  -0.0619 -0.0624 93  SER   B CA  
1043 C  C   . SER   B 84  ? 0.9672 0.7593 0.6616 0.4203  -0.0387 -0.0518 93  SER   B C   
1044 O  O   . SER   B 84  ? 0.9343 0.7428 0.6527 0.4032  -0.0283 -0.0477 93  SER   B O   
1045 C  CB  . SER   B 84  ? 1.0256 0.7656 0.7010 0.4103  -0.0747 -0.0669 93  SER   B CB  
1046 O  OG  . SER   B 84  ? 1.0442 0.7650 0.7210 0.3948  -0.0889 -0.0726 93  SER   B OG  
1047 N  N   . GLU   B 85  ? 0.9464 0.7481 0.6357 0.4345  -0.0320 -0.0475 94  GLU   B N   
1048 C  CA  . GLU   B 85  ? 0.9055 0.7374 0.6195 0.4294  -0.0121 -0.0371 94  GLU   B CA  
1049 C  C   . GLU   B 85  ? 0.8454 0.6791 0.5883 0.4031  -0.0108 -0.0371 94  GLU   B C   
1050 O  O   . GLU   B 85  ? 0.8260 0.6382 0.5674 0.3923  -0.0258 -0.0446 94  GLU   B O   
1051 C  CB  . GLU   B 85  ? 0.9306 0.7689 0.6293 0.4519  -0.0077 -0.0331 94  GLU   B CB  
1052 C  CG  . GLU   B 85  ? 0.9491 0.7960 0.6247 0.4781  -0.0029 -0.0295 94  GLU   B CG  
1053 C  CD  . GLU   B 85  ? 0.9715 0.8295 0.6316 0.5027  0.0035  -0.0237 94  GLU   B CD  
1054 O  OE1 . GLU   B 85  ? 0.9487 0.8173 0.6224 0.4989  0.0108  -0.0186 94  GLU   B OE1 
1055 O  OE2 . GLU   B 85  ? 0.9962 0.8529 0.6296 0.5270  0.0015  -0.0238 94  GLU   B OE2 
1056 N  N   . VAL   B 86  ? 0.8012 0.6606 0.5700 0.3932  0.0065  -0.0285 95  VAL   B N   
1057 C  CA  . VAL   B 86  ? 0.7651 0.6308 0.5632 0.3693  0.0110  -0.0271 95  VAL   B CA  
1058 C  C   . VAL   B 86  ? 0.7470 0.6328 0.5581 0.3722  0.0255  -0.0184 95  VAL   B C   
1059 O  O   . VAL   B 86  ? 0.7641 0.6626 0.5656 0.3897  0.0339  -0.0122 95  VAL   B O   
1060 C  CB  . VAL   B 86  ? 0.7277 0.6030 0.5475 0.3495  0.0169  -0.0259 95  VAL   B CB  
1061 C  CG1 . VAL   B 86  ? 0.7358 0.5929 0.5412 0.3490  0.0037  -0.0333 95  VAL   B CG1 
1062 C  CG2 . VAL   B 86  ? 0.7125 0.6143 0.5451 0.3512  0.0347  -0.0165 95  VAL   B CG2 
1063 N  N   . GLN   B 87  ? 0.7296 0.6196 0.5629 0.3552  0.0291  -0.0171 96  GLN   B N   
1064 C  CA  . GLN   B 87  ? 0.7196 0.6296 0.5690 0.3547  0.0440  -0.0082 96  GLN   B CA  
1065 C  C   . GLN   B 87  ? 0.6724 0.5976 0.5516 0.3333  0.0551  -0.0039 96  GLN   B C   
1066 O  O   . GLN   B 87  ? 0.6967 0.6143 0.5880 0.3163  0.0499  -0.0087 96  GLN   B O   
1067 C  CB  . GLN   B 87  ? 0.7393 0.6403 0.5847 0.3582  0.0387  -0.0101 96  GLN   B CB  
1068 C  CG  . GLN   B 87  ? 0.7720 0.6653 0.5892 0.3832  0.0331  -0.0109 96  GLN   B CG  
1069 C  CD  . GLN   B 87  ? 0.7884 0.6711 0.5994 0.3876  0.0261  -0.0136 96  GLN   B CD  
1070 O  OE1 . GLN   B 87  ? 0.7610 0.6460 0.5905 0.3731  0.0280  -0.0130 96  GLN   B OE1 
1071 N  NE2 . GLN   B 87  ? 0.8228 0.6932 0.6059 0.4088  0.0171  -0.0170 96  GLN   B NE2 
1072 N  N   . LEU   B 88  ? 0.6407 0.5872 0.5313 0.3347  0.0698  0.0054  97  LEU   B N   
1073 C  CA  . LEU   B 88  ? 0.6119 0.5735 0.5308 0.3167  0.0815  0.0110  97  LEU   B CA  
1074 C  C   . LEU   B 88  ? 0.6042 0.5671 0.5311 0.3153  0.0848  0.0137  97  LEU   B C   
1075 O  O   . LEU   B 88  ? 0.6161 0.5866 0.5362 0.3293  0.0903  0.0200  97  LEU   B O   
1076 C  CB  . LEU   B 88  ? 0.6067 0.5899 0.5329 0.3205  0.0947  0.0211  97  LEU   B CB  
1077 C  CG  . LEU   B 88  ? 0.5909 0.5889 0.5452 0.3028  0.1061  0.0275  97  LEU   B CG  
1078 C  CD1 . LEU   B 88  ? 0.5841 0.5746 0.5515 0.2830  0.1018  0.0205  97  LEU   B CD1 
1079 C  CD2 . LEU   B 88  ? 0.5865 0.6062 0.5486 0.3062  0.1181  0.0386  97  LEU   B CD2 
1080 N  N   A LEU   B 89  ? 0.5915 0.5474 0.5317 0.2995  0.0813  0.0093  98  LEU   B N   
1081 N  N   B LEU   B 89  ? 0.5915 0.5474 0.5317 0.2995  0.0813  0.0093  98  LEU   B N   
1082 N  N   C LEU   B 89  ? 0.5899 0.5459 0.5303 0.2994  0.0814  0.0093  98  LEU   B N   
1083 N  N   D LEU   B 89  ? 0.5899 0.5459 0.5303 0.2994  0.0814  0.0093  98  LEU   B N   
1084 C  CA  A LEU   B 89  ? 0.5850 0.5449 0.5377 0.2950  0.0867  0.0127  98  LEU   B CA  
1085 C  CA  B LEU   B 89  ? 0.5850 0.5449 0.5377 0.2950  0.0867  0.0127  98  LEU   B CA  
1086 C  CA  C LEU   B 89  ? 0.5827 0.5426 0.5354 0.2949  0.0867  0.0127  98  LEU   B CA  
1087 C  CA  D LEU   B 89  ? 0.5827 0.5426 0.5354 0.2949  0.0867  0.0127  98  LEU   B CA  
1088 C  C   A LEU   B 89  ? 0.5681 0.5457 0.5427 0.2848  0.1008  0.0210  98  LEU   B C   
1089 C  C   B LEU   B 89  ? 0.5681 0.5457 0.5427 0.2848  0.1008  0.0210  98  LEU   B C   
1090 C  C   C LEU   B 89  ? 0.5668 0.5443 0.5414 0.2848  0.1008  0.0210  98  LEU   B C   
1091 C  C   D LEU   B 89  ? 0.5668 0.5443 0.5414 0.2848  0.1008  0.0210  98  LEU   B C   
1092 O  O   A LEU   B 89  ? 0.5622 0.5401 0.5538 0.2678  0.1022  0.0189  98  LEU   B O   
1093 O  O   B LEU   B 89  ? 0.5622 0.5401 0.5538 0.2678  0.1022  0.0189  98  LEU   B O   
1094 O  O   C LEU   B 89  ? 0.5611 0.5390 0.5528 0.2677  0.1022  0.0190  98  LEU   B O   
1095 O  O   D LEU   B 89  ? 0.5611 0.5390 0.5528 0.2677  0.1022  0.0190  98  LEU   B O   
1096 C  CB  A LEU   B 89  ? 0.5796 0.5264 0.5377 0.2826  0.0773  0.0051  98  LEU   B CB  
1097 C  CB  B LEU   B 89  ? 0.5796 0.5264 0.5377 0.2826  0.0773  0.0051  98  LEU   B CB  
1098 C  CB  C LEU   B 89  ? 0.5758 0.5224 0.5337 0.2826  0.0771  0.0050  98  LEU   B CB  
1099 C  CB  D LEU   B 89  ? 0.5758 0.5224 0.5337 0.2826  0.0771  0.0050  98  LEU   B CB  
1100 C  CG  A LEU   B 89  ? 0.5762 0.5250 0.5444 0.2794  0.0809  0.0074  98  LEU   B CG  
1101 C  CG  B LEU   B 89  ? 0.5762 0.5250 0.5444 0.2794  0.0809  0.0074  98  LEU   B CG  
1102 C  CG  C LEU   B 89  ? 0.5674 0.5171 0.5391 0.2761  0.0816  0.0073  98  LEU   B CG  
1103 C  CG  D LEU   B 89  ? 0.5674 0.5171 0.5391 0.2761  0.0816  0.0073  98  LEU   B CG  
1104 C  CD1 A LEU   B 89  ? 0.5925 0.5404 0.5453 0.2977  0.0808  0.0104  98  LEU   B CD1 
1105 C  CD1 B LEU   B 89  ? 0.5925 0.5404 0.5453 0.2977  0.0808  0.0104  98  LEU   B CD1 
1106 C  CD1 C LEU   B 89  ? 0.5670 0.5293 0.5413 0.2854  0.0932  0.0165  98  LEU   B CD1 
1107 C  CD1 D LEU   B 89  ? 0.5670 0.5293 0.5413 0.2854  0.0932  0.0165  98  LEU   B CD1 
1108 C  CD2 A LEU   B 89  ? 0.5737 0.5115 0.5470 0.2677  0.0711  0.0004  98  LEU   B CD2 
1109 C  CD2 B LEU   B 89  ? 0.5737 0.5115 0.5470 0.2677  0.0711  0.0004  98  LEU   B CD2 
1110 C  CD2 C LEU   B 89  ? 0.5771 0.5123 0.5394 0.2783  0.0693  0.0010  98  LEU   B CD2 
1111 C  CD2 D LEU   B 89  ? 0.5771 0.5123 0.5394 0.2783  0.0693  0.0010  98  LEU   B CD2 
1112 N  N   . ALA   B 90  ? 0.5734 0.5651 0.5469 0.2952  0.1103  0.0304  99  ALA   B N   
1113 C  CA  . ALA   B 90  ? 0.5675 0.5763 0.5611 0.2862  0.1230  0.0397  99  ALA   B CA  
1114 C  C   . ALA   B 90  ? 0.5756 0.5858 0.5843 0.2779  0.1281  0.0428  99  ALA   B C   
1115 O  O   . ALA   B 90  ? 0.6030 0.6100 0.6036 0.2881  0.1271  0.0439  99  ALA   B O   
1116 C  CB  . ALA   B 90  ? 0.5731 0.5976 0.5609 0.3003  0.1308  0.0499  99  ALA   B CB  
1117 N  N   . VAL   B 91  ? 0.5636 0.5779 0.5924 0.2611  0.1331  0.0441  100 VAL   B N   
1118 C  CA  . VAL   B 91  ? 0.5553 0.5712 0.5987 0.2535  0.1388  0.0479  100 VAL   B CA  
1119 C  C   . VAL   B 91  ? 0.5494 0.5794 0.6095 0.2463  0.1493  0.0580  100 VAL   B C   
1120 O  O   . VAL   B 91  ? 0.5329 0.5626 0.6077 0.2311  0.1508  0.0564  100 VAL   B O   
1121 C  CB  . VAL   B 91  ? 0.5482 0.5524 0.5984 0.2407  0.1328  0.0387  100 VAL   B CB  
1122 C  CG1 . VAL   B 91  ? 0.5444 0.5497 0.6085 0.2339  0.1385  0.0422  100 VAL   B CG1 
1123 C  CG2 . VAL   B 91  ? 0.5616 0.5529 0.5955 0.2480  0.1216  0.0303  100 VAL   B CG2 
1124 N  N   . PRO   B 92  ? 0.5749 0.6175 0.6328 0.2571  0.1563  0.0691  101 PRO   B N   
1125 C  CA  . PRO   B 92  ? 0.5767 0.6344 0.6499 0.2510  0.1654  0.0804  101 PRO   B CA  
1126 C  C   . PRO   B 92  ? 0.5872 0.6430 0.6771 0.2395  0.1697  0.0840  101 PRO   B C   
1127 O  O   . PRO   B 92  ? 0.5935 0.6397 0.6809 0.2409  0.1675  0.0801  101 PRO   B O   
1128 C  CB  . PRO   B 92  ? 0.5931 0.6649 0.6568 0.2681  0.1704  0.0912  101 PRO   B CB  
1129 C  CG  . PRO   B 92  ? 0.6068 0.6688 0.6474 0.2842  0.1629  0.0835  101 PRO   B CG  
1130 C  CD  . PRO   B 92  ? 0.5928 0.6368 0.6337 0.2761  0.1556  0.0721  101 PRO   B CD  
1131 N  N   . PRO   B 93  ? 0.5948 0.6580 0.7018 0.2272  0.1751  0.0907  102 PRO   B N   
1132 C  CA  . PRO   B 93  ? 0.6098 0.6699 0.7316 0.2171  0.1787  0.0947  102 PRO   B CA  
1133 C  C   . PRO   B 93  ? 0.6136 0.6776 0.7334 0.2271  0.1834  0.1040  102 PRO   B C   
1134 O  O   . PRO   B 93  ? 0.6166 0.6941 0.7321 0.2381  0.1878  0.1143  102 PRO   B O   
1135 C  CB  . PRO   B 93  ? 0.6031 0.6725 0.7409 0.2048  0.1828  0.1020  102 PRO   B CB  
1136 C  CG  . PRO   B 93  ? 0.5929 0.6639 0.7252 0.2037  0.1789  0.0950  102 PRO   B CG  
1137 C  CD  . PRO   B 93  ? 0.6013 0.6746 0.7144 0.2215  0.1768  0.0937  102 PRO   B CD  
1138 N  N   . GLY   B 94  ? 0.6116 0.6641 0.7336 0.2241  0.1821  0.1002  103 GLY   B N   
1139 C  CA  . GLY   B 94  ? 0.6131 0.6663 0.7335 0.2324  0.1858  0.1073  103 GLY   B CA  
1140 C  C   . GLY   B 94  ? 0.6295 0.6860 0.7319 0.2511  0.1846  0.1078  103 GLY   B C   
1141 O  O   . GLY   B 94  ? 0.6740 0.7342 0.7749 0.2593  0.1885  0.1155  103 GLY   B O   
1142 N  N   . GLU   B 95  ? 0.6395 0.6940 0.7278 0.2584  0.1790  0.0999  104 GLU   B N   
1143 C  CA  . GLU   B 95  ? 0.6342 0.6907 0.7029 0.2776  0.1767  0.0998  104 GLU   B CA  
1144 C  C   . GLU   B 95  ? 0.6358 0.6759 0.6920 0.2794  0.1665  0.0852  104 GLU   B C   
1145 O  O   . GLU   B 95  ? 0.6258 0.6576 0.6882 0.2665  0.1620  0.0765  104 GLU   B O   
1146 C  CB  . GLU   B 95  ? 0.6407 0.7109 0.7028 0.2862  0.1790  0.1056  104 GLU   B CB  
1147 C  CG  . GLU   B 95  ? 0.6395 0.7289 0.7147 0.2853  0.1891  0.1222  104 GLU   B CG  
1148 C  CD  . GLU   B 95  ? 0.6627 0.7684 0.7337 0.2926  0.1920  0.1291  104 GLU   B CD  
1149 O  OE1 . GLU   B 95  ? 0.6536 0.7543 0.7116 0.2975  0.1860  0.1198  104 GLU   B OE1 
1150 O  OE2 . GLU   B 95  ? 0.6786 0.8030 0.7599 0.2935  0.2003  0.1445  104 GLU   B OE2 
1151 N  N   . ARG   B 96  ? 0.6732 0.7090 0.7127 0.2945  0.1625  0.0830  105 ARG   B N   
1152 C  CA  . ARG   B 96  ? 0.7058 0.7261 0.7327 0.2970  0.1516  0.0703  105 ARG   B CA  
1153 C  C   . ARG   B 96  ? 0.6915 0.7073 0.7080 0.2979  0.1442  0.0626  105 ARG   B C   
1154 O  O   . ARG   B 96  ? 0.6736 0.6989 0.6845 0.3054  0.1472  0.0676  105 ARG   B O   
1155 C  CB  . ARG   B 96  ? 0.7877 0.8051 0.7980 0.3145  0.1489  0.0708  105 ARG   B CB  
1156 C  CG  . ARG   B 96  ? 0.8518 0.8537 0.8555 0.3134  0.1388  0.0600  105 ARG   B CG  
1157 C  CD  . ARG   B 96  ? 0.9085 0.9088 0.9058 0.3243  0.1395  0.0629  105 ARG   B CD  
1158 N  NE  . ARG   B 96  ? 0.9600 0.9680 0.9426 0.3433  0.1426  0.0699  105 ARG   B NE  
1159 C  CZ  . ARG   B 96  ? 1.0237 1.0440 1.0102 0.3504  0.1526  0.0819  105 ARG   B CZ  
1160 N  NH1 . ARG   B 96  ? 1.0084 1.0331 1.0130 0.3398  0.1602  0.0883  105 ARG   B NH1 
1161 N  NH2 . ARG   B 96  ? 1.0521 1.0802 1.0232 0.3690  0.1545  0.0878  105 ARG   B NH2 
1162 N  N   . ALA   B 97  ? 0.6725 0.6749 0.6868 0.2907  0.1347  0.0513  106 ALA   B N   
1163 C  CA  . ALA   B 97  ? 0.6724 0.6660 0.6740 0.2925  0.1247  0.0426  106 ALA   B CA  
1164 C  C   . ALA   B 97  ? 0.6928 0.6864 0.6723 0.3131  0.1217  0.0441  106 ALA   B C   
1165 O  O   . ALA   B 97  ? 0.7012 0.6902 0.6705 0.3238  0.1189  0.0438  106 ALA   B O   
1166 C  CB  . ALA   B 97  ? 0.6552 0.6349 0.6568 0.2844  0.1147  0.0326  106 ALA   B CB  
1167 N  N   . LYS   B 98  ? 0.7126 0.7110 0.6840 0.3190  0.1219  0.0453  107 LYS   B N   
1168 C  CA  . LYS   B 98  ? 0.7634 0.7614 0.7113 0.3401  0.1183  0.0459  107 LYS   B CA  
1169 C  C   . LYS   B 98  ? 0.7481 0.7353 0.6825 0.3415  0.1081  0.0371  107 LYS   B C   
1170 O  O   . LYS   B 98  ? 0.7421 0.7345 0.6874 0.3303  0.1109  0.0374  107 LYS   B O   
1171 C  CB  . LYS   B 98  ? 0.8158 0.8343 0.7675 0.3482  0.1308  0.0590  107 LYS   B CB  
1172 C  CG  . LYS   B 98  ? 0.8833 0.9067 0.8133 0.3724  0.1311  0.0635  107 LYS   B CG  
1173 C  CD  . LYS   B 98  ? 0.9397 0.9867 0.8754 0.3793  0.1438  0.0778  107 LYS   B CD  
1174 C  CE  . LYS   B 98  ? 0.9502 1.0071 0.9056 0.3624  0.1493  0.0811  107 LYS   B CE  
1175 N  NZ  . LYS   B 98  ? 0.9901 1.0663 0.9423 0.3727  0.1564  0.0912  107 LYS   B NZ  
1176 N  N   . ASN   B 99  ? 0.7398 0.7118 0.6513 0.3544  0.0961  0.0296  108 ASN   B N   
1177 C  CA  . ASN   B 99  ? 0.7407 0.7012 0.6349 0.3598  0.0856  0.0220  108 ASN   B CA  
1178 C  C   . ASN   B 99  ? 0.7520 0.7246 0.6331 0.3772  0.0914  0.0285  108 ASN   B C   
1179 O  O   . ASN   B 99  ? 0.7951 0.7750 0.6655 0.3944  0.0957  0.0346  108 ASN   B O   
1180 C  CB  . ASN   B 99  ? 0.7472 0.6852 0.6206 0.3673  0.0692  0.0117  108 ASN   B CB  
1181 C  CG  . ASN   B 99  ? 0.7434 0.6713 0.6303 0.3496  0.0628  0.0058  108 ASN   B CG  
1182 O  OD1 . ASN   B 99  ? 0.7519 0.6883 0.6557 0.3416  0.0707  0.0103  108 ASN   B OD1 
1183 N  ND2 . ASN   B 99  ? 0.7346 0.6451 0.6141 0.3438  0.0486  -0.0033 108 ASN   B ND2 
1184 N  N   . ILE   B 100 ? 0.7293 0.7038 0.6094 0.3745  0.0908  0.0272  109 ILE   B N   
1185 C  CA  . ILE   B 100 ? 0.7376 0.7240 0.6039 0.3920  0.0956  0.0331  109 ILE   B CA  
1186 C  C   . ILE   B 100 ? 0.7437 0.7126 0.5904 0.3969  0.0825  0.0229  109 ILE   B C   
1187 O  O   . ILE   B 100 ? 0.7551 0.7184 0.6124 0.3804  0.0790  0.0179  109 ILE   B O   
1188 C  CB  . ILE   B 100 ? 0.7210 0.7314 0.6090 0.3827  0.1100  0.0440  109 ILE   B CB  
1189 C  CG1 . ILE   B 100 ? 0.7155 0.7386 0.6268 0.3717  0.1209  0.0526  109 ILE   B CG1 
1190 C  CG2 . ILE   B 100 ? 0.7328 0.7590 0.6082 0.4012  0.1158  0.0519  109 ILE   B CG2 
1191 C  CD1 . ILE   B 100 ? 0.7233 0.7584 0.6275 0.3891  0.1279  0.0624  109 ILE   B CD1 
1192 N  N   . GLN   B 101 ? 0.7802 0.7385 0.5986 0.4185  0.0742  0.0193  110 GLN   B N   
1193 C  CA  . GLN   B 101 ? 0.8117 0.7488 0.6086 0.4240  0.0593  0.0086  110 GLN   B CA  
1194 C  C   . GLN   B 101 ? 0.8264 0.7755 0.6156 0.4342  0.0645  0.0127  110 GLN   B C   
1195 O  O   . GLN   B 101 ? 0.8235 0.7931 0.6100 0.4490  0.0758  0.0230  110 GLN   B O   
1196 C  CB  . GLN   B 101 ? 0.8484 0.7653 0.6163 0.4431  0.0461  0.0017  110 GLN   B CB  
1197 C  CG  . GLN   B 101 ? 0.8713 0.7630 0.6168 0.4476  0.0289  -0.0095 110 GLN   B CG  
1198 C  CD  . GLN   B 101 ? 0.8989 0.7662 0.6218 0.4586  0.0130  -0.0179 110 GLN   B CD  
1199 O  OE1 . GLN   B 101 ? 0.9070 0.7714 0.6389 0.4515  0.0118  -0.0183 110 GLN   B OE1 
1200 N  NE2 . GLN   B 101 ? 0.9170 0.7665 0.6090 0.4773  0.0007  -0.0244 110 GLN   B NE2 
1201 N  N   . THR   B 102 ? 0.8292 0.7665 0.6151 0.4266  0.0564  0.0055  111 THR   B N   
1202 C  CA  . THR   B 102 ? 0.8240 0.7711 0.6032 0.4342  0.0602  0.0084  111 THR   B CA  
1203 C  C   . THR   B 102 ? 0.8267 0.7496 0.5909 0.4317  0.0447  -0.0031 111 THR   B C   
1204 O  O   . THR   B 102 ? 0.8517 0.7555 0.6209 0.4164  0.0341  -0.0113 111 THR   B O   
1205 C  CB  . THR   B 102 ? 0.8070 0.7812 0.6166 0.4183  0.0765  0.0187  111 THR   B CB  
1206 O  OG1 . THR   B 102 ? 0.8071 0.7955 0.6093 0.4296  0.0819  0.0239  111 THR   B OG1 
1207 C  CG2 . THR   B 102 ? 0.7814 0.7507 0.6154 0.3907  0.0753  0.0145  111 THR   B CG2 
1208 N  N   . LEU   B 103 ? 0.8183 0.7423 0.5638 0.4473  0.0434  -0.0032 112 LEU   B N   
1209 C  CA  . LEU   B 103 ? 0.8209 0.7261 0.5537 0.4452  0.0312  -0.0122 112 LEU   B CA  
1210 C  C   . LEU   B 103 ? 0.7872 0.7111 0.5428 0.4294  0.0417  -0.0071 112 LEU   B C   
1211 O  O   . LEU   B 103 ? 0.7733 0.7224 0.5331 0.4378  0.0548  0.0025  112 LEU   B O   
1212 C  CB  . LEU   B 103 ? 0.8567 0.7525 0.5540 0.4735  0.0240  -0.0150 112 LEU   B CB  
1213 C  CG  . LEU   B 103 ? 0.8657 0.7425 0.5499 0.4717  0.0119  -0.0235 112 LEU   B CG  
1214 C  CD1 . LEU   B 103 ? 0.8803 0.7232 0.5549 0.4631  -0.0074 -0.0355 112 LEU   B CD1 
1215 C  CD2 . LEU   B 103 ? 0.8994 0.7762 0.5538 0.4991  0.0101  -0.0233 112 LEU   B CD2 
1216 N  N   . PRO   B 104 ? 0.7713 0.6855 0.5432 0.4062  0.0367  -0.0126 113 PRO   B N   
1217 C  CA  . PRO   B 104 ? 0.7523 0.6834 0.5470 0.3898  0.0463  -0.0083 113 PRO   B CA  
1218 C  C   . PRO   B 104 ? 0.7722 0.7074 0.5527 0.4015  0.0462  -0.0078 113 PRO   B C   
1219 O  O   . PRO   B 104 ? 0.7997 0.7152 0.5518 0.4174  0.0340  -0.0148 113 PRO   B O   
1220 C  CB  . PRO   B 104 ? 0.7387 0.6535 0.5466 0.3666  0.0374  -0.0161 113 PRO   B CB  
1221 C  CG  . PRO   B 104 ? 0.7421 0.6414 0.5458 0.3663  0.0293  -0.0203 113 PRO   B CG  
1222 C  CD  . PRO   B 104 ? 0.7796 0.6696 0.5523 0.3932  0.0232  -0.0217 113 PRO   B CD  
1223 N  N   . GLY   B 105 ? 0.7687 0.7295 0.5686 0.3944  0.0600  0.0007  114 GLY   B N   
1224 C  CA  . GLY   B 105 ? 0.7838 0.7529 0.5792 0.3986  0.0621  0.0022  114 GLY   B CA  
1225 C  C   . GLY   B 105 ? 0.7787 0.7366 0.5865 0.3770  0.0562  -0.0046 114 GLY   B C   
1226 O  O   . GLY   B 105 ? 0.7492 0.6878 0.5608 0.3640  0.0470  -0.0119 114 GLY   B O   
1227 N  N   . ILE   B 106 ? 0.7788 0.7494 0.5929 0.3735  0.0614  -0.0017 115 ILE   B N   
1228 C  CA  . ILE   B 106 ? 0.7735 0.7330 0.5948 0.3565  0.0550  -0.0084 115 ILE   B CA  
1229 C  C   . ILE   B 106 ? 0.7408 0.7257 0.5878 0.3424  0.0680  -0.0010 115 ILE   B C   
1230 O  O   . ILE   B 106 ? 0.7507 0.7565 0.5972 0.3530  0.0773  0.0071  115 ILE   B O   
1231 C  CB  . ILE   B 106 ? 0.8218 0.7625 0.6142 0.3714  0.0429  -0.0154 115 ILE   B CB  
1232 C  CG1 . ILE   B 106 ? 0.8649 0.7769 0.6309 0.3842  0.0276  -0.0237 115 ILE   B CG1 
1233 C  CG2 . ILE   B 106 ? 0.8401 0.7729 0.6408 0.3546  0.0379  -0.0206 115 ILE   B CG2 
1234 C  CD1 . ILE   B 106 ? 0.8590 0.7479 0.6308 0.3663  0.0156  -0.0319 115 ILE   B CD1 
1235 N  N   . PHE   B 107 ? 0.7302 0.7130 0.5986 0.3193  0.0681  -0.0037 116 PHE   B N   
1236 C  CA  . PHE   B 107 ? 0.7058 0.7050 0.5944 0.3047  0.0759  -0.0002 116 PHE   B CA  
1237 C  C   . PHE   B 107 ? 0.7371 0.7199 0.6130 0.3037  0.0654  -0.0082 116 PHE   B C   
1238 O  O   . PHE   B 107 ? 0.7394 0.7006 0.6131 0.2940  0.0546  -0.0164 116 PHE   B O   
1239 C  CB  . PHE   B 107 ? 0.6758 0.6793 0.5919 0.2817  0.0805  0.0001  116 PHE   B CB  
1240 C  CG  . PHE   B 107 ? 0.6549 0.6786 0.5887 0.2792  0.0928  0.0096  116 PHE   B CG  
1241 C  CD1 . PHE   B 107 ? 0.6648 0.7032 0.5908 0.2966  0.0995  0.0181  116 PHE   B CD1 
1242 C  CD2 . PHE   B 107 ? 0.6288 0.6566 0.5866 0.2597  0.0974  0.0104  116 PHE   B CD2 
1243 C  CE1 . PHE   B 107 ? 0.6572 0.7142 0.6004 0.2933  0.1105  0.0277  116 PHE   B CE1 
1244 C  CE2 . PHE   B 107 ? 0.6299 0.6747 0.6037 0.2570  0.1079  0.0193  116 PHE   B CE2 
1245 C  CZ  . PHE   B 107 ? 0.6253 0.6846 0.5924 0.2731  0.1144  0.0281  116 PHE   B CZ  
1246 N  N   . LYS   B 108 ? 0.7449 0.7373 0.6120 0.3140  0.0679  -0.0055 117 LYS   B N   
1247 C  CA  . LYS   B 108 ? 0.7934 0.7731 0.6505 0.3121  0.0595  -0.0120 117 LYS   B CA  
1248 C  C   . LYS   B 108 ? 0.7449 0.7395 0.6282 0.2913  0.0668  -0.0096 117 LYS   B C   
1249 O  O   . LYS   B 108 ? 0.7270 0.7473 0.6244 0.2906  0.0790  -0.0008 117 LYS   B O   
1250 C  CB  . LYS   B 108 ? 0.8638 0.8455 0.6957 0.3359  0.0580  -0.0106 117 LYS   B CB  
1251 C  CG  . LYS   B 108 ? 0.9604 0.9158 0.7603 0.3549  0.0445  -0.0176 117 LYS   B CG  
1252 C  CD  . LYS   B 108 ? 1.0500 1.0144 0.8272 0.3828  0.0476  -0.0129 117 LYS   B CD  
1253 C  CE  . LYS   B 108 ? 1.1455 1.0886 0.8967 0.4006  0.0374  -0.0179 117 LYS   B CE  
1254 N  NZ  . LYS   B 108 ? 1.2269 1.1706 0.9477 0.4304  0.0358  -0.0165 117 LYS   B NZ  
1255 N  N   . THR   B 109 ? 0.7321 0.7119 0.6223 0.2746  0.0596  -0.0166 118 THR   B N   
1256 C  CA  . THR   B 109 ? 0.7254 0.7169 0.6396 0.2544  0.0654  -0.0155 118 THR   B CA  
1257 C  C   . THR   B 109 ? 0.7703 0.7471 0.6751 0.2508  0.0559  -0.0222 118 THR   B C   
1258 O  O   . THR   B 109 ? 0.7730 0.7267 0.6565 0.2591  0.0433  -0.0285 118 THR   B O   
1259 C  CB  . THR   B 109 ? 0.6987 0.6912 0.6356 0.2353  0.0683  -0.0159 118 THR   B CB  
1260 O  OG1 . THR   B 109 ? 0.6871 0.6582 0.6213 0.2256  0.0571  -0.0238 118 THR   B OG1 
1261 C  CG2 . THR   B 109 ? 0.6880 0.6863 0.6286 0.2403  0.0737  -0.0113 118 THR   B CG2 
1262 N  N   . LYS   B 110 ? 0.8194 0.8087 0.7397 0.2385  0.0612  -0.0207 119 LYS   B N   
1263 C  CA  . LYS   B 110 ? 0.8375 0.8161 0.7527 0.2327  0.0538  -0.0262 119 LYS   B CA  
1264 C  C   . LYS   B 110 ? 0.8388 0.7933 0.7515 0.2226  0.0417  -0.0334 119 LYS   B C   
1265 O  O   . LYS   B 110 ? 0.8785 0.8152 0.7759 0.2250  0.0308  -0.0386 119 LYS   B O   
1266 C  CB  . LYS   B 110 ? 0.8307 0.8293 0.7675 0.2189  0.0630  -0.0227 119 LYS   B CB  
1267 C  CG  . LYS   B 110 ? 0.8548 0.8560 0.8154 0.1975  0.0658  -0.0239 119 LYS   B CG  
1268 C  CD  . LYS   B 110 ? 0.8495 0.8734 0.8322 0.1861  0.0767  -0.0190 119 LYS   B CD  
1269 C  CE  . LYS   B 110 ? 0.8684 0.8895 0.8653 0.1677  0.0751  -0.0231 119 LYS   B CE  
1270 N  NZ  . LYS   B 110 ? 0.8970 0.9103 0.9044 0.1565  0.0735  -0.0256 119 LYS   B NZ  
1271 N  N   . ASP   B 111 ? 0.7911 0.7450 0.7174 0.2125  0.0433  -0.0333 120 ASP   B N   
1272 C  CA  . ASP   B 111 ? 0.7840 0.7192 0.7118 0.2013  0.0330  -0.0386 120 ASP   B CA  
1273 C  C   . ASP   B 111 ? 0.7923 0.7085 0.7017 0.2128  0.0231  -0.0414 120 ASP   B C   
1274 O  O   . ASP   B 111 ? 0.8012 0.7030 0.7128 0.2035  0.0144  -0.0448 120 ASP   B O   
1275 C  CB  . ASP   B 111 ? 0.7790 0.7253 0.7324 0.1841  0.0403  -0.0367 120 ASP   B CB  
1276 C  CG  . ASP   B 111 ? 0.7828 0.7450 0.7549 0.1708  0.0483  -0.0350 120 ASP   B CG  
1277 O  OD1 . ASP   B 111 ? 0.7924 0.7556 0.7584 0.1731  0.0471  -0.0357 120 ASP   B OD1 
1278 O  OD2 . ASP   B 111 ? 0.8648 0.8371 0.8565 0.1586  0.0550  -0.0334 120 ASP   B OD2 
1279 N  N   . GLY   B 112 ? 0.7882 0.7051 0.6809 0.2319  0.0243  -0.0396 121 GLY   B N   
1280 C  CA  . GLY   B 112 ? 0.8039 0.7020 0.6773 0.2443  0.0145  -0.0426 121 GLY   B CA  
1281 C  C   . GLY   B 112 ? 0.7953 0.7055 0.6677 0.2564  0.0231  -0.0377 121 GLY   B C   
1282 O  O   . GLY   B 112 ? 0.7697 0.7029 0.6607 0.2516  0.0368  -0.0315 121 GLY   B O   
1283 N  N   . ASP   B 113 ? 0.8115 0.7052 0.6625 0.2714  0.0143  -0.0405 122 ASP   B N   
1284 C  CA  . ASP   B 113 ? 0.8075 0.7089 0.6522 0.2862  0.0200  -0.0365 122 ASP   B CA  
1285 C  C   . ASP   B 113 ? 0.7935 0.6942 0.6534 0.2750  0.0211  -0.0361 122 ASP   B C   
1286 O  O   . ASP   B 113 ? 0.7754 0.6577 0.6351 0.2650  0.0098  -0.0416 122 ASP   B O   
1287 C  CB  . ASP   B 113 ? 0.8469 0.7279 0.6592 0.3082  0.0082  -0.0408 122 ASP   B CB  
1288 C  CG  . ASP   B 113 ? 0.9006 0.7806 0.6927 0.3242  0.0064  -0.0413 122 ASP   B CG  
1289 O  OD1 . ASP   B 113 ? 0.9107 0.8069 0.7152 0.3174  0.0145  -0.0381 122 ASP   B OD1 
1290 O  OD2 . ASP   B 113 ? 0.9628 0.8255 0.7261 0.3441  -0.0034 -0.0452 122 ASP   B OD2 
1291 N  N   . ILE   B 114 ? 0.7808 0.7009 0.6528 0.2770  0.0337  -0.0294 123 ILE   B N   
1292 C  CA  . ILE   B 114 ? 0.7581 0.6794 0.6426 0.2701  0.0362  -0.0281 123 ILE   B CA  
1293 C  C   . ILE   B 114 ? 0.7300 0.6548 0.6004 0.2898  0.0392  -0.0244 123 ILE   B C   
1294 O  O   . ILE   B 114 ? 0.7133 0.6544 0.5795 0.3023  0.0479  -0.0184 123 ILE   B O   
1295 C  CB  . ILE   B 114 ? 0.7556 0.6978 0.6701 0.2528  0.0494  -0.0227 123 ILE   B CB  
1296 C  CG1 . ILE   B 114 ? 0.7866 0.7379 0.7131 0.2410  0.0533  -0.0223 123 ILE   B CG1 
1297 C  CG2 . ILE   B 114 ? 0.7567 0.6922 0.6843 0.2390  0.0467  -0.0250 123 ILE   B CG2 
1298 C  CD1 . ILE   B 114 ? 0.7856 0.7586 0.7387 0.2277  0.0669  -0.0162 123 ILE   B CD1 
1299 N  N   . GLY   B 115 ? 0.7135 0.6257 0.5782 0.2923  0.0328  -0.0271 124 GLY   B N   
1300 C  CA  . GLY   B 115 ? 0.7113 0.6303 0.5686 0.3078  0.0380  -0.0224 124 GLY   B CA  
1301 C  C   . GLY   B 115 ? 0.6830 0.6296 0.5633 0.3021  0.0552  -0.0127 124 GLY   B C   
1302 O  O   . GLY   B 115 ? 0.6506 0.6068 0.5548 0.2830  0.0614  -0.0111 124 GLY   B O   
1303 N  N   . ALA   B 116 ? 0.7127 0.6721 0.5851 0.3189  0.0626  -0.0060 125 ALA   B N   
1304 C  CA  . ALA   B 116 ? 0.7076 0.6934 0.5996 0.3163  0.0783  0.0048  125 ALA   B CA  
1305 C  C   . ALA   B 116 ? 0.7122 0.7000 0.5933 0.3327  0.0804  0.0090  125 ALA   B C   
1306 O  O   . ALA   B 116 ? 0.7343 0.7109 0.5890 0.3526  0.0729  0.0058  125 ALA   B O   
1307 C  CB  . ALA   B 116 ? 0.7152 0.7205 0.6098 0.3206  0.0867  0.0115  125 ALA   B CB  
1308 N  N   A VAL   B 117 ? 0.6953 0.6961 0.5953 0.3253  0.0899  0.0156  126 VAL   B N   
1309 N  N   B VAL   B 117 ? 0.6951 0.6964 0.5955 0.3251  0.0901  0.0158  126 VAL   B N   
1310 N  N   C VAL   B 117 ? 0.6953 0.6961 0.5953 0.3253  0.0899  0.0156  126 VAL   B N   
1311 N  N   D VAL   B 117 ? 0.6951 0.6964 0.5955 0.3251  0.0901  0.0158  126 VAL   B N   
1312 C  CA  A VAL   B 117 ? 0.7091 0.7149 0.6019 0.3398  0.0937  0.0211  126 VAL   B CA  
1313 C  CA  B VAL   B 117 ? 0.7079 0.7142 0.6024 0.3385  0.0941  0.0213  126 VAL   B CA  
1314 C  CA  C VAL   B 117 ? 0.7091 0.7149 0.6019 0.3398  0.0937  0.0211  126 VAL   B CA  
1315 C  CA  D VAL   B 117 ? 0.7079 0.7142 0.6024 0.3385  0.0941  0.0213  126 VAL   B CA  
1316 C  C   A VAL   B 117 ? 0.6999 0.7346 0.6076 0.3418  0.1091  0.0349  126 VAL   B C   
1317 C  C   B VAL   B 117 ? 0.6997 0.7348 0.6078 0.3416  0.1093  0.0351  126 VAL   B C   
1318 C  C   C VAL   B 117 ? 0.6999 0.7346 0.6076 0.3418  0.1091  0.0349  126 VAL   B C   
1319 C  C   D VAL   B 117 ? 0.6997 0.7348 0.6078 0.3416  0.1093  0.0351  126 VAL   B C   
1320 O  O   A VAL   B 117 ? 0.6847 0.7312 0.6173 0.3238  0.1167  0.0393  126 VAL   B O   
1321 O  O   B VAL   B 117 ? 0.6843 0.7318 0.6173 0.3239  0.1172  0.0398  126 VAL   B O   
1322 O  O   C VAL   B 117 ? 0.6847 0.7312 0.6173 0.3238  0.1167  0.0393  126 VAL   B O   
1323 O  O   D VAL   B 117 ? 0.6843 0.7318 0.6173 0.3239  0.1172  0.0398  126 VAL   B O   
1324 C  CB  A VAL   B 117 ? 0.7072 0.7005 0.6074 0.3300  0.0897  0.0169  126 VAL   B CB  
1325 C  CB  B VAL   B 117 ? 0.7033 0.6984 0.6081 0.3264  0.0910  0.0174  126 VAL   B CB  
1326 C  CB  C VAL   B 117 ? 0.7072 0.7005 0.6074 0.3300  0.0897  0.0169  126 VAL   B CB  
1327 C  CB  D VAL   B 117 ? 0.7033 0.6984 0.6081 0.3264  0.0910  0.0174  126 VAL   B CB  
1328 C  CG1 A VAL   B 117 ? 0.7092 0.6785 0.6043 0.3200  0.0758  0.0050  126 VAL   B CG1 
1329 C  CG1 B VAL   B 117 ? 0.6979 0.7064 0.6101 0.3316  0.1005  0.0263  126 VAL   B CG1 
1330 C  CG1 C VAL   B 117 ? 0.7092 0.6785 0.6043 0.3200  0.0758  0.0050  126 VAL   B CG1 
1331 C  CG1 D VAL   B 117 ? 0.6979 0.7064 0.6101 0.3316  0.1005  0.0263  126 VAL   B CG1 
1332 C  CG2 A VAL   B 117 ? 0.6824 0.6911 0.6113 0.3131  0.1010  0.0238  126 VAL   B CG2 
1333 C  CG2 B VAL   B 117 ? 0.7232 0.6915 0.6079 0.3315  0.0752  0.0062  126 VAL   B CG2 
1334 C  CG2 C VAL   B 117 ? 0.6824 0.6911 0.6113 0.3131  0.1010  0.0238  126 VAL   B CG2 
1335 C  CG2 D VAL   B 117 ? 0.7232 0.6915 0.6079 0.3315  0.0752  0.0062  126 VAL   B CG2 
1336 N  N   . ALA   B 118 ? 0.7200 0.7657 0.6122 0.3635  0.1129  0.0418  127 ALA   B N   
1337 C  CA  . ALA   B 118 ? 0.7154 0.7912 0.6195 0.3683  0.1272  0.0568  127 ALA   B CA  
1338 C  C   . ALA   B 118 ? 0.7174 0.8016 0.6283 0.3718  0.1339  0.0648  127 ALA   B C   
1339 O  O   . ALA   B 118 ? 0.7101 0.7960 0.6020 0.3929  0.1336  0.0676  127 ALA   B O   
1340 C  CB  . ALA   B 118 ? 0.7339 0.8194 0.6173 0.3905  0.1279  0.0607  127 ALA   B CB  
1341 N  N   . LEU   B 119 ? 0.6968 0.7833 0.6322 0.3521  0.1385  0.0670  128 LEU   B N   
1342 C  CA  . LEU   B 119 ? 0.7097 0.8029 0.6538 0.3529  0.1448  0.0744  128 LEU   B CA  
1343 C  C   . LEU   B 119 ? 0.7163 0.8257 0.6907 0.3333  0.1549  0.0837  128 LEU   B C   
1344 O  O   . LEU   B 119 ? 0.7265 0.8305 0.7149 0.3148  0.1530  0.0784  128 LEU   B O   
1345 C  CB  . LEU   B 119 ? 0.7046 0.7732 0.6412 0.3500  0.1352  0.0630  128 LEU   B CB  
1346 C  CG  . LEU   B 119 ? 0.7137 0.7638 0.6199 0.3690  0.1237  0.0539  128 LEU   B CG  
1347 C  CD1 . LEU   B 119 ? 0.7016 0.7272 0.6043 0.3616  0.1129  0.0425  128 LEU   B CD1 
1348 C  CD2 . LEU   B 119 ? 0.7388 0.8005 0.6294 0.3927  0.1283  0.0624  128 LEU   B CD2 
1349 N  N   . ASP   B 120 ? 0.7393 0.8687 0.7229 0.3380  0.1650  0.0977  129 ASP   B N   
1350 C  CA  . ASP   B 120 ? 0.7497 0.8954 0.7615 0.3207  0.1742  0.1085  129 ASP   B CA  
1351 C  C   . ASP   B 120 ? 0.7420 0.8776 0.7649 0.3104  0.1745  0.1071  129 ASP   B C   
1352 O  O   . ASP   B 120 ? 0.7956 0.9314 0.8093 0.3231  0.1758  0.1105  129 ASP   B O   
1353 C  CB  . ASP   B 120 ? 0.7760 0.9503 0.7935 0.3306  0.1849  0.1265  129 ASP   B CB  
1354 C  CG  . ASP   B 120 ? 0.8153 1.0070 0.8301 0.3369  0.1876  0.1320  129 ASP   B CG  
1355 O  OD1 . ASP   B 120 ? 0.8223 1.0028 0.8300 0.3335  0.1809  0.1213  129 ASP   B OD1 
1356 O  OD2 . ASP   B 120 ? 0.8576 1.0749 0.8765 0.3462  0.1962  0.1478  129 ASP   B OD2 
1357 N  N   . TYR   B 121 ? 0.6977 0.8258 0.7389 0.2892  0.1737  0.1028  130 TYR   B N   
1358 C  CA  . TYR   B 121 ? 0.7016 0.8228 0.7566 0.2778  0.1754  0.1033  130 TYR   B CA  
1359 C  C   . TYR   B 121 ? 0.6778 0.8043 0.7571 0.2569  0.1792  0.1068  130 TYR   B C   
1360 O  O   . TYR   B 121 ? 0.6611 0.7910 0.7454 0.2491  0.1783  0.1048  130 TYR   B O   
1361 C  CB  . TYR   B 121 ? 0.7403 0.8376 0.7854 0.2763  0.1663  0.0888  130 TYR   B CB  
1362 C  CG  . TYR   B 121 ? 0.7927 0.8832 0.8158 0.2958  0.1623  0.0863  130 TYR   B CG  
1363 C  CD1 . TYR   B 121 ? 0.8074 0.9013 0.8307 0.3029  0.1665  0.0930  130 TYR   B CD1 
1364 C  CD2 . TYR   B 121 ? 0.8308 0.9111 0.8321 0.3077  0.1538  0.0775  130 TYR   B CD2 
1365 C  CE1 . TYR   B 121 ? 0.8516 0.9393 0.8538 0.3216  0.1625  0.0906  130 TYR   B CE1 
1366 C  CE2 . TYR   B 121 ? 0.8705 0.9430 0.8501 0.3263  0.1490  0.0748  130 TYR   B CE2 
1367 C  CZ  . TYR   B 121 ? 0.8874 0.9640 0.8674 0.3334  0.1535  0.0813  130 TYR   B CZ  
1368 O  OH  . TYR   B 121 ? 0.9573 1.0264 0.9155 0.3522  0.1485  0.0785  130 TYR   B OH  
1369 N  N   . PRO   B 122 ? 0.6599 0.7859 0.7543 0.2473  0.1831  0.1119  131 PRO   B N   
1370 C  CA  . PRO   B 122 ? 0.6464 0.7739 0.7623 0.2276  0.1853  0.1142  131 PRO   B CA  
1371 C  C   . PRO   B 122 ? 0.6198 0.7310 0.7360 0.2156  0.1782  0.0995  131 PRO   B C   
1372 O  O   . PRO   B 122 ? 0.6156 0.7118 0.7187 0.2199  0.1716  0.0881  131 PRO   B O   
1373 C  CB  . PRO   B 122 ? 0.6596 0.7824 0.7857 0.2221  0.1881  0.1186  131 PRO   B CB  
1374 C  CG  . PRO   B 122 ? 0.6783 0.8026 0.7898 0.2403  0.1895  0.1221  131 PRO   B CG  
1375 C  CD  . PRO   B 122 ? 0.6883 0.8100 0.7784 0.2551  0.1845  0.1145  131 PRO   B CD  
1376 N  N   . ALA   B 123 ? 0.6006 0.7149 0.7322 0.2003  0.1792  0.1004  132 ALA   B N   
1377 C  CA  . ALA   B 123 ? 0.5715 0.6732 0.7050 0.1884  0.1733  0.0878  132 ALA   B CA  
1378 C  C   . ALA   B 123 ? 0.5514 0.6344 0.6832 0.1837  0.1687  0.0775  132 ALA   B C   
1379 O  O   . ALA   B 123 ? 0.5259 0.5973 0.6514 0.1805  0.1623  0.0657  132 ALA   B O   
1380 C  CB  . ALA   B 123 ? 0.5713 0.6801 0.7227 0.1732  0.1758  0.0921  132 ALA   B CB  
1381 N  N   . GLY   B 124 ? 0.5372 0.6180 0.6740 0.1841  0.1717  0.0821  133 GLY   B N   
1382 C  CA  . GLY   B 124 ? 0.5129 0.5778 0.6485 0.1808  0.1681  0.0738  133 GLY   B CA  
1383 C  C   . GLY   B 124 ? 0.5039 0.5594 0.6216 0.1922  0.1621  0.0653  133 GLY   B C   
1384 O  O   . GLY   B 124 ? 0.4885 0.5317 0.6052 0.1891  0.1583  0.0579  133 GLY   B O   
1385 N  N   . THR   B 125 ? 0.5017 0.5619 0.6051 0.2051  0.1605  0.0661  134 THR   B N   
1386 C  CA  . THR   B 125 ? 0.5227 0.5722 0.6073 0.2165  0.1531  0.0579  134 THR   B CA  
1387 C  C   . THR   B 125 ? 0.5125 0.5529 0.5926 0.2103  0.1455  0.0470  134 THR   B C   
1388 O  O   . THR   B 125 ? 0.5175 0.5466 0.5835 0.2168  0.1376  0.0394  134 THR   B O   
1389 C  CB  . THR   B 125 ? 0.5478 0.6054 0.6169 0.2353  0.1545  0.0640  134 THR   B CB  
1390 O  OG1 . THR   B 125 ? 0.5638 0.6337 0.6408 0.2388  0.1630  0.0763  134 THR   B OG1 
1391 C  CG2 . THR   B 125 ? 0.5589 0.6045 0.6085 0.2486  0.1472  0.0574  134 THR   B CG2 
1392 N  N   . SER   B 126 ? 0.4905 0.5351 0.5821 0.1980  0.1471  0.0465  135 SER   B N   
1393 C  CA  . SER   B 126 ? 0.4753 0.5124 0.5651 0.1904  0.1406  0.0370  135 SER   B CA  
1394 C  C   . SER   B 126 ? 0.4659 0.4885 0.5533 0.1861  0.1337  0.0279  135 SER   B C   
1395 O  O   . SER   B 126 ? 0.4632 0.4835 0.5615 0.1788  0.1363  0.0281  135 SER   B O   
1396 C  CB  . SER   B 126 ? 0.4664 0.5097 0.5715 0.1764  0.1440  0.0381  135 SER   B CB  
1397 O  OG  . SER   B 126 ? 0.4784 0.5362 0.5859 0.1796  0.1494  0.0466  135 SER   B OG  
1398 N  N   . GLY   B 127 ? 0.4610 0.4743 0.5352 0.1902  0.1250  0.0205  136 GLY   B N   
1399 C  CA  . GLY   B 127 ? 0.4703 0.4712 0.5432 0.1848  0.1175  0.0124  136 GLY   B CA  
1400 C  C   . GLY   B 127 ? 0.4841 0.4766 0.5421 0.1970  0.1115  0.0107  136 GLY   B C   
1401 O  O   . GLY   B 127 ? 0.4925 0.4747 0.5470 0.1939  0.1033  0.0043  136 GLY   B O   
1402 N  N   . SER   B 128 ? 0.4987 0.4962 0.5478 0.2108  0.1151  0.0168  137 SER   B N   
1403 C  CA  . SER   B 128 ? 0.5033 0.4932 0.5360 0.2250  0.1096  0.0157  137 SER   B CA  
1404 C  C   . SER   B 128 ? 0.5084 0.4858 0.5249 0.2291  0.0978  0.0079  137 SER   B C   
1405 O  O   . SER   B 128 ? 0.4978 0.4768 0.5085 0.2312  0.0966  0.0073  137 SER   B O   
1406 C  CB  . SER   B 128 ? 0.5230 0.5228 0.5492 0.2391  0.1164  0.0242  137 SER   B CB  
1407 O  OG  . SER   B 128 ? 0.5232 0.5315 0.5632 0.2355  0.1255  0.0313  137 SER   B OG  
1408 N  N   . PRO   B 129 ? 0.5080 0.4724 0.5166 0.2305  0.0882  0.0022  138 PRO   B N   
1409 C  CA  . PRO   B 129 ? 0.5196 0.4700 0.5130 0.2334  0.0752  -0.0048 138 PRO   B CA  
1410 C  C   . PRO   B 129 ? 0.5521 0.4970 0.5225 0.2521  0.0705  -0.0049 138 PRO   B C   
1411 O  O   . PRO   B 129 ? 0.5636 0.5116 0.5259 0.2656  0.0739  -0.0008 138 PRO   B O   
1412 C  CB  . PRO   B 129 ? 0.5213 0.4611 0.5155 0.2286  0.0667  -0.0093 138 PRO   B CB  
1413 C  CG  . PRO   B 129 ? 0.5142 0.4612 0.5156 0.2318  0.0748  -0.0042 138 PRO   B CG  
1414 C  CD  . PRO   B 129 ? 0.5043 0.4667 0.5189 0.2287  0.0886  0.0026  138 PRO   B CD  
1415 N  N   . ILE   B 130 ? 0.5634 0.4984 0.5221 0.2533  0.0613  -0.0101 139 ILE   B N   
1416 C  CA  . ILE   B 130 ? 0.5990 0.5238 0.5322 0.2709  0.0532  -0.0126 139 ILE   B CA  
1417 C  C   . ILE   B 130 ? 0.6193 0.5228 0.5402 0.2704  0.0366  -0.0205 139 ILE   B C   
1418 O  O   . ILE   B 130 ? 0.5922 0.4902 0.5226 0.2553  0.0308  -0.0244 139 ILE   B O   
1419 C  CB  . ILE   B 130 ? 0.6019 0.5312 0.5311 0.2726  0.0551  -0.0122 139 ILE   B CB  
1420 C  CG1 . ILE   B 130 ? 0.6015 0.5528 0.5441 0.2724  0.0708  -0.0034 139 ILE   B CG1 
1421 C  CG2 . ILE   B 130 ? 0.6303 0.5473 0.5317 0.2914  0.0457  -0.0156 139 ILE   B CG2 
1422 C  CD1 . ILE   B 130 ? 0.6017 0.5596 0.5519 0.2637  0.0737  -0.0033 139 ILE   B CD1 
1423 N  N   . LEU   B 131 ? 0.6634 0.5563 0.5644 0.2863  0.0294  -0.0222 140 LEU   B N   
1424 C  CA  . LEU   B 131 ? 0.7132 0.5857 0.6021 0.2871  0.0130  -0.0288 140 LEU   B CA  
1425 C  C   . LEU   B 131 ? 0.7397 0.5937 0.6002 0.3023  -0.0004 -0.0342 140 LEU   B C   
1426 O  O   . LEU   B 131 ? 0.7808 0.6388 0.6262 0.3200  0.0041  -0.0319 140 LEU   B O   
1427 C  CB  . LEU   B 131 ? 0.7345 0.6083 0.6223 0.2943  0.0148  -0.0266 140 LEU   B CB  
1428 C  CG  . LEU   B 131 ? 0.7216 0.6140 0.6336 0.2843  0.0296  -0.0203 140 LEU   B CG  
1429 C  CD1 . LEU   B 131 ? 0.7243 0.6158 0.6334 0.2919  0.0297  -0.0187 140 LEU   B CD1 
1430 C  CD2 . LEU   B 131 ? 0.7137 0.6085 0.6469 0.2628  0.0295  -0.0218 140 LEU   B CD2 
1431 N  N   . ASP   B 132 ? 0.7590 0.5931 0.6119 0.2966  -0.0170 -0.0408 141 ASP   B N   
1432 C  CA  . ASP   B 132 ? 0.8098 0.6202 0.6334 0.3109  -0.0341 -0.0472 141 ASP   B CA  
1433 C  C   . ASP   B 132 ? 0.8595 0.6593 0.6717 0.3203  -0.0423 -0.0490 141 ASP   B C   
1434 O  O   . ASP   B 132 ? 0.8302 0.6421 0.6588 0.3143  -0.0341 -0.0450 141 ASP   B O   
1435 C  CB  . ASP   B 132 ? 0.7941 0.5870 0.6151 0.2992  -0.0492 -0.0527 141 ASP   B CB  
1436 C  CG  . ASP   B 132 ? 0.7950 0.5822 0.6310 0.2811  -0.0581 -0.0539 141 ASP   B CG  
1437 O  OD1 . ASP   B 132 ? 0.7789 0.5719 0.6234 0.2796  -0.0552 -0.0518 141 ASP   B OD1 
1438 O  OD2 . ASP   B 132 ? 0.8238 0.6022 0.6639 0.2681  -0.0676 -0.0563 141 ASP   B OD2 
1439 N  N   . LYS   B 133 ? 0.9114 0.6882 0.6959 0.3343  -0.0587 -0.0550 142 LYS   B N   
1440 C  CA  . LYS   B 133 ? 0.9730 0.7382 0.7399 0.3490  -0.0671 -0.0572 142 LYS   B CA  
1441 C  C   . LYS   B 133 ? 0.9503 0.7114 0.7326 0.3328  -0.0746 -0.0579 142 LYS   B C   
1442 O  O   . LYS   B 133 ? 0.9276 0.6880 0.7057 0.3402  -0.0755 -0.0574 142 LYS   B O   
1443 C  CB  . LYS   B 133 ? 1.0336 0.7734 0.7656 0.3681  -0.0839 -0.0642 142 LYS   B CB  
1444 C  CG  . LYS   B 133 ? 1.0752 0.8228 0.7895 0.3900  -0.0744 -0.0621 142 LYS   B CG  
1445 C  CD  . LYS   B 133 ? 1.1449 0.8696 0.8276 0.4057  -0.0889 -0.0689 142 LYS   B CD  
1446 C  CE  . LYS   B 133 ? 1.1699 0.9060 0.8352 0.4295  -0.0781 -0.0657 142 LYS   B CE  
1447 N  NZ  . LYS   B 133 ? 1.2238 0.9366 0.8555 0.4476  -0.0927 -0.0727 142 LYS   B NZ  
1448 N  N   . CYS   B 134 ? 0.9375 0.6985 0.7381 0.3115  -0.0784 -0.0582 143 CYS   B N   
1449 C  CA  . CYS   B 134 ? 0.9160 0.6748 0.7324 0.2951  -0.0861 -0.0581 143 CYS   B CA  
1450 C  C   . CYS   B 134 ? 0.8662 0.6506 0.7118 0.2827  -0.0680 -0.0517 143 CYS   B C   
1451 O  O   . CYS   B 134 ? 0.8721 0.6592 0.7343 0.2677  -0.0716 -0.0505 143 CYS   B O   
1452 C  CB  . CYS   B 134 ? 0.9520 0.6975 0.7717 0.2796  -0.1005 -0.0610 143 CYS   B CB  
1453 S  SG  . CYS   B 134 ? 1.0214 0.7316 0.8062 0.2924  -0.1263 -0.0691 143 CYS   B SG  
1454 N  N   . GLY   B 135 ? 0.8361 0.6386 0.6873 0.2892  -0.0497 -0.0472 144 GLY   B N   
1455 C  CA  . GLY   B 135 ? 0.8001 0.6255 0.6782 0.2777  -0.0325 -0.0412 144 GLY   B CA  
1456 C  C   . GLY   B 135 ? 0.7567 0.5918 0.6566 0.2580  -0.0274 -0.0399 144 GLY   B C   
1457 O  O   . GLY   B 135 ? 0.7131 0.5650 0.6344 0.2481  -0.0147 -0.0356 144 GLY   B O   
1458 N  N   . ARG   B 136 ? 0.7649 0.5903 0.6595 0.2530  -0.0359 -0.0432 145 ARG   B N   
1459 C  CA  . ARG   B 136 ? 0.7378 0.5727 0.6525 0.2346  -0.0312 -0.0419 145 ARG   B CA  
1460 C  C   . ARG   B 136 ? 0.6967 0.5475 0.6185 0.2360  -0.0148 -0.0386 145 ARG   B C   
1461 O  O   . ARG   B 136 ? 0.7026 0.5512 0.6077 0.2513  -0.0127 -0.0388 145 ARG   B O   
1462 C  CB  . ARG   B 136 ? 0.7802 0.5979 0.6867 0.2281  -0.0481 -0.0462 145 ARG   B CB  
1463 C  CG  . ARG   B 136 ? 0.8270 0.6355 0.7377 0.2186  -0.0621 -0.0471 145 ARG   B CG  
1464 C  CD  . ARG   B 136 ? 0.8815 0.6727 0.7844 0.2116  -0.0792 -0.0503 145 ARG   B CD  
1465 N  NE  . ARG   B 136 ? 0.9513 0.7231 0.8255 0.2292  -0.0885 -0.0551 145 ARG   B NE  
1466 C  CZ  . ARG   B 136 ? 1.0107 0.7680 0.8707 0.2316  -0.0978 -0.0586 145 ARG   B CZ  
1467 N  NH1 . ARG   B 136 ? 1.0559 0.8156 0.9281 0.2163  -0.0993 -0.0576 145 ARG   B NH1 
1468 N  NH2 . ARG   B 136 ? 1.0516 0.7918 0.8838 0.2503  -0.1055 -0.0630 145 ARG   B NH2 
1469 N  N   . VAL   B 137 ? 0.6481 0.5149 0.5931 0.2215  -0.0037 -0.0354 146 VAL   B N   
1470 C  CA  . VAL   B 137 ? 0.6202 0.5024 0.5737 0.2213  0.0113  -0.0319 146 VAL   B CA  
1471 C  C   . VAL   B 137 ? 0.6161 0.4928 0.5639 0.2182  0.0064  -0.0346 146 VAL   B C   
1472 O  O   . VAL   B 137 ? 0.6064 0.4804 0.5632 0.2043  0.0006  -0.0365 146 VAL   B O   
1473 C  CB  . VAL   B 137 ? 0.5936 0.4929 0.5719 0.2083  0.0243  -0.0279 146 VAL   B CB  
1474 C  CG1 . VAL   B 137 ? 0.5816 0.4950 0.5674 0.2082  0.0380  -0.0242 146 VAL   B CG1 
1475 C  CG2 . VAL   B 137 ? 0.6071 0.5106 0.5905 0.2113  0.0284  -0.0253 146 VAL   B CG2 
1476 N  N   . ILE   B 138 ? 0.6144 0.4908 0.5479 0.2313  0.0090  -0.0344 147 ILE   B N   
1477 C  CA  . ILE   B 138 ? 0.6144 0.4854 0.5399 0.2311  0.0047  -0.0369 147 ILE   B CA  
1478 C  C   . ILE   B 138 ? 0.5962 0.4865 0.5376 0.2247  0.0198  -0.0327 147 ILE   B C   
1479 O  O   . ILE   B 138 ? 0.5854 0.4748 0.5227 0.2239  0.0186  -0.0340 147 ILE   B O   
1480 C  CB  . ILE   B 138 ? 0.6356 0.4934 0.5331 0.2511  -0.0029 -0.0395 147 ILE   B CB  
1481 C  CG1 . ILE   B 138 ? 0.6363 0.5074 0.5295 0.2663  0.0095  -0.0343 147 ILE   B CG1 
1482 C  CG2 . ILE   B 138 ? 0.6548 0.4906 0.5361 0.2556  -0.0203 -0.0445 147 ILE   B CG2 
1483 C  CD1 . ILE   B 138 ? 0.6708 0.5341 0.5377 0.2870  0.0051  -0.0357 147 ILE   B CD1 
1484 N  N   . GLY   B 139 ? 0.5632 0.4696 0.5217 0.2204  0.0329  -0.0277 148 GLY   B N   
1485 C  CA  . GLY   B 139 ? 0.5471 0.4707 0.5227 0.2119  0.0460  -0.0237 148 GLY   B CA  
1486 C  C   . GLY   B 139 ? 0.5391 0.4775 0.5257 0.2143  0.0592  -0.0173 148 GLY   B C   
1487 O  O   . GLY   B 139 ? 0.5415 0.4769 0.5216 0.2231  0.0584  -0.0161 148 GLY   B O   
1488 N  N   . LEU   B 140 ? 0.5389 0.4922 0.5411 0.2067  0.0704  -0.0132 149 LEU   B N   
1489 C  CA  . LEU   B 140 ? 0.5290 0.4962 0.5438 0.2067  0.0827  -0.0063 149 LEU   B CA  
1490 C  C   . LEU   B 140 ? 0.5398 0.5195 0.5523 0.2148  0.0909  -0.0002 149 LEU   B C   
1491 O  O   . LEU   B 140 ? 0.5395 0.5202 0.5481 0.2143  0.0893  -0.0016 149 LEU   B O   
1492 C  CB  . LEU   B 140 ? 0.5190 0.4925 0.5554 0.1898  0.0883  -0.0061 149 LEU   B CB  
1493 C  CG  . LEU   B 140 ? 0.5183 0.4831 0.5598 0.1807  0.0815  -0.0110 149 LEU   B CG  
1494 C  CD1 . LEU   B 140 ? 0.5006 0.4736 0.5623 0.1668  0.0887  -0.0100 149 LEU   B CD1 
1495 C  CD2 . LEU   B 140 ? 0.5280 0.4858 0.5609 0.1896  0.0773  -0.0111 149 LEU   B CD2 
1496 N  N   . TYR   B 141 ? 0.5319 0.5209 0.5463 0.2225  0.0989  0.0067  150 TYR   B N   
1497 C  CA  . TYR   B 141 ? 0.5457 0.5495 0.5585 0.2321  0.1074  0.0150  150 TYR   B CA  
1498 C  C   . TYR   B 141 ? 0.5331 0.5510 0.5685 0.2188  0.1177  0.0210  150 TYR   B C   
1499 O  O   . TYR   B 141 ? 0.5205 0.5374 0.5682 0.2098  0.1201  0.0211  150 TYR   B O   
1500 C  CB  . TYR   B 141 ? 0.5730 0.5783 0.5736 0.2490  0.1090  0.0197  150 TYR   B CB  
1501 C  CG  . TYR   B 141 ? 0.5678 0.5919 0.5716 0.2576  0.1199  0.0311  150 TYR   B CG  
1502 C  CD1 . TYR   B 141 ? 0.5638 0.5985 0.5841 0.2521  0.1291  0.0389  150 TYR   B CD1 
1503 C  CD2 . TYR   B 141 ? 0.5787 0.6102 0.5687 0.2723  0.1209  0.0348  150 TYR   B CD2 
1504 C  CE1 . TYR   B 141 ? 0.5713 0.6240 0.5954 0.2596  0.1387  0.0507  150 TYR   B CE1 
1505 C  CE2 . TYR   B 141 ? 0.5794 0.6306 0.5728 0.2810  0.1311  0.0467  150 TYR   B CE2 
1506 C  CZ  . TYR   B 141 ? 0.5820 0.6444 0.5934 0.2739  0.1400  0.0552  150 TYR   B CZ  
1507 O  OH  . TYR   B 141 ? 0.5822 0.6649 0.5985 0.2814  0.1498  0.0684  150 TYR   B OH  
1508 N  N   . GLY   B 142 ? 0.5433 0.5741 0.5830 0.2186  0.1233  0.0262  151 GLY   B N   
1509 C  CA  . GLY   B 142 ? 0.5410 0.5854 0.6015 0.2070  0.1326  0.0332  151 GLY   B CA  
1510 C  C   . GLY   B 142 ? 0.5353 0.5853 0.6046 0.1963  0.1335  0.0321  151 GLY   B C   
1511 O  O   . GLY   B 142 ? 0.5226 0.5821 0.6093 0.1857  0.1400  0.0373  151 GLY   B O   
1512 N  N   . ASN   B 143 ? 0.5294 0.5729 0.5874 0.1986  0.1268  0.0257  152 ASN   B N   
1513 C  CA  . ASN   B 143 ? 0.5200 0.5712 0.5841 0.1916  0.1283  0.0259  152 ASN   B CA  
1514 C  C   . ASN   B 143 ? 0.5271 0.5827 0.5744 0.2067  0.1267  0.0278  152 ASN   B C   
1515 O  O   . ASN   B 143 ? 0.5359 0.5784 0.5654 0.2154  0.1185  0.0213  152 ASN   B O   
1516 C  CB  . ASN   B 143 ? 0.5121 0.5527 0.5804 0.1784  0.1222  0.0166  152 ASN   B CB  
1517 C  CG  . ASN   B 143 ? 0.5068 0.5569 0.5846 0.1695  0.1251  0.0177  152 ASN   B CG  
1518 O  OD1 . ASN   B 143 ? 0.5071 0.5721 0.5959 0.1674  0.1327  0.0257  152 ASN   B OD1 
1519 N  ND2 . ASN   B 143 ? 0.4980 0.5398 0.5723 0.1639  0.1189  0.0102  152 ASN   B ND2 
1520 N  N   . GLY   B 144 ? 0.5416 0.6151 0.5946 0.2095  0.1341  0.0367  153 GLY   B N   
1521 C  CA  . GLY   B 144 ? 0.5847 0.6651 0.6222 0.2248  0.1337  0.0396  153 GLY   B CA  
1522 C  C   . GLY   B 144 ? 0.5992 0.7030 0.6485 0.2243  0.1428  0.0510  153 GLY   B C   
1523 O  O   . GLY   B 144 ? 0.5608 0.6717 0.6291 0.2085  0.1464  0.0529  153 GLY   B O   
1524 N  N   A VAL   B 145 ? 0.6211 0.7374 0.6595 0.2417  0.1465  0.0590  154 VAL   B N   
1525 N  N   B VAL   B 145 ? 0.6210 0.7373 0.6594 0.2417  0.1465  0.0590  154 VAL   B N   
1526 N  N   C VAL   B 145 ? 0.6309 0.7475 0.6696 0.2415  0.1465  0.0591  154 VAL   B N   
1527 N  N   D VAL   B 145 ? 0.6308 0.7474 0.6695 0.2415  0.1465  0.0591  154 VAL   B N   
1528 C  CA  A VAL   B 145 ? 0.6347 0.7754 0.6787 0.2463  0.1539  0.0705  154 VAL   B CA  
1529 C  CA  B VAL   B 145 ? 0.6343 0.7750 0.6783 0.2463  0.1539  0.0705  154 VAL   B CA  
1530 C  CA  C VAL   B 145 ? 0.6498 0.7906 0.6955 0.2446  0.1540  0.0703  154 VAL   B CA  
1531 C  CA  D VAL   B 145 ? 0.6495 0.7903 0.6952 0.2446  0.1540  0.0703  154 VAL   B CA  
1532 C  C   A VAL   B 145 ? 0.6586 0.8164 0.7045 0.2574  0.1618  0.0837  154 VAL   B C   
1533 C  C   B VAL   B 145 ? 0.6585 0.8164 0.7045 0.2574  0.1618  0.0837  154 VAL   B C   
1534 C  C   C VAL   B 145 ? 0.6958 0.8541 0.7402 0.2584  0.1614  0.0834  154 VAL   B C   
1535 C  C   D VAL   B 145 ? 0.6961 0.8543 0.7405 0.2584  0.1614  0.0834  154 VAL   B C   
1536 O  O   A VAL   B 145 ? 0.6663 0.8147 0.7010 0.2672  0.1599  0.0819  154 VAL   B O   
1537 O  O   B VAL   B 145 ? 0.6659 0.8143 0.7006 0.2672  0.1599  0.0819  154 VAL   B O   
1538 O  O   C VAL   B 145 ? 0.7048 0.8538 0.7357 0.2702  0.1593  0.0815  154 VAL   B O   
1539 O  O   D VAL   B 145 ? 0.7047 0.8538 0.7357 0.2701  0.1593  0.0815  154 VAL   B O   
1540 C  CB  A VAL   B 145 ? 0.6445 0.7838 0.6684 0.2600  0.1493  0.0665  154 VAL   B CB  
1541 C  CB  B VAL   B 145 ? 0.6441 0.7833 0.6680 0.2600  0.1493  0.0665  154 VAL   B CB  
1542 C  CB  C VAL   B 145 ? 0.6521 0.7911 0.6815 0.2538  0.1492  0.0655  154 VAL   B CB  
1543 C  CB  D VAL   B 145 ? 0.6518 0.7908 0.6812 0.2538  0.1492  0.0655  154 VAL   B CB  
1544 C  CG1 A VAL   B 145 ? 0.6468 0.8126 0.6745 0.2673  0.1569  0.0788  154 VAL   B CG1 
1545 C  CG1 B VAL   B 145 ? 0.6467 0.8125 0.6744 0.2673  0.1569  0.0788  154 VAL   B CG1 
1546 C  CG1 C VAL   B 145 ? 0.6620 0.8015 0.6666 0.2783  0.1476  0.0671  154 VAL   B CG1 
1547 C  CG1 D VAL   B 145 ? 0.6612 0.8007 0.6657 0.2783  0.1475  0.0671  154 VAL   B CG1 
1548 C  CG2 A VAL   B 145 ? 0.6385 0.7611 0.6611 0.2486  0.1414  0.0543  154 VAL   B CG2 
1549 C  CG2 B VAL   B 145 ? 0.6382 0.7608 0.6607 0.2486  0.1414  0.0543  154 VAL   B CG2 
1550 C  CG2 C VAL   B 145 ? 0.6454 0.8038 0.6888 0.2460  0.1545  0.0723  154 VAL   B CG2 
1551 C  CG2 D VAL   B 145 ? 0.6454 0.8038 0.6888 0.2460  0.1545  0.0722  154 VAL   B CG2 
1552 N  N   A VAL   B 146 ? 0.6776 0.8604 0.7376 0.2557  0.1701  0.0971  155 VAL   B N   
1553 N  N   B VAL   B 146 ? 0.6778 0.8606 0.7378 0.2557  0.1701  0.0971  155 VAL   B N   
1554 N  N   C VAL   B 146 ? 0.7363 0.9195 0.7945 0.2568  0.1697  0.0966  155 VAL   B N   
1555 N  N   D VAL   B 146 ? 0.7368 0.9201 0.7951 0.2568  0.1697  0.0966  155 VAL   B N   
1556 C  CA  A VAL   B 146 ? 0.7014 0.9060 0.7635 0.2677  0.1784  0.1125  155 VAL   B CA  
1557 C  CA  B VAL   B 146 ? 0.7013 0.9059 0.7634 0.2677  0.1784  0.1125  155 VAL   B CA  
1558 C  CA  C VAL   B 146 ? 0.7707 0.9765 0.8283 0.2712  0.1777  0.1118  155 VAL   B CA  
1559 C  CA  D VAL   B 146 ? 0.7707 0.9765 0.8283 0.2712  0.1777  0.1118  155 VAL   B CA  
1560 C  C   A VAL   B 146 ? 0.7306 0.9546 0.7817 0.2840  0.1813  0.1198  155 VAL   B C   
1561 C  C   B VAL   B 146 ? 0.7303 0.9544 0.7814 0.2840  0.1813  0.1198  155 VAL   B C   
1562 C  C   C VAL   B 146 ? 0.8199 1.0402 0.8631 0.2879  0.1787  0.1158  155 VAL   B C   
1563 C  C   D VAL   B 146 ? 0.8204 1.0407 0.8635 0.2879  0.1787  0.1158  155 VAL   B C   
1564 O  O   A VAL   B 146 ? 0.7248 0.9671 0.7906 0.2760  0.1855  0.1275  155 VAL   B O   
1565 O  O   B VAL   B 146 ? 0.7248 0.9671 0.7906 0.2760  0.1855  0.1275  155 VAL   B O   
1566 O  O   C VAL   B 146 ? 0.8320 1.0567 0.8807 0.2801  0.1778  0.1140  155 VAL   B O   
1567 O  O   D VAL   B 146 ? 0.8332 1.0578 0.8818 0.2801  0.1777  0.1140  155 VAL   B O   
1568 C  CB  A VAL   B 146 ? 0.6876 0.9067 0.7773 0.2513  0.1854  0.1241  155 VAL   B CB  
1569 C  CB  B VAL   B 146 ? 0.6874 0.9065 0.7770 0.2513  0.1854  0.1241  155 VAL   B CB  
1570 C  CB  C VAL   B 146 ? 0.7609 0.9853 0.8456 0.2568  0.1857  0.1253  155 VAL   B CB  
1571 C  CB  D VAL   B 146 ? 0.7608 0.9853 0.8456 0.2568  0.1857  0.1253  155 VAL   B CB  
1572 C  CG1 A VAL   B 146 ? 0.6933 0.9375 0.7869 0.2627  0.1940  0.1418  155 VAL   B CG1 
1573 C  CG1 B VAL   B 146 ? 0.6930 0.9371 0.7866 0.2627  0.1940  0.1418  155 VAL   B CG1 
1574 C  CG1 C VAL   B 146 ? 0.7752 1.0243 0.8608 0.2708  0.1939  0.1423  155 VAL   B CG1 
1575 C  CG1 D VAL   B 146 ? 0.7756 1.0247 0.8612 0.2708  0.1939  0.1423  155 VAL   B CG1 
1576 C  CG2 A VAL   B 146 ? 0.6793 0.8788 0.7779 0.2372  0.1825  0.1168  155 VAL   B CG2 
1577 C  CG2 B VAL   B 146 ? 0.6789 0.8784 0.7775 0.2372  0.1825  0.1168  155 VAL   B CG2 
1578 C  CG2 C VAL   B 146 ? 0.7553 0.9629 0.8524 0.2409  0.1838  0.1200  155 VAL   B CG2 
1579 C  CG2 D VAL   B 146 ? 0.7555 0.9631 0.8526 0.2409  0.1838  0.1200  155 VAL   B CG2 
1580 N  N   A ILE   B 147 ? 0.7758 0.9960 0.8017 0.3066  0.1788  0.1176  156 ILE   B N   
1581 N  N   B ILE   B 147 ? 0.7757 0.9960 0.8016 0.3066  0.1788  0.1176  156 ILE   B N   
1582 N  N   C ILE   B 147 ? 0.8714 1.0976 0.8952 0.3108  0.1800  0.1202  156 ILE   B N   
1583 N  N   D ILE   B 147 ? 0.8716 1.0979 0.8954 0.3108  0.1801  0.1202  156 ILE   B N   
1584 C  CA  A ILE   B 147 ? 0.8100 1.0419 0.8181 0.3254  0.1790  0.1202  156 ILE   B CA  
1585 C  CA  B ILE   B 147 ? 0.8098 1.0418 0.8180 0.3254  0.1790  0.1202  156 ILE   B CA  
1586 C  CA  C ILE   B 147 ? 0.9081 1.1427 0.9111 0.3311  0.1791  0.1210  156 ILE   B CA  
1587 C  CA  D ILE   B 147 ? 0.9078 1.1424 0.9108 0.3310  0.1791  0.1210  156 ILE   B CA  
1588 C  C   A ILE   B 147 ? 0.8274 1.0948 0.8463 0.3330  0.1900  0.1398  156 ILE   B C   
1589 C  C   B ILE   B 147 ? 0.8272 1.0946 0.8460 0.3330  0.1900  0.1398  156 ILE   B C   
1590 C  C   C ILE   B 147 ? 0.9303 1.2005 0.9420 0.3402  0.1899  0.1403  156 ILE   B C   
1591 C  C   D ILE   B 147 ? 0.9302 1.2004 0.9419 0.3402  0.1899  0.1403  156 ILE   B C   
1592 O  O   A ILE   B 147 ? 0.8181 1.0978 0.8555 0.3250  0.1964  0.1508  156 ILE   B O   
1593 O  O   B ILE   B 147 ? 0.8175 1.0972 0.8548 0.3250  0.1964  0.1508  156 ILE   B O   
1594 O  O   C ILE   B 147 ? 0.9040 1.1894 0.9366 0.3309  0.1970  0.1523  156 ILE   B O   
1595 O  O   D ILE   B 147 ? 0.9030 1.1884 0.9355 0.3310  0.1970  0.1523  156 ILE   B O   
1596 C  CB  A ILE   B 147 ? 0.8378 1.0513 0.8137 0.3478  0.1716  0.1108  156 ILE   B CB  
1597 C  CB  B ILE   B 147 ? 0.8379 1.0514 0.8138 0.3478  0.1716  0.1108  156 ILE   B CB  
1598 C  CB  C ILE   B 147 ? 0.9468 1.1612 0.9184 0.3523  0.1715  0.1112  156 ILE   B CB  
1599 C  CB  D ILE   B 147 ? 0.9471 1.1614 0.9187 0.3523  0.1715  0.1112  156 ILE   B CB  
1600 C  CG1 A ILE   B 147 ? 0.8556 1.0679 0.8250 0.3590  0.1737  0.1149  156 ILE   B CG1 
1601 C  CG1 B ILE   B 147 ? 0.8567 1.0690 0.8261 0.3590  0.1737  0.1149  156 ILE   B CG1 
1602 C  CG1 C ILE   B 147 ? 0.9746 1.1891 0.9425 0.3616  0.1743  0.1161  156 ILE   B CG1 
1603 C  CG1 D ILE   B 147 ? 0.9758 1.1903 0.9436 0.3617  0.1743  0.1161  156 ILE   B CG1 
1604 C  CG2 A ILE   B 147 ? 0.8402 1.0219 0.8055 0.3401  0.1597  0.0925  156 ILE   B CG2 
1605 C  CG2 B ILE   B 147 ? 0.8407 1.0224 0.8060 0.3401  0.1597  0.0925  156 ILE   B CG2 
1606 C  CG2 C ILE   B 147 ? 0.9497 1.1316 0.9115 0.3438  0.1596  0.0929  156 ILE   B CG2 
1607 C  CG2 D ILE   B 147 ? 0.9502 1.1321 0.9120 0.3437  0.1596  0.0929  156 ILE   B CG2 
1608 C  CD1 A ILE   B 147 ? 0.8818 1.0815 0.8182 0.3848  0.1674  0.1086  156 ILE   B CD1 
1609 C  CD1 B ILE   B 147 ? 0.8830 1.0826 0.8193 0.3848  0.1673  0.1086  156 ILE   B CD1 
1610 C  CD1 C ILE   B 147 ? 0.9993 1.2055 0.9351 0.3891  0.1696  0.1124  156 ILE   B CD1 
1611 C  CD1 D ILE   B 147 ? 1.0002 1.2062 0.9358 0.3891  0.1696  0.1123  156 ILE   B CD1 
1612 N  N   A LYS   B 148 ? 0.8627 1.1458 0.8700 0.3479  0.1917  0.1444  157 LYS   B N   
1613 N  N   B LYS   B 148 ? 0.8631 1.1462 0.8704 0.3479  0.1917  0.1444  157 LYS   B N   
1614 N  N   C LYS   B 148 ? 0.9726 1.2557 0.9686 0.3582  0.1907  0.1435  157 LYS   B N   
1615 N  N   D LYS   B 148 ? 0.9728 1.2558 0.9687 0.3582  0.1907  0.1435  157 LYS   B N   
1616 C  CA  A LYS   B 148 ? 0.8804 1.2007 0.8969 0.3565  0.2019  0.1638  157 LYS   B CA  
1617 C  CA  B LYS   B 148 ? 0.8804 1.2008 0.8970 0.3565  0.2019  0.1638  157 LYS   B CA  
1618 C  CA  C LYS   B 148 ? 0.9987 1.3189 1.0024 0.3678  0.2007  0.1623  157 LYS   B CA  
1619 C  CA  D LYS   B 148 ? 0.9990 1.3193 1.0027 0.3677  0.2007  0.1623  157 LYS   B CA  
1620 C  C   A LYS   B 148 ? 0.8945 1.2302 0.9207 0.3600  0.2094  0.1778  157 LYS   B C   
1621 C  C   B LYS   B 148 ? 0.8946 1.2302 0.9208 0.3600  0.2094  0.1778  157 LYS   B C   
1622 C  C   C LYS   B 148 ? 1.0030 1.3414 1.0116 0.3769  0.2087  0.1770  157 LYS   B C   
1623 C  C   D LYS   B 148 ? 1.0030 1.3414 1.0116 0.3769  0.2086  0.1770  157 LYS   B C   
1624 O  O   A LYS   B 148 ? 0.8776 1.2340 0.9306 0.3454  0.2163  0.1916  157 LYS   B O   
1625 O  O   B LYS   B 148 ? 0.8768 1.2330 0.9299 0.3452  0.2162  0.1915  157 LYS   B O   
1626 O  O   C LYS   B 148 ? 1.0054 1.3770 1.0239 0.3830  0.2175  0.1948  157 LYS   B O   
1627 O  O   D LYS   B 148 ? 1.0053 1.3769 1.0237 0.3830  0.2175  0.1947  157 LYS   B O   
1628 C  CB  A LYS   B 148 ? 0.9074 1.2363 0.8974 0.3833  0.2014  0.1646  157 LYS   B CB  
1629 C  CB  B LYS   B 148 ? 0.9080 1.2369 0.8979 0.3833  0.2014  0.1646  157 LYS   B CB  
1630 C  CB  C LYS   B 148 ? 1.0393 1.3660 1.0177 0.3914  0.1991  0.1612  157 LYS   B CB  
1631 C  CB  D LYS   B 148 ? 1.0403 1.3669 1.0186 0.3914  0.1991  0.1612  157 LYS   B CB  
1632 C  CG  A LYS   B 148 ? 0.9120 1.2282 0.8907 0.3826  0.1943  0.1526  157 LYS   B CG  
1633 C  CG  B LYS   B 148 ? 0.9124 1.2286 0.8910 0.3826  0.1943  0.1526  157 LYS   B CG  
1634 C  CG  C LYS   B 148 ? 1.0765 1.3825 1.0205 0.4159  0.1924  0.1511  157 LYS   B CG  
1635 C  CG  D LYS   B 148 ? 1.0776 1.3836 1.0216 0.4159  0.1924  0.1511  157 LYS   B CG  
1636 C  CD  A LYS   B 148 ? 0.9349 1.2603 0.8867 0.4104  0.1940  0.1542  157 LYS   B CD  
1637 C  CD  B LYS   B 148 ? 0.9352 1.2606 0.8869 0.4104  0.1940  0.1542  157 LYS   B CD  
1638 C  CD  C LYS   B 148 ? 1.1002 1.4258 1.0216 0.4456  0.1958  0.1591  157 LYS   B CD  
1639 C  CD  D LYS   B 148 ? 1.1008 1.4264 1.0222 0.4457  0.1958  0.1591  157 LYS   B CD  
1640 C  CE  A LYS   B 148 ? 0.9426 1.2493 0.8795 0.4107  0.1853  0.1401  157 LYS   B CE  
1641 C  CE  B LYS   B 148 ? 0.9431 1.2496 0.8799 0.4107  0.1852  0.1401  157 LYS   B CE  
1642 C  CE  C LYS   B 148 ? 1.1196 1.4569 1.0298 0.4664  0.2009  0.1687  157 LYS   B CE  
1643 C  CE  D LYS   B 148 ? 1.1201 1.4574 1.0303 0.4665  0.2009  0.1687  157 LYS   B CE  
1644 N  NZ  A LYS   B 148 ? 0.9592 1.2863 0.8808 0.4321  0.1882  0.1470  157 LYS   B NZ  
1645 N  NZ  B LYS   B 148 ? 0.9600 1.2871 0.8815 0.4321  0.1882  0.1470  157 LYS   B NZ  
1646 N  NZ  C LYS   B 148 ? 1.1126 1.4800 1.0520 0.4559  0.2125  0.1877  157 LYS   B NZ  
1647 N  NZ  D LYS   B 148 ? 1.1134 1.4808 1.0527 0.4560  0.2125  0.1877  157 LYS   B NZ  
1648 N  N   A ASN   B 149 ? 0.9269 1.2509 0.9317 0.3781  0.2073  0.1738  158 ASN   B N   
1649 N  N   B ASN   B 149 ? 0.9272 1.2513 0.9321 0.3781  0.2073  0.1738  158 ASN   B N   
1650 N  N   C ASN   B 149 ? 1.0158 1.3345 1.0179 0.3780  0.2056  0.1706  158 ASN   B N   
1651 N  N   D ASN   B 149 ? 1.0165 1.3351 1.0186 0.3780  0.2056  0.1707  158 ASN   B N   
1652 C  CA  A ASN   B 149 ? 0.9444 1.2834 0.9516 0.3881  0.2143  0.1870  158 ASN   B CA  
1653 C  CA  B ASN   B 149 ? 0.9446 1.2837 0.9519 0.3881  0.2143  0.1870  158 ASN   B CA  
1654 C  CA  C ASN   B 149 ? 1.0187 1.3506 1.0216 0.3887  0.2122  0.1829  158 ASN   B CA  
1655 C  CA  D ASN   B 149 ? 1.0193 1.3512 1.0222 0.3886  0.2122  0.1829  158 ASN   B CA  
1656 C  C   A ASN   B 149 ? 0.9340 1.2635 0.9637 0.3663  0.2151  0.1875  158 ASN   B C   
1657 C  C   B ASN   B 149 ? 0.9339 1.2634 0.9636 0.3663  0.2151  0.1875  158 ASN   B C   
1658 C  C   C ASN   B 149 ? 0.9731 1.3065 1.0049 0.3656  0.2160  0.1892  158 ASN   B C   
1659 C  C   D ASN   B 149 ? 0.9731 1.3065 1.0049 0.3656  0.2160  0.1892  158 ASN   B C   
1660 O  O   A ASN   B 149 ? 0.9386 1.2745 0.9689 0.3733  0.2196  0.1959  158 ASN   B O   
1661 O  O   B ASN   B 149 ? 0.9379 1.2738 0.9682 0.3733  0.2196  0.1958  158 ASN   B O   
1662 O  O   C ASN   B 149 ? 0.9740 1.3260 1.0136 0.3709  0.2234  0.2040  158 ASN   B O   
1663 O  O   D ASN   B 149 ? 0.9738 1.3259 1.0134 0.3709  0.2234  0.2040  158 ASN   B O   
1664 C  CB  A ASN   B 149 ? 0.9725 1.2991 0.9472 0.4151  0.2104  0.1805  158 ASN   B CB  
1665 C  CB  B ASN   B 149 ? 0.9729 1.2996 0.9477 0.4151  0.2104  0.1806  158 ASN   B CB  
1666 C  CB  C ASN   B 149 ? 1.0572 1.3656 1.0316 0.4074  0.2058  0.1716  158 ASN   B CB  
1667 C  CB  D ASN   B 149 ? 1.0582 1.3666 1.0325 0.4074  0.2058  0.1716  158 ASN   B CB  
1668 C  CG  A ASN   B 149 ? 0.9824 1.2691 0.9393 0.4127  0.1981  0.1587  158 ASN   B CG  
1669 C  CG  B ASN   B 149 ? 0.9830 1.2698 0.9400 0.4127  0.1981  0.1588  158 ASN   B CG  
1670 C  CG  C ASN   B 149 ? 1.0865 1.3852 1.0287 0.4302  0.1992  0.1622  158 ASN   B CG  
1671 C  CG  D ASN   B 149 ? 1.0873 1.3860 1.0295 0.4302  0.1992  0.1622  158 ASN   B CG  
1672 O  OD1 A ASN   B 149 ? 0.9915 1.2631 0.9387 0.4106  0.1907  0.1468  158 ASN   B OD1 
1673 O  OD1 B ASN   B 149 ? 0.9929 1.2645 0.9401 0.4106  0.1907  0.1468  158 ASN   B OD1 
1674 O  OD1 C ASN   B 149 ? 1.1007 1.4050 1.0410 0.4301  0.1982  0.1608  158 ASN   B OD1 
1675 O  OD1 D ASN   B 149 ? 1.1019 1.4062 1.0422 0.4301  0.1981  0.1608  158 ASN   B OD1 
1676 N  ND2 A ASN   B 149 ? 0.9855 1.2557 0.9384 0.4130  0.1954  0.1540  158 ASN   B ND2 
1677 N  ND2 B ASN   B 149 ? 0.9858 1.2561 0.9386 0.4132  0.1954  0.1540  158 ASN   B ND2 
1678 N  ND2 C ASN   B 149 ? 1.1110 1.3937 1.0270 0.4499  0.1941  0.1554  158 ASN   B ND2 
1679 N  ND2 D ASN   B 149 ? 1.1118 1.3945 1.0278 0.4499  0.1941  0.1554  158 ASN   B ND2 
1680 N  N   . GLY   B 150 ? 0.9432 1.2574 0.9892 0.3419  0.2109  0.1786  159 GLY   B N   
1681 C  CA  . GLY   B 150 ? 0.8682 1.1760 0.9376 0.3204  0.2123  0.1806  159 GLY   B CA  
1682 C  C   . GLY   B 150 ? 0.8405 1.1172 0.8994 0.3188  0.2055  0.1659  159 GLY   B C   
1683 O  O   . GLY   B 150 ? 0.7935 1.0598 0.8696 0.3005  0.2051  0.1642  159 GLY   B O   
1684 N  N   A SER   B 151 ? 0.8445 1.1059 0.8757 0.3374  0.1996  0.1554  160 SER   B N   
1685 N  N   B SER   B 151 ? 0.8413 1.1028 0.8725 0.3374  0.1996  0.1554  160 SER   B N   
1686 N  N   C SER   B 151 ? 0.8482 1.1097 0.8794 0.3374  0.1996  0.1554  160 SER   B N   
1687 N  N   D SER   B 151 ? 0.8445 1.1060 0.8756 0.3374  0.1996  0.1554  160 SER   B N   
1688 C  CA  A SER   B 151 ? 0.8395 1.0714 0.8574 0.3385  0.1919  0.1410  160 SER   B CA  
1689 C  CA  B SER   B 151 ? 0.8344 1.0662 0.8518 0.3388  0.1917  0.1409  160 SER   B CA  
1690 C  CA  C SER   B 151 ? 0.8430 1.0749 0.8610 0.3384  0.1919  0.1410  160 SER   B CA  
1691 C  CA  D SER   B 151 ? 0.8369 1.0687 0.8543 0.3388  0.1917  0.1409  160 SER   B CA  
1692 C  C   A SER   B 151 ? 0.8100 1.0174 0.8308 0.3210  0.1832  0.1248  160 SER   B C   
1693 C  C   B SER   B 151 ? 0.8067 1.0141 0.8276 0.3208  0.1832  0.1248  160 SER   B C   
1694 C  C   C SER   B 151 ? 0.8117 1.0190 0.8325 0.3209  0.1832  0.1248  160 SER   B C   
1695 C  C   D SER   B 151 ? 0.8078 1.0152 0.8288 0.3207  0.1832  0.1248  160 SER   B C   
1696 O  O   A SER   B 151 ? 0.8019 1.0133 0.8262 0.3148  0.1821  0.1227  160 SER   B O   
1697 O  O   B SER   B 151 ? 0.7973 1.0088 0.8224 0.3141  0.1822  0.1228  160 SER   B O   
1698 O  O   C SER   B 151 ? 0.8009 1.0122 0.8252 0.3147  0.1821  0.1227  160 SER   B O   
1699 O  O   D SER   B 151 ? 0.7958 1.0072 0.8210 0.3140  0.1822  0.1228  160 SER   B O   
1700 C  CB  A SER   B 151 ? 0.8675 1.0924 0.8546 0.3647  0.1878  0.1365  160 SER   B CB  
1701 C  CB  B SER   B 151 ? 0.8585 1.0834 0.8449 0.3651  0.1875  0.1362  160 SER   B CB  
1702 C  CB  C SER   B 151 ? 0.8730 1.0978 0.8602 0.3647  0.1878  0.1365  160 SER   B CB  
1703 C  CB  D SER   B 151 ? 0.8617 1.0867 0.8481 0.3651  0.1875  0.1362  160 SER   B CB  
1704 O  OG  A SER   B 151 ? 0.8803 1.0800 0.8570 0.3657  0.1810  0.1255  160 SER   B OG  
1705 O  OG  B SER   B 151 ? 0.8659 1.0966 0.8384 0.3763  0.1856  0.1346  160 SER   B OG  
1706 O  OG  C SER   B 151 ? 0.8881 1.0878 0.8650 0.3656  0.1810  0.1255  160 SER   B OG  
1707 O  OG  D SER   B 151 ? 0.8673 1.0987 0.8400 0.3764  0.1858  0.1349  160 SER   B OG  
1708 N  N   . TYR   B 152 ? 0.7912 0.9754 0.8105 0.3138  0.1775  0.1142  161 TYR   B N   
1709 C  CA  . TYR   B 152 ? 0.7383 0.8991 0.7604 0.2976  0.1692  0.0993  161 TYR   B CA  
1710 C  C   . TYR   B 152 ? 0.6870 0.8260 0.6828 0.3096  0.1584  0.0855  161 TYR   B C   
1711 O  O   . TYR   B 152 ? 0.6670 0.7984 0.6454 0.3250  0.1555  0.0837  161 TYR   B O   
1712 C  CB  . TYR   B 152 ? 0.7270 0.8762 0.7622 0.2839  0.1689  0.0966  161 TYR   B CB  
1713 C  CG  . TYR   B 152 ? 0.7064 0.8359 0.7481 0.2662  0.1620  0.0835  161 TYR   B CG  
1714 C  CD1 . TYR   B 152 ? 0.7022 0.8367 0.7597 0.2501  0.1633  0.0833  161 TYR   B CD1 
1715 C  CD2 . TYR   B 152 ? 0.7184 0.8253 0.7504 0.2657  0.1541  0.0720  161 TYR   B CD2 
1716 C  CE1 . TYR   B 152 ? 0.6867 0.8048 0.7501 0.2346  0.1575  0.0720  161 TYR   B CE1 
1717 C  CE2 . TYR   B 152 ? 0.7162 0.8078 0.7556 0.2494  0.1484  0.0615  161 TYR   B CE2 
1718 C  CZ  . TYR   B 152 ? 0.7071 0.8044 0.7617 0.2343  0.1503  0.0615  161 TYR   B CZ  
1719 O  OH  . TYR   B 152 ? 0.7088 0.7927 0.7704 0.2191  0.1452  0.0518  161 TYR   B OH  
1720 N  N   . VAL   B 153 ? 0.6613 0.7882 0.6555 0.3008  0.1519  0.0755  162 VAL   B N   
1721 C  CA  . VAL   B 153 ? 0.6574 0.7592 0.6298 0.3069  0.1397  0.0612  162 VAL   B CA  
1722 C  C   . VAL   B 153 ? 0.6169 0.7022 0.6015 0.2855  0.1339  0.0509  162 VAL   B C   
1723 O  O   . VAL   B 153 ? 0.5827 0.6745 0.5809 0.2724  0.1361  0.0512  162 VAL   B O   
1724 C  CB  . VAL   B 153 ? 0.6658 0.7698 0.6197 0.3209  0.1364  0.0596  162 VAL   B CB  
1725 C  CG1 . VAL   B 153 ? 0.6822 0.7596 0.6100 0.3315  0.1232  0.0468  162 VAL   B CG1 
1726 C  CG2 . VAL   B 153 ? 0.6925 0.8208 0.6407 0.3392  0.1450  0.0727  162 VAL   B CG2 
1727 N  N   . SER   B 154 ? 0.6035 0.6686 0.5821 0.2833  0.1264  0.0423  163 SER   B N   
1728 C  CA  . SER   B 154 ? 0.5756 0.6253 0.5644 0.2648  0.1206  0.0330  163 SER   B CA  
1729 C  C   . SER   B 154 ? 0.5752 0.6044 0.5458 0.2680  0.1080  0.0216  163 SER   B C   
1730 O  O   . SER   B 154 ? 0.5777 0.5961 0.5269 0.2838  0.1014  0.0186  163 SER   B O   
1731 C  CB  . SER   B 154 ? 0.5730 0.6154 0.5682 0.2601  0.1205  0.0320  163 SER   B CB  
1732 O  OG  . SER   B 154 ? 0.5486 0.5753 0.5494 0.2457  0.1134  0.0226  163 SER   B OG  
1733 N  N   . ALA   B 155 ? 0.5499 0.5726 0.5295 0.2524  0.1042  0.0155  164 ALA   B N   
1734 C  CA  . ALA   B 155 ? 0.5609 0.5622 0.5284 0.2500  0.0915  0.0048  164 ALA   B CA  
1735 C  C   . ALA   B 155 ? 0.5798 0.5669 0.5445 0.2492  0.0854  0.0006  164 ALA   B C   
1736 O  O   . ALA   B 155 ? 0.5761 0.5700 0.5553 0.2429  0.0920  0.0045  164 ALA   B O   
1737 C  CB  . ALA   B 155 ? 0.5497 0.5503 0.5315 0.2318  0.0905  0.0009  164 ALA   B CB  
1738 N  N   . ILE   B 156 ? 0.5950 0.5624 0.5410 0.2555  0.0727  -0.0068 165 ILE   B N   
1739 C  CA  . ILE   B 156 ? 0.5946 0.5459 0.5411 0.2483  0.0638  -0.0127 165 ILE   B CA  
1740 C  C   . ILE   B 156 ? 0.5746 0.5238 0.5370 0.2284  0.0617  -0.0166 165 ILE   B C   
1741 O  O   . ILE   B 156 ? 0.5639 0.5006 0.5172 0.2265  0.0519  -0.0222 165 ILE   B O   
1742 C  CB  . ILE   B 156 ? 0.6158 0.5461 0.5366 0.2616  0.0496  -0.0190 165 ILE   B CB  
1743 C  CG1 . ILE   B 156 ? 0.6348 0.5683 0.5368 0.2840  0.0519  -0.0153 165 ILE   B CG1 
1744 C  CG2 . ILE   B 156 ? 0.6198 0.5365 0.5437 0.2535  0.0411  -0.0234 165 ILE   B CG2 
1745 C  CD1 . ILE   B 156 ? 0.6617 0.5732 0.5351 0.2994  0.0373  -0.0219 165 ILE   B CD1 
1746 N  N   . THR   B 157 ? 0.5612 0.5211 0.5456 0.2147  0.0700  -0.0138 166 THR   B N   
1747 C  CA  . THR   B 157 ? 0.5440 0.5046 0.5447 0.1963  0.0696  -0.0167 166 THR   B CA  
1748 C  C   . THR   B 157 ? 0.5500 0.4978 0.5523 0.1887  0.0605  -0.0216 166 THR   B C   
1749 O  O   . THR   B 157 ? 0.5509 0.5007 0.5602 0.1875  0.0636  -0.0198 166 THR   B O   
1750 C  CB  . THR   B 157 ? 0.5303 0.5077 0.5525 0.1863  0.0822  -0.0115 166 THR   B CB  
1751 O  OG1 . THR   B 157 ? 0.5164 0.5064 0.5373 0.1932  0.0896  -0.0060 166 THR   B OG1 
1752 C  CG2 . THR   B 157 ? 0.5171 0.4953 0.5544 0.1692  0.0820  -0.0147 166 THR   B CG2 
1753 N  N   . GLN   B 158 ? 0.5458 0.4816 0.5422 0.1836  0.0498  -0.0268 167 GLN   B N   
1754 C  CA  . GLN   B 158 ? 0.5483 0.4730 0.5471 0.1750  0.0399  -0.0305 167 GLN   B CA  
1755 C  C   . GLN   B 158 ? 0.5559 0.4849 0.5697 0.1584  0.0400  -0.0319 167 GLN   B C   
1756 O  O   . GLN   B 158 ? 0.5318 0.4632 0.5448 0.1564  0.0410  -0.0325 167 GLN   B O   
1757 C  CB  . GLN   B 158 ? 0.5545 0.4598 0.5318 0.1841  0.0250  -0.0347 167 GLN   B CB  
1758 C  CG  . GLN   B 158 ? 0.5522 0.4460 0.5306 0.1770  0.0135  -0.0372 167 GLN   B CG  
1759 C  CD  . GLN   B 158 ? 0.5432 0.4437 0.5329 0.1746  0.0187  -0.0348 167 GLN   B CD  
1760 O  OE1 . GLN   B 158 ? 0.5071 0.4221 0.5148 0.1664  0.0298  -0.0320 167 GLN   B OE1 
1761 N  NE2 . GLN   B 158 ? 0.5516 0.4404 0.5302 0.1816  0.0095  -0.0363 167 GLN   B NE2 
1762 N  N   . GLY   B 159 ? 0.5768 0.5073 0.6035 0.1478  0.0391  -0.0320 168 GLY   B N   
1763 C  CA  . GLY   B 159 ? 0.6292 0.5637 0.6695 0.1329  0.0381  -0.0330 168 GLY   B CA  
1764 C  C   . GLY   B 159 ? 0.7066 0.6273 0.7385 0.1295  0.0234  -0.0358 168 GLY   B C   
1765 O  O   . GLY   B 159 ? 0.7407 0.6474 0.7552 0.1392  0.0139  -0.0375 168 GLY   B O   
1766 N  N   . LYS   B 160 ? 0.7992 0.7237 0.8424 0.1165  0.0215  -0.0359 169 LYS   B N   
1767 C  CA  . LYS   B 160 ? 0.8751 0.7888 0.9148 0.1097  0.0076  -0.0369 169 LYS   B CA  
1768 C  C   . LYS   B 160 ? 0.9090 0.8286 0.9628 0.1004  0.0062  -0.0346 169 LYS   B C   
1769 O  O   . LYS   B 160 ? 0.8455 0.7797 0.9143 0.0958  0.0175  -0.0329 169 LYS   B O   
1770 C  CB  . LYS   B 160 ? 0.9215 0.8371 0.9636 0.1026  0.0070  -0.0376 169 LYS   B CB  
1771 C  CG  . LYS   B 160 ? 0.9995 0.8988 1.0294 0.1013  -0.0086 -0.0391 169 LYS   B CG  
1772 C  CD  . LYS   B 160 ? 1.0249 0.9279 1.0618 0.0906  -0.0100 -0.0385 169 LYS   B CD  
1773 C  CE  . LYS   B 160 ? 1.0548 0.9518 1.0957 0.0800  -0.0227 -0.0364 169 LYS   B CE  
1774 N  NZ  . LYS   B 160 ? 1.0913 1.0021 1.1484 0.0673  -0.0180 -0.0339 169 LYS   B NZ  
1775 N  N   . ARG   B 161 ? 0.9681 0.8765 1.0164 0.0986  -0.0073 -0.0344 170 ARG   B N   
1776 C  CA  . ARG   B 161 ? 0.9787 0.8925 1.0398 0.0889  -0.0116 -0.0312 170 ARG   B CA  
1777 C  C   . ARG   B 161 ? 1.0638 0.9796 1.1323 0.0764  -0.0181 -0.0293 170 ARG   B C   
1778 O  O   . ARG   B 161 ? 1.1418 1.0481 1.2004 0.0772  -0.0237 -0.0312 170 ARG   B O   
1779 C  CB  . ARG   B 161 ? 0.9582 0.8588 1.0084 0.0954  -0.0227 -0.0316 170 ARG   B CB  
1780 C  CG  . ARG   B 161 ? 0.9177 0.8261 0.9802 0.0897  -0.0238 -0.0281 170 ARG   B CG  
1781 C  CD  . ARG   B 161 ? 0.9376 0.8320 0.9883 0.0963  -0.0360 -0.0287 170 ARG   B CD  
1782 N  NE  . ARG   B 161 ? 0.9481 0.8490 1.0110 0.0878  -0.0416 -0.0245 170 ARG   B NE  
1783 C  CZ  . ARG   B 161 ? 0.9386 0.8442 1.0052 0.0913  -0.0391 -0.0231 170 ARG   B CZ  
1784 N  NH1 . ARG   B 161 ? 0.9136 0.8178 0.9729 0.1032  -0.0310 -0.0256 170 ARG   B NH1 
1785 N  NH2 . ARG   B 161 ? 0.9529 0.8657 1.0312 0.0828  -0.0449 -0.0187 170 ARG   B NH2 
1786 N  N   . GLU   B 162 ? 1.1378 1.0669 1.2232 0.0657  -0.0166 -0.0253 171 GLU   B N   
1787 C  CA  . GLU   B 162 ? 1.1775 1.1119 1.2722 0.0532  -0.0222 -0.0217 171 GLU   B CA  
1788 C  C   . GLU   B 162 ? 1.1385 1.0758 1.2416 0.0459  -0.0317 -0.0165 171 GLU   B C   
1789 O  O   . GLU   B 162 ? 1.1754 1.1061 1.2778 0.0386  -0.0450 -0.0133 171 GLU   B O   
1790 C  CB  . GLU   B 162 ? 1.2421 1.1947 1.3510 0.0476  -0.0087 -0.0210 171 GLU   B CB  
1791 C  CG  . GLU   B 162 ? 1.2994 1.2514 1.4024 0.0534  0.0007  -0.0253 171 GLU   B CG  
1792 C  CD  . GLU   B 162 ? 1.4068 1.3531 1.5039 0.0504  -0.0038 -0.0264 171 GLU   B CD  
1793 O  OE1 . GLU   B 162 ? 1.4025 1.3549 1.5010 0.0515  0.0055  -0.0285 171 GLU   B OE1 
1794 O  OE2 . GLU   B 162 ? 1.4768 1.4122 1.5680 0.0467  -0.0173 -0.0249 171 GLU   B OE2 
1795 S  S   A DMS   C .   ? 0.6549 0.7616 0.7483 0.2171  0.1651  0.0790  201 DMS   B S   
1796 S  S   B DMS   C .   ? 0.6551 0.7618 0.7484 0.2171  0.1651  0.0790  201 DMS   B S   
1797 O  O   A DMS   C .   ? 0.6619 0.7829 0.7437 0.2322  0.1672  0.0854  201 DMS   B O   
1798 O  O   B DMS   C .   ? 0.6618 0.7828 0.7436 0.2322  0.1672  0.0854  201 DMS   B O   
1799 C  C1  A DMS   C .   ? 0.6421 0.7406 0.7432 0.2001  0.1602  0.0688  201 DMS   B C1  
1800 C  C1  B DMS   C .   ? 0.6420 0.7405 0.7431 0.2001  0.1602  0.0688  201 DMS   B C1  
1801 C  C2  A DMS   C .   ? 0.6623 0.7469 0.7367 0.2251  0.1560  0.0661  201 DMS   B C2  
1802 C  C2  B DMS   C .   ? 0.6623 0.7469 0.7367 0.2251  0.1560  0.0661  201 DMS   B C2  
1803 S  S   . DMS   D .   ? 0.9718 0.9667 1.1704 0.0566  0.1355  -0.0237 202 DMS   B S   
1804 O  O   . DMS   D .   ? 0.9416 0.9431 1.1352 0.0598  0.1336  -0.0247 202 DMS   B O   
1805 C  C1  . DMS   D .   ? 0.9745 0.9620 1.1717 0.0621  0.1367  -0.0238 202 DMS   B C1  
1806 C  C2  . DMS   D .   ? 0.9255 0.9216 1.1272 0.0574  0.1381  -0.0147 202 DMS   B C2  
1807 S  S   A DMS   E .   ? 0.5124 0.6155 0.6157 0.1851  0.1540  0.0582  203 DMS   B S   
1808 S  S   B DMS   E .   ? 0.5124 0.6155 0.6156 0.1851  0.1540  0.0582  203 DMS   B S   
1809 O  O   A DMS   E .   ? 0.5174 0.6116 0.5995 0.1976  0.1473  0.0510  203 DMS   B O   
1810 O  O   B DMS   E .   ? 0.5167 0.6109 0.5988 0.1976  0.1473  0.0510  203 DMS   B O   
1811 C  C1  A DMS   E .   ? 0.5018 0.5924 0.6175 0.1652  0.1500  0.0481  203 DMS   B C1  
1812 C  C1  B DMS   E .   ? 0.5022 0.5927 0.6178 0.1652  0.1500  0.0481  203 DMS   B C1  
1813 C  C2  A DMS   E .   ? 0.5085 0.6339 0.6236 0.1814  0.1601  0.0687  203 DMS   B C2  
1814 C  C2  B DMS   E .   ? 0.5087 0.6341 0.6237 0.1814  0.1601  0.0686  203 DMS   B C2  
1815 N  N1  C A1BGM F .   ? 0.7398 0.8144 0.8711 0.1343  0.1420  0.0297  204 A1BGM B N1  
1816 N  N1  D A1BGM F .   ? 0.7408 0.8154 0.8721 0.1343  0.1420  0.0297  204 A1BGM B N1  
1817 N  N3  C A1BGM F .   ? 0.6787 0.7773 0.8042 0.1756  0.1617  0.0673  204 A1BGM B N3  
1818 N  N3  D A1BGM F .   ? 0.6787 0.7773 0.8042 0.1756  0.1617  0.0673  204 A1BGM B N3  
1819 C  C4  C A1BGM F .   ? 0.6989 0.7836 0.8453 0.1347  0.1517  0.0444  204 A1BGM B C4  
1820 C  C4  D A1BGM F .   ? 0.6986 0.7834 0.8451 0.1347  0.1517  0.0444  204 A1BGM B C4  
1821 C  C5  C A1BGM F .   ? 0.6832 0.7772 0.8202 0.1544  0.1570  0.0566  204 A1BGM B C5  
1822 C  C5  D A1BGM F .   ? 0.6828 0.7767 0.8198 0.1544  0.1570  0.0566  204 A1BGM B C5  
1823 C  C6  C A1BGM F .   ? 0.6856 0.7828 0.8075 0.1720  0.1576  0.0606  204 A1BGM B C6  
1824 C  C6  D A1BGM F .   ? 0.6854 0.7826 0.8074 0.1720  0.1576  0.0606  204 A1BGM B C6  
1825 C  C7  C A1BGM F .   ? 0.6769 0.7801 0.7902 0.1920  0.1634  0.0727  204 A1BGM B C7  
1826 C  C7  D A1BGM F .   ? 0.6769 0.7802 0.7902 0.1920  0.1634  0.0727  204 A1BGM B C7  
1827 C  C8  C A1BGM F .   ? 0.6741 0.7632 0.7717 0.2012  0.1579  0.0649  204 A1BGM B C8  
1828 C  C8  D A1BGM F .   ? 0.6738 0.7629 0.7714 0.2012  0.1579  0.0649  204 A1BGM B C8  
1829 C  C10 C A1BGM F .   ? 0.6891 0.8013 0.7756 0.2268  0.1666  0.0830  204 A1BGM B C10 
1830 C  C10 D A1BGM F .   ? 0.6890 0.8012 0.7755 0.2268  0.1666  0.0830  204 A1BGM B C10 
1831 C  C13 C A1BGM F .   ? 0.6914 0.8740 0.7888 0.2542  0.1908  0.1305  204 A1BGM B C13 
1832 C  C13 D A1BGM F .   ? 0.6913 0.8739 0.7887 0.2542  0.1908  0.1306  204 A1BGM B C13 
1833 C  C15 C A1BGM F .   ? 0.6873 0.8861 0.7811 0.2600  0.1923  0.1348  204 A1BGM B C15 
1834 C  C15 D A1BGM F .   ? 0.6869 0.8858 0.7807 0.2601  0.1923  0.1348  204 A1BGM B C15 
1835 C  C17 C A1BGM F .   ? 0.6734 0.7959 0.7900 0.1994  0.1703  0.0863  204 A1BGM B C17 
1836 C  C17 D A1BGM F .   ? 0.6732 0.7957 0.7898 0.1994  0.1703  0.0863  204 A1BGM B C17 
1837 C  C1  C A1BGM F .   ? 0.7461 0.8108 0.8765 0.1261  0.1364  0.0198  204 A1BGM B C1  
1838 C  C1  D A1BGM F .   ? 0.7474 0.8122 0.8778 0.1261  0.1364  0.0198  204 A1BGM B C1  
1839 C  C2  C A1BGM F .   ? 0.7481 0.8377 0.8792 0.1390  0.1454  0.0369  204 A1BGM B C2  
1840 C  C2  D A1BGM F .   ? 0.7493 0.8388 0.8803 0.1390  0.1454  0.0369  204 A1BGM B C2  
1841 C  C3  C A1BGM F .   ? 0.7180 0.7940 0.8639 0.1262  0.1464  0.0340  204 A1BGM B C3  
1842 C  C3  D A1BGM F .   ? 0.7186 0.7947 0.8645 0.1262  0.1464  0.0340  204 A1BGM B C3  
1843 N  N2  C A1BGM F .   ? 0.6934 0.7800 0.8265 0.1492  0.1516  0.0470  204 A1BGM B N2  
1844 N  N2  D A1BGM F .   ? 0.6932 0.7797 0.8262 0.1492  0.1516  0.0470  204 A1BGM B N2  
1845 C  C9  C A1BGM F .   ? 0.6819 0.7750 0.7663 0.2183  0.1593  0.0699  204 A1BGM B C9  
1846 C  C9  D A1BGM F .   ? 0.6815 0.7746 0.7659 0.2183  0.1593  0.0699  204 A1BGM B C9  
1847 CL CL1 C A1BGM F .   ? 0.6884 0.7624 0.7531 0.2292  0.1510  0.0599  204 A1BGM B CL1 
1848 CL CL1 D A1BGM F .   ? 0.6880 0.7620 0.7527 0.2292  0.1510  0.0599  204 A1BGM B CL1 
1849 C  C11 C A1BGM F .   ? 0.6796 0.8076 0.7831 0.2171  0.1724  0.0919  204 A1BGM B C11 
1850 C  C11 D A1BGM F .   ? 0.6794 0.8073 0.7828 0.2171  0.1724  0.0919  204 A1BGM B C11 
1851 C  C12 C A1BGM F .   ? 0.6830 0.8346 0.7911 0.2250  0.1804  0.1080  204 A1BGM B C12 
1852 C  C12 D A1BGM F .   ? 0.6829 0.8345 0.7910 0.2251  0.1804  0.1080  204 A1BGM B C12 
1853 O  O1  C A1BGM F .   ? 0.6892 0.8544 0.8133 0.2150  0.1844  0.1159  204 A1BGM B O1  
1854 O  O1  D A1BGM F .   ? 0.6899 0.8551 0.8140 0.2150  0.1844  0.1158  204 A1BGM B O1  
1855 N  N4  C A1BGM F .   ? 0.6912 0.8489 0.7857 0.2434  0.1825  0.1135  204 A1BGM B N4  
1856 N  N4  D A1BGM F .   ? 0.6912 0.8490 0.7857 0.2434  0.1825  0.1135  204 A1BGM B N4  
1857 C  C14 C A1BGM F .   ? 0.7075 0.8887 0.7865 0.2745  0.1912  0.1321  204 A1BGM B C14 
1858 C  C14 D A1BGM F .   ? 0.7075 0.8888 0.7865 0.2745  0.1912  0.1321  204 A1BGM B C14 
1859 C  C16 C A1BGM F .   ? 0.6755 0.8691 0.7969 0.2403  0.1972  0.1430  204 A1BGM B C16 
1860 C  C16 D A1BGM F .   ? 0.6749 0.8686 0.7964 0.2403  0.1972  0.1430  204 A1BGM B C16 
1861 O  O2  C A1BGM F .   ? 0.6786 0.8580 0.8037 0.2353  0.1963  0.1400  204 A1BGM B O2  
1862 O  O2  D A1BGM F .   ? 0.6784 0.8578 0.8035 0.2353  0.1963  0.1400  204 A1BGM B O2  
1863 C  C18 C A1BGM F .   ? 0.6865 0.7837 0.8405 0.1428  0.1608  0.0617  204 A1BGM B C18 
1864 C  C18 D A1BGM F .   ? 0.6861 0.7833 0.8401 0.1428  0.1608  0.0617  204 A1BGM B C18 
1865 S  S1  C A1BGM F .   ? 0.7004 0.7925 0.8651 0.1261  0.1578  0.0542  204 A1BGM B S1  
1866 S  S1  D A1BGM F .   ? 0.7012 0.7933 0.8659 0.1261  0.1578  0.0542  204 A1BGM B S1  
1867 S  S   C DMS   G .   ? 1.3322 1.1929 1.0113 0.4516  -0.0006 -0.0350 205 DMS   B S   
1868 S  S   D DMS   G .   ? 1.3322 1.1929 1.0113 0.4516  -0.0006 -0.0350 205 DMS   B S   
1869 O  O   C DMS   G .   ? 1.2970 1.1463 0.9793 0.4465  -0.0058 -0.0375 205 DMS   B O   
1870 O  O   D DMS   G .   ? 1.2970 1.1463 0.9793 0.4465  -0.0058 -0.0375 205 DMS   B O   
1871 C  C1  C DMS   G .   ? 1.2891 1.1924 1.0039 0.4392  0.0233  -0.0211 205 DMS   B C1  
1872 C  C1  D DMS   G .   ? 1.2891 1.1924 1.0039 0.4392  0.0233  -0.0211 205 DMS   B C1  
1873 C  C2  C DMS   G .   ? 1.3455 1.2131 0.9913 0.4886  0.0018  -0.0314 205 DMS   B C2  
1874 C  C2  D DMS   G .   ? 1.3455 1.2131 0.9913 0.4886  0.0018  -0.0314 205 DMS   B C2  
1875 S  S   C SO4   H .   ? 1.2358 1.5312 1.3113 0.3359  0.2250  0.2035  206 SO4   B S   
1876 S  S   D SO4   H .   ? 1.2367 1.5320 1.3121 0.3359  0.2250  0.2035  206 SO4   B S   
1877 O  O1  C SO4   H .   ? 1.2198 1.5154 1.3142 0.3232  0.2286  0.2115  206 SO4   B O1  
1878 O  O1  D SO4   H .   ? 1.2197 1.5154 1.3141 0.3232  0.2286  0.2115  206 SO4   B O1  
1879 O  O2  C SO4   H .   ? 1.1850 1.5022 1.2747 0.3288  0.2288  0.2132  206 SO4   B O2  
1880 O  O2  D SO4   H .   ? 1.1831 1.5002 1.2726 0.3289  0.2288  0.2132  206 SO4   B O2  
1881 O  O3  C SO4   H .   ? 1.2220 1.4868 1.2873 0.3290  0.2151  0.1825  206 SO4   B O3  
1882 O  O3  D SO4   H .   ? 1.2220 1.4868 1.2874 0.3290  0.2150  0.1825  206 SO4   B O3  
1883 O  O4  C SO4   H .   ? 1.2668 1.5711 1.3191 0.3631  0.2270  0.2074  206 SO4   B O4  
1884 O  O4  D SO4   H .   ? 1.2683 1.5725 1.3205 0.3631  0.2269  0.2073  206 SO4   B O4  
# 
