data_7I1N
# 
_entry.id   7I1N 
# 
_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   7I1N         pdb_00007i1n 10.2210/pdb7i1n/pdb 
WWPDB D_1001408202 ?            ?                   
# 
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 2025-03-05 ? 
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                        7I1N 
_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   2025-02-20 
_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  
'Balaji, G.'          9  
'Phelps, J.'          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 'Balaji, G.'          ? 9  
primary 'Phelps, J.'          ? 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 '(5P)-8-methyl-5-(2-methyl-1H-imidazol-4-yl)quinoline' 223.273   1  ?                           ?    ? ? 
5 water       nat water                                                  18.015    93 ?                           ?    ? ? 
# 
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 '(5P)-8-methyl-5-(2-methyl-1H-imidazol-4-yl)quinoline' A1BXG 
5 water                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BXG non-polymer         . '(5P)-8-methyl-5-(2-methyl-1H-imidazol-4-yl)quinoline' ? 'C14 H13 N3'     223.273 
ALA   'L-peptide linking' y ALANINE                                                ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                               ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                             ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                        ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                               ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                   ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                              ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                        ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                              ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                  ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                             ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                 ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                             ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                          ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                 ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                              ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                             ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                               ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                 ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BXG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXG 
_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 A1BXG 1  204 301 A1BXG LIG B . 
G 3 DMS   1  205 302 DMS   DMS B . 
H 5 HOH   1  101 105 HOH   HOH A . 
H 5 HOH   2  102 34  HOH   HOH A . 
H 5 HOH   3  103 81  HOH   HOH A . 
H 5 HOH   4  104 16  HOH   HOH A . 
H 5 HOH   5  105 20  HOH   HOH A . 
H 5 HOH   6  106 48  HOH   HOH A . 
H 5 HOH   7  107 121 HOH   HOH A . 
H 5 HOH   8  108 103 HOH   HOH A . 
H 5 HOH   9  109 77  HOH   HOH A . 
H 5 HOH   10 110 110 HOH   HOH A . 
H 5 HOH   11 111 65  HOH   HOH A . 
H 5 HOH   12 112 70  HOH   HOH A . 
H 5 HOH   13 113 98  HOH   HOH A . 
H 5 HOH   14 114 119 HOH   HOH A . 
H 5 HOH   15 115 118 HOH   HOH A . 
H 5 HOH   16 116 36  HOH   HOH A . 
H 5 HOH   17 117 50  HOH   HOH A . 
H 5 HOH   18 118 40  HOH   HOH A . 
H 5 HOH   19 119 49  HOH   HOH A . 
H 5 HOH   20 120 29  HOH   HOH A . 
H 5 HOH   21 121 27  HOH   HOH A . 
H 5 HOH   22 122 120 HOH   HOH A . 
I 5 HOH   1  301 5   HOH   HOH B . 
I 5 HOH   2  302 51  HOH   HOH B . 
I 5 HOH   3  303 11  HOH   HOH B . 
I 5 HOH   4  304 58  HOH   HOH B . 
I 5 HOH   5  305 125 HOH   HOH B . 
I 5 HOH   6  306 46  HOH   HOH B . 
I 5 HOH   7  307 62  HOH   HOH B . 
I 5 HOH   8  308 90  HOH   HOH B . 
I 5 HOH   9  309 57  HOH   HOH B . 
I 5 HOH   10 310 4   HOH   HOH B . 
I 5 HOH   11 311 79  HOH   HOH B . 
I 5 HOH   12 312 89  HOH   HOH B . 
I 5 HOH   13 313 92  HOH   HOH B . 
I 5 HOH   14 314 14  HOH   HOH B . 
I 5 HOH   15 315 32  HOH   HOH B . 
I 5 HOH   16 316 23  HOH   HOH B . 
I 5 HOH   17 317 1   HOH   HOH B . 
I 5 HOH   18 318 42  HOH   HOH B . 
I 5 HOH   19 319 115 HOH   HOH B . 
I 5 HOH   20 320 13  HOH   HOH B . 
I 5 HOH   21 321 24  HOH   HOH B . 
I 5 HOH   22 322 30  HOH   HOH B . 
I 5 HOH   23 323 100 HOH   HOH B . 
I 5 HOH   24 324 116 HOH   HOH B . 
I 5 HOH   25 325 117 HOH   HOH B . 
I 5 HOH   26 326 108 HOH   HOH B . 
I 5 HOH   27 327 66  HOH   HOH B . 
I 5 HOH   28 328 56  HOH   HOH B . 
I 5 HOH   29 329 73  HOH   HOH B . 
I 5 HOH   30 330 2   HOH   HOH B . 
I 5 HOH   31 331 35  HOH   HOH B . 
I 5 HOH   32 332 10  HOH   HOH B . 
I 5 HOH   33 333 43  HOH   HOH B . 
I 5 HOH   34 334 69  HOH   HOH B . 
I 5 HOH   35 335 83  HOH   HOH B . 
I 5 HOH   36 336 21  HOH   HOH B . 
I 5 HOH   37 337 63  HOH   HOH B . 
I 5 HOH   38 338 39  HOH   HOH B . 
I 5 HOH   39 339 68  HOH   HOH B . 
I 5 HOH   40 340 60  HOH   HOH B . 
I 5 HOH   41 341 17  HOH   HOH B . 
I 5 HOH   42 342 28  HOH   HOH B . 
I 5 HOH   43 343 102 HOH   HOH B . 
I 5 HOH   44 344 18  HOH   HOH B . 
I 5 HOH   45 345 31  HOH   HOH B . 
I 5 HOH   46 346 122 HOH   HOH B . 
I 5 HOH   47 347 54  HOH   HOH B . 
I 5 HOH   48 348 82  HOH   HOH B . 
I 5 HOH   49 349 72  HOH   HOH B . 
I 5 HOH   50 350 94  HOH   HOH B . 
I 5 HOH   51 351 87  HOH   HOH B . 
I 5 HOH   52 352 12  HOH   HOH B . 
I 5 HOH   53 353 124 HOH   HOH B . 
I 5 HOH   54 354 9   HOH   HOH B . 
I 5 HOH   55 355 64  HOH   HOH B . 
I 5 HOH   56 356 106 HOH   HOH B . 
I 5 HOH   57 357 3   HOH   HOH B . 
I 5 HOH   58 358 80  HOH   HOH B . 
I 5 HOH   59 359 26  HOH   HOH B . 
I 5 HOH   60 360 112 HOH   HOH B . 
I 5 HOH   61 361 67  HOH   HOH B . 
I 5 HOH   62 362 123 HOH   HOH B . 
I 5 HOH   63 363 107 HOH   HOH B . 
I 5 HOH   64 364 45  HOH   HOH B . 
I 5 HOH   65 365 126 HOH   HOH B . 
I 5 HOH   66 366 59  HOH   HOH B . 
I 5 HOH   67 367 61  HOH   HOH B . 
I 5 HOH   68 368 109 HOH   HOH B . 
I 5 HOH   69 369 75  HOH   HOH B . 
I 5 HOH   70 370 85  HOH   HOH B . 
I 5 HOH   71 371 44  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       REFMAC  5.8.0267 ? 1 ? ? ? ? 
refinement       BUSTER  .        ? 2 ? ? ? ? 
'data scaling'   Aimless .        ? 3 ? ? ? ? 
phasing          PHASER  .        ? 4 ? ? ? ? 
'data reduction' XDS     .        ? 5 ? ? ? ? 
# 
_cell.entry_id           7I1N 
_cell.length_a           42.326 
_cell.length_b           42.326 
_cell.length_c           216.467 
_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                         7I1N 
_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          7I1N 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.09 
_exptl_crystal.density_percent_sol   41.17 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-10-10 
_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                     7I1N 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.51 
_reflns.d_resolution_high            1.76 
_reflns.number_obs                   20703 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.170 
_reflns.pdbx_netI_over_sigmaI        6.4 
_reflns.pdbx_redundancy              25.3 
_reflns.pdbx_Rrim_I_all              0.173 
_reflns.pdbx_Rpim_I_all              0.035 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     523682 
_reflns.pdbx_chi_squared             0.22 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.76 
_reflns_shell.d_res_low                   1.80 
_reflns_shell.number_measured_all         28148 
_reflns_shell.number_unique_obs           1153 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.06 
_reflns_shell.pdbx_redundancy             24.4 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             11.846 
_reflns_shell.pdbx_Rpim_I_all             2.380 
_reflns_shell.pdbx_CC_half                0.370 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1N 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     16564 
_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                             54.12 
_refine.ls_d_res_high                            1.77 
_refine.ls_percent_reflns_obs                    85.38 
_refine.ls_R_factor_obs                          0.24068 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23801 
_refine.ls_R_factor_R_free                       0.29188 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_number_reflns_R_free                  844 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.B_iso_mean                               57.587 
_refine.aniso_B[1][1]                            0.29 
_refine.aniso_B[2][2]                            0.29 
_refine.aniso_B[3][3]                            -0.58 
_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                       0.208 
_refine.pdbx_overall_ESU_R_Free                  0.187 
_refine.overall_SU_ML                            0.301 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             24.400 
_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         33 
_refine_hist.number_atoms_solvent             93 
_refine_hist.number_atoms_total               1602 
_refine_hist.d_res_high                       1.77 
_refine_hist.d_res_low                        54.12 
# 
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             0.010  0.014  ? 2049 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.015  ? 1697 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.664  1.636  ? 2479 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.216  1.594  ? 3916 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.698  5.000  ? 241  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.406 22.500 ? 80   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.629 15.000 ? 289  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.985 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.071  0.200  ? 222  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2132 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 412  '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                  1.667  2.951  ? 1048 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.702  2.731  ? 994  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.101  3.999  ? 1167 'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.101  4.003  ? 1168 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.800  3.260  ? 1001 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.799  3.275  ? 1002 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              3.180  4.500  ? 1313 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       10.171 30.293 ? 1963 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         10.135 29.762 ? 1944 '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                       1.769 
_refine_ls_shell.d_res_low                        1.814 
_refine_ls_shell.number_reflns_R_work             91 
_refine_ls_shell.R_factor_R_work                  0.665 
_refine_ls_shell.percent_reflns_obs               6.34 
_refine_ls_shell.R_factor_R_free                  0.878 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             1 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7I1N 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with MFP-0011710-001-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1N 
_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 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I1N A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I1N 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 7I1N SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I1N MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I1N MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I1N LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.373 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 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 THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O 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                   7I1N 
_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 OG1 A THR 60 ? A OE2 A GLU 62 ? ? 2.16 
2 1 OG1 A THR 60 ? C OE2 A GLU 62 ? ? 2.16 
# 
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 A 64  ? C 70.03   60.32   
2 1 ASP A 64  ? D 70.03   60.32   
3 1 ASP B 20  ? ? -47.29  154.99  
4 1 LEU B 30  ? ? -109.94 -166.51 
5 1 CYS B 80  ? ? 76.38   -6.94   
6 1 LEU B 92  ? ? -124.87 -60.14  
7 1 LYS B 157 ? A -24.48  -53.54  
8 1 LYS B 157 ? B -24.48  -53.54  
# 
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 338 ? I HOH . 
2 1 B HOH 364 ? I HOH . 
3 1 B HOH 371 ? I HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.2448 -2.1641 -19.2330 0.4181 0.4463 0.0680 0.1045 0.0799 0.0817 1.6234 1.6829 0.8643 -0.0148 
-0.4788 0.4864  0.2604 0.2562 0.2276 -0.2076 -0.2318 -0.1888 -0.0397 0.1181 -0.0285 
'X-RAY DIFFRACTION' 2 ? refined -18.1329 0.3862  -15.8109 0.4921 0.4683 0.1246 0.1451 0.0499 0.0089 0.3335 0.0893 0.7034 -0.0037 
0.3912  -0.0835 0.1978 0.1136 0.0935 -0.0785 -0.1569 0.0609  0.1482  0.1702 -0.0409 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 302 ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BXG N1   N Y N 1   
A1BXG N3   N Y N 2   
A1BXG C4   C Y N 3   
A1BXG C5   C Y N 4   
A1BXG C6   C Y N 5   
A1BXG C7   C Y N 6   
A1BXG C8   C Y N 7   
A1BXG C10  C Y N 8   
A1BXG C13  C Y N 9   
A1BXG C1   C N N 10  
A1BXG C2   C Y N 11  
A1BXG C3   C Y N 12  
A1BXG N2   N Y N 13  
A1BXG C9   C Y N 14  
A1BXG C11  C Y N 15  
A1BXG C12  C Y N 16  
A1BXG C14  C N N 17  
A1BXG H4   H N N 18  
A1BXG H6   H N N 19  
A1BXG H7   H N N 20  
A1BXG H8   H N N 21  
A1BXG H3   H N N 22  
A1BXG H1   H N N 23  
A1BXG H2   H N N 24  
A1BXG H5   H N N 25  
A1BXG H9   H N N 26  
A1BXG H10  H N N 27  
A1BXG H12  H N N 28  
A1BXG H11  H N N 29  
A1BXG H13  H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
DMS   S    S N N 118 
DMS   O    O N N 119 
DMS   C1   C N N 120 
DMS   C2   C N N 121 
DMS   H11  H N N 122 
DMS   H12  H N N 123 
DMS   H13  H N N 124 
DMS   H21  H N N 125 
DMS   H22  H N N 126 
DMS   H23  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
THR   N    N N N 344 
THR   CA   C N S 345 
THR   C    C N N 346 
THR   O    O N N 347 
THR   CB   C N R 348 
THR   OG1  O N N 349 
THR   CG2  C N N 350 
THR   OXT  O N N 351 
THR   H    H N N 352 
THR   H2   H N N 353 
THR   HA   H N N 354 
THR   HB   H N N 355 
THR   HG1  H N N 356 
THR   HG21 H N N 357 
THR   HG22 H N N 358 
THR   HG23 H N N 359 
THR   HXT  H N N 360 
TRP   N    N N N 361 
TRP   CA   C N S 362 
TRP   C    C N N 363 
TRP   O    O N N 364 
TRP   CB   C N N 365 
TRP   CG   C Y N 366 
TRP   CD1  C Y N 367 
TRP   CD2  C Y N 368 
TRP   NE1  N Y N 369 
TRP   CE2  C Y N 370 
TRP   CE3  C Y N 371 
TRP   CZ2  C Y N 372 
TRP   CZ3  C Y N 373 
TRP   CH2  C Y N 374 
TRP   OXT  O N N 375 
TRP   H    H N N 376 
TRP   H2   H N N 377 
TRP   HA   H N N 378 
TRP   HB2  H N N 379 
TRP   HB3  H N N 380 
TRP   HD1  H N N 381 
TRP   HE1  H N N 382 
TRP   HE3  H N N 383 
TRP   HZ2  H N N 384 
TRP   HZ3  H N N 385 
TRP   HH2  H N N 386 
TRP   HXT  H N N 387 
TYR   N    N N N 388 
TYR   CA   C N S 389 
TYR   C    C N N 390 
TYR   O    O N N 391 
TYR   CB   C N N 392 
TYR   CG   C Y N 393 
TYR   CD1  C Y N 394 
TYR   CD2  C Y N 395 
TYR   CE1  C Y N 396 
TYR   CE2  C Y N 397 
TYR   CZ   C Y N 398 
TYR   OH   O N N 399 
TYR   OXT  O N N 400 
TYR   H    H N N 401 
TYR   H2   H N N 402 
TYR   HA   H N N 403 
TYR   HB2  H N N 404 
TYR   HB3  H N N 405 
TYR   HD1  H N N 406 
TYR   HD2  H N N 407 
TYR   HE1  H N N 408 
TYR   HE2  H N N 409 
TYR   HH   H N N 410 
TYR   HXT  H N N 411 
VAL   N    N N N 412 
VAL   CA   C N S 413 
VAL   C    C N N 414 
VAL   O    O N N 415 
VAL   CB   C N N 416 
VAL   CG1  C N N 417 
VAL   CG2  C N N 418 
VAL   OXT  O N N 419 
VAL   H    H N N 420 
VAL   H2   H N N 421 
VAL   HA   H N N 422 
VAL   HB   H N N 423 
VAL   HG11 H N N 424 
VAL   HG12 H N N 425 
VAL   HG13 H N N 426 
VAL   HG21 H N N 427 
VAL   HG22 H N N 428 
VAL   HG23 H N N 429 
VAL   HXT  H N N 430 
# 
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 
A1BXG C1  C2   sing N N 1   
A1BXG C2  N1   doub Y N 2   
A1BXG N1  C3   sing Y N 3   
A1BXG C3  C4   doub Y N 4   
A1BXG C4  N2   sing Y N 5   
A1BXG C3  C5   sing N N 6   
A1BXG C5  C6   doub Y N 7   
A1BXG C6  C7   sing Y N 8   
A1BXG C7  C8   doub Y N 9   
A1BXG C8  C9   sing Y N 10  
A1BXG C9  N3   doub Y N 11  
A1BXG N3  C10  sing Y N 12  
A1BXG C10 C11  doub Y N 13  
A1BXG C11 C12  sing Y N 14  
A1BXG C12 C13  doub Y N 15  
A1BXG C8  C14  sing N N 16  
A1BXG C2  N2   sing Y N 17  
A1BXG C5  C13  sing Y N 18  
A1BXG C9  C13  sing Y N 19  
A1BXG C4  H4   sing N N 20  
A1BXG C6  H6   sing N N 21  
A1BXG C7  H7   sing N N 22  
A1BXG C10 H8   sing N N 23  
A1BXG C1  H3   sing N N 24  
A1BXG C1  H1   sing N N 25  
A1BXG C1  H2   sing N N 26  
A1BXG N2  H5   sing N N 27  
A1BXG C11 H9   sing N N 28  
A1BXG C12 H10  sing N N 29  
A1BXG C14 H12  sing N N 30  
A1BXG C14 H11  sing N N 31  
A1BXG C14 H13  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
DMS   S   O    doub N N 115 
DMS   S   C1   sing N N 116 
DMS   S   C2   sing N N 117 
DMS   C1  H11  sing N N 118 
DMS   C1  H12  sing N N 119 
DMS   C1  H13  sing N N 120 
DMS   C2  H21  sing N N 121 
DMS   C2  H22  sing N N 122 
DMS   C2  H23  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TRP   N   CA   sing N N 347 
TRP   N   H    sing N N 348 
TRP   N   H2   sing N N 349 
TRP   CA  C    sing N N 350 
TRP   CA  CB   sing N N 351 
TRP   CA  HA   sing N N 352 
TRP   C   O    doub N N 353 
TRP   C   OXT  sing N N 354 
TRP   CB  CG   sing N N 355 
TRP   CB  HB2  sing N N 356 
TRP   CB  HB3  sing N N 357 
TRP   CG  CD1  doub Y N 358 
TRP   CG  CD2  sing Y N 359 
TRP   CD1 NE1  sing Y N 360 
TRP   CD1 HD1  sing N N 361 
TRP   CD2 CE2  doub Y N 362 
TRP   CD2 CE3  sing Y N 363 
TRP   NE1 CE2  sing Y N 364 
TRP   NE1 HE1  sing N N 365 
TRP   CE2 CZ2  sing Y N 366 
TRP   CE3 CZ3  doub Y N 367 
TRP   CE3 HE3  sing N N 368 
TRP   CZ2 CH2  doub Y N 369 
TRP   CZ2 HZ2  sing N N 370 
TRP   CZ3 CH2  sing Y N 371 
TRP   CZ3 HZ3  sing N N 372 
TRP   CH2 HH2  sing N N 373 
TRP   OXT HXT  sing N N 374 
TYR   N   CA   sing N N 375 
TYR   N   H    sing N N 376 
TYR   N   H2   sing N N 377 
TYR   CA  C    sing N N 378 
TYR   CA  CB   sing N N 379 
TYR   CA  HA   sing N N 380 
TYR   C   O    doub N N 381 
TYR   C   OXT  sing N N 382 
TYR   CB  CG   sing N N 383 
TYR   CB  HB2  sing N N 384 
TYR   CB  HB3  sing N N 385 
TYR   CG  CD1  doub Y N 386 
TYR   CG  CD2  sing Y N 387 
TYR   CD1 CE1  sing Y N 388 
TYR   CD1 HD1  sing N N 389 
TYR   CD2 CE2  doub Y N 390 
TYR   CD2 HD2  sing N N 391 
TYR   CE1 CZ   doub Y N 392 
TYR   CE1 HE1  sing N N 393 
TYR   CE2 CZ   sing Y N 394 
TYR   CE2 HE2  sing N N 395 
TYR   CZ  OH   sing N N 396 
TYR   OH  HH   sing N N 397 
TYR   OXT HXT  sing N N 398 
VAL   N   CA   sing N N 399 
VAL   N   H    sing N N 400 
VAL   N   H2   sing N N 401 
VAL   CA  C    sing N N 402 
VAL   CA  CB   sing N N 403 
VAL   CA  HA   sing N N 404 
VAL   C   O    doub N N 405 
VAL   C   OXT  sing N N 406 
VAL   CB  CG1  sing N N 407 
VAL   CB  CG2  sing N N 408 
VAL   CB  HB   sing N N 409 
VAL   CG1 HG11 sing N N 410 
VAL   CG1 HG12 sing N N 411 
VAL   CG1 HG13 sing N N 412 
VAL   CG2 HG21 sing N N 413 
VAL   CG2 HG22 sing N N 414 
VAL   CG2 HG23 sing N N 415 
VAL   OXT HXT  sing N N 416 
# 
_pdbx_audit_support.funding_organization   'Australian Research Council (ARC)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           IC180100021 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002340 
_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' 
# 
_pdbx_initial_refinement_model.accession_code   8PN6 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7I1N 
_atom_sites.fract_transf_matrix[1][1]   0.023626 
_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]   0.023626 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -22.039 19.021  -7.166  1.00 71.88  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.921 17.867  -7.467  1.00 71.42  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.481 17.298  -8.827  1.00 67.23  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.153 18.054  -9.757  1.00 71.35  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -24.422 18.219  -7.379  1.00 72.64  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -25.168 17.726  -6.130  1.00 75.87  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.452 18.572  -5.235  1.00 80.04  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.539 16.514  -6.076  1.00 73.84  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.381 15.989  -8.883  1.00 61.55  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.272 15.222  -10.130 1.00 59.74  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.691 14.956  -10.633 1.00 56.95  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.616 14.828  -9.778  1.00 56.33  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.540 13.905  -9.880  1.00 58.89  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.144 14.119  -9.394  1.00 60.32  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.294 12.544  -9.185  1.00 61.35  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.630 13.154  -8.903  1.00 61.83  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.850 14.885  -11.961 1.00 53.77  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.132 14.596  -12.656 1.00 52.91  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -24.871 13.610  -13.797 1.00 51.52  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.735 13.431  -14.232 1.00 49.78  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.812 15.881  -13.130 1.00 54.41  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.014 16.708  -14.097 1.00 56.15  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.013 17.549  -13.654 1.00 57.17  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.237 16.619  -15.466 1.00 57.71  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.263 18.304  -14.546 1.00 58.69  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.508 17.373  -16.371 1.00 58.82  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.518 18.221  -15.904 1.00 59.50  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.774 18.961  -16.777 1.00 61.78  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -25.933 12.927  -14.205 1.00 51.64  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -25.886 11.923  -15.292 1.00 51.45  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.647 12.474  -16.514 1.00 53.20  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.603 13.265  -16.323 1.00 52.98  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.387 10.550  -14.804 1.00 49.90  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -27.810 10.578  -14.258 1.00 49.89  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.411 9.951   -13.813 1.00 49.94  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.460 9.210   -14.231 1.00 49.43  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.169 12.119  -17.714 1.00 54.15  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -26.840 12.338  -19.031 1.00 54.34  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -26.755 11.030  -19.828 1.00 51.70  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -25.664 10.441  -19.904 1.00 48.09  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.179 13.442  -19.846 1.00 57.55  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -25.955 14.738  -19.117 1.00 59.76  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.351 15.784  -20.040 1.00 63.79  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.424 15.456  -20.814 1.00 64.26  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.824 16.923  -20.011 1.00 69.96  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -27.893 10.564  -20.332 1.00 51.96  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -27.975 9.370   -21.210 1.00 52.28  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.070 9.569   -22.427 1.00 52.73  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.036 10.715  -22.961 1.00 54.41  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.405 9.135   -21.679 1.00 53.56  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -29.701 7.676   -21.977 1.00 53.97  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.195 7.384   -21.993 1.00 55.48  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.470 5.981   -22.261 1.00 56.24  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.212 5.374   -23.429 1.00 57.30  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -30.669 6.057   -24.423 1.00 59.30  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.466 4.085   -23.602 1.00 55.73  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.348 8.503   -22.811 1.00 52.15  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.418 8.445   -23.972 1.00 52.19  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -25.763 7.309   -24.950 1.00 51.50  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.002 7.181   -25.907 1.00 52.06  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -23.981 8.306   -23.499 1.00 51.06  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -26.817 6.511   -24.754 1.00 50.59  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.137 5.430   -25.711 1.00 51.34  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -27.777 4.204   -25.089 1.00 51.85  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -27.763 4.113   -23.817 1.00 50.10  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.266 3.278   -25.943 1.00 52.64  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -28.822 1.943   -25.577 1.00 53.90  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -27.659 0.996   -25.341 1.00 54.56  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.546 1.314   -25.844 1.00 54.49  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -29.713 1.301   -26.638 1.00 54.45  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -30.993 2.071   -26.835 1.00 57.11  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.190 3.044   -26.090 1.00 56.58  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -31.779 1.712   -27.735 1.00 58.80  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -27.910 -0.076  -24.576 1.00 54.49  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -26.926 -1.181  -24.418 1.00 55.08  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.342 -2.296  -25.379 1.00 54.41  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.297 -3.057  -25.081 1.00 53.80  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -26.801 -1.623  -22.965 1.00 55.26  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.027 -0.559  -22.186 1.00 56.46  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.144 -2.988  -22.879 1.00 54.98  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.360 -0.541  -20.741 1.00 55.36  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.614 -2.365  -26.500 0.25 54.84  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.661 -2.380  -26.523 0.25 54.84  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.614 -2.365  -26.500 0.25 54.84  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.661 -2.380  -26.523 0.25 54.84  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -26.874 -3.212  -27.695 0.25 56.05  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -26.967 -3.343  -27.614 0.25 55.90  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -26.874 -3.212  -27.695 0.25 56.05  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -26.967 -3.343  -27.614 0.25 55.90  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.549 -3.760  -28.260 0.25 56.00  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -25.665 -3.749  -28.337 0.25 56.13  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.549 -3.760  -28.260 0.25 56.00  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -25.665 -3.749  -28.337 0.25 56.13  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.535 -2.937  -28.413 0.25 55.41  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -24.794 -2.834  -28.648 0.25 55.80  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.535 -2.937  -28.413 0.25 55.41  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -24.794 -2.834  -28.648 0.25 55.80  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -27.547 -2.396  -28.805 0.25 57.28  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.024 -2.749  -28.557 0.25 56.98  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -27.547 -2.396  -28.805 0.25 57.28  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.024 -2.749  -28.557 0.25 56.98  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -26.679 -1.315  -29.150 0.25 57.00  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.251 -2.646  -27.828 0.25 56.02  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -26.679 -1.315  -29.150 0.25 57.00  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.251 -2.646  -27.828 0.25 56.02  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -28.895 -1.849  -28.397 0.25 57.66  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.241 -3.565  -29.811 0.25 58.03  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -28.895 -1.849  -28.397 0.25 57.66  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.241 -3.565  -29.811 0.25 58.03  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.533 -5.067  -28.590 1.00 56.52  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.467 -5.610  -29.473 1.00 61.78  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -24.700 -5.012  -30.873 1.00 68.70  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -25.844 -5.087  -31.363 1.00 70.57  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.506 -7.139  -29.501 1.00 63.54  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.372 -7.744  -30.272 1.00 65.02  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.314 -7.963  -31.618 1.00 65.47  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.135 -8.249  -29.735 1.00 64.89  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.113 -8.525  -31.951 1.00 65.02  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.382 -8.746  -30.820 1.00 65.60  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.597 -8.343  -28.453 1.00 62.25  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.116 -9.306  -30.648 1.00 66.29  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.346 -8.888  -28.290 1.00 62.47  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -19.619 -9.377  -29.362 1.00 61.66  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -23.707 -4.348  -31.461 1.00 74.68  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -23.842 -3.738  -32.810 1.00 82.01  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.030 -4.580  -33.791 1.00 82.25  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -21.779 -4.507  -33.757 1.00 79.61  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -23.364 -2.281  -32.841 1.00 89.41  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -24.118 -1.371  -31.870 1.00 96.59  ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -25.586 -1.134  -32.203 1.00 99.96  ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -25.876 -0.771  -33.377 1.00 106.56 ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -26.433 -1.303  -31.292 1.00 101.75 ? 62  GLU   A OE2 1 
ATOM   133  N N   A LYS   A 1 20  ? -23.710 -5.339  -34.657 0.25 83.64  ? 63  LYS   A N   1 
ATOM   134  N N   B LYS   A 1 20  ? -23.710 -5.339  -34.657 0.25 83.64  ? 63  LYS   A N   1 
ATOM   135  N N   C LYS   A 1 20  ? -23.728 -5.381  -34.607 0.25 82.84  ? 63  LYS   A N   1 
ATOM   136  N N   D LYS   A 1 20  ? -23.728 -5.381  -34.607 0.25 82.84  ? 63  LYS   A N   1 
ATOM   137  C CA  A LYS   A 1 20  ? -23.060 -6.207  -35.678 0.25 84.49  ? 63  LYS   A CA  1 
ATOM   138  C CA  B LYS   A 1 20  ? -23.060 -6.207  -35.678 0.25 84.49  ? 63  LYS   A CA  1 
ATOM   139  C CA  C LYS   A 1 20  ? -23.142 -6.187  -35.712 0.25 83.33  ? 63  LYS   A CA  1 
ATOM   140  C CA  D LYS   A 1 20  ? -23.142 -6.187  -35.712 0.25 83.33  ? 63  LYS   A CA  1 
ATOM   141  C C   A LYS   A 1 20  ? -22.227 -5.310  -36.600 0.25 83.20  ? 63  LYS   A C   1 
ATOM   142  C C   B LYS   A 1 20  ? -22.227 -5.310  -36.600 0.25 83.20  ? 63  LYS   A C   1 
ATOM   143  C C   C LYS   A 1 20  ? -22.348 -5.241  -36.613 0.25 82.64  ? 63  LYS   A C   1 
ATOM   144  C C   D LYS   A 1 20  ? -22.348 -5.241  -36.613 0.25 82.64  ? 63  LYS   A C   1 
ATOM   145  O O   A LYS   A 1 20  ? -22.662 -4.178  -36.869 0.25 84.63  ? 63  LYS   A O   1 
ATOM   146  O O   B LYS   A 1 20  ? -22.662 -4.178  -36.869 0.25 84.63  ? 63  LYS   A O   1 
ATOM   147  O O   C LYS   A 1 20  ? -22.850 -4.140  -36.896 0.25 84.66  ? 63  LYS   A O   1 
ATOM   148  O O   D LYS   A 1 20  ? -22.850 -4.140  -36.896 0.25 84.66  ? 63  LYS   A O   1 
ATOM   149  C CB  A LYS   A 1 20  ? -24.103 -7.039  -36.431 0.25 87.00  ? 63  LYS   A CB  1 
ATOM   150  C CB  B LYS   A 1 20  ? -24.103 -7.039  -36.431 0.25 87.00  ? 63  LYS   A CB  1 
ATOM   151  C CB  C LYS   A 1 20  ? -24.240 -6.932  -36.480 0.25 84.97  ? 63  LYS   A CB  1 
ATOM   152  C CB  D LYS   A 1 20  ? -24.240 -6.932  -36.480 0.25 84.97  ? 63  LYS   A CB  1 
ATOM   153  C CG  A LYS   A 1 20  ? -23.617 -8.418  -36.860 0.25 89.16  ? 63  LYS   A CG  1 
ATOM   154  C CG  B LYS   A 1 20  ? -23.617 -8.418  -36.860 0.25 89.16  ? 63  LYS   A CG  1 
ATOM   155  C CG  C LYS   A 1 20  ? -24.312 -8.432  -36.222 0.25 85.27  ? 63  LYS   A CG  1 
ATOM   156  C CG  D LYS   A 1 20  ? -24.312 -8.432  -36.222 0.25 85.27  ? 63  LYS   A CG  1 
ATOM   157  C CD  A LYS   A 1 20  ? -24.725 -9.402  -37.178 0.25 91.29  ? 63  LYS   A CD  1 
ATOM   158  C CD  B LYS   A 1 20  ? -24.725 -9.402  -37.178 0.25 91.29  ? 63  LYS   A CD  1 
ATOM   159  C CD  C LYS   A 1 20  ? -23.580 -9.268  -37.261 0.25 87.19  ? 63  LYS   A CD  1 
ATOM   160  C CD  D LYS   A 1 20  ? -23.580 -9.268  -37.261 0.25 87.19  ? 63  LYS   A CD  1 
ATOM   161  C CE  A LYS   A 1 20  ? -24.218 -10.823 -37.323 0.25 92.48  ? 63  LYS   A CE  1 
ATOM   162  C CE  B LYS   A 1 20  ? -24.218 -10.823 -37.323 0.25 92.48  ? 63  LYS   A CE  1 
ATOM   163  C CE  C LYS   A 1 20  ? -23.355 -10.706 -36.835 0.25 86.64  ? 63  LYS   A CE  1 
ATOM   164  C CE  D LYS   A 1 20  ? -23.355 -10.706 -36.835 0.25 86.64  ? 63  LYS   A CE  1 
ATOM   165  N NZ  A LYS   A 1 20  ? -25.312 -11.816 -37.209 0.25 93.38  ? 63  LYS   A NZ  1 
ATOM   166  N NZ  B LYS   A 1 20  ? -25.312 -11.816 -37.209 0.25 93.38  ? 63  LYS   A NZ  1 
ATOM   167  N NZ  C LYS   A 1 20  ? -24.611 -11.360 -36.392 0.25 86.57  ? 63  LYS   A NZ  1 
ATOM   168  N NZ  D LYS   A 1 20  ? -24.611 -11.360 -36.392 0.25 86.57  ? 63  LYS   A NZ  1 
ATOM   169  N N   A ASP   A 1 21  ? -21.047 -5.777  -37.008 0.25 81.70  ? 64  ASP   A N   1 
ATOM   170  N N   B ASP   A 1 21  ? -21.047 -5.777  -37.008 0.25 81.70  ? 64  ASP   A N   1 
ATOM   171  N N   C ASP   A 1 21  ? -21.136 -5.633  -36.999 0.25 81.36  ? 64  ASP   A N   1 
ATOM   172  N N   D ASP   A 1 21  ? -21.136 -5.633  -36.999 0.25 81.36  ? 64  ASP   A N   1 
ATOM   173  C CA  A ASP   A 1 21  ? -20.079 -4.995  -37.824 0.25 83.15  ? 64  ASP   A CA  1 
ATOM   174  C CA  B ASP   A 1 21  ? -20.079 -4.995  -37.824 0.25 83.15  ? 64  ASP   A CA  1 
ATOM   175  C CA  C ASP   A 1 21  ? -20.250 -4.800  -37.850 0.25 83.13  ? 64  ASP   A CA  1 
ATOM   176  C CA  D ASP   A 1 21  ? -20.250 -4.800  -37.850 0.25 83.13  ? 64  ASP   A CA  1 
ATOM   177  C C   A ASP   A 1 21  ? -19.714 -3.710  -37.061 0.25 80.60  ? 64  ASP   A C   1 
ATOM   178  C C   B ASP   A 1 21  ? -19.714 -3.710  -37.061 0.25 80.60  ? 64  ASP   A C   1 
ATOM   179  C C   C ASP   A 1 21  ? -19.762 -3.600  -37.028 0.25 80.50  ? 64  ASP   A C   1 
ATOM   180  C C   D ASP   A 1 21  ? -19.762 -3.600  -37.028 0.25 80.50  ? 64  ASP   A C   1 
ATOM   181  O O   A ASP   A 1 21  ? -20.069 -2.614  -37.532 0.25 82.20  ? 64  ASP   A O   1 
ATOM   182  O O   B ASP   A 1 21  ? -20.069 -2.614  -37.532 0.25 82.20  ? 64  ASP   A O   1 
ATOM   183  O O   C ASP   A 1 21  ? -20.061 -2.458  -37.425 0.25 82.04  ? 64  ASP   A O   1 
ATOM   184  O O   D ASP   A 1 21  ? -20.061 -2.458  -37.425 0.25 82.04  ? 64  ASP   A O   1 
ATOM   185  C CB  A ASP   A 1 21  ? -20.633 -4.716  -39.230 0.25 86.50  ? 64  ASP   A CB  1 
ATOM   186  C CB  B ASP   A 1 21  ? -20.633 -4.716  -39.230 0.25 86.50  ? 64  ASP   A CB  1 
ATOM   187  C CB  C ASP   A 1 21  ? -20.983 -4.341  -39.120 0.25 86.35  ? 64  ASP   A CB  1 
ATOM   188  C CB  D ASP   A 1 21  ? -20.983 -4.341  -39.120 0.25 86.35  ? 64  ASP   A CB  1 
ATOM   189  C CG  A ASP   A 1 21  ? -20.494 -5.870  -40.217 0.25 88.21  ? 64  ASP   A CG  1 
ATOM   190  C CG  B ASP   A 1 21  ? -20.494 -5.870  -40.217 0.25 88.21  ? 64  ASP   A CG  1 
ATOM   191  C CG  C ASP   A 1 21  ? -21.432 -5.465  -40.046 0.25 88.36  ? 64  ASP   A CG  1 
ATOM   192  C CG  D ASP   A 1 21  ? -21.432 -5.465  -40.046 0.25 88.36  ? 64  ASP   A CG  1 
ATOM   193  O OD1 A ASP   A 1 21  ? -19.349 -6.169  -40.622 0.25 88.40  ? 64  ASP   A OD1 1 
ATOM   194  O OD1 B ASP   A 1 21  ? -19.349 -6.169  -40.622 0.25 88.40  ? 64  ASP   A OD1 1 
ATOM   195  O OD1 C ASP   A 1 21  ? -20.551 -6.172  -40.589 0.25 89.35  ? 64  ASP   A OD1 1 
ATOM   196  O OD1 D ASP   A 1 21  ? -20.551 -6.172  -40.589 0.25 89.35  ? 64  ASP   A OD1 1 
ATOM   197  O OD2 A ASP   A 1 21  ? -21.535 -6.458  -40.586 0.25 89.89  ? 64  ASP   A OD2 1 
ATOM   198  O OD2 B ASP   A 1 21  ? -21.535 -6.458  -40.586 0.25 89.89  ? 64  ASP   A OD2 1 
ATOM   199  O OD2 C ASP   A 1 21  ? -22.663 -5.620  -40.225 0.25 89.16  ? 64  ASP   A OD2 1 
ATOM   200  O OD2 D ASP   A 1 21  ? -22.663 -5.620  -40.225 0.25 89.16  ? 64  ASP   A OD2 1 
ATOM   201  N N   A ALA   A 1 22  ? -19.047 -3.863  -35.911 0.25 77.54  ? 65  ALA   A N   1 
ATOM   202  N N   B ALA   A 1 22  ? -19.047 -3.863  -35.911 0.25 77.54  ? 65  ALA   A N   1 
ATOM   203  N N   C ALA   A 1 22  ? -19.055 -3.846  -35.917 0.25 77.53  ? 65  ALA   A N   1 
ATOM   204  N N   D ALA   A 1 22  ? -19.055 -3.846  -35.917 0.25 77.53  ? 65  ALA   A N   1 
ATOM   205  C CA  A ALA   A 1 22  ? -18.376 -2.799  -35.125 0.25 74.58  ? 65  ALA   A CA  1 
ATOM   206  C CA  B ALA   A 1 22  ? -18.376 -2.799  -35.125 0.25 74.58  ? 65  ALA   A CA  1 
ATOM   207  C CA  C ALA   A 1 22  ? -18.373 -2.800  -35.116 0.25 74.56  ? 65  ALA   A CA  1 
ATOM   208  C CA  D ALA   A 1 22  ? -18.373 -2.800  -35.116 0.25 74.56  ? 65  ALA   A CA  1 
ATOM   209  C C   A ALA   A 1 22  ? -16.860 -2.930  -35.313 0.25 73.07  ? 65  ALA   A C   1 
ATOM   210  C C   B ALA   A 1 22  ? -16.860 -2.930  -35.313 0.25 73.07  ? 65  ALA   A C   1 
ATOM   211  C C   C ALA   A 1 22  ? -16.859 -2.932  -35.309 0.25 73.06  ? 65  ALA   A C   1 
ATOM   212  C C   D ALA   A 1 22  ? -16.859 -2.932  -35.309 0.25 73.06  ? 65  ALA   A C   1 
ATOM   213  O O   A ALA   A 1 22  ? -16.412 -4.032  -35.714 0.25 72.39  ? 65  ALA   A O   1 
ATOM   214  O O   B ALA   A 1 22  ? -16.412 -4.032  -35.714 0.25 72.39  ? 65  ALA   A O   1 
ATOM   215  O O   C ALA   A 1 22  ? -16.411 -4.034  -35.708 0.25 72.38  ? 65  ALA   A O   1 
ATOM   216  O O   D ALA   A 1 22  ? -16.411 -4.034  -35.708 0.25 72.38  ? 65  ALA   A O   1 
ATOM   217  C CB  A ALA   A 1 22  ? -18.753 -2.919  -33.671 0.25 73.69  ? 65  ALA   A CB  1 
ATOM   218  C CB  B ALA   A 1 22  ? -18.753 -2.919  -33.671 0.25 73.69  ? 65  ALA   A CB  1 
ATOM   219  C CB  C ALA   A 1 22  ? -18.752 -2.925  -33.664 0.25 73.68  ? 65  ALA   A CB  1 
ATOM   220  C CB  D ALA   A 1 22  ? -18.752 -2.925  -33.664 0.25 73.68  ? 65  ALA   A CB  1 
ATOM   221  N N   . GLU   A 1 23  ? -16.110 -1.853  -35.011 1.00 72.23  ? 66  GLU   A N   1 
ATOM   222  C CA  . GLU   A 1 23  ? -14.625 -1.825  -35.164 1.00 72.39  ? 66  GLU   A CA  1 
ATOM   223  C C   . GLU   A 1 23  ? -13.951 -2.863  -34.242 1.00 69.51  ? 66  GLU   A C   1 
ATOM   224  O O   . GLU   A 1 23  ? -14.159 -2.799  -32.997 1.00 60.84  ? 66  GLU   A O   1 
ATOM   225  C CB  . GLU   A 1 23  ? -14.131 -0.413  -34.852 1.00 78.15  ? 66  GLU   A CB  1 
ATOM   226  C CG  . GLU   A 1 23  ? -12.618 -0.273  -34.826 1.00 83.08  ? 66  GLU   A CG  1 
ATOM   227  C CD  . GLU   A 1 23  ? -12.160 1.005   -34.142 1.00 89.72  ? 66  GLU   A CD  1 
ATOM   228  O OE1 . GLU   A 1 23  ? -13.016 1.938   -33.964 1.00 91.86  ? 66  GLU   A OE1 1 
ATOM   229  O OE2 . GLU   A 1 23  ? -10.957 1.057   -33.771 1.00 93.23  ? 66  GLU   A OE2 1 
ATOM   230  N N   . VAL   A 1 24  ? -13.183 -3.800  -34.811 1.00 66.21  ? 67  VAL   A N   1 
ATOM   231  C CA  . VAL   A 1 24  ? -12.574 -4.941  -34.065 1.00 65.35  ? 67  VAL   A CA  1 
ATOM   232  C C   . VAL   A 1 24  ? -11.082 -4.656  -33.897 1.00 65.73  ? 67  VAL   A C   1 
ATOM   233  O O   . VAL   A 1 24  ? -10.396 -4.432  -34.907 1.00 65.85  ? 67  VAL   A O   1 
ATOM   234  C CB  . VAL   A 1 24  ? -12.808 -6.296  -34.753 1.00 66.06  ? 67  VAL   A CB  1 
ATOM   235  C CG1 . VAL   A 1 24  ? -12.166 -7.421  -33.966 1.00 64.56  ? 67  VAL   A CG1 1 
ATOM   236  C CG2 . VAL   A 1 24  ? -14.286 -6.571  -34.997 1.00 66.43  ? 67  VAL   A CG2 1 
ATOM   237  N N   . THR   A 1 25  ? -10.591 -4.666  -32.662 1.00 63.46  ? 68  THR   A N   1 
ATOM   238  C CA  . THR   A 1 25  ? -9.251  -4.145  -32.309 1.00 63.85  ? 68  THR   A CA  1 
ATOM   239  C C   . THR   A 1 25  ? -8.897  -4.645  -30.909 1.00 63.86  ? 68  THR   A C   1 
ATOM   240  O O   . THR   A 1 25  ? -9.752  -5.339  -30.291 1.00 61.18  ? 68  THR   A O   1 
ATOM   241  C CB  . THR   A 1 25  ? -9.232  -2.613  -32.426 1.00 65.30  ? 68  THR   A CB  1 
ATOM   242  O OG1 . THR   A 1 25  ? -7.875  -2.163  -32.420 1.00 67.06  ? 68  THR   A OG1 1 
ATOM   243  C CG2 . THR   A 1 25  ? -10.002 -1.900  -31.333 1.00 64.89  ? 68  THR   A CG2 1 
ATOM   244  N N   . GLY   A 1 26  ? -7.686  -4.292  -30.466 1.00 64.19  ? 69  GLY   A N   1 
ATOM   245  C CA  . GLY   A 1 26  ? -7.046  -4.740  -29.217 1.00 64.18  ? 69  GLY   A CA  1 
ATOM   246  C C   . GLY   A 1 26  ? -6.659  -6.220  -29.245 1.00 64.23  ? 69  GLY   A C   1 
ATOM   247  O O   . GLY   A 1 26  ? -7.396  -7.058  -29.838 1.00 67.29  ? 69  GLY   A O   1 
ATOM   248  N N   . ASN   A 1 27  ? -5.580  -6.518  -28.483 1.00 65.56  ? 70  ASN   A N   1 
ATOM   249  C CA  . ASN   A 1 27  ? -5.012  -7.879  -28.271 1.00 65.62  ? 70  ASN   A CA  1 
ATOM   250  C C   . ASN   A 1 27  ? -5.653  -8.515  -27.009 1.00 62.02  ? 70  ASN   A C   1 
ATOM   251  O O   . ASN   A 1 27  ? -6.701  -7.967  -26.543 1.00 59.23  ? 70  ASN   A O   1 
ATOM   252  C CB  . ASN   A 1 27  ? -3.487  -7.764  -28.232 1.00 68.33  ? 70  ASN   A CB  1 
ATOM   253  C CG  . ASN   A 1 27  ? -3.033  -7.074  -26.963 1.00 70.87  ? 70  ASN   A CG  1 
ATOM   254  O OD1 . ASN   A 1 27  ? -3.424  -5.937  -26.708 1.00 71.77  ? 70  ASN   A OD1 1 
ATOM   255  N ND2 . ASN   A 1 27  ? -2.265  -7.767  -26.132 1.00 74.10  ? 70  ASN   A ND2 1 
ATOM   256  N N   . SER   A 1 28  ? -5.096  -9.643  -26.513 1.00 60.14  ? 71  SER   A N   1 
ATOM   257  C CA  . SER   A 1 28  ? -5.657  -10.510 -25.435 1.00 60.39  ? 71  SER   A CA  1 
ATOM   258  C C   . SER   A 1 28  ? -4.564  -10.997 -24.491 1.00 60.55  ? 71  SER   A C   1 
ATOM   259  O O   . SER   A 1 28  ? -4.355  -12.209 -24.414 1.00 61.51  ? 71  SER   A O   1 
ATOM   260  C CB  . SER   A 1 28  ? -6.358  -11.716 -25.997 1.00 61.93  ? 71  SER   A CB  1 
ATOM   261  O OG  . SER   A 1 28  ? -7.195  -11.372 -27.087 1.00 66.13  ? 71  SER   A OG  1 
ATOM   262  N N   . PRO   A 1 29  ? -3.841  -10.119 -23.749 1.00 61.21  ? 72  PRO   A N   1 
ATOM   263  C CA  . PRO   A 1 29  ? -2.703  -10.561 -22.928 1.00 63.09  ? 72  PRO   A CA  1 
ATOM   264  C C   . PRO   A 1 29  ? -3.133  -11.367 -21.687 1.00 60.67  ? 72  PRO   A C   1 
ATOM   265  O O   . PRO   A 1 29  ? -4.193  -11.083 -21.152 1.00 56.67  ? 72  PRO   A O   1 
ATOM   266  C CB  . PRO   A 1 29  ? -1.983  -9.246  -22.555 1.00 63.66  ? 72  PRO   A CB  1 
ATOM   267  C CG  . PRO   A 1 29  ? -3.101  -8.197  -22.559 1.00 62.83  ? 72  PRO   A CG  1 
ATOM   268  C CD  . PRO   A 1 29  ? -4.085  -8.672  -23.619 1.00 62.03  ? 72  PRO   A CD  1 
ATOM   269  N N   . ARG   A 1 30  ? -2.356  -12.403 -21.348 1.00 64.38  ? 73  ARG   A N   1 
ATOM   270  C CA  . ARG   A 1 30  ? -2.383  -13.129 -20.035 1.00 68.57  ? 73  ARG   A CA  1 
ATOM   271  C C   . ARG   A 1 30  ? -1.416  -12.414 -19.074 1.00 66.58  ? 73  ARG   A C   1 
ATOM   272  O O   . ARG   A 1 30  ? -0.201  -12.431 -19.349 1.00 65.29  ? 73  ARG   A O   1 
ATOM   273  C CB  . ARG   A 1 30  ? -2.032  -14.619 -20.183 1.00 72.60  ? 73  ARG   A CB  1 
ATOM   274  C CG  . ARG   A 1 30  ? -3.125  -15.450 -20.842 1.00 77.73  ? 73  ARG   A CG  1 
ATOM   275  C CD  . ARG   A 1 30  ? -2.669  -16.771 -21.458 1.00 86.73  ? 73  ARG   A CD  1 
ATOM   276  N NE  . ARG   A 1 30  ? -3.624  -17.308 -22.444 1.00 92.94  ? 73  ARG   A NE  1 
ATOM   277  C CZ  . ARG   A 1 30  ? -4.664  -18.109 -22.170 1.00 93.83  ? 73  ARG   A CZ  1 
ATOM   278  N NH1 . ARG   A 1 30  ? -4.897  -18.500 -20.925 1.00 96.79  ? 73  ARG   A NH1 1 
ATOM   279  N NH2 . ARG   A 1 30  ? -5.470  -18.513 -23.142 1.00 90.07  ? 73  ARG   A NH2 1 
ATOM   280  N N   . LEU   A 1 31  ? -1.938  -11.749 -18.033 1.00 62.79  ? 74  LEU   A N   1 
ATOM   281  C CA  . LEU   A 1 31  ? -1.115  -10.914 -17.115 1.00 62.82  ? 74  LEU   A CA  1 
ATOM   282  C C   . LEU   A 1 31  ? -1.236  -11.416 -15.662 1.00 59.99  ? 74  LEU   A C   1 
ATOM   283  O O   . LEU   A 1 31  ? -2.354  -11.752 -15.218 1.00 55.97  ? 74  LEU   A O   1 
ATOM   284  C CB  . LEU   A 1 31  ? -1.561  -9.456  -17.250 1.00 63.59  ? 74  LEU   A CB  1 
ATOM   285  C CG  . LEU   A 1 31  ? -1.321  -8.799  -18.608 1.00 63.73  ? 74  LEU   A CG  1 
ATOM   286  C CD1 . LEU   A 1 31  ? -1.967  -7.418  -18.641 1.00 63.36  ? 74  LEU   A CD1 1 
ATOM   287  C CD2 . LEU   A 1 31  ? 0.174   -8.702  -18.930 1.00 64.91  ? 74  LEU   A CD2 1 
ATOM   288  N N   . ASP   A 1 32  ? -0.096  -11.498 -14.975 1.00 60.99  ? 75  ASP   A N   1 
ATOM   289  C CA  . ASP   A 1 32  ? 0.013   -11.804 -13.529 1.00 60.53  ? 75  ASP   A CA  1 
ATOM   290  C C   . ASP   A 1 32  ? -0.194  -10.505 -12.754 1.00 58.50  ? 75  ASP   A C   1 
ATOM   291  O O   . ASP   A 1 32  ? 0.681   -9.598  -12.874 1.00 58.00  ? 75  ASP   A O   1 
ATOM   292  C CB  . ASP   A 1 32  ? 1.376   -12.399 -13.197 1.00 64.54  ? 75  ASP   A CB  1 
ATOM   293  C CG  . ASP   A 1 32  ? 1.505   -13.891 -13.472 1.00 67.90  ? 75  ASP   A CG  1 
ATOM   294  O OD1 . ASP   A 1 32  ? 0.499   -14.625 -13.318 1.00 68.53  ? 75  ASP   A OD1 1 
ATOM   295  O OD2 . ASP   A 1 32  ? 2.624   -14.305 -13.834 1.00 73.33  ? 75  ASP   A OD2 1 
ATOM   296  N N   . VAL   A 1 33  ? -1.295  -10.415 -11.995 1.00 56.66  ? 76  VAL   A N   1 
ATOM   297  C CA  . VAL   A 1 33  ? -1.679  -9.170  -11.249 1.00 56.52  ? 76  VAL   A CA  1 
ATOM   298  C C   . VAL   A 1 33  ? -2.008  -9.497  -9.785  1.00 55.38  ? 76  VAL   A C   1 
ATOM   299  O O   . VAL   A 1 33  ? -2.483  -10.637 -9.480  1.00 53.87  ? 76  VAL   A O   1 
ATOM   300  C CB  . VAL   A 1 33  ? -2.840  -8.396  -11.913 1.00 54.69  ? 76  VAL   A CB  1 
ATOM   301  C CG1 . VAL   A 1 33  ? -2.510  -7.979  -13.346 1.00 55.82  ? 76  VAL   A CG1 1 
ATOM   302  C CG2 . VAL   A 1 33  ? -4.146  -9.168  -11.862 1.00 53.23  ? 76  VAL   A CG2 1 
ATOM   303  N N   . ALA   A 1 34  ? -1.803  -8.504  -8.919  1.00 55.84  ? 77  ALA   A N   1 
ATOM   304  C CA  . ALA   A 1 34  ? -2.204  -8.503  -7.489  1.00 55.57  ? 77  ALA   A CA  1 
ATOM   305  C C   . ALA   A 1 34  ? -3.230  -7.387  -7.302  1.00 54.40  ? 77  ALA   A C   1 
ATOM   306  O O   . ALA   A 1 34  ? -3.100  -6.380  -7.991  1.00 55.39  ? 77  ALA   A O   1 
ATOM   307  C CB  . ALA   A 1 34  ? -1.000  -8.318  -6.596  1.00 56.64  ? 77  ALA   A CB  1 
ATOM   308  N N   . LEU   A 1 35  ? -4.243  -7.607  -6.469  1.00 53.48  ? 78  LEU   A N   1 
ATOM   309  C CA  . LEU   A 1 35  ? -5.294  -6.621  -6.112  1.00 53.23  ? 78  LEU   A CA  1 
ATOM   310  C C   . LEU   A 1 35  ? -5.101  -6.251  -4.634  1.00 54.70  ? 78  LEU   A C   1 
ATOM   311  O O   . LEU   A 1 35  ? -5.123  -7.155  -3.780  1.00 55.74  ? 78  LEU   A O   1 
ATOM   312  C CB  . LEU   A 1 35  ? -6.669  -7.249  -6.390  1.00 52.57  ? 78  LEU   A CB  1 
ATOM   313  C CG  . LEU   A 1 35  ? -7.893  -6.391  -6.042  1.00 52.77  ? 78  LEU   A CG  1 
ATOM   314  C CD1 . LEU   A 1 35  ? -7.868  -5.045  -6.747  1.00 53.21  ? 78  LEU   A CD1 1 
ATOM   315  C CD2 . LEU   A 1 35  ? -9.197  -7.116  -6.341  1.00 51.58  ? 78  LEU   A CD2 1 
ATOM   316  N N   . ASP   A 1 36  ? -4.859  -4.972  -4.351  1.00 55.40  ? 79  ASP   A N   1 
ATOM   317  C CA  . ASP   A 1 36  ? -4.600  -4.443  -2.989  1.00 55.31  ? 79  ASP   A CA  1 
ATOM   318  C C   . ASP   A 1 36  ? -5.947  -4.098  -2.317  1.00 54.90  ? 79  ASP   A C   1 
ATOM   319  O O   . ASP   A 1 36  ? -7.034  -4.164  -2.982  1.00 52.28  ? 79  ASP   A O   1 
ATOM   320  C CB  . ASP   A 1 36  ? -3.556  -3.318  -3.056  1.00 56.36  ? 79  ASP   A CB  1 
ATOM   321  C CG  . ASP   A 1 36  ? -4.097  -1.942  -3.420  1.00 56.25  ? 79  ASP   A CG  1 
ATOM   322  O OD1 . ASP   A 1 36  ? -5.322  -1.810  -3.582  1.00 56.41  ? 79  ASP   A OD1 1 
ATOM   323  O OD2 . ASP   A 1 36  ? -3.290  -1.004  -3.500  1.00 57.58  ? 79  ASP   A OD2 1 
ATOM   324  N N   . GLU   A 1 37  ? -5.899  -3.790  -1.017  1.00 55.09  ? 80  GLU   A N   1 
ATOM   325  C CA  . GLU   A 1 37  ? -7.098  -3.472  -0.205  1.00 54.80  ? 80  GLU   A CA  1 
ATOM   326  C C   . GLU   A 1 37  ? -7.767  -2.185  -0.717  1.00 52.70  ? 80  GLU   A C   1 
ATOM   327  O O   . GLU   A 1 37  ? -8.977  -2.049  -0.519  1.00 50.23  ? 80  GLU   A O   1 
ATOM   328  C CB  . GLU   A 1 37  ? -6.713  -3.377  1.280   1.00 57.70  ? 80  GLU   A CB  1 
ATOM   329  C CG  . GLU   A 1 37  ? -7.886  -3.677  2.195   1.00 58.68  ? 80  GLU   A CG  1 
ATOM   330  C CD  . GLU   A 1 37  ? -7.638  -3.597  3.708   1.00 60.78  ? 80  GLU   A CD  1 
ATOM   331  O OE1 . GLU   A 1 37  ? -7.063  -2.579  4.198   1.00 58.44  ? 80  GLU   A OE1 1 
ATOM   332  O OE2 . GLU   A 1 37  ? -8.051  -4.559  4.397   1.00 62.73  ? 80  GLU   A OE2 1 
ATOM   333  N N   . SER   A 1 38  ? -7.008  -1.271  -1.332  1.00 54.00  ? 81  SER   A N   1 
ATOM   334  C CA  . SER   A 1 38  ? -7.504  0.004   -1.915  1.00 54.13  ? 81  SER   A CA  1 
ATOM   335  C C   . SER   A 1 38  ? -8.140  -0.219  -3.289  1.00 52.75  ? 81  SER   A C   1 
ATOM   336  O O   . SER   A 1 38  ? -8.495  0.801   -3.897  1.00 52.46  ? 81  SER   A O   1 
ATOM   337  C CB  . SER   A 1 38  ? -6.411  1.022   -2.036  1.00 56.07  ? 81  SER   A CB  1 
ATOM   338  O OG  . SER   A 1 38  ? -5.797  1.249   -0.782  1.00 59.95  ? 81  SER   A OG  1 
ATOM   339  N N   . GLY   A 1 39  ? -8.260  -1.469  -3.763  1.00 52.48  ? 82  GLY   A N   1 
ATOM   340  C CA  . GLY   A 1 39  ? -8.879  -1.806  -5.072  1.00 52.99  ? 82  GLY   A CA  1 
ATOM   341  C C   . GLY   A 1 39  ? -8.008  -1.492  -6.310  1.00 53.50  ? 82  GLY   A C   1 
ATOM   342  O O   . GLY   A 1 39  ? -8.574  -1.473  -7.437  1.00 50.35  ? 82  GLY   A O   1 
ATOM   343  N N   . ASP   A 1 40  ? -6.695  -1.258  -6.136  1.00 54.65  ? 83  ASP   A N   1 
ATOM   344  C CA  . ASP   A 1 40  ? -5.727  -0.956  -7.231  1.00 55.71  ? 83  ASP   A CA  1 
ATOM   345  C C   . ASP   A 1 40  ? -5.030  -2.258  -7.666  1.00 54.65  ? 83  ASP   A C   1 
ATOM   346  O O   . ASP   A 1 40  ? -4.374  -2.926  -6.829  1.00 54.17  ? 83  ASP   A O   1 
ATOM   347  C CB  . ASP   A 1 40  ? -4.722  0.127   -6.809  1.00 58.19  ? 83  ASP   A CB  1 
ATOM   348  C CG  . ASP   A 1 40  ? -5.324  1.496   -6.510  1.00 60.04  ? 83  ASP   A CG  1 
ATOM   349  O OD1 . ASP   A 1 40  ? -6.304  1.887   -7.180  1.00 61.59  ? 83  ASP   A OD1 1 
ATOM   350  O OD2 . ASP   A 1 40  ? -4.816  2.163   -5.603  1.00 64.96  ? 83  ASP   A OD2 1 
ATOM   351  N N   . PHE   A 1 41  ? -5.144  -2.607  -8.947  1.00 53.48  ? 84  PHE   A N   1 
ATOM   352  C CA  . PHE   A 1 41  ? -4.417  -3.747  -9.563  1.00 52.03  ? 84  PHE   A CA  1 
ATOM   353  C C   . PHE   A 1 41  ? -2.959  -3.352  -9.798  1.00 54.63  ? 84  PHE   A C   1 
ATOM   354  O O   . PHE   A 1 41  ? -2.653  -2.167  -9.910  1.00 55.12  ? 84  PHE   A O   1 
ATOM   355  C CB  . PHE   A 1 41  ? -5.073  -4.172  -10.865 1.00 49.00  ? 84  PHE   A CB  1 
ATOM   356  C CG  . PHE   A 1 41  ? -6.343  -4.973  -10.748 1.00 46.50  ? 84  PHE   A CG  1 
ATOM   357  C CD1 . PHE   A 1 41  ? -6.301  -6.307  -10.391 1.00 45.62  ? 84  PHE   A CD1 1 
ATOM   358  C CD2 . PHE   A 1 41  ? -7.572  -4.420  -11.086 1.00 45.19  ? 84  PHE   A CD2 1 
ATOM   359  C CE1 . PHE   A 1 41  ? -7.466  -7.056  -10.340 1.00 45.21  ? 84  PHE   A CE1 1 
ATOM   360  C CE2 . PHE   A 1 41  ? -8.739  -5.168  -11.016 1.00 43.37  ? 84  PHE   A CE2 1 
ATOM   361  C CZ  . PHE   A 1 41  ? -8.678  -6.491  -10.682 1.00 43.87  ? 84  PHE   A CZ  1 
ATOM   362  N N   . SER   A 1 42  ? -2.076  -4.341  -9.853  1.00 56.93  ? 85  SER   A N   1 
ATOM   363  C CA  . SER   A 1 42  ? -0.624  -4.156  -10.081 1.00 60.08  ? 85  SER   A CA  1 
ATOM   364  C C   . SER   A 1 42  ? -0.047  -5.417  -10.734 1.00 61.75  ? 85  SER   A C   1 
ATOM   365  O O   . SER   A 1 42  ? -0.626  -6.504  -10.550 1.00 59.07  ? 85  SER   A O   1 
ATOM   366  C CB  . SER   A 1 42  ? 0.052   -3.856  -8.785  1.00 62.22  ? 85  SER   A CB  1 
ATOM   367  O OG  . SER   A 1 42  ? -0.171  -4.921  -7.863  1.00 63.46  ? 85  SER   A OG  1 
ATOM   368  N N   . LEU   A 1 43  ? 1.046   -5.270  -11.487 1.00 66.06  ? 86  LEU   A N   1 
ATOM   369  C CA  . LEU   A 1 43  ? 1.692   -6.403  -12.195 1.00 66.91  ? 86  LEU   A CA  1 
ATOM   370  C C   . LEU   A 1 43  ? 2.630   -7.130  -11.227 1.00 67.62  ? 86  LEU   A C   1 
ATOM   371  O O   . LEU   A 1 43  ? 3.603   -6.545  -10.730 1.00 63.89  ? 86  LEU   A O   1 
ATOM   372  C CB  . LEU   A 1 43  ? 2.424   -5.896  -13.437 1.00 69.17  ? 86  LEU   A CB  1 
ATOM   373  C CG  . LEU   A 1 43  ? 1.518   -5.631  -14.633 1.00 69.97  ? 86  LEU   A CG  1 
ATOM   374  C CD1 . LEU   A 1 43  ? 2.203   -4.704  -15.620 1.00 71.95  ? 86  LEU   A CD1 1 
ATOM   375  C CD2 . LEU   A 1 43  ? 1.112   -6.943  -15.298 1.00 70.93  ? 86  LEU   A CD2 1 
ATOM   376  N N   . VAL   A 1 44  ? 2.277   -8.371  -10.944 1.00 70.10  ? 87  VAL   A N   1 
ATOM   377  C CA  . VAL   A 1 44  ? 3.134   -9.358  -10.241 1.00 74.66  ? 87  VAL   A CA  1 
ATOM   378  C C   . VAL   A 1 44  ? 4.096   -9.924  -11.277 1.00 79.02  ? 87  VAL   A C   1 
ATOM   379  O O   . VAL   A 1 44  ? 3.634   -10.310 -12.360 1.00 81.08  ? 87  VAL   A O   1 
ATOM   380  C CB  . VAL   A 1 44  ? 2.252   -10.458 -9.639  1.00 72.98  ? 87  VAL   A CB  1 
ATOM   381  C CG1 . VAL   A 1 44  ? 3.079   -11.652 -9.190  1.00 74.86  ? 87  VAL   A CG1 1 
ATOM   382  C CG2 . VAL   A 1 44  ? 1.375   -9.883  -8.535  1.00 72.39  ? 87  VAL   A CG2 1 
ATOM   383  N N   . GLU   A 1 45  ? 5.384   -9.963  -10.980 1.00 84.51  ? 88  GLU   A N   1 
ATOM   384  C CA  . GLU   A 1 45  ? 6.382   -10.449 -11.969 1.00 90.04  ? 88  GLU   A CA  1 
ATOM   385  C C   . GLU   A 1 45  ? 7.440   -11.306 -11.251 1.00 92.25  ? 88  GLU   A C   1 
ATOM   386  O O   . GLU   A 1 45  ? 7.165   -12.316 -10.571 1.00 88.57  ? 88  GLU   A O   1 
ATOM   387  C CB  . GLU   A 1 45  ? 6.932   -9.229  -12.715 1.00 92.15  ? 88  GLU   A CB  1 
ATOM   388  C CG  . GLU   A 1 45  ? 5.866   -8.418  -13.447 1.00 92.33  ? 88  GLU   A CG  1 
ATOM   389  C CD  . GLU   A 1 45  ? 5.311   -9.085  -14.695 1.00 90.61  ? 88  GLU   A CD  1 
ATOM   390  O OE1 . GLU   A 1 45  ? 4.060   -9.166  -14.842 1.00 87.51  ? 88  GLU   A OE1 1 
ATOM   391  O OE2 . GLU   A 1 45  ? 6.140   -9.524  -15.509 1.00 89.88  ? 88  GLU   A OE2 1 
ATOM   392  N N   . GLY   B 2 7   ? -36.619 11.645  -11.811 1.00 86.46  ? 16  GLY   B N   1 
ATOM   393  C CA  . GLY   B 2 7   ? -35.524 11.753  -12.836 1.00 86.53  ? 16  GLY   B CA  1 
ATOM   394  C C   . GLY   B 2 7   ? -35.688 10.768  -13.999 1.00 87.34  ? 16  GLY   B C   1 
ATOM   395  O O   . GLY   B 2 7   ? -36.687 9.991   -13.989 1.00 91.64  ? 16  GLY   B O   1 
ATOM   396  N N   . GLU   B 2 8   ? -34.752 10.795  -14.969 1.00 80.45  ? 17  GLU   B N   1 
ATOM   397  C CA  . GLU   B 2 8   ? -34.649 9.830   -16.109 1.00 75.53  ? 17  GLU   B CA  1 
ATOM   398  C C   . GLU   B 2 8   ? -34.151 8.471   -15.588 1.00 69.88  ? 17  GLU   B C   1 
ATOM   399  O O   . GLU   B 2 8   ? -32.969 8.341   -15.207 1.00 68.52  ? 17  GLU   B O   1 
ATOM   400  C CB  . GLU   B 2 8   ? -33.708 10.349  -17.203 1.00 79.12  ? 17  GLU   B CB  1 
ATOM   401  C CG  . GLU   B 2 8   ? -33.580 9.418   -18.401 1.00 80.59  ? 17  GLU   B CG  1 
ATOM   402  C CD  . GLU   B 2 8   ? -32.772 9.984   -19.563 1.00 83.93  ? 17  GLU   B CD  1 
ATOM   403  O OE1 . GLU   B 2 8   ? -31.765 10.707  -19.318 1.00 81.34  ? 17  GLU   B OE1 1 
ATOM   404  O OE2 . GLU   B 2 8   ? -33.167 9.723   -20.725 1.00 91.54  ? 17  GLU   B OE2 1 
ATOM   405  N N   A THR   B 2 9   ? -35.040 7.477   -15.576 0.25 68.11  ? 18  THR   B N   1 
ATOM   406  N N   B THR   B 2 9   ? -35.048 7.483   -15.589 0.25 68.51  ? 18  THR   B N   1 
ATOM   407  N N   C THR   B 2 9   ? -35.040 7.477   -15.576 0.25 68.11  ? 18  THR   B N   1 
ATOM   408  N N   D THR   B 2 9   ? -35.048 7.483   -15.589 0.25 68.51  ? 18  THR   B N   1 
ATOM   409  C CA  A THR   B 2 9   ? -34.784 6.118   -15.032 0.25 66.69  ? 18  THR   B CA  1 
ATOM   410  C CA  B THR   B 2 9   ? -34.833 6.124   -15.034 0.25 67.33  ? 18  THR   B CA  1 
ATOM   411  C CA  C THR   B 2 9   ? -34.784 6.118   -15.032 0.25 66.69  ? 18  THR   B CA  1 
ATOM   412  C CA  D THR   B 2 9   ? -34.833 6.124   -15.034 0.25 67.33  ? 18  THR   B CA  1 
ATOM   413  C C   A THR   B 2 9   ? -34.610 5.116   -16.180 0.25 65.35  ? 18  THR   B C   1 
ATOM   414  C C   B THR   B 2 9   ? -34.625 5.120   -16.177 0.25 65.71  ? 18  THR   B C   1 
ATOM   415  C C   C THR   B 2 9   ? -34.610 5.116   -16.180 0.25 65.35  ? 18  THR   B C   1 
ATOM   416  C C   D THR   B 2 9   ? -34.625 5.120   -16.177 0.25 65.71  ? 18  THR   B C   1 
ATOM   417  O O   A THR   B 2 9   ? -34.414 3.920   -15.884 0.25 65.67  ? 18  THR   B O   1 
ATOM   418  O O   B THR   B 2 9   ? -34.417 3.928   -15.874 0.25 66.04  ? 18  THR   B O   1 
ATOM   419  O O   C THR   B 2 9   ? -34.414 3.920   -15.884 0.25 65.67  ? 18  THR   B O   1 
ATOM   420  O O   D THR   B 2 9   ? -34.417 3.928   -15.874 0.25 66.04  ? 18  THR   B O   1 
ATOM   421  C CB  A THR   B 2 9   ? -35.922 5.694   -14.095 0.25 66.59  ? 18  THR   B CB  1 
ATOM   422  C CB  B THR   B 2 9   ? -36.021 5.736   -14.145 0.25 67.74  ? 18  THR   B CB  1 
ATOM   423  C CB  C THR   B 2 9   ? -35.922 5.694   -14.095 0.25 66.59  ? 18  THR   B CB  1 
ATOM   424  C CB  D THR   B 2 9   ? -36.021 5.736   -14.145 0.25 67.74  ? 18  THR   B CB  1 
ATOM   425  O OG1 A THR   B 2 9   ? -36.317 6.839   -13.338 0.25 66.54  ? 18  THR   B OG1 1 
ATOM   426  O OG1 B THR   B 2 9   ? -37.181 5.706   -14.977 0.25 68.20  ? 18  THR   B OG1 1 
ATOM   427  O OG1 C THR   B 2 9   ? -36.317 6.839   -13.338 0.25 66.54  ? 18  THR   B OG1 1 
ATOM   428  O OG1 D THR   B 2 9   ? -37.181 5.706   -14.977 0.25 68.20  ? 18  THR   B OG1 1 
ATOM   429  C CG2 A THR   B 2 9   ? -35.529 4.554   -13.182 0.25 66.29  ? 18  THR   B CG2 1 
ATOM   430  C CG2 B THR   B 2 9   ? -36.237 6.697   -12.996 0.25 68.03  ? 18  THR   B CG2 1 
ATOM   431  C CG2 C THR   B 2 9   ? -35.529 4.554   -13.182 0.25 66.29  ? 18  THR   B CG2 1 
ATOM   432  C CG2 D THR   B 2 9   ? -36.237 6.697   -12.996 0.25 68.03  ? 18  THR   B CG2 1 
ATOM   433  N N   . THR   B 2 10  ? -34.670 5.582   -17.434 1.00 64.36  ? 19  THR   B N   1 
ATOM   434  C CA  . THR   B 2 10  ? -34.643 4.708   -18.644 1.00 60.14  ? 19  THR   B CA  1 
ATOM   435  C C   . THR   B 2 10  ? -33.372 3.852   -18.635 1.00 53.11  ? 19  THR   B C   1 
ATOM   436  O O   . THR   B 2 10  ? -32.297 4.417   -18.402 1.00 50.48  ? 19  THR   B O   1 
ATOM   437  C CB  . THR   B 2 10  ? -34.753 5.519   -19.953 1.00 61.72  ? 19  THR   B CB  1 
ATOM   438  O OG1 . THR   B 2 10  ? -35.810 6.482   -19.942 1.00 66.48  ? 19  THR   B OG1 1 
ATOM   439  C CG2 . THR   B 2 10  ? -35.046 4.641   -21.145 1.00 62.17  ? 19  THR   B CG2 1 
ATOM   440  N N   . ASP   B 2 11  ? -33.493 2.541   -18.853 1.00 49.88  ? 20  ASP   B N   1 
ATOM   441  C CA  . ASP   B 2 11  ? -32.325 1.645   -19.072 1.00 51.26  ? 20  ASP   B CA  1 
ATOM   442  C C   . ASP   B 2 11  ? -31.328 2.237   -20.100 1.00 50.52  ? 20  ASP   B C   1 
ATOM   443  O O   . ASP   B 2 11  ? -31.766 3.014   -20.968 1.00 50.81  ? 20  ASP   B O   1 
ATOM   444  C CB  . ASP   B 2 11  ? -32.774 0.274   -19.576 1.00 53.45  ? 20  ASP   B CB  1 
ATOM   445  C CG  . ASP   B 2 11  ? -33.266 -0.700  -18.517 1.00 55.74  ? 20  ASP   B CG  1 
ATOM   446  O OD1 . ASP   B 2 11  ? -33.654 -0.234  -17.424 1.00 53.75  ? 20  ASP   B OD1 1 
ATOM   447  O OD2 . ASP   B 2 11  ? -33.194 -1.944  -18.807 1.00 59.50  ? 20  ASP   B OD2 1 
ATOM   448  N N   . GLY   B 2 12  ? -30.037 1.866   -20.058 1.00 48.82  ? 21  GLY   B N   1 
ATOM   449  C CA  . GLY   B 2 12  ? -29.026 2.407   -20.986 1.00 47.49  ? 21  GLY   B CA  1 
ATOM   450  C C   . GLY   B 2 12  ? -27.747 2.853   -20.319 1.00 46.79  ? 21  GLY   B C   1 
ATOM   451  O O   . GLY   B 2 12  ? -27.614 2.727   -19.061 1.00 45.06  ? 21  GLY   B O   1 
ATOM   452  N N   . VAL   B 2 13  ? -26.826 3.402   -21.117 1.00 45.25  ? 22  VAL   B N   1 
ATOM   453  C CA  . VAL   B 2 13  ? -25.491 3.864   -20.640 1.00 44.22  ? 22  VAL   B CA  1 
ATOM   454  C C   . VAL   B 2 13  ? -25.593 5.377   -20.491 1.00 44.68  ? 22  VAL   B C   1 
ATOM   455  O O   . VAL   B 2 13  ? -26.412 5.981   -21.251 1.00 45.03  ? 22  VAL   B O   1 
ATOM   456  C CB  . VAL   B 2 13  ? -24.342 3.394   -21.543 1.00 44.92  ? 22  VAL   B CB  1 
ATOM   457  C CG1 . VAL   B 2 13  ? -24.491 3.882   -23.022 1.00 45.21  ? 22  VAL   B CG1 1 
ATOM   458  C CG2 . VAL   B 2 13  ? -22.990 3.797   -20.971 1.00 44.62  ? 22  VAL   B CG2 1 
ATOM   459  N N   . TYR   B 2 14  ? -24.918 5.944   -19.475 1.00 43.64  ? 23  TYR   B N   1 
ATOM   460  C CA  . TYR   B 2 14  ? -25.000 7.375   -19.116 1.00 43.14  ? 23  TYR   B CA  1 
ATOM   461  C C   . TYR   B 2 14  ? -23.609 7.928   -18.904 1.00 43.61  ? 23  TYR   B C   1 
ATOM   462  O O   . TYR   B 2 14  ? -22.748 7.200   -18.421 1.00 43.36  ? 23  TYR   B O   1 
ATOM   463  C CB  . TYR   B 2 14  ? -25.757 7.589   -17.810 1.00 42.71  ? 23  TYR   B CB  1 
ATOM   464  C CG  . TYR   B 2 14  ? -27.233 7.409   -17.952 1.00 42.08  ? 23  TYR   B CG  1 
ATOM   465  C CD1 . TYR   B 2 14  ? -27.756 6.168   -18.246 1.00 42.18  ? 23  TYR   B CD1 1 
ATOM   466  C CD2 . TYR   B 2 14  ? -28.082 8.491   -17.875 1.00 42.53  ? 23  TYR   B CD2 1 
ATOM   467  C CE1 . TYR   B 2 14  ? -29.111 5.981   -18.420 1.00 42.29  ? 23  TYR   B CE1 1 
ATOM   468  C CE2 . TYR   B 2 14  ? -29.450 8.336   -18.056 1.00 43.26  ? 23  TYR   B CE2 1 
ATOM   469  C CZ  . TYR   B 2 14  ? -29.960 7.077   -18.347 1.00 43.36  ? 23  TYR   B CZ  1 
ATOM   470  O OH  . TYR   B 2 14  ? -31.304 6.886   -18.501 1.00 44.54  ? 23  TYR   B OH  1 
ATOM   471  N N   . ARG   B 2 15  ? -23.444 9.214   -19.172 1.00 44.38  ? 24  ARG   B N   1 
ATOM   472  C CA  . ARG   B 2 15  ? -22.246 9.958   -18.730 1.00 45.20  ? 24  ARG   B CA  1 
ATOM   473  C C   . ARG   B 2 15  ? -22.480 10.439  -17.294 1.00 45.08  ? 24  ARG   B C   1 
ATOM   474  O O   . ARG   B 2 15  ? -23.626 10.869  -16.977 1.00 43.90  ? 24  ARG   B O   1 
ATOM   475  C CB  . ARG   B 2 15  ? -21.958 11.160  -19.627 1.00 46.48  ? 24  ARG   B CB  1 
ATOM   476  C CG  . ARG   B 2 15  ? -21.777 10.833  -21.107 1.00 47.25  ? 24  ARG   B CG  1 
ATOM   477  C CD  . ARG   B 2 15  ? -21.852 12.077  -21.974 1.00 48.89  ? 24  ARG   B CD  1 
ATOM   478  N NE  . ARG   B 2 15  ? -21.946 11.743  -23.401 1.00 49.61  ? 24  ARG   B NE  1 
ATOM   479  C CZ  . ARG   B 2 15  ? -20.916 11.589  -24.229 1.00 50.74  ? 24  ARG   B CZ  1 
ATOM   480  N NH1 . ARG   B 2 15  ? -19.669 11.768  -23.802 1.00 50.51  ? 24  ARG   B NH1 1 
ATOM   481  N NH2 . ARG   B 2 15  ? -21.153 11.241  -25.490 1.00 51.29  ? 24  ARG   B NH2 1 
ATOM   482  N N   . VAL   B 2 16  ? -21.390 10.447  -16.532 1.00 44.72  ? 25  VAL   B N   1 
ATOM   483  C CA  . VAL   B 2 16  ? -21.272 11.053  -15.189 1.00 45.91  ? 25  VAL   B CA  1 
ATOM   484  C C   . VAL   B 2 16  ? -20.429 12.327  -15.310 1.00 45.87  ? 25  VAL   B C   1 
ATOM   485  O O   . VAL   B 2 16  ? -19.270 12.220  -15.652 1.00 45.06  ? 25  VAL   B O   1 
ATOM   486  C CB  . VAL   B 2 16  ? -20.658 10.001  -14.223 1.00 46.45  ? 25  VAL   B CB  1 
ATOM   487  C CG1 . VAL   B 2 16  ? -20.590 10.504  -12.783 1.00 46.35  ? 25  VAL   B CG1 1 
ATOM   488  C CG2 . VAL   B 2 16  ? -21.394 8.667   -14.290 1.00 45.61  ? 25  VAL   B CG2 1 
ATOM   489  N N   . MET   B 2 17  ? -21.017 13.481  -15.003 1.00 47.83  ? 26  MET   B N   1 
ATOM   490  C CA  . MET   B 2 17  ? -20.421 14.823  -15.205 1.00 50.32  ? 26  MET   B CA  1 
ATOM   491  C C   . MET   B 2 17  ? -20.241 15.550  -13.863 1.00 51.57  ? 26  MET   B C   1 
ATOM   492  O O   . MET   B 2 17  ? -21.067 15.340  -12.989 1.00 50.30  ? 26  MET   B O   1 
ATOM   493  C CB  . MET   B 2 17  ? -21.357 15.674  -16.065 1.00 51.40  ? 26  MET   B CB  1 
ATOM   494  C CG  . MET   B 2 17  ? -21.829 14.988  -17.380 1.00 52.24  ? 26  MET   B CG  1 
ATOM   495  S SD  . MET   B 2 17  ? -20.484 14.610  -18.591 1.00 52.27  ? 26  MET   B SD  1 
ATOM   496  C CE  . MET   B 2 17  ? -19.722 16.226  -18.740 1.00 53.55  ? 26  MET   B CE  1 
ATOM   497  N N   . THR   B 2 18  ? -19.259 16.451  -13.783 1.00 53.91  ? 27  THR   B N   1 
ATOM   498  C CA  . THR   B 2 18  ? -19.065 17.425  -12.689 1.00 57.97  ? 27  THR   B CA  1 
ATOM   499  C C   . THR   B 2 18  ? -18.837 18.844  -13.242 1.00 62.04  ? 27  THR   B C   1 
ATOM   500  O O   . THR   B 2 18  ? -18.206 18.992  -14.318 1.00 56.92  ? 27  THR   B O   1 
ATOM   501  C CB  . THR   B 2 18  ? -17.929 16.961  -11.765 1.00 58.85  ? 27  THR   B CB  1 
ATOM   502  O OG1 . THR   B 2 18  ? -18.075 17.718  -10.557 1.00 61.98  ? 27  THR   B OG1 1 
ATOM   503  C CG2 . THR   B 2 18  ? -16.538 17.086  -12.364 1.00 57.63  ? 27  THR   B CG2 1 
ATOM   504  N N   . ARG   B 2 19  ? -19.292 19.855  -12.481 1.00 68.04  ? 28  ARG   B N   1 
ATOM   505  C CA  . ARG   B 2 19  ? -19.005 21.301  -12.714 1.00 74.10  ? 28  ARG   B CA  1 
ATOM   506  C C   . ARG   B 2 19  ? -17.982 21.821  -11.684 1.00 74.18  ? 28  ARG   B C   1 
ATOM   507  O O   . ARG   B 2 19  ? -17.669 23.015  -11.733 1.00 74.23  ? 28  ARG   B O   1 
ATOM   508  C CB  . ARG   B 2 19  ? -20.326 22.078  -12.733 1.00 77.74  ? 28  ARG   B CB  1 
ATOM   509  C CG  . ARG   B 2 19  ? -21.305 21.586  -13.795 1.00 81.60  ? 28  ARG   B CG  1 
ATOM   510  C CD  . ARG   B 2 19  ? -22.028 22.711  -14.520 1.00 86.44  ? 28  ARG   B CD  1 
ATOM   511  N NE  . ARG   B 2 19  ? -23.153 22.307  -15.374 1.00 90.30  ? 28  ARG   B NE  1 
ATOM   512  C CZ  . ARG   B 2 19  ? -24.414 22.102  -14.966 1.00 91.58  ? 28  ARG   B CZ  1 
ATOM   513  N NH1 . ARG   B 2 19  ? -24.745 22.227  -13.689 1.00 91.51  ? 28  ARG   B NH1 1 
ATOM   514  N NH2 . ARG   B 2 19  ? -25.341 21.754  -15.845 1.00 90.02  ? 28  ARG   B NH2 1 
ATOM   515  N N   . ARG   B 2 20  ? -17.406 20.934  -10.860 1.00 78.09  ? 29  ARG   B N   1 
ATOM   516  C CA  . ARG   B 2 20  ? -16.471 21.256  -9.737  1.00 81.48  ? 29  ARG   B CA  1 
ATOM   517  C C   . ARG   B 2 20  ? -15.102 21.689  -10.291 1.00 79.59  ? 29  ARG   B C   1 
ATOM   518  O O   . ARG   B 2 20  ? -14.304 22.245  -9.524  1.00 81.22  ? 29  ARG   B O   1 
ATOM   519  C CB  . ARG   B 2 20  ? -16.344 20.037  -8.816  1.00 84.44  ? 29  ARG   B CB  1 
ATOM   520  C CG  . ARG   B 2 20  ? -16.081 20.362  -7.353  1.00 90.80  ? 29  ARG   B CG  1 
ATOM   521  C CD  . ARG   B 2 20  ? -15.698 19.115  -6.558  1.00 96.35  ? 29  ARG   B CD  1 
ATOM   522  N NE  . ARG   B 2 20  ? -14.480 18.478  -7.075  1.00 100.01 ? 29  ARG   B NE  1 
ATOM   523  C CZ  . ARG   B 2 20  ? -13.263 18.507  -6.510  1.00 102.11 ? 29  ARG   B CZ  1 
ATOM   524  N NH1 . ARG   B 2 20  ? -13.051 19.124  -5.356  1.00 102.44 ? 29  ARG   B NH1 1 
ATOM   525  N NH2 . ARG   B 2 20  ? -12.249 17.903  -7.111  1.00 99.61  ? 29  ARG   B NH2 1 
ATOM   526  N N   . LEU   B 2 21  ? -14.816 21.398  -11.563 1.00 77.29  ? 30  LEU   B N   1 
ATOM   527  C CA  . LEU   B 2 21  ? -13.599 21.858  -12.285 1.00 74.70  ? 30  LEU   B CA  1 
ATOM   528  C C   . LEU   B 2 21  ? -14.007 22.894  -13.338 1.00 71.66  ? 30  LEU   B C   1 
ATOM   529  O O   . LEU   B 2 21  ? -15.165 23.398  -13.291 1.00 70.19  ? 30  LEU   B O   1 
ATOM   530  C CB  . LEU   B 2 21  ? -12.924 20.658  -12.951 1.00 75.14  ? 30  LEU   B CB  1 
ATOM   531  C CG  . LEU   B 2 21  ? -12.180 19.670  -12.059 1.00 77.25  ? 30  LEU   B CG  1 
ATOM   532  C CD1 . LEU   B 2 21  ? -12.353 19.953  -10.577 1.00 77.34  ? 30  LEU   B CD1 1 
ATOM   533  C CD2 . LEU   B 2 21  ? -12.615 18.247  -12.393 1.00 78.79  ? 30  LEU   B CD2 1 
ATOM   534  N N   . LEU   B 2 22  ? -13.082 23.198  -14.254 1.00 71.61  ? 31  LEU   B N   1 
ATOM   535  C CA  . LEU   B 2 22  ? -13.334 24.054  -15.437 1.00 68.85  ? 31  LEU   B CA  1 
ATOM   536  C C   . LEU   B 2 22  ? -14.455 23.430  -16.257 1.00 68.16  ? 31  LEU   B C   1 
ATOM   537  O O   . LEU   B 2 22  ? -14.456 22.190  -16.385 1.00 68.48  ? 31  LEU   B O   1 
ATOM   538  C CB  . LEU   B 2 22  ? -12.062 24.154  -16.269 1.00 68.59  ? 31  LEU   B CB  1 
ATOM   539  C CG  . LEU   B 2 22  ? -12.132 25.218  -17.354 1.00 68.32  ? 31  LEU   B CG  1 
ATOM   540  C CD1 . LEU   B 2 22  ? -11.949 26.604  -16.758 1.00 66.76  ? 31  LEU   B CD1 1 
ATOM   541  C CD2 . LEU   B 2 22  ? -11.104 24.933  -18.444 1.00 70.46  ? 31  LEU   B CD2 1 
ATOM   542  N N   . GLY   B 2 23  ? -15.372 24.249  -16.772 1.00 67.79  ? 32  GLY   B N   1 
ATOM   543  C CA  . GLY   B 2 23  ? -16.500 23.786  -17.609 1.00 66.58  ? 32  GLY   B CA  1 
ATOM   544  C C   . GLY   B 2 23  ? -17.285 22.648  -16.961 1.00 64.56  ? 32  GLY   B C   1 
ATOM   545  O O   . GLY   B 2 23  ? -17.332 22.586  -15.724 1.00 64.20  ? 32  GLY   B O   1 
ATOM   546  N N   . SER   B 2 24  ? -17.964 21.843  -17.783 1.00 62.97  ? 33  SER   B N   1 
ATOM   547  C CA  . SER   B 2 24  ? -18.541 20.521  -17.430 1.00 60.97  ? 33  SER   B CA  1 
ATOM   548  C C   . SER   B 2 24  ? -17.533 19.457  -17.861 1.00 58.30  ? 33  SER   B C   1 
ATOM   549  O O   . SER   B 2 24  ? -17.124 19.494  -19.041 1.00 56.93  ? 33  SER   B O   1 
ATOM   550  C CB  . SER   B 2 24  ? -19.879 20.304  -18.086 1.00 61.20  ? 33  SER   B CB  1 
ATOM   551  O OG  . SER   B 2 24  ? -20.742 21.395  -17.811 1.00 64.33  ? 33  SER   B OG  1 
ATOM   552  N N   . THR   B 2 25  ? -17.136 18.573  -16.943 1.00 54.93  ? 34  THR   B N   1 
ATOM   553  C CA  . THR   B 2 25  ? -16.044 17.577  -17.120 1.00 54.33  ? 34  THR   B CA  1 
ATOM   554  C C   . THR   B 2 25  ? -16.637 16.180  -16.915 1.00 53.95  ? 34  THR   B C   1 
ATOM   555  O O   . THR   B 2 25  ? -17.368 15.961  -15.886 1.00 54.07  ? 34  THR   B O   1 
ATOM   556  C CB  . THR   B 2 25  ? -14.866 17.875  -16.179 1.00 54.99  ? 34  THR   B CB  1 
ATOM   557  O OG1 . THR   B 2 25  ? -14.524 19.258  -16.307 1.00 55.26  ? 34  THR   B OG1 1 
ATOM   558  C CG2 . THR   B 2 25  ? -13.645 17.023  -16.468 1.00 55.12  ? 34  THR   B CG2 1 
ATOM   559  N N   . GLN   B 2 26  ? -16.371 15.258  -17.834 1.00 52.32  ? 35  GLN   B N   1 
ATOM   560  C CA  . GLN   B 2 26  ? -16.866 13.865  -17.698 1.00 52.14  ? 35  GLN   B CA  1 
ATOM   561  C C   . GLN   B 2 26  ? -15.867 13.082  -16.842 1.00 52.54  ? 35  GLN   B C   1 
ATOM   562  O O   . GLN   B 2 26  ? -14.682 12.949  -17.260 1.00 52.56  ? 35  GLN   B O   1 
ATOM   563  C CB  . GLN   B 2 26  ? -17.058 13.173  -19.042 1.00 52.04  ? 35  GLN   B CB  1 
ATOM   564  C CG  . GLN   B 2 26  ? -17.826 11.873  -18.920 1.00 51.48  ? 35  GLN   B CG  1 
ATOM   565  C CD  . GLN   B 2 26  ? -18.045 11.210  -20.253 1.00 50.99  ? 35  GLN   B CD  1 
ATOM   566  O OE1 . GLN   B 2 26  ? -18.779 11.718  -21.098 1.00 53.19  ? 35  GLN   B OE1 1 
ATOM   567  N NE2 . GLN   B 2 26  ? -17.446 10.052  -20.430 1.00 49.80  ? 35  GLN   B NE2 1 
ATOM   568  N N   . VAL   B 2 27  ? -16.323 12.590  -15.689 1.00 51.06  ? 36  VAL   B N   1 
ATOM   569  C CA  . VAL   B 2 27  ? -15.458 11.898  -14.686 1.00 50.11  ? 36  VAL   B CA  1 
ATOM   570  C C   . VAL   B 2 27  ? -15.564 10.384  -14.911 1.00 47.58  ? 36  VAL   B C   1 
ATOM   571  O O   . VAL   B 2 27  ? -14.615 9.668   -14.574 1.00 47.63  ? 36  VAL   B O   1 
ATOM   572  C CB  . VAL   B 2 27  ? -15.852 12.357  -13.261 1.00 52.95  ? 36  VAL   B CB  1 
ATOM   573  C CG1 . VAL   B 2 27  ? -15.634 13.856  -13.072 1.00 54.87  ? 36  VAL   B CG1 1 
ATOM   574  C CG2 . VAL   B 2 27  ? -17.297 12.035  -12.896 1.00 52.40  ? 36  VAL   B CG2 1 
ATOM   575  N N   . GLY   B 2 28  ? -16.679 9.916   -15.491 1.00 45.74  ? 37  GLY   B N   1 
ATOM   576  C CA  . GLY   B 2 28  ? -16.890 8.506   -15.878 1.00 44.07  ? 37  GLY   B CA  1 
ATOM   577  C C   . GLY   B 2 28  ? -18.251 8.283   -16.534 1.00 43.71  ? 37  GLY   B C   1 
ATOM   578  O O   . GLY   B 2 28  ? -18.908 9.277   -17.002 1.00 44.13  ? 37  GLY   B O   1 
ATOM   579  N N   . VAL   B 2 29  ? -18.710 7.022   -16.480 1.00 42.79  ? 38  VAL   B N   1 
ATOM   580  C CA  . VAL   B 2 29  ? -19.895 6.448   -17.200 1.00 42.29  ? 38  VAL   B CA  1 
ATOM   581  C C   . VAL   B 2 29  ? -20.595 5.445   -16.274 1.00 41.35  ? 38  VAL   B C   1 
ATOM   582  O O   . VAL   B 2 29  ? -19.891 4.798   -15.478 1.00 41.11  ? 38  VAL   B O   1 
ATOM   583  C CB  . VAL   B 2 29  ? -19.402 5.706   -18.468 1.00 42.41  ? 38  VAL   B CB  1 
ATOM   584  C CG1 . VAL   B 2 29  ? -20.531 5.105   -19.298 1.00 42.44  ? 38  VAL   B CG1 1 
ATOM   585  C CG2 . VAL   B 2 29  ? -18.529 6.600   -19.331 1.00 42.86  ? 38  VAL   B CG2 1 
ATOM   586  N N   . GLY   B 2 30  ? -21.871 5.174   -16.492 1.00 40.70  ? 39  GLY   B N   1 
ATOM   587  C CA  . GLY   B 2 30  ? -22.517 4.024   -15.857 1.00 40.00  ? 39  GLY   B CA  1 
ATOM   588  C C   . GLY   B 2 30  ? -23.671 3.501   -16.645 1.00 39.95  ? 39  GLY   B C   1 
ATOM   589  O O   . GLY   B 2 30  ? -23.951 4.048   -17.732 1.00 40.13  ? 39  GLY   B O   1 
ATOM   590  N N   . VAL   B 2 31  ? -24.314 2.489   -16.077 1.00 39.77  ? 40  VAL   B N   1 
ATOM   591  C CA  . VAL   B 2 31  ? -25.406 1.657   -16.648 1.00 40.17  ? 40  VAL   B CA  1 
ATOM   592  C C   . VAL   B 2 31  ? -26.621 1.793   -15.745 1.00 41.12  ? 40  VAL   B C   1 
ATOM   593  O O   . VAL   B 2 31  ? -26.458 1.516   -14.493 1.00 40.58  ? 40  VAL   B O   1 
ATOM   594  C CB  . VAL   B 2 31  ? -24.985 0.179   -16.736 1.00 40.51  ? 40  VAL   B CB  1 
ATOM   595  C CG1 . VAL   B 2 31  ? -26.121 -0.699  -17.214 1.00 41.03  ? 40  VAL   B CG1 1 
ATOM   596  C CG2 . VAL   B 2 31  ? -23.776 -0.035  -17.622 1.00 40.51  ? 40  VAL   B CG2 1 
ATOM   597  N N   . MET   B 2 32  ? -27.748 2.254   -16.284 1.00 41.42  ? 41  MET   B N   1 
ATOM   598  C CA  . MET   B 2 32  ? -29.068 2.169   -15.636 1.00 43.54  ? 41  MET   B CA  1 
ATOM   599  C C   . MET   B 2 32  ? -29.710 0.848   -16.048 1.00 44.57  ? 41  MET   B C   1 
ATOM   600  O O   . MET   B 2 32  ? -29.910 0.660   -17.243 1.00 43.58  ? 41  MET   B O   1 
ATOM   601  C CB  . MET   B 2 32  ? -29.966 3.339   -16.054 1.00 44.97  ? 41  MET   B CB  1 
ATOM   602  C CG  . MET   B 2 32  ? -31.195 3.517   -15.195 1.00 46.80  ? 41  MET   B CG  1 
ATOM   603  S SD  . MET   B 2 32  ? -30.810 4.102   -13.502 1.00 49.17  ? 41  MET   B SD  1 
ATOM   604  C CE  . MET   B 2 32  ? -30.134 5.718   -13.880 1.00 49.48  ? 41  MET   B CE  1 
ATOM   605  N N   . GLN   B 2 33  ? -30.071 -0.011  -15.092 1.00 45.63  ? 42  GLN   B N   1 
ATOM   606  C CA  . GLN   B 2 33  ? -30.830 -1.249  -15.364 1.00 47.63  ? 42  GLN   B CA  1 
ATOM   607  C C   . GLN   B 2 33  ? -31.780 -1.498  -14.208 1.00 49.46  ? 42  GLN   B C   1 
ATOM   608  O O   . GLN   B 2 33  ? -31.343 -1.374  -13.046 1.00 49.16  ? 42  GLN   B O   1 
ATOM   609  C CB  . GLN   B 2 33  ? -29.909 -2.446  -15.570 1.00 48.66  ? 42  GLN   B CB  1 
ATOM   610  C CG  . GLN   B 2 33  ? -30.677 -3.602  -16.194 1.00 51.89  ? 42  GLN   B CG  1 
ATOM   611  C CD  . GLN   B 2 33  ? -29.795 -4.742  -16.626 1.00 54.24  ? 42  GLN   B CD  1 
ATOM   612  O OE1 . GLN   B 2 33  ? -29.951 -5.882  -16.173 1.00 56.85  ? 42  GLN   B OE1 1 
ATOM   613  N NE2 . GLN   B 2 33  ? -28.808 -4.422  -17.443 1.00 54.38  ? 42  GLN   B NE2 1 
ATOM   614  N N   . GLU   B 2 34  ? -33.035 -1.787  -14.509 1.00 51.24  ? 43  GLU   B N   1 
ATOM   615  C CA  . GLU   B 2 34  ? -34.066 -2.111  -13.499 1.00 52.70  ? 43  GLU   B CA  1 
ATOM   616  C C   . GLU   B 2 34  ? -34.157 -0.994  -12.439 1.00 51.31  ? 43  GLU   B C   1 
ATOM   617  O O   . GLU   B 2 34  ? -34.563 -1.294  -11.314 1.00 49.97  ? 43  GLU   B O   1 
ATOM   618  C CB  . GLU   B 2 34  ? -33.741 -3.486  -12.896 1.00 55.78  ? 43  GLU   B CB  1 
ATOM   619  C CG  . GLU   B 2 34  ? -33.976 -4.638  -13.876 1.00 57.64  ? 43  GLU   B CG  1 
ATOM   620  C CD  . GLU   B 2 34  ? -33.281 -5.957  -13.565 1.00 59.31  ? 43  GLU   B CD  1 
ATOM   621  O OE1 . GLU   B 2 34  ? -33.817 -6.737  -12.767 1.00 60.09  ? 43  GLU   B OE1 1 
ATOM   622  O OE2 . GLU   B 2 34  ? -32.208 -6.210  -14.149 1.00 63.70  ? 43  GLU   B OE2 1 
ATOM   623  N N   . GLY   B 2 35  ? -33.847 0.251   -12.787 1.00 48.69  ? 44  GLY   B N   1 
ATOM   624  C CA  . GLY   B 2 35  ? -34.057 1.410   -11.905 1.00 48.51  ? 44  GLY   B CA  1 
ATOM   625  C C   . GLY   B 2 35  ? -32.842 1.682   -11.044 1.00 47.98  ? 44  GLY   B C   1 
ATOM   626  O O   . GLY   B 2 35  ? -32.895 2.635   -10.228 1.00 48.67  ? 44  GLY   B O   1 
ATOM   627  N N   . VAL   B 2 36  ? -31.775 0.901   -11.242 1.00 45.78  ? 45  VAL   B N   1 
ATOM   628  C CA  . VAL   B 2 36  ? -30.505 0.985   -10.474 1.00 44.36  ? 45  VAL   B CA  1 
ATOM   629  C C   . VAL   B 2 36  ? -29.411 1.579   -11.366 1.00 43.38  ? 45  VAL   B C   1 
ATOM   630  O O   . VAL   B 2 36  ? -29.291 1.118   -12.546 1.00 44.51  ? 45  VAL   B O   1 
ATOM   631  C CB  . VAL   B 2 36  ? -30.153 -0.398  -9.881  1.00 44.71  ? 45  VAL   B CB  1 
ATOM   632  C CG1 . VAL   B 2 36  ? -28.747 -0.436  -9.311  1.00 45.12  ? 45  VAL   B CG1 1 
ATOM   633  C CG2 . VAL   B 2 36  ? -31.134 -0.777  -8.760  1.00 45.35  ? 45  VAL   B CG2 1 
ATOM   634  N N   . PHE   B 2 37  ? -28.628 2.534   -10.856 1.00 41.31  ? 46  PHE   B N   1 
ATOM   635  C CA  . PHE   B 2 37  ? -27.461 3.092   -11.581 1.00 40.58  ? 46  PHE   B CA  1 
ATOM   636  C C   . PHE   B 2 37  ? -26.206 2.366   -11.094 1.00 39.49  ? 46  PHE   B C   1 
ATOM   637  O O   . PHE   B 2 37  ? -25.980 2.342   -9.892  1.00 38.43  ? 46  PHE   B O   1 
ATOM   638  C CB  . PHE   B 2 37  ? -27.375 4.613   -11.440 1.00 40.94  ? 46  PHE   B CB  1 
ATOM   639  C CG  . PHE   B 2 37  ? -26.375 5.210   -12.406 1.00 41.68  ? 46  PHE   B CG  1 
ATOM   640  C CD1 . PHE   B 2 37  ? -26.561 5.100   -13.765 1.00 42.36  ? 46  PHE   B CD1 1 
ATOM   641  C CD2 . PHE   B 2 37  ? -25.227 5.830   -11.963 1.00 42.40  ? 46  PHE   B CD2 1 
ATOM   642  C CE1 . PHE   B 2 37  ? -25.659 5.648   -14.661 1.00 42.97  ? 46  PHE   B CE1 1 
ATOM   643  C CE2 . PHE   B 2 37  ? -24.286 6.320   -12.855 1.00 42.68  ? 46  PHE   B CE2 1 
ATOM   644  C CZ  . PHE   B 2 37  ? -24.505 6.231   -14.204 1.00 43.16  ? 46  PHE   B CZ  1 
ATOM   645  N N   . HIS   B 2 38  ? -25.411 1.792   -11.992 1.00 38.52  ? 47  HIS   B N   1 
ATOM   646  C CA  . HIS   B 2 38  ? -24.170 1.035   -11.702 1.00 38.19  ? 47  HIS   B CA  1 
ATOM   647  C C   . HIS   B 2 38  ? -22.960 1.781   -12.245 1.00 38.73  ? 47  HIS   B C   1 
ATOM   648  O O   . HIS   B 2 38  ? -22.975 2.141   -13.454 1.00 38.01  ? 47  HIS   B O   1 
ATOM   649  C CB  . HIS   B 2 38  ? -24.223 -0.327  -12.326 1.00 38.19  ? 47  HIS   B CB  1 
ATOM   650  C CG  . HIS   B 2 38  ? -25.471 -1.084  -12.070 1.00 38.32  ? 47  HIS   B CG  1 
ATOM   651  N ND1 . HIS   B 2 38  ? -26.687 -0.685  -12.551 1.00 38.82  ? 47  HIS   B ND1 1 
ATOM   652  C CD2 . HIS   B 2 38  ? -25.690 -2.239  -11.403 1.00 38.74  ? 47  HIS   B CD2 1 
ATOM   653  C CE1 . HIS   B 2 38  ? -27.611 -1.582  -12.238 1.00 38.90  ? 47  HIS   B CE1 1 
ATOM   654  N NE2 . HIS   B 2 38  ? -27.032 -2.520  -11.490 1.00 38.96  ? 47  HIS   B NE2 1 
ATOM   655  N N   . THR   B 2 39  ? -21.956 2.051   -11.402 1.00 39.14  ? 48  THR   B N   1 
ATOM   656  C CA  . THR   B 2 39  ? -20.718 2.682   -11.899 1.00 39.84  ? 48  THR   B CA  1 
ATOM   657  C C   . THR   B 2 39  ? -19.542 2.138   -11.107 1.00 40.82  ? 48  THR   B C   1 
ATOM   658  O O   . THR   B 2 39  ? -19.740 1.175   -10.303 1.00 39.69  ? 48  THR   B O   1 
ATOM   659  C CB  . THR   B 2 39  ? -20.896 4.195   -11.953 1.00 40.04  ? 48  THR   B CB  1 
ATOM   660  O OG1 . THR   B 2 39  ? -19.794 4.842   -12.589 1.00 39.88  ? 48  THR   B OG1 1 
ATOM   661  C CG2 . THR   B 2 39  ? -21.091 4.807   -10.586 1.00 40.13  ? 48  THR   B CG2 1 
ATOM   662  N N   . MET   B 2 40  ? -18.370 2.701   -11.365 1.00 41.93  ? 49  MET   B N   1 
ATOM   663  C CA  . MET   B 2 40  ? -17.160 2.360   -10.606 1.00 43.32  ? 49  MET   B CA  1 
ATOM   664  C C   . MET   B 2 40  ? -17.015 3.353   -9.444  1.00 43.37  ? 49  MET   B C   1 
ATOM   665  O O   . MET   B 2 40  ? -17.386 4.523   -9.591  1.00 43.19  ? 49  MET   B O   1 
ATOM   666  C CB  . MET   B 2 40  ? -15.946 2.342   -11.523 1.00 44.64  ? 49  MET   B CB  1 
ATOM   667  C CG  . MET   B 2 40  ? -16.212 1.473   -12.754 1.00 46.72  ? 49  MET   B CG  1 
ATOM   668  S SD  . MET   B 2 40  ? -14.734 0.665   -13.289 1.00 51.10  ? 49  MET   B SD  1 
ATOM   669  C CE  . MET   B 2 40  ? -14.969 -0.945  -12.529 1.00 49.18  ? 49  MET   B CE  1 
ATOM   670  N N   A TRP   B 2 41  ? -16.485 2.881   -8.311  0.22 43.29  ? 50  TRP   B N   1 
ATOM   671  N N   B TRP   B 2 41  ? -16.487 2.881   -8.312  0.17 43.11  ? 50  TRP   B N   1 
ATOM   672  N N   C TRP   B 2 41  ? -16.484 2.881   -8.311  0.25 43.27  ? 50  TRP   B N   1 
ATOM   673  N N   D TRP   B 2 41  ? -16.485 2.881   -8.313  0.25 43.06  ? 50  TRP   B N   1 
ATOM   674  C CA  A TRP   B 2 41  ? -16.398 3.662   -7.047  0.22 43.51  ? 50  TRP   B CA  1 
ATOM   675  C CA  B TRP   B 2 41  ? -16.413 3.672   -7.056  0.17 43.17  ? 50  TRP   B CA  1 
ATOM   676  C CA  C TRP   B 2 41  ? -16.399 3.662   -7.048  0.25 43.51  ? 50  TRP   B CA  1 
ATOM   677  C CA  D TRP   B 2 41  ? -16.413 3.671   -7.057  0.25 43.15  ? 50  TRP   B CA  1 
ATOM   678  C C   A TRP   B 2 41  ? -15.467 4.862   -7.241  0.22 44.08  ? 50  TRP   B C   1 
ATOM   679  C C   B TRP   B 2 41  ? -15.469 4.865   -7.243  0.17 43.87  ? 50  TRP   B C   1 
ATOM   680  C C   C TRP   B 2 41  ? -15.467 4.862   -7.241  0.25 44.08  ? 50  TRP   B C   1 
ATOM   681  C C   D TRP   B 2 41  ? -15.470 4.865   -7.246  0.25 43.87  ? 50  TRP   B C   1 
ATOM   682  O O   A TRP   B 2 41  ? -15.780 5.936   -6.693  0.22 44.05  ? 50  TRP   B O   1 
ATOM   683  O O   B TRP   B 2 41  ? -15.778 5.940   -6.694  0.17 43.85  ? 50  TRP   B O   1 
ATOM   684  O O   C TRP   B 2 41  ? -15.780 5.936   -6.694  0.25 44.05  ? 50  TRP   B O   1 
ATOM   685  O O   D TRP   B 2 41  ? -15.780 5.941   -6.701  0.25 43.85  ? 50  TRP   B O   1 
ATOM   686  C CB  A TRP   B 2 41  ? -15.934 2.786   -5.875  0.22 43.38  ? 50  TRP   B CB  1 
ATOM   687  C CB  B TRP   B 2 41  ? -15.981 2.812   -5.862  0.17 42.75  ? 50  TRP   B CB  1 
ATOM   688  C CB  C TRP   B 2 41  ? -15.933 2.786   -5.875  0.25 43.37  ? 50  TRP   B CB  1 
ATOM   689  C CB  D TRP   B 2 41  ? -15.981 2.811   -5.862  0.25 42.74  ? 50  TRP   B CB  1 
ATOM   690  C CG  A TRP   B 2 41  ? -16.090 3.447   -4.539  0.22 43.17  ? 50  TRP   B CG  1 
ATOM   691  C CG  B TRP   B 2 41  ? -15.893 3.618   -4.604  0.17 42.32  ? 50  TRP   B CG  1 
ATOM   692  C CG  C TRP   B 2 41  ? -16.090 3.448   -4.540  0.25 43.16  ? 50  TRP   B CG  1 
ATOM   693  C CG  D TRP   B 2 41  ? -15.893 3.618   -4.605  0.25 42.29  ? 50  TRP   B CG  1 
ATOM   694  C CD1 A TRP   B 2 41  ? -17.124 3.287   -3.666  0.22 43.17  ? 50  TRP   B CD1 1 
ATOM   695  C CD1 B TRP   B 2 41  ? -14.875 4.448   -4.234  0.17 42.22  ? 50  TRP   B CD1 1 
ATOM   696  C CD1 C TRP   B 2 41  ? -17.124 3.288   -3.667  0.25 43.17  ? 50  TRP   B CD1 1 
ATOM   697  C CD1 D TRP   B 2 41  ? -14.876 4.448   -4.235  0.25 42.19  ? 50  TRP   B CD1 1 
ATOM   698  C CD2 A TRP   B 2 41  ? -15.190 4.388   -3.923  0.22 43.20  ? 50  TRP   B CD2 1 
ATOM   699  C CD2 B TRP   B 2 41  ? -16.891 3.723   -3.576  0.17 42.12  ? 50  TRP   B CD2 1 
ATOM   700  C CD2 C TRP   B 2 41  ? -15.190 4.388   -3.923  0.25 43.19  ? 50  TRP   B CD2 1 
ATOM   701  C CD2 D TRP   B 2 41  ? -16.891 3.724   -3.577  0.25 42.12  ? 50  TRP   B CD2 1 
ATOM   702  N NE1 A TRP   B 2 41  ? -16.925 4.051   -2.546  0.22 43.19  ? 50  TRP   B NE1 1 
ATOM   703  N NE1 B TRP   B 2 41  ? -15.156 5.041   -3.036  0.17 42.04  ? 50  TRP   B NE1 1 
ATOM   704  N NE1 C TRP   B 2 41  ? -16.925 4.051   -2.547  0.25 43.20  ? 50  TRP   B NE1 1 
ATOM   705  N NE1 D TRP   B 2 41  ? -15.156 5.042   -3.038  0.25 42.00  ? 50  TRP   B NE1 1 
ATOM   706  C CE2 A TRP   B 2 41  ? -15.748 4.740   -2.678  0.22 43.27  ? 50  TRP   B CE2 1 
ATOM   707  C CE2 B TRP   B 2 41  ? -16.386 4.615   -2.605  0.17 42.03  ? 50  TRP   B CE2 1 
ATOM   708  C CE2 C TRP   B 2 41  ? -15.748 4.740   -2.678  0.25 43.28  ? 50  TRP   B CE2 1 
ATOM   709  C CE2 D TRP   B 2 41  ? -16.387 4.616   -2.607  0.25 42.04  ? 50  TRP   B CE2 1 
ATOM   710  C CE3 A TRP   B 2 41  ? -13.971 4.964   -4.295  0.22 43.51  ? 50  TRP   B CE3 1 
ATOM   711  C CE3 B TRP   B 2 41  ? -18.145 3.138   -3.367  0.17 42.05  ? 50  TRP   B CE3 1 
ATOM   712  C CE3 C TRP   B 2 41  ? -13.971 4.964   -4.294  0.25 43.52  ? 50  TRP   B CE3 1 
ATOM   713  C CE3 D TRP   B 2 41  ? -18.145 3.137   -3.368  0.25 42.06  ? 50  TRP   B CE3 1 
ATOM   714  C CZ2 A TRP   B 2 41  ? -15.126 5.636   -1.809  0.22 43.35  ? 50  TRP   B CZ2 1 
ATOM   715  C CZ2 B TRP   B 2 41  ? -17.099 4.937   -1.450  0.17 41.82  ? 50  TRP   B CZ2 1 
ATOM   716  C CZ2 C TRP   B 2 41  ? -15.126 5.636   -1.808  0.25 43.36  ? 50  TRP   B CZ2 1 
ATOM   717  C CZ2 D TRP   B 2 41  ? -17.101 4.938   -1.452  0.25 41.80  ? 50  TRP   B CZ2 1 
ATOM   718  C CZ3 A TRP   B 2 41  ? -13.356 5.846   -3.435  0.22 43.50  ? 50  TRP   B CZ3 1 
ATOM   719  C CZ3 B TRP   B 2 41  ? -18.848 3.460   -2.227  0.17 41.92  ? 50  TRP   B CZ3 1 
ATOM   720  C CZ3 C TRP   B 2 41  ? -13.356 5.847   -3.434  0.25 43.50  ? 50  TRP   B CZ3 1 
ATOM   721  C CZ3 D TRP   B 2 41  ? -18.849 3.460   -2.228  0.25 41.92  ? 50  TRP   B CZ3 1 
ATOM   722  C CH2 A TRP   B 2 41  ? -13.929 6.180   -2.211  0.22 43.50  ? 50  TRP   B CH2 1 
ATOM   723  C CH2 B TRP   B 2 41  ? -18.329 4.344   -1.280  0.17 41.82  ? 50  TRP   B CH2 1 
ATOM   724  C CH2 C TRP   B 2 41  ? -13.929 6.180   -2.210  0.25 43.51  ? 50  TRP   B CH2 1 
ATOM   725  C CH2 D TRP   B 2 41  ? -18.330 4.345   -1.280  0.25 41.82  ? 50  TRP   B CH2 1 
ATOM   726  N N   . HIS   B 2 42  ? -14.367 4.687   -7.982  1.00 44.46  ? 51  HIS   B N   1 
ATOM   727  C CA  . HIS   B 2 42  ? -13.376 5.780   -8.205  1.00 46.39  ? 51  HIS   B CA  1 
ATOM   728  C C   . HIS   B 2 42  ? -13.997 6.930   -9.016  1.00 47.77  ? 51  HIS   B C   1 
ATOM   729  O O   . HIS   B 2 42  ? -13.508 8.050   -8.904  1.00 49.15  ? 51  HIS   B O   1 
ATOM   730  C CB  . HIS   B 2 42  ? -12.063 5.268   -8.778  1.00 47.53  ? 51  HIS   B CB  1 
ATOM   731  C CG  . HIS   B 2 42  ? -12.097 4.960   -10.228 1.00 48.33  ? 51  HIS   B CG  1 
ATOM   732  N ND1 . HIS   B 2 42  ? -12.112 3.645   -10.713 1.00 48.21  ? 51  HIS   B ND1 1 
ATOM   733  C CD2 . HIS   B 2 42  ? -11.990 5.773   -11.313 1.00 49.01  ? 51  HIS   B CD2 1 
ATOM   734  C CE1 . HIS   B 2 42  ? -12.070 3.693   -12.037 1.00 48.41  ? 51  HIS   B CE1 1 
ATOM   735  N NE2 . HIS   B 2 42  ? -12.025 4.985   -12.419 1.00 47.10  ? 51  HIS   B NE2 1 
ATOM   736  N N   . VAL   B 2 43  ? -15.106 6.700   -9.707  1.00 47.90  ? 52  VAL   B N   1 
ATOM   737  C CA  . VAL   B 2 43  ? -15.803 7.758   -10.479 1.00 48.10  ? 52  VAL   B CA  1 
ATOM   738  C C   . VAL   B 2 43  ? -16.504 8.718   -9.500  1.00 48.23  ? 52  VAL   B C   1 
ATOM   739  O O   . VAL   B 2 43  ? -16.252 9.940   -9.621  1.00 49.19  ? 52  VAL   B O   1 
ATOM   740  C CB  . VAL   B 2 43  ? -16.763 7.097   -11.484 1.00 48.46  ? 52  VAL   B CB  1 
ATOM   741  C CG1 . VAL   B 2 43  ? -17.726 8.089   -12.111 1.00 49.39  ? 52  VAL   B CG1 1 
ATOM   742  C CG2 . VAL   B 2 43  ? -16.003 6.345   -12.576 1.00 49.88  ? 52  VAL   B CG2 1 
ATOM   743  N N   . THR   B 2 44  ? -17.359 8.211   -8.591  1.00 46.70  ? 53  THR   B N   1 
ATOM   744  C CA  . THR   B 2 44  ? -18.270 9.050   -7.731  1.00 46.68  ? 53  THR   B CA  1 
ATOM   745  C C   . THR   B 2 44  ? -17.695 9.278   -6.323  1.00 47.01  ? 53  THR   B C   1 
ATOM   746  O O   . THR   B 2 44  ? -18.085 10.306  -5.705  1.00 46.71  ? 53  THR   B O   1 
ATOM   747  C CB  . THR   B 2 44  ? -19.690 8.471   -7.719  1.00 45.62  ? 53  THR   B CB  1 
ATOM   748  O OG1 . THR   B 2 44  ? -19.664 7.191   -7.085  1.00 43.32  ? 53  THR   B OG1 1 
ATOM   749  C CG2 . THR   B 2 44  ? -20.206 8.333   -9.142  1.00 46.10  ? 53  THR   B CG2 1 
ATOM   750  N N   . LYS   B 2 45  ? -16.775 8.412   -5.896  1.00 48.77  ? 54  LYS   B N   1 
ATOM   751  C CA  . LYS   B 2 45  ? -16.247 8.263   -4.507  1.00 54.27  ? 54  LYS   B CA  1 
ATOM   752  C C   . LYS   B 2 45  ? -17.406 8.013   -3.527  1.00 52.27  ? 54  LYS   B C   1 
ATOM   753  O O   . LYS   B 2 45  ? -17.249 8.410   -2.383  1.00 53.97  ? 54  LYS   B O   1 
ATOM   754  C CB  . LYS   B 2 45  ? -15.478 9.504   -4.030  1.00 57.20  ? 54  LYS   B CB  1 
ATOM   755  C CG  . LYS   B 2 45  ? -14.304 9.938   -4.884  1.00 62.41  ? 54  LYS   B CG  1 
ATOM   756  C CD  . LYS   B 2 45  ? -13.151 8.976   -4.864  1.00 65.79  ? 54  LYS   B CD  1 
ATOM   757  C CE  . LYS   B 2 45  ? -12.039 9.443   -5.785  1.00 71.42  ? 54  LYS   B CE  1 
ATOM   758  N NZ  . LYS   B 2 45  ? -11.265 8.322   -6.398  1.00 75.39  ? 54  LYS   B NZ  1 
ATOM   759  N N   . GLY   B 2 46  ? -18.528 7.437   -3.979  1.00 51.39  ? 55  GLY   B N   1 
ATOM   760  C CA  . GLY   B 2 46  ? -19.722 7.174   -3.155  1.00 51.33  ? 55  GLY   B CA  1 
ATOM   761  C C   . GLY   B 2 46  ? -20.666 8.363   -3.055  1.00 51.34  ? 55  GLY   B C   1 
ATOM   762  O O   . GLY   B 2 46  ? -21.710 8.209   -2.452  1.00 52.07  ? 55  GLY   B O   1 
ATOM   763  N N   . ALA   B 2 47  ? -20.375 9.493   -3.694  1.00 51.40  ? 56  ALA   B N   1 
ATOM   764  C CA  . ALA   B 2 47  ? -21.229 10.700  -3.604  1.00 50.77  ? 56  ALA   B CA  1 
ATOM   765  C C   . ALA   B 2 47  ? -22.555 10.454  -4.335  1.00 50.86  ? 56  ALA   B C   1 
ATOM   766  O O   . ALA   B 2 47  ? -22.589 9.648   -5.293  1.00 49.67  ? 56  ALA   B O   1 
ATOM   767  C CB  . ALA   B 2 47  ? -20.503 11.891  -4.187  1.00 51.20  ? 56  ALA   B CB  1 
ATOM   768  N N   . ALA   B 2 48  ? -23.603 11.173  -3.940  1.00 50.28  ? 57  ALA   B N   1 
ATOM   769  C CA  . ALA   B 2 48  ? -24.917 11.126  -4.610  1.00 51.56  ? 57  ALA   B CA  1 
ATOM   770  C C   . ALA   B 2 48  ? -24.832 11.837  -5.974  1.00 52.85  ? 57  ALA   B C   1 
ATOM   771  O O   . ALA   B 2 48  ? -23.856 12.560  -6.219  1.00 54.27  ? 57  ALA   B O   1 
ATOM   772  C CB  . ALA   B 2 48  ? -25.979 11.719  -3.730  1.00 52.10  ? 57  ALA   B CB  1 
ATOM   773  N N   . LEU   B 2 49  ? -25.832 11.622  -6.829  1.00 52.84  ? 58  LEU   B N   1 
ATOM   774  C CA  . LEU   B 2 49  ? -25.873 12.097  -8.240  1.00 54.69  ? 58  LEU   B CA  1 
ATOM   775  C C   . LEU   B 2 49  ? -27.216 12.776  -8.513  1.00 56.80  ? 58  LEU   B C   1 
ATOM   776  O O   . LEU   B 2 49  ? -28.219 12.413  -7.855  1.00 58.14  ? 58  LEU   B O   1 
ATOM   777  C CB  . LEU   B 2 49  ? -25.710 10.905  -9.189  1.00 52.86  ? 58  LEU   B CB  1 
ATOM   778  C CG  . LEU   B 2 49  ? -24.507 10.001  -8.960  1.00 51.60  ? 58  LEU   B CG  1 
ATOM   779  C CD1 . LEU   B 2 49  ? -24.641 8.723   -9.757  1.00 50.88  ? 58  LEU   B CD1 1 
ATOM   780  C CD2 . LEU   B 2 49  ? -23.221 10.720  -9.298  1.00 51.79  ? 58  LEU   B CD2 1 
ATOM   781  N N   . ARG   B 2 50  ? -27.231 13.705  -9.469  1.00 59.41  ? 59  ARG   B N   1 
ATOM   782  C CA  . ARG   B 2 50  ? -28.459 14.353  -9.994  1.00 61.04  ? 59  ARG   B CA  1 
ATOM   783  C C   . ARG   B 2 50  ? -28.847 13.715  -11.340 1.00 60.15  ? 59  ARG   B C   1 
ATOM   784  O O   . ARG   B 2 50  ? -27.947 13.344  -12.121 1.00 56.40  ? 59  ARG   B O   1 
ATOM   785  C CB  . ARG   B 2 50  ? -28.153 15.847  -10.064 1.00 65.85  ? 59  ARG   B CB  1 
ATOM   786  C CG  . ARG   B 2 50  ? -29.325 16.734  -10.458 1.00 71.71  ? 59  ARG   B CG  1 
ATOM   787  C CD  . ARG   B 2 50  ? -29.073 18.193  -10.095 1.00 75.57  ? 59  ARG   B CD  1 
ATOM   788  N NE  . ARG   B 2 50  ? -27.658 18.549  -10.230 1.00 79.70  ? 59  ARG   B NE  1 
ATOM   789  C CZ  . ARG   B 2 50  ? -27.043 18.902  -11.361 1.00 83.16  ? 59  ARG   B CZ  1 
ATOM   790  N NH1 . ARG   B 2 50  ? -27.704 18.960  -12.510 1.00 86.15  ? 59  ARG   B NH1 1 
ATOM   791  N NH2 . ARG   B 2 50  ? -25.752 19.200  -11.335 1.00 85.47  ? 59  ARG   B NH2 1 
ATOM   792  N N   . SER   B 2 51  ? -30.144 13.534  -11.577 1.00 61.55  ? 60  SER   B N   1 
ATOM   793  C CA  . SER   B 2 51  ? -30.744 13.262  -12.912 1.00 64.84  ? 60  SER   B CA  1 
ATOM   794  C C   . SER   B 2 51  ? -31.915 14.236  -13.164 1.00 68.40  ? 60  SER   B C   1 
ATOM   795  O O   . SER   B 2 51  ? -33.085 13.877  -12.885 1.00 68.57  ? 60  SER   B O   1 
ATOM   796  C CB  . SER   B 2 51  ? -31.183 11.835  -13.011 1.00 63.57  ? 60  SER   B CB  1 
ATOM   797  O OG  . SER   B 2 51  ? -31.870 11.619  -14.229 1.00 64.63  ? 60  SER   B OG  1 
ATOM   798  N N   . GLY   B 2 52  ? -31.628 15.449  -13.642 1.00 72.75  ? 61  GLY   B N   1 
ATOM   799  C CA  . GLY   B 2 52  ? -32.633 16.528  -13.739 1.00 77.04  ? 61  GLY   B CA  1 
ATOM   800  C C   . GLY   B 2 52  ? -32.781 17.231  -12.402 1.00 81.66  ? 61  GLY   B C   1 
ATOM   801  O O   . GLY   B 2 52  ? -31.761 17.759  -11.911 1.00 81.59  ? 61  GLY   B O   1 
ATOM   802  N N   . GLU   B 2 53  ? -33.983 17.223  -11.814 1.00 88.10  ? 62  GLU   B N   1 
ATOM   803  C CA  . GLU   B 2 53  ? -34.179 17.627  -10.392 1.00 91.62  ? 62  GLU   B CA  1 
ATOM   804  C C   . GLU   B 2 53  ? -34.347 16.383  -9.502  1.00 85.50  ? 62  GLU   B C   1 
ATOM   805  O O   . GLU   B 2 53  ? -34.504 16.587  -8.292  1.00 83.02  ? 62  GLU   B O   1 
ATOM   806  C CB  . GLU   B 2 53  ? -35.312 18.653  -10.261 1.00 98.70  ? 62  GLU   B CB  1 
ATOM   807  C CG  . GLU   B 2 53  ? -34.828 20.083  -10.489 1.00 108.29 ? 62  GLU   B CG  1 
ATOM   808  C CD  . GLU   B 2 53  ? -35.099 21.103  -9.386  1.00 118.79 ? 62  GLU   B CD  1 
ATOM   809  O OE1 . GLU   B 2 53  ? -36.069 20.921  -8.607  1.00 128.53 ? 62  GLU   B OE1 1 
ATOM   810  O OE2 . GLU   B 2 53  ? -34.326 22.089  -9.306  1.00 123.03 ? 62  GLU   B OE2 1 
ATOM   811  N N   . GLY   B 2 54  ? -34.254 15.162  -10.061 1.00 78.74  ? 63  GLY   B N   1 
ATOM   812  C CA  . GLY   B 2 54  ? -34.207 13.886  -9.314  1.00 75.70  ? 63  GLY   B CA  1 
ATOM   813  C C   . GLY   B 2 54  ? -32.844 13.646  -8.662  1.00 72.85  ? 63  GLY   B C   1 
ATOM   814  O O   . GLY   B 2 54  ? -31.837 14.137  -9.212  1.00 72.20  ? 63  GLY   B O   1 
ATOM   815  N N   . ARG   B 2 55  ? -32.809 12.931  -7.524  1.00 67.78  ? 64  ARG   B N   1 
ATOM   816  C CA  . ARG   B 2 55  ? -31.580 12.576  -6.746  1.00 66.38  ? 64  ARG   B CA  1 
ATOM   817  C C   . ARG   B 2 55  ? -31.384 11.056  -6.773  1.00 62.47  ? 64  ARG   B C   1 
ATOM   818  O O   . ARG   B 2 55  ? -32.373 10.317  -6.603  1.00 60.62  ? 64  ARG   B O   1 
ATOM   819  C CB  . ARG   B 2 55  ? -31.660 13.017  -5.274  1.00 69.40  ? 64  ARG   B CB  1 
ATOM   820  C CG  . ARG   B 2 55  ? -30.349 12.943  -4.498  1.00 72.21  ? 64  ARG   B CG  1 
ATOM   821  C CD  . ARG   B 2 55  ? -30.516 13.363  -3.037  1.00 76.43  ? 64  ARG   B CD  1 
ATOM   822  N NE  . ARG   B 2 55  ? -29.394 13.022  -2.152  1.00 79.06  ? 64  ARG   B NE  1 
ATOM   823  C CZ  . ARG   B 2 55  ? -28.625 13.876  -1.447  1.00 81.60  ? 64  ARG   B CZ  1 
ATOM   824  N NH1 . ARG   B 2 55  ? -28.823 15.184  -1.496  1.00 81.50  ? 64  ARG   B NH1 1 
ATOM   825  N NH2 . ARG   B 2 55  ? -27.653 13.403  -0.672  1.00 82.76  ? 64  ARG   B NH2 1 
ATOM   826  N N   . LEU   B 2 56  ? -30.146 10.604  -6.959  1.00 58.54  ? 65  LEU   B N   1 
ATOM   827  C CA  . LEU   B 2 56  ? -29.766 9.177   -6.854  1.00 56.19  ? 65  LEU   B CA  1 
ATOM   828  C C   . LEU   B 2 56  ? -28.872 9.047   -5.625  1.00 53.00  ? 65  LEU   B C   1 
ATOM   829  O O   . LEU   B 2 56  ? -27.812 9.734   -5.614  1.00 51.11  ? 65  LEU   B O   1 
ATOM   830  C CB  . LEU   B 2 56  ? -29.007 8.742   -8.119  1.00 55.66  ? 65  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 2 56  ? -29.705 8.916   -9.462  1.00 58.24  ? 65  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 2 56  ? -29.179 7.881   -10.457 1.00 56.75  ? 65  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 2 56  ? -31.214 8.789   -9.335  1.00 58.75  ? 65  LEU   B CD2 1 
ATOM   834  N N   . ASP   B 2 57  ? -29.252 8.210   -4.650  1.00 51.75  ? 66  ASP   B N   1 
ATOM   835  C CA  . ASP   B 2 57  ? -28.420 7.992   -3.436  1.00 50.22  ? 66  ASP   B CA  1 
ATOM   836  C C   . ASP   B 2 57  ? -27.727 6.641   -3.527  1.00 46.79  ? 66  ASP   B C   1 
ATOM   837  O O   . ASP   B 2 57  ? -28.336 5.647   -3.936  1.00 45.99  ? 66  ASP   B O   1 
ATOM   838  C CB  . ASP   B 2 57  ? -29.237 8.080   -2.150  1.00 54.25  ? 66  ASP   B CB  1 
ATOM   839  C CG  . ASP   B 2 57  ? -29.689 9.502   -1.858  1.00 57.06  ? 66  ASP   B CG  1 
ATOM   840  O OD1 . ASP   B 2 57  ? -28.839 10.403  -1.905  1.00 61.79  ? 66  ASP   B OD1 1 
ATOM   841  O OD2 . ASP   B 2 57  ? -30.883 9.700   -1.655  1.00 59.44  ? 66  ASP   B OD2 1 
ATOM   842  N N   . PRO   B 2 58  ? -26.455 6.552   -3.088  1.00 43.77  ? 67  PRO   B N   1 
ATOM   843  C CA  . PRO   B 2 58  ? -25.764 5.275   -3.079  1.00 42.91  ? 67  PRO   B CA  1 
ATOM   844  C C   . PRO   B 2 58  ? -26.586 4.293   -2.231  1.00 42.87  ? 67  PRO   B C   1 
ATOM   845  O O   . PRO   B 2 58  ? -27.277 4.690   -1.277  1.00 43.53  ? 67  PRO   B O   1 
ATOM   846  C CB  . PRO   B 2 58  ? -24.364 5.603   -2.540  1.00 43.04  ? 67  PRO   B CB  1 
ATOM   847  C CG  . PRO   B 2 58  ? -24.533 6.904   -1.784  1.00 43.14  ? 67  PRO   B CG  1 
ATOM   848  C CD  . PRO   B 2 58  ? -25.654 7.636   -2.488  1.00 43.66  ? 67  PRO   B CD  1 
ATOM   849  N N   . TYR   B 2 59  ? -26.548 3.025   -2.616  1.00 41.03  ? 68  TYR   B N   1 
ATOM   850  C CA  . TYR   B 2 59  ? -27.264 1.928   -1.941  1.00 40.31  ? 68  TYR   B CA  1 
ATOM   851  C C   . TYR   B 2 59  ? -26.221 0.910   -1.496  1.00 39.65  ? 68  TYR   B C   1 
ATOM   852  O O   . TYR   B 2 59  ? -26.366 0.320   -0.430  1.00 38.58  ? 68  TYR   B O   1 
ATOM   853  C CB  . TYR   B 2 59  ? -28.365 1.382   -2.855  1.00 40.60  ? 68  TYR   B CB  1 
ATOM   854  C CG  . TYR   B 2 59  ? -29.204 0.263   -2.284  1.00 40.66  ? 68  TYR   B CG  1 
ATOM   855  C CD1 . TYR   B 2 59  ? -28.702 -1.020  -2.231  1.00 40.63  ? 68  TYR   B CD1 1 
ATOM   856  C CD2 . TYR   B 2 59  ? -30.512 0.469   -1.851  1.00 41.02  ? 68  TYR   B CD2 1 
ATOM   857  C CE1 . TYR   B 2 59  ? -29.459 -2.071  -1.730  1.00 41.41  ? 68  TYR   B CE1 1 
ATOM   858  C CE2 . TYR   B 2 59  ? -31.292 -0.577  -1.369  1.00 41.53  ? 68  TYR   B CE2 1 
ATOM   859  C CZ  . TYR   B 2 59  ? -30.757 -1.861  -1.281  1.00 41.91  ? 68  TYR   B CZ  1 
ATOM   860  O OH  . TYR   B 2 59  ? -31.447 -2.947  -0.757  1.00 42.51  ? 68  TYR   B OH  1 
ATOM   861  N N   . TRP   B 2 60  ? -25.194 0.695   -2.302  1.00 38.93  ? 69  TRP   B N   1 
ATOM   862  C CA  . TRP   B 2 60  ? -24.221 -0.411  -2.122  1.00 38.81  ? 69  TRP   B CA  1 
ATOM   863  C C   . TRP   B 2 60  ? -22.906 0.044   -2.717  1.00 39.47  ? 69  TRP   B C   1 
ATOM   864  O O   . TRP   B 2 60  ? -22.922 0.735   -3.788  1.00 40.00  ? 69  TRP   B O   1 
ATOM   865  C CB  . TRP   B 2 60  ? -24.689 -1.775  -2.664  1.00 38.56  ? 69  TRP   B CB  1 
ATOM   866  C CG  . TRP   B 2 60  ? -23.580 -2.779  -2.629  1.00 39.04  ? 69  TRP   B CG  1 
ATOM   867  C CD1 . TRP   B 2 60  ? -23.211 -3.548  -1.565  1.00 39.60  ? 69  TRP   B CD1 1 
ATOM   868  C CD2 . TRP   B 2 60  ? -22.644 -3.101  -3.683  1.00 39.60  ? 69  TRP   B CD2 1 
ATOM   869  N NE1 . TRP   B 2 60  ? -22.084 -4.271  -1.861  1.00 39.84  ? 69  TRP   B NE1 1 
ATOM   870  C CE2 . TRP   B 2 60  ? -21.716 -4.026  -3.158  1.00 39.32  ? 69  TRP   B CE2 1 
ATOM   871  C CE3 . TRP   B 2 60  ? -22.490 -2.684  -5.023  1.00 39.48  ? 69  TRP   B CE3 1 
ATOM   872  C CZ2 . TRP   B 2 60  ? -20.671 -4.551  -3.911  1.00 39.20  ? 69  TRP   B CZ2 1 
ATOM   873  C CZ3 . TRP   B 2 60  ? -21.455 -3.200  -5.775  1.00 39.02  ? 69  TRP   B CZ3 1 
ATOM   874  C CH2 . TRP   B 2 60  ? -20.567 -4.131  -5.235  1.00 39.61  ? 69  TRP   B CH2 1 
ATOM   875  N N   . GLY   B 2 61  ? -21.806 -0.359  -2.094  1.00 39.70  ? 70  GLY   B N   1 
ATOM   876  C CA  . GLY   B 2 61  ? -20.480 -0.095  -2.659  1.00 39.94  ? 70  GLY   B CA  1 
ATOM   877  C C   . GLY   B 2 61  ? -19.429 -0.891  -1.962  1.00 40.64  ? 70  GLY   B C   1 
ATOM   878  O O   . GLY   B 2 61  ? -19.642 -1.253  -0.739  1.00 39.69  ? 70  GLY   B O   1 
ATOM   879  N N   . ASP   B 2 62  ? -18.295 -1.012  -2.622  1.00 40.66  ? 71  ASP   B N   1 
ATOM   880  C CA  . ASP   B 2 62  ? -17.100 -1.721  -2.122  1.00 42.61  ? 71  ASP   B CA  1 
ATOM   881  C C   . ASP   B 2 62  ? -15.888 -1.189  -2.883  1.00 42.74  ? 71  ASP   B C   1 
ATOM   882  O O   . ASP   B 2 62  ? -15.839 -1.441  -4.109  1.00 43.83  ? 71  ASP   B O   1 
ATOM   883  C CB  . ASP   B 2 62  ? -17.322 -3.212  -2.298  1.00 45.02  ? 71  ASP   B CB  1 
ATOM   884  C CG  . ASP   B 2 62  ? -16.199 -4.052  -1.759  1.00 48.19  ? 71  ASP   B CG  1 
ATOM   885  O OD1 . ASP   B 2 62  ? -15.168 -3.477  -1.412  1.00 51.65  ? 71  ASP   B OD1 1 
ATOM   886  O OD2 . ASP   B 2 62  ? -16.403 -5.274  -1.632  1.00 54.22  ? 71  ASP   B OD2 1 
ATOM   887  N N   . VAL   B 2 63  ? -15.019 -0.418  -2.227  1.00 42.66  ? 72  VAL   B N   1 
ATOM   888  C CA  . VAL   B 2 63  ? -13.738 0.156   -2.742  1.00 43.87  ? 72  VAL   B CA  1 
ATOM   889  C C   . VAL   B 2 63  ? -12.856 -0.977  -3.296  1.00 45.09  ? 72  VAL   B C   1 
ATOM   890  O O   . VAL   B 2 63  ? -12.071 -0.713  -4.223  1.00 46.42  ? 72  VAL   B O   1 
ATOM   891  C CB  . VAL   B 2 63  ? -12.986 0.939   -1.641  1.00 44.04  ? 72  VAL   B CB  1 
ATOM   892  C CG1 . VAL   B 2 63  ? -11.492 0.969   -1.833  1.00 44.75  ? 72  VAL   B CG1 1 
ATOM   893  C CG2 . VAL   B 2 63  ? -13.493 2.358   -1.452  1.00 44.95  ? 72  VAL   B CG2 1 
ATOM   894  N N   . LYS   B 2 64  ? -12.946 -2.203  -2.779  1.00 46.17  ? 73  LYS   B N   1 
ATOM   895  C CA  . LYS   B 2 64  ? -12.021 -3.262  -3.259  1.00 47.06  ? 73  LYS   B CA  1 
ATOM   896  C C   . LYS   B 2 64  ? -12.439 -3.795  -4.649  1.00 45.92  ? 73  LYS   B C   1 
ATOM   897  O O   . LYS   B 2 64  ? -11.537 -4.046  -5.447  1.00 45.72  ? 73  LYS   B O   1 
ATOM   898  C CB  . LYS   B 2 64  ? -11.906 -4.429  -2.292  1.00 47.72  ? 73  LYS   B CB  1 
ATOM   899  C CG  . LYS   B 2 64  ? -10.810 -5.365  -2.762  1.00 49.52  ? 73  LYS   B CG  1 
ATOM   900  C CD  . LYS   B 2 64  ? -10.374 -6.335  -1.770  1.00 50.73  ? 73  LYS   B CD  1 
ATOM   901  C CE  . LYS   B 2 64  ? -9.085  -6.969  -2.225  1.00 53.36  ? 73  LYS   B CE  1 
ATOM   902  N NZ  . LYS   B 2 64  ? -8.833  -8.165  -1.398  1.00 55.64  ? 73  LYS   B NZ  1 
ATOM   903  N N   . GLN   B 2 65  ? -13.733 -4.070  -4.844  1.00 45.23  ? 74  GLN   B N   1 
ATOM   904  C CA  . GLN   B 2 65  ? -14.381 -4.449  -6.115  1.00 45.54  ? 74  GLN   B CA  1 
ATOM   905  C C   . GLN   B 2 65  ? -14.371 -3.249  -7.087  1.00 44.71  ? 74  GLN   B C   1 
ATOM   906  O O   . GLN   B 2 65  ? -14.472 -3.505  -8.286  1.00 43.60  ? 74  GLN   B O   1 
ATOM   907  C CB  . GLN   B 2 65  ? -15.822 -4.900  -5.908  1.00 46.72  ? 74  GLN   B CB  1 
ATOM   908  C CG  . GLN   B 2 65  ? -15.962 -6.272  -5.248  1.00 48.65  ? 74  GLN   B CG  1 
ATOM   909  C CD  . GLN   B 2 65  ? -17.418 -6.615  -4.983  1.00 50.74  ? 74  GLN   B CD  1 
ATOM   910  O OE1 . GLN   B 2 65  ? -18.247 -6.792  -5.884  1.00 54.75  ? 74  GLN   B OE1 1 
ATOM   911  N NE2 . GLN   B 2 65  ? -17.781 -6.689  -3.720  1.00 52.20  ? 74  GLN   B NE2 1 
ATOM   912  N N   . ASP   B 2 66  ? -14.215 -2.030  -6.548  1.00 43.17  ? 75  ASP   B N   1 
ATOM   913  C CA  . ASP   B 2 66  ? -14.301 -0.685  -7.173  1.00 42.22  ? 75  ASP   B CA  1 
ATOM   914  C C   . ASP   B 2 66  ? -15.645 -0.545  -7.861  1.00 41.21  ? 75  ASP   B C   1 
ATOM   915  O O   . ASP   B 2 66  ? -15.626 0.008   -8.971  1.00 40.08  ? 75  ASP   B O   1 
ATOM   916  C CB  . ASP   B 2 66  ? -13.153 -0.403  -8.159  1.00 43.19  ? 75  ASP   B CB  1 
ATOM   917  C CG  . ASP   B 2 66  ? -13.056 1.025   -8.672  1.00 43.17  ? 75  ASP   B CG  1 
ATOM   918  O OD1 . ASP   B 2 66  ? -13.528 1.943   -8.011  1.00 42.42  ? 75  ASP   B OD1 1 
ATOM   919  O OD2 . ASP   B 2 66  ? -12.536 1.195   -9.825  1.00 46.04  ? 75  ASP   B OD2 1 
ATOM   920  N N   . LEU   B 2 67  ? -16.744 -0.933  -7.187  1.00 39.68  ? 76  LEU   B N   1 
ATOM   921  C CA  . LEU   B 2 67  ? -18.132 -0.833  -7.706  1.00 38.83  ? 76  LEU   B CA  1 
ATOM   922  C C   . LEU   B 2 67  ? -19.043 -0.088  -6.748  1.00 39.47  ? 76  LEU   B C   1 
ATOM   923  O O   . LEU   B 2 67  ? -18.789 -0.122  -5.494  1.00 38.98  ? 76  LEU   B O   1 
ATOM   924  C CB  . LEU   B 2 67  ? -18.624 -2.256  -7.956  1.00 38.68  ? 76  LEU   B CB  1 
ATOM   925  C CG  . LEU   B 2 67  ? -17.910 -2.979  -9.109  1.00 38.62  ? 76  LEU   B CG  1 
ATOM   926  C CD1 . LEU   B 2 67  ? -18.389 -4.409  -9.219  1.00 38.50  ? 76  LEU   B CD1 1 
ATOM   927  C CD2 . LEU   B 2 67  ? -18.138 -2.211  -10.433 1.00 39.05  ? 76  LEU   B CD2 1 
ATOM   928  N N   . VAL   B 2 68  ? -20.105 0.514   -7.285  1.00 39.38  ? 77  VAL   B N   1 
ATOM   929  C CA  . VAL   B 2 68  ? -21.152 1.213   -6.491  1.00 39.11  ? 77  VAL   B CA  1 
ATOM   930  C C   . VAL   B 2 68  ? -22.460 1.179   -7.279  1.00 38.91  ? 77  VAL   B C   1 
ATOM   931  O O   . VAL   B 2 68  ? -22.401 1.327   -8.540  1.00 39.41  ? 77  VAL   B O   1 
ATOM   932  C CB  . VAL   B 2 68  ? -20.712 2.644   -6.142  1.00 39.66  ? 77  VAL   B CB  1 
ATOM   933  C CG1 . VAL   B 2 68  ? -20.378 3.459   -7.389  1.00 40.46  ? 77  VAL   B CG1 1 
ATOM   934  C CG2 . VAL   B 2 68  ? -21.773 3.362   -5.294  1.00 39.84  ? 77  VAL   B CG2 1 
ATOM   935  N N   . SER   B 2 69  ? -23.585 0.997   -6.586  1.00 37.96  ? 78  SER   B N   1 
ATOM   936  C CA  . SER   B 2 69  ? -24.961 0.975   -7.117  1.00 37.69  ? 78  SER   B CA  1 
ATOM   937  C C   . SER   B 2 69  ? -25.773 2.052   -6.436  1.00 38.00  ? 78  SER   B C   1 
ATOM   938  O O   . SER   B 2 69  ? -25.577 2.263   -5.166  1.00 37.50  ? 78  SER   B O   1 
ATOM   939  C CB  . SER   B 2 69  ? -25.591 -0.375  -6.974  1.00 38.31  ? 78  SER   B CB  1 
ATOM   940  O OG  . SER   B 2 69  ? -26.039 -0.606  -5.625  1.00 38.84  ? 78  SER   B OG  1 
ATOM   941  N N   . TYR   B 2 70  ? -26.716 2.635   -7.172  1.00 38.26  ? 79  TYR   B N   1 
ATOM   942  C CA  . TYR   B 2 70  ? -27.572 3.757   -6.723  1.00 38.63  ? 79  TYR   B CA  1 
ATOM   943  C C   . TYR   B 2 70  ? -29.024 3.325   -6.852  1.00 39.54  ? 79  TYR   B C   1 
ATOM   944  O O   . TYR   B 2 70  ? -29.347 2.752   -7.880  1.00 38.77  ? 79  TYR   B O   1 
ATOM   945  C CB  . TYR   B 2 70  ? -27.300 5.022   -7.535  1.00 38.67  ? 79  TYR   B CB  1 
ATOM   946  C CG  . TYR   B 2 70  ? -25.950 5.634   -7.276  1.00 38.69  ? 79  TYR   B CG  1 
ATOM   947  C CD1 . TYR   B 2 70  ? -24.778 5.075   -7.756  1.00 38.82  ? 79  TYR   B CD1 1 
ATOM   948  C CD2 . TYR   B 2 70  ? -25.837 6.771   -6.510  1.00 39.59  ? 79  TYR   B CD2 1 
ATOM   949  C CE1 . TYR   B 2 70  ? -23.542 5.656   -7.517  1.00 38.74  ? 79  TYR   B CE1 1 
ATOM   950  C CE2 . TYR   B 2 70  ? -24.612 7.347   -6.221  1.00 39.61  ? 79  TYR   B CE2 1 
ATOM   951  C CZ  . TYR   B 2 70  ? -23.462 6.785   -6.725  1.00 39.56  ? 79  TYR   B CZ  1 
ATOM   952  O OH  . TYR   B 2 70  ? -22.290 7.406   -6.396  1.00 40.82  ? 79  TYR   B OH  1 
ATOM   953  N N   . CYS   B 2 71  ? -29.846 3.626   -5.835  1.00 40.83  ? 80  CYS   B N   1 
ATOM   954  C CA  . CYS   B 2 71  ? -31.322 3.430   -5.774  1.00 42.65  ? 80  CYS   B CA  1 
ATOM   955  C C   . CYS   B 2 71  ? -31.644 1.958   -5.533  1.00 42.07  ? 80  CYS   B C   1 
ATOM   956  O O   . CYS   B 2 71  ? -32.801 1.629   -5.294  1.00 43.75  ? 80  CYS   B O   1 
ATOM   957  C CB  . CYS   B 2 71  ? -32.043 3.893   -7.032  1.00 45.16  ? 80  CYS   B CB  1 
ATOM   958  S SG  . CYS   B 2 71  ? -31.580 5.592   -7.463  1.00 51.00  ? 80  CYS   B SG  1 
ATOM   959  N N   . GLY   B 2 72  ? -30.662 1.072   -5.553  1.00 40.48  ? 81  GLY   B N   1 
ATOM   960  C CA  . GLY   B 2 72  ? -31.027 -0.322  -5.318  1.00 39.92  ? 81  GLY   B CA  1 
ATOM   961  C C   . GLY   B 2 72  ? -29.772 -1.152  -5.354  1.00 39.39  ? 81  GLY   B C   1 
ATOM   962  O O   . GLY   B 2 72  ? -28.669 -0.641  -5.567  1.00 38.82  ? 81  GLY   B O   1 
ATOM   963  N N   . PRO   B 2 73  ? -29.963 -2.469  -5.131  1.00 39.76  ? 82  PRO   B N   1 
ATOM   964  C CA  . PRO   B 2 73  ? -28.859 -3.433  -5.146  1.00 40.46  ? 82  PRO   B CA  1 
ATOM   965  C C   . PRO   B 2 73  ? -28.311 -3.665  -6.564  1.00 41.29  ? 82  PRO   B C   1 
ATOM   966  O O   . PRO   B 2 73  ? -29.079 -3.529  -7.523  1.00 42.22  ? 82  PRO   B O   1 
ATOM   967  C CB  . PRO   B 2 73  ? -29.467 -4.723  -4.568  1.00 40.30  ? 82  PRO   B CB  1 
ATOM   968  C CG  . PRO   B 2 73  ? -30.967 -4.567  -4.684  1.00 40.46  ? 82  PRO   B CG  1 
ATOM   969  C CD  . PRO   B 2 73  ? -31.268 -3.083  -4.831  1.00 40.13  ? 82  PRO   B CD  1 
ATOM   970  N N   . TRP   B 2 74  ? -27.047 -4.086  -6.665  1.00 41.86  ? 83  TRP   B N   1 
ATOM   971  C CA  . TRP   B 2 74  ? -26.388 -4.465  -7.935  1.00 42.55  ? 83  TRP   B CA  1 
ATOM   972  C C   . TRP   B 2 74  ? -27.286 -5.436  -8.721  1.00 44.87  ? 83  TRP   B C   1 
ATOM   973  O O   . TRP   B 2 74  ? -27.560 -6.507  -8.169  1.00 44.41  ? 83  TRP   B O   1 
ATOM   974  C CB  . TRP   B 2 74  ? -24.998 -5.054  -7.676  1.00 41.71  ? 83  TRP   B CB  1 
ATOM   975  C CG  . TRP   B 2 74  ? -24.185 -5.195  -8.927  1.00 40.71  ? 83  TRP   B CG  1 
ATOM   976  C CD1 . TRP   B 2 74  ? -24.118 -6.282  -9.750  1.00 40.65  ? 83  TRP   B CD1 1 
ATOM   977  C CD2 . TRP   B 2 74  ? -23.314 -4.207  -9.498  1.00 39.99  ? 83  TRP   B CD2 1 
ATOM   978  N NE1 . TRP   B 2 74  ? -23.237 -6.055  -10.772 1.00 40.13  ? 83  TRP   B NE1 1 
ATOM   979  C CE2 . TRP   B 2 74  ? -22.766 -4.772  -10.672 1.00 39.98  ? 83  TRP   B CE2 1 
ATOM   980  C CE3 . TRP   B 2 74  ? -22.981 -2.892  -9.157  1.00 39.46  ? 83  TRP   B CE3 1 
ATOM   981  C CZ2 . TRP   B 2 74  ? -21.884 -4.068  -11.493 1.00 39.89  ? 83  TRP   B CZ2 1 
ATOM   982  C CZ3 . TRP   B 2 74  ? -22.131 -2.187  -9.971  1.00 39.53  ? 83  TRP   B CZ3 1 
ATOM   983  C CH2 . TRP   B 2 74  ? -21.592 -2.772  -11.136 1.00 39.84  ? 83  TRP   B CH2 1 
ATOM   984  N N   . LYS   B 2 75  ? -27.585 -5.130  -10.016 1.00 46.64  ? 84  LYS   B N   1 
ATOM   985  C CA  . LYS   B 2 75  ? -28.559 -5.863  -10.859 1.00 48.30  ? 84  LYS   B CA  1 
ATOM   986  C C   . LYS   B 2 75  ? -27.891 -6.772  -11.907 1.00 50.46  ? 84  LYS   B C   1 
ATOM   987  O O   . LYS   B 2 75  ? -28.596 -7.639  -12.440 1.00 52.77  ? 84  LYS   B O   1 
ATOM   988  C CB  . LYS   B 2 75  ? -29.429 -4.838  -11.569 1.00 49.40  ? 84  LYS   B CB  1 
ATOM   989  C CG  . LYS   B 2 75  ? -30.307 -4.034  -10.638 1.00 49.04  ? 84  LYS   B CG  1 
ATOM   990  C CD  . LYS   B 2 75  ? -31.343 -4.904  -9.985  1.00 50.18  ? 84  LYS   B CD  1 
ATOM   991  C CE  . LYS   B 2 75  ? -32.144 -4.126  -8.970  1.00 51.24  ? 84  LYS   B CE  1 
ATOM   992  N NZ  . LYS   B 2 75  ? -33.156 -5.005  -8.367  1.00 53.64  ? 84  LYS   B NZ  1 
ATOM   993  N N   . LEU   B 2 76  ? -26.608 -6.586  -12.215 1.00 51.30  ? 85  LEU   B N   1 
ATOM   994  C CA  . LEU   B 2 76  ? -25.940 -7.113  -13.443 1.00 51.07  ? 85  LEU   B CA  1 
ATOM   995  C C   . LEU   B 2 76  ? -25.202 -8.390  -13.072 1.00 53.47  ? 85  LEU   B C   1 
ATOM   996  O O   . LEU   B 2 76  ? -24.222 -8.294  -12.303 1.00 53.50  ? 85  LEU   B O   1 
ATOM   997  C CB  . LEU   B 2 76  ? -24.965 -6.053  -13.953 1.00 49.59  ? 85  LEU   B CB  1 
ATOM   998  C CG  . LEU   B 2 76  ? -25.560 -4.648  -14.087 1.00 48.72  ? 85  LEU   B CG  1 
ATOM   999  C CD1 . LEU   B 2 76  ? -24.496 -3.649  -14.516 1.00 48.66  ? 85  LEU   B CD1 1 
ATOM   1000 C CD2 . LEU   B 2 76  ? -26.729 -4.622  -15.061 1.00 48.82  ? 85  LEU   B CD2 1 
ATOM   1001 N N   . ASP   B 2 77  ? -25.666 -9.530  -13.574 1.00 56.89  ? 86  ASP   B N   1 
ATOM   1002 C CA  . ASP   B 2 77  ? -25.207 -10.865 -13.109 1.00 60.56  ? 86  ASP   B CA  1 
ATOM   1003 C C   . ASP   B 2 77  ? -24.672 -11.694 -14.279 1.00 59.86  ? 86  ASP   B C   1 
ATOM   1004 O O   . ASP   B 2 77  ? -24.323 -12.846 -14.033 1.00 61.27  ? 86  ASP   B O   1 
ATOM   1005 C CB  . ASP   B 2 77  ? -26.325 -11.603 -12.358 1.00 64.04  ? 86  ASP   B CB  1 
ATOM   1006 C CG  . ASP   B 2 77  ? -27.587 -11.838 -13.179 1.00 69.00  ? 86  ASP   B CG  1 
ATOM   1007 O OD1 . ASP   B 2 77  ? -27.765 -11.139 -14.215 1.00 69.36  ? 86  ASP   B OD1 1 
ATOM   1008 O OD2 . ASP   B 2 77  ? -28.394 -12.711 -12.773 1.00 73.84  ? 86  ASP   B OD2 1 
ATOM   1009 N N   . ALA   B 2 78  ? -24.558 -11.147 -15.495 1.00 58.61  ? 87  ALA   B N   1 
ATOM   1010 C CA  . ALA   B 2 78  ? -23.982 -11.877 -16.644 1.00 55.71  ? 87  ALA   B CA  1 
ATOM   1011 C C   . ALA   B 2 78  ? -22.452 -11.897 -16.494 1.00 54.48  ? 87  ALA   B C   1 
ATOM   1012 O O   . ALA   B 2 78  ? -21.878 -10.962 -15.863 1.00 53.96  ? 87  ALA   B O   1 
ATOM   1013 C CB  . ALA   B 2 78  ? -24.442 -11.251 -17.951 1.00 56.30  ? 87  ALA   B CB  1 
ATOM   1014 N N   . ALA   B 2 79  ? -21.815 -12.916 -17.079 1.00 53.54  ? 88  ALA   B N   1 
ATOM   1015 C CA  . ALA   B 2 79  ? -20.381 -13.267 -16.961 1.00 53.21  ? 88  ALA   B CA  1 
ATOM   1016 C C   . ALA   B 2 79  ? -19.774 -13.552 -18.352 1.00 53.51  ? 88  ALA   B C   1 
ATOM   1017 O O   . ALA   B 2 79  ? -20.446 -14.241 -19.082 1.00 51.06  ? 88  ALA   B O   1 
ATOM   1018 C CB  . ALA   B 2 79  ? -20.299 -14.518 -16.124 1.00 53.70  ? 88  ALA   B CB  1 
ATOM   1019 N N   . TRP   B 2 80  ? -18.537 -13.104 -18.652 1.00 53.94  ? 89  TRP   B N   1 
ATOM   1020 C CA  . TRP   B 2 80  ? -17.715 -13.566 -19.809 1.00 55.64  ? 89  TRP   B CA  1 
ATOM   1021 C C   . TRP   B 2 80  ? -17.634 -15.092 -19.754 1.00 57.33  ? 89  TRP   B C   1 
ATOM   1022 O O   . TRP   B 2 80  ? -17.514 -15.650 -18.638 1.00 55.94  ? 89  TRP   B O   1 
ATOM   1023 C CB  . TRP   B 2 80  ? -16.311 -12.935 -19.851 1.00 55.13  ? 89  TRP   B CB  1 
ATOM   1024 C CG  . TRP   B 2 80  ? -15.473 -13.368 -21.025 1.00 56.17  ? 89  TRP   B CG  1 
ATOM   1025 C CD1 . TRP   B 2 80  ? -15.873 -13.510 -22.328 1.00 55.75  ? 89  TRP   B CD1 1 
ATOM   1026 C CD2 . TRP   B 2 80  ? -14.062 -13.660 -21.011 1.00 56.02  ? 89  TRP   B CD2 1 
ATOM   1027 N NE1 . TRP   B 2 80  ? -14.821 -13.881 -23.117 1.00 56.77  ? 89  TRP   B NE1 1 
ATOM   1028 C CE2 . TRP   B 2 80  ? -13.696 -13.977 -22.340 1.00 56.54  ? 89  TRP   B CE2 1 
ATOM   1029 C CE3 . TRP   B 2 80  ? -13.081 -13.710 -20.005 1.00 56.22  ? 89  TRP   B CE3 1 
ATOM   1030 C CZ2 . TRP   B 2 80  ? -12.400 -14.354 -22.681 1.00 56.41  ? 89  TRP   B CZ2 1 
ATOM   1031 C CZ3 . TRP   B 2 80  ? -11.792 -14.070 -20.349 1.00 56.35  ? 89  TRP   B CZ3 1 
ATOM   1032 C CH2 . TRP   B 2 80  ? -11.460 -14.370 -21.678 1.00 56.38  ? 89  TRP   B CH2 1 
ATOM   1033 N N   . ASP   B 2 81  ? -17.747 -15.747 -20.910 1.00 59.93  ? 90  ASP   B N   1 
ATOM   1034 C CA  . ASP   B 2 81  ? -17.836 -17.228 -20.967 1.00 61.95  ? 90  ASP   B CA  1 
ATOM   1035 C C   . ASP   B 2 81  ? -16.429 -17.806 -21.096 1.00 63.50  ? 90  ASP   B C   1 
ATOM   1036 O O   . ASP   B 2 81  ? -16.340 -19.032 -21.094 1.00 67.49  ? 90  ASP   B O   1 
ATOM   1037 C CB  . ASP   B 2 81  ? -18.779 -17.692 -22.075 1.00 63.18  ? 90  ASP   B CB  1 
ATOM   1038 C CG  . ASP   B 2 81  ? -18.323 -17.383 -23.479 1.00 63.07  ? 90  ASP   B CG  1 
ATOM   1039 O OD1 . ASP   B 2 81  ? -17.286 -16.679 -23.658 1.00 64.35  ? 90  ASP   B OD1 1 
ATOM   1040 O OD2 . ASP   B 2 81  ? -19.015 -17.846 -24.385 1.00 67.11  ? 90  ASP   B OD2 1 
ATOM   1041 N N   . GLY   B 2 82  ? -15.404 -16.945 -21.157 1.00 63.62  ? 91  GLY   B N   1 
ATOM   1042 C CA  . GLY   B 2 82  ? -13.978 -17.305 -21.228 1.00 64.28  ? 91  GLY   B CA  1 
ATOM   1043 C C   . GLY   B 2 82  ? -13.544 -17.655 -22.646 1.00 64.92  ? 91  GLY   B C   1 
ATOM   1044 O O   . GLY   B 2 82  ? -12.357 -17.997 -22.821 1.00 65.19  ? 91  GLY   B O   1 
ATOM   1045 N N   . LEU   B 2 83  ? -14.451 -17.578 -23.625 1.00 66.11  ? 92  LEU   B N   1 
ATOM   1046 C CA  . LEU   B 2 83  ? -14.223 -18.058 -25.019 1.00 66.91  ? 92  LEU   B CA  1 
ATOM   1047 C C   . LEU   B 2 83  ? -14.481 -16.951 -26.037 1.00 67.89  ? 92  LEU   B C   1 
ATOM   1048 O O   . LEU   B 2 83  ? -13.571 -16.669 -26.832 1.00 69.24  ? 92  LEU   B O   1 
ATOM   1049 C CB  . LEU   B 2 83  ? -15.193 -19.200 -25.315 1.00 68.21  ? 92  LEU   B CB  1 
ATOM   1050 C CG  . LEU   B 2 83  ? -14.688 -20.624 -25.102 1.00 69.99  ? 92  LEU   B CG  1 
ATOM   1051 C CD1 . LEU   B 2 83  ? -15.269 -21.531 -26.192 1.00 70.95  ? 92  LEU   B CD1 1 
ATOM   1052 C CD2 . LEU   B 2 83  ? -13.164 -20.711 -25.115 1.00 70.59  ? 92  LEU   B CD2 1 
ATOM   1053 N N   . SER   B 2 84  ? -15.708 -16.421 -26.070 1.00 66.78  ? 93  SER   B N   1 
ATOM   1054 C CA  . SER   B 2 84  ? -16.234 -15.567 -27.167 1.00 65.42  ? 93  SER   B CA  1 
ATOM   1055 C C   . SER   B 2 84  ? -15.687 -14.139 -27.042 1.00 65.01  ? 93  SER   B C   1 
ATOM   1056 O O   . SER   B 2 84  ? -15.236 -13.732 -25.948 1.00 65.55  ? 93  SER   B O   1 
ATOM   1057 C CB  . SER   B 2 84  ? -17.743 -15.554 -27.155 1.00 66.96  ? 93  SER   B CB  1 
ATOM   1058 O OG  . SER   B 2 84  ? -18.252 -16.388 -26.110 1.00 68.11  ? 93  SER   B OG  1 
ATOM   1059 N N   . GLU   B 2 85  ? -15.760 -13.381 -28.128 1.00 63.36  ? 94  GLU   B N   1 
ATOM   1060 C CA  . GLU   B 2 85  ? -15.398 -11.946 -28.151 1.00 61.31  ? 94  GLU   B CA  1 
ATOM   1061 C C   . GLU   B 2 85  ? -16.554 -11.198 -27.361 1.00 57.95  ? 94  GLU   B C   1 
ATOM   1062 O O   . GLU   B 2 85  ? -17.689 -11.787 -27.121 1.00 57.00  ? 94  GLU   B O   1 
ATOM   1063 C CB  . GLU   B 2 85  ? -15.167 -11.469 -29.606 1.00 64.26  ? 94  GLU   B CB  1 
ATOM   1064 C CG  . GLU   B 2 85  ? -13.840 -11.959 -30.251 1.00 64.84  ? 94  GLU   B CG  1 
ATOM   1065 C CD  . GLU   B 2 85  ? -13.436 -11.462 -31.645 1.00 66.21  ? 94  GLU   B CD  1 
ATOM   1066 O OE1 . GLU   B 2 85  ? -13.986 -10.434 -32.145 1.00 63.20  ? 94  GLU   B OE1 1 
ATOM   1067 O OE2 . GLU   B 2 85  ? -12.530 -12.091 -32.226 1.00 66.70  ? 94  GLU   B OE2 1 
ATOM   1068 N N   . VAL   B 2 86  ? -16.264 -9.903  -27.175 1.00 54.05  ? 95  VAL   B N   1 
ATOM   1069 C CA  . VAL   B 2 86  ? -17.152 -8.949  -26.448 1.00 52.23  ? 95  VAL   B CA  1 
ATOM   1070 C C   . VAL   B 2 86  ? -17.015 -7.577  -27.082 1.00 50.79  ? 95  VAL   B C   1 
ATOM   1071 O O   . VAL   B 2 86  ? -16.001 -7.371  -27.836 1.00 51.46  ? 95  VAL   B O   1 
ATOM   1072 C CB  . VAL   B 2 86  ? -16.770 -8.876  -24.944 1.00 50.36  ? 95  VAL   B CB  1 
ATOM   1073 C CG1 . VAL   B 2 86  ? -16.718 -10.264 -24.346 1.00 49.91  ? 95  VAL   B CG1 1 
ATOM   1074 C CG2 . VAL   B 2 86  ? -15.441 -8.165  -24.731 1.00 50.61  ? 95  VAL   B CG2 1 
ATOM   1075 N N   . GLN   B 2 87  ? -17.927 -6.668  -26.685 1.00 49.54  ? 96  GLN   B N   1 
ATOM   1076 C CA  . GLN   B 2 87  ? -17.886 -5.242  -27.093 1.00 50.12  ? 96  GLN   B CA  1 
ATOM   1077 C C   . GLN   B 2 87  ? -17.814 -4.347  -25.859 1.00 47.85  ? 96  GLN   B C   1 
ATOM   1078 O O   . GLN   B 2 87  ? -18.778 -4.371  -25.107 1.00 49.33  ? 96  GLN   B O   1 
ATOM   1079 C CB  . GLN   B 2 87  ? -19.087 -4.886  -27.991 1.00 50.07  ? 96  GLN   B CB  1 
ATOM   1080 C CG  . GLN   B 2 87  ? -19.063 -5.673  -29.289 1.00 51.13  ? 96  GLN   B CG  1 
ATOM   1081 C CD  . GLN   B 2 87  ? -20.001 -5.188  -30.383 1.00 51.65  ? 96  GLN   B CD  1 
ATOM   1082 O OE1 . GLN   B 2 87  ? -20.880 -4.322  -30.202 1.00 51.02  ? 96  GLN   B OE1 1 
ATOM   1083 N NE2 . GLN   B 2 87  ? -19.845 -5.811  -31.542 1.00 51.37  ? 96  GLN   B NE2 1 
ATOM   1084 N N   . LEU   B 2 88  ? -16.739 -3.561  -25.736 1.00 46.09  ? 97  LEU   B N   1 
ATOM   1085 C CA  . LEU   B 2 88  ? -16.728 -2.306  -24.952 1.00 45.73  ? 97  LEU   B CA  1 
ATOM   1086 C C   . LEU   B 2 88  ? -17.674 -1.302  -25.613 1.00 46.00  ? 97  LEU   B C   1 
ATOM   1087 O O   . LEU   B 2 88  ? -17.403 -0.889  -26.751 1.00 46.65  ? 97  LEU   B O   1 
ATOM   1088 C CB  . LEU   B 2 88  ? -15.296 -1.775  -24.883 1.00 45.59  ? 97  LEU   B CB  1 
ATOM   1089 C CG  . LEU   B 2 88  ? -15.133 -0.466  -24.122 1.00 45.51  ? 97  LEU   B CG  1 
ATOM   1090 C CD1 . LEU   B 2 88  ? -15.569 -0.638  -22.660 1.00 46.06  ? 97  LEU   B CD1 1 
ATOM   1091 C CD2 . LEU   B 2 88  ? -13.695 0.013   -24.158 1.00 45.82  ? 97  LEU   B CD2 1 
ATOM   1092 N N   . LEU   B 2 89  ? -18.802 -0.988  -24.992 1.00 45.01  ? 98  LEU   B N   1 
ATOM   1093 C CA  . LEU   B 2 89  ? -19.605 0.164   -25.413 1.00 44.79  ? 98  LEU   B CA  1 
ATOM   1094 C C   . LEU   B 2 89  ? -18.913 1.357   -24.771 1.00 45.02  ? 98  LEU   B C   1 
ATOM   1095 O O   . LEU   B 2 89  ? -19.286 1.708   -23.620 1.00 47.65  ? 98  LEU   B O   1 
ATOM   1096 C CB  . LEU   B 2 89  ? -21.061 -0.090  -25.026 1.00 44.58  ? 98  LEU   B CB  1 
ATOM   1097 C CG  . LEU   B 2 89  ? -22.072 1.063   -25.170 1.00 45.75  ? 98  LEU   B CG  1 
ATOM   1098 C CD1 . LEU   B 2 89  ? -21.807 1.964   -26.340 1.00 47.25  ? 98  LEU   B CD1 1 
ATOM   1099 C CD2 . LEU   B 2 89  ? -23.508 0.550   -25.285 1.00 46.07  ? 98  LEU   B CD2 1 
ATOM   1100 N N   . ALA   B 2 90  ? -17.841 1.860   -25.397 1.00 44.80  ? 99  ALA   B N   1 
ATOM   1101 C CA  . ALA   B 2 90  ? -17.031 2.997   -24.890 1.00 45.03  ? 99  ALA   B CA  1 
ATOM   1102 C C   . ALA   B 2 90  ? -17.827 4.284   -25.002 1.00 45.80  ? 99  ALA   B C   1 
ATOM   1103 O O   . ALA   B 2 90  ? -18.421 4.462   -26.073 1.00 45.67  ? 99  ALA   B O   1 
ATOM   1104 C CB  . ALA   B 2 90  ? -15.742 3.171   -25.639 1.00 45.61  ? 99  ALA   B CB  1 
ATOM   1105 N N   . VAL   B 2 91  ? -17.836 5.137   -23.949 1.00 45.60  ? 100 VAL   B N   1 
ATOM   1106 C CA  . VAL   B 2 91  ? -18.497 6.473   -23.983 1.00 45.44  ? 100 VAL   B CA  1 
ATOM   1107 C C   . VAL   B 2 91  ? -17.489 7.541   -23.576 1.00 46.67  ? 100 VAL   B C   1 
ATOM   1108 O O   . VAL   B 2 91  ? -17.481 7.996   -22.442 1.00 45.97  ? 100 VAL   B O   1 
ATOM   1109 C CB  . VAL   B 2 91  ? -19.760 6.468   -23.127 1.00 45.21  ? 100 VAL   B CB  1 
ATOM   1110 C CG1 . VAL   B 2 91  ? -20.393 7.847   -23.053 1.00 45.06  ? 100 VAL   B CG1 1 
ATOM   1111 C CG2 . VAL   B 2 91  ? -20.748 5.412   -23.618 1.00 45.34  ? 100 VAL   B CG2 1 
ATOM   1112 N N   . PRO   B 2 92  ? -16.597 7.992   -24.495 1.00 48.65  ? 101 PRO   B N   1 
ATOM   1113 C CA  . PRO   B 2 92  ? -15.482 8.862   -24.128 1.00 48.59  ? 101 PRO   B CA  1 
ATOM   1114 C C   . PRO   B 2 92  ? -15.897 10.315  -23.946 1.00 48.52  ? 101 PRO   B C   1 
ATOM   1115 O O   . PRO   B 2 92  ? -16.964 10.742  -24.380 1.00 49.22  ? 101 PRO   B O   1 
ATOM   1116 C CB  . PRO   B 2 92  ? -14.455 8.680   -25.256 1.00 49.35  ? 101 PRO   B CB  1 
ATOM   1117 C CG  . PRO   B 2 92  ? -15.082 7.674   -26.218 1.00 50.10  ? 101 PRO   B CG  1 
ATOM   1118 C CD  . PRO   B 2 92  ? -16.566 7.650   -25.920 1.00 49.78  ? 101 PRO   B CD  1 
ATOM   1119 N N   . PRO   B 2 93  ? -15.060 11.127  -23.276 1.00 49.83  ? 102 PRO   B N   1 
ATOM   1120 C CA  . PRO   B 2 93  ? -15.448 12.496  -22.960 1.00 51.21  ? 102 PRO   B CA  1 
ATOM   1121 C C   . PRO   B 2 93  ? -15.622 13.305  -24.258 1.00 53.00  ? 102 PRO   B C   1 
ATOM   1122 O O   . PRO   B 2 93  ? -14.706 13.395  -25.065 1.00 54.76  ? 102 PRO   B O   1 
ATOM   1123 C CB  . PRO   B 2 93  ? -14.332 12.991  -22.024 1.00 50.46  ? 102 PRO   B CB  1 
ATOM   1124 C CG  . PRO   B 2 93  ? -13.691 11.702  -21.506 1.00 50.48  ? 102 PRO   B CG  1 
ATOM   1125 C CD  . PRO   B 2 93  ? -13.756 10.760  -22.687 1.00 50.33  ? 102 PRO   B CD  1 
ATOM   1126 N N   . GLY   B 2 94  ? -16.829 13.825  -24.446 1.00 53.97  ? 103 GLY   B N   1 
ATOM   1127 C CA  . GLY   B 2 94  ? -17.185 14.728  -25.547 1.00 54.88  ? 103 GLY   B CA  1 
ATOM   1128 C C   . GLY   B 2 94  ? -17.381 14.024  -26.889 1.00 55.86  ? 103 GLY   B C   1 
ATOM   1129 O O   . GLY   B 2 94  ? -17.610 14.741  -27.849 1.00 55.38  ? 103 GLY   B O   1 
ATOM   1130 N N   . GLU   B 2 95  ? -17.345 12.687  -26.955 1.00 55.99  ? 104 GLU   B N   1 
ATOM   1131 C CA  . GLU   B 2 95  ? -17.518 11.902  -28.215 1.00 56.05  ? 104 GLU   B CA  1 
ATOM   1132 C C   . GLU   B 2 95  ? -18.705 10.964  -28.014 1.00 56.01  ? 104 GLU   B C   1 
ATOM   1133 O O   . GLU   B 2 95  ? -19.068 10.740  -26.841 1.00 57.50  ? 104 GLU   B O   1 
ATOM   1134 C CB  . GLU   B 2 95  ? -16.225 11.144  -28.540 1.00 56.10  ? 104 GLU   B CB  1 
ATOM   1135 C CG  . GLU   B 2 95  ? -14.997 12.052  -28.466 1.00 57.34  ? 104 GLU   B CG  1 
ATOM   1136 C CD  . GLU   B 2 95  ? -13.597 11.336  -28.548 1.00 59.06  ? 104 GLU   B CD  1 
ATOM   1137 O OE1 . GLU   B 2 95  ? -13.584 10.104  -28.450 1.00 60.68  ? 104 GLU   B OE1 1 
ATOM   1138 O OE2 . GLU   B 2 95  ? -12.555 12.036  -28.643 1.00 61.18  ? 104 GLU   B OE2 1 
ATOM   1139 N N   . ARG   B 2 96  ? -19.285 10.467  -29.094 1.00 56.51  ? 105 ARG   B N   1 
ATOM   1140 C CA  . ARG   B 2 96  ? -20.497 9.621   -29.116 1.00 58.80  ? 105 ARG   B CA  1 
ATOM   1141 C C   . ARG   B 2 96  ? -20.146 8.225   -28.625 1.00 56.32  ? 105 ARG   B C   1 
ATOM   1142 O O   . ARG   B 2 96  ? -18.985 7.786   -28.824 1.00 56.33  ? 105 ARG   B O   1 
ATOM   1143 C CB  . ARG   B 2 96  ? -21.049 9.515   -30.546 1.00 64.14  ? 105 ARG   B CB  1 
ATOM   1144 C CG  . ARG   B 2 96  ? -22.428 8.866   -30.630 1.00 68.31  ? 105 ARG   B CG  1 
ATOM   1145 C CD  . ARG   B 2 96  ? -23.255 9.310   -31.839 1.00 72.65  ? 105 ARG   B CD  1 
ATOM   1146 N NE  . ARG   B 2 96  ? -22.482 9.251   -33.071 1.00 76.08  ? 105 ARG   B NE  1 
ATOM   1147 C CZ  . ARG   B 2 96  ? -21.903 10.290  -33.681 1.00 80.90  ? 105 ARG   B CZ  1 
ATOM   1148 N NH1 . ARG   B 2 96  ? -22.032 11.531  -33.230 1.00 81.02  ? 105 ARG   B NH1 1 
ATOM   1149 N NH2 . ARG   B 2 96  ? -21.202 10.076  -34.780 1.00 85.22  ? 105 ARG   B NH2 1 
ATOM   1150 N N   . ALA   B 2 97  ? -21.131 7.554   -28.020 1.00 55.08  ? 106 ALA   B N   1 
ATOM   1151 C CA  . ALA   B 2 97  ? -21.058 6.122   -27.674 1.00 55.02  ? 106 ALA   B CA  1 
ATOM   1152 C C   . ALA   B 2 97  ? -20.563 5.375   -28.913 1.00 56.32  ? 106 ALA   B C   1 
ATOM   1153 O O   . ALA   B 2 97  ? -21.171 5.577   -29.962 1.00 56.55  ? 106 ALA   B O   1 
ATOM   1154 C CB  . ALA   B 2 97  ? -22.418 5.639   -27.257 1.00 53.96  ? 106 ALA   B CB  1 
ATOM   1155 N N   . LYS   B 2 98  ? -19.561 4.513   -28.781 1.00 57.46  ? 107 LYS   B N   1 
ATOM   1156 C CA  . LYS   B 2 98  ? -19.003 3.701   -29.891 1.00 59.69  ? 107 LYS   B CA  1 
ATOM   1157 C C   . LYS   B 2 98  ? -18.702 2.267   -29.419 1.00 57.06  ? 107 LYS   B C   1 
ATOM   1158 O O   . LYS   B 2 98  ? -17.864 2.164   -28.484 1.00 56.53  ? 107 LYS   B O   1 
ATOM   1159 C CB  . LYS   B 2 98  ? -17.739 4.445   -30.337 1.00 65.56  ? 107 LYS   B CB  1 
ATOM   1160 C CG  . LYS   B 2 98  ? -17.045 3.948   -31.609 1.00 71.33  ? 107 LYS   B CG  1 
ATOM   1161 C CD  . LYS   B 2 98  ? -15.581 4.398   -31.712 1.00 74.93  ? 107 LYS   B CD  1 
ATOM   1162 C CE  . LYS   B 2 98  ? -14.925 4.558   -30.344 1.00 76.10  ? 107 LYS   B CE  1 
ATOM   1163 N NZ  . LYS   B 2 98  ? -13.448 4.459   -30.408 1.00 78.45  ? 107 LYS   B NZ  1 
ATOM   1164 N N   . ASN   B 2 99  ? -19.352 1.226   -29.995 1.00 53.08  ? 108 ASN   B N   1 
ATOM   1165 C CA  . ASN   B 2 99  ? -19.055 -0.211  -29.720 1.00 52.86  ? 108 ASN   B CA  1 
ATOM   1166 C C   . ASN   B 2 99  ? -17.690 -0.601  -30.318 1.00 52.82  ? 108 ASN   B C   1 
ATOM   1167 O O   . ASN   B 2 99  ? -17.443 -0.310  -31.470 1.00 54.22  ? 108 ASN   B O   1 
ATOM   1168 C CB  . ASN   B 2 99  ? -20.093 -1.201  -30.263 1.00 52.41  ? 108 ASN   B CB  1 
ATOM   1169 C CG  . ASN   B 2 99  ? -21.476 -1.057  -29.637 1.00 52.18  ? 108 ASN   B CG  1 
ATOM   1170 O OD1 . ASN   B 2 99  ? -22.093 0.026   -29.719 1.00 54.07  ? 108 ASN   B OD1 1 
ATOM   1171 N ND2 . ASN   B 2 99  ? -22.023 -2.157  -29.136 1.00 51.29  ? 108 ASN   B ND2 1 
ATOM   1172 N N   . ILE   B 2 100 ? -16.845 -1.291  -29.575 1.00 50.97  ? 109 ILE   B N   1 
ATOM   1173 C CA  . ILE   B 2 100 ? -15.499 -1.732  -30.022 1.00 51.18  ? 109 ILE   B CA  1 
ATOM   1174 C C   . ILE   B 2 100 ? -15.387 -3.181  -29.652 1.00 51.78  ? 109 ILE   B C   1 
ATOM   1175 O O   . ILE   B 2 100 ? -15.433 -3.500  -28.415 1.00 55.23  ? 109 ILE   B O   1 
ATOM   1176 C CB  . ILE   B 2 100 ? -14.395 -0.924  -29.341 1.00 52.04  ? 109 ILE   B CB  1 
ATOM   1177 C CG1 . ILE   B 2 100 ? -14.617 0.580   -29.473 1.00 53.46  ? 109 ILE   B CG1 1 
ATOM   1178 C CG2 . ILE   B 2 100 ? -13.025 -1.372  -29.786 1.00 52.52  ? 109 ILE   B CG2 1 
ATOM   1179 C CD1 . ILE   B 2 100 ? -14.529 1.108   -30.881 1.00 54.30  ? 109 ILE   B CD1 1 
ATOM   1180 N N   . GLN   B 2 101 ? -15.204 -4.041  -30.620 1.00 51.94  ? 110 GLN   B N   1 
ATOM   1181 C CA  . GLN   B 2 101 ? -15.240 -5.488  -30.376 1.00 53.64  ? 110 GLN   B CA  1 
ATOM   1182 C C   . GLN   B 2 101 ? -13.817 -6.003  -30.193 1.00 55.07  ? 110 GLN   B C   1 
ATOM   1183 O O   . GLN   B 2 101 ? -12.879 -5.450  -30.856 1.00 54.72  ? 110 GLN   B O   1 
ATOM   1184 C CB  . GLN   B 2 101 ? -15.974 -6.199  -31.482 1.00 55.58  ? 110 GLN   B CB  1 
ATOM   1185 C CG  . GLN   B 2 101 ? -15.849 -7.698  -31.380 1.00 56.64  ? 110 GLN   B CG  1 
ATOM   1186 C CD  . GLN   B 2 101 ? -16.924 -8.316  -32.245 1.00 58.10  ? 110 GLN   B CD  1 
ATOM   1187 O OE1 . GLN   B 2 101 ? -17.960 -7.694  -32.521 1.00 59.55  ? 110 GLN   B OE1 1 
ATOM   1188 N NE2 . GLN   B 2 101 ? -16.652 -9.518  -32.722 1.00 58.92  ? 110 GLN   B NE2 1 
ATOM   1189 N N   . THR   B 2 102 ? -13.669 -6.980  -29.267 1.00 54.61  ? 111 THR   B N   1 
ATOM   1190 C CA  . THR   B 2 102 ? -12.356 -7.502  -28.826 1.00 53.89  ? 111 THR   B CA  1 
ATOM   1191 C C   . THR   B 2 102 ? -12.546 -8.878  -28.152 1.00 54.22  ? 111 THR   B C   1 
ATOM   1192 O O   . THR   B 2 102 ? -13.708 -9.211  -27.643 1.00 57.48  ? 111 THR   B O   1 
ATOM   1193 C CB  . THR   B 2 102 ? -11.681 -6.398  -28.004 1.00 53.42  ? 111 THR   B CB  1 
ATOM   1194 O OG1 . THR   B 2 102 ? -10.263 -6.700  -27.918 1.00 53.25  ? 111 THR   B OG1 1 
ATOM   1195 C CG2 . THR   B 2 102 ? -12.304 -6.234  -26.629 1.00 52.72  ? 111 THR   B CG2 1 
ATOM   1196 N N   . LEU   B 2 103 ? -11.460 -9.681  -28.171 1.00 54.25  ? 112 LEU   B N   1 
ATOM   1197 C CA  . LEU   B 2 103 ? -11.382 -10.941 -27.402 1.00 53.90  ? 112 LEU   B CA  1 
ATOM   1198 C C   . LEU   B 2 103 ? -10.603 -10.623 -26.128 1.00 54.32  ? 112 LEU   B C   1 
ATOM   1199 O O   . LEU   B 2 103 ? -9.413  -10.252 -26.167 1.00 53.42  ? 112 LEU   B O   1 
ATOM   1200 C CB  . LEU   B 2 103 ? -10.679 -12.073 -28.163 1.00 54.48  ? 112 LEU   B CB  1 
ATOM   1201 C CG  . LEU   B 2 103 ? -10.628 -13.384 -27.370 1.00 53.94  ? 112 LEU   B CG  1 
ATOM   1202 C CD1 . LEU   B 2 103 ? -11.965 -14.086 -27.415 1.00 53.73  ? 112 LEU   B CD1 1 
ATOM   1203 C CD2 . LEU   B 2 103 ? -9.550  -14.310 -27.878 1.00 55.78  ? 112 LEU   B CD2 1 
ATOM   1204 N N   . PRO   B 2 104 ? -11.252 -10.736 -24.952 1.00 54.31  ? 113 PRO   B N   1 
ATOM   1205 C CA  . PRO   B 2 104 ? -10.559 -10.500 -23.693 1.00 54.61  ? 113 PRO   B CA  1 
ATOM   1206 C C   . PRO   B 2 104 ? -9.316  -11.413 -23.547 1.00 55.27  ? 113 PRO   B C   1 
ATOM   1207 O O   . PRO   B 2 104 ? -9.264  -12.625 -24.067 1.00 58.97  ? 113 PRO   B O   1 
ATOM   1208 C CB  . PRO   B 2 104 ? -11.627 -10.766 -22.624 1.00 53.60  ? 113 PRO   B CB  1 
ATOM   1209 C CG  . PRO   B 2 104 ? -12.917 -10.504 -23.337 1.00 53.40  ? 113 PRO   B CG  1 
ATOM   1210 C CD  . PRO   B 2 104 ? -12.680 -11.027 -24.753 1.00 54.75  ? 113 PRO   B CD  1 
ATOM   1211 N N   . GLY   B 2 105 ? -8.298  -10.756 -22.935 1.00 54.83  ? 114 GLY   B N   1 
ATOM   1212 C CA  . GLY   B 2 105 ? -7.203  -11.446 -22.239 1.00 55.91  ? 114 GLY   B CA  1 
ATOM   1213 C C   . GLY   B 2 105 ? -7.638  -11.817 -20.824 1.00 55.57  ? 114 GLY   B C   1 
ATOM   1214 O O   . GLY   B 2 105 ? -8.859  -11.843 -20.578 1.00 53.11  ? 114 GLY   B O   1 
ATOM   1215 N N   . ILE   B 2 106 ? -6.665  -12.067 -19.948 1.00 56.79  ? 115 ILE   B N   1 
ATOM   1216 C CA  . ILE   B 2 106 ? -6.839  -12.658 -18.585 1.00 57.08  ? 115 ILE   B CA  1 
ATOM   1217 C C   . ILE   B 2 106 ? -5.993  -11.869 -17.582 1.00 57.36  ? 115 ILE   B C   1 
ATOM   1218 O O   . ILE   B 2 106 ? -4.790  -11.721 -17.803 1.00 59.12  ? 115 ILE   B O   1 
ATOM   1219 C CB  . ILE   B 2 106 ? -6.415  -14.139 -18.566 1.00 58.18  ? 115 ILE   B CB  1 
ATOM   1220 C CG1 . ILE   B 2 106 ? -7.251  -15.010 -19.497 1.00 60.23  ? 115 ILE   B CG1 1 
ATOM   1221 C CG2 . ILE   B 2 106 ? -6.445  -14.684 -17.153 1.00 59.84  ? 115 ILE   B CG2 1 
ATOM   1222 C CD1 . ILE   B 2 106 ? -8.630  -15.306 -19.011 1.00 59.55  ? 115 ILE   B CD1 1 
ATOM   1223 N N   . PHE   B 2 107 ? -6.596  -11.473 -16.461 1.00 57.70  ? 116 PHE   B N   1 
ATOM   1224 C CA  . PHE   B 2 107 ? -5.889  -11.144 -15.200 1.00 56.30  ? 116 PHE   B CA  1 
ATOM   1225 C C   . PHE   B 2 107 ? -5.792  -12.427 -14.363 1.00 57.84  ? 116 PHE   B C   1 
ATOM   1226 O O   . PHE   B 2 107 ? -6.856  -12.922 -13.891 1.00 58.91  ? 116 PHE   B O   1 
ATOM   1227 C CB  . PHE   B 2 107 ? -6.665  -10.061 -14.462 1.00 55.24  ? 116 PHE   B CB  1 
ATOM   1228 C CG  . PHE   B 2 107 ? -6.347  -8.650  -14.859 1.00 54.30  ? 116 PHE   B CG  1 
ATOM   1229 C CD1 . PHE   B 2 107 ? -5.583  -8.369  -15.979 1.00 54.31  ? 116 PHE   B CD1 1 
ATOM   1230 C CD2 . PHE   B 2 107 ? -6.853  -7.604  -14.111 1.00 53.47  ? 116 PHE   B CD2 1 
ATOM   1231 C CE1 . PHE   B 2 107 ? -5.297  -7.062  -16.316 1.00 54.17  ? 116 PHE   B CE1 1 
ATOM   1232 C CE2 . PHE   B 2 107 ? -6.583  -6.297  -14.464 1.00 53.63  ? 116 PHE   B CE2 1 
ATOM   1233 C CZ  . PHE   B 2 107 ? -5.791  -6.030  -15.548 1.00 53.99  ? 116 PHE   B CZ  1 
ATOM   1234 N N   . LYS   B 2 108 ? -4.580  -12.975 -14.226 1.00 60.27  ? 117 LYS   B N   1 
ATOM   1235 C CA  . LYS   B 2 108 ? -4.272  -14.133 -13.338 1.00 62.27  ? 117 LYS   B CA  1 
ATOM   1236 C C   . LYS   B 2 108 ? -3.940  -13.566 -11.950 1.00 60.62  ? 117 LYS   B C   1 
ATOM   1237 O O   . LYS   B 2 108 ? -2.908  -12.852 -11.831 1.00 58.11  ? 117 LYS   B O   1 
ATOM   1238 C CB  . LYS   B 2 108 ? -3.119  -14.993 -13.882 1.00 66.64  ? 117 LYS   B CB  1 
ATOM   1239 C CG  . LYS   B 2 108 ? -3.517  -16.368 -14.417 1.00 71.93  ? 117 LYS   B CG  1 
ATOM   1240 C CD  . LYS   B 2 108 ? -2.551  -16.946 -15.459 1.00 77.21  ? 117 LYS   B CD  1 
ATOM   1241 C CE  . LYS   B 2 108 ? -3.110  -18.150 -16.208 1.00 82.42  ? 117 LYS   B CE  1 
ATOM   1242 N NZ  . LYS   B 2 108 ? -2.400  -18.444 -17.489 1.00 85.71  ? 117 LYS   B NZ  1 
ATOM   1243 N N   . THR   B 2 109 ? -4.805  -13.836 -10.963 1.00 59.80  ? 118 THR   B N   1 
ATOM   1244 C CA  . THR   B 2 109 ? -4.633  -13.411 -9.542  1.00 60.59  ? 118 THR   B CA  1 
ATOM   1245 C C   . THR   B 2 109 ? -4.632  -14.637 -8.629  1.00 61.01  ? 118 THR   B C   1 
ATOM   1246 O O   . THR   B 2 109 ? -5.204  -15.678 -9.006  1.00 58.82  ? 118 THR   B O   1 
ATOM   1247 C CB  . THR   B 2 109 ? -5.727  -12.440 -9.074  1.00 60.23  ? 118 THR   B CB  1 
ATOM   1248 O OG1 . THR   B 2 109 ? -6.874  -13.154 -8.591  1.00 59.16  ? 118 THR   B OG1 1 
ATOM   1249 C CG2 . THR   B 2 109 ? -6.119  -11.450 -10.150 1.00 59.95  ? 118 THR   B CG2 1 
ATOM   1250 N N   . LYS   B 2 110 ? -4.069  -14.486 -7.429  1.00 65.50  ? 119 LYS   B N   1 
ATOM   1251 C CA  . LYS   B 2 110 ? -4.015  -15.554 -6.388  1.00 68.02  ? 119 LYS   B CA  1 
ATOM   1252 C C   . LYS   B 2 110 ? -5.441  -16.040 -6.047  1.00 69.11  ? 119 LYS   B C   1 
ATOM   1253 O O   . LYS   B 2 110 ? -5.563  -17.229 -5.657  1.00 72.47  ? 119 LYS   B O   1 
ATOM   1254 C CB  . LYS   B 2 110 ? -3.236  -15.047 -5.171  1.00 68.43  ? 119 LYS   B CB  1 
ATOM   1255 C CG  . LYS   B 2 110 ? -4.002  -14.130 -4.226  1.00 71.82  ? 119 LYS   B CG  1 
ATOM   1256 C CD  . LYS   B 2 110 ? -3.093  -13.454 -3.182  1.00 74.46  ? 119 LYS   B CD  1 
ATOM   1257 C CE  . LYS   B 2 110 ? -3.754  -13.166 -1.850  1.00 76.04  ? 119 LYS   B CE  1 
ATOM   1258 N NZ  . LYS   B 2 110 ? -4.919  -12.262 -2.006  1.00 77.45  ? 119 LYS   B NZ  1 
ATOM   1259 N N   . ASP   B 2 111 ? -6.475  -15.197 -6.216  1.00 67.42  ? 120 ASP   B N   1 
ATOM   1260 C CA  . ASP   B 2 111 ? -7.901  -15.521 -5.922  1.00 67.30  ? 120 ASP   B CA  1 
ATOM   1261 C C   . ASP   B 2 111 ? -8.659  -16.069 -7.138  1.00 67.23  ? 120 ASP   B C   1 
ATOM   1262 O O   . ASP   B 2 111 ? -9.820  -16.470 -6.941  1.00 69.78  ? 120 ASP   B O   1 
ATOM   1263 C CB  . ASP   B 2 111 ? -8.674  -14.287 -5.453  1.00 67.45  ? 120 ASP   B CB  1 
ATOM   1264 C CG  . ASP   B 2 111 ? -8.388  -13.906 -4.019  1.00 68.56  ? 120 ASP   B CG  1 
ATOM   1265 O OD1 . ASP   B 2 111 ? -7.401  -14.436 -3.461  1.00 65.49  ? 120 ASP   B OD1 1 
ATOM   1266 O OD2 . ASP   B 2 111 ? -9.166  -13.088 -3.473  1.00 71.51  ? 120 ASP   B OD2 1 
ATOM   1267 N N   . GLY   B 2 112 ? -8.092  -16.039 -8.345  1.00 66.35  ? 121 GLY   B N   1 
ATOM   1268 C CA  . GLY   B 2 112 ? -8.841  -16.427 -9.555  1.00 65.74  ? 121 GLY   B CA  1 
ATOM   1269 C C   . GLY   B 2 112 ? -8.434  -15.656 -10.794 1.00 65.00  ? 121 GLY   B C   1 
ATOM   1270 O O   . GLY   B 2 112 ? -7.723  -14.641 -10.669 1.00 63.21  ? 121 GLY   B O   1 
ATOM   1271 N N   . ASP   B 2 113 ? -8.862  -16.165 -11.955 1.00 65.24  ? 122 ASP   B N   1 
ATOM   1272 C CA  . ASP   B 2 113 ? -8.707  -15.530 -13.291 1.00 64.39  ? 122 ASP   B CA  1 
ATOM   1273 C C   . ASP   B 2 113 ? -9.875  -14.563 -13.520 1.00 62.63  ? 122 ASP   B C   1 
ATOM   1274 O O   . ASP   B 2 113 ? -11.032 -14.899 -13.123 1.00 59.37  ? 122 ASP   B O   1 
ATOM   1275 C CB  . ASP   B 2 113 ? -8.685  -16.571 -14.406 1.00 64.80  ? 122 ASP   B CB  1 
ATOM   1276 C CG  . ASP   B 2 113 ? -7.445  -17.445 -14.448 1.00 67.79  ? 122 ASP   B CG  1 
ATOM   1277 O OD1 . ASP   B 2 113 ? -6.599  -17.325 -13.541 1.00 68.22  ? 122 ASP   B OD1 1 
ATOM   1278 O OD2 . ASP   B 2 113 ? -7.353  -18.256 -15.406 1.00 71.32  ? 122 ASP   B OD2 1 
ATOM   1279 N N   . ILE   B 2 114 ? -9.579  -13.409 -14.129 1.00 61.08  ? 123 ILE   B N   1 
ATOM   1280 C CA  . ILE   B 2 114 ? -10.574 -12.364 -14.505 1.00 59.07  ? 123 ILE   B CA  1 
ATOM   1281 C C   . ILE   B 2 114 ? -10.335 -12.052 -15.983 1.00 55.99  ? 123 ILE   B C   1 
ATOM   1282 O O   . ILE   B 2 114 ? -9.174  -11.852 -16.355 1.00 53.14  ? 123 ILE   B O   1 
ATOM   1283 C CB  . ILE   B 2 114 ? -10.431 -11.075 -13.666 1.00 59.45  ? 123 ILE   B CB  1 
ATOM   1284 C CG1 . ILE   B 2 114 ? -9.725  -11.317 -12.336 1.00 63.62  ? 123 ILE   B CG1 1 
ATOM   1285 C CG2 . ILE   B 2 114 ? -11.779 -10.394 -13.476 1.00 58.70  ? 123 ILE   B CG2 1 
ATOM   1286 C CD1 . ILE   B 2 114 ? -9.321  -10.040 -11.591 1.00 65.19  ? 123 ILE   B CD1 1 
ATOM   1287 N N   . GLY   B 2 115 ? -11.397 -11.913 -16.762 1.00 55.01  ? 124 GLY   B N   1 
ATOM   1288 C CA  . GLY   B 2 115 ? -11.285 -11.279 -18.085 1.00 53.87  ? 124 GLY   B CA  1 
ATOM   1289 C C   . GLY   B 2 115 ? -10.638 -9.907  -17.962 1.00 53.64  ? 124 GLY   B C   1 
ATOM   1290 O O   . GLY   B 2 115 ? -10.814 -9.223  -16.930 1.00 51.51  ? 124 GLY   B O   1 
ATOM   1291 N N   . ALA   B 2 116 ? -9.892  -9.524  -18.996 1.00 54.43  ? 125 ALA   B N   1 
ATOM   1292 C CA  . ALA   B 2 116 ? -9.259  -8.197  -19.153 1.00 54.53  ? 125 ALA   B CA  1 
ATOM   1293 C C   . ALA   B 2 116 ? -9.445  -7.766  -20.616 1.00 54.08  ? 125 ALA   B C   1 
ATOM   1294 O O   . ALA   B 2 116 ? -9.390  -8.615  -21.485 1.00 54.76  ? 125 ALA   B O   1 
ATOM   1295 C CB  . ALA   B 2 116 ? -7.799  -8.282  -18.767 1.00 55.12  ? 125 ALA   B CB  1 
ATOM   1296 N N   A VAL   B 2 117 ? -9.685  -6.473  -20.857 0.25 53.85  ? 126 VAL   B N   1 
ATOM   1297 N N   B VAL   B 2 117 ? -9.638  -6.465  -20.848 0.25 54.16  ? 126 VAL   B N   1 
ATOM   1298 N N   C VAL   B 2 117 ? -9.685  -6.473  -20.857 0.25 53.85  ? 126 VAL   B N   1 
ATOM   1299 N N   D VAL   B 2 117 ? -9.638  -6.465  -20.848 0.25 54.16  ? 126 VAL   B N   1 
ATOM   1300 C CA  A VAL   B 2 117 ? -9.823  -5.886  -22.226 0.25 54.80  ? 126 VAL   B CA  1 
ATOM   1301 C CA  B VAL   B 2 117 ? -9.831  -5.862  -22.200 0.25 55.28  ? 126 VAL   B CA  1 
ATOM   1302 C CA  C VAL   B 2 117 ? -9.823  -5.886  -22.226 0.25 54.80  ? 126 VAL   B CA  1 
ATOM   1303 C CA  D VAL   B 2 117 ? -9.831  -5.862  -22.200 0.25 55.28  ? 126 VAL   B CA  1 
ATOM   1304 C C   A VAL   B 2 117 ? -8.688  -4.878  -22.441 0.25 55.17  ? 126 VAL   B C   1 
ATOM   1305 C C   B VAL   B 2 117 ? -8.700  -4.855  -22.452 0.25 55.46  ? 126 VAL   B C   1 
ATOM   1306 C C   C VAL   B 2 117 ? -8.688  -4.878  -22.441 0.25 55.17  ? 126 VAL   B C   1 
ATOM   1307 C C   D VAL   B 2 117 ? -8.700  -4.855  -22.452 0.25 55.46  ? 126 VAL   B C   1 
ATOM   1308 O O   A VAL   B 2 117 ? -8.553  -3.949  -21.620 0.25 54.64  ? 126 VAL   B O   1 
ATOM   1309 O O   B VAL   B 2 117 ? -8.576  -3.899  -21.661 0.25 54.96  ? 126 VAL   B O   1 
ATOM   1310 O O   C VAL   B 2 117 ? -8.553  -3.949  -21.620 0.25 54.64  ? 126 VAL   B O   1 
ATOM   1311 O O   D VAL   B 2 117 ? -8.576  -3.899  -21.661 0.25 54.96  ? 126 VAL   B O   1 
ATOM   1312 C CB  A VAL   B 2 117 ? -11.208 -5.250  -22.442 0.25 54.41  ? 126 VAL   B CB  1 
ATOM   1313 C CB  B VAL   B 2 117 ? -11.228 -5.227  -22.318 0.25 55.26  ? 126 VAL   B CB  1 
ATOM   1314 C CB  C VAL   B 2 117 ? -11.208 -5.250  -22.442 0.25 54.41  ? 126 VAL   B CB  1 
ATOM   1315 C CB  D VAL   B 2 117 ? -11.228 -5.227  -22.318 0.25 55.26  ? 126 VAL   B CB  1 
ATOM   1316 C CG1 A VAL   B 2 117 ? -12.317 -6.168  -21.952 0.25 54.22  ? 126 VAL   B CG1 1 
ATOM   1317 C CG1 B VAL   B 2 117 ? -11.257 -4.093  -23.324 0.25 55.48  ? 126 VAL   B CG1 1 
ATOM   1318 C CG1 C VAL   B 2 117 ? -12.317 -6.168  -21.952 0.25 54.22  ? 126 VAL   B CG1 1 
ATOM   1319 C CG1 D VAL   B 2 117 ? -11.257 -4.093  -23.324 0.25 55.48  ? 126 VAL   B CG1 1 
ATOM   1320 C CG2 A VAL   B 2 117 ? -11.316 -3.878  -21.798 0.25 53.71  ? 126 VAL   B CG2 1 
ATOM   1321 C CG2 B VAL   B 2 117 ? -12.281 -6.274  -22.654 0.25 55.48  ? 126 VAL   B CG2 1 
ATOM   1322 C CG2 C VAL   B 2 117 ? -11.316 -3.878  -21.798 0.25 53.71  ? 126 VAL   B CG2 1 
ATOM   1323 C CG2 D VAL   B 2 117 ? -12.281 -6.274  -22.654 0.25 55.48  ? 126 VAL   B CG2 1 
ATOM   1324 N N   . ALA   B 2 118 ? -7.878  -5.097  -23.482 1.00 55.96  ? 127 ALA   B N   1 
ATOM   1325 C CA  . ALA   B 2 118 ? -6.723  -4.227  -23.832 1.00 57.17  ? 127 ALA   B CA  1 
ATOM   1326 C C   . ALA   B 2 118 ? -7.213  -3.144  -24.795 1.00 58.97  ? 127 ALA   B C   1 
ATOM   1327 O O   . ALA   B 2 118 ? -7.059  -3.319  -26.012 1.00 58.76  ? 127 ALA   B O   1 
ATOM   1328 C CB  . ALA   B 2 118 ? -5.587  -5.030  -24.423 1.00 56.50  ? 127 ALA   B CB  1 
ATOM   1329 N N   . LEU   B 2 119 ? -7.901  -2.131  -24.263 1.00 58.19  ? 128 LEU   B N   1 
ATOM   1330 C CA  . LEU   B 2 119 ? -8.354  -0.965  -25.046 1.00 57.57  ? 128 LEU   B CA  1 
ATOM   1331 C C   . LEU   B 2 119 ? -8.018  0.261   -24.216 1.00 59.27  ? 128 LEU   B C   1 
ATOM   1332 O O   . LEU   B 2 119 ? -8.246  0.238   -22.995 1.00 60.97  ? 128 LEU   B O   1 
ATOM   1333 C CB  . LEU   B 2 119 ? -9.847  -1.106  -25.325 1.00 56.27  ? 128 LEU   B CB  1 
ATOM   1334 C CG  . LEU   B 2 119 ? -10.232 -2.295  -26.195 1.00 55.40  ? 128 LEU   B CG  1 
ATOM   1335 C CD1 . LEU   B 2 119 ? -11.730 -2.508  -26.185 1.00 54.11  ? 128 LEU   B CD1 1 
ATOM   1336 C CD2 . LEU   B 2 119 ? -9.731  -2.084  -27.632 1.00 57.09  ? 128 LEU   B CD2 1 
ATOM   1337 N N   . ASP   B 2 120 ? -7.414  1.244   -24.848 1.00 60.56  ? 129 ASP   B N   1 
ATOM   1338 C CA  . ASP   B 2 120 ? -6.905  2.465   -24.195 1.00 62.49  ? 129 ASP   B CA  1 
ATOM   1339 C C   . ASP   B 2 120 ? -7.900  3.597   -24.442 1.00 61.75  ? 129 ASP   B C   1 
ATOM   1340 O O   . ASP   B 2 120 ? -8.190  3.852   -25.588 1.00 62.99  ? 129 ASP   B O   1 
ATOM   1341 C CB  . ASP   B 2 120 ? -5.555  2.822   -24.791 1.00 65.65  ? 129 ASP   B CB  1 
ATOM   1342 C CG  . ASP   B 2 120 ? -4.531  3.159   -23.741 1.00 70.57  ? 129 ASP   B CG  1 
ATOM   1343 O OD1 . ASP   B 2 120 ? -4.854  3.981   -22.824 1.00 72.56  ? 129 ASP   B OD1 1 
ATOM   1344 O OD2 . ASP   B 2 120 ? -3.435  2.565   -23.834 1.00 76.15  ? 129 ASP   B OD2 1 
ATOM   1345 N N   . TYR   B 2 121 ? -8.358  4.278   -23.409 1.00 59.37  ? 130 TYR   B N   1 
ATOM   1346 C CA  . TYR   B 2 121 ? -9.300  5.412   -23.503 1.00 59.90  ? 130 TYR   B CA  1 
ATOM   1347 C C   . TYR   B 2 121 ? -9.010  6.385   -22.371 1.00 59.22  ? 130 TYR   B C   1 
ATOM   1348 O O   . TYR   B 2 121 ? -8.353  6.020   -21.399 1.00 60.31  ? 130 TYR   B O   1 
ATOM   1349 C CB  . TYR   B 2 121 ? -10.735 4.897   -23.459 1.00 61.27  ? 130 TYR   B CB  1 
ATOM   1350 C CG  . TYR   B 2 121 ? -11.224 4.297   -24.754 1.00 63.40  ? 130 TYR   B CG  1 
ATOM   1351 C CD1 . TYR   B 2 121 ? -11.680 5.111   -25.783 1.00 65.27  ? 130 TYR   B CD1 1 
ATOM   1352 C CD2 . TYR   B 2 121 ? -11.246 2.925   -24.952 1.00 65.02  ? 130 TYR   B CD2 1 
ATOM   1353 C CE1 . TYR   B 2 121 ? -12.135 4.574   -26.977 1.00 67.13  ? 130 TYR   B CE1 1 
ATOM   1354 C CE2 . TYR   B 2 121 ? -11.707 2.370   -26.138 1.00 67.09  ? 130 TYR   B CE2 1 
ATOM   1355 C CZ  . TYR   B 2 121 ? -12.150 3.200   -27.158 1.00 68.21  ? 130 TYR   B CZ  1 
ATOM   1356 O OH  . TYR   B 2 121 ? -12.598 2.678   -28.335 1.00 72.43  ? 130 TYR   B OH  1 
ATOM   1357 N N   . PRO   B 2 122 ? -9.486  7.644   -22.435 1.00 57.97  ? 131 PRO   B N   1 
ATOM   1358 C CA  . PRO   B 2 122 ? -9.232  8.587   -21.358 1.00 59.15  ? 131 PRO   B CA  1 
ATOM   1359 C C   . PRO   B 2 122 ? -9.907  8.053   -20.082 1.00 56.59  ? 131 PRO   B C   1 
ATOM   1360 O O   . PRO   B 2 122 ? -10.871 7.292   -20.169 1.00 55.06  ? 131 PRO   B O   1 
ATOM   1361 C CB  . PRO   B 2 122 ? -9.812  9.906   -21.887 1.00 59.38  ? 131 PRO   B CB  1 
ATOM   1362 C CG  . PRO   B 2 122 ? -9.920  9.692   -23.367 1.00 60.37  ? 131 PRO   B CG  1 
ATOM   1363 C CD  . PRO   B 2 122 ? -10.312 8.233   -23.488 1.00 59.83  ? 131 PRO   B CD  1 
ATOM   1364 N N   . ALA   B 2 123 ? -9.353  8.417   -18.937 1.00 55.99  ? 132 ALA   B N   1 
ATOM   1365 C CA  . ALA   B 2 123 ? -9.858  8.008   -17.602 1.00 54.87  ? 132 ALA   B CA  1 
ATOM   1366 C C   . ALA   B 2 123 ? -11.357 8.296   -17.453 1.00 52.61  ? 132 ALA   B C   1 
ATOM   1367 O O   . ALA   B 2 123 ? -12.039 7.475   -16.798 1.00 52.59  ? 132 ALA   B O   1 
ATOM   1368 C CB  . ALA   B 2 123 ? -9.043  8.669   -16.533 1.00 55.08  ? 132 ALA   B CB  1 
ATOM   1369 N N   . GLY   B 2 124 ? -11.874 9.338   -18.116 1.00 50.57  ? 133 GLY   B N   1 
ATOM   1370 C CA  . GLY   B 2 124 ? -13.307 9.704   -18.093 1.00 48.21  ? 133 GLY   B CA  1 
ATOM   1371 C C   . GLY   B 2 124 ? -14.212 8.631   -18.708 1.00 46.58  ? 133 GLY   B C   1 
ATOM   1372 O O   . GLY   B 2 124 ? -15.454 8.762   -18.590 1.00 45.64  ? 133 GLY   B O   1 
ATOM   1373 N N   . THR   B 2 125 ? -13.638 7.602   -19.342 1.00 45.50  ? 134 THR   B N   1 
ATOM   1374 C CA  . THR   B 2 125 ? -14.400 6.467   -19.925 1.00 45.67  ? 134 THR   B CA  1 
ATOM   1375 C C   . THR   B 2 125 ? -14.684 5.387   -18.860 1.00 45.35  ? 134 THR   B C   1 
ATOM   1376 O O   . THR   B 2 125 ? -15.500 4.473   -19.166 1.00 45.44  ? 134 THR   B O   1 
ATOM   1377 C CB  . THR   B 2 125 ? -13.660 5.901   -21.149 1.00 47.11  ? 134 THR   B CB  1 
ATOM   1378 O OG1 . THR   B 2 125 ? -13.134 6.991   -21.911 1.00 48.21  ? 134 THR   B OG1 1 
ATOM   1379 C CG2 . THR   B 2 125 ? -14.555 5.128   -22.089 1.00 46.86  ? 134 THR   B CG2 1 
ATOM   1380 N N   . SER   B 2 126 ? -14.045 5.449   -17.679 1.00 44.47  ? 135 SER   B N   1 
ATOM   1381 C CA  . SER   B 2 126 ? -14.254 4.467   -16.572 1.00 43.70  ? 135 SER   B CA  1 
ATOM   1382 C C   . SER   B 2 126 ? -15.769 4.265   -16.353 1.00 42.07  ? 135 SER   B C   1 
ATOM   1383 O O   . SER   B 2 126 ? -16.490 5.289   -16.235 1.00 43.07  ? 135 SER   B O   1 
ATOM   1384 C CB  . SER   B 2 126 ? -13.575 4.911   -15.325 1.00 44.00  ? 135 SER   B CB  1 
ATOM   1385 O OG  . SER   B 2 126 ? -12.163 4.761   -15.399 1.00 45.17  ? 135 SER   B OG  1 
ATOM   1386 N N   . GLY   B 2 127 ? -16.243 3.019   -16.371 1.00 40.92  ? 136 GLY   B N   1 
ATOM   1387 C CA  . GLY   B 2 127 ? -17.653 2.667   -16.077 1.00 40.45  ? 136 GLY   B CA  1 
ATOM   1388 C C   . GLY   B 2 127 ? -18.409 2.238   -17.308 1.00 41.41  ? 136 GLY   B C   1 
ATOM   1389 O O   . GLY   B 2 127 ? -19.554 1.709   -17.144 1.00 42.07  ? 136 GLY   B O   1 
ATOM   1390 N N   . SER   B 2 128 ? -17.786 2.386   -18.502 1.00 40.70  ? 137 SER   B N   1 
ATOM   1391 C CA  . SER   B 2 128 ? -18.382 1.964   -19.785 1.00 40.41  ? 137 SER   B CA  1 
ATOM   1392 C C   . SER   B 2 128 ? -18.648 0.472   -19.707 1.00 39.43  ? 137 SER   B C   1 
ATOM   1393 O O   . SER   B 2 128 ? -17.758 -0.284  -19.332 1.00 39.62  ? 137 SER   B O   1 
ATOM   1394 C CB  . SER   B 2 128 ? -17.478 2.339   -20.945 1.00 41.42  ? 137 SER   B CB  1 
ATOM   1395 O OG  . SER   B 2 128 ? -17.371 3.761   -21.073 1.00 42.31  ? 137 SER   B OG  1 
ATOM   1396 N N   . PRO   B 2 129 ? -19.848 -0.010  -20.085 1.00 38.64  ? 138 PRO   B N   1 
ATOM   1397 C CA  . PRO   B 2 129 ? -20.134 -1.426  -19.996 1.00 39.02  ? 138 PRO   B CA  1 
ATOM   1398 C C   . PRO   B 2 129 ? -19.470 -2.275  -21.075 1.00 40.59  ? 138 PRO   B C   1 
ATOM   1399 O O   . PRO   B 2 129 ? -19.218 -1.796  -22.217 1.00 41.15  ? 138 PRO   B O   1 
ATOM   1400 C CB  . PRO   B 2 129 ? -21.652 -1.518  -20.130 1.00 38.64  ? 138 PRO   B CB  1 
ATOM   1401 C CG  . PRO   B 2 129 ? -22.063 -0.253  -20.873 1.00 38.44  ? 138 PRO   B CG  1 
ATOM   1402 C CD  . PRO   B 2 129 ? -20.991 0.770   -20.582 1.00 38.32  ? 138 PRO   B CD  1 
ATOM   1403 N N   . ILE   B 2 130 ? -19.276 -3.530  -20.717 1.00 41.38  ? 139 ILE   B N   1 
ATOM   1404 C CA  . ILE   B 2 130 ? -18.757 -4.611  -21.574 1.00 43.50  ? 139 ILE   B CA  1 
ATOM   1405 C C   . ILE   B 2 130 ? -19.923 -5.579  -21.743 1.00 45.70  ? 139 ILE   B C   1 
ATOM   1406 O O   . ILE   B 2 130 ? -20.624 -5.771  -20.762 1.00 43.88  ? 139 ILE   B O   1 
ATOM   1407 C CB  . ILE   B 2 130 ? -17.517 -5.242  -20.962 1.00 43.38  ? 139 ILE   B CB  1 
ATOM   1408 C CG1 . ILE   B 2 130 ? -16.374 -4.233  -20.890 1.00 43.60  ? 139 ILE   B CG1 1 
ATOM   1409 C CG2 . ILE   B 2 130 ? -17.119 -6.499  -21.721 1.00 43.89  ? 139 ILE   B CG2 1 
ATOM   1410 C CD1 . ILE   B 2 130 ? -15.488 -4.468  -19.696 1.00 44.17  ? 139 ILE   B CD1 1 
ATOM   1411 N N   . LEU   B 2 131 ? -20.192 -6.000  -22.993 1.00 48.47  ? 140 LEU   B N   1 
ATOM   1412 C CA  . LEU   B 2 131 ? -21.421 -6.735  -23.392 1.00 51.24  ? 140 LEU   B CA  1 
ATOM   1413 C C   . LEU   B 2 131 ? -21.060 -8.073  -24.028 1.00 52.16  ? 140 LEU   B C   1 
ATOM   1414 O O   . LEU   B 2 131 ? -20.029 -8.134  -24.702 1.00 53.04  ? 140 LEU   B O   1 
ATOM   1415 C CB  . LEU   B 2 131 ? -22.205 -5.930  -24.433 1.00 52.94  ? 140 LEU   B CB  1 
ATOM   1416 C CG  . LEU   B 2 131 ? -22.196 -4.422  -24.255 1.00 53.86  ? 140 LEU   B CG  1 
ATOM   1417 C CD1 . LEU   B 2 131 ? -22.834 -3.757  -25.467 1.00 54.27  ? 140 LEU   B CD1 1 
ATOM   1418 C CD2 . LEU   B 2 131 ? -22.919 -4.044  -22.966 1.00 54.24  ? 140 LEU   B CD2 1 
ATOM   1419 N N   . ASP   B 2 132 ? -21.955 -9.056  -23.872 1.00 53.01  ? 141 ASP   B N   1 
ATOM   1420 C CA  . ASP   B 2 132 ? -21.917 -10.362 -24.571 1.00 54.12  ? 141 ASP   B CA  1 
ATOM   1421 C C   . ASP   B 2 132 ? -22.834 -10.320 -25.815 1.00 56.87  ? 141 ASP   B C   1 
ATOM   1422 O O   . ASP   B 2 132 ? -23.557 -9.304  -26.044 1.00 54.73  ? 141 ASP   B O   1 
ATOM   1423 C CB  . ASP   B 2 132 ? -22.310 -11.509 -23.655 1.00 52.45  ? 141 ASP   B CB  1 
ATOM   1424 C CG  . ASP   B 2 132 ? -23.784 -11.580 -23.315 1.00 52.82  ? 141 ASP   B CG  1 
ATOM   1425 O OD1 . ASP   B 2 132 ? -24.575 -10.667 -23.725 1.00 51.06  ? 141 ASP   B OD1 1 
ATOM   1426 O OD2 . ASP   B 2 132 ? -24.122 -12.544 -22.574 1.00 54.84  ? 141 ASP   B OD2 1 
ATOM   1427 N N   . LYS   B 2 133 ? -22.812 -11.410 -26.587 1.00 60.94  ? 142 LYS   B N   1 
ATOM   1428 C CA  . LYS   B 2 133 ? -23.427 -11.482 -27.946 1.00 64.30  ? 142 LYS   B CA  1 
ATOM   1429 C C   . LYS   B 2 133 ? -24.929 -11.217 -27.795 1.00 63.04  ? 142 LYS   B C   1 
ATOM   1430 O O   . LYS   B 2 133 ? -25.498 -10.640 -28.712 1.00 60.69  ? 142 LYS   B O   1 
ATOM   1431 C CB  . LYS   B 2 133 ? -23.048 -12.805 -28.631 1.00 68.53  ? 142 LYS   B CB  1 
ATOM   1432 C CG  . LYS   B 2 133 ? -21.688 -12.775 -29.341 1.00 72.61  ? 142 LYS   B CG  1 
ATOM   1433 C CD  . LYS   B 2 133 ? -21.004 -14.139 -29.629 1.00 76.29  ? 142 LYS   B CD  1 
ATOM   1434 C CE  . LYS   B 2 133 ? -19.534 -14.004 -30.022 1.00 77.58  ? 142 LYS   B CE  1 
ATOM   1435 N NZ  . LYS   B 2 133 ? -18.910 -15.269 -30.507 1.00 78.17  ? 142 LYS   B NZ  1 
ATOM   1436 N N   . CYS   B 2 134 ? -25.512 -11.489 -26.618 1.00 61.88  ? 143 CYS   B N   1 
ATOM   1437 C CA  . CYS   B 2 134 ? -26.956 -11.258 -26.363 1.00 60.15  ? 143 CYS   B CA  1 
ATOM   1438 C C   . CYS   B 2 134 ? -27.228 -9.827  -25.864 1.00 57.59  ? 143 CYS   B C   1 
ATOM   1439 O O   . CYS   B 2 134 ? -28.393 -9.559  -25.506 1.00 58.30  ? 143 CYS   B O   1 
ATOM   1440 C CB  . CYS   B 2 134 ? -27.467 -12.258 -25.344 1.00 61.91  ? 143 CYS   B CB  1 
ATOM   1441 S SG  . CYS   B 2 134 ? -27.638 -13.933 -25.999 1.00 64.01  ? 143 CYS   B SG  1 
ATOM   1442 N N   . GLY   B 2 135 ? -26.239 -8.920  -25.878 1.00 56.06  ? 144 GLY   B N   1 
ATOM   1443 C CA  . GLY   B 2 135 ? -26.394 -7.547  -25.341 1.00 55.48  ? 144 GLY   B CA  1 
ATOM   1444 C C   . GLY   B 2 135 ? -26.466 -7.447  -23.797 1.00 53.95  ? 144 GLY   B C   1 
ATOM   1445 O O   . GLY   B 2 135 ? -26.915 -6.402  -23.281 1.00 52.56  ? 144 GLY   B O   1 
ATOM   1446 N N   . ARG   B 2 136 ? -26.031 -8.455  -23.046 1.00 54.28  ? 145 ARG   B N   1 
ATOM   1447 C CA  . ARG   B 2 136 ? -26.070 -8.424  -21.550 1.00 53.56  ? 145 ARG   B CA  1 
ATOM   1448 C C   . ARG   B 2 136 ? -24.776 -7.820  -20.992 1.00 50.70  ? 145 ARG   B C   1 
ATOM   1449 O O   . ARG   B 2 136 ? -23.709 -8.124  -21.562 1.00 49.06  ? 145 ARG   B O   1 
ATOM   1450 C CB  . ARG   B 2 136 ? -26.319 -9.831  -21.026 1.00 56.27  ? 145 ARG   B CB  1 
ATOM   1451 C CG  . ARG   B 2 136 ? -27.782 -10.222 -21.160 1.00 60.01  ? 145 ARG   B CG  1 
ATOM   1452 C CD  . ARG   B 2 136 ? -27.997 -11.636 -20.685 1.00 63.61  ? 145 ARG   B CD  1 
ATOM   1453 N NE  . ARG   B 2 136 ? -27.122 -12.495 -21.461 1.00 68.23  ? 145 ARG   B NE  1 
ATOM   1454 C CZ  . ARG   B 2 136 ? -26.681 -13.697 -21.113 1.00 73.76  ? 145 ARG   B CZ  1 
ATOM   1455 N NH1 . ARG   B 2 136 ? -26.983 -14.231 -19.934 1.00 79.86  ? 145 ARG   B NH1 1 
ATOM   1456 N NH2 . ARG   B 2 136 ? -25.906 -14.359 -21.959 1.00 77.50  ? 145 ARG   B NH2 1 
ATOM   1457 N N   . VAL   B 2 137 ? -24.843 -7.021  -19.903 1.00 48.43  ? 146 VAL   B N   1 
ATOM   1458 C CA  . VAL   B 2 137 ? -23.609 -6.402  -19.335 1.00 46.29  ? 146 VAL   B CA  1 
ATOM   1459 C C   . VAL   B 2 137 ? -22.925 -7.467  -18.473 1.00 46.43  ? 146 VAL   B C   1 
ATOM   1460 O O   . VAL   B 2 137 ? -23.538 -7.969  -17.503 1.00 46.54  ? 146 VAL   B O   1 
ATOM   1461 C CB  . VAL   B 2 137 ? -23.851 -5.090  -18.578 1.00 45.50  ? 146 VAL   B CB  1 
ATOM   1462 C CG1 . VAL   B 2 137 ? -22.545 -4.450  -18.142 1.00 45.27  ? 146 VAL   B CG1 1 
ATOM   1463 C CG2 . VAL   B 2 137 ? -24.654 -4.091  -19.380 1.00 46.05  ? 146 VAL   B CG2 1 
ATOM   1464 N N   . ILE   B 2 138 ? -21.691 -7.803  -18.823 1.00 45.52  ? 147 ILE   B N   1 
ATOM   1465 C CA  . ILE   B 2 138 ? -20.867 -8.837  -18.139 1.00 44.98  ? 147 ILE   B CA  1 
ATOM   1466 C C   . ILE   B 2 138 ? -19.809 -8.150  -17.263 1.00 44.10  ? 147 ILE   B C   1 
ATOM   1467 O O   . ILE   B 2 138 ? -19.007 -8.879  -16.604 1.00 43.10  ? 147 ILE   B O   1 
ATOM   1468 C CB  . ILE   B 2 138 ? -20.190 -9.754  -19.177 1.00 45.74  ? 147 ILE   B CB  1 
ATOM   1469 C CG1 . ILE   B 2 138 ? -19.417 -8.943  -20.220 1.00 45.69  ? 147 ILE   B CG1 1 
ATOM   1470 C CG2 . ILE   B 2 138 ? -21.205 -10.677 -19.817 1.00 46.38  ? 147 ILE   B CG2 1 
ATOM   1471 C CD1 . ILE   B 2 138 ? -18.370 -9.739  -20.979 1.00 47.03  ? 147 ILE   B CD1 1 
ATOM   1472 N N   . GLY   B 2 139 ? -19.745 -6.818  -17.286 1.00 43.27  ? 148 GLY   B N   1 
ATOM   1473 C CA  . GLY   B 2 139 ? -18.827 -6.098  -16.379 1.00 42.87  ? 148 GLY   B CA  1 
ATOM   1474 C C   . GLY   B 2 139 ? -18.632 -4.675  -16.804 1.00 42.51  ? 148 GLY   B C   1 
ATOM   1475 O O   . GLY   B 2 139 ? -19.256 -4.276  -17.852 1.00 42.72  ? 148 GLY   B O   1 
ATOM   1476 N N   . LEU   B 2 140 ? -17.790 -3.947  -16.080 1.00 42.05  ? 149 LEU   B N   1 
ATOM   1477 C CA  . LEU   B 2 140 ? -17.509 -2.527  -16.362 1.00 42.48  ? 149 LEU   B CA  1 
ATOM   1478 C C   . LEU   B 2 140 ? -16.013 -2.347  -16.528 1.00 42.67  ? 149 LEU   B C   1 
ATOM   1479 O O   . LEU   B 2 140 ? -15.227 -3.103  -15.909 1.00 41.51  ? 149 LEU   B O   1 
ATOM   1480 C CB  . LEU   B 2 140 ? -18.024 -1.587  -15.272 1.00 42.22  ? 149 LEU   B CB  1 
ATOM   1481 C CG  . LEU   B 2 140 ? -19.510 -1.601  -14.914 1.00 42.74  ? 149 LEU   B CG  1 
ATOM   1482 C CD1 . LEU   B 2 140 ? -19.764 -0.524  -13.855 1.00 43.12  ? 149 LEU   B CD1 1 
ATOM   1483 C CD2 . LEU   B 2 140 ? -20.454 -1.401  -16.079 1.00 43.34  ? 149 LEU   B CD2 1 
ATOM   1484 N N   . TYR   B 2 141 ? -15.686 -1.381  -17.397 1.00 43.10  ? 150 TYR   B N   1 
ATOM   1485 C CA  . TYR   B 2 141 ? -14.332 -1.080  -17.907 1.00 44.49  ? 150 TYR   B CA  1 
ATOM   1486 C C   . TYR   B 2 141 ? -13.758 0.101   -17.114 1.00 44.57  ? 150 TYR   B C   1 
ATOM   1487 O O   . TYR   B 2 141 ? -14.497 1.083   -16.878 1.00 45.85  ? 150 TYR   B O   1 
ATOM   1488 C CB  . TYR   B 2 141 ? -14.394 -0.691  -19.402 1.00 46.05  ? 150 TYR   B CB  1 
ATOM   1489 C CG  . TYR   B 2 141 ? -13.153 -0.028  -19.950 1.00 46.40  ? 150 TYR   B CG  1 
ATOM   1490 C CD1 . TYR   B 2 141 ? -12.981 1.343   -19.851 1.00 46.81  ? 150 TYR   B CD1 1 
ATOM   1491 C CD2 . TYR   B 2 141 ? -12.139 -0.776  -20.544 1.00 47.16  ? 150 TYR   B CD2 1 
ATOM   1492 C CE1 . TYR   B 2 141 ? -11.821 1.960   -20.321 1.00 48.62  ? 150 TYR   B CE1 1 
ATOM   1493 C CE2 . TYR   B 2 141 ? -10.996 -0.172  -21.051 1.00 48.43  ? 150 TYR   B CE2 1 
ATOM   1494 C CZ  . TYR   B 2 141 ? -10.846 1.211   -20.976 1.00 49.55  ? 150 TYR   B CZ  1 
ATOM   1495 O OH  . TYR   B 2 141 ? -9.715  1.832   -21.470 1.00 50.78  ? 150 TYR   B OH  1 
ATOM   1496 N N   . GLY   B 2 142 ? -12.481 0.036   -16.758 1.00 45.13  ? 151 GLY   B N   1 
ATOM   1497 C CA  . GLY   B 2 142 ? -11.845 1.236   -16.160 1.00 45.88  ? 151 GLY   B CA  1 
ATOM   1498 C C   . GLY   B 2 142 ? -11.106 0.998   -14.854 1.00 46.55  ? 151 GLY   B C   1 
ATOM   1499 O O   . GLY   B 2 142 ? -10.559 2.009   -14.320 1.00 46.37  ? 151 GLY   B O   1 
ATOM   1500 N N   . ASN   B 2 143 ? -11.031 -0.252  -14.359 1.00 47.00  ? 152 ASN   B N   1 
ATOM   1501 C CA  . ASN   B 2 143 ? -10.045 -0.577  -13.292 1.00 46.62  ? 152 ASN   B CA  1 
ATOM   1502 C C   . ASN   B 2 143 ? -9.091  -1.653  -13.792 1.00 46.57  ? 152 ASN   B C   1 
ATOM   1503 O O   . ASN   B 2 143 ? -9.536  -2.760  -14.087 1.00 46.50  ? 152 ASN   B O   1 
ATOM   1504 C CB  . ASN   B 2 143 ? -10.690 -1.049  -11.978 1.00 47.04  ? 152 ASN   B CB  1 
ATOM   1505 C CG  . ASN   B 2 143 ? -9.722  -1.047  -10.800 1.00 47.02  ? 152 ASN   B CG  1 
ATOM   1506 O OD1 . ASN   B 2 143 ? -8.827  -0.187  -10.682 1.00 46.30  ? 152 ASN   B OD1 1 
ATOM   1507 N ND2 . ASN   B 2 143 ? -9.912  -2.014  -9.914  1.00 46.95  ? 152 ASN   B ND2 1 
ATOM   1508 N N   . GLY   B 2 144 ? -7.813  -1.338  -13.834 1.00 47.27  ? 153 GLY   B N   1 
ATOM   1509 C CA  . GLY   B 2 144 ? -6.837  -2.300  -14.345 1.00 49.54  ? 153 GLY   B CA  1 
ATOM   1510 C C   . GLY   B 2 144 ? -5.442  -1.766  -14.170 1.00 51.73  ? 153 GLY   B C   1 
ATOM   1511 O O   . GLY   B 2 144 ? -5.173  -1.141  -13.113 1.00 50.33  ? 153 GLY   B O   1 
ATOM   1512 N N   . VAL   B 2 145 ? -4.611  -1.968  -15.193 1.00 54.77  ? 154 VAL   B N   1 
ATOM   1513 C CA  . VAL   B 2 145 ? -3.133  -1.947  -15.080 1.00 58.27  ? 154 VAL   B CA  1 
ATOM   1514 C C   . VAL   B 2 145 ? -2.544  -1.366  -16.375 1.00 62.99  ? 154 VAL   B C   1 
ATOM   1515 O O   . VAL   B 2 145 ? -3.262  -1.355  -17.379 1.00 65.06  ? 154 VAL   B O   1 
ATOM   1516 C CB  . VAL   B 2 145 ? -2.662  -3.375  -14.750 1.00 58.89  ? 154 VAL   B CB  1 
ATOM   1517 C CG1 . VAL   B 2 145 ? -2.288  -4.189  -15.978 1.00 58.54  ? 154 VAL   B CG1 1 
ATOM   1518 C CG2 . VAL   B 2 145 ? -1.553  -3.361  -13.708 1.00 59.81  ? 154 VAL   B CG2 1 
ATOM   1519 N N   . VAL   B 2 146 ? -1.314  -0.846  -16.296 1.00 66.19  ? 155 VAL   B N   1 
ATOM   1520 C CA  . VAL   B 2 146 ? -0.487  -0.272  -17.394 1.00 69.51  ? 155 VAL   B CA  1 
ATOM   1521 C C   . VAL   B 2 146 ? 0.607   -1.296  -17.738 1.00 74.58  ? 155 VAL   B C   1 
ATOM   1522 O O   . VAL   B 2 146 ? 1.277   -1.718  -16.783 1.00 75.20  ? 155 VAL   B O   1 
ATOM   1523 C CB  . VAL   B 2 146 ? 0.091   1.082   -16.943 1.00 68.57  ? 155 VAL   B CB  1 
ATOM   1524 C CG1 . VAL   B 2 146 ? 1.054   1.638   -17.973 1.00 71.97  ? 155 VAL   B CG1 1 
ATOM   1525 C CG2 . VAL   B 2 146 ? -1.012  2.086   -16.657 1.00 67.19  ? 155 VAL   B CG2 1 
ATOM   1526 N N   . ILE   B 2 147 ? 0.777   -1.730  -19.005 1.00 76.26  ? 156 ILE   B N   1 
ATOM   1527 C CA  . ILE   B 2 147 ? 1.629   -2.928  -19.301 1.00 80.83  ? 156 ILE   B CA  1 
ATOM   1528 C C   . ILE   B 2 147 ? 2.995   -2.480  -19.832 1.00 85.00  ? 156 ILE   B C   1 
ATOM   1529 O O   . ILE   B 2 147 ? 3.189   -1.271  -20.047 1.00 82.12  ? 156 ILE   B O   1 
ATOM   1530 C CB  . ILE   B 2 147 ? 0.940   -3.954  -20.229 1.00 81.83  ? 156 ILE   B CB  1 
ATOM   1531 C CG1 . ILE   B 2 147 ? 0.489   -3.377  -21.578 1.00 83.86  ? 156 ILE   B CG1 1 
ATOM   1532 C CG2 . ILE   B 2 147 ? -0.195  -4.643  -19.493 1.00 81.13  ? 156 ILE   B CG2 1 
ATOM   1533 C CD1 . ILE   B 2 147 ? 0.392   -4.422  -22.695 1.00 82.72  ? 156 ILE   B CD1 1 
ATOM   1534 N N   A LYS   B 2 148 ? 3.905   -3.452  -20.000 0.25 86.94  ? 157 LYS   B N   1 
ATOM   1535 N N   B LYS   B 2 148 ? 3.905   -3.452  -20.000 0.25 86.94  ? 157 LYS   B N   1 
ATOM   1536 N N   C LYS   B 2 148 ? 3.916   -3.430  -20.023 0.25 86.79  ? 157 LYS   B N   1 
ATOM   1537 N N   D LYS   B 2 148 ? 3.916   -3.430  -20.023 0.25 86.79  ? 157 LYS   B N   1 
ATOM   1538 C CA  A LYS   B 2 148 ? 5.257   -3.305  -20.612 0.25 89.78  ? 157 LYS   B CA  1 
ATOM   1539 C CA  B LYS   B 2 148 ? 5.257   -3.305  -20.612 0.25 89.78  ? 157 LYS   B CA  1 
ATOM   1540 C CA  C LYS   B 2 148 ? 5.298   -3.183  -20.521 0.25 89.47  ? 157 LYS   B CA  1 
ATOM   1541 C CA  D LYS   B 2 148 ? 5.298   -3.183  -20.521 0.25 89.47  ? 157 LYS   B CA  1 
ATOM   1542 C C   A LYS   B 2 148 ? 5.279   -2.102  -21.557 0.25 90.06  ? 157 LYS   B C   1 
ATOM   1543 C C   B LYS   B 2 148 ? 5.279   -2.102  -21.557 0.25 90.06  ? 157 LYS   B C   1 
ATOM   1544 C C   C LYS   B 2 148 ? 5.294   -2.064  -21.566 0.25 89.97  ? 157 LYS   B C   1 
ATOM   1545 C C   D LYS   B 2 148 ? 5.294   -2.064  -21.566 0.25 89.97  ? 157 LYS   B C   1 
ATOM   1546 O O   A LYS   B 2 148 ? 6.152   -1.232  -21.394 0.25 90.32  ? 157 LYS   B O   1 
ATOM   1547 O O   B LYS   B 2 148 ? 6.152   -1.232  -21.394 0.25 90.32  ? 157 LYS   B O   1 
ATOM   1548 O O   C LYS   B 2 148 ? 6.179   -1.194  -21.484 0.25 90.44  ? 157 LYS   B O   1 
ATOM   1549 O O   D LYS   B 2 148 ? 6.179   -1.194  -21.484 0.25 90.44  ? 157 LYS   B O   1 
ATOM   1550 C CB  A LYS   B 2 148 ? 5.619   -4.541  -21.443 0.25 91.65  ? 157 LYS   B CB  1 
ATOM   1551 C CB  B LYS   B 2 148 ? 5.619   -4.541  -21.443 0.25 91.65  ? 157 LYS   B CB  1 
ATOM   1552 C CB  C LYS   B 2 148 ? 5.885   -4.454  -21.139 0.25 91.20  ? 157 LYS   B CB  1 
ATOM   1553 C CB  D LYS   B 2 148 ? 5.885   -4.454  -21.139 0.25 91.20  ? 157 LYS   B CB  1 
ATOM   1554 C CG  A LYS   B 2 148 ? 5.961   -5.801  -20.661 0.25 92.82  ? 157 LYS   B CG  1 
ATOM   1555 C CG  B LYS   B 2 148 ? 5.961   -5.801  -20.661 0.25 92.82  ? 157 LYS   B CG  1 
ATOM   1556 C CG  C LYS   B 2 148 ? 6.133   -5.592  -20.158 0.25 91.73  ? 157 LYS   B CG  1 
ATOM   1557 C CG  D LYS   B 2 148 ? 6.133   -5.592  -20.158 0.25 91.73  ? 157 LYS   B CG  1 
ATOM   1558 C CD  A LYS   B 2 148 ? 6.589   -6.883  -21.522 0.25 93.93  ? 157 LYS   B CD  1 
ATOM   1559 C CD  B LYS   B 2 148 ? 6.589   -6.883  -21.522 0.25 93.93  ? 157 LYS   B CD  1 
ATOM   1560 C CD  C LYS   B 2 148 ? 7.445   -5.470  -19.409 0.25 91.99  ? 157 LYS   B CD  1 
ATOM   1561 C CD  D LYS   B 2 148 ? 7.445   -5.470  -19.409 0.25 91.99  ? 157 LYS   B CD  1 
ATOM   1562 C CE  A LYS   B 2 148 ? 7.838   -6.415  -22.241 0.25 95.02  ? 157 LYS   B CE  1 
ATOM   1563 C CE  B LYS   B 2 148 ? 7.838   -6.415  -22.241 0.25 95.02  ? 157 LYS   B CE  1 
ATOM   1564 C CE  C LYS   B 2 148 ? 8.594   -5.046  -20.302 0.25 92.43  ? 157 LYS   B CE  1 
ATOM   1565 C CE  D LYS   B 2 148 ? 8.594   -5.046  -20.302 0.25 92.43  ? 157 LYS   B CE  1 
ATOM   1566 N NZ  A LYS   B 2 148 ? 8.834   -5.853  -21.298 0.25 95.65  ? 157 LYS   B NZ  1 
ATOM   1567 N NZ  B LYS   B 2 148 ? 8.834   -5.853  -21.298 0.25 95.65  ? 157 LYS   B NZ  1 
ATOM   1568 N NZ  C LYS   B 2 148 ? 9.896   -5.548  -19.800 0.25 92.12  ? 157 LYS   B NZ  1 
ATOM   1569 N NZ  D LYS   B 2 148 ? 9.896   -5.548  -19.800 0.25 92.12  ? 157 LYS   B NZ  1 
ATOM   1570 N N   . ASN   B 2 149 ? 4.329   -2.092  -22.495 1.00 91.08  ? 158 ASN   B N   1 
ATOM   1571 C CA  . ASN   B 2 149 ? 4.240   -1.143  -23.643 1.00 90.39  ? 158 ASN   B CA  1 
ATOM   1572 C C   . ASN   B 2 149 ? 3.970   0.308   -23.210 1.00 86.81  ? 158 ASN   B C   1 
ATOM   1573 O O   . ASN   B 2 149 ? 4.287   1.211   -23.998 1.00 87.68  ? 158 ASN   B O   1 
ATOM   1574 C CB  . ASN   B 2 149 ? 3.125   -1.578  -24.611 1.00 92.29  ? 158 ASN   B CB  1 
ATOM   1575 C CG  . ASN   B 2 149 ? 2.977   -3.082  -24.789 1.00 94.62  ? 158 ASN   B CG  1 
ATOM   1576 O OD1 . ASN   B 2 149 ? 3.543   -3.879  -24.035 1.00 96.85  ? 158 ASN   B OD1 1 
ATOM   1577 N ND2 . ASN   B 2 149 ? 2.219   -3.490  -25.797 1.00 95.68  ? 158 ASN   B ND2 1 
ATOM   1578 N N   . GLY   B 2 150 ? 3.349   0.531   -22.049 1.00 82.73  ? 159 GLY   B N   1 
ATOM   1579 C CA  . GLY   B 2 150 ? 2.776   1.842   -21.666 1.00 77.72  ? 159 GLY   B CA  1 
ATOM   1580 C C   . GLY   B 2 150 ? 1.267   1.933   -21.893 1.00 74.86  ? 159 GLY   B C   1 
ATOM   1581 O O   . GLY   B 2 150 ? 0.646   2.952   -21.487 1.00 72.16  ? 159 GLY   B O   1 
ATOM   1582 N N   A SER   B 2 151 ? 0.680   0.907   -22.524 0.25 74.21  ? 160 SER   B N   1 
ATOM   1583 N N   B SER   B 2 151 ? 0.692   0.896   -22.516 0.25 73.93  ? 160 SER   B N   1 
ATOM   1584 N N   C SER   B 2 151 ? 0.680   0.907   -22.524 0.25 74.21  ? 160 SER   B N   1 
ATOM   1585 N N   D SER   B 2 151 ? 0.692   0.896   -22.516 0.25 73.93  ? 160 SER   B N   1 
ATOM   1586 C CA  A SER   B 2 151 ? -0.776  0.798   -22.811 0.25 72.63  ? 160 SER   B CA  1 
ATOM   1587 C CA  B SER   B 2 151 ? -0.758  0.742   -22.806 0.25 72.20  ? 160 SER   B CA  1 
ATOM   1588 C CA  C SER   B 2 151 ? -0.776  0.798   -22.811 0.25 72.63  ? 160 SER   B CA  1 
ATOM   1589 C CA  D SER   B 2 151 ? -0.758  0.742   -22.806 0.25 72.20  ? 160 SER   B CA  1 
ATOM   1590 C C   A SER   B 2 151 ? -1.529  0.298   -21.569 0.25 70.92  ? 160 SER   B C   1 
ATOM   1591 C C   B SER   B 2 151 ? -1.521  0.330   -21.538 0.25 70.64  ? 160 SER   B C   1 
ATOM   1592 C C   C SER   B 2 151 ? -1.529  0.298   -21.569 0.25 70.92  ? 160 SER   B C   1 
ATOM   1593 C C   D SER   B 2 151 ? -1.521  0.330   -21.538 0.25 70.64  ? 160 SER   B C   1 
ATOM   1594 O O   A SER   B 2 151 ? -0.890  -0.318  -20.691 0.25 70.25  ? 160 SER   B O   1 
ATOM   1595 O O   B SER   B 2 151 ? -0.877  -0.184  -20.603 0.25 69.95  ? 160 SER   B O   1 
ATOM   1596 O O   C SER   B 2 151 ? -0.890  -0.318  -20.691 0.25 70.25  ? 160 SER   B O   1 
ATOM   1597 O O   D SER   B 2 151 ? -0.877  -0.184  -20.603 0.25 69.95  ? 160 SER   B O   1 
ATOM   1598 C CB  A SER   B 2 151 ? -1.026  -0.098  -23.997 0.25 73.00  ? 160 SER   B CB  1 
ATOM   1599 C CB  B SER   B 2 151 ? -0.956  -0.265  -23.907 0.25 72.25  ? 160 SER   B CB  1 
ATOM   1600 C CB  C SER   B 2 151 ? -1.026  -0.098  -23.997 0.25 73.00  ? 160 SER   B CB  1 
ATOM   1601 C CB  D SER   B 2 151 ? -0.956  -0.265  -23.907 0.25 72.25  ? 160 SER   B CB  1 
ATOM   1602 O OG  A SER   B 2 151 ? -2.342  0.082   -24.507 0.25 72.45  ? 160 SER   B OG  1 
ATOM   1603 O OG  B SER   B 2 151 ? -0.107  -1.389  -23.720 0.25 71.87  ? 160 SER   B OG  1 
ATOM   1604 O OG  C SER   B 2 151 ? -2.342  0.082   -24.507 0.25 72.45  ? 160 SER   B OG  1 
ATOM   1605 O OG  D SER   B 2 151 ? -0.107  -1.389  -23.720 0.25 71.87  ? 160 SER   B OG  1 
ATOM   1606 N N   . TYR   B 2 152 ? -2.845  0.536   -21.532 1.00 69.37  ? 161 TYR   B N   1 
ATOM   1607 C CA  . TYR   B 2 152 ? -3.749  0.180   -20.405 1.00 68.02  ? 161 TYR   B CA  1 
ATOM   1608 C C   . TYR   B 2 152 ? -4.559  -1.095  -20.706 1.00 63.89  ? 161 TYR   B C   1 
ATOM   1609 O O   . TYR   B 2 152 ? -5.212  -1.163  -21.734 1.00 59.67  ? 161 TYR   B O   1 
ATOM   1610 C CB  . TYR   B 2 152 ? -4.707  1.352   -20.180 1.00 69.90  ? 161 TYR   B CB  1 
ATOM   1611 C CG  . TYR   B 2 152 ? -5.630  1.219   -18.998 1.00 69.91  ? 161 TYR   B CG  1 
ATOM   1612 C CD1 . TYR   B 2 152 ? -5.167  1.461   -17.713 1.00 70.45  ? 161 TYR   B CD1 1 
ATOM   1613 C CD2 . TYR   B 2 152 ? -6.966  0.881   -19.165 1.00 69.69  ? 161 TYR   B CD2 1 
ATOM   1614 C CE1 . TYR   B 2 152 ? -6.001  1.363   -16.614 1.00 69.29  ? 161 TYR   B CE1 1 
ATOM   1615 C CE2 . TYR   B 2 152 ? -7.812  0.774   -18.073 1.00 71.95  ? 161 TYR   B CE2 1 
ATOM   1616 C CZ  . TYR   B 2 152 ? -7.324  1.002   -16.793 1.00 70.08  ? 161 TYR   B CZ  1 
ATOM   1617 O OH  . TYR   B 2 152 ? -8.150  0.909   -15.709 1.00 75.25  ? 161 TYR   B OH  1 
ATOM   1618 N N   . VAL   B 2 153 ? -4.566  -2.049  -19.770 1.00 59.28  ? 162 VAL   B N   1 
ATOM   1619 C CA  . VAL   B 2 153 ? -5.468  -3.242  -19.762 1.00 57.29  ? 162 VAL   B CA  1 
ATOM   1620 C C   . VAL   B 2 153 ? -6.427  -3.118  -18.557 1.00 53.89  ? 162 VAL   B C   1 
ATOM   1621 O O   . VAL   B 2 153 ? -5.926  -3.012  -17.471 1.00 51.94  ? 162 VAL   B O   1 
ATOM   1622 C CB  . VAL   B 2 153 ? -4.636  -4.539  -19.682 1.00 58.42  ? 162 VAL   B CB  1 
ATOM   1623 C CG1 . VAL   B 2 153 ? -5.441  -5.767  -20.065 1.00 58.20  ? 162 VAL   B CG1 1 
ATOM   1624 C CG2 . VAL   B 2 153 ? -3.375  -4.452  -20.519 1.00 61.35  ? 162 VAL   B CG2 1 
ATOM   1625 N N   . SER   B 2 154 ? -7.740  -3.171  -18.772 1.00 51.40  ? 163 SER   B N   1 
ATOM   1626 C CA  . SER   B 2 154 ? -8.812  -3.128  -17.755 1.00 49.54  ? 163 SER   B CA  1 
ATOM   1627 C C   . SER   B 2 154 ? -9.288  -4.547  -17.415 1.00 49.06  ? 163 SER   B C   1 
ATOM   1628 O O   . SER   B 2 154 ? -9.505  -5.340  -18.322 1.00 48.62  ? 163 SER   B O   1 
ATOM   1629 C CB  . SER   B 2 154 ? -9.964  -2.301  -18.250 1.00 48.85  ? 163 SER   B CB  1 
ATOM   1630 O OG  . SER   B 2 154 ? -11.084 -2.363  -17.346 1.00 46.75  ? 163 SER   B OG  1 
ATOM   1631 N N   . ALA   B 2 155 ? -9.573  -4.820  -16.146 1.00 47.51  ? 164 ALA   B N   1 
ATOM   1632 C CA  . ALA   B 2 155 ? -10.405 -5.973  -15.749 1.00 46.84  ? 164 ALA   B CA  1 
ATOM   1633 C C   . ALA   B 2 155 ? -11.802 -5.718  -16.365 1.00 46.76  ? 164 ALA   B C   1 
ATOM   1634 O O   . ALA   B 2 155 ? -12.217 -4.523  -16.708 1.00 47.52  ? 164 ALA   B O   1 
ATOM   1635 C CB  . ALA   B 2 155 ? -10.471 -6.118  -14.235 1.00 47.08  ? 164 ALA   B CB  1 
ATOM   1636 N N   . ILE   B 2 156 ? -12.459 -6.829  -16.694 1.00 46.45  ? 165 ILE   B N   1 
ATOM   1637 C CA  . ILE   B 2 156 ? -13.943 -6.903  -16.744 1.00 46.07  ? 165 ILE   B CA  1 
ATOM   1638 C C   . ILE   B 2 156 ? -14.419 -7.067  -15.281 1.00 45.27  ? 165 ILE   B C   1 
ATOM   1639 O O   . ILE   B 2 156 ? -14.469 -8.212  -14.798 1.00 43.60  ? 165 ILE   B O   1 
ATOM   1640 C CB  . ILE   B 2 156 ? -14.404 -8.079  -17.613 1.00 46.66  ? 165 ILE   B CB  1 
ATOM   1641 C CG1 . ILE   B 2 156 ? -13.683 -8.098  -18.963 1.00 48.47  ? 165 ILE   B CG1 1 
ATOM   1642 C CG2 . ILE   B 2 156 ? -15.920 -8.035  -17.738 1.00 46.34  ? 165 ILE   B CG2 1 
ATOM   1643 C CD1 . ILE   B 2 156 ? -13.811 -9.404  -19.687 1.00 49.71  ? 165 ILE   B CD1 1 
ATOM   1644 N N   . THR   B 2 157 ? -14.714 -5.941  -14.628 1.00 44.75  ? 166 THR   B N   1 
ATOM   1645 C CA  . THR   B 2 157 ? -15.196 -5.837  -13.221 1.00 44.33  ? 166 THR   B CA  1 
ATOM   1646 C C   . THR   B 2 157 ? -16.719 -6.043  -13.201 1.00 44.18  ? 166 THR   B C   1 
ATOM   1647 O O   . THR   B 2 157 ? -17.458 -5.124  -13.715 1.00 43.47  ? 166 THR   B O   1 
ATOM   1648 C CB  . THR   B 2 157 ? -14.800 -4.488  -12.613 1.00 44.10  ? 166 THR   B CB  1 
ATOM   1649 O OG1 . THR   B 2 157 ? -13.365 -4.386  -12.680 1.00 43.17  ? 166 THR   B OG1 1 
ATOM   1650 C CG2 . THR   B 2 157 ? -15.292 -4.332  -11.181 1.00 43.61  ? 166 THR   B CG2 1 
ATOM   1651 N N   . GLN   B 2 158 ? -17.156 -7.168  -12.598 1.00 43.71  ? 167 GLN   B N   1 
ATOM   1652 C CA  . GLN   B 2 158 ? -18.587 -7.498  -12.371 1.00 44.29  ? 167 GLN   B CA  1 
ATOM   1653 C C   . GLN   B 2 158 ? -18.891 -7.602  -10.851 1.00 45.70  ? 167 GLN   B C   1 
ATOM   1654 O O   . GLN   B 2 158 ? -18.068 -8.147  -10.083 1.00 44.06  ? 167 GLN   B O   1 
ATOM   1655 C CB  . GLN   B 2 158 ? -18.911 -8.796  -13.109 1.00 43.67  ? 167 GLN   B CB  1 
ATOM   1656 C CG  . GLN   B 2 158 ? -20.390 -9.177  -13.121 1.00 43.48  ? 167 GLN   B CG  1 
ATOM   1657 C CD  . GLN   B 2 158 ? -21.325 -8.109  -13.653 1.00 43.33  ? 167 GLN   B CD  1 
ATOM   1658 O OE1 . GLN   B 2 158 ? -21.386 -6.994  -13.147 1.00 42.66  ? 167 GLN   B OE1 1 
ATOM   1659 N NE2 . GLN   B 2 158 ? -22.094 -8.451  -14.685 1.00 42.86  ? 167 GLN   B NE2 1 
ATOM   1660 N N   . GLY   B 2 159 ? -20.067 -7.142  -10.446 1.00 48.35  ? 168 GLY   B N   1 
ATOM   1661 C CA  . GLY   B 2 159 ? -20.558 -7.271  -9.060  1.00 52.88  ? 168 GLY   B CA  1 
ATOM   1662 C C   . GLY   B 2 159 ? -21.247 -8.606  -8.873  1.00 57.29  ? 168 GLY   B C   1 
ATOM   1663 O O   . GLY   B 2 159 ? -21.287 -9.386  -9.831  1.00 58.22  ? 168 GLY   B O   1 
ATOM   1664 N N   . LYS   B 2 160 ? -21.693 -8.882  -7.653  1.00 65.98  ? 169 LYS   B N   1 
ATOM   1665 C CA  . LYS   B 2 160 ? -22.546 -10.040 -7.279  1.00 72.46  ? 169 LYS   B CA  1 
ATOM   1666 C C   . LYS   B 2 160 ? -23.984 -9.519  -7.118  1.00 76.95  ? 169 LYS   B C   1 
ATOM   1667 O O   . LYS   B 2 160 ? -24.160 -8.459  -6.474  1.00 79.36  ? 169 LYS   B O   1 
ATOM   1668 C CB  . LYS   B 2 160 ? -21.999 -10.708 -6.007  1.00 75.61  ? 169 LYS   B CB  1 
ATOM   1669 C CG  . LYS   B 2 160 ? -22.498 -12.131 -5.797  1.00 78.39  ? 169 LYS   B CG  1 
ATOM   1670 C CD  . LYS   B 2 160 ? -22.108 -12.766 -4.493  1.00 78.84  ? 169 LYS   B CD  1 
ATOM   1671 C CE  . LYS   B 2 160 ? -23.267 -13.468 -3.821  1.00 80.67  ? 169 LYS   B CE  1 
ATOM   1672 N NZ  . LYS   B 2 160 ? -23.312 -13.119 -2.379  1.00 82.77  ? 169 LYS   B NZ  1 
ATOM   1673 N N   . ARG   B 2 161 ? -24.964 -10.201 -7.723  1.00 79.80  ? 170 ARG   B N   1 
ATOM   1674 C CA  . ARG   B 2 161 ? -26.426 -9.963  -7.532  1.00 83.44  ? 170 ARG   B CA  1 
ATOM   1675 C C   . ARG   B 2 161 ? -26.923 -10.876 -6.390  1.00 88.64  ? 170 ARG   B C   1 
ATOM   1676 O O   . ARG   B 2 161 ? -26.471 -12.043 -6.349  1.00 92.94  ? 170 ARG   B O   1 
ATOM   1677 C CB  . ARG   B 2 161 ? -27.132 -10.222 -8.871  1.00 82.01  ? 170 ARG   B CB  1 
ATOM   1678 C CG  . ARG   B 2 161 ? -28.555 -9.689  -8.980  1.00 81.35  ? 170 ARG   B CG  1 
ATOM   1679 C CD  . ARG   B 2 161 ? -29.311 -10.209 -10.202 1.00 81.81  ? 170 ARG   B CD  1 
ATOM   1680 N NE  . ARG   B 2 161 ? -30.759 -10.021 -10.083 1.00 82.91  ? 170 ARG   B NE  1 
ATOM   1681 C CZ  . ARG   B 2 161 ? -31.531 -9.209  -10.822 1.00 83.15  ? 170 ARG   B CZ  1 
ATOM   1682 N NH1 . ARG   B 2 161 ? -31.043 -8.466  -11.804 1.00 78.97  ? 170 ARG   B NH1 1 
ATOM   1683 N NH2 . ARG   B 2 161 ? -32.825 -9.144  -10.558 1.00 84.98  ? 170 ARG   B NH2 1 
ATOM   1684 N N   . GLU   B 2 162 ? -27.787 -10.377 -5.485  1.00 92.01  ? 171 GLU   B N   1 
ATOM   1685 C CA  . GLU   B 2 162 ? -28.277 -11.116 -4.276  1.00 95.03  ? 171 GLU   B CA  1 
ATOM   1686 C C   . GLU   B 2 162 ? -29.769 -11.425 -4.453  1.00 90.89  ? 171 GLU   B C   1 
ATOM   1687 O O   . GLU   B 2 162 ? -30.134 -12.504 -4.897  1.00 87.56  ? 171 GLU   B O   1 
ATOM   1688 C CB  . GLU   B 2 162 ? -28.072 -10.332 -2.968  1.00 98.08  ? 171 GLU   B CB  1 
ATOM   1689 C CG  . GLU   B 2 162 ? -26.783 -9.518  -2.882  1.00 101.49 ? 171 GLU   B CG  1 
ATOM   1690 C CD  . GLU   B 2 162 ? -25.573 -10.199 -2.255  1.00 106.50 ? 171 GLU   B CD  1 
ATOM   1691 O OE1 . GLU   B 2 162 ? -25.730 -10.856 -1.189  1.00 109.86 ? 171 GLU   B OE1 1 
ATOM   1692 O OE2 . GLU   B 2 162 ? -24.462 -10.048 -2.822  1.00 107.67 ? 171 GLU   B OE2 1 
HETATM 1693 S S   A DMS   C 3 .   ? -7.479  5.578   -17.821 0.16 114.18 ? 201 DMS   B S   1 
HETATM 1694 S S   B DMS   C 3 .   ? -7.479  5.578   -17.821 0.16 114.18 ? 201 DMS   B S   1 
HETATM 1695 O O   A DMS   C 3 .   ? -6.114  4.992   -18.064 0.16 114.45 ? 201 DMS   B O   1 
HETATM 1696 O O   B DMS   C 3 .   ? -6.114  4.992   -18.064 0.16 114.45 ? 201 DMS   B O   1 
HETATM 1697 C C1  A DMS   C 3 .   ? -7.815  5.356   -16.093 0.16 113.81 ? 201 DMS   B C1  1 
HETATM 1698 C C1  B DMS   C 3 .   ? -7.815  5.356   -16.093 0.16 113.81 ? 201 DMS   B C1  1 
HETATM 1699 C C2  A DMS   C 3 .   ? -8.652  4.395   -18.438 0.16 113.81 ? 201 DMS   B C2  1 
HETATM 1700 C C2  B DMS   C 3 .   ? -8.652  4.395   -18.438 0.16 113.81 ? 201 DMS   B C2  1 
HETATM 1701 S S   . DMS   D 3 .   ? -18.639 11.391  -0.091  1.00 86.98  ? 202 DMS   B S   1 
HETATM 1702 O O   . DMS   D 3 .   ? -19.127 9.985   -0.342  1.00 81.01  ? 202 DMS   B O   1 
HETATM 1703 C C1  . DMS   D 3 .   ? -19.757 12.488  -0.918  1.00 83.95  ? 202 DMS   B C1  1 
HETATM 1704 C C2  . DMS   D 3 .   ? -17.234 11.646  -1.143  1.00 82.49  ? 202 DMS   B C2  1 
HETATM 1705 S S   A DMS   E 3 .   ? -7.037  2.949   -13.536 0.16 77.11  ? 203 DMS   B S   1 
HETATM 1706 S S   B DMS   E 3 .   ? -7.037  2.949   -13.536 0.16 77.11  ? 203 DMS   B S   1 
HETATM 1707 O O   A DMS   E 3 .   ? -6.745  1.477   -13.555 0.16 75.41  ? 203 DMS   B O   1 
HETATM 1708 O O   B DMS   E 3 .   ? -6.745  1.477   -13.555 0.16 75.41  ? 203 DMS   B O   1 
HETATM 1709 C C1  A DMS   E 3 .   ? -8.021  3.245   -12.083 0.16 76.73  ? 203 DMS   B C1  1 
HETATM 1710 C C1  B DMS   E 3 .   ? -8.021  3.245   -12.083 0.16 76.73  ? 203 DMS   B C1  1 
HETATM 1711 C C2  A DMS   E 3 .   ? -5.547  3.742   -12.983 0.16 77.34  ? 203 DMS   B C2  1 
HETATM 1712 C C2  B DMS   E 3 .   ? -5.547  3.742   -12.983 0.16 77.34  ? 203 DMS   B C2  1 
HETATM 1713 N N1  C A1BXG F 4 .   ? -7.437  6.607   -13.143 0.34 82.39  ? 204 A1BXG B N1  1 
HETATM 1714 N N1  D A1BXG F 4 .   ? -7.437  6.607   -13.143 0.34 82.39  ? 204 A1BXG B N1  1 
HETATM 1715 N N3  C A1BXG F 4 .   ? -6.368  5.138   -18.394 0.34 80.38  ? 204 A1BXG B N3  1 
HETATM 1716 N N3  D A1BXG F 4 .   ? -6.368  5.138   -18.394 0.34 80.38  ? 204 A1BXG B N3  1 
HETATM 1717 C C4  C A1BXG F 4 .   ? -8.129  4.561   -12.579 0.34 82.53  ? 204 A1BXG B C4  1 
HETATM 1718 C C4  D A1BXG F 4 .   ? -8.129  4.561   -12.579 0.34 82.53  ? 204 A1BXG B C4  1 
HETATM 1719 C C5  C A1BXG F 4 .   ? -8.084  5.108   -15.078 0.34 81.18  ? 204 A1BXG B C5  1 
HETATM 1720 C C5  D A1BXG F 4 .   ? -8.084  5.108   -15.078 0.34 81.18  ? 204 A1BXG B C5  1 
HETATM 1721 C C6  C A1BXG F 4 .   ? -9.312  4.628   -15.480 0.34 80.11  ? 204 A1BXG B C6  1 
HETATM 1722 C C6  D A1BXG F 4 .   ? -9.312  4.628   -15.480 0.34 80.11  ? 204 A1BXG B C6  1 
HETATM 1723 C C7  C A1BXG F 4 .   ? -9.566  4.325   -16.827 0.34 79.33  ? 204 A1BXG B C7  1 
HETATM 1724 C C7  D A1BXG F 4 .   ? -9.566  4.325   -16.827 0.34 79.33  ? 204 A1BXG B C7  1 
HETATM 1725 C C8  C A1BXG F 4 .   ? -8.613  4.489   -17.797 0.34 80.01  ? 204 A1BXG B C8  1 
HETATM 1726 C C8  D A1BXG F 4 .   ? -8.613  4.489   -17.797 0.34 80.01  ? 204 A1BXG B C8  1 
HETATM 1727 C C10 C A1BXG F 4 .   ? -5.176  5.590   -18.032 0.34 80.27  ? 204 A1BXG B C10 1 
HETATM 1728 C C10 D A1BXG F 4 .   ? -5.176  5.590   -18.032 0.34 80.27  ? 204 A1BXG B C10 1 
HETATM 1729 C C13 C A1BXG F 4 .   ? -7.049  5.287   -16.057 0.34 80.60  ? 204 A1BXG B C13 1 
HETATM 1730 C C13 D A1BXG F 4 .   ? -7.049  5.287   -16.057 0.34 80.60  ? 204 A1BXG B C13 1 
HETATM 1731 C C1  C A1BXG F 4 .   ? -6.973  7.540   -10.864 0.34 81.93  ? 204 A1BXG B C1  1 
HETATM 1732 C C1  D A1BXG F 4 .   ? -6.973  7.540   -10.864 0.34 81.93  ? 204 A1BXG B C1  1 
HETATM 1733 C C2  C A1BXG F 4 .   ? -7.401  6.484   -11.818 0.34 82.72  ? 204 A1BXG B C2  1 
HETATM 1734 C C2  D A1BXG F 4 .   ? -7.401  6.484   -11.818 0.34 82.72  ? 204 A1BXG B C2  1 
HETATM 1735 C C3  C A1BXG F 4 .   ? -7.886  5.389   -13.641 0.34 81.49  ? 204 A1BXG B C3  1 
HETATM 1736 C C3  D A1BXG F 4 .   ? -7.886  5.389   -13.641 0.34 81.49  ? 204 A1BXG B C3  1 
HETATM 1737 N N2  C A1BXG F 4 .   ? -7.818  5.258   -11.450 0.34 82.62  ? 204 A1BXG B N2  1 
HETATM 1738 N N2  D A1BXG F 4 .   ? -7.818  5.258   -11.450 0.34 82.62  ? 204 A1BXG B N2  1 
HETATM 1739 C C9  C A1BXG F 4 .   ? -7.324  4.980   -17.421 0.34 80.75  ? 204 A1BXG B C9  1 
HETATM 1740 C C9  D A1BXG F 4 .   ? -7.324  4.980   -17.421 0.34 80.75  ? 204 A1BXG B C9  1 
HETATM 1741 C C11 C A1BXG F 4 .   ? -4.819  5.918   -16.711 0.34 80.25  ? 204 A1BXG B C11 1 
HETATM 1742 C C11 D A1BXG F 4 .   ? -4.819  5.918   -16.711 0.34 80.25  ? 204 A1BXG B C11 1 
HETATM 1743 C C12 C A1BXG F 4 .   ? -5.754  5.767   -15.729 0.34 80.58  ? 204 A1BXG B C12 1 
HETATM 1744 C C12 D A1BXG F 4 .   ? -5.754  5.767   -15.729 0.34 80.58  ? 204 A1BXG B C12 1 
HETATM 1745 C C14 C A1BXG F 4 .   ? -8.921  4.151   -19.227 0.34 81.25  ? 204 A1BXG B C14 1 
HETATM 1746 C C14 D A1BXG F 4 .   ? -8.921  4.151   -19.227 0.34 81.25  ? 204 A1BXG B C14 1 
HETATM 1747 S S   C DMS   G 3 .   ? -20.671 -9.116  1.342   0.50 205.92 ? 205 DMS   B S   1 
HETATM 1748 S S   D DMS   G 3 .   ? -20.671 -9.116  1.342   0.50 205.92 ? 205 DMS   B S   1 
HETATM 1749 O O   C DMS   G 3 .   ? -21.230 -8.677  2.682   0.50 203.36 ? 205 DMS   B O   1 
HETATM 1750 O O   D DMS   G 3 .   ? -21.230 -8.677  2.682   0.50 203.36 ? 205 DMS   B O   1 
HETATM 1751 C C1  C DMS   G 3 .   ? -20.220 -7.627  0.475   0.50 205.09 ? 205 DMS   B C1  1 
HETATM 1752 C C1  D DMS   G 3 .   ? -20.220 -7.627  0.475   0.50 205.09 ? 205 DMS   B C1  1 
HETATM 1753 C C2  C DMS   G 3 .   ? -22.068 -9.545  0.323   0.50 205.69 ? 205 DMS   B C2  1 
HETATM 1754 C C2  D DMS   G 3 .   ? -22.068 -9.545  0.323   0.50 205.69 ? 205 DMS   B C2  1 
HETATM 1755 O O   . HOH   H 5 .   ? -27.567 -6.368  -28.273 1.00 57.88  ? 101 HOH   A O   1 
HETATM 1756 O O   . HOH   H 5 .   ? -1.891  -4.126  -6.264  1.00 52.19  ? 102 HOH   A O   1 
HETATM 1757 O O   A HOH   H 5 .   ? 5.527   -5.521  -12.153 0.50 108.76 ? 103 HOH   A O   1 
HETATM 1758 O O   B HOH   H 5 .   ? 5.527   -5.521  -12.153 0.50 108.76 ? 103 HOH   A O   1 
HETATM 1759 O O   A HOH   H 5 .   ? -28.666 15.451  -15.327 0.50 70.34  ? 104 HOH   A O   1 
HETATM 1760 O O   B HOH   H 5 .   ? -28.666 15.451  -15.327 0.50 70.34  ? 104 HOH   A O   1 
HETATM 1761 O O   A HOH   H 5 .   ? -6.828  -9.007  -2.993  0.50 56.11  ? 105 HOH   A O   1 
HETATM 1762 O O   B HOH   H 5 .   ? -6.828  -9.007  -2.993  0.50 56.11  ? 105 HOH   A O   1 
HETATM 1763 O O   . HOH   H 5 .   ? -7.736  -0.088  3.636   1.00 60.27  ? 106 HOH   A O   1 
HETATM 1764 O O   . HOH   H 5 .   ? -31.362 -0.505  -29.119 1.00 56.77  ? 107 HOH   A O   1 
HETATM 1765 O O   A HOH   H 5 .   ? -26.185 1.289   -29.326 0.50 65.57  ? 108 HOH   A O   1 
HETATM 1766 O O   B HOH   H 5 .   ? -26.185 1.289   -29.326 0.50 65.57  ? 108 HOH   A O   1 
HETATM 1767 O O   A HOH   H 5 .   ? -8.143  2.975   -8.798  0.16 56.74  ? 109 HOH   A O   1 
HETATM 1768 O O   B HOH   H 5 .   ? -8.143  2.975   -8.798  0.16 56.74  ? 109 HOH   A O   1 
HETATM 1769 O O   A HOH   H 5 .   ? -3.552  -4.187  0.310   0.50 74.21  ? 110 HOH   A O   1 
HETATM 1770 O O   B HOH   H 5 .   ? -3.552  -4.187  0.310   0.50 74.21  ? 110 HOH   A O   1 
HETATM 1771 O O   . HOH   H 5 .   ? -23.620 8.984   -27.446 1.00 53.17  ? 111 HOH   A O   1 
HETATM 1772 O O   A HOH   H 5 .   ? -25.974 -3.981  -35.449 0.50 84.99  ? 112 HOH   A O   1 
HETATM 1773 O O   B HOH   H 5 .   ? -25.974 -3.981  -35.449 0.50 84.99  ? 112 HOH   A O   1 
HETATM 1774 O O   A HOH   H 5 .   ? -23.742 18.738  -19.351 0.50 65.12  ? 113 HOH   A O   1 
HETATM 1775 O O   B HOH   H 5 .   ? -23.742 18.738  -19.351 0.50 65.12  ? 113 HOH   A O   1 
HETATM 1776 O O   . HOH   H 5 .   ? -4.110  -0.844  -0.052  1.00 56.24  ? 114 HOH   A O   1 
HETATM 1777 O O   . HOH   H 5 .   ? -3.601  -14.735 -25.355 1.00 49.44  ? 115 HOH   A O   1 
HETATM 1778 O O   . HOH   H 5 .   ? -30.168 12.154  -16.539 1.00 61.04  ? 116 HOH   A O   1 
HETATM 1779 O O   A HOH   H 5 .   ? -30.298 0.177   -23.121 0.50 62.94  ? 117 HOH   A O   1 
HETATM 1780 O O   B HOH   H 5 .   ? -30.298 0.177   -23.121 0.50 62.94  ? 117 HOH   A O   1 
HETATM 1781 O O   A HOH   H 5 .   ? -5.544  1.772   -10.019 0.16 39.38  ? 118 HOH   A O   1 
HETATM 1782 O O   B HOH   H 5 .   ? -5.544  1.772   -10.019 0.16 39.38  ? 118 HOH   A O   1 
HETATM 1783 O O   . HOH   H 5 .   ? -8.064  -1.774  7.056   1.00 58.00  ? 119 HOH   A O   1 
HETATM 1784 O O   . HOH   H 5 .   ? -4.739  -10.691 -5.564  1.00 55.14  ? 120 HOH   A O   1 
HETATM 1785 O O   . HOH   H 5 .   ? -2.800  -9.415  -3.237  1.00 69.04  ? 121 HOH   A O   1 
HETATM 1786 O O   A HOH   H 5 .   ? -21.692 -9.494  -35.146 0.50 78.50  ? 122 HOH   A O   1 
HETATM 1787 O O   B HOH   H 5 .   ? -21.692 -9.494  -35.146 0.50 78.50  ? 122 HOH   A O   1 
HETATM 1788 O O   . HOH   I 5 .   ? -25.633 -8.375  -16.688 1.00 45.49  ? 301 HOH   B O   1 
HETATM 1789 O O   . HOH   I 5 .   ? -30.176 12.411  -19.396 1.00 56.63  ? 302 HOH   B O   1 
HETATM 1790 O O   . HOH   I 5 .   ? -33.620 1.302   -15.645 1.00 54.52  ? 303 HOH   B O   1 
HETATM 1791 O O   . HOH   I 5 .   ? -17.038 12.453  -5.502  1.00 53.93  ? 304 HOH   B O   1 
HETATM 1792 O O   C HOH   I 5 .   ? -20.866 13.596  -33.604 0.50 63.83  ? 305 HOH   B O   1 
HETATM 1793 O O   D HOH   I 5 .   ? -20.866 13.596  -33.604 0.50 63.83  ? 305 HOH   B O   1 
HETATM 1794 O O   . HOH   I 5 .   ? -16.173 20.312  -14.174 1.00 64.27  ? 306 HOH   B O   1 
HETATM 1795 O O   A HOH   I 5 .   ? -14.470 -6.767  -1.493  0.50 63.99  ? 307 HOH   B O   1 
HETATM 1796 O O   B HOH   I 5 .   ? -14.470 -6.767  -1.493  0.50 63.99  ? 307 HOH   B O   1 
HETATM 1797 O O   A HOH   I 5 .   ? -19.377 -12.519 -25.477 0.50 61.70  ? 308 HOH   B O   1 
HETATM 1798 O O   B HOH   I 5 .   ? -19.377 -12.519 -25.477 0.50 61.70  ? 308 HOH   B O   1 
HETATM 1799 O O   A HOH   I 5 .   ? -15.802 25.798  -12.801 0.50 80.79  ? 309 HOH   B O   1 
HETATM 1800 O O   B HOH   I 5 .   ? -15.802 25.798  -12.801 0.50 80.79  ? 309 HOH   B O   1 
HETATM 1801 O O   . HOH   I 5 .   ? -17.642 -11.012 -16.510 1.00 42.25  ? 310 HOH   B O   1 
HETATM 1802 O O   . HOH   I 5 .   ? -23.485 -7.088  -4.438  1.00 56.38  ? 311 HOH   B O   1 
HETATM 1803 O O   . HOH   I 5 .   ? -28.561 -4.745  -22.263 1.00 61.97  ? 312 HOH   B O   1 
HETATM 1804 O O   A HOH   I 5 .   ? -15.404 -10.474 -15.515 0.50 66.98  ? 313 HOH   B O   1 
HETATM 1805 O O   B HOH   I 5 .   ? -15.404 -10.474 -15.515 0.50 66.98  ? 313 HOH   B O   1 
HETATM 1806 O O   . HOH   I 5 .   ? -6.289  -0.572  -10.764 1.00 46.99  ? 314 HOH   B O   1 
HETATM 1807 O O   . HOH   I 5 .   ? -11.958 -3.597  -9.935  1.00 51.74  ? 315 HOH   B O   1 
HETATM 1808 O O   A HOH   I 5 .   ? -31.245 6.536   -4.413  0.50 80.10  ? 316 HOH   B O   1 
HETATM 1809 O O   B HOH   I 5 .   ? -31.245 6.536   -4.413  0.50 80.10  ? 316 HOH   B O   1 
HETATM 1810 O O   . HOH   I 5 .   ? -12.855 -2.615  -14.912 1.00 41.72  ? 317 HOH   B O   1 
HETATM 1811 O O   . HOH   I 5 .   ? -20.491 -8.096  -5.335  1.00 69.58  ? 318 HOH   B O   1 
HETATM 1812 O O   . HOH   I 5 .   ? -15.399 8.932   -0.544  1.00 53.58  ? 319 HOH   B O   1 
HETATM 1813 O O   A HOH   I 5 .   ? -29.489 -1.157  -19.142 0.25 49.68  ? 320 HOH   B O   1 
HETATM 1814 O O   B HOH   I 5 .   ? -29.489 -1.157  -19.142 0.25 49.68  ? 320 HOH   B O   1 
HETATM 1815 O O   C HOH   I 5 .   ? -28.948 -2.291  -19.156 0.25 39.79  ? 320 HOH   B O   1 
HETATM 1816 O O   D HOH   I 5 .   ? -28.948 -2.291  -19.156 0.25 39.79  ? 320 HOH   B O   1 
HETATM 1817 O O   . HOH   I 5 .   ? -16.295 -7.395  -8.245  1.00 60.58  ? 321 HOH   B O   1 
HETATM 1818 O O   . HOH   I 5 .   ? -10.578 11.462  -19.093 1.00 48.42  ? 322 HOH   B O   1 
HETATM 1819 O O   A HOH   I 5 .   ? -34.958 4.388   -10.521 0.50 88.17  ? 323 HOH   B O   1 
HETATM 1820 O O   B HOH   I 5 .   ? -34.958 4.388   -10.521 0.50 88.17  ? 323 HOH   B O   1 
HETATM 1821 O O   . HOH   I 5 .   ? -14.045 -12.491 -16.380 1.00 56.87  ? 324 HOH   B O   1 
HETATM 1822 O O   . HOH   I 5 .   ? -9.190  -6.827  -25.391 1.00 63.29  ? 325 HOH   B O   1 
HETATM 1823 O O   A HOH   I 5 .   ? -21.854 -12.079 -13.073 0.50 87.69  ? 326 HOH   B O   1 
HETATM 1824 O O   B HOH   I 5 .   ? -21.854 -12.079 -13.073 0.50 87.69  ? 326 HOH   B O   1 
HETATM 1825 O O   A HOH   I 5 .   ? -11.347 -18.246 -27.460 0.50 72.36  ? 327 HOH   B O   1 
HETATM 1826 O O   B HOH   I 5 .   ? -11.347 -18.246 -27.460 0.50 72.36  ? 327 HOH   B O   1 
HETATM 1827 O O   . HOH   I 5 .   ? -15.613 -14.824 -16.745 1.00 57.30  ? 328 HOH   B O   1 
HETATM 1828 O O   . HOH   I 5 .   ? -10.056 7.545   -13.580 1.00 56.95  ? 329 HOH   B O   1 
HETATM 1829 O O   . HOH   I 5 .   ? -27.363 -6.688  -18.674 1.00 55.32  ? 330 HOH   B O   1 
HETATM 1830 O O   . HOH   I 5 .   ? -15.640 -14.461 -30.757 1.00 62.08  ? 331 HOH   B O   1 
HETATM 1831 O O   . HOH   I 5 .   ? -18.488 14.438  -22.201 1.00 55.16  ? 332 HOH   B O   1 
HETATM 1832 O O   A HOH   I 5 .   ? -18.405 24.812  -14.282 0.50 64.73  ? 333 HOH   B O   1 
HETATM 1833 O O   B HOH   I 5 .   ? -18.405 24.812  -14.282 0.50 64.73  ? 333 HOH   B O   1 
HETATM 1834 O O   A HOH   I 5 .   ? -7.861  -10.978 -7.007  0.50 77.50  ? 334 HOH   B O   1 
HETATM 1835 O O   B HOH   I 5 .   ? -7.861  -10.978 -7.007  0.50 77.50  ? 334 HOH   B O   1 
HETATM 1836 O O   A HOH   I 5 .   ? -9.292  6.341   -7.048  0.16 55.96  ? 335 HOH   B O   1 
HETATM 1837 O O   B HOH   I 5 .   ? -9.292  6.341   -7.048  0.16 55.96  ? 335 HOH   B O   1 
HETATM 1838 O O   . HOH   I 5 .   ? -14.667 16.026  -20.029 1.00 61.92  ? 336 HOH   B O   1 
HETATM 1839 O O   A HOH   I 5 .   ? -27.476 -7.270  -5.384  0.50 71.79  ? 337 HOH   B O   1 
HETATM 1840 O O   B HOH   I 5 .   ? -27.476 -7.270  -5.384  0.50 71.79  ? 337 HOH   B O   1 
HETATM 1841 O O   . HOH   I 5 .   ? -21.163 6.777   0.000   0.50 52.31  ? 338 HOH   B O   1 
HETATM 1842 O O   A HOH   I 5 .   ? -21.951 -14.255 -21.721 0.50 59.05  ? 339 HOH   B O   1 
HETATM 1843 O O   B HOH   I 5 .   ? -21.951 -14.255 -21.721 0.50 59.05  ? 339 HOH   B O   1 
HETATM 1844 O O   A HOH   I 5 .   ? -20.335 6.525   -32.588 0.50 77.00  ? 340 HOH   B O   1 
HETATM 1845 O O   B HOH   I 5 .   ? -20.335 6.525   -32.588 0.50 77.00  ? 340 HOH   B O   1 
HETATM 1846 O O   A HOH   I 5 .   ? -0.423  -0.176  -13.598 0.50 68.28  ? 341 HOH   B O   1 
HETATM 1847 O O   B HOH   I 5 .   ? -0.423  -0.176  -13.598 0.50 68.28  ? 341 HOH   B O   1 
HETATM 1848 O O   . HOH   I 5 .   ? -2.646  -11.991 -6.775  1.00 48.51  ? 342 HOH   B O   1 
HETATM 1849 O O   . HOH   I 5 .   ? -30.610 4.350   -2.542  1.00 61.09  ? 343 HOH   B O   1 
HETATM 1850 O O   A HOH   I 5 .   ? -19.410 -13.941 -22.626 0.50 66.83  ? 344 HOH   B O   1 
HETATM 1851 O O   B HOH   I 5 .   ? -19.410 -13.941 -22.626 0.50 66.83  ? 344 HOH   B O   1 
HETATM 1852 O O   A HOH   I 5 .   ? -12.171 2.214   -5.314  0.20 32.35  ? 345 HOH   B O   1 
HETATM 1853 O O   B HOH   I 5 .   ? -12.171 2.214   -5.314  0.20 32.35  ? 345 HOH   B O   1 
HETATM 1854 O O   A HOH   I 5 .   ? -19.936 24.190  -16.750 0.25 53.80  ? 346 HOH   B O   1 
HETATM 1855 O O   B HOH   I 5 .   ? -19.936 24.190  -16.750 0.25 53.80  ? 346 HOH   B O   1 
HETATM 1856 O O   C HOH   I 5 .   ? -9.297  44.302  -8.157  0.25 44.00  ? 346 HOH   B O   1 
HETATM 1857 O O   D HOH   I 5 .   ? -9.297  44.302  -8.157  0.25 44.00  ? 346 HOH   B O   1 
HETATM 1858 O O   A HOH   I 5 .   ? -33.939 -4.851  -17.957 0.50 86.96  ? 347 HOH   B O   1 
HETATM 1859 O O   B HOH   I 5 .   ? -33.939 -4.851  -17.957 0.50 86.96  ? 347 HOH   B O   1 
HETATM 1860 O O   A HOH   I 5 .   ? -10.818 -5.289  -8.221  0.50 65.49  ? 348 HOH   B O   1 
HETATM 1861 O O   B HOH   I 5 .   ? -10.818 -5.289  -8.221  0.50 65.49  ? 348 HOH   B O   1 
HETATM 1862 O O   . HOH   I 5 .   ? -16.788 14.552  -30.897 1.00 55.72  ? 349 HOH   B O   1 
HETATM 1863 O O   . HOH   I 5 .   ? -9.894  -19.187 -11.985 1.00 76.97  ? 350 HOH   B O   1 
HETATM 1864 O O   . HOH   I 5 .   ? -1.123  -14.768 -9.957  1.00 71.45  ? 351 HOH   B O   1 
HETATM 1865 O O   A HOH   I 5 .   ? -7.003  -6.456  0.687   0.50 90.76  ? 352 HOH   B O   1 
HETATM 1866 O O   B HOH   I 5 .   ? -7.003  -6.456  0.687   0.50 90.76  ? 352 HOH   B O   1 
HETATM 1867 O O   C HOH   I 5 .   ? -9.724  -16.537 -24.070 0.50 54.69  ? 353 HOH   B O   1 
HETATM 1868 O O   D HOH   I 5 .   ? -9.724  -16.537 -24.070 0.50 54.69  ? 353 HOH   B O   1 
HETATM 1869 O O   . HOH   I 5 .   ? -15.224 -5.071  1.464   1.00 51.52  ? 354 HOH   B O   1 
HETATM 1870 O O   A HOH   I 5 .   ? -19.558 -6.144  -0.803  0.50 60.58  ? 355 HOH   B O   1 
HETATM 1871 O O   B HOH   I 5 .   ? -19.558 -6.144  -0.803  0.50 60.58  ? 355 HOH   B O   1 
HETATM 1872 O O   A HOH   I 5 .   ? -17.921 17.838  -21.822 0.50 72.49  ? 356 HOH   B O   1 
HETATM 1873 O O   B HOH   I 5 .   ? -17.921 17.838  -21.822 0.50 72.49  ? 356 HOH   B O   1 
HETATM 1874 O O   A HOH   I 5 .   ? -25.571 -5.805  -4.173  0.50 55.64  ? 357 HOH   B O   1 
HETATM 1875 O O   B HOH   I 5 .   ? -25.571 -5.805  -4.173  0.50 55.64  ? 357 HOH   B O   1 
HETATM 1876 O O   A HOH   I 5 .   ? -30.088 -7.687  -6.257  0.50 77.59  ? 358 HOH   B O   1 
HETATM 1877 O O   B HOH   I 5 .   ? -30.088 -7.687  -6.257  0.50 77.59  ? 358 HOH   B O   1 
HETATM 1878 O O   A HOH   I 5 .   ? -16.719 15.872  -21.729 0.50 61.78  ? 359 HOH   B O   1 
HETATM 1879 O O   B HOH   I 5 .   ? -16.719 15.872  -21.729 0.50 61.78  ? 359 HOH   B O   1 
HETATM 1880 O O   A HOH   I 5 .   ? -30.208 -8.230  -4.391  0.50 132.36 ? 360 HOH   B O   1 
HETATM 1881 O O   B HOH   I 5 .   ? -30.208 -8.230  -4.391  0.50 132.36 ? 360 HOH   B O   1 
HETATM 1882 O O   . HOH   I 5 .   ? -23.797 -15.675 -17.611 1.00 63.22  ? 361 HOH   B O   1 
HETATM 1883 O O   C HOH   I 5 .   ? -8.810  4.752   -8.144  0.33 56.77  ? 362 HOH   B O   1 
HETATM 1884 O O   D HOH   I 5 .   ? -8.810  4.752   -8.144  0.33 56.77  ? 362 HOH   B O   1 
HETATM 1885 O O   A HOH   I 5 .   ? -9.780  -11.256 -7.934  0.50 69.18  ? 363 HOH   B O   1 
HETATM 1886 O O   B HOH   I 5 .   ? -9.780  -11.256 -7.934  0.50 69.18  ? 363 HOH   B O   1 
HETATM 1887 O O   A HOH   I 5 .   ? -29.967 -12.359 -27.058 0.25 99.51  ? 364 HOH   B O   1 
HETATM 1888 O O   B HOH   I 5 .   ? -29.967 -12.359 -27.058 0.25 99.51  ? 364 HOH   B O   1 
HETATM 1889 O O   C HOH   I 5 .   ? -18.149 -10.492 -6.688  0.50 72.49  ? 365 HOH   B O   1 
HETATM 1890 O O   D HOH   I 5 .   ? -18.149 -10.492 -6.688  0.50 72.49  ? 365 HOH   B O   1 
HETATM 1891 O O   A HOH   I 5 .   ? -19.344 -12.391 -13.322 0.50 68.03  ? 366 HOH   B O   1 
HETATM 1892 O O   B HOH   I 5 .   ? -19.344 -12.391 -13.322 0.50 68.03  ? 366 HOH   B O   1 
HETATM 1893 O O   . HOH   I 5 .   ? -29.108 -6.185  -1.035  1.00 53.94  ? 367 HOH   B O   1 
HETATM 1894 O O   . HOH   I 5 .   ? -11.291 -7.274  1.775   1.00 62.04  ? 368 HOH   B O   1 
HETATM 1895 O O   A HOH   I 5 .   ? -11.664 14.714  -14.656 0.50 69.84  ? 369 HOH   B O   1 
HETATM 1896 O O   B HOH   I 5 .   ? -11.664 14.714  -14.656 0.50 69.84  ? 369 HOH   B O   1 
HETATM 1897 O O   A HOH   I 5 .   ? -8.330  6.736   -9.496  0.16 39.03  ? 370 HOH   B O   1 
HETATM 1898 O O   B HOH   I 5 .   ? -8.330  6.736   -9.496  0.16 39.03  ? 370 HOH   B O   1 
HETATM 1899 O O   . HOH   I 5 .   ? -21.163 4.082   0.000   0.50 66.74  ? 371 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 0.9611 0.8476 0.9223 -0.0400 0.2061  -0.0129 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.9596 0.8534 0.9003 -0.0307 0.1941  -0.0114 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.9099 0.8082 0.8363 -0.0145 0.1872  0.0084  50  ASP   A C   
4    O O   . ASP   A 7   ? 0.9609 0.8521 0.8978 -0.0050 0.1936  0.0230  50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.9729 0.8605 0.9263 -0.0258 0.1967  -0.0180 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.0145 0.9055 0.9627 -0.0387 0.1952  -0.0383 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.0636 0.9476 1.0296 -0.0501 0.2055  -0.0524 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.9929 0.8927 0.9199 -0.0370 0.1848  -0.0403 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.8425 0.7516 0.7445 -0.0127 0.1753  0.0087  51  MET   A N   
10   C CA  . MET   A 8   ? 0.8232 0.7380 0.7084 0.0031  0.1671  0.0242  51  MET   A CA  
11   C C   . MET   A 8   ? 0.7886 0.7030 0.6721 0.0152  0.1616  0.0245  51  MET   A C   
12   O O   . MET   A 8   ? 0.7792 0.6936 0.6673 0.0080  0.1610  0.0098  51  MET   A O   
13   C CB  . MET   A 8   ? 0.8165 0.7428 0.6784 -0.0011 0.1570  0.0222  51  MET   A CB  
14   C CG  . MET   A 8   ? 0.8325 0.7617 0.6977 -0.0122 0.1606  0.0213  51  MET   A CG  
15   S SD  . MET   A 8   ? 0.8496 0.7924 0.6890 -0.0146 0.1478  0.0208  51  MET   A SD  
16   C CE  . MET   A 8   ? 0.8502 0.7966 0.7023 -0.0243 0.1539  0.0225  51  MET   A CE  
17   N N   . TYR   A 9   ? 0.7502 0.6650 0.6276 0.0325  0.1580  0.0401  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.7392 0.6563 0.6145 0.0466  0.1506  0.0423  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.7267 0.6524 0.5783 0.0598  0.1405  0.0540  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.7078 0.6350 0.5486 0.0607  0.1418  0.0635  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.7545 0.6609 0.6519 0.0560  0.1579  0.0491  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.7784 0.6765 0.6783 0.0651  0.1650  0.0681  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.7898 0.6795 0.7025 0.0544  0.1774  0.0691  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.8018 0.7006 0.6901 0.0840  0.1596  0.0849  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.8111 0.6921 0.7268 0.0621  0.1857  0.0869  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.8189 0.7087 0.7072 0.0924  0.1675  0.1035  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.8258 0.7060 0.7286 0.0812  0.1812  0.1047  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.8577 0.7280 0.7614 0.0884  0.1908  0.1229  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.7284 0.6606 0.5731 0.0690  0.1306  0.0510  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.7304 0.6717 0.5526 0.0818  0.1199  0.0592  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.7521 0.6920 0.5773 0.1007  0.1168  0.0713  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.7441 0.6794 0.5894 0.1032  0.1191  0.0679  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.7116 0.6627 0.5214 0.0766  0.1101  0.0455  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.7063 0.6587 0.5306 0.0745  0.1080  0.0318  53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.7146 0.6667 0.5160 0.0610  0.1121  0.0385  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.7014 0.6637 0.5129 0.0747  0.0976  0.0218  53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.7693 0.7128 0.5752 0.1135  0.1124  0.0852  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.7733 0.7184 0.5727 0.1333  0.1059  0.0974  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.7447 0.7021 0.5175 0.1410  0.0943  0.0979  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.7033 0.6627 0.4609 0.1365  0.0964  0.1008  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.8176 0.7513 0.6174 0.1422  0.1153  0.1173  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.8418 0.7615 0.6672 0.1335  0.1292  0.1181  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.8972 0.8043 0.7222 0.1436  0.1390  0.1393  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 0.9094 0.8178 0.7143 0.1480  0.1406  0.1510  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 0.9725 0.8679 0.8176 0.1473  0.1457  0.1443  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.7459 0.7123 0.5158 0.1513  0.0824  0.0932  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.7539 0.7325 0.4998 0.1603  0.0706  0.0926  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.7676 0.7436 0.4922 0.1721  0.0730  0.1114  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.7903 0.7571 0.5197 0.1809  0.0788  0.1264  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.7654 0.7538 0.5157 0.1714  0.0578  0.0860  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.7714 0.7736 0.5055 0.1724  0.0460  0.0748  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.7826 0.7956 0.5298 0.1773  0.0347  0.0617  55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.7926 0.8181 0.5261 0.1772  0.0244  0.0498  55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.8114 0.8445 0.5210 0.1889  0.0163  0.0555  55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.8430 0.8722 0.5379 0.2016  0.0177  0.0738  55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.7914 0.8351 0.4909 0.1876  0.0079  0.0429  55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.7652 0.7481 0.4680 0.1717  0.0700  0.1107  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.7737 0.7559 0.4531 0.1817  0.0728  0.1262  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.7688 0.7638 0.4241 0.1926  0.0602  0.1229  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.7828 0.7779 0.4170 0.2005  0.0629  0.1343  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.7614 0.7394 0.4392 0.1700  0.0839  0.1285  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.7528 0.7582 0.4111 0.1926  0.0479  0.1075  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.7653 0.7833 0.4018 0.2026  0.0360  0.1028  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.7669 0.7943 0.4086 0.1943  0.0274  0.0821  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.7404 0.7634 0.3997 0.1791  0.0323  0.0724  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.7782 0.8177 0.4041 0.2033  0.0157  0.0755  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.7905 0.8393 0.4180 0.1968  0.0075  0.0558  58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.8039 0.8500 0.4189 0.1884  0.0134  0.0539  58  ASP   A C   
69   O O   . ASP   A 15  ? 0.8093 0.8505 0.4103 0.1921  0.0209  0.0678  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.7965 0.8597 0.4125 0.2094  -0.0069 0.0484  58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.8231 0.8921 0.4545 0.2181  -0.0155 0.0474  58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.8123 0.8730 0.4642 0.2133  -0.0090 0.0515  58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.8427 0.9249 0.4664 0.2297  -0.0287 0.0422  58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.8002 0.8486 0.4215 0.1776  0.0108  0.0380  59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.8121 0.8590 0.4215 0.1714  0.0141  0.0346  59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.8050 0.8628 0.3993 0.1797  0.0042  0.0250  59  ILE   A C   
77   O O   . ILE   A 16  ? 0.7926 0.8559 0.3956 0.1759  -0.0028 0.0090  59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.8119 0.8520 0.4355 0.1546  0.0188  0.0254  59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.8273 0.8573 0.4604 0.1471  0.0294  0.0362  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.8119 0.8522 0.4246 0.1502  0.0185  0.0188  59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.8098 0.8338 0.4597 0.1321  0.0326  0.0271  59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.8167 0.8772 0.3895 0.1903  0.0049  0.0342  60  THR   A N   
83   N N   B THR   A 17  ? 0.8165 0.8775 0.3893 0.1906  0.0045  0.0338  60  THR   A N   
84   N N   C THR   A 17  ? 0.8167 0.8772 0.3895 0.1903  0.0049  0.0342  60  THR   A N   
85   N N   D THR   A 17  ? 0.8165 0.8775 0.3893 0.1906  0.0045  0.0338  60  THR   A N   
86   C CA  A THR   A 17  ? 0.8349 0.9063 0.3883 0.2011  -0.0037 0.0277  60  THR   A CA  
87   C CA  B THR   A 17  ? 0.8323 0.9042 0.3872 0.2001  -0.0045 0.0253  60  THR   A CA  
88   C CA  C THR   A 17  ? 0.8349 0.9063 0.3883 0.2011  -0.0037 0.0277  60  THR   A CA  
89   C CA  D THR   A 17  ? 0.8323 0.9042 0.3872 0.2001  -0.0045 0.0253  60  THR   A CA  
90   C C   A THR   A 17  ? 0.8414 0.9108 0.3752 0.2034  0.0033  0.0338  60  THR   A C   
91   C C   B THR   A 17  ? 0.8429 0.9132 0.3763 0.2044  0.0021  0.0333  60  THR   A C   
92   C C   C THR   A 17  ? 0.8414 0.9108 0.3752 0.2034  0.0033  0.0338  60  THR   A C   
93   C C   D THR   A 17  ? 0.8429 0.9132 0.3763 0.2044  0.0021  0.0333  60  THR   A C   
94   O O   A THR   A 17  ? 0.8381 0.9006 0.3665 0.2051  0.0135  0.0505  60  THR   A O   
95   O O   B THR   A 17  ? 0.8431 0.9076 0.3693 0.2083  0.0111  0.0506  60  THR   A O   
96   O O   C THR   A 17  ? 0.8381 0.9006 0.3665 0.2051  0.0135  0.0505  60  THR   A O   
97   O O   D THR   A 17  ? 0.8431 0.9076 0.3693 0.2083  0.0111  0.0506  60  THR   A O   
98   C CB  A THR   A 17  ? 0.8514 0.9300 0.3948 0.2166  -0.0112 0.0354  60  THR   A CB  
99   C CB  B THR   A 17  ? 0.8443 0.9258 0.3946 0.2138  -0.0151 0.0267  60  THR   A CB  
100  C CB  C THR   A 17  ? 0.8514 0.9300 0.3948 0.2166  -0.0112 0.0354  60  THR   A CB  
101  C CB  D THR   A 17  ? 0.8443 0.9258 0.3946 0.2138  -0.0151 0.0267  60  THR   A CB  
102  O OG1 A THR   A 17  ? 0.8535 0.9238 0.3882 0.2216  -0.0016 0.0557  60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.8232 0.9081 0.3970 0.2085  -0.0215 0.0151  60  THR   A OG1 
104  O OG1 C THR   A 17  ? 0.8535 0.9238 0.3882 0.2216  -0.0016 0.0557  60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.8232 0.9081 0.3970 0.2085  -0.0215 0.0151  60  THR   A OG1 
106  C CG2 A THR   A 17  ? 0.8479 0.9306 0.4120 0.2167  -0.0192 0.0292  60  THR   A CG2 
107  C CG2 B THR   A 17  ? 0.8609 0.9545 0.3892 0.2249  -0.0246 0.0198  60  THR   A CG2 
108  C CG2 C THR   A 17  ? 0.8479 0.9306 0.4120 0.2167  -0.0192 0.0292  60  THR   A CG2 
109  C CG2 D THR   A 17  ? 0.8609 0.9545 0.3892 0.2249  -0.0246 0.0198  60  THR   A CG2 
110  N N   . TRP   A 18  ? 0.8491 0.9240 0.3740 0.2034  -0.0009 0.0207  61  TRP   A N   
111  C CA  . TRP   A 18  ? 0.9225 0.9986 0.4260 0.2095  0.0040  0.0249  61  TRP   A CA  
112  C C   . TRP   A 18  ? 1.0152 1.0985 0.4964 0.2252  0.0000  0.0333  61  TRP   A C   
113  O O   . TRP   A 18  ? 1.0366 1.1294 0.5151 0.2319  -0.0123 0.0250  61  TRP   A O   
114  C CB  . TRP   A 18  ? 0.9443 1.0242 0.4453 0.2061  0.0002  0.0075  61  TRP   A CB  
115  C CG  . TRP   A 18  ? 0.9691 1.0494 0.4517 0.2111  0.0067  0.0102  61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 0.9800 1.0685 0.4387 0.2231  0.0043  0.0096  61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 0.9683 1.0413 0.4556 0.2042  0.0168  0.0130  61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 0.9786 1.0645 0.4274 0.2238  0.0136  0.0119  61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 0.9827 1.0597 0.4500 0.2126  0.0210  0.0137  61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 0.9317 0.9957 0.4376 0.1921  0.0223  0.0147  61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 0.9923 1.0650 0.4611 0.2094  0.0307  0.0159  61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 0.9357 0.9960 0.4418 0.1895  0.0305  0.0176  61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 0.9295 0.9942 0.4190 0.1980  0.0348  0.0179  61  TRP   A CH2 
124  N N   . GLU   A 19  ? 1.0972 1.1761 0.5639 0.2310  0.0096  0.0500  62  GLU   A N   
125  C CA  . GLU   A 19  ? 1.1970 1.2805 0.6385 0.2463  0.0073  0.0607  62  GLU   A CA  
126  C C   . GLU   A 19  ? 1.2069 1.2946 0.6234 0.2520  0.0114  0.0583  62  GLU   A C   
127  O O   . GLU   A 19  ? 1.1766 1.2576 0.5904 0.2491  0.0251  0.0675  62  GLU   A O   
128  C CB  . GLU   A 19  ? 1.2937 1.3676 0.7356 0.2493  0.0170  0.0826  62  GLU   A CB  
129  C CG  . GLU   A 19  ? 1.3777 1.4466 0.8454 0.2437  0.0145  0.0849  62  GLU   A CG  
130  C CD  . GLU   A 19  ? 1.4171 1.4944 0.8864 0.2521  -0.0005 0.0792  62  GLU   A CD  
131  O OE1 . GLU   A 19  ? 1.5064 1.5887 0.9534 0.2667  -0.0060 0.0871  62  GLU   A OE1 
132  O OE2 . GLU   A 19  ? 1.4312 1.5105 0.9240 0.2441  -0.0068 0.0669  62  GLU   A OE2 
133  N N   A LYS   A 20  ? 1.2263 1.3254 0.6260 0.2599  0.0002  0.0456  63  LYS   A N   
134  N N   B LYS   A 20  ? 1.2263 1.3254 0.6260 0.2599  0.0002  0.0456  63  LYS   A N   
135  N N   C LYS   A 20  ? 1.2158 1.3149 0.6166 0.2593  0.0000  0.0448  63  LYS   A N   
136  N N   D LYS   A 20  ? 1.2158 1.3149 0.6166 0.2593  0.0000  0.0448  63  LYS   A N   
137  C CA  A LYS   A 20  ? 1.2440 1.3481 0.6181 0.2659  0.0033  0.0404  63  LYS   A CA  
138  C CA  B LYS   A 20  ? 1.2440 1.3481 0.6181 0.2659  0.0033  0.0404  63  LYS   A CA  
139  C CA  C LYS   A 20  ? 1.2292 1.3339 0.6028 0.2664  0.0024  0.0402  63  LYS   A CA  
140  C CA  D LYS   A 20  ? 1.2292 1.3339 0.6028 0.2664  0.0024  0.0402  63  LYS   A CA  
141  C C   A LYS   A 20  ? 1.2371 1.3370 0.5869 0.2754  0.0141  0.0609  63  LYS   A C   
142  C C   B LYS   A 20  ? 1.2371 1.3370 0.5869 0.2754  0.0141  0.0609  63  LYS   A C   
143  C C   C LYS   A 20  ? 1.2300 1.3302 0.5797 0.2761  0.0128  0.0611  63  LYS   A C   
144  C C   D LYS   A 20  ? 1.2300 1.3302 0.5797 0.2761  0.0128  0.0611  63  LYS   A C   
145  O O   A LYS   A 20  ? 1.2577 1.3554 0.6022 0.2825  0.0118  0.0751  63  LYS   A O   
146  O O   B LYS   A 20  ? 1.2577 1.3554 0.6022 0.2825  0.0118  0.0751  63  LYS   A O   
147  O O   C LYS   A 20  ? 1.2577 1.3565 0.6022 0.2834  0.0096  0.0745  63  LYS   A O   
148  O O   D LYS   A 20  ? 1.2577 1.3565 0.6022 0.2834  0.0096  0.0745  63  LYS   A O   
149  C CB  A LYS   A 20  ? 1.2753 1.3934 0.6367 0.2726  -0.0121 0.0222  63  LYS   A CB  
150  C CB  B LYS   A 20  ? 1.2753 1.3934 0.6367 0.2726  -0.0121 0.0222  63  LYS   A CB  
151  C CB  C LYS   A 20  ? 1.2496 1.3684 0.6104 0.2737  -0.0136 0.0228  63  LYS   A CB  
152  C CB  D LYS   A 20  ? 1.2496 1.3684 0.6104 0.2737  -0.0136 0.0228  63  LYS   A CB  
153  C CG  A LYS   A 20  ? 1.3047 1.4271 0.6557 0.2713  -0.0100 0.0062  63  LYS   A CG  
154  C CG  B LYS   A 20  ? 1.3047 1.4271 0.6557 0.2713  -0.0100 0.0062  63  LYS   A CG  
155  C CG  C LYS   A 20  ? 1.2493 1.3724 0.6181 0.2664  -0.0166 0.0001  63  LYS   A CG  
156  C CG  D LYS   A 20  ? 1.2493 1.3724 0.6181 0.2664  -0.0166 0.0001  63  LYS   A CG  
157  C CD  A LYS   A 20  ? 1.3277 1.4627 0.6783 0.2727  -0.0252 -0.0168 63  LYS   A CD  
158  C CD  B LYS   A 20  ? 1.3277 1.4627 0.6783 0.2727  -0.0252 -0.0168 63  LYS   A CD  
159  C CD  C LYS   A 20  ? 1.2809 1.4081 0.6238 0.2722  -0.0117 -0.0058 63  LYS   A CD  
160  C CD  D LYS   A 20  ? 1.2809 1.4081 0.6238 0.2722  -0.0117 -0.0058 63  LYS   A CD  
161  C CE  A LYS   A 20  ? 1.3431 1.4791 0.6914 0.2683  -0.0213 -0.0341 63  LYS   A CE  
162  C CE  B LYS   A 20  ? 1.3431 1.4791 0.6914 0.2683  -0.0213 -0.0341 63  LYS   A CE  
163  C CE  C LYS   A 20  ? 1.2699 1.3966 0.6254 0.2634  -0.0102 -0.0253 63  LYS   A CE  
164  C CE  D LYS   A 20  ? 1.2699 1.3966 0.6254 0.2634  -0.0102 -0.0253 63  LYS   A CE  
165  N NZ  A LYS   A 20  ? 1.3477 1.4927 0.7075 0.2648  -0.0343 -0.0581 63  LYS   A NZ  
166  N NZ  B LYS   A 20  ? 1.3477 1.4927 0.7075 0.2648  -0.0343 -0.0581 63  LYS   A NZ  
167  N NZ  C LYS   A 20  ? 1.2611 1.3943 0.6339 0.2584  -0.0239 -0.0448 63  LYS   A NZ  
168  N NZ  D LYS   A 20  ? 1.2611 1.3943 0.6339 0.2584  -0.0239 -0.0448 63  LYS   A NZ  
169  N N   A ASP   A 21  ? 1.2230 1.3205 0.5605 0.2752  0.0266  0.0629  64  ASP   A N   
170  N N   B ASP   A 21  ? 1.2230 1.3205 0.5605 0.2752  0.0266  0.0629  64  ASP   A N   
171  N N   C ASP   A 21  ? 1.2187 1.3159 0.5565 0.2757  0.0260  0.0644  64  ASP   A N   
172  N N   D ASP   A 21  ? 1.2187 1.3159 0.5565 0.2757  0.0260  0.0644  64  ASP   A N   
173  C CA  A ASP   A 21  ? 1.2503 1.3424 0.5663 0.2824  0.0408  0.0823  64  ASP   A CA  
174  C CA  B ASP   A 21  ? 1.2503 1.3424 0.5663 0.2824  0.0408  0.0823  64  ASP   A CA  
175  C CA  C ASP   A 21  ? 1.2504 1.3423 0.5657 0.2836  0.0392  0.0842  64  ASP   A CA  
176  C CA  D ASP   A 21  ? 1.2504 1.3423 0.5657 0.2836  0.0392  0.0842  64  ASP   A CA  
177  C C   A ASP   A 21  ? 1.2156 1.2959 0.5509 0.2772  0.0500  0.1008  64  ASP   A C   
178  C C   B ASP   A 21  ? 1.2156 1.2959 0.5509 0.2772  0.0500  0.1008  64  ASP   A C   
179  C C   C ASP   A 21  ? 1.2142 1.2940 0.5504 0.2772  0.0498  0.1020  64  ASP   A C   
180  C C   D ASP   A 21  ? 1.2142 1.2940 0.5504 0.2772  0.0498  0.1020  64  ASP   A C   
181  O O   A ASP   A 21  ? 1.2408 1.3175 0.5649 0.2853  0.0496  0.1162  64  ASP   A O   
182  O O   B ASP   A 21  ? 1.2408 1.3175 0.5649 0.2853  0.0496  0.1162  64  ASP   A O   
183  O O   C ASP   A 21  ? 1.2382 1.3135 0.5652 0.2846  0.0504  0.1181  64  ASP   A O   
184  O O   D ASP   A 21  ? 1.2382 1.3135 0.5652 0.2846  0.0504  0.1181  64  ASP   A O   
185  C CB  A ASP   A 21  ? 1.3028 1.4016 0.5822 0.2979  0.0339  0.0868  64  ASP   A CB  
186  C CB  B ASP   A 21  ? 1.3028 1.4016 0.5822 0.2979  0.0339  0.0868  64  ASP   A CB  
187  C CB  C ASP   A 21  ? 1.3000 1.3981 0.5826 0.2990  0.0305  0.0901  64  ASP   A CB  
188  C CB  D ASP   A 21  ? 1.3000 1.3981 0.5826 0.2990  0.0305  0.0901  64  ASP   A CB  
189  C CG  A ASP   A 21  ? 1.3297 1.4384 0.5832 0.3035  0.0317  0.0719  64  ASP   A CG  
190  C CG  B ASP   A 21  ? 1.3297 1.4384 0.5832 0.3035  0.0317  0.0719  64  ASP   A CG  
191  C CG  C ASP   A 21  ? 1.3290 1.4403 0.5879 0.3058  0.0201  0.0719  64  ASP   A CG  
192  C CG  D ASP   A 21  ? 1.3290 1.4403 0.5879 0.3058  0.0201  0.0719  64  ASP   A CG  
193  O OD1 A ASP   A 21  ? 1.3370 1.4426 0.5793 0.3032  0.0467  0.0750  64  ASP   A OD1 
194  O OD1 B ASP   A 21  ? 1.3370 1.4426 0.5793 0.3032  0.0467  0.0750  64  ASP   A OD1 
195  O OD1 C ASP   A 21  ? 1.3462 1.4585 0.5899 0.3062  0.0299  0.0675  64  ASP   A OD1 
196  O OD1 D ASP   A 21  ? 1.3462 1.4585 0.5899 0.3062  0.0299  0.0675  64  ASP   A OD1 
197  O OD2 A ASP   A 21  ? 1.3499 1.4698 0.5955 0.3080  0.0153  0.0564  64  ASP   A OD2 
198  O OD2 B ASP   A 21  ? 1.3499 1.4698 0.5955 0.3080  0.0153  0.0564  64  ASP   A OD2 
199  O OD2 C ASP   A 21  ? 1.3364 1.4575 0.5935 0.3106  0.0024  0.0615  64  ASP   A OD2 
200  O OD2 D ASP   A 21  ? 1.3364 1.4575 0.5935 0.3106  0.0024  0.0615  64  ASP   A OD2 
201  N N   A ALA   A 22  ? 1.1693 1.2439 0.5328 0.2641  0.0574  0.0989  65  ALA   A N   
202  N N   B ALA   A 22  ? 1.1693 1.2439 0.5328 0.2641  0.0574  0.0989  65  ALA   A N   
203  N N   C ALA   A 22  ? 1.1693 1.2438 0.5327 0.2642  0.0574  0.0991  65  ALA   A N   
204  N N   D ALA   A 22  ? 1.1693 1.2438 0.5327 0.2642  0.0574  0.0991  65  ALA   A N   
205  C CA  A ALA   A 22  ? 1.1286 1.1925 0.5125 0.2567  0.0691  0.1140  65  ALA   A CA  
206  C CA  B ALA   A 22  ? 1.1286 1.1925 0.5125 0.2567  0.0691  0.1140  65  ALA   A CA  
207  C CA  C ALA   A 22  ? 1.1282 1.1921 0.5124 0.2567  0.0692  0.1140  65  ALA   A CA  
208  C CA  D ALA   A 22  ? 1.1282 1.1921 0.5124 0.2567  0.0692  0.1140  65  ALA   A CA  
209  C C   A ALA   A 22  ? 1.1110 1.1718 0.4935 0.2539  0.0865  0.1206  65  ALA   A C   
210  C C   B ALA   A 22  ? 1.1110 1.1718 0.4935 0.2539  0.0865  0.1206  65  ALA   A C   
211  C C   C ALA   A 22  ? 1.1108 1.1716 0.4934 0.2539  0.0865  0.1206  65  ALA   A C   
212  C C   D ALA   A 22  ? 1.1108 1.1716 0.4934 0.2539  0.0865  0.1206  65  ALA   A C   
213  O O   A ALA   A 22  ? 1.1035 1.1703 0.4767 0.2550  0.0878  0.1098  65  ALA   A O   
214  O O   B ALA   A 22  ? 1.1035 1.1703 0.4767 0.2550  0.0878  0.1098  65  ALA   A O   
215  O O   C ALA   A 22  ? 1.1033 1.1701 0.4767 0.2549  0.0878  0.1097  65  ALA   A O   
216  O O   D ALA   A 22  ? 1.1033 1.1701 0.4767 0.2549  0.0878  0.1097  65  ALA   A O   
217  C CB  A ALA   A 22  ? 1.1074 1.1689 0.5235 0.2439  0.0636  0.1053  65  ALA   A CB  
218  C CB  B ALA   A 22  ? 1.1074 1.1689 0.5235 0.2439  0.0636  0.1053  65  ALA   A CB  
219  C CB  C ALA   A 22  ? 1.1072 1.1686 0.5234 0.2438  0.0635  0.1052  65  ALA   A CB  
220  C CB  D ALA   A 22  ? 1.1072 1.1686 0.5234 0.2438  0.0635  0.1052  65  ALA   A CB  
221  N N   . GLU   A 23  ? 1.0994 1.1515 0.4933 0.2501  0.0998  0.1367  66  GLU   A N   
222  C CA  . GLU   A 23  ? 1.1013 1.1510 0.4982 0.2469  0.1178  0.1439  66  GLU   A CA  
223  C C   . GLU   A 23  ? 1.0557 1.1095 0.4756 0.2363  0.1179  0.1303  66  GLU   A C   
224  O O   . GLU   A 23  ? 0.9380 0.9895 0.3839 0.2259  0.1124  0.1257  66  GLU   A O   
225  C CB  . GLU   A 23  ? 1.1731 1.2126 0.5834 0.2432  0.1302  0.1620  66  GLU   A CB  
226  C CG  . GLU   A 23  ? 1.2326 1.2703 0.6537 0.2377  0.1489  0.1687  66  GLU   A CG  
227  C CD  . GLU   A 23  ? 1.3119 1.3403 0.7567 0.2299  0.1594  0.1817  66  GLU   A CD  
228  O OE1 . GLU   A 23  ? 1.3408 1.3620 0.7872 0.2315  0.1545  0.1891  66  GLU   A OE1 
229  O OE2 . GLU   A 23  ? 1.3498 1.3788 0.8135 0.2220  0.1722  0.1834  66  GLU   A OE2 
230  N N   . VAL   A 24  ? 1.0153 1.0746 0.4258 0.2389  0.1239  0.1239  67  VAL   A N   
231  C CA  . VAL   A 24  ? 0.9964 1.0598 0.4265 0.2311  0.1229  0.1105  67  VAL   A CA  
232  C C   . VAL   A 24  ? 0.9962 1.0589 0.4421 0.2264  0.1397  0.1186  67  VAL   A C   
233  O O   . VAL   A 24  ? 1.0028 1.0663 0.4329 0.2328  0.1529  0.1263  67  VAL   A O   
234  C CB  . VAL   A 24  ? 1.0090 1.0792 0.4218 0.2372  0.1172  0.0950  67  VAL   A CB  
235  C CG1 . VAL   A 24  ? 0.9821 1.0544 0.4165 0.2299  0.1168  0.0830  67  VAL   A CG1 
236  C CG2 . VAL   A 24  ? 1.0176 1.0904 0.4159 0.2419  0.1006  0.0856  67  VAL   A CG2 
237  N N   . THR   A 25  ? 0.9576 1.0195 0.4338 0.2155  0.1392  0.1167  68  THR   A N   
238  C CA  . THR   A 25  ? 0.9554 1.0175 0.4530 0.2095  0.1535  0.1252  68  THR   A CA  
239  C C   . THR   A 25  ? 0.9450 1.0090 0.4724 0.1986  0.1468  0.1171  68  THR   A C   
240  O O   . THR   A 25  ? 0.9109 0.9742 0.4391 0.1962  0.1324  0.1064  68  THR   A O   
241  C CB  . THR   A 25  ? 0.9758 1.0308 0.4744 0.2085  0.1625  0.1415  68  THR   A CB  
242  O OG1 . THR   A 25  ? 0.9920 1.0484 0.5074 0.2043  0.1791  0.1492  68  THR   A OG1 
243  C CG2 . THR   A 25  ? 0.9671 1.0165 0.4818 0.2007  0.1531  0.1425  68  THR   A CG2 
244  N N   . GLY   A 26  ? 0.9406 1.0073 0.4910 0.1925  0.1571  0.1221  69  GLY   A N   
245  C CA  . GLY   A 26  ? 0.9296 0.9999 0.5087 0.1830  0.1524  0.1160  69  GLY   A CA  
246  C C   . GLY   A 26  ? 0.9279 1.0039 0.5085 0.1861  0.1483  0.1044  69  GLY   A C   
247  O O   . GLY   A 26  ? 0.9739 1.0489 0.5339 0.1929  0.1422  0.0964  69  GLY   A O   
248  N N   . ASN   A 27  ? 0.9340 1.0157 0.5411 0.1804  0.1501  0.1027  70  ASN   A N   
249  C CA  . ASN   A 27  ? 0.9299 1.0167 0.5464 0.1824  0.1464  0.0929  70  ASN   A CA  
250  C C   . ASN   A 27  ? 0.8833 0.9657 0.5073 0.1761  0.1298  0.0855  70  ASN   A C   
251  O O   . ASN   A 27  ? 0.8527 0.9283 0.4692 0.1717  0.1220  0.0864  70  ASN   A O   
252  C CB  . ASN   A 27  ? 0.9529 1.0490 0.5942 0.1810  0.1579  0.0964  70  ASN   A CB  
253  C CG  . ASN   A 27  ? 0.9753 1.0737 0.6435 0.1702  0.1540  0.1001  70  ASN   A CG  
254  O OD1 . ASN   A 27  ? 0.9883 1.0825 0.6562 0.1647  0.1552  0.1069  70  ASN   A OD1 
255  N ND2 . ASN   A 27  ? 1.0065 1.1113 0.6976 0.1672  0.1483  0.0953  70  ASN   A ND2 
256  N N   . SER   A 28  ? 0.8542 0.9393 0.4914 0.1763  0.1250  0.0785  71  SER   A N   
257  C CA  . SER   A 28  ? 0.8580 0.9373 0.4989 0.1720  0.1104  0.0713  71  SER   A CA  
258  C C   . SER   A 28  ? 0.8499 0.9342 0.5165 0.1686  0.1073  0.0711  71  SER   A C   
259  O O   . SER   A 28  ? 0.8613 0.9446 0.5311 0.1727  0.1034  0.0647  71  SER   A O   
260  C CB  . SER   A 28  ? 0.8848 0.9592 0.5089 0.1787  0.1061  0.0611  71  SER   A CB  
261  O OG  . SER   A 28  ? 0.9464 1.0194 0.5466 0.1841  0.1094  0.0603  71  SER   A OG  
262  N N   . PRO   A 29  ? 0.8497 0.9398 0.5362 0.1614  0.1085  0.0777  72  PRO   A N   
263  C CA  . PRO   A 29  ? 0.8623 0.9601 0.5745 0.1593  0.1049  0.0775  72  PRO   A CA  
264  C C   . PRO   A 29  ? 0.8337 0.9245 0.5469 0.1551  0.0894  0.0735  72  PRO   A C   
265  O O   . PRO   A 29  ? 0.7904 0.8721 0.4904 0.1493  0.0825  0.0728  72  PRO   A O   
266  C CB  . PRO   A 29  ? 0.8605 0.9666 0.5914 0.1519  0.1105  0.0846  72  PRO   A CB  
267  C CG  . PRO   A 29  ? 0.8586 0.9560 0.5726 0.1467  0.1106  0.0878  72  PRO   A CG  
268  C CD  . PRO   A 29  ? 0.8601 0.9499 0.5468 0.1549  0.1125  0.0849  72  PRO   A CD  
269  N N   . ARG   A 30  ? 0.8748 0.9689 0.6022 0.1590  0.0851  0.0710  73  ARG   A N   
270  C CA  . ARG   A 30  ? 0.9276 1.0166 0.6609 0.1552  0.0709  0.0700  73  ARG   A CA  
271  C C   . ARG   A 30  ? 0.8911 0.9912 0.6473 0.1485  0.0669  0.0750  73  ARG   A C   
272  O O   . ARG   A 30  ? 0.8629 0.9763 0.6414 0.1525  0.0720  0.0763  73  ARG   A O   
273  C CB  . ARG   A 30  ? 0.9783 1.0642 0.7157 0.1640  0.0682  0.0655  73  ARG   A CB  
274  C CG  . ARG   A 30  ? 1.0551 1.1282 0.7701 0.1686  0.0689  0.0585  73  ARG   A CG  
275  C CD  . ARG   A 30  ? 1.1678 1.2396 0.8879 0.1788  0.0720  0.0527  73  ARG   A CD  
276  N NE  . ARG   A 30  ? 1.2563 1.3197 0.9553 0.1833  0.0764  0.0445  73  ARG   A NE  
277  C CZ  . ARG   A 30  ? 1.2767 1.3261 0.9621 0.1821  0.0698  0.0385  73  ARG   A CZ  
278  N NH1 . ARG   A 30  ? 1.3162 1.3564 1.0047 0.1767  0.0592  0.0410  73  ARG   A NH1 
279  N NH2 . ARG   A 30  ? 1.2362 1.2811 0.9046 0.1861  0.0739  0.0298  73  ARG   A NH2 
280  N N   . LEU   A 31  ? 0.8459 0.9419 0.5978 0.1383  0.0590  0.0767  74  LEU   A N   
281  C CA  . LEU   A 31  ? 0.8358 0.9430 0.6080 0.1304  0.0551  0.0799  74  LEU   A CA  
282  C C   . LEU   A 31  ? 0.8021 0.9045 0.5728 0.1250  0.0391  0.0797  74  LEU   A C   
283  O O   . LEU   A 31  ? 0.7631 0.8507 0.5125 0.1219  0.0334  0.0780  74  LEU   A O   
284  C CB  . LEU   A 31  ? 0.8466 0.9540 0.6153 0.1224  0.0622  0.0819  74  LEU   A CB  
285  C CG  . LEU   A 31  ? 0.8462 0.9585 0.6167 0.1271  0.0784  0.0843  74  LEU   A CG  
286  C CD1 . LEU   A 31  ? 0.8450 0.9532 0.6090 0.1195  0.0841  0.0872  74  LEU   A CD1 
287  C CD2 . LEU   A 31  ? 0.8464 0.9752 0.6448 0.1300  0.0857  0.0860  74  LEU   A CD2 
288  N N   . ASP   A 32  ? 0.8031 0.9180 0.5959 0.1245  0.0324  0.0814  75  ASP   A N   
289  C CA  . ASP   A 32  ? 0.7978 0.9113 0.5907 0.1192  0.0166  0.0824  75  ASP   A CA  
290  C C   . ASP   A 32  ? 0.7709 0.8879 0.5640 0.1062  0.0147  0.0820  75  ASP   A C   
291  O O   . ASP   A 32  ? 0.7517 0.8844 0.5673 0.1030  0.0194  0.0820  75  ASP   A O   
292  C CB  . ASP   A 32  ? 0.8352 0.9631 0.6536 0.1252  0.0095  0.0841  75  ASP   A CB  
293  C CG  . ASP   A 32  ? 0.8807 1.0014 0.6974 0.1371  0.0064  0.0847  75  ASP   A CG  
294  O OD1 . ASP   A 32  ? 0.9028 1.0050 0.6959 0.1379  0.0033  0.0843  75  ASP   A OD1 
295  O OD2 . ASP   A 32  ? 0.9370 1.0708 0.7781 0.1452  0.0077  0.0851  75  ASP   A OD2 
296  N N   . VAL   A 33  ? 0.7598 0.8626 0.5303 0.0987  0.0090  0.0808  76  VAL   A N   
297  C CA  . VAL   A 33  ? 0.7586 0.8622 0.5266 0.0858  0.0082  0.0789  76  VAL   A CA  
298  C C   . VAL   A 33  ? 0.7510 0.8475 0.5055 0.0786  -0.0059 0.0783  76  VAL   A C   
299  O O   . VAL   A 33  ? 0.7417 0.8254 0.4795 0.0828  -0.0124 0.0798  76  VAL   A O   
300  C CB  . VAL   A 33  ? 0.7436 0.8370 0.4972 0.0825  0.0192  0.0773  76  VAL   A CB  
301  C CG1 . VAL   A 33  ? 0.7525 0.8521 0.5161 0.0894  0.0335  0.0791  76  VAL   A CG1 
302  C CG2 . VAL   A 33  ? 0.7399 0.8150 0.4673 0.0838  0.0168  0.0756  76  VAL   A CG2 
303  N N   . ALA   A 34  ? 0.7525 0.8562 0.5129 0.0676  -0.0096 0.0760  77  ALA   A N   
304  C CA  . ALA   A 34  ? 0.7565 0.8538 0.5011 0.0581  -0.0213 0.0743  77  ALA   A CA  
305  C C   . ALA   A 34  ? 0.7478 0.8373 0.4817 0.0470  -0.0141 0.0695  77  ALA   A C   
306  O O   . ALA   A 34  ? 0.7534 0.8495 0.5016 0.0452  -0.0036 0.0681  77  ALA   A O   
307  C CB  . ALA   A 34  ? 0.7586 0.8731 0.5204 0.0550  -0.0330 0.0740  77  ALA   A CB  
308  N N   . LEU   A 35  ? 0.7491 0.8238 0.4590 0.0406  -0.0185 0.0676  78  LEU   A N   
309  C CA  . LEU   A 35  ? 0.7522 0.8185 0.4515 0.0295  -0.0125 0.0621  78  LEU   A CA  
310  C C   . LEU   A 35  ? 0.7720 0.8409 0.4652 0.0179  -0.0224 0.0583  78  LEU   A C   
311  O O   . LEU   A 35  ? 0.7928 0.8554 0.4695 0.0180  -0.0331 0.0605  78  LEU   A O   
312  C CB  . LEU   A 35  ? 0.7576 0.8051 0.4346 0.0317  -0.0084 0.0617  78  LEU   A CB  
313  C CG  . LEU   A 35  ? 0.7671 0.8046 0.4330 0.0215  -0.0021 0.0557  78  LEU   A CG  
314  C CD1 . LEU   A 35  ? 0.7647 0.8094 0.4476 0.0194  0.0083  0.0538  78  LEU   A CD1 
315  C CD2 . LEU   A 35  ? 0.7638 0.7849 0.4111 0.0242  0.0012  0.0545  78  LEU   A CD2 
316  N N   . ASP   A 36  ? 0.7736 0.8514 0.4799 0.0084  -0.0190 0.0529  79  ASP   A N   
317  C CA  . ASP   A 36  ? 0.7718 0.8548 0.4746 -0.0037 -0.0277 0.0471  79  ASP   A CA  
318  C C   . ASP   A 36  ? 0.7799 0.8464 0.4595 -0.0137 -0.0238 0.0415  79  ASP   A C   
319  O O   . ASP   A 36  ? 0.7541 0.8072 0.4251 -0.0111 -0.0140 0.0420  79  ASP   A O   
320  C CB  . ASP   A 36  ? 0.7690 0.8711 0.5011 -0.0087 -0.0258 0.0429  79  ASP   A CB  
321  C CG  . ASP   A 36  ? 0.7652 0.8647 0.5072 -0.0166 -0.0118 0.0373  79  ASP   A CG  
322  O OD1 . ASP   A 36  ? 0.7777 0.8614 0.5039 -0.0182 -0.0043 0.0362  79  ASP   A OD1 
323  O OD2 . ASP   A 36  ? 0.7692 0.8825 0.5361 -0.0212 -0.0084 0.0336  79  ASP   A OD2 
324  N N   . GLU   A 37  ? 0.7855 0.8531 0.4545 -0.0249 -0.0315 0.0359  80  GLU   A N   
325  C CA  . GLU   A 37  ? 0.7942 0.8470 0.4407 -0.0357 -0.0279 0.0294  80  GLU   A CA  
326  C C   . GLU   A 37  ? 0.7640 0.8146 0.4236 -0.0416 -0.0133 0.0228  80  GLU   A C   
327  O O   . GLU   A 37  ? 0.7424 0.7786 0.3872 -0.0464 -0.0065 0.0188  80  GLU   A O   
328  C CB  . GLU   A 37  ? 0.8341 0.8911 0.4668 -0.0462 -0.0396 0.0245  80  GLU   A CB  
329  C CG  . GLU   A 37  ? 0.8634 0.9020 0.4642 -0.0541 -0.0385 0.0213  80  GLU   A CG  
330  C CD  . GLU   A 37  ? 0.8960 0.9364 0.4767 -0.0651 -0.0492 0.0163  80  GLU   A CD  
331  O OE1 . GLU   A 37  ? 0.8578 0.9117 0.4508 -0.0741 -0.0515 0.0076  80  GLU   A OE1 
332  O OE2 . GLU   A 37  ? 0.9348 0.9621 0.4865 -0.0649 -0.0548 0.0208  80  GLU   A OE2 
333  N N   . SER   A 38  ? 0.7669 0.8307 0.4541 -0.0412 -0.0083 0.0217  81  SER   A N   
334  C CA  . SER   A 38  ? 0.7640 0.8257 0.4670 -0.0453 0.0059  0.0173  81  SER   A CA  
335  C C   . SER   A 38  ? 0.7484 0.8021 0.4535 -0.0339 0.0158  0.0242  81  SER   A C   
336  O O   . SER   A 38  ? 0.7409 0.7927 0.4594 -0.0351 0.0273  0.0227  81  SER   A O   
337  C CB  . SER   A 38  ? 0.7737 0.8513 0.5053 -0.0494 0.0082  0.0142  81  SER   A CB  
338  O OG  . SER   A 38  ? 0.8200 0.9070 0.5506 -0.0601 -0.0019 0.0064  81  SER   A OG  
339  N N   . GLY   A 39  ? 0.7506 0.7999 0.4434 -0.0232 0.0115  0.0312  82  GLY   A N   
340  C CA  . GLY   A 39  ? 0.7595 0.8020 0.4517 -0.0119 0.0194  0.0367  82  GLY   A CA  
341  C C   . GLY   A 39  ? 0.7552 0.8085 0.4689 -0.0029 0.0255  0.0428  82  GLY   A C   
342  O O   . GLY   A 39  ? 0.7172 0.7653 0.4304 0.0052  0.0337  0.0465  82  GLY   A O   
343  N N   . ASP   A 40  ? 0.7588 0.8270 0.4905 -0.0041 0.0220  0.0435  83  ASP   A N   
344  C CA  . ASP   A 40  ? 0.7609 0.8406 0.5151 0.0032  0.0289  0.0488  83  ASP   A CA  
345  C C   . ASP   A 40  ? 0.7460 0.8314 0.4990 0.0147  0.0222  0.0547  83  ASP   A C   
346  O O   . ASP   A 40  ? 0.7381 0.8299 0.4901 0.0135  0.0100  0.0540  83  ASP   A O   
347  C CB  . ASP   A 40  ? 0.7795 0.8729 0.5586 -0.0057 0.0306  0.0447  83  ASP   A CB  
348  C CG  . ASP   A 40  ? 0.8030 0.8905 0.5877 -0.0165 0.0395  0.0386  83  ASP   A CG  
349  O OD1 . ASP   A 40  ? 0.8288 0.9041 0.6071 -0.0136 0.0492  0.0408  83  ASP   A OD1 
350  O OD2 . ASP   A 40  ? 0.8589 0.9541 0.6548 -0.0276 0.0363  0.0313  83  ASP   A OD2 
351  N N   . PHE   A 41  ? 0.7319 0.8149 0.4849 0.0258  0.0299  0.0603  84  PHE   A N   
352  C CA  . PHE   A 41  ? 0.7107 0.7996 0.4665 0.0375  0.0266  0.0652  84  PHE   A CA  
353  C C   . PHE   A 41  ? 0.7282 0.8353 0.5120 0.0384  0.0287  0.0666  84  PHE   A C   
354  O O   . PHE   A 41  ? 0.7271 0.8399 0.5273 0.0321  0.0369  0.0652  84  PHE   A O   
355  C CB  . PHE   A 41  ? 0.6786 0.7592 0.4240 0.0483  0.0350  0.0690  84  PHE   A CB  
356  C CG  . PHE   A 41  ? 0.6602 0.7255 0.3808 0.0502  0.0311  0.0672  84  PHE   A CG  
357  C CD1 . PHE   A 41  ? 0.6540 0.7153 0.3640 0.0546  0.0219  0.0676  84  PHE   A CD1 
358  C CD2 . PHE   A 41  ? 0.6508 0.7056 0.3604 0.0484  0.0374  0.0654  84  PHE   A CD2 
359  C CE1 . PHE   A 41  ? 0.6605 0.7073 0.3498 0.0559  0.0200  0.0655  84  PHE   A CE1 
360  C CE2 . PHE   A 41  ? 0.6385 0.6807 0.3284 0.0499  0.0344  0.0626  84  PHE   A CE2 
361  C CZ  . PHE   A 41  ? 0.6495 0.6877 0.3295 0.0535  0.0264  0.0625  84  PHE   A CZ  
362  N N   . SER   A 42  ? 0.7520 0.8679 0.5429 0.0459  0.0219  0.0690  85  SER   A N   
363  C CA  . SER   A 42  ? 0.7758 0.9109 0.5961 0.0480  0.0231  0.0698  85  SER   A CA  
364  C C   . SER   A 42  ? 0.7946 0.9336 0.6179 0.0613  0.0211  0.0738  85  SER   A C   
365  O O   . SER   A 42  ? 0.7711 0.8989 0.5743 0.0666  0.0137  0.0751  85  SER   A O   
366  C CB  . SER   A 42  ? 0.7950 0.9418 0.6271 0.0386  0.0110  0.0650  85  SER   A CB  
367  O OG  . SER   A 42  ? 0.8186 0.9600 0.6325 0.0401  -0.0043 0.0654  85  SER   A OG  
368  N N   . LEU   A 43  ? 0.8360 0.9895 0.6845 0.0663  0.0286  0.0754  86  LEU   A N   
369  C CA  . LEU   A 43  ? 0.8427 1.0014 0.6980 0.0792  0.0289  0.0782  86  LEU   A CA  
370  C C   . LEU   A 43  ? 0.8429 1.0138 0.7124 0.0806  0.0129  0.0773  86  LEU   A C   
371  O O   . LEU   A 43  ? 0.7813 0.9698 0.6764 0.0752  0.0094  0.0746  86  LEU   A O   
372  C CB  . LEU   A 43  ? 0.8613 1.0298 0.7369 0.0837  0.0456  0.0800  86  LEU   A CB  
373  C CG  . LEU   A 43  ? 0.8824 1.0373 0.7387 0.0878  0.0601  0.0831  86  LEU   A CG  
374  C CD1 . LEU   A 43  ? 0.8982 1.0619 0.7735 0.0880  0.0777  0.0855  86  LEU   A CD1 
375  C CD2 . LEU   A 43  ? 0.9034 1.0496 0.7420 0.0998  0.0591  0.0842  86  LEU   A CD2 
376  N N   . VAL   A 44  ? 0.8832 1.0443 0.7359 0.0876  0.0031  0.0793  87  VAL   A N   
377  C CA  . VAL   A 44  ? 0.9344 1.1041 0.7980 0.0934  -0.0117 0.0807  87  VAL   A CA  
378  C C   . VAL   A 44  ? 0.9780 1.1591 0.8651 0.1053  -0.0042 0.0819  87  VAL   A C   
379  O O   . VAL   A 44  ? 1.0108 1.1822 0.8877 0.1123  0.0074  0.0829  87  VAL   A O   
380  C CB  . VAL   A 44  ? 0.9293 1.0798 0.7635 0.0963  -0.0222 0.0833  87  VAL   A CB  
381  C CG1 . VAL   A 44  ? 0.9481 1.1039 0.7922 0.1059  -0.0353 0.0868  87  VAL   A CG1 
382  C CG2 . VAL   A 44  ? 0.9324 1.0731 0.7448 0.0838  -0.0291 0.0815  87  VAL   A CG2 
383  N N   . GLU   A 45  ? 1.0303 1.2320 0.9484 0.1075  -0.0102 0.0811  88  GLU   A N   
384  C CA  . GLU   A 45  ? 1.0874 1.3018 1.0319 0.1185  -0.0015 0.0812  88  GLU   A CA  
385  C C   . GLU   A 45  ? 1.1031 1.3318 1.0699 0.1256  -0.0176 0.0820  88  GLU   A C   
386  O O   . GLU   A 45  ? 1.0651 1.2835 1.0167 0.1308  -0.0317 0.0855  88  GLU   A O   
387  C CB  . GLU   A 45  ? 1.1020 1.3301 1.0693 0.1130  0.0148  0.0785  88  GLU   A CB  
388  C CG  . GLU   A 45  ? 1.1171 1.3297 1.0612 0.1077  0.0300  0.0793  88  GLU   A CG  
389  C CD  . GLU   A 45  ? 1.1056 1.3051 1.0319 0.1179  0.0422  0.0814  88  GLU   A CD  
390  O OE1 . GLU   A 45  ? 1.0832 1.2637 0.9779 0.1169  0.0432  0.0825  88  GLU   A OE1 
391  O OE2 . GLU   A 45  ? 1.0869 1.2962 1.0319 0.1265  0.0506  0.0811  88  GLU   A OE2 
392  N N   . GLY   B 7   ? 1.1777 1.1599 0.9472 0.0909  0.0678  -0.0333 16  GLY   B N   
393  C CA  . GLY   B 7   ? 1.1821 1.1585 0.9469 0.0956  0.0675  -0.0278 16  GLY   B CA  
394  C C   . GLY   B 7   ? 1.1960 1.1691 0.9531 0.0997  0.0636  -0.0247 16  GLY   B C   
395  O O   . GLY   B 7   ? 1.2505 1.2253 1.0061 0.0984  0.0608  -0.0268 16  GLY   B O   
396  N N   . GLU   B 8   ? 1.1117 1.0808 0.8641 0.1044  0.0632  -0.0199 17  GLU   B N   
397  C CA  . GLU   B 8   ? 1.0535 1.0191 0.7971 0.1091  0.0594  -0.0166 17  GLU   B CA  
398  C C   . GLU   B 8   ? 0.9853 0.9496 0.7199 0.1063  0.0574  -0.0169 17  GLU   B C   
399  O O   . GLU   B 8   ? 0.9695 0.9334 0.7006 0.1054  0.0590  -0.0152 17  GLU   B O   
400  C CB  . GLU   B 8   ? 1.1004 1.0637 0.8420 0.1149  0.0601  -0.0115 17  GLU   B CB  
401  C CG  . GLU   B 8   ? 1.1231 1.0831 0.8555 0.1204  0.0563  -0.0084 17  GLU   B CG  
402  C CD  . GLU   B 8   ? 1.1662 1.1256 0.8971 0.1264  0.0569  -0.0032 17  GLU   B CD  
403  O OE1 . GLU   B 8   ? 1.1320 1.0932 0.8652 0.1255  0.0600  -0.0009 17  GLU   B OE1 
404  O OE2 . GLU   B 8   ? 1.2644 1.2218 0.9918 0.1316  0.0541  -0.0014 17  GLU   B OE2 
405  N N   A THR   B 9   ? 0.9645 0.9279 0.6952 0.1048  0.0536  -0.0188 18  THR   B N   
406  N N   B THR   B 9   ? 0.9697 0.9331 0.7003 0.1049  0.0536  -0.0188 18  THR   B N   
407  N N   C THR   B 9   ? 0.9645 0.9279 0.6952 0.1048  0.0536  -0.0188 18  THR   B N   
408  N N   D THR   B 9   ? 0.9697 0.9331 0.7003 0.1049  0.0536  -0.0188 18  THR   B N   
409  C CA  A THR   B 9   ? 0.9502 0.9114 0.6720 0.1015  0.0506  -0.0194 18  THR   B CA  
410  C CA  B THR   B 9   ? 0.9583 0.9196 0.6802 0.1014  0.0505  -0.0195 18  THR   B CA  
411  C CA  C THR   B 9   ? 0.9502 0.9114 0.6720 0.1015  0.0506  -0.0194 18  THR   B CA  
412  C CA  D THR   B 9   ? 0.9583 0.9196 0.6802 0.1014  0.0505  -0.0195 18  THR   B CA  
413  C C   A THR   B 9   ? 0.9388 0.8940 0.6500 0.1070  0.0457  -0.0166 18  THR   B C   
414  C C   B THR   B 9   ? 0.9434 0.8986 0.6546 0.1070  0.0457  -0.0167 18  THR   B C   
415  C C   C THR   B 9   ? 0.9388 0.8940 0.6500 0.1070  0.0457  -0.0166 18  THR   B C   
416  C C   D THR   B 9   ? 0.9434 0.8986 0.6546 0.1070  0.0457  -0.0167 18  THR   B C   
417  O O   A THR   B 9   ? 0.9470 0.8987 0.6494 0.1052  0.0421  -0.0170 18  THR   B O   
418  O O   B THR   B 9   ? 0.9516 0.9033 0.6541 0.1051  0.0421  -0.0170 18  THR   B O   
419  O O   C THR   B 9   ? 0.9470 0.8987 0.6494 0.1052  0.0421  -0.0170 18  THR   B O   
420  O O   D THR   B 9   ? 0.9516 0.9033 0.6541 0.1051  0.0421  -0.0170 18  THR   B O   
421  C CB  A THR   B 9   ? 0.9470 0.9116 0.6715 0.0948  0.0492  -0.0234 18  THR   B CB  
422  C CB  B THR   B 9   ? 0.9613 0.9260 0.6862 0.0949  0.0492  -0.0235 18  THR   B CB  
423  C CB  C THR   B 9   ? 0.9470 0.9116 0.6715 0.0948  0.0492  -0.0234 18  THR   B CB  
424  C CB  D THR   B 9   ? 0.9613 0.9260 0.6862 0.0949  0.0492  -0.0235 18  THR   B CB  
425  O OG1 A THR   B 9   ? 0.9407 0.9114 0.6761 0.0918  0.0536  -0.0263 18  THR   B OG1 
426  O OG1 B THR   B 9   ? 0.9667 0.9314 0.6930 0.0975  0.0464  -0.0237 18  THR   B OG1 
427  O OG1 C THR   B 9   ? 0.9407 0.9114 0.6761 0.0918  0.0536  -0.0263 18  THR   B OG1 
428  O OG1 D THR   B 9   ? 0.9667 0.9314 0.6930 0.0975  0.0464  -0.0237 18  THR   B OG1 
429  C CG2 A THR   B 9   ? 0.9460 0.9091 0.6632 0.0894  0.0471  -0.0243 18  THR   B CG2 
430  C CG2 B THR   B 9   ? 0.9594 0.9307 0.6944 0.0900  0.0538  -0.0268 18  THR   B CG2 
431  C CG2 C THR   B 9   ? 0.9460 0.9091 0.6632 0.0894  0.0471  -0.0243 18  THR   B CG2 
432  C CG2 D THR   B 9   ? 0.9594 0.9307 0.6944 0.0900  0.0538  -0.0268 18  THR   B CG2 
433  N N   . THR   B 10  ? 0.9266 0.8804 0.6382 0.1137  0.0453  -0.0140 19  THR   B N   
434  C CA  . THR   B 10  ? 0.8783 0.8267 0.5801 0.1197  0.0405  -0.0117 19  THR   B CA  
435  C C   . THR   B 10  ? 0.7937 0.7387 0.4852 0.1219  0.0391  -0.0099 19  THR   B C   
436  O O   . THR   B 10  ? 0.7589 0.7067 0.4522 0.1226  0.0430  -0.0082 19  THR   B O   
437  C CB  . THR   B 10  ? 0.8973 0.8458 0.6020 0.1265  0.0412  -0.0088 19  THR   B CB  
438  O OG1 . THR   B 10  ? 0.9530 0.9048 0.6680 0.1251  0.0430  -0.0104 19  THR   B OG1 
439  C CG2 . THR   B 10  ? 0.9077 0.8511 0.6034 0.1322  0.0359  -0.0072 19  THR   B CG2 
440  N N   . ASP   B 11  ? 0.7584 0.6976 0.4392 0.1229  0.0335  -0.0102 20  ASP   B N   
441  C CA  . ASP   B 11  ? 0.7810 0.7161 0.4505 0.1270  0.0312  -0.0086 20  ASP   B CA  
442  C C   . ASP   B 11  ? 0.7711 0.7085 0.4396 0.1349  0.0336  -0.0048 20  ASP   B C   
443  O O   . ASP   B 11  ? 0.7724 0.7117 0.4461 0.1382  0.0348  -0.0033 20  ASP   B O   
444  C CB  . ASP   B 11  ? 0.8153 0.7423 0.4731 0.1292  0.0237  -0.0092 20  ASP   B CB  
445  C CG  . ASP   B 11  ? 0.8469 0.7703 0.5007 0.1217  0.0200  -0.0120 20  ASP   B CG  
446  O OD1 . ASP   B 11  ? 0.8172 0.7456 0.4794 0.1142  0.0233  -0.0139 20  ASP   B OD1 
447  O OD2 . ASP   B 11  ? 0.9012 0.8165 0.5428 0.1238  0.0135  -0.0121 20  ASP   B OD2 
448  N N   . GLY   B 12  ? 0.7517 0.6895 0.4137 0.1379  0.0340  -0.0032 21  GLY   B N   
449  C CA  . GLY   B 12  ? 0.7338 0.6757 0.3949 0.1450  0.0364  0.0006  21  GLY   B CA  
450  C C   . GLY   B 12  ? 0.7223 0.6698 0.3854 0.1435  0.0408  0.0022  21  GLY   B C   
451  O O   . GLY   B 12  ? 0.6996 0.6474 0.3649 0.1368  0.0422  0.0000  21  GLY   B O   
452  N N   . VAL   B 13  ? 0.7012 0.6540 0.3641 0.1491  0.0432  0.0063  22  VAL   B N   
453  C CA  . VAL   B 13  ? 0.6854 0.6449 0.3499 0.1482  0.0474  0.0087  22  VAL   B CA  
454  C C   . VAL   B 13  ? 0.6853 0.6498 0.3622 0.1443  0.0525  0.0106  22  VAL   B C   
455  O O   . VAL   B 13  ? 0.6886 0.6522 0.3700 0.1459  0.0523  0.0113  22  VAL   B O   
456  C CB  . VAL   B 13  ? 0.6961 0.6591 0.3514 0.1566  0.0462  0.0121  22  VAL   B CB  
457  C CG1 . VAL   B 13  ? 0.6989 0.6645 0.3542 0.1635  0.0459  0.0156  22  VAL   B CG1 
458  C CG2 . VAL   B 13  ? 0.6892 0.6599 0.3461 0.1552  0.0503  0.0146  22  VAL   B CG2 
459  N N   . TYR   B 14  ? 0.6692 0.6376 0.3513 0.1387  0.0564  0.0108  23  TYR   B N   
460  C CA  . TYR   B 14  ? 0.6579 0.6297 0.3514 0.1340  0.0608  0.0120  23  TYR   B CA  
461  C C   . TYR   B 14  ? 0.6613 0.6399 0.3558 0.1333  0.0643  0.0159  23  TYR   B C   
462  O O   . TYR   B 14  ? 0.6595 0.6398 0.3481 0.1334  0.0641  0.0159  23  TYR   B O   
463  C CB  . TYR   B 14  ? 0.6511 0.6204 0.3513 0.1260  0.0621  0.0073  23  TYR   B CB  
464  C CG  . TYR   B 14  ? 0.6438 0.6085 0.3462 0.1253  0.0596  0.0038  23  TYR   B CG  
465  C CD1 . TYR   B 14  ? 0.6494 0.6096 0.3437 0.1277  0.0549  0.0019  23  TYR   B CD1 
466  C CD2 . TYR   B 14  ? 0.6462 0.6111 0.3584 0.1228  0.0614  0.0027  23  TYR   B CD2 
467  C CE1 . TYR   B 14  ? 0.6514 0.6080 0.3474 0.1269  0.0524  -0.0007 23  TYR   B CE1 
468  C CE2 . TYR   B 14  ? 0.6557 0.6177 0.3701 0.1226  0.0591  -0.0002 23  TYR   B CE2 
469  C CZ  . TYR   B 14  ? 0.6610 0.6191 0.3673 0.1245  0.0547  -0.0018 23  TYR   B CZ  
470  O OH  . TYR   B 14  ? 0.6759 0.6318 0.3843 0.1237  0.0522  -0.0045 23  TYR   B OH  
471  N N   . ARG   B 15  ? 0.6674 0.6492 0.3695 0.1320  0.0672  0.0192  24  ARG   B N   
472  C CA  . ARG   B 15  ? 0.6747 0.6627 0.3799 0.1289  0.0707  0.0228  24  ARG   B CA  
473  C C   . ARG   B 15  ? 0.6715 0.6574 0.3837 0.1206  0.0731  0.0192  24  ARG   B C   
474  O O   . ARG   B 15  ? 0.6561 0.6374 0.3744 0.1177  0.0729  0.0156  24  ARG   B O   
475  C CB  . ARG   B 15  ? 0.6880 0.6798 0.3979 0.1304  0.0723  0.0283  24  ARG   B CB  
476  C CG  . ARG   B 15  ? 0.6988 0.6936 0.4027 0.1385  0.0702  0.0322  24  ARG   B CG  
477  C CD  . ARG   B 15  ? 0.7170 0.7138 0.4267 0.1391  0.0711  0.0370  24  ARG   B CD  
478  N NE  . ARG   B 15  ? 0.7273 0.7261 0.4315 0.1468  0.0689  0.0400  24  ARG   B NE  
479  C CZ  . ARG   B 15  ? 0.7407 0.7478 0.4394 0.1516  0.0690  0.0452  24  ARG   B CZ  
480  N NH1 . ARG   B 15  ? 0.7353 0.7502 0.4334 0.1494  0.0714  0.0485  24  ARG   B NH1 
481  N NH2 . ARG   B 15  ? 0.7489 0.7572 0.4426 0.1588  0.0667  0.0470  24  ARG   B NH2 
482  N N   . VAL   B 16  ? 0.6657 0.6559 0.3772 0.1173  0.0752  0.0205  25  VAL   B N   
483  C CA  . VAL   B 16  ? 0.6788 0.6687 0.3967 0.1094  0.0780  0.0182  25  VAL   B CA  
484  C C   . VAL   B 16  ? 0.6751 0.6694 0.3983 0.1072  0.0807  0.0233  25  VAL   B C   
485  O O   . VAL   B 16  ? 0.6639 0.6646 0.3832 0.1091  0.0814  0.0280  25  VAL   B O   
486  C CB  . VAL   B 16  ? 0.6872 0.6781 0.3994 0.1073  0.0778  0.0159  25  VAL   B CB  
487  C CG1 . VAL   B 16  ? 0.6841 0.6746 0.4022 0.0991  0.0804  0.0131  25  VAL   B CG1 
488  C CG2 . VAL   B 16  ? 0.6805 0.6666 0.3858 0.1100  0.0741  0.0120  25  VAL   B CG2 
489  N N   . MET   B 17  ? 0.6983 0.6891 0.4298 0.1031  0.0819  0.0223  26  MET   B N   
490  C CA  . MET   B 17  ? 0.7273 0.7202 0.4642 0.1007  0.0835  0.0272  26  MET   B CA  
491  C C   . MET   B 17  ? 0.7418 0.7329 0.4845 0.0930  0.0857  0.0248  26  MET   B C   
492  O O   . MET   B 17  ? 0.7263 0.7133 0.4715 0.0902  0.0857  0.0187  26  MET   B O   
493  C CB  . MET   B 17  ? 0.7409 0.7294 0.4825 0.1030  0.0822  0.0278  26  MET   B CB  
494  C CG  . MET   B 17  ? 0.7531 0.7419 0.4896 0.1105  0.0798  0.0291  26  MET   B CG  
495  S SD  . MET   B 17  ? 0.7530 0.7510 0.4819 0.1162  0.0795  0.0370  26  MET   B SD  
496  C CE  . MET   B 17  ? 0.7661 0.7670 0.5015 0.1118  0.0812  0.0436  26  MET   B CE  
497  N N   . THR   B 18  ? 0.7696 0.7638 0.5147 0.0897  0.0871  0.0297  27  THR   B N   
498  C CA  . THR   B 18  ? 0.8200 0.8116 0.5710 0.0825  0.0887  0.0284  27  THR   B CA  
499  C C   . THR   B 18  ? 0.8705 0.8604 0.6262 0.0810  0.0882  0.0335  27  THR   B C   
500  O O   . THR   B 18  ? 0.8048 0.7996 0.5581 0.0840  0.0876  0.0402  27  THR   B O   
501  C CB  . THR   B 18  ? 0.8303 0.8272 0.5784 0.0786  0.0905  0.0291  27  THR   B CB  
502  O OG1 . THR   B 18  ? 0.8694 0.8621 0.6231 0.0719  0.0918  0.0256  27  THR   B OG1 
503  C CG2 . THR   B 18  ? 0.8131 0.8183 0.5580 0.0793  0.0911  0.0369  27  THR   B CG2 
504  N N   . ARG   B 19  ? 0.9466 0.9300 0.7086 0.0763  0.0883  0.0304  28  ARG   B N   
505  C CA  . ARG   B 19  ? 1.0230 1.0029 0.7894 0.0732  0.0874  0.0348  28  ARG   B CA  
506  C C   . ARG   B 19  ? 1.0233 1.0043 0.7909 0.0661  0.0888  0.0363  28  ARG   B C   
507  O O   . ARG   B 19  ? 1.0240 1.0014 0.7948 0.0625  0.0876  0.0399  28  ARG   B O   
508  C CB  . ARG   B 19  ? 1.0704 1.0411 0.8423 0.0742  0.0857  0.0301  28  ARG   B CB  
509  C CG  . ARG   B 19  ? 1.1198 1.0898 0.8906 0.0811  0.0842  0.0291  28  ARG   B CG  
510  C CD  . ARG   B 19  ? 1.1819 1.1451 0.9570 0.0829  0.0818  0.0302  28  ARG   B CD  
511  N NE  . ARG   B 19  ? 1.2314 1.1931 1.0065 0.0890  0.0803  0.0280  28  ARG   B NE  
512  C CZ  . ARG   B 19  ? 1.2479 1.2058 1.0259 0.0906  0.0800  0.0207  28  ARG   B CZ  
513  N NH1 . ARG   B 19  ? 1.2466 1.2023 1.0279 0.0868  0.0812  0.0145  28  ARG   B NH1 
514  N NH2 . ARG   B 19  ? 1.2285 1.1856 1.0061 0.0961  0.0784  0.0197  28  ARG   B NH2 
515  N N   . ARG   B 20  ? 1.0721 1.0582 0.8366 0.0641  0.0908  0.0344  29  ARG   B N   
516  C CA  . ARG   B 20  ? 1.1143 1.1020 0.8796 0.0572  0.0923  0.0350  29  ARG   B CA  
517  C C   . ARG   B 20  ? 1.0887 1.0833 0.8520 0.0552  0.0923  0.0442  29  ARG   B C   
518  O O   . ARG   B 20  ? 1.1086 1.1039 0.8733 0.0490  0.0929  0.0460  29  ARG   B O   
519  C CB  . ARG   B 20  ? 1.1516 1.1430 0.9135 0.0566  0.0942  0.0303  29  ARG   B CB  
520  C CG  . ARG   B 20  ? 1.2320 1.2213 0.9965 0.0497  0.0956  0.0266  29  ARG   B CG  
521  C CD  . ARG   B 20  ? 1.3020 1.2964 1.0622 0.0489  0.0973  0.0238  29  ARG   B CD  
522  N NE  . ARG   B 20  ? 1.3472 1.3507 1.1020 0.0506  0.0977  0.0300  29  ARG   B NE  
523  C CZ  . ARG   B 20  ? 1.3723 1.3815 1.1257 0.0464  0.0991  0.0334  29  ARG   B CZ  
524  N NH1 . ARG   B 20  ? 1.3763 1.3826 1.1331 0.0395  0.1000  0.0313  29  ARG   B NH1 
525  N NH2 . ARG   B 20  ? 1.3393 1.3577 1.0877 0.0493  0.0994  0.0389  29  ARG   B NH2 
526  N N   . LEU   B 21  ? 1.0587 1.0592 0.8187 0.0603  0.0916  0.0498  30  LEU   B N   
527  C CA  . LEU   B 21  ? 1.0237 1.0324 0.7820 0.0590  0.0913  0.0593  30  LEU   B CA  
528  C C   . LEU   B 21  ? 0.9858 0.9901 0.7467 0.0601  0.0888  0.0636  30  LEU   B C   
529  O O   . LEU   B 21  ? 0.9693 0.9632 0.7342 0.0609  0.0873  0.0588  30  LEU   B O   
530  C CB  . LEU   B 21  ? 1.0276 1.0479 0.7793 0.0645  0.0923  0.0623  30  LEU   B CB  
531  C CG  . LEU   B 21  ? 1.0535 1.0801 0.8015 0.0634  0.0944  0.0602  30  LEU   B CG  
532  C CD1 . LEU   B 21  ? 1.0556 1.0757 0.8073 0.0567  0.0954  0.0547  30  LEU   B CD1 
533  C CD2 . LEU   B 21  ? 1.0742 1.1028 0.8167 0.0708  0.0943  0.0561  30  LEU   B CD2 
534  N N   . LEU   B 22  ? 0.9830 0.9957 0.7419 0.0601  0.0882  0.0725  31  LEU   B N   
535  C CA  . LEU   B 22  ? 0.9483 0.9590 0.7086 0.0615  0.0857  0.0781  31  LEU   B CA  
536  C C   . LEU   B 22  ? 0.9409 0.9487 0.7000 0.0695  0.0850  0.0742  31  LEU   B C   
537  O O   . LEU   B 22  ? 0.9445 0.9582 0.6991 0.0747  0.0865  0.0716  31  LEU   B O   
538  C CB  . LEU   B 22  ? 0.9417 0.9655 0.6987 0.0609  0.0858  0.0882  31  LEU   B CB  
539  C CG  . LEU   B 22  ? 0.9383 0.9604 0.6970 0.0601  0.0829  0.0953  31  LEU   B CG  
540  C CD1 . LEU   B 22  ? 0.9199 0.9333 0.6831 0.0515  0.0807  0.0977  31  LEU   B CD1 
541  C CD2 . LEU   B 22  ? 0.9617 0.9995 0.7160 0.0624  0.0833  0.1044  31  LEU   B CD2 
542  N N   . GLY   B 23  ? 0.9381 0.9368 0.7007 0.0705  0.0826  0.0737  32  GLY   B N   
543  C CA  . GLY   B 23  ? 0.9241 0.9195 0.6861 0.0778  0.0815  0.0704  32  GLY   B CA  
544  C C   . GLY   B 23  ? 0.8995 0.8929 0.6604 0.0812  0.0830  0.0615  32  GLY   B C   
545  O O   . GLY   B 23  ? 0.8955 0.8855 0.6582 0.0771  0.0843  0.0563  32  GLY   B O   
546  N N   . SER   B 24  ? 0.8800 0.8745 0.6380 0.0882  0.0824  0.0597  33  SER   B N   
547  C CA  . SER   B 24  ? 0.8557 0.8505 0.6104 0.0921  0.0833  0.0529  33  SER   B CA  
548  C C   . SER   B 24  ? 0.8206 0.8262 0.5680 0.0956  0.0844  0.0566  33  SER   B C   
549  O O   . SER   B 24  ? 0.8022 0.8139 0.5467 0.0995  0.0835  0.0626  33  SER   B O   
550  C CB  . SER   B 24  ? 0.8602 0.8492 0.6157 0.0974  0.0815  0.0491  33  SER   B CB  
551  O OG  . SER   B 24  ? 0.9007 0.8806 0.6629 0.0949  0.0803  0.0464  33  SER   B OG  
552  N N   . THR   B 25  ? 0.7781 0.7864 0.5226 0.0943  0.0859  0.0530  34  THR   B N   
553  C CA  . THR   B 25  ? 0.7694 0.7880 0.5068 0.0972  0.0869  0.0560  34  THR   B CA  
554  C C   . THR   B 25  ? 0.7670 0.7835 0.4994 0.1018  0.0862  0.0496  34  THR   B C   
555  O O   . THR   B 25  ? 0.7700 0.7796 0.5048 0.0986  0.0865  0.0429  34  THR   B O   
556  C CB  . THR   B 25  ? 0.7757 0.7995 0.5140 0.0909  0.0889  0.0585  34  THR   B CB  
557  O OG1 . THR   B 25  ? 0.7776 0.8008 0.5211 0.0857  0.0887  0.0638  34  THR   B OG1 
558  C CG2 . THR   B 25  ? 0.7755 0.8115 0.5071 0.0941  0.0898  0.0625  34  THR   B CG2 
559  N N   . GLN   B 26  ? 0.7468 0.7688 0.4721 0.1089  0.0851  0.0515  35  GLN   B N   
560  C CA  . GLN   B 26  ? 0.7475 0.7668 0.4666 0.1134  0.0837  0.0459  35  GLN   B CA  
561  C C   . GLN   B 26  ? 0.7523 0.7768 0.4669 0.1119  0.0849  0.0452  35  GLN   B C   
562  O O   . GLN   B 26  ? 0.7505 0.7850 0.4612 0.1143  0.0856  0.0504  35  GLN   B O   
563  C CB  . GLN   B 26  ? 0.7477 0.7692 0.4603 0.1221  0.0814  0.0475  35  GLN   B CB  
564  C CG  . GLN   B 26  ? 0.7444 0.7602 0.4514 0.1260  0.0790  0.0414  35  GLN   B CG  
565  C CD  . GLN   B 26  ? 0.7400 0.7570 0.4401 0.1347  0.0764  0.0427  35  GLN   B CD  
566  O OE1 . GLN   B 26  ? 0.7679 0.7822 0.4707 0.1368  0.0754  0.0439  35  GLN   B OE1 
567  N NE2 . GLN   B 26  ? 0.7268 0.7474 0.4179 0.1401  0.0749  0.0423  35  GLN   B NE2 
568  N N   . VAL   B 27  ? 0.7353 0.7539 0.4505 0.1082  0.0849  0.0391  36  VAL   B N   
569  C CA  . VAL   B 27  ? 0.7234 0.7455 0.4350 0.1057  0.0860  0.0378  36  VAL   B CA  
570  C C   . VAL   B 27  ? 0.6948 0.7159 0.3971 0.1120  0.0833  0.0347  36  VAL   B C   
571  O O   . VAL   B 27  ? 0.6955 0.7218 0.3923 0.1132  0.0834  0.0354  36  VAL   B O   
572  C CB  . VAL   B 27  ? 0.7591 0.7756 0.4770 0.0973  0.0876  0.0333  36  VAL   B CB  
573  C CG1 . VAL   B 27  ? 0.7806 0.7974 0.5066 0.0916  0.0896  0.0365  36  VAL   B CG1 
574  C CG2 . VAL   B 27  ? 0.7546 0.7618 0.4743 0.0965  0.0861  0.0266  36  VAL   B CG2 
575  N N   . GLY   B 28  ? 0.6743 0.6887 0.3746 0.1159  0.0807  0.0315  37  GLY   B N   
576  C CA  . GLY   B 28  ? 0.6572 0.6691 0.3481 0.1224  0.0772  0.0289  37  GLY   B CA  
577  C C   . GLY   B 28  ? 0.6553 0.6594 0.3459 0.1253  0.0744  0.0259  37  GLY   B C   
578  O O   . GLY   B 28  ? 0.6588 0.6615 0.3563 0.1242  0.0753  0.0271  37  GLY   B O   
579  N N   . VAL   B 29  ? 0.6480 0.6467 0.3311 0.1283  0.0708  0.0219  38  VAL   B N   
580  C CA  . VAL   B 29  ? 0.6451 0.6367 0.3250 0.1323  0.0670  0.0192  38  VAL   B CA  
581  C C   . VAL   B 29  ? 0.6369 0.6208 0.3134 0.1289  0.0643  0.0135  38  VAL   B C   
582  O O   . VAL   B 29  ? 0.6349 0.6196 0.3071 0.1272  0.0640  0.0125  38  VAL   B O   
583  C CB  . VAL   B 29  ? 0.6490 0.6432 0.3192 0.1421  0.0641  0.0218  38  VAL   B CB  
584  C CG1 . VAL   B 29  ? 0.6532 0.6400 0.3192 0.1467  0.0599  0.0195  38  VAL   B CG1 
585  C CG2 . VAL   B 29  ? 0.6506 0.6544 0.3232 0.1453  0.0669  0.0280  38  VAL   B CG2 
586  N N   . GLY   B 30  ? 0.6307 0.6079 0.3075 0.1288  0.0616  0.0104  39  GLY   B N   
587  C CA  . GLY   B 30  ? 0.6261 0.5963 0.2975 0.1266  0.0577  0.0059  39  GLY   B CA  
588  C C   . GLY   B 30  ? 0.6286 0.5926 0.2967 0.1299  0.0535  0.0041  39  GLY   B C   
589  O O   . GLY   B 30  ? 0.6298 0.5950 0.2999 0.1345  0.0537  0.0065  39  GLY   B O   
590  N N   . VAL   B 31  ? 0.6301 0.5876 0.2933 0.1272  0.0496  0.0004  40  VAL   B N   
591  C CA  . VAL   B 31  ? 0.6394 0.5896 0.2970 0.1294  0.0441  -0.0016 40  VAL   B CA  
592  C C   . VAL   B 31  ? 0.6500 0.5981 0.3143 0.1211  0.0442  -0.0052 40  VAL   B C   
593  O O   . VAL   B 31  ? 0.6429 0.5910 0.3078 0.1145  0.0449  -0.0073 40  VAL   B O   
594  C CB  . VAL   B 31  ? 0.6503 0.5944 0.2943 0.1333  0.0384  -0.0025 40  VAL   B CB  
595  C CG1 . VAL   B 31  ? 0.6618 0.5974 0.2997 0.1344  0.0322  -0.0046 40  VAL   B CG1 
596  C CG2 . VAL   B 31  ? 0.6517 0.5990 0.2884 0.1423  0.0380  0.0005  40  VAL   B CG2 
597  N N   . MET   B 32  ? 0.6523 0.5996 0.3218 0.1212  0.0438  -0.0058 41  MET   B N   
598  C CA  . MET   B 32  ? 0.6782 0.6238 0.3523 0.1147  0.0426  -0.0093 41  MET   B CA  
599  C C   . MET   B 32  ? 0.6971 0.6352 0.3611 0.1163  0.0357  -0.0104 41  MET   B C   
600  O O   . MET   B 32  ? 0.6870 0.6222 0.3466 0.1229  0.0329  -0.0089 41  MET   B O   
601  C CB  . MET   B 32  ? 0.6916 0.6405 0.3763 0.1145  0.0454  -0.0093 41  MET   B CB  
602  C CG  . MET   B 32  ? 0.7120 0.6623 0.4037 0.1074  0.0457  -0.0130 41  MET   B CG  
603  S SD  . MET   B 32  ? 0.7378 0.6934 0.4370 0.0988  0.0507  -0.0155 41  MET   B SD  
604  C CE  . MET   B 32  ? 0.7371 0.6972 0.4453 0.1018  0.0565  -0.0129 41  MET   B CE  
605  N N   . GLN   B 33  ? 0.7128 0.6477 0.3731 0.1101  0.0327  -0.0130 42  GLN   B N   
606  C CA  . GLN   B 33  ? 0.7438 0.6709 0.3949 0.1099  0.0254  -0.0141 42  GLN   B CA  
607  C C   . GLN   B 33  ? 0.7654 0.6935 0.4202 0.1002  0.0245  -0.0169 42  GLN   B C   
608  O O   . GLN   B 33  ? 0.7595 0.6909 0.4172 0.0944  0.0274  -0.0181 42  GLN   B O   
609  C CB  . GLN   B 33  ? 0.7638 0.6837 0.4010 0.1144  0.0204  -0.0133 42  GLN   B CB  
610  C CG  . GLN   B 33  ? 0.8114 0.7219 0.4383 0.1162  0.0123  -0.0139 42  GLN   B CG  
611  C CD  . GLN   B 33  ? 0.8486 0.7510 0.4610 0.1227  0.0067  -0.0134 42  GLN   B CD  
612  O OE1 . GLN   B 33  ? 0.8874 0.7818 0.4906 0.1197  0.0004  -0.0147 42  GLN   B OE1 
613  N NE2 . GLN   B 33  ? 0.8502 0.7552 0.4605 0.1314  0.0089  -0.0113 42  GLN   B NE2 
614  N N   . GLU   B 34  ? 0.7884 0.7147 0.4435 0.0982  0.0209  -0.0178 43  GLU   B N   
615  C CA  . GLU   B 34  ? 0.8052 0.7335 0.4633 0.0887  0.0193  -0.0202 43  GLU   B CA  
616  C C   . GLU   B 34  ? 0.7801 0.7184 0.4510 0.0830  0.0264  -0.0220 43  GLU   B C   
617  O O   . GLU   B 34  ? 0.7617 0.7027 0.4342 0.0748  0.0261  -0.0240 43  GLU   B O   
618  C CB  . GLU   B 34  ? 0.8506 0.7715 0.4970 0.0851  0.0133  -0.0205 43  GLU   B CB  
619  C CG  . GLU   B 34  ? 0.8820 0.7921 0.5156 0.0896  0.0050  -0.0194 43  GLU   B CG  
620  C CD  . GLU   B 34  ? 0.9110 0.8113 0.5308 0.0894  -0.0012 -0.0192 43  GLU   B CD  
621  O OE1 . GLU   B 34  ? 0.9232 0.8206 0.5393 0.0815  -0.0056 -0.0201 43  GLU   B OE1 
622  O OE2 . GLU   B 34  ? 0.9706 0.8664 0.5830 0.0974  -0.0020 -0.0181 43  GLU   B OE2 
623  N N   . GLY   B 35  ? 0.7423 0.6856 0.4218 0.0868  0.0322  -0.0214 44  GLY   B N   
624  C CA  . GLY   B 35  ? 0.7332 0.6851 0.4249 0.0822  0.0384  -0.0235 44  GLY   B CA  
625  C C   . GLY   B 35  ? 0.7255 0.6792 0.4180 0.0803  0.0423  -0.0234 44  GLY   B C   
626  O O   . GLY   B 35  ? 0.7290 0.6892 0.4310 0.0764  0.0474  -0.0252 44  GLY   B O   
627  N N   . VAL   B 36  ? 0.7028 0.6510 0.3855 0.0834  0.0400  -0.0214 45  VAL   B N   
628  C CA  . VAL   B 36  ? 0.6847 0.6344 0.3664 0.0820  0.0430  -0.0209 45  VAL   B CA  
629  C C   . VAL   B 36  ? 0.6724 0.6223 0.3535 0.0897  0.0456  -0.0176 45  VAL   B C   
630  O O   . VAL   B 36  ? 0.6904 0.6360 0.3647 0.0968  0.0422  -0.0155 45  VAL   B O   
631  C CB  . VAL   B 36  ? 0.6945 0.6386 0.3654 0.0789  0.0380  -0.0213 45  VAL   B CB  
632  C CG1 . VAL   B 36  ? 0.7004 0.6451 0.3685 0.0791  0.0403  -0.0203 45  VAL   B CG1 
633  C CG2 . VAL   B 36  ? 0.7012 0.6474 0.3744 0.0694  0.0366  -0.0242 45  VAL   B CG2 
634  N N   . PHE   B 37  ? 0.6422 0.5973 0.3299 0.0883  0.0511  -0.0170 46  PHE   B N   
635  C CA  . PHE   B 37  ? 0.6326 0.5893 0.3197 0.0945  0.0536  -0.0134 46  PHE   B CA  
636  C C   . PHE   B 37  ? 0.6216 0.5776 0.3011 0.0947  0.0530  -0.0123 46  PHE   B C   
637  O O   . PHE   B 37  ? 0.6069 0.5647 0.2884 0.0882  0.0547  -0.0141 46  PHE   B O   
638  C CB  . PHE   B 37  ? 0.6315 0.5938 0.3300 0.0932  0.0594  -0.0128 46  PHE   B CB  
639  C CG  . PHE   B 37  ? 0.6404 0.6046 0.3384 0.0996  0.0612  -0.0084 46  PHE   B CG  
640  C CD1 . PHE   B 37  ? 0.6508 0.6131 0.3453 0.1067  0.0589  -0.0060 46  PHE   B CD1 
641  C CD2 . PHE   B 37  ? 0.6473 0.6157 0.3478 0.0982  0.0650  -0.0063 46  PHE   B CD2 
642  C CE1 . PHE   B 37  ? 0.6577 0.6230 0.3517 0.1123  0.0606  -0.0016 46  PHE   B CE1 
643  C CE2 . PHE   B 37  ? 0.6502 0.6216 0.3498 0.1036  0.0665  -0.0017 46  PHE   B CE2 
644  C CZ  . PHE   B 37  ? 0.6578 0.6279 0.3542 0.1107  0.0643  0.0006  46  PHE   B CZ  
645  N N   . HIS   B 38  ? 0.6129 0.5668 0.2837 0.1020  0.0505  -0.0096 47  HIS   B N   
646  C CA  . HIS   B 38  ? 0.6118 0.5651 0.2741 0.1039  0.0493  -0.0085 47  HIS   B CA  
647  C C   . HIS   B 38  ? 0.6159 0.5756 0.2800 0.1089  0.0532  -0.0046 47  HIS   B C   
648  O O   . HIS   B 38  ? 0.6064 0.5672 0.2703 0.1154  0.0531  -0.0021 47  HIS   B O   
649  C CB  . HIS   B 38  ? 0.6184 0.5644 0.2681 0.1092  0.0426  -0.0088 47  HIS   B CB  
650  C CG  . HIS   B 38  ? 0.6232 0.5625 0.2702 0.1051  0.0378  -0.0117 47  HIS   B CG  
651  N ND1 . HIS   B 38  ? 0.6278 0.5667 0.2802 0.1043  0.0375  -0.0125 47  HIS   B ND1 
652  C CD2 . HIS   B 38  ? 0.6332 0.5662 0.2725 0.1013  0.0328  -0.0137 47  HIS   B CD2 
653  C CE1 . HIS   B 38  ? 0.6324 0.5654 0.2802 0.1003  0.0324  -0.0147 47  HIS   B CE1 
654  N NE2 . HIS   B 38  ? 0.6369 0.5662 0.2770 0.0979  0.0295  -0.0155 47  HIS   B NE2 
655  N N   . THR   B 39  ? 0.6189 0.5832 0.2848 0.1056  0.0565  -0.0038 48  THR   B N   
656  C CA  . THR   B 39  ? 0.6252 0.5965 0.2920 0.1100  0.0598  0.0003  48  THR   B CA  
657  C C   . THR   B 39  ? 0.6385 0.6122 0.3003 0.1088  0.0600  0.0007  48  THR   B C   
658  O O   . THR   B 39  ? 0.6275 0.5960 0.2841 0.1055  0.0569  -0.0023 48  THR   B O   
659  C CB  . THR   B 39  ? 0.6222 0.5984 0.3007 0.1070  0.0648  0.0020  48  THR   B CB  
660  O OG1 . THR   B 39  ? 0.6176 0.6006 0.2968 0.1110  0.0675  0.0068  48  THR   B OG1 
661  C CG2 . THR   B 39  ? 0.6203 0.5975 0.3067 0.0979  0.0681  -0.0005 48  THR   B CG2 
662  N N   . MET   B 40  ? 0.6495 0.6308 0.3125 0.1115  0.0632  0.0046  49  MET   B N   
663  C CA  . MET   B 40  ? 0.6669 0.6523 0.3266 0.1102  0.0642  0.0054  49  MET   B CA  
664  C C   . MET   B 40  ? 0.6630 0.6521 0.3326 0.1012  0.0691  0.0051  49  MET   B C   
665  O O   . MET   B 40  ? 0.6570 0.6483 0.3356 0.0986  0.0724  0.0062  49  MET   B O   
666  C CB  . MET   B 40  ? 0.6827 0.6756 0.3375 0.1182  0.0647  0.0099  49  MET   B CB  
667  C CG  . MET   B 40  ? 0.7135 0.7026 0.3589 0.1277  0.0599  0.0099  49  MET   B CG  
668  S SD  . MET   B 40  ? 0.7705 0.7660 0.4051 0.1371  0.0580  0.0125  49  MET   B SD  
669  C CE  . MET   B 40  ? 0.7535 0.7379 0.3770 0.1370  0.0517  0.0074  49  MET   B CE  
670  N N   A TRP   B 41  ? 0.6626 0.6518 0.3301 0.0966  0.0692  0.0035  50  TRP   B N   
671  N N   B TRP   B 41  ? 0.6604 0.6495 0.3278 0.0966  0.0692  0.0035  50  TRP   B N   
672  N N   C TRP   B 41  ? 0.6624 0.6516 0.3298 0.0966  0.0692  0.0035  50  TRP   B N   
673  N N   D TRP   B 41  ? 0.6597 0.6489 0.3272 0.0966  0.0692  0.0035  50  TRP   B N   
674  C CA  A TRP   B 41  ? 0.6619 0.6536 0.3377 0.0875  0.0733  0.0024  50  TRP   B CA  
675  C CA  B TRP   B 41  ? 0.6575 0.6491 0.3334 0.0875  0.0733  0.0023  50  TRP   B CA  
676  C CA  C TRP   B 41  ? 0.6618 0.6535 0.3376 0.0875  0.0733  0.0024  50  TRP   B CA  
677  C CA  D TRP   B 41  ? 0.6572 0.6489 0.3331 0.0875  0.0733  0.0023  50  TRP   B CA  
678  C C   A TRP   B 41  ? 0.6643 0.6642 0.3463 0.0871  0.0779  0.0068  50  TRP   B C   
679  C C   B TRP   B 41  ? 0.6616 0.6615 0.3436 0.0871  0.0779  0.0068  50  TRP   B C   
680  C C   C TRP   B 41  ? 0.6643 0.6642 0.3463 0.0871  0.0779  0.0068  50  TRP   B C   
681  C C   D TRP   B 41  ? 0.6615 0.6615 0.3436 0.0872  0.0779  0.0068  50  TRP   B C   
682  O O   A TRP   B 41  ? 0.6605 0.6613 0.3517 0.0810  0.0812  0.0063  50  TRP   B O   
683  O O   B TRP   B 41  ? 0.6580 0.6587 0.3491 0.0810  0.0812  0.0063  50  TRP   B O   
684  O O   C TRP   B 41  ? 0.6606 0.6613 0.3517 0.0810  0.0812  0.0063  50  TRP   B O   
685  O O   D TRP   B 41  ? 0.6580 0.6588 0.3492 0.0810  0.0812  0.0063  50  TRP   B O   
686  C CB  A TRP   B 41  ? 0.6623 0.6525 0.3332 0.0834  0.0719  0.0001  50  TRP   B CB  
687  C CB  B TRP   B 41  ? 0.6544 0.6444 0.3255 0.0832  0.0720  0.0000  50  TRP   B CB  
688  C CB  C TRP   B 41  ? 0.6623 0.6525 0.3331 0.0834  0.0719  0.0001  50  TRP   B CB  
689  C CB  D TRP   B 41  ? 0.6542 0.6443 0.3254 0.0832  0.0720  0.0000  50  TRP   B CB  
690  C CG  A TRP   B 41  ? 0.6566 0.6480 0.3353 0.0738  0.0754  -0.0019 50  TRP   B CG  
691  C CG  B TRP   B 41  ? 0.6453 0.6381 0.3247 0.0742  0.0761  -0.0011 50  TRP   B CG  
692  C CG  C TRP   B 41  ? 0.6565 0.6479 0.3352 0.0738  0.0754  -0.0019 50  TRP   B CG  
693  C CG  D TRP   B 41  ? 0.6449 0.6377 0.3243 0.0742  0.0761  -0.0011 50  TRP   B CG  
694  C CD1 A TRP   B 41  ? 0.6572 0.6441 0.3386 0.0673  0.0747  -0.0063 50  TRP   B CD1 
695  C CD1 B TRP   B 41  ? 0.6402 0.6398 0.3241 0.0717  0.0801  0.0016  50  TRP   B CD1 
696  C CD1 C TRP   B 41  ? 0.6573 0.6442 0.3386 0.0673  0.0747  -0.0063 50  TRP   B CD1 
697  C CD1 D TRP   B 41  ? 0.6397 0.6393 0.3237 0.0717  0.0801  0.0016  50  TRP   B CD1 
698  C CD2 A TRP   B 41  ? 0.6529 0.6508 0.3376 0.0696  0.0799  0.0001  50  TRP   B CD2 
699  C CD2 B TRP   B 41  ? 0.6423 0.6314 0.3264 0.0664  0.0765  -0.0055 50  TRP   B CD2 
700  C CD2 C TRP   B 41  ? 0.6527 0.6507 0.3375 0.0696  0.0799  0.0001  50  TRP   B CD2 
701  C CD2 D TRP   B 41  ? 0.6423 0.6314 0.3264 0.0664  0.0765  -0.0055 50  TRP   B CD2 
702  N NE1 A TRP   B 41  ? 0.6541 0.6443 0.3425 0.0598  0.0786  -0.0074 50  TRP   B NE1 
703  N NE1 B TRP   B 41  ? 0.6356 0.6351 0.3263 0.0632  0.0828  -0.0009 50  TRP   B NE1 
704  N NE1 C TRP   B 41  ? 0.6542 0.6445 0.3427 0.0598  0.0786  -0.0074 50  TRP   B NE1 
705  N NE1 D TRP   B 41  ? 0.6351 0.6346 0.3258 0.0632  0.0828  -0.0009 50  TRP   B NE1 
706  C CE2 A TRP   B 41  ? 0.6523 0.6486 0.3429 0.0610  0.0817  -0.0035 50  TRP   B CE2 
707  C CE2 B TRP   B 41  ? 0.6374 0.6311 0.3285 0.0600  0.0809  -0.0054 50  TRP   B CE2 
708  C CE2 C TRP   B 41  ? 0.6524 0.6488 0.3430 0.0610  0.0817  -0.0035 50  TRP   B CE2 
709  C CE2 D TRP   B 41  ? 0.6375 0.6311 0.3286 0.0600  0.0809  -0.0054 50  TRP   B CE2 
710  C CE3 A TRP   B 41  ? 0.6540 0.6595 0.3397 0.0721  0.0825  0.0048  50  TRP   B CE3 
711  C CE3 B TRP   B 41  ? 0.6438 0.6270 0.3268 0.0641  0.0736  -0.0094 50  TRP   B CE3 
712  C CE3 C TRP   B 41  ? 0.6541 0.6595 0.3398 0.0721  0.0825  0.0048  50  TRP   B CE3 
713  C CE3 D TRP   B 41  ? 0.6440 0.6272 0.3270 0.0641  0.0735  -0.0094 50  TRP   B CE3 
714  C CZ2 A TRP   B 41  ? 0.6497 0.6505 0.3465 0.0551  0.0858  -0.0028 50  TRP   B CZ2 
715  C CZ2 B TRP   B 41  ? 0.6332 0.6257 0.3300 0.0520  0.0824  -0.0095 50  TRP   B CZ2 
716  C CZ2 C TRP   B 41  ? 0.6499 0.6507 0.3467 0.0551  0.0858  -0.0028 50  TRP   B CZ2 
717  C CZ2 D TRP   B 41  ? 0.6329 0.6254 0.3297 0.0520  0.0824  -0.0095 50  TRP   B CZ2 
718  C CZ3 A TRP   B 41  ? 0.6502 0.6601 0.3422 0.0657  0.0864  0.0059  50  TRP   B CZ3 
719  C CZ3 B TRP   B 41  ? 0.6401 0.6233 0.3291 0.0559  0.0752  -0.0131 50  TRP   B CZ3 
720  C CZ3 C TRP   B 41  ? 0.6502 0.6602 0.3422 0.0657  0.0864  0.0059  50  TRP   B CZ3 
721  C CZ3 D TRP   B 41  ? 0.6402 0.6234 0.3292 0.0559  0.0752  -0.0131 50  TRP   B CZ3 
722  C CH2 A TRP   B 41  ? 0.6493 0.6565 0.3467 0.0575  0.0879  0.0019  50  TRP   B CH2 
723  C CH2 B TRP   B 41  ? 0.6351 0.6229 0.3308 0.0502  0.0796  -0.0133 50  TRP   B CH2 
724  C CH2 C TRP   B 41  ? 0.6495 0.6567 0.3469 0.0575  0.0879  0.0019  50  TRP   B CH2 
725  C CH2 D TRP   B 41  ? 0.6351 0.6228 0.3308 0.0502  0.0796  -0.0133 50  TRP   B CH2 
726  N N   . HIS   B 42  ? 0.6686 0.6747 0.3458 0.0934  0.0778  0.0110  51  HIS   B N   
727  C CA  . HIS   B 42  ? 0.6883 0.7035 0.3707 0.0928  0.0817  0.0162  51  HIS   B CA  
728  C C   . HIS   B 42  ? 0.7034 0.7186 0.3931 0.0931  0.0834  0.0182  51  HIS   B C   
729  O O   . HIS   B 42  ? 0.7170 0.7370 0.4133 0.0895  0.0866  0.0215  51  HIS   B O   
730  C CB  . HIS   B 42  ? 0.7024 0.7258 0.3777 0.0994  0.0811  0.0202  51  HIS   B CB  
731  C CG  . HIS   B 42  ? 0.7136 0.7388 0.3837 0.1088  0.0789  0.0226  51  HIS   B CG  
732  N ND1 . HIS   B 42  ? 0.7169 0.7387 0.3763 0.1164  0.0744  0.0207  51  HIS   B ND1 
733  C CD2 . HIS   B 42  ? 0.7194 0.7499 0.3926 0.1122  0.0804  0.0270  51  HIS   B CD2 
734  C CE1 . HIS   B 42  ? 0.7191 0.7443 0.3757 0.1242  0.0735  0.0235  51  HIS   B CE1 
735  N NE2 . HIS   B 42  ? 0.6979 0.7286 0.3631 0.1215  0.0771  0.0275  51  HIS   B NE2 
736  N N   . VAL   B 43  ? 0.7073 0.7165 0.3962 0.0964  0.0810  0.0161  52  VAL   B N   
737  C CA  . VAL   B 43  ? 0.7079 0.7162 0.4035 0.0969  0.0821  0.0176  52  VAL   B CA  
738  C C   . VAL   B 43  ? 0.7075 0.7122 0.4126 0.0886  0.0845  0.0147  52  VAL   B C   
739  O O   . VAL   B 43  ? 0.7166 0.7240 0.4284 0.0862  0.0871  0.0177  52  VAL   B O   
740  C CB  . VAL   B 43  ? 0.7157 0.7187 0.4067 0.1033  0.0785  0.0160  52  VAL   B CB  
741  C CG1 . VAL   B 43  ? 0.7260 0.7264 0.4242 0.1030  0.0792  0.0164  52  VAL   B CG1 
742  C CG2 . VAL   B 43  ? 0.7353 0.7425 0.4173 0.1123  0.0762  0.0193  52  VAL   B CG2 
743  N N   . THR   B 44  ? 0.6899 0.6889 0.3953 0.0845  0.0835  0.0091  53  THR   B N   
744  C CA  . THR   B 44  ? 0.6879 0.6836 0.4021 0.0777  0.0853  0.0053  53  THR   B CA  
745  C C   . THR   B 44  ? 0.6905 0.6882 0.4075 0.0703  0.0878  0.0038  53  THR   B C   
746  O O   . THR   B 44  ? 0.6844 0.6810 0.4092 0.0651  0.0901  0.0020  53  THR   B O   
747  C CB  . THR   B 44  ? 0.6766 0.6664 0.3903 0.0778  0.0828  0.0004  53  THR   B CB  
748  O OG1 . THR   B 44  ? 0.6504 0.6384 0.3572 0.0766  0.0804  -0.0021 53  THR   B OG1 
749  C CG2 . THR   B 44  ? 0.6841 0.6721 0.3953 0.0851  0.0804  0.0023  53  THR   B CG2 
750  N N   . LYS   B 45  ? 0.7141 0.7143 0.4246 0.0703  0.0872  0.0046  54  LYS   B N   
751  C CA  . LYS   B 45  ? 0.7831 0.7847 0.4941 0.0636  0.0888  0.0026  54  LYS   B CA  
752  C C   . LYS   B 45  ? 0.7584 0.7553 0.4720 0.0582  0.0882  -0.0034 54  LYS   B C   
753  O O   . LYS   B 45  ? 0.7784 0.7763 0.4959 0.0516  0.0904  -0.0054 54  LYS   B O   
754  C CB  . LYS   B 45  ? 0.8165 0.8223 0.5342 0.0589  0.0925  0.0052  54  LYS   B CB  
755  C CG  . LYS   B 45  ? 0.8808 0.8929 0.5973 0.0626  0.0934  0.0118  54  LYS   B CG  
756  C CD  . LYS   B 45  ? 0.9244 0.9418 0.6332 0.0655  0.0926  0.0142  54  LYS   B CD  
757  C CE  . LYS   B 45  ? 0.9933 1.0189 0.7012 0.0694  0.0936  0.0210  54  LYS   B CE  
758  N NZ  . LYS   B 45  ? 1.0450 1.0755 0.7437 0.0767  0.0916  0.0231  54  LYS   B NZ  
759  N N   . GLY   B 46  ? 0.7494 0.7419 0.4610 0.0607  0.0854  -0.0060 55  GLY   B N   
760  C CA  . GLY   B 46  ? 0.7490 0.7383 0.4629 0.0557  0.0846  -0.0114 55  GLY   B CA  
761  C C   . GLY   B 46  ? 0.7460 0.7351 0.4694 0.0533  0.0868  -0.0137 55  GLY   B C   
762  O O   . GLY   B 46  ? 0.7549 0.7428 0.4808 0.0498  0.0863  -0.0182 55  GLY   B O   
763  N N   . ALA   B 47  ? 0.7448 0.7350 0.4732 0.0556  0.0888  -0.0108 56  ALA   B N   
764  C CA  . ALA   B 47  ? 0.7341 0.7232 0.4714 0.0538  0.0905  -0.0131 56  ALA   B CA  
765  C C   . ALA   B 47  ? 0.7360 0.7224 0.4738 0.0574  0.0882  -0.0153 56  ALA   B C   
766  O O   . ALA   B 47  ? 0.7235 0.7085 0.4552 0.0627  0.0855  -0.0131 56  ALA   B O   
767  C CB  . ALA   B 47  ? 0.7380 0.7280 0.4791 0.0554  0.0924  -0.0087 56  ALA   B CB  
768  N N   . ALA   B 48  ? 0.7265 0.7123 0.4714 0.0551  0.0891  -0.0193 57  ALA   B N   
769  C CA  . ALA   B 48  ? 0.7426 0.7267 0.4894 0.0583  0.0872  -0.0214 57  ALA   B CA  
770  C C   . ALA   B 48  ? 0.7592 0.7414 0.5074 0.0645  0.0868  -0.0173 57  ALA   B C   
771  O O   . ALA   B 48  ? 0.7767 0.7593 0.5259 0.0651  0.0884  -0.0134 57  ALA   B O   
772  C CB  . ALA   B 48  ? 0.7467 0.7321 0.5006 0.0543  0.0885  -0.0270 57  ALA   B CB  
773  N N   . LEU   B 49  ? 0.7597 0.7402 0.5078 0.0686  0.0845  -0.0180 58  LEU   B N   
774  C CA  . LEU   B 49  ? 0.7837 0.7623 0.5320 0.0749  0.0835  -0.0141 58  LEU   B CA  
775  C C   . LEU   B 49  ? 0.8086 0.7859 0.5636 0.0762  0.0830  -0.0172 58  LEU   B C   
776  O O   . LEU   B 49  ? 0.8246 0.8030 0.5813 0.0735  0.0825  -0.0221 58  LEU   B O   
777  C CB  . LEU   B 49  ? 0.7636 0.7413 0.5033 0.0799  0.0804  -0.0114 58  LEU   B CB  
778  C CG  . LEU   B 49  ? 0.7499 0.7289 0.4817 0.0798  0.0801  -0.0090 58  LEU   B CG  
779  C CD1 . LEU   B 49  ? 0.7445 0.7214 0.4673 0.0847  0.0762  -0.0081 58  LEU   B CD1 
780  C CD2 . LEU   B 49  ? 0.7512 0.7329 0.4835 0.0811  0.0823  -0.0039 58  LEU   B CD2 
781  N N   . ARG   B 50  ? 0.8412 0.8166 0.5994 0.0803  0.0830  -0.0143 59  ARG   B N   
782  C CA  . ARG   B 50  ? 0.8606 0.8342 0.6243 0.0830  0.0820  -0.0164 59  ARG   B CA  
783  C C   . ARG   B 50  ? 0.8513 0.8236 0.6105 0.0890  0.0791  -0.0137 59  ARG   B C   
784  O O   . ARG   B 50  ? 0.8058 0.7780 0.5592 0.0922  0.0784  -0.0088 59  ARG   B O   
785  C CB  . ARG   B 50  ? 0.9201 0.8916 0.6901 0.0829  0.0835  -0.0149 59  ARG   B CB  
786  C CG  . ARG   B 50  ? 0.9930 0.9622 0.7695 0.0856  0.0826  -0.0175 59  ARG   B CG  
787  C CD  . ARG   B 50  ? 1.0409 1.0070 0.8235 0.0840  0.0838  -0.0177 59  ARG   B CD  
788  N NE  . ARG   B 50  ? 1.0943 1.0595 0.8744 0.0825  0.0848  -0.0120 59  ARG   B NE  
789  C CZ  . ARG   B 50  ? 1.1392 1.1030 0.9174 0.0857  0.0838  -0.0056 59  ARG   B CZ  
790  N NH1 . ARG   B 50  ? 1.1775 1.1397 0.9559 0.0909  0.0818  -0.0040 59  ARG   B NH1 
791  N NH2 . ARG   B 50  ? 1.1689 1.1335 0.9451 0.0834  0.0848  -0.0006 59  ARG   B NH2 
792  N N   . SER   B 51  ? 0.8683 0.8404 0.6296 0.0905  0.0774  -0.0170 60  SER   B N   
793  C CA  . SER   B 51  ? 0.9114 0.8816 0.6704 0.0964  0.0746  -0.0148 60  SER   B CA  
794  C C   . SER   B 51  ? 0.9541 0.9237 0.7210 0.0981  0.0744  -0.0174 60  SER   B C   
795  O O   . SER   B 51  ? 0.9549 0.9264 0.7239 0.0973  0.0732  -0.0217 60  SER   B O   
796  C CB  . SER   B 51  ? 0.8975 0.8680 0.6497 0.0968  0.0717  -0.0160 60  SER   B CB  
797  O OG  . SER   B 51  ? 0.9121 0.8807 0.6625 0.1021  0.0689  -0.0145 60  SER   B OG  
798  N N   . GLY   B 52  ? 1.0084 0.9757 0.7798 0.1002  0.0753  -0.0149 61  GLY   B N   
799  C CA  . GLY   B 52  ? 1.0606 1.0265 0.8398 0.1017  0.0751  -0.0177 61  GLY   B CA  
800  C C   . GLY   B 52  ? 1.1168 1.0839 0.9019 0.0970  0.0773  -0.0226 61  GLY   B C   
801  O O   . GLY   B 52  ? 1.1162 1.0819 0.9016 0.0942  0.0791  -0.0209 61  GLY   B O   
802  N N   . GLU   B 53  ? 1.1959 1.1660 0.9855 0.0962  0.0772  -0.0284 62  GLU   B N   
803  C CA  . GLU   B 53  ? 1.2379 1.2109 1.0321 0.0915  0.0793  -0.0340 62  GLU   B CA  
804  C C   . GLU   B 53  ? 1.1597 1.1382 0.9504 0.0868  0.0797  -0.0368 62  GLU   B C   
805  O O   . GLU   B 53  ? 1.1261 1.1080 0.9200 0.0826  0.0816  -0.0414 62  GLU   B O   
806  C CB  . GLU   B 53  ? 1.3249 1.2983 1.1270 0.0938  0.0790  -0.0387 62  GLU   B CB  
807  C CG  . GLU   B 53  ? 1.4472 1.4141 1.2530 0.0957  0.0791  -0.0371 62  GLU   B CG  
808  C CD  . GLU   B 53  ? 1.5783 1.5449 1.3900 0.0939  0.0803  -0.0428 62  GLU   B CD  
809  O OE1 . GLU   B 53  ? 1.6985 1.6712 1.5136 0.0930  0.0809  -0.0490 62  GLU   B OE1 
810  O OE2 . GLU   B 53  ? 1.6338 1.5943 1.4465 0.0933  0.0805  -0.0408 62  GLU   B OE2 
811  N N   . GLY   B 54  ? 1.0762 1.0551 0.8601 0.0875  0.0779  -0.0341 63  GLY   B N   
812  C CA  . GLY   B 54  ? 1.0383 1.0207 0.8171 0.0828  0.0775  -0.0355 63  GLY   B CA  
813  C C   . GLY   B 54  ? 1.0040 0.9852 0.7786 0.0792  0.0793  -0.0335 63  GLY   B C   
814  O O   . GLY   B 54  ? 0.9974 0.9750 0.7707 0.0815  0.0800  -0.0291 63  GLY   B O   
815  N N   . ARG   B 55  ? 0.9392 0.9241 0.7120 0.0736  0.0799  -0.0363 64  ARG   B N   
816  C CA  . ARG   B 55  ? 0.9229 0.9076 0.6916 0.0695  0.0815  -0.0349 64  ARG   B CA  
817  C C   . ARG   B 55  ? 0.8763 0.8608 0.6363 0.0681  0.0789  -0.0335 64  ARG   B C   
818  O O   . ARG   B 55  ? 0.8525 0.8393 0.6114 0.0664  0.0768  -0.0361 64  ARG   B O   
819  C CB  . ARG   B 55  ? 0.9582 0.9468 0.7317 0.0636  0.0842  -0.0397 64  ARG   B CB  
820  C CG  . ARG   B 55  ? 0.9950 0.9831 0.7656 0.0596  0.0861  -0.0381 64  ARG   B CG  
821  C CD  . ARG   B 55  ? 1.0455 1.0377 0.8208 0.0538  0.0886  -0.0432 64  ARG   B CD  
822  N NE  . ARG   B 55  ? 1.0799 1.0724 0.8516 0.0490  0.0901  -0.0422 64  ARG   B NE  
823  C CZ  . ARG   B 55  ? 1.1113 1.1032 0.8859 0.0464  0.0927  -0.0426 64  ARG   B CZ  
824  N NH1 . ARG   B 55  ? 1.1084 1.0985 0.8894 0.0481  0.0939  -0.0440 64  ARG   B NH1 
825  N NH2 . ARG   B 55  ? 1.1269 1.1198 0.8978 0.0420  0.0938  -0.0415 64  ARG   B NH2 
826  N N   . LEU   B 56  ? 0.8295 0.8114 0.5831 0.0687  0.0788  -0.0296 65  LEU   B N   
827  C CA  . LEU   B 56  ? 0.8032 0.7839 0.5476 0.0675  0.0762  -0.0284 65  LEU   B CA  
828  C C   . LEU   B 56  ? 0.7626 0.7452 0.5060 0.0619  0.0783  -0.0292 65  LEU   B C   
829  O O   . LEU   B 56  ? 0.7383 0.7206 0.4830 0.0625  0.0808  -0.0267 65  LEU   B O   
830  C CB  . LEU   B 56  ? 0.8002 0.7769 0.5376 0.0738  0.0741  -0.0233 65  LEU   B CB  
831  C CG  . LEU   B 56  ? 0.8334 0.8080 0.5712 0.0800  0.0720  -0.0217 65  LEU   B CG  
832  C CD1 . LEU   B 56  ? 0.8190 0.7901 0.5469 0.0852  0.0686  -0.0181 65  LEU   B CD1 
833  C CD2 . LEU   B 56  ? 0.8382 0.8142 0.5796 0.0784  0.0704  -0.0256 65  LEU   B CD2 
834  N N   . ASP   B 57  ? 0.7467 0.7314 0.4879 0.0563  0.0772  -0.0322 66  ASP   B N   
835  C CA  . ASP   B 57  ? 0.7273 0.7137 0.4670 0.0507  0.0790  -0.0331 66  ASP   B CA  
836  C C   . ASP   B 57  ? 0.6884 0.6716 0.4177 0.0508  0.0758  -0.0306 66  ASP   B C   
837  O O   . ASP   B 57  ? 0.6810 0.6617 0.4047 0.0517  0.0717  -0.0306 66  ASP   B O   
838  C CB  . ASP   B 57  ? 0.7750 0.7666 0.5195 0.0438  0.0803  -0.0381 66  ASP   B CB  
839  C CG  . ASP   B 57  ? 0.8062 0.8010 0.5606 0.0438  0.0838  -0.0410 66  ASP   B CG  
840  O OD1 . ASP   B 57  ? 0.8658 0.8589 0.6229 0.0451  0.0863  -0.0394 66  ASP   B OD1 
841  O OD2 . ASP   B 57  ? 0.8335 0.8322 0.5927 0.0428  0.0836  -0.0447 66  ASP   B OD2 
842  N N   . PRO   B 58  ? 0.6512 0.6342 0.3774 0.0497  0.0772  -0.0287 67  PRO   B N   
843  C CA  . PRO   B 58  ? 0.6448 0.6247 0.3609 0.0501  0.0739  -0.0268 67  PRO   B CA  
844  C C   . PRO   B 58  ? 0.6452 0.6251 0.3583 0.0441  0.0710  -0.0300 67  PRO   B C   
845  O O   . PRO   B 58  ? 0.6500 0.6344 0.3693 0.0382  0.0730  -0.0335 67  PRO   B O   
846  C CB  . PRO   B 58  ? 0.6459 0.6275 0.3616 0.0488  0.0769  -0.0248 67  PRO   B CB  
847  C CG  . PRO   B 58  ? 0.6425 0.6282 0.3683 0.0447  0.0814  -0.0271 67  PRO   B CG  
848  C CD  . PRO   B 58  ? 0.6471 0.6327 0.3790 0.0476  0.0816  -0.0284 67  PRO   B CD  
849  N N   . TYR   B 59  ? 0.6269 0.6018 0.3302 0.0457  0.0660  -0.0287 68  TYR   B N   
850  C CA  . TYR   B 59  ? 0.6197 0.5933 0.3183 0.0400  0.0620  -0.0307 68  TYR   B CA  
851  C C   . TYR   B 59  ? 0.6159 0.5855 0.3049 0.0390  0.0593  -0.0292 68  TYR   B C   
852  O O   . TYR   B 59  ? 0.6028 0.5731 0.2898 0.0320  0.0580  -0.0309 68  TYR   B O   
853  C CB  . TYR   B 59  ? 0.6256 0.5958 0.3212 0.0427  0.0574  -0.0307 68  TYR   B CB  
854  C CG  . TYR   B 59  ? 0.6285 0.5972 0.3189 0.0366  0.0525  -0.0322 68  TYR   B CG  
855  C CD1 . TYR   B 59  ? 0.6343 0.5961 0.3133 0.0363  0.0472  -0.0307 68  TYR   B CD1 
856  C CD2 . TYR   B 59  ? 0.6292 0.6035 0.3257 0.0314  0.0528  -0.0349 68  TYR   B CD2 
857  C CE1 . TYR   B 59  ? 0.6467 0.6063 0.3203 0.0301  0.0420  -0.0316 68  TYR   B CE1 
858  C CE2 . TYR   B 59  ? 0.6375 0.6112 0.3290 0.0252  0.0479  -0.0356 68  TYR   B CE2 
859  C CZ  . TYR   B 59  ? 0.6488 0.6147 0.3287 0.0241  0.0423  -0.0338 68  TYR   B CZ  
860  O OH  . TYR   B 59  ? 0.6590 0.6231 0.3329 0.0172  0.0367  -0.0341 68  TYR   B OH  
861  N N   . TRP   B 60  ? 0.6100 0.5759 0.2932 0.0459  0.0584  -0.0261 69  TRP   B N   
862  C CA  . TRP   B 60  ? 0.6136 0.5748 0.2862 0.0470  0.0548  -0.0246 69  TRP   B CA  
863  C C   . TRP   B 60  ? 0.6216 0.5843 0.2934 0.0536  0.0574  -0.0215 69  TRP   B C   
864  O O   . TRP   B 60  ? 0.6269 0.5908 0.3019 0.0597  0.0591  -0.0197 69  TRP   B O   
865  C CB  . TRP   B 60  ? 0.6168 0.5698 0.2785 0.0491  0.0473  -0.0243 69  TRP   B CB  
866  C CG  . TRP   B 60  ? 0.6284 0.5760 0.2789 0.0522  0.0435  -0.0228 69  TRP   B CG  
867  C CD1 . TRP   B 60  ? 0.6378 0.5834 0.2832 0.0466  0.0413  -0.0236 69  TRP   B CD1 
868  C CD2 . TRP   B 60  ? 0.6390 0.5833 0.2823 0.0618  0.0417  -0.0202 69  TRP   B CD2 
869  N NE1 . TRP   B 60  ? 0.6456 0.5867 0.2814 0.0523  0.0383  -0.0218 69  TRP   B NE1 
870  C CE2 . TRP   B 60  ? 0.6396 0.5803 0.2738 0.0619  0.0385  -0.0198 69  TRP   B CE2 
871  C CE3 . TRP   B 60  ? 0.6373 0.5820 0.2807 0.0707  0.0424  -0.0181 69  TRP   B CE3 
872  C CZ2 . TRP   B 60  ? 0.6420 0.5798 0.2674 0.0708  0.0361  -0.0178 69  TRP   B CZ2 
873  C CZ3 . TRP   B 60  ? 0.6351 0.5776 0.2699 0.0791  0.0401  -0.0159 69  TRP   B CZ3 
874  C CH2 . TRP   B 60  ? 0.6467 0.5858 0.2725 0.0795  0.0369  -0.0159 69  TRP   B CH2 
875  N N   . GLY   B 61  ? 0.6261 0.5890 0.2934 0.0526  0.0575  -0.0206 70  GLY   B N   
876  C CA  . GLY   B 61  ? 0.6289 0.5942 0.2941 0.0590  0.0594  -0.0173 70  GLY   B CA  
877  C C   . GLY   B 61  ? 0.6406 0.6049 0.2985 0.0580  0.0577  -0.0168 70  GLY   B C   
878  O O   . GLY   B 61  ? 0.6288 0.5925 0.2868 0.0501  0.0572  -0.0191 70  GLY   B O   
879  N N   . ASP   B 62  ? 0.6420 0.6077 0.2951 0.0652  0.0576  -0.0138 71  ASP   B N   
880  C CA  . ASP   B 62  ? 0.6690 0.6349 0.3149 0.0662  0.0562  -0.0128 71  ASP   B CA  
881  C C   . ASP   B 62  ? 0.6684 0.6410 0.3146 0.0733  0.0591  -0.0090 71  ASP   B C   
882  O O   . ASP   B 62  ? 0.6842 0.6554 0.3255 0.0818  0.0568  -0.0074 71  ASP   B O   
883  C CB  . ASP   B 62  ? 0.7068 0.6634 0.3403 0.0690  0.0486  -0.0140 71  ASP   B CB  
884  C CG  . ASP   B 62  ? 0.7501 0.7055 0.3752 0.0702  0.0461  -0.0135 71  ASP   B CG  
885  O OD1 . ASP   B 62  ? 0.7902 0.7531 0.4189 0.0701  0.0505  -0.0118 71  ASP   B OD1 
886  O OD2 . ASP   B 62  ? 0.8327 0.7795 0.4477 0.0707  0.0395  -0.0149 71  ASP   B OD2 
887  N N   . VAL   B 63  ? 0.6629 0.6429 0.3149 0.0698  0.0640  -0.0075 72  VAL   B N   
888  C CA  . VAL   B 63  ? 0.6751 0.6635 0.3282 0.0748  0.0672  -0.0034 72  VAL   B CA  
889  C C   . VAL   B 63  ? 0.6947 0.6822 0.3359 0.0833  0.0628  -0.0020 72  VAL   B C   
890  O O   . VAL   B 63  ? 0.7100 0.7038 0.3499 0.0906  0.0640  0.0014  72  VAL   B O   
891  C CB  . VAL   B 63  ? 0.6727 0.6677 0.3326 0.0677  0.0721  -0.0026 72  VAL   B CB  
892  C CG1 . VAL   B 63  ? 0.6800 0.6829 0.3371 0.0720  0.0735  0.0013  72  VAL   B CG1 
893  C CG2 . VAL   B 63  ? 0.6793 0.6774 0.3510 0.0623  0.0771  -0.0025 72  VAL   B CG2 
894  N N   . LYS   B 64  ? 0.7139 0.6940 0.3462 0.0828  0.0577  -0.0045 73  LYS   B N   
895  C CA  . LYS   B 64  ? 0.7294 0.7085 0.3500 0.0916  0.0533  -0.0036 73  LYS   B CA  
896  C C   . LYS   B 64  ? 0.7189 0.6933 0.3325 0.1012  0.0489  -0.0034 73  LYS   B C   
897  O O   . LYS   B 64  ? 0.7168 0.6956 0.3246 0.1103  0.0480  -0.0012 73  LYS   B O   
898  C CB  . LYS   B 64  ? 0.7429 0.7147 0.3553 0.0885  0.0484  -0.0062 73  LYS   B CB  
899  C CG  . LYS   B 64  ? 0.7694 0.7415 0.3704 0.0982  0.0444  -0.0051 73  LYS   B CG  
900  C CD  . LYS   B 64  ? 0.7889 0.7559 0.3825 0.0956  0.0404  -0.0068 73  LYS   B CD  
901  C CE  . LYS   B 64  ? 0.8240 0.7947 0.4085 0.1057  0.0380  -0.0054 73  LYS   B CE  
902  N NZ  . LYS   B 64  ? 0.8591 0.8212 0.4337 0.1045  0.0320  -0.0076 73  LYS   B NZ  
903  N N   . GLN   B 65  ? 0.7133 0.6789 0.3263 0.0991  0.0458  -0.0058 74  GLN   B N   
904  C CA  . GLN   B 65  ? 0.7207 0.6810 0.3285 0.1066  0.0418  -0.0060 74  GLN   B CA  
905  C C   . GLN   B 65  ? 0.7047 0.6733 0.3208 0.1100  0.0470  -0.0030 74  GLN   B C   
906  O O   . GLN   B 65  ? 0.6927 0.6600 0.3038 0.1185  0.0445  -0.0021 74  GLN   B O   
907  C CB  . GLN   B 65  ? 0.7393 0.6893 0.3463 0.1014  0.0379  -0.0091 74  GLN   B CB  
908  C CG  . GLN   B 65  ? 0.7709 0.7105 0.3671 0.0994  0.0308  -0.0116 74  GLN   B CG  
909  C CD  . GLN   B 65  ? 0.7999 0.7312 0.3966 0.0927  0.0273  -0.0141 74  GLN   B CD  
910  O OE1 . GLN   B 65  ? 0.8530 0.7794 0.4475 0.0961  0.0242  -0.0144 74  GLN   B OE1 
911  N NE2 . GLN   B 65  ? 0.8177 0.7480 0.4176 0.0826  0.0277  -0.0157 74  GLN   B NE2 
912  N N   . ASP   B 66  ? 0.6786 0.6551 0.3063 0.1036  0.0535  -0.0016 75  ASP   B N   
913  C CA  . ASP   B 66  ? 0.6609 0.6447 0.2985 0.1037  0.0589  0.0011  75  ASP   B CA  
914  C C   . ASP   B 66  ? 0.6493 0.6271 0.2891 0.1042  0.0572  -0.0002 75  ASP   B C   
915  O O   . ASP   B 66  ? 0.6331 0.6147 0.2748 0.1099  0.0585  0.0023  75  ASP   B O   
916  C CB  . ASP   B 66  ? 0.6708 0.6638 0.3063 0.1122  0.0605  0.0056  75  ASP   B CB  
917  C CG  . ASP   B 66  ? 0.6644 0.6657 0.3101 0.1111  0.0659  0.0093  75  ASP   B CG  
918  O OD1 . ASP   B 66  ? 0.6516 0.6530 0.3069 0.1031  0.0694  0.0086  75  ASP   B OD1 
919  O OD2 . ASP   B 66  ? 0.6995 0.7067 0.3428 0.1189  0.0661  0.0128  75  ASP   B OD2 
920  N N   . LEU   B 67  ? 0.6322 0.6025 0.2726 0.0980  0.0549  -0.0040 76  LEU   B N   
921  C CA  . LEU   B 67  ? 0.6224 0.5874 0.2654 0.0974  0.0532  -0.0057 76  LEU   B CA  
922  C C   . LEU   B 67  ? 0.6269 0.5925 0.2801 0.0877  0.0564  -0.0081 76  LEU   B C   
923  O O   . LEU   B 67  ? 0.6196 0.5865 0.2749 0.0806  0.0579  -0.0097 76  LEU   B O   
924  C CB  . LEU   B 67  ? 0.6277 0.5827 0.2590 0.1005  0.0457  -0.0079 76  LEU   B CB  
925  C CG  . LEU   B 67  ? 0.6310 0.5846 0.2517 0.1117  0.0419  -0.0060 76  LEU   B CG  
926  C CD1 . LEU   B 67  ? 0.6374 0.5795 0.2459 0.1139  0.0338  -0.0085 76  LEU   B CD1 
927  C CD2 . LEU   B 67  ? 0.6339 0.5914 0.2584 0.1179  0.0439  -0.0036 76  LEU   B CD2 
928  N N   . VAL   B 68  ? 0.6240 0.5888 0.2832 0.0875  0.0572  -0.0087 77  VAL   B N   
929  C CA  . VAL   B 68  ? 0.6172 0.5828 0.2860 0.0794  0.0598  -0.0116 77  VAL   B CA  
930  C C   . VAL   B 68  ? 0.6156 0.5774 0.2854 0.0813  0.0573  -0.0128 77  VAL   B C   
931  O O   . VAL   B 68  ? 0.6227 0.5841 0.2907 0.0888  0.0564  -0.0104 77  VAL   B O   
932  C CB  . VAL   B 68  ? 0.6182 0.5909 0.2976 0.0764  0.0662  -0.0103 77  VAL   B CB  
933  C CG1 . VAL   B 68  ? 0.6264 0.6023 0.3084 0.0831  0.0680  -0.0066 77  VAL   B CG1 
934  C CG2 . VAL   B 68  ? 0.6169 0.5907 0.3058 0.0689  0.0686  -0.0138 77  VAL   B CG2 
935  N N   . SER   B 69  ? 0.6032 0.5631 0.2758 0.0748  0.0561  -0.0161 78  SER   B N   
936  C CA  . SER   B 69  ? 0.5999 0.5573 0.2746 0.0749  0.0538  -0.0177 78  SER   B CA  
937  C C   . SER   B 69  ? 0.5982 0.5608 0.2847 0.0689  0.0582  -0.0201 78  SER   B C   
938  O O   . SER   B 69  ? 0.5894 0.5554 0.2797 0.0619  0.0608  -0.0220 78  SER   B O   
939  C CB  . SER   B 69  ? 0.6130 0.5637 0.2788 0.0731  0.0474  -0.0192 78  SER   B CB  
940  O OG  . SER   B 69  ? 0.6185 0.5706 0.2866 0.0638  0.0476  -0.0220 78  SER   B OG  
941  N N   . TYR   B 70  ? 0.5995 0.5627 0.2913 0.0711  0.0585  -0.0204 79  TYR   B N   
942  C CA  . TYR   B 70  ? 0.5988 0.5668 0.3019 0.0671  0.0623  -0.0229 79  TYR   B CA  
943  C C   . TYR   B 70  ? 0.6105 0.5776 0.3141 0.0653  0.0591  -0.0253 79  TYR   B C   
944  O O   . TYR   B 70  ? 0.6040 0.5667 0.3021 0.0702  0.0551  -0.0238 79  TYR   B O   
945  C CB  . TYR   B 70  ? 0.5964 0.5665 0.3061 0.0721  0.0659  -0.0207 79  TYR   B CB  
946  C CG  . TYR   B 70  ? 0.5954 0.5680 0.3064 0.0723  0.0696  -0.0182 79  TYR   B CG  
947  C CD1 . TYR   B 70  ? 0.6001 0.5715 0.3033 0.0767  0.0684  -0.0147 79  TYR   B CD1 
948  C CD2 . TYR   B 70  ? 0.6026 0.5791 0.3224 0.0681  0.0740  -0.0195 79  TYR   B CD2 
949  C CE1 . TYR   B 70  ? 0.5974 0.5724 0.3021 0.0766  0.0718  -0.0121 79  TYR   B CE1 
950  C CE2 . TYR   B 70  ? 0.6017 0.5805 0.3226 0.0676  0.0771  -0.0170 79  TYR   B CE2 
951  C CZ  . TYR   B 70  ? 0.6036 0.5821 0.3172 0.0716  0.0761  -0.0132 79  TYR   B CZ  
952  O OH  . TYR   B 70  ? 0.6179 0.5998 0.3333 0.0704  0.0792  -0.0106 79  TYR   B OH  
953  N N   . CYS   B 71  ? 0.6231 0.5950 0.3333 0.0585  0.0607  -0.0288 80  CYS   B N   
954  C CA  . CYS   B 71  ? 0.6445 0.6185 0.3575 0.0555  0.0586  -0.0314 80  CYS   B CA  
955  C C   . CYS   B 71  ? 0.6415 0.6116 0.3451 0.0520  0.0528  -0.0314 80  CYS   B C   
956  O O   . CYS   B 71  ? 0.6615 0.6341 0.3664 0.0479  0.0505  -0.0333 80  CYS   B O   
957  C CB  . CYS   B 71  ? 0.6756 0.6486 0.3914 0.0617  0.0578  -0.0305 80  CYS   B CB  
958  S SG  . CYS   B 71  ? 0.7455 0.7211 0.4710 0.0663  0.0635  -0.0296 80  CYS   B SG  
959  N N   . GLY   B 72  ? 0.6265 0.5908 0.3205 0.0532  0.0501  -0.0294 81  GLY   B N   
960  C CA  . GLY   B 72  ? 0.6242 0.5835 0.3087 0.0496  0.0437  -0.0295 81  GLY   B CA  
961  C C   . GLY   B 72  ? 0.6233 0.5759 0.2974 0.0523  0.0412  -0.0274 81  GLY   B C   
962  O O   . GLY   B 72  ? 0.6156 0.5689 0.2904 0.0568  0.0445  -0.0258 81  GLY   B O   
963  N N   . PRO   B 73  ? 0.6334 0.5797 0.2976 0.0493  0.0347  -0.0273 82  PRO   B N   
964  C CA  . PRO   B 73  ? 0.6484 0.5873 0.3013 0.0521  0.0309  -0.0257 82  PRO   B CA  
965  C C   . PRO   B 73  ? 0.6633 0.5961 0.3092 0.0628  0.0284  -0.0233 82  PRO   B C   
966  O O   . PRO   B 73  ? 0.6753 0.6068 0.3221 0.0664  0.0269  -0.0230 82  PRO   B O   
967  C CB  . PRO   B 73  ? 0.6512 0.5844 0.2956 0.0455  0.0239  -0.0264 82  PRO   B CB  
968  C CG  . PRO   B 73  ? 0.6502 0.5869 0.2999 0.0413  0.0228  -0.0275 82  PRO   B CG  
969  C CD  . PRO   B 73  ? 0.6383 0.5847 0.3016 0.0430  0.0304  -0.0286 82  PRO   B CD  
970  N N   . TRP   B 74  ? 0.6741 0.6035 0.3127 0.0675  0.0276  -0.0219 83  TRP   B N   
971  C CA  . TRP   B 74  ? 0.6874 0.6114 0.3176 0.0780  0.0247  -0.0198 83  TRP   B CA  
972  C C   . TRP   B 74  ? 0.7228 0.6377 0.3443 0.0802  0.0170  -0.0200 83  TRP   B C   
973  O O   . TRP   B 74  ? 0.7219 0.6300 0.3355 0.0756  0.0110  -0.0209 83  TRP   B O   
974  C CB  . TRP   B 74  ? 0.6804 0.6019 0.3023 0.0814  0.0235  -0.0188 83  TRP   B CB  
975  C CG  . TRP   B 74  ? 0.6707 0.5901 0.2860 0.0927  0.0222  -0.0167 83  TRP   B CG  
976  C CD1 . TRP   B 74  ? 0.6771 0.5874 0.2798 0.0995  0.0150  -0.0165 83  TRP   B CD1 
977  C CD2 . TRP   B 74  ? 0.6571 0.5844 0.2779 0.0986  0.0281  -0.0145 83  TRP   B CD2 
978  N NE1 . TRP   B 74  ? 0.6707 0.5834 0.2706 0.1096  0.0163  -0.0145 83  TRP   B NE1 
979  C CE2 . TRP   B 74  ? 0.6614 0.5849 0.2726 0.1090  0.0243  -0.0130 83  TRP   B CE2 
980  C CE3 . TRP   B 74  ? 0.6431 0.5802 0.2759 0.0960  0.0358  -0.0135 83  TRP   B CE3 
981  C CZ2 . TRP   B 74  ? 0.6572 0.5877 0.2706 0.1164  0.0284  -0.0102 83  TRP   B CZ2 
982  C CZ3 . TRP   B 74  ? 0.6415 0.5843 0.2763 0.1029  0.0394  -0.0106 83  TRP   B CZ3 
983  C CH2 . TRP   B 74  ? 0.6493 0.5895 0.2747 0.1129  0.0359  -0.0088 83  TRP   B CH2 
984  N N   . LYS   B 75  ? 0.7453 0.6595 0.3671 0.0876  0.0166  -0.0188 84  LYS   B N   
985  C CA  . LYS   B 75  ? 0.7712 0.6777 0.3863 0.0897  0.0099  -0.0189 84  LYS   B CA  
986  C C   . LYS   B 75  ? 0.8060 0.7034 0.4075 0.0996  0.0040  -0.0178 84  LYS   B C   
987  O O   . LYS   B 75  ? 0.8410 0.7296 0.4342 0.1007  -0.0031 -0.0181 84  LYS   B O   
988  C CB  . LYS   B 75  ? 0.7798 0.6920 0.4050 0.0911  0.0137  -0.0186 84  LYS   B CB  
989  C CG  . LYS   B 75  ? 0.7684 0.6888 0.4061 0.0821  0.0183  -0.0203 84  LYS   B CG  
990  C CD  . LYS   B 75  ? 0.7850 0.7020 0.4193 0.0739  0.0129  -0.0218 84  LYS   B CD  
991  C CE  . LYS   B 75  ? 0.7912 0.7180 0.4377 0.0652  0.0177  -0.0238 84  LYS   B CE  
992  N NZ  . LYS   B 75  ? 0.8234 0.7482 0.4663 0.0569  0.0122  -0.0247 84  LYS   B NZ  
993  N N   . LEU   B 76  ? 0.8167 0.7165 0.4157 0.1068  0.0065  -0.0165 85  LEU   B N   
994  C CA  . LEU   B 76  ? 0.8189 0.7138 0.4074 0.1183  0.0027  -0.0153 85  LEU   B CA  
995  C C   . LEU   B 76  ? 0.8568 0.7429 0.4317 0.1203  -0.0036 -0.0161 85  LEU   B C   
996  O O   . LEU   B 76  ? 0.8556 0.7457 0.4312 0.1190  -0.0006 -0.0160 85  LEU   B O   
997  C CB  . LEU   B 76  ? 0.7947 0.6997 0.3897 0.1245  0.0099  -0.0130 85  LEU   B CB  
998  C CG  . LEU   B 76  ? 0.7758 0.6898 0.3854 0.1214  0.0169  -0.0121 85  LEU   B CG  
999  C CD1 . LEU   B 76  ? 0.7701 0.6936 0.3852 0.1267  0.0233  -0.0094 85  LEU   B CD1 
1000 C CD2 . LEU   B 76  ? 0.7781 0.6886 0.3881 0.1236  0.0141  -0.0122 85  LEU   B CD2 
1001 N N   . ASP   B 77  ? 0.9083 0.7823 0.4709 0.1230  -0.0125 -0.0170 86  ASP   B N   
1002 C CA  . ASP   B 77  ? 0.9632 0.8260 0.5118 0.1233  -0.0203 -0.0182 86  ASP   B CA  
1003 C C   . ASP   B 77  ? 0.9618 0.8161 0.4962 0.1357  -0.0269 -0.0184 86  ASP   B C   
1004 O O   . ASP   B 77  ? 0.9876 0.8312 0.5091 0.1373  -0.0344 -0.0196 86  ASP   B O   
1005 C CB  . ASP   B 77  ? 1.0109 0.8655 0.5567 0.1129  -0.0264 -0.0194 86  ASP   B CB  
1006 C CG  . ASP   B 77  ? 1.0763 0.9250 0.6202 0.1127  -0.0312 -0.0194 86  ASP   B CG  
1007 O OD1 . ASP   B 77  ? 1.0777 0.9312 0.6264 0.1190  -0.0278 -0.0186 86  ASP   B OD1 
1008 O OD2 . ASP   B 77  ? 1.1426 0.9823 0.6804 0.1059  -0.0384 -0.0200 86  ASP   B OD2 
1009 N N   . ALA   B 78  ? 0.9439 0.8029 0.4801 0.1445  -0.0243 -0.0172 87  ALA   B N   
1010 C CA  . ALA   B 78  ? 0.9138 0.7663 0.4365 0.1573  -0.0300 -0.0175 87  ALA   B CA  
1011 C C   . ALA   B 78  ? 0.8973 0.7557 0.4167 0.1642  -0.0273 -0.0171 87  ALA   B C   
1012 O O   . ALA   B 78  ? 0.8830 0.7536 0.4135 0.1604  -0.0190 -0.0157 87  ALA   B O   
1013 C CB  . ALA   B 78  ? 0.9187 0.7752 0.4452 0.1635  -0.0279 -0.0162 87  ALA   B CB  
1014 N N   . ALA   B 79  ? 0.8933 0.7434 0.3975 0.1743  -0.0344 -0.0184 88  ALA   B N   
1015 C CA  . ALA   B 79  ? 0.8902 0.7437 0.3875 0.1822  -0.0344 -0.0186 88  ALA   B CA  
1016 C C   . ALA   B 79  ? 0.8971 0.7511 0.3847 0.1972  -0.0370 -0.0187 88  ALA   B C   
1017 O O   . ALA   B 79  ? 0.8729 0.7155 0.3513 0.2011  -0.0443 -0.0201 88  ALA   B O   
1018 C CB  . ALA   B 79  ? 0.9050 0.7447 0.3905 0.1793  -0.0428 -0.0210 88  ALA   B CB  
1019 N N   . TRP   B 80  ? 0.8978 0.7647 0.3869 0.2051  -0.0318 -0.0172 89  TRP   B N   
1020 C CA  . TRP   B 80  ? 0.9226 0.7911 0.4003 0.2203  -0.0350 -0.0177 89  TRP   B CA  
1021 C C   . TRP   B 80  ? 0.9558 0.8069 0.4153 0.2258  -0.0465 -0.0214 89  TRP   B C   
1022 O O   . TRP   B 80  ? 0.9415 0.7856 0.3981 0.2194  -0.0495 -0.0228 89  TRP   B O   
1023 C CB  . TRP   B 80  ? 0.9089 0.7948 0.3909 0.2262  -0.0278 -0.0155 89  TRP   B CB  
1024 C CG  . TRP   B 80  ? 0.9244 0.8143 0.3953 0.2419  -0.0306 -0.0159 89  TRP   B CG  
1025 C CD1 . TRP   B 80  ? 0.9218 0.8093 0.3870 0.2505  -0.0337 -0.0162 89  TRP   B CD1 
1026 C CD2 . TRP   B 80  ? 0.9216 0.8203 0.3863 0.2511  -0.0301 -0.0160 89  TRP   B CD2 
1027 N NE1 . TRP   B 80  ? 0.9358 0.8300 0.3913 0.2645  -0.0353 -0.0167 89  TRP   B NE1 
1028 C CE2 . TRP   B 80  ? 0.9305 0.8320 0.3857 0.2653  -0.0331 -0.0165 89  TRP   B CE2 
1029 C CE3 . TRP   B 80  ? 0.9218 0.8265 0.3878 0.2489  -0.0277 -0.0158 89  TRP   B CE3 
1030 C CZ2 . TRP   B 80  ? 0.9285 0.8392 0.3754 0.2775  -0.0337 -0.0170 89  TRP   B CZ2 
1031 C CZ3 . TRP   B 80  ? 0.9231 0.8367 0.3812 0.2607  -0.0283 -0.0160 89  TRP   B CZ3 
1032 C CH2 . TRP   B 80  ? 0.9254 0.8424 0.3742 0.2749  -0.0311 -0.0166 89  TRP   B CH2 
1033 N N   . ASP   B 81  ? 0.9953 0.8391 0.4427 0.2368  -0.0531 -0.0231 90  ASP   B N   
1034 C CA  . ASP   B 81  ? 1.0335 0.8579 0.4623 0.2421  -0.0654 -0.0268 90  ASP   B CA  
1035 C C   . ASP   B 81  ? 1.0556 0.8833 0.4736 0.2546  -0.0677 -0.0285 90  ASP   B C   
1036 O O   . ASP   B 81  ? 1.1168 0.9287 0.5187 0.2601  -0.0781 -0.0318 90  ASP   B O   
1037 C CB  . ASP   B 81  ? 1.0556 0.8684 0.4762 0.2468  -0.0724 -0.0281 90  ASP   B CB  
1038 C CG  . ASP   B 81  ? 1.0521 0.8741 0.4700 0.2604  -0.0704 -0.0276 90  ASP   B CG  
1039 O OD1 . ASP   B 81  ? 1.0604 0.9001 0.4843 0.2658  -0.0627 -0.0257 90  ASP   B OD1 
1040 O OD2 . ASP   B 81  ? 1.1094 0.9213 0.5191 0.2651  -0.0768 -0.0290 90  ASP   B OD2 
1041 N N   . GLY   B 82  ? 1.0476 0.8951 0.4742 0.2583  -0.0585 -0.0260 91  GLY   B N   
1042 C CA  . GLY   B 82  ? 1.0560 0.9113 0.4749 0.2697  -0.0588 -0.0269 91  GLY   B CA  
1043 C C   . GLY   B 82  ? 1.0669 0.9249 0.4749 0.2861  -0.0622 -0.0282 91  GLY   B C   
1044 O O   . GLY   B 82  ? 1.0702 0.9358 0.4708 0.2972  -0.0628 -0.0293 91  GLY   B O   
1045 N N   . LEU   B 83  ? 1.0841 0.9368 0.4908 0.2880  -0.0643 -0.0283 92  LEU   B N   
1046 C CA  . LEU   B 83  ? 1.0987 0.9506 0.4930 0.3037  -0.0693 -0.0301 92  LEU   B CA  
1047 C C   . LEU   B 83  ? 1.1025 0.9693 0.5074 0.3051  -0.0616 -0.0265 92  LEU   B C   
1048 O O   . LEU   B 83  ? 1.1150 0.9972 0.5184 0.3163  -0.0581 -0.0255 92  LEU   B O   
1049 C CB  . LEU   B 83  ? 1.1280 0.9556 0.5079 0.3050  -0.0815 -0.0340 92  LEU   B CB  
1050 C CG  . LEU   B 83  ? 1.1624 0.9739 0.5230 0.3136  -0.0929 -0.0387 92  LEU   B CG  
1051 C CD1 . LEU   B 83  ? 1.1854 0.9804 0.5299 0.3233  -0.1036 -0.0422 92  LEU   B CD1 
1052 C CD2 . LEU   B 83  ? 1.1667 0.9921 0.5231 0.3253  -0.0904 -0.0394 92  LEU   B CD2 
1053 N N   . SER   B 84  ? 1.0871 0.9491 0.5011 0.2948  -0.0598 -0.0249 93  SER   B N   
1054 C CA  . SER   B 84  ? 1.0645 0.9351 0.4859 0.2965  -0.0552 -0.0222 93  SER   B CA  
1055 C C   . SER   B 84  ? 1.0462 0.9392 0.4847 0.2920  -0.0429 -0.0172 93  SER   B C   
1056 O O   . SER   B 84  ? 1.0481 0.9473 0.4951 0.2840  -0.0378 -0.0158 93  SER   B O   
1057 C CB  . SER   B 84  ? 1.0874 0.9444 0.5122 0.2868  -0.0582 -0.0225 93  SER   B CB  
1058 O OG  . SER   B 84  ? 1.1094 0.9492 0.5290 0.2786  -0.0649 -0.0251 93  SER   B OG  
1059 N N   . GLU   B 85  ? 1.0198 0.9242 0.4633 0.2965  -0.0384 -0.0144 94  GLU   B N   
1060 C CA  . GLU   B 85  ? 0.9817 0.9061 0.4416 0.2916  -0.0274 -0.0091 94  GLU   B CA  
1061 C C   . GLU   B 85  ? 0.9362 0.8552 0.4104 0.2756  -0.0236 -0.0077 94  GLU   B C   
1062 O O   . GLU   B 85  ? 0.9311 0.8328 0.4018 0.2702  -0.0298 -0.0105 94  GLU   B O   
1063 C CB  . GLU   B 85  ? 1.0152 0.9520 0.4744 0.3016  -0.0250 -0.0066 94  GLU   B CB  
1064 C CG  . GLU   B 85  ? 1.0224 0.9704 0.4705 0.3166  -0.0263 -0.0072 94  GLU   B CG  
1065 C CD  . GLU   B 85  ? 1.0348 0.9985 0.4822 0.3269  -0.0233 -0.0043 94  GLU   B CD  
1066 O OE1 . GLU   B 85  ? 0.9907 0.9612 0.4492 0.3218  -0.0180 -0.0003 94  GLU   B OE1 
1067 O OE2 . GLU   B 85  ? 1.0429 1.0129 0.4786 0.3403  -0.0263 -0.0059 94  GLU   B OE2 
1068 N N   . VAL   B 86  ? 0.8765 0.8113 0.3657 0.2696  -0.0142 -0.0032 95  VAL   B N   
1069 C CA  . VAL   B 86  ? 0.8485 0.7827 0.3531 0.2554  -0.0089 -0.0014 95  VAL   B CA  
1070 C C   . VAL   B 86  ? 0.8209 0.7710 0.3378 0.2545  -0.0008 0.0036  95  VAL   B C   
1071 O O   . VAL   B 86  ? 0.8257 0.7894 0.3399 0.2635  0.0015  0.0061  95  VAL   B O   
1072 C CB  . VAL   B 86  ? 0.8229 0.7573 0.3331 0.2459  -0.0062 -0.0018 95  VAL   B CB  
1073 C CG1 . VAL   B 86  ? 0.8266 0.7463 0.3234 0.2477  -0.0145 -0.0064 95  VAL   B CG1 
1074 C CG2 . VAL   B 86  ? 0.8181 0.7707 0.3342 0.2474  0.0008  0.0016  95  VAL   B CG2 
1075 N N   . GLN   B 87  ? 0.8011 0.7501 0.3311 0.2435  0.0032  0.0050  96  GLN   B N   
1076 C CA  . GLN   B 87  ? 0.7994 0.7619 0.3427 0.2404  0.0110  0.0100  96  GLN   B CA  
1077 C C   . GLN   B 87  ? 0.7647 0.7317 0.3213 0.2284  0.0172  0.0115  96  GLN   B C   
1078 O O   . GLN   B 87  ? 0.7853 0.7424 0.3464 0.2196  0.0162  0.0091  96  GLN   B O   
1079 C CB  . GLN   B 87  ? 0.7996 0.7570 0.3459 0.2401  0.0098  0.0104  96  GLN   B CB  
1080 C CG  . GLN   B 87  ? 0.8182 0.7727 0.3514 0.2525  0.0040  0.0093  96  GLN   B CG  
1081 C CD  . GLN   B 87  ? 0.8242 0.7776 0.3605 0.2540  0.0037  0.0108  96  GLN   B CD  
1082 O OE1 . GLN   B 87  ? 0.8126 0.7652 0.3604 0.2456  0.0070  0.0122  96  GLN   B OE1 
1083 N NE2 . GLN   B 87  ? 0.8248 0.7775 0.3496 0.2654  -0.0007 0.0102  96  GLN   B NE2 
1084 N N   . LEU   B 88  ? 0.7355 0.7174 0.2981 0.2282  0.0233  0.0155  97  LEU   B N   
1085 C CA  . LEU   B 88  ? 0.7238 0.7125 0.3012 0.2175  0.0304  0.0184  97  LEU   B CA  
1086 C C   . LEU   B 88  ? 0.7240 0.7130 0.3107 0.2143  0.0328  0.0206  97  LEU   B C   
1087 O O   . LEU   B 88  ? 0.7297 0.7269 0.3157 0.2207  0.0339  0.0241  97  LEU   B O   
1088 C CB  . LEU   B 88  ? 0.7157 0.7207 0.2955 0.2194  0.0353  0.0226  97  LEU   B CB  
1089 C CG  . LEU   B 88  ? 0.7075 0.7198 0.3016 0.2089  0.0422  0.0260  97  LEU   B CG  
1090 C CD1 . LEU   B 88  ? 0.7163 0.7193 0.3143 0.1991  0.0422  0.0223  97  LEU   B CD1 
1091 C CD2 . LEU   B 88  ? 0.7055 0.7344 0.3010 0.2111  0.0465  0.0307  97  LEU   B CD2 
1092 N N   . LEU   B 89  ? 0.7119 0.6921 0.3059 0.2055  0.0330  0.0186  98  LEU   B N   
1093 C CA  . LEU   B 89  ? 0.7050 0.6869 0.3099 0.2013  0.0363  0.0209  98  LEU   B CA  
1094 C C   . LEU   B 89  ? 0.7008 0.6930 0.3168 0.1947  0.0430  0.0246  98  LEU   B C   
1095 O O   . LEU   B 89  ? 0.7327 0.7213 0.3561 0.1854  0.0450  0.0228  98  LEU   B O   
1096 C CB  . LEU   B 89  ? 0.7058 0.6749 0.3129 0.1956  0.0332  0.0169  98  LEU   B CB  
1097 C CG  . LEU   B 89  ? 0.7166 0.6856 0.3358 0.1898  0.0363  0.0182  98  LEU   B CG  
1098 C CD1 . LEU   B 89  ? 0.7316 0.7093 0.3543 0.1945  0.0390  0.0230  98  LEU   B CD1 
1099 C CD2 . LEU   B 89  ? 0.7251 0.6826 0.3428 0.1881  0.0317  0.0145  98  LEU   B CD2 
1100 N N   . ALA   B 90  ? 0.6937 0.6987 0.3097 0.1992  0.0460  0.0295  99  ALA   B N   
1101 C CA  . ALA   B 90  ? 0.6898 0.7057 0.3153 0.1933  0.0520  0.0339  99  ALA   B CA  
1102 C C   . ALA   B 90  ? 0.6959 0.7108 0.3332 0.1868  0.0550  0.0360  99  ALA   B C   
1103 O O   . ALA   B 90  ? 0.6948 0.7087 0.3316 0.1911  0.0535  0.0372  99  ALA   B O   
1104 C CB  . ALA   B 90  ? 0.6934 0.7240 0.3155 0.1998  0.0538  0.0390  99  ALA   B CB  
1105 N N   . VAL   B 91  ? 0.6900 0.7051 0.3372 0.1773  0.0587  0.0362  100 VAL   B N   
1106 C CA  . VAL   B 91  ? 0.6844 0.6988 0.3432 0.1712  0.0616  0.0383  100 VAL   B CA  
1107 C C   . VAL   B 91  ? 0.6945 0.7186 0.3601 0.1661  0.0662  0.0432  100 VAL   B C   
1108 O O   . VAL   B 91  ? 0.6841 0.7062 0.3561 0.1583  0.0685  0.0418  100 VAL   B O   
1109 C CB  . VAL   B 91  ? 0.6836 0.6866 0.3475 0.1647  0.0607  0.0329  100 VAL   B CB  
1110 C CG1 . VAL   B 91  ? 0.6780 0.6802 0.3536 0.1587  0.0635  0.0345  100 VAL   B CG1 
1111 C CG2 . VAL   B 91  ? 0.6907 0.6846 0.3474 0.1694  0.0557  0.0288  100 VAL   B CG2 
1112 N N   . PRO   B 92  ? 0.7161 0.7517 0.3806 0.1703  0.0676  0.0494  101 PRO   B N   
1113 C CA  . PRO   B 92  ? 0.7103 0.7563 0.3797 0.1657  0.0715  0.0546  101 PRO   B CA  
1114 C C   . PRO   B 92  ? 0.7062 0.7503 0.3868 0.1579  0.0739  0.0573  101 PRO   B C   
1115 O O   . PRO   B 92  ? 0.7162 0.7531 0.4006 0.1575  0.0727  0.0562  101 PRO   B O   
1116 C CB  . PRO   B 92  ? 0.7174 0.7770 0.3804 0.1735  0.0714  0.0601  101 PRO   B CB  
1117 C CG  . PRO   B 92  ? 0.7315 0.7863 0.3857 0.1829  0.0673  0.0571  101 PRO   B CG  
1118 C CD  . PRO   B 92  ? 0.7312 0.7710 0.3890 0.1795  0.0654  0.0518  101 PRO   B CD  
1119 N N   . PRO   B 93  ? 0.7190 0.7692 0.4050 0.1513  0.0770  0.0609  102 PRO   B N   
1120 C CA  . PRO   B 93  ? 0.7344 0.7808 0.4305 0.1436  0.0787  0.0628  102 PRO   B CA  
1121 C C   . PRO   B 93  ? 0.7553 0.8050 0.4533 0.1461  0.0781  0.0685  102 PRO   B C   
1122 O O   . PRO   B 93  ? 0.7747 0.8362 0.4694 0.1496  0.0786  0.0745  102 PRO   B O   
1123 C CB  . PRO   B 93  ? 0.7215 0.7746 0.4208 0.1370  0.0815  0.0657  102 PRO   B CB  
1124 C CG  . PRO   B 93  ? 0.7233 0.7799 0.4148 0.1404  0.0812  0.0626  102 PRO   B CG  
1125 C CD  . PRO   B 93  ? 0.7233 0.7829 0.4060 0.1507  0.0786  0.0627  102 PRO   B CD  
1126 N N   . GLY   B 94  ? 0.7692 0.8090 0.4722 0.1448  0.0769  0.0662  103 GLY   B N   
1127 C CA  . GLY   B 94  ? 0.7794 0.8198 0.4856 0.1460  0.0761  0.0709  103 GLY   B CA  
1128 C C   . GLY   B 94  ? 0.7932 0.8370 0.4922 0.1552  0.0739  0.0721  103 GLY   B C   
1129 O O   . GLY   B 94  ? 0.7859 0.8312 0.4871 0.1564  0.0732  0.0765  103 GLY   B O   
1130 N N   . GLU   B 95  ? 0.7975 0.8417 0.4881 0.1615  0.0724  0.0681  104 GLU   B N   
1131 C CA  . GLU   B 95  ? 0.8000 0.8468 0.4825 0.1711  0.0698  0.0685  104 GLU   B CA  
1132 C C   . GLU   B 95  ? 0.8046 0.8392 0.4840 0.1736  0.0669  0.0610  104 GLU   B C   
1133 O O   . GLU   B 95  ? 0.8251 0.8524 0.5071 0.1685  0.0673  0.0559  104 GLU   B O   
1134 C CB  . GLU   B 95  ? 0.7993 0.8588 0.4732 0.1769  0.0702  0.0713  104 GLU   B CB  
1135 C CG  . GLU   B 95  ? 0.8094 0.8819 0.4871 0.1726  0.0734  0.0786  104 GLU   B CG  
1136 C CD  . GLU   B 95  ? 0.8289 0.9159 0.4991 0.1775  0.0743  0.0812  104 GLU   B CD  
1137 O OE1 . GLU   B 95  ? 0.8528 0.9378 0.5148 0.1837  0.0724  0.0763  104 GLU   B OE1 
1138 O OE2 . GLU   B 95  ? 0.8506 0.9504 0.5232 0.1746  0.0766  0.0880  104 GLU   B OE2 
1139 N N   . ARG   B 96  ? 0.8134 0.8459 0.4875 0.1807  0.0640  0.0604  105 ARG   B N   
1140 C CA  . ARG   B 96  ? 0.8473 0.8684 0.5182 0.1833  0.0606  0.0541  105 ARG   B CA  
1141 C C   . ARG   B 96  ? 0.8197 0.8390 0.4812 0.1868  0.0586  0.0496  105 ARG   B C   
1142 O O   . ARG   B 96  ? 0.8188 0.8474 0.4740 0.1912  0.0591  0.0521  105 ARG   B O   
1143 C CB  . ARG   B 96  ? 0.9163 0.9371 0.5833 0.1905  0.0579  0.0557  105 ARG   B CB  
1144 C CG  . ARG   B 96  ? 0.9738 0.9826 0.6391 0.1920  0.0543  0.0500  105 ARG   B CG  
1145 C CD  . ARG   B 96  ? 1.0289 1.0358 0.6956 0.1955  0.0525  0.0520  105 ARG   B CD  
1146 N NE  . ARG   B 96  ? 1.0712 1.0878 0.7317 0.2028  0.0522  0.0571  105 ARG   B NE  
1147 C CZ  . ARG   B 96  ? 1.1278 1.1534 0.7924 0.2021  0.0545  0.0638  105 ARG   B CZ  
1148 N NH1 . ARG   B 96  ? 1.1261 1.1510 0.8011 0.1945  0.0571  0.0663  105 ARG   B NH1 
1149 N NH2 . ARG   B 96  ? 1.1815 1.2170 0.8395 0.2092  0.0540  0.0681  105 ARG   B NH2 
1150 N N   . ALA   B 97  ? 0.8079 0.8160 0.4686 0.1850  0.0561  0.0434  106 ALA   B N   
1151 C CA  . ALA   B 97  ? 0.8121 0.8155 0.4628 0.1887  0.0527  0.0387  106 ALA   B CA  
1152 C C   . ALA   B 97  ? 0.8306 0.8387 0.4705 0.1993  0.0499  0.0405  106 ALA   B C   
1153 O O   . ALA   B 97  ? 0.8340 0.8410 0.4735 0.2032  0.0483  0.0418  106 ALA   B O   
1154 C CB  . ALA   B 97  ? 0.8026 0.7937 0.4540 0.1858  0.0497  0.0331  106 ALA   B CB  
1155 N N   . LYS   B 98  ? 0.8464 0.8590 0.4775 0.2040  0.0489  0.0401  107 LYS   B N   
1156 C CA  . LYS   B 98  ? 0.8769 0.8944 0.4964 0.2151  0.0459  0.0410  107 LYS   B CA  
1157 C C   . LYS   B 98  ? 0.8493 0.8610 0.4574 0.2194  0.0418  0.0361  107 LYS   B C   
1158 O O   . LYS   B 98  ? 0.8412 0.8569 0.4498 0.2164  0.0438  0.0359  107 LYS   B O   
1159 C CB  . LYS   B 98  ? 0.9452 0.9791 0.5667 0.2170  0.0500  0.0476  107 LYS   B CB  
1160 C CG  . LYS   B 98  ? 1.0183 1.0618 0.6299 0.2283  0.0483  0.0501  107 LYS   B CG  
1161 C CD  . LYS   B 98  ? 1.0579 1.1192 0.6700 0.2297  0.0521  0.0558  107 LYS   B CD  
1162 C CE  . LYS   B 98  ? 1.0705 1.1336 0.6873 0.2223  0.0551  0.0554  107 LYS   B CE  
1163 N NZ  . LYS   B 98  ? 1.0962 1.1755 0.7090 0.2263  0.0571  0.0592  107 LYS   B NZ  
1164 N N   . ASN   B 99  ? 0.8053 0.8076 0.4037 0.2258  0.0360  0.0323  108 ASN   B N   
1165 C CA  . ASN   B 99  ? 0.8090 0.8047 0.3946 0.2313  0.0309  0.0277  108 ASN   B CA  
1166 C C   . ASN   B 99  ? 0.8073 0.8151 0.3842 0.2412  0.0309  0.0300  108 ASN   B C   
1167 O O   . ASN   B 99  ? 0.8229 0.8391 0.3979 0.2478  0.0314  0.0333  108 ASN   B O   
1168 C CB  . ASN   B 99  ? 0.8109 0.7929 0.3876 0.2358  0.0240  0.0234  108 ASN   B CB  
1169 C CG  . ASN   B 99  ? 0.8098 0.7797 0.3932 0.2267  0.0229  0.0206  108 ASN   B CG  
1170 O OD1 . ASN   B 99  ? 0.8292 0.8013 0.4238 0.2211  0.0265  0.0228  108 ASN   B OD1 
1171 N ND2 . ASN   B 99  ? 0.8052 0.7624 0.3811 0.2259  0.0173  0.0157  108 ASN   B ND2 
1172 N N   . ILE   B 100 ? 0.7854 0.7943 0.3567 0.2425  0.0301  0.0280  109 ILE   B N   
1173 C CA  . ILE   B 100 ? 0.7869 0.8081 0.3496 0.2521  0.0301  0.0297  109 ILE   B CA  
1174 C C   . ILE   B 100 ? 0.8022 0.8129 0.3519 0.2576  0.0237  0.0240  109 ILE   B C   
1175 O O   . ILE   B 100 ? 0.8479 0.8513 0.3990 0.2508  0.0233  0.0212  109 ILE   B O   
1176 C CB  . ILE   B 100 ? 0.7903 0.8259 0.3610 0.2470  0.0364  0.0339  109 ILE   B CB  
1177 C CG1 . ILE   B 100 ? 0.8011 0.8441 0.3857 0.2391  0.0422  0.0394  109 ILE   B CG1 
1178 C CG2 . ILE   B 100 ? 0.7944 0.8442 0.3567 0.2569  0.0364  0.0357  109 ILE   B CG2 
1179 C CD1 . ILE   B 100 ? 0.8087 0.8615 0.3930 0.2453  0.0431  0.0440  109 ILE   B CD1 
1180 N N   . GLN   B 101 ? 0.8088 0.8186 0.3459 0.2694  0.0187  0.0222  110 GLN   B N   
1181 C CA  . GLN   B 101 ? 0.8394 0.8361 0.3624 0.2753  0.0112  0.0164  110 GLN   B CA  
1182 C C   . GLN   B 101 ? 0.8565 0.8637 0.3721 0.2829  0.0112  0.0163  110 GLN   B C   
1183 O O   . GLN   B 101 ? 0.8454 0.8709 0.3625 0.2884  0.0155  0.0207  110 GLN   B O   
1184 C CB  . GLN   B 101 ? 0.8707 0.8577 0.3834 0.2837  0.0047  0.0137  110 GLN   B CB  
1185 C CG  . GLN   B 101 ? 0.8937 0.8680 0.3903 0.2915  -0.0037 0.0080  110 GLN   B CG  
1186 C CD  . GLN   B 101 ? 0.9196 0.8797 0.4079 0.2959  -0.0105 0.0051  110 GLN   B CD  
1187 O OE1 . GLN   B 101 ? 0.9366 0.8931 0.4329 0.2897  -0.0091 0.0066  110 GLN   B OE1 
1188 N NE2 . GLN   B 101 ? 0.9380 0.8906 0.4101 0.3071  -0.0181 0.0011  110 GLN   B NE2 
1189 N N   . THR   B 102 ? 0.8566 0.8531 0.3650 0.2824  0.0068  0.0118  111 THR   B N   
1190 C CA  . THR   B 102 ? 0.8469 0.8517 0.3488 0.2881  0.0067  0.0112  111 THR   B CA  
1191 C C   . THR   B 102 ? 0.8611 0.8480 0.3509 0.2901  -0.0013 0.0050  111 THR   B C   
1192 O O   . THR   B 102 ? 0.9082 0.8772 0.3984 0.2824  -0.0052 0.0020  111 THR   B O   
1193 C CB  . THR   B 102 ? 0.8316 0.8506 0.3473 0.2788  0.0151  0.0159  111 THR   B CB  
1194 O OG1 . THR   B 102 ? 0.8266 0.8595 0.3370 0.2862  0.0161  0.0168  111 THR   B OG1 
1195 C CG2 . THR   B 102 ? 0.8238 0.8316 0.3475 0.2653  0.0161  0.0142  111 THR   B CG2 
1196 N N   . LEU   B 103 ? 0.8637 0.8551 0.3423 0.3003  -0.0043 0.0031  112 LEU   B N   
1197 C CA  . LEU   B 103 ? 0.8682 0.8443 0.3353 0.3021  -0.0117 -0.0022 112 LEU   B CA  
1198 C C   . LEU   B 103 ? 0.8686 0.8521 0.3430 0.2945  -0.0070 -0.0007 112 LEU   B C   
1199 O O   . LEU   B 103 ? 0.8505 0.8522 0.3270 0.2988  -0.0023 0.0021  112 LEU   B O   
1200 C CB  . LEU   B 103 ? 0.8817 0.8570 0.3312 0.3186  -0.0187 -0.0057 112 LEU   B CB  
1201 C CG  . LEU   B 103 ? 0.8849 0.8426 0.3218 0.3204  -0.0273 -0.0113 112 LEU   B CG  
1202 C CD1 . LEU   B 103 ? 0.8923 0.8263 0.3228 0.3170  -0.0352 -0.0150 112 LEU   B CD1 
1203 C CD2 . LEU   B 103 ? 0.9119 0.8738 0.3334 0.3366  -0.0323 -0.0142 112 LEU   B CD2 
1204 N N   . PRO   B 104 ? 0.8714 0.8418 0.3501 0.2827  -0.0079 -0.0025 113 PRO   B N   
1205 C CA  . PRO   B 104 ? 0.8713 0.8472 0.3562 0.2753  -0.0039 -0.0015 113 PRO   B CA  
1206 C C   . PRO   B 104 ? 0.8823 0.8623 0.3552 0.2858  -0.0076 -0.0036 113 PRO   B C   
1207 O O   . PRO   B 104 ? 0.9381 0.9075 0.3949 0.2972  -0.0163 -0.0080 113 PRO   B O   
1208 C CB  . PRO   B 104 ? 0.8635 0.8216 0.3512 0.2630  -0.0067 -0.0041 113 PRO   B CB  
1209 C CG  . PRO   B 104 ? 0.8628 0.8127 0.3532 0.2605  -0.0080 -0.0042 113 PRO   B CG  
1210 C CD  . PRO   B 104 ? 0.8833 0.8347 0.3621 0.2753  -0.0124 -0.0051 113 PRO   B CD  
1211 N N   . GLY   B 105 ? 0.8686 0.8649 0.3496 0.2825  -0.0008 -0.0002 114 GLY   B N   
1212 C CA  . GLY   B 105 ? 0.8836 0.8830 0.3576 0.2869  -0.0028 -0.0019 114 GLY   B CA  
1213 C C   . GLY   B 105 ? 0.8836 0.8682 0.3592 0.2756  -0.0050 -0.0045 114 GLY   B C   
1214 O O   . GLY   B 105 ? 0.8567 0.8262 0.3348 0.2673  -0.0072 -0.0060 114 GLY   B O   
1215 N N   . ILE   B 106 ? 0.8978 0.8877 0.3722 0.2753  -0.0043 -0.0047 115 ILE   B N   
1216 C CA  . ILE   B 106 ? 0.9065 0.8828 0.3793 0.2669  -0.0076 -0.0075 115 ILE   B CA  
1217 C C   . ILE   B 106 ? 0.9015 0.8923 0.3855 0.2589  0.0000  -0.0041 115 ILE   B C   
1218 O O   . ILE   B 106 ? 0.9186 0.9260 0.4017 0.2661  0.0029  -0.0020 115 ILE   B O   
1219 C CB  . ILE   B 106 ? 0.9303 0.8948 0.3851 0.2777  -0.0175 -0.0125 115 ILE   B CB  
1220 C CG1 . ILE   B 106 ? 0.9661 0.9141 0.4083 0.2855  -0.0262 -0.0162 115 ILE   B CG1 
1221 C CG2 . ILE   B 106 ? 0.9557 0.9085 0.4092 0.2689  -0.0205 -0.0147 115 ILE   B CG2 
1222 C CD1 . ILE   B 106 ? 0.9641 0.8916 0.4068 0.2748  -0.0306 -0.0183 115 ILE   B CD1 
1223 N N   . PHE   B 107 ? 0.9050 0.8890 0.3982 0.2446  0.0024  -0.0039 116 PHE   B N   
1224 C CA  . PHE   B 107 ? 0.8828 0.8735 0.3827 0.2364  0.0067  -0.0025 116 PHE   B CA  
1225 C C   . PHE   B 107 ? 0.9111 0.8869 0.3994 0.2373  -0.0010 -0.0070 116 PHE   B C   
1226 O O   . PHE   B 107 ? 0.9316 0.8893 0.4174 0.2305  -0.0059 -0.0099 116 PHE   B O   
1227 C CB  . PHE   B 107 ? 0.8643 0.8549 0.3796 0.2210  0.0131  -0.0003 116 PHE   B CB  
1228 C CG  . PHE   B 107 ? 0.8420 0.8504 0.3705 0.2180  0.0220  0.0049  116 PHE   B CG  
1229 C CD1 . PHE   B 107 ? 0.8377 0.8611 0.3645 0.2284  0.0241  0.0079  116 PHE   B CD1 
1230 C CD2 . PHE   B 107 ? 0.8264 0.8361 0.3688 0.2047  0.0280  0.0069  116 PHE   B CD2 
1231 C CE1 . PHE   B 107 ? 0.8266 0.8659 0.3654 0.2246  0.0318  0.0133  116 PHE   B CE1 
1232 C CE2 . PHE   B 107 ? 0.8197 0.8441 0.3737 0.2015  0.0354  0.0118  116 PHE   B CE2 
1233 C CZ  . PHE   B 107 ? 0.8199 0.8590 0.3721 0.2111  0.0373  0.0153  116 PHE   B CZ  
1234 N N   . LYS   B 108 ? 0.9420 0.9249 0.4228 0.2458  -0.0027 -0.0075 117 LYS   B N   
1235 C CA  . LYS   B 108 ? 0.9751 0.9456 0.4450 0.2467  -0.0099 -0.0113 117 LYS   B CA  
1236 C C   . LYS   B 108 ? 0.9488 0.9247 0.4294 0.2340  -0.0043 -0.0094 117 LYS   B C   
1237 O O   . LYS   B 108 ? 0.9084 0.9032 0.3961 0.2345  0.0024  -0.0059 117 LYS   B O   
1238 C CB  . LYS   B 108 ? 1.0332 1.0092 0.4896 0.2629  -0.0146 -0.0131 117 LYS   B CB  
1239 C CG  . LYS   B 108 ? 1.1125 1.0693 0.5511 0.2732  -0.0261 -0.0184 117 LYS   B CG  
1240 C CD  . LYS   B 108 ? 1.1806 1.1459 0.6071 0.2917  -0.0297 -0.0199 117 LYS   B CD  
1241 C CE  . LYS   B 108 ? 1.2586 1.2045 0.6681 0.3022  -0.0409 -0.0250 117 LYS   B CE  
1242 N NZ  . LYS   B 108 ? 1.3001 1.2564 0.7001 0.3200  -0.0428 -0.0260 117 LYS   B NZ  
1243 N N   . THR   B 109 ? 0.9432 0.9037 0.4252 0.2226  -0.0069 -0.0114 118 THR   B N   
1244 C CA  . THR   B 109 ? 0.9494 0.9122 0.4404 0.2097  -0.0026 -0.0102 118 THR   B CA  
1245 C C   . THR   B 109 ? 0.9637 0.9105 0.4436 0.2084  -0.0108 -0.0140 118 THR   B C   
1246 O O   . THR   B 109 ? 0.9457 0.8758 0.4131 0.2134  -0.0198 -0.0174 118 THR   B O   
1247 C CB  . THR   B 109 ? 0.9409 0.9018 0.4457 0.1953  0.0028  -0.0088 118 THR   B CB  
1248 O OG1 . THR   B 109 ? 0.9353 0.8768 0.4354 0.1887  -0.0035 -0.0120 118 THR   B OG1 
1249 C CG2 . THR   B 109 ? 0.9316 0.9015 0.4445 0.1971  0.0081  -0.0060 118 THR   B CG2 
1250 N N   . LYS   B 110 ? 1.0177 0.9687 0.5022 0.2008  -0.0080 -0.0132 119 LYS   B N   
1251 C CA  . LYS   B 110 ? 1.0574 0.9942 0.5327 0.1977  -0.0152 -0.0161 119 LYS   B CA  
1252 C C   . LYS   B 110 ? 1.0786 0.9957 0.5514 0.1888  -0.0208 -0.0185 119 LYS   B C   
1253 O O   . LYS   B 110 ? 1.1308 1.0318 0.5909 0.1901  -0.0301 -0.0215 119 LYS   B O   
1254 C CB  . LYS   B 110 ? 1.0562 1.0036 0.5400 0.1894  -0.0093 -0.0142 119 LYS   B CB  
1255 C CG  . LYS   B 110 ? 1.0943 1.0423 0.5921 0.1729  -0.0031 -0.0126 119 LYS   B CG  
1256 C CD  . LYS   B 110 ? 1.1202 1.0816 0.6272 0.1660  0.0037  -0.0102 119 LYS   B CD  
1257 C CE  . LYS   B 110 ? 1.1396 1.0952 0.6542 0.1504  0.0057  -0.0106 119 LYS   B CE  
1258 N NZ  . LYS   B 110 ? 1.1540 1.1090 0.6795 0.1420  0.0103  -0.0099 119 LYS   B NZ  
1259 N N   . ASP   B 111 ? 1.0533 0.9713 0.5369 0.1805  -0.0160 -0.0172 120 ASP   B N   
1260 C CA  . ASP   B 111 ? 1.0574 0.9593 0.5403 0.1713  -0.0204 -0.0189 120 ASP   B CA  
1261 C C   . ASP   B 111 ? 1.0630 0.9542 0.5371 0.1792  -0.0268 -0.0206 120 ASP   B C   
1262 O O   . ASP   B 111 ? 1.1006 0.9780 0.5726 0.1722  -0.0316 -0.0220 120 ASP   B O   
1263 C CB  . ASP   B 111 ? 1.0513 0.9605 0.5509 0.1583  -0.0119 -0.0169 120 ASP   B CB  
1264 C CG  . ASP   B 111 ? 1.0611 0.9749 0.5687 0.1467  -0.0075 -0.0161 120 ASP   B CG  
1265 O OD1 . ASP   B 111 ? 1.0239 0.9387 0.5255 0.1495  -0.0096 -0.0165 120 ASP   B OD1 
1266 O OD2 . ASP   B 111 ? 1.0937 1.0101 0.6130 0.1354  -0.0022 -0.0154 120 ASP   B OD2 
1267 N N   . GLY   B 112 ? 1.0510 0.9490 0.5207 0.1925  -0.0267 -0.0202 121 GLY   B N   
1268 C CA  . GLY   B 112 ? 1.0487 0.9378 0.5112 0.1998  -0.0319 -0.0216 121 GLY   B CA  
1269 C C   . GLY   B 112 ? 1.0329 0.9369 0.4998 0.2093  -0.0263 -0.0195 121 GLY   B C   
1270 O O   . GLY   B 112 ? 1.0005 0.9225 0.4785 0.2078  -0.0173 -0.0163 121 GLY   B O   
1271 N N   . ASP   B 113 ? 1.0416 0.9380 0.4992 0.2187  -0.0319 -0.0211 122 ASP   B N   
1272 C CA  . ASP   B 113 ? 1.0258 0.9342 0.4862 0.2279  -0.0278 -0.0192 122 ASP   B CA  
1273 C C   . ASP   B 113 ? 0.9989 0.9084 0.4720 0.2186  -0.0226 -0.0173 122 ASP   B C   
1274 O O   . ASP   B 113 ? 0.9628 0.8576 0.4352 0.2101  -0.0267 -0.0189 122 ASP   B O   
1275 C CB  . ASP   B 113 ? 1.0398 0.9384 0.4838 0.2424  -0.0368 -0.0223 122 ASP   B CB  
1276 C CG  . ASP   B 113 ? 1.0815 0.9816 0.5126 0.2548  -0.0417 -0.0244 122 ASP   B CG  
1277 O OD1 . ASP   B 113 ? 1.0832 0.9910 0.5177 0.2518  -0.0385 -0.0235 122 ASP   B OD1 
1278 O OD2 . ASP   B 113 ? 1.1331 1.0262 0.5505 0.2679  -0.0490 -0.0271 122 ASP   B OD2 
1279 N N   . ILE   B 114 ? 0.9701 0.8965 0.4540 0.2199  -0.0141 -0.0137 123 ILE   B N   
1280 C CA  . ILE   B 114 ? 0.9394 0.8690 0.4357 0.2128  -0.0086 -0.0115 123 ILE   B CA  
1281 C C   . ILE   B 114 ? 0.8981 0.8366 0.3925 0.2243  -0.0073 -0.0099 123 ILE   B C   
1282 O O   . ILE   B 114 ? 0.8575 0.8103 0.3510 0.2324  -0.0043 -0.0080 123 ILE   B O   
1283 C CB  . ILE   B 114 ? 0.9345 0.8767 0.4475 0.2013  0.0011  -0.0082 123 ILE   B CB  
1284 C CG1 . ILE   B 114 ? 0.9869 0.9300 0.5003 0.1956  0.0017  -0.0088 123 ILE   B CG1 
1285 C CG2 . ILE   B 114 ? 0.9233 0.8605 0.4467 0.1904  0.0036  -0.0080 123 ILE   B CG2 
1286 C CD1 . ILE   B 114 ? 0.9969 0.9543 0.5256 0.1862  0.0113  -0.0054 123 ILE   B CD1 
1287 N N   . GLY   B 115 ? 0.8876 0.8196 0.3827 0.2242  -0.0089 -0.0102 124 GLY   B N   
1288 C CA  . GLY   B 115 ? 0.8688 0.8117 0.3663 0.2322  -0.0055 -0.0076 124 GLY   B CA  
1289 C C   . GLY   B 115 ? 0.8544 0.8169 0.3664 0.2279  0.0047  -0.0028 124 GLY   B C   
1290 O O   . GLY   B 115 ? 0.8232 0.7877 0.3463 0.2160  0.0096  -0.0016 124 GLY   B O   
1291 N N   . ALA   B 116 ? 0.8600 0.8367 0.3713 0.2375  0.0075  0.0000  125 ALA   B N   
1292 C CA  . ALA   B 116 ? 0.8506 0.8467 0.3745 0.2347  0.0166  0.0053  125 ALA   B CA  
1293 C C   . ALA   B 116 ? 0.8426 0.8457 0.3664 0.2424  0.0176  0.0076  125 ALA   B C   
1294 O O   . ALA   B 116 ? 0.8565 0.8557 0.3682 0.2538  0.0119  0.0054  125 ALA   B O   
1295 C CB  . ALA   B 116 ? 0.8541 0.8639 0.3761 0.2389  0.0188  0.0068  125 ALA   B CB  
1296 N N   A VAL   B 117 ? 0.8321 0.8447 0.3690 0.2362  0.0244  0.0120  126 VAL   B N   
1297 N N   B VAL   B 117 ? 0.8359 0.8490 0.3728 0.2363  0.0246  0.0121  126 VAL   B N   
1298 N N   C VAL   B 117 ? 0.8321 0.8447 0.3690 0.2362  0.0244  0.0120  126 VAL   B N   
1299 N N   D VAL   B 117 ? 0.8359 0.8490 0.3728 0.2363  0.0246  0.0121  126 VAL   B N   
1300 C CA  A VAL   B 117 ? 0.8408 0.8619 0.3793 0.2423  0.0263  0.0152  126 VAL   B CA  
1301 C CA  B VAL   B 117 ? 0.8468 0.8679 0.3857 0.2419  0.0264  0.0152  126 VAL   B CA  
1302 C CA  C VAL   B 117 ? 0.8408 0.8619 0.3793 0.2423  0.0263  0.0152  126 VAL   B CA  
1303 C CA  D VAL   B 117 ? 0.8468 0.8679 0.3857 0.2419  0.0264  0.0152  126 VAL   B CA  
1304 C C   A VAL   B 117 ? 0.8358 0.8786 0.3818 0.2426  0.0334  0.0212  126 VAL   B C   
1305 C C   B VAL   B 117 ? 0.8393 0.8822 0.3856 0.2425  0.0335  0.0213  126 VAL   B C   
1306 C C   C VAL   B 117 ? 0.8358 0.8786 0.3818 0.2426  0.0334  0.0212  126 VAL   B C   
1307 C C   D VAL   B 117 ? 0.8393 0.8822 0.3856 0.2425  0.0335  0.0213  126 VAL   B C   
1308 O O   A VAL   B 117 ? 0.8235 0.8714 0.3812 0.2320  0.0390  0.0240  126 VAL   B O   
1309 O O   B VAL   B 117 ? 0.8273 0.8755 0.3854 0.2320  0.0392  0.0242  126 VAL   B O   
1310 O O   C VAL   B 117 ? 0.8235 0.8714 0.3812 0.2320  0.0390  0.0240  126 VAL   B O   
1311 O O   D VAL   B 117 ? 0.8273 0.8755 0.3854 0.2320  0.0392  0.0242  126 VAL   B O   
1312 C CB  A VAL   B 117 ? 0.8362 0.8483 0.3828 0.2348  0.0272  0.0153  126 VAL   B CB  
1313 C CB  B VAL   B 117 ? 0.8468 0.8584 0.3941 0.2337  0.0274  0.0152  126 VAL   B CB  
1314 C CB  C VAL   B 117 ? 0.8362 0.8483 0.3828 0.2348  0.0272  0.0153  126 VAL   B CB  
1315 C CB  D VAL   B 117 ? 0.8468 0.8584 0.3941 0.2337  0.0274  0.0152  126 VAL   B CB  
1316 C CG1 A VAL   B 117 ? 0.8425 0.8342 0.3834 0.2315  0.0207  0.0099  126 VAL   B CG1 
1317 C CG1 B VAL   B 117 ? 0.8430 0.8667 0.3982 0.2347  0.0323  0.0203  126 VAL   B CG1 
1318 C CG1 C VAL   B 117 ? 0.8425 0.8342 0.3834 0.2315  0.0207  0.0099  126 VAL   B CG1 
1319 C CG1 D VAL   B 117 ? 0.8430 0.8667 0.3982 0.2347  0.0323  0.0203  126 VAL   B CG1 
1320 C CG2 A VAL   B 117 ? 0.8197 0.8388 0.3822 0.2228  0.0347  0.0191  126 VAL   B CG2 
1321 C CG2 B VAL   B 117 ? 0.8590 0.8524 0.3963 0.2372  0.0195  0.0103  126 VAL   B CG2 
1322 C CG2 C VAL   B 117 ? 0.8197 0.8388 0.3822 0.2228  0.0347  0.0191  126 VAL   B CG2 
1323 C CG2 D VAL   B 117 ? 0.8590 0.8524 0.3963 0.2372  0.0195  0.0103  126 VAL   B CG2 
1324 N N   . ALA   B 118 ? 0.8440 0.8992 0.3830 0.2545  0.0328  0.0230  127 ALA   B N   
1325 C CA  . ALA   B 118 ? 0.8498 0.9278 0.3945 0.2560  0.0389  0.0292  127 ALA   B CA  
1326 C C   . ALA   B 118 ? 0.8677 0.9522 0.4206 0.2540  0.0426  0.0339  127 ALA   B C   
1327 O O   . ALA   B 118 ? 0.8648 0.9562 0.4115 0.2642  0.0411  0.0351  127 ALA   B O   
1328 C CB  . ALA   B 118 ? 0.8413 0.9309 0.3743 0.2699  0.0364  0.0288  127 ALA   B CB  
1329 N N   . LEU   B 119 ? 0.8550 0.9353 0.4204 0.2417  0.0466  0.0359  128 LEU   B N   
1330 C CA  . LEU   B 119 ? 0.8423 0.9282 0.4167 0.2383  0.0503  0.0407  128 LEU   B CA  
1331 C C   . LEU   B 119 ? 0.8570 0.9503 0.4447 0.2263  0.0566  0.0452  128 LEU   B C   
1332 O O   . LEU   B 119 ? 0.8800 0.9646 0.4717 0.2179  0.0571  0.0426  128 LEU   B O   
1333 C CB  . LEU   B 119 ? 0.8316 0.9000 0.4062 0.2363  0.0470  0.0371  128 LEU   B CB  
1334 C CG  . LEU   B 119 ? 0.8280 0.8879 0.3891 0.2478  0.0403  0.0328  128 LEU   B CG  
1335 C CD1 . LEU   B 119 ? 0.8176 0.8589 0.3793 0.2438  0.0367  0.0288  128 LEU   B CD1 
1336 C CD2 . LEU   B 119 ? 0.8458 0.9200 0.4031 0.2579  0.0409  0.0367  128 LEU   B CD2 
1337 N N   . ASP   B 120 ? 0.8660 0.9754 0.4594 0.2258  0.0608  0.0519  129 ASP   B N   
1338 C CA  . ASP   B 120 ? 0.8834 1.0020 0.4886 0.2152  0.0664  0.0572  129 ASP   B CA  
1339 C C   . ASP   B 120 ? 0.8728 0.9852 0.4881 0.2074  0.0684  0.0595  129 ASP   B C   
1340 O O   . ASP   B 120 ? 0.8877 1.0035 0.5020 0.2122  0.0679  0.0620  129 ASP   B O   
1341 C CB  . ASP   B 120 ? 0.9162 1.0574 0.5205 0.2198  0.0693  0.0638  129 ASP   B CB  
1342 C CG  . ASP   B 120 ? 0.9740 1.1245 0.5828 0.2132  0.0727  0.0664  129 ASP   B CG  
1343 O OD1 . ASP   B 120 ? 0.9979 1.1424 0.6167 0.2013  0.0753  0.0671  129 ASP   B OD1 
1344 O OD2 . ASP   B 120 ? 1.0425 1.2062 0.6447 0.2204  0.0723  0.0672  129 ASP   B OD2 
1345 N N   . TYR   B 121 ? 0.8422 0.9466 0.4668 0.1961  0.0706  0.0588  130 TYR   B N   
1346 C CA  . TYR   B 121 ? 0.8477 0.9457 0.4825 0.1883  0.0724  0.0605  130 TYR   B CA  
1347 C C   . TYR   B 121 ? 0.8354 0.9344 0.4803 0.1766  0.0763  0.0626  130 TYR   B C   
1348 O O   . TYR   B 121 ? 0.8489 0.9498 0.4927 0.1741  0.0771  0.0612  130 TYR   B O   
1349 C CB  . TYR   B 121 ? 0.8716 0.9514 0.5049 0.1884  0.0689  0.0542  130 TYR   B CB  
1350 C CG  . TYR   B 121 ? 0.9018 0.9796 0.5273 0.1984  0.0653  0.0532  130 TYR   B CG  
1351 C CD1 . TYR   B 121 ? 0.9232 1.0037 0.5529 0.1991  0.0661  0.0571  130 TYR   B CD1 
1352 C CD2 . TYR   B 121 ? 0.9280 1.0006 0.5417 0.2071  0.0606  0.0484  130 TYR   B CD2 
1353 C CE1 . TYR   B 121 ? 0.9498 1.0285 0.5723 0.2082  0.0628  0.0562  130 TYR   B CE1 
1354 C CE2 . TYR   B 121 ? 0.9575 1.0276 0.5637 0.2164  0.0569  0.0473  130 TYR   B CE2 
1355 C CZ  . TYR   B 121 ? 0.9691 1.0427 0.5798 0.2169  0.0582  0.0513  130 TYR   B CZ  
1356 O OH  . TYR   B 121 ? 1.0258 1.0971 0.6290 0.2259  0.0546  0.0503  130 TYR   B OH  
1357 N N   . PRO   B 122 ? 0.8168 0.9142 0.4715 0.1692  0.0786  0.0659  131 PRO   B N   
1358 C CA  . PRO   B 122 ? 0.8287 0.9259 0.4925 0.1583  0.0818  0.0676  131 PRO   B CA  
1359 C C   . PRO   B 122 ? 0.8008 0.8840 0.4653 0.1535  0.0809  0.0603  131 PRO   B C   
1360 O O   . PRO   B 122 ? 0.7865 0.8584 0.4470 0.1568  0.0778  0.0547  131 PRO   B O   
1361 C CB  . PRO   B 122 ? 0.8294 0.9249 0.5017 0.1534  0.0830  0.0716  131 PRO   B CB  
1362 C CG  . PRO   B 122 ? 0.8418 0.9427 0.5089 0.1623  0.0813  0.0743  131 PRO   B CG  
1363 C CD  . PRO   B 122 ? 0.8405 0.9348 0.4979 0.1708  0.0779  0.0678  131 PRO   B CD  
1364 N N   . ALA   B 123 ? 0.7911 0.8761 0.4601 0.1459  0.0833  0.0606  132 ALA   B N   
1365 C CA  . ALA   B 123 ? 0.7802 0.8539 0.4506 0.1402  0.0829  0.0543  132 ALA   B CA  
1366 C C   . ALA   B 123 ? 0.7547 0.8140 0.4299 0.1365  0.0818  0.0498  132 ALA   B C   
1367 O O   . ALA   B 123 ? 0.7588 0.8081 0.4312 0.1360  0.0797  0.0436  132 ALA   B O   
1368 C CB  . ALA   B 123 ? 0.7793 0.8581 0.4553 0.1318  0.0861  0.0565  132 ALA   B CB  
1369 N N   . GLY   B 124 ? 0.7270 0.7856 0.4085 0.1348  0.0827  0.0528  133 GLY   B N   
1370 C CA  . GLY   B 124 ? 0.6996 0.7460 0.3861 0.1321  0.0817  0.0489  133 GLY   B CA  
1371 C C   . GLY   B 124 ? 0.6837 0.7227 0.3633 0.1392  0.0779  0.0445  133 GLY   B C   
1372 O O   . GLY   B 124 ? 0.6740 0.7028 0.3571 0.1369  0.0767  0.0406  133 GLY   B O   
1373 N N   . THR   B 125 ? 0.6718 0.7155 0.3416 0.1476  0.0757  0.0450  134 THR   B N   
1374 C CA  . THR   B 125 ? 0.6791 0.7152 0.3407 0.1547  0.0713  0.0408  134 THR   B CA  
1375 C C   . THR   B 125 ? 0.6795 0.7070 0.3366 0.1528  0.0690  0.0346  134 THR   B C   
1376 O O   . THR   B 125 ? 0.6856 0.7043 0.3365 0.1568  0.0649  0.0306  134 THR   B O   
1377 C CB  . THR   B 125 ? 0.6974 0.7423 0.3502 0.1652  0.0697  0.0440  134 THR   B CB  
1378 O OG1 . THR   B 125 ? 0.7061 0.7617 0.3639 0.1651  0.0725  0.0507  134 THR   B OG1 
1379 C CG2 . THR   B 125 ? 0.6990 0.7364 0.3450 0.1725  0.0653  0.0411  134 THR   B CG2 
1380 N N   . SER   B 126 ? 0.6669 0.6965 0.3263 0.1468  0.0712  0.0341  135 SER   B N   
1381 C CA  . SER   B 126 ? 0.6610 0.6828 0.3163 0.1440  0.0690  0.0286  135 SER   B CA  
1382 C C   . SER   B 126 ? 0.6439 0.6532 0.3011 0.1408  0.0666  0.0236  135 SER   B C   
1383 O O   . SER   B 126 ? 0.6541 0.6616 0.3207 0.1354  0.0690  0.0238  135 SER   B O   
1384 C CB  . SER   B 126 ? 0.6619 0.6874 0.3224 0.1362  0.0724  0.0290  135 SER   B CB  
1385 O OG  . SER   B 126 ? 0.6743 0.7109 0.3309 0.1395  0.0736  0.0327  135 SER   B OG  
1386 N N   . GLY   B 127 ? 0.6350 0.6363 0.2835 0.1444  0.0619  0.0196  136 GLY   B N   
1387 C CA  . GLY   B 127 ? 0.6324 0.6225 0.2818 0.1409  0.0590  0.0150  136 GLY   B CA  
1388 C C   . GLY   B 127 ? 0.6479 0.6333 0.2922 0.1479  0.0552  0.0146  136 GLY   B C   
1389 O O   . GLY   B 127 ? 0.6598 0.6358 0.3027 0.1459  0.0517  0.0108  136 GLY   B O   
1390 N N   . SER   B 128 ? 0.6378 0.6299 0.2787 0.1559  0.0553  0.0185  137 SER   B N   
1391 C CA  . SER   B 128 ? 0.6373 0.6257 0.2723 0.1637  0.0515  0.0185  137 SER   B CA  
1392 C C   . SER   B 128 ? 0.6319 0.6110 0.2552 0.1676  0.0453  0.0144  137 SER   B C   
1393 O O   . SER   B 128 ? 0.6364 0.6167 0.2522 0.1702  0.0438  0.0137  137 SER   B O   
1394 C CB  . SER   B 128 ? 0.6472 0.6462 0.2801 0.1714  0.0530  0.0236  137 SER   B CB  
1395 O OG  . SER   B 128 ? 0.6525 0.6587 0.2963 0.1671  0.0580  0.0278  137 SER   B OG  
1396 N N   . PRO   B 129 ? 0.6261 0.5954 0.2467 0.1682  0.0410  0.0115  138 PRO   B N   
1397 C CA  . PRO   B 129 ? 0.6381 0.5972 0.2470 0.1711  0.0344  0.0078  138 PRO   B CA  
1398 C C   . PRO   B 129 ? 0.6622 0.6216 0.2584 0.1829  0.0302  0.0085  138 PRO   B C   
1399 O O   . PRO   B 129 ? 0.6669 0.6331 0.2634 0.1894  0.0316  0.0116  138 PRO   B O   
1400 C CB  . PRO   B 129 ? 0.6357 0.5856 0.2468 0.1676  0.0314  0.0052  138 PRO   B CB  
1401 C CG  . PRO   B 129 ? 0.6278 0.5837 0.2488 0.1675  0.0357  0.0082  138 PRO   B CG  
1402 C CD  . PRO   B 129 ? 0.6201 0.5873 0.2485 0.1658  0.0421  0.0118  138 PRO   B CD  
1403 N N   . ILE   B 130 ? 0.6785 0.6301 0.2636 0.1853  0.0246  0.0054  139 ILE   B N   
1404 C CA  . ILE   B 130 ? 0.7111 0.6597 0.2818 0.1967  0.0188  0.0045  139 ILE   B CA  
1405 C C   . ILE   B 130 ? 0.7467 0.6800 0.3097 0.1966  0.0114  0.0008  139 ILE   B C   
1406 O O   . ILE   B 130 ? 0.7250 0.6511 0.2910 0.1876  0.0102  -0.0014 139 ILE   B O   
1407 C CB  . ILE   B 130 ? 0.7110 0.6626 0.2748 0.1996  0.0181  0.0040  139 ILE   B CB  
1408 C CG1 . ILE   B 130 ? 0.7057 0.6736 0.2773 0.1996  0.0255  0.0083  139 ILE   B CG1 
1409 C CG2 . ILE   B 130 ? 0.7246 0.6705 0.2723 0.2113  0.0109  0.0019  139 ILE   B CG2 
1410 C CD1 . ILE   B 130 ? 0.7121 0.6827 0.2835 0.1957  0.0269  0.0076  139 ILE   B CD1 
1411 N N   . LEU   B 131 ? 0.7855 0.7154 0.3407 0.2055  0.0071  0.0007  140 LEU   B N   
1412 C CA  . LEU   B 131 ? 0.8273 0.7434 0.3762 0.2055  0.0002  -0.0019 140 LEU   B CA  
1413 C C   . LEU   B 131 ? 0.8476 0.7549 0.3792 0.2160  -0.0080 -0.0043 140 LEU   B C   
1414 O O   . LEU   B 131 ? 0.8580 0.7730 0.3842 0.2258  -0.0072 -0.0030 140 LEU   B O   
1415 C CB  . LEU   B 131 ? 0.8456 0.7649 0.4010 0.2069  0.0023  0.0001  140 LEU   B CB  
1416 C CG  . LEU   B 131 ? 0.8479 0.7791 0.4192 0.2010  0.0110  0.0034  140 LEU   B CG  
1417 C CD1 . LEU   B 131 ? 0.8510 0.7848 0.4262 0.2046  0.0120  0.0056  140 LEU   B CD1 
1418 C CD2 . LEU   B 131 ? 0.8504 0.7787 0.4315 0.1886  0.0133  0.0019  140 LEU   B CD2 
1419 N N   . ASP   B 132 ? 0.8661 0.7582 0.3897 0.2138  -0.0157 -0.0075 141 ASP   B N   
1420 C CA  . ASP   B 132 ? 0.8899 0.7700 0.3963 0.2232  -0.0252 -0.0101 141 ASP   B CA  
1421 C C   . ASP   B 132 ? 0.9268 0.8029 0.4311 0.2276  -0.0281 -0.0099 141 ASP   B C   
1422 O O   . ASP   B 132 ? 0.8935 0.7756 0.4101 0.2225  -0.0229 -0.0077 141 ASP   B O   
1423 C CB  . ASP   B 132 ? 0.8767 0.7416 0.3744 0.2179  -0.0328 -0.0135 141 ASP   B CB  
1424 C CG  . ASP   B 132 ? 0.8831 0.7387 0.3848 0.2077  -0.0357 -0.0143 141 ASP   B CG  
1425 O OD1 . ASP   B 132 ? 0.8553 0.7165 0.3679 0.2042  -0.0312 -0.0125 141 ASP   B OD1 
1426 O OD2 . ASP   B 132 ? 0.9154 0.7586 0.4096 0.2027  -0.0424 -0.0166 141 ASP   B OD2 
1427 N N   . LYS   B 133 ? 0.9869 0.8525 0.4757 0.2369  -0.0366 -0.0122 142 LYS   B N   
1428 C CA  . LYS   B 133 ? 1.0322 0.8946 0.5163 0.2440  -0.0400 -0.0120 142 LYS   B CA  
1429 C C   . LYS   B 133 ? 1.0159 0.8717 0.5074 0.2339  -0.0409 -0.0119 142 LYS   B C   
1430 O O   . LYS   B 133 ? 0.9835 0.8428 0.4794 0.2360  -0.0391 -0.0103 142 LYS   B O   
1431 C CB  . LYS   B 133 ? 1.0960 0.9470 0.5607 0.2558  -0.0497 -0.0152 142 LYS   B CB  
1432 C CG  . LYS   B 133 ? 1.1458 1.0081 0.6047 0.2689  -0.0475 -0.0145 142 LYS   B CG  
1433 C CD  . LYS   B 133 ? 1.2023 1.0544 0.6417 0.2805  -0.0567 -0.0184 142 LYS   B CD  
1434 C CE  . LYS   B 133 ? 1.2149 1.0817 0.6509 0.2919  -0.0530 -0.0176 142 LYS   B CE  
1435 N NZ  . LYS   B 133 ? 1.2318 1.0897 0.6484 0.3053  -0.0621 -0.0216 142 LYS   B NZ  
1436 N N   . CYS   B 134 ? 1.0025 0.8513 0.4970 0.2228  -0.0425 -0.0132 143 CYS   B N   
1437 C CA  . CYS   B 134 ? 0.9798 0.8238 0.4817 0.2126  -0.0433 -0.0132 143 CYS   B CA  
1438 C C   . CYS   B 134 ? 0.9366 0.7941 0.4574 0.2043  -0.0332 -0.0107 143 CYS   B C   
1439 O O   . CYS   B 134 ? 0.9438 0.7992 0.4721 0.1953  -0.0331 -0.0108 143 CYS   B O   
1440 C CB  . CYS   B 134 ? 1.0086 0.8395 0.5042 0.2044  -0.0503 -0.0155 143 CYS   B CB  
1441 S SG  . CYS   B 134 ? 1.0493 0.8601 0.5227 0.2120  -0.0643 -0.0185 143 CYS   B SG  
1442 N N   . GLY   B 135 ? 0.9101 0.7812 0.4384 0.2071  -0.0252 -0.0084 144 GLY   B N   
1443 C CA  . GLY   B 135 ? 0.8931 0.7761 0.4387 0.1993  -0.0160 -0.0062 144 GLY   B CA  
1444 C C   . GLY   B 135 ? 0.8714 0.7547 0.4238 0.1881  -0.0135 -0.0073 144 GLY   B C   
1445 O O   . GLY   B 135 ? 0.8466 0.7372 0.4129 0.1804  -0.0072 -0.0063 144 GLY   B O   
1446 N N   . ARG   B 136 ? 0.8810 0.7570 0.4242 0.1870  -0.0182 -0.0094 145 ARG   B N   
1447 C CA  . ARG   B 136 ? 0.8698 0.7462 0.4188 0.1762  -0.0161 -0.0105 145 ARG   B CA  
1448 C C   . ARG   B 136 ? 0.8283 0.7156 0.3823 0.1769  -0.0093 -0.0091 145 ARG   B C   
1449 O O   . ARG   B 136 ? 0.8093 0.6989 0.3555 0.1864  -0.0101 -0.0084 145 ARG   B O   
1450 C CB  . ARG   B 136 ? 0.9132 0.7754 0.4494 0.1739  -0.0252 -0.0132 145 ARG   B CB  
1451 C CG  . ARG   B 136 ? 0.9639 0.8172 0.4991 0.1683  -0.0307 -0.0142 145 ARG   B CG  
1452 C CD  . ARG   B 136 ? 1.0188 0.8573 0.5404 0.1658  -0.0405 -0.0163 145 ARG   B CD  
1453 N NE  . ARG   B 136 ? 1.0847 0.9161 0.5913 0.1777  -0.0463 -0.0172 145 ARG   B NE  
1454 C CZ  . ARG   B 136 ? 1.1633 0.9830 0.6560 0.1796  -0.0541 -0.0191 145 ARG   B CZ  
1455 N NH1 . ARG   B 136 ? 1.2430 1.0565 0.7345 0.1697  -0.0573 -0.0200 145 ARG   B NH1 
1456 N NH2 . ARG   B 136 ? 1.2169 1.0313 0.6964 0.1919  -0.0589 -0.0201 145 ARG   B NH2 
1457 N N   . VAL   B 137 ? 0.7932 0.6873 0.3594 0.1673  -0.0031 -0.0087 146 VAL   B N   
1458 C CA  . VAL   B 137 ? 0.7609 0.6654 0.3323 0.1673  0.0033  -0.0071 146 VAL   B CA  
1459 C C   . VAL   B 137 ? 0.7680 0.6665 0.3296 0.1666  -0.0009 -0.0091 146 VAL   B C   
1460 O O   . VAL   B 137 ? 0.7719 0.6634 0.3330 0.1582  -0.0038 -0.0111 146 VAL   B O   
1461 C CB  . VAL   B 137 ? 0.7424 0.6563 0.3298 0.1584  0.0114  -0.0060 146 VAL   B CB  
1462 C CG1 . VAL   B 137 ? 0.7345 0.6589 0.3264 0.1590  0.0175  -0.0039 146 VAL   B CG1 
1463 C CG2 . VAL   B 137 ? 0.7450 0.6631 0.3416 0.1587  0.0146  -0.0044 146 VAL   B CG2 
1464 N N   . ILE   B 138 ? 0.7580 0.6595 0.3120 0.1753  -0.0013 -0.0083 147 ILE   B N   
1465 C CA  . ILE   B 138 ? 0.7564 0.6526 0.2999 0.1768  -0.0057 -0.0101 147 ILE   B CA  
1466 C C   . ILE   B 138 ? 0.7388 0.6466 0.2901 0.1735  0.0013  -0.0085 147 ILE   B C   
1467 O O   . ILE   B 138 ? 0.7294 0.6347 0.2734 0.1744  -0.0012 -0.0097 147 ILE   B O   
1468 C CB  . ILE   B 138 ? 0.7724 0.6644 0.3010 0.1902  -0.0117 -0.0107 147 ILE   B CB  
1469 C CG1 . ILE   B 138 ? 0.7661 0.6715 0.2981 0.1990  -0.0063 -0.0077 147 ILE   B CG1 
1470 C CG2 . ILE   B 138 ? 0.7887 0.6661 0.3072 0.1925  -0.0205 -0.0129 147 ILE   B CG2 
1471 C CD1 . ILE   B 138 ? 0.7875 0.6933 0.3059 0.2123  -0.0105 -0.0082 147 ILE   B CD1 
1472 N N   . GLY   B 139 ? 0.7198 0.6394 0.2845 0.1702  0.0095  -0.0058 148 GLY   B N   
1473 C CA  . GLY   B 139 ? 0.7087 0.6387 0.2814 0.1655  0.0161  -0.0042 148 GLY   B CA  
1474 C C   . GLY   B 139 ? 0.6958 0.6383 0.2808 0.1650  0.0239  -0.0007 148 GLY   B C   
1475 O O   . GLY   B 139 ? 0.6978 0.6405 0.2847 0.1686  0.0239  0.0003  148 GLY   B O   
1476 N N   . LEU   B 140 ? 0.6845 0.6365 0.2767 0.1610  0.0297  0.0011  149 LEU   B N   
1477 C CA  . LEU   B 140 ? 0.6820 0.6458 0.2861 0.1593  0.0370  0.0048  149 LEU   B CA  
1478 C C   . LEU   B 140 ? 0.6813 0.6565 0.2834 0.1646  0.0399  0.0081  149 LEU   B C   
1479 O O   . LEU   B 140 ? 0.6690 0.6437 0.2644 0.1658  0.0380  0.0069  149 LEU   B O   
1480 C CB  . LEU   B 140 ? 0.6741 0.6393 0.2908 0.1478  0.0419  0.0043  149 LEU   B CB  
1481 C CG  . LEU   B 140 ? 0.6821 0.6387 0.3029 0.1411  0.0401  0.0012  149 LEU   B CG  
1482 C CD1 . LEU   B 140 ? 0.6813 0.6421 0.3148 0.1310  0.0458  0.0010  149 LEU   B CD1 
1483 C CD2 . LEU   B 140 ? 0.6904 0.6442 0.3118 0.1452  0.0384  0.0016  149 LEU   B CD2 
1484 N N   . TYR   B 141 ? 0.6816 0.6667 0.2892 0.1678  0.0440  0.0122  150 TYR   B N   
1485 C CA  . TYR   B 141 ? 0.6952 0.6936 0.3013 0.1740  0.0468  0.0164  150 TYR   B CA  
1486 C C   . TYR   B 141 ? 0.6892 0.6971 0.3069 0.1658  0.0534  0.0196  150 TYR   B C   
1487 O O   . TYR   B 141 ? 0.7025 0.7089 0.3305 0.1585  0.0565  0.0200  150 TYR   B O   
1488 C CB  . TYR   B 141 ? 0.7134 0.7173 0.3187 0.1819  0.0470  0.0196  150 TYR   B CB  
1489 C CG  . TYR   B 141 ? 0.7118 0.7319 0.3190 0.1860  0.0511  0.0251  150 TYR   B CG  
1490 C CD1 . TYR   B 141 ? 0.7103 0.7389 0.3292 0.1796  0.0569  0.0294  150 TYR   B CD1 
1491 C CD2 . TYR   B 141 ? 0.7226 0.7497 0.3195 0.1962  0.0489  0.0259  150 TYR   B CD2 
1492 C CE1 . TYR   B 141 ? 0.7275 0.7715 0.3481 0.1824  0.0605  0.0350  150 TYR   B CE1 
1493 C CE2 . TYR   B 141 ? 0.7325 0.7763 0.3312 0.1998  0.0528  0.0313  150 TYR   B CE2 
1494 C CZ  . TYR   B 141 ? 0.7398 0.7923 0.3505 0.1926  0.0585  0.0362  150 TYR   B CZ  
1495 O OH  . TYR   B 141 ? 0.7490 0.8186 0.3616 0.1952  0.0621  0.0421  150 TYR   B OH  
1496 N N   . GLY   B 142 ? 0.6938 0.7111 0.3095 0.1672  0.0553  0.0217  151 GLY   B N   
1497 C CA  . GLY   B 142 ? 0.6965 0.7238 0.3229 0.1599  0.0614  0.0255  151 GLY   B CA  
1498 C C   . GLY   B 142 ? 0.7044 0.7332 0.3310 0.1545  0.0627  0.0244  151 GLY   B C   
1499 O O   . GLY   B 142 ? 0.6966 0.7334 0.3318 0.1480  0.0676  0.0276  151 GLY   B O   
1500 N N   . ASN   B 143 ? 0.7155 0.7373 0.3328 0.1570  0.0582  0.0204  152 ASN   B N   
1501 C CA  . ASN   B 143 ? 0.7099 0.7357 0.3256 0.1541  0.0591  0.0201  152 ASN   B CA  
1502 C C   . ASN   B 143 ? 0.7121 0.7418 0.3155 0.1650  0.0553  0.0201  152 ASN   B C   
1503 O O   . ASN   B 143 ? 0.7179 0.7375 0.3113 0.1708  0.0494  0.0164  152 ASN   B O   
1504 C CB  . ASN   B 143 ? 0.7189 0.7331 0.3351 0.1458  0.0574  0.0155  152 ASN   B CB  
1505 C CG  . ASN   B 143 ? 0.7164 0.7359 0.3340 0.1408  0.0596  0.0159  152 ASN   B CG  
1506 O OD1 . ASN   B 143 ? 0.7013 0.7327 0.3250 0.1387  0.0644  0.0200  152 ASN   B OD1 
1507 N ND2 . ASN   B 143 ? 0.7205 0.7309 0.3323 0.1383  0.0558  0.0118  152 ASN   B ND2 
1508 N N   . GLY   B 144 ? 0.7160 0.7599 0.3200 0.1675  0.0584  0.0240  153 GLY   B N   
1509 C CA  . GLY   B 144 ? 0.7466 0.7964 0.3391 0.1788  0.0551  0.0240  153 GLY   B CA  
1510 C C   . GLY   B 144 ? 0.7675 0.8348 0.3632 0.1790  0.0596  0.0287  153 GLY   B C   
1511 O O   . GLY   B 144 ? 0.7462 0.8161 0.3499 0.1693  0.0633  0.0299  153 GLY   B O   
1512 N N   . VAL   B 145 ? 0.8038 0.8835 0.3937 0.1897  0.0591  0.0315  154 VAL   B N   
1513 C CA  . VAL   B 145 ? 0.8429 0.9398 0.4313 0.1933  0.0614  0.0351  154 VAL   B CA  
1514 C C   . VAL   B 145 ? 0.8967 1.0106 0.4858 0.2003  0.0638  0.0407  154 VAL   B C   
1515 O O   . VAL   B 145 ? 0.9250 1.0348 0.5122 0.2049  0.0622  0.0403  154 VAL   B O   
1516 C CB  . VAL   B 145 ? 0.8566 0.9486 0.4323 0.2013  0.0558  0.0305  154 VAL   B CB  
1517 C CG1 . VAL   B 145 ? 0.8545 0.9512 0.4185 0.2164  0.0517  0.0298  154 VAL   B CG1 
1518 C CG2 . VAL   B 145 ? 0.8646 0.9656 0.4420 0.1976  0.0581  0.0319  154 VAL   B CG2 
1519 N N   . VAL   B 146 ? 0.9299 1.0625 0.5224 0.2000  0.0678  0.0459  155 VAL   B N   
1520 C CA  . VAL   B 146 ? 0.9648 1.1178 0.5582 0.2058  0.0706  0.0523  155 VAL   B CA  
1521 C C   . VAL   B 146 ? 1.0290 1.1935 0.6111 0.2185  0.0679  0.0514  155 VAL   B C   
1522 O O   . VAL   B 146 ? 1.0370 1.2030 0.6173 0.2170  0.0676  0.0501  155 VAL   B O   
1523 C CB  . VAL   B 146 ? 0.9447 1.1103 0.5502 0.1949  0.0766  0.0590  155 VAL   B CB  
1524 C CG1 . VAL   B 146 ? 0.9799 1.1682 0.5862 0.2000  0.0793  0.0662  155 VAL   B CG1 
1525 C CG2 . VAL   B 146 ? 0.9278 1.0813 0.5437 0.1835  0.0788  0.0593  155 VAL   B CG2 
1526 N N   . ILE   B 147 ? 1.0504 1.2224 0.6246 0.2310  0.0656  0.0518  156 ILE   B N   
1527 C CA  . ILE   B 147 ? 1.1103 1.2891 0.6716 0.2448  0.0616  0.0490  156 ILE   B CA  
1528 C C   . ILE   B 147 ? 1.1535 1.3600 0.7159 0.2496  0.0654  0.0555  156 ILE   B C   
1529 O O   . ILE   B 147 ? 1.1095 1.3283 0.6822 0.2421  0.0706  0.0623  156 ILE   B O   
1530 C CB  . ILE   B 147 ? 1.1310 1.2979 0.6803 0.2568  0.0553  0.0436  156 ILE   B CB  
1531 C CG1 . ILE   B 147 ? 1.1541 1.3268 0.7051 0.2605  0.0565  0.0468  156 ILE   B CG1 
1532 C CG2 . ILE   B 147 ? 1.1318 1.2724 0.6780 0.2524  0.0506  0.0368  156 ILE   B CG2 
1533 C CD1 . ILE   B 147 ? 1.1449 1.3156 0.6822 0.2762  0.0508  0.0429  156 ILE   B CD1 
1534 N N   A LYS   B 148 ? 1.1784 1.3943 0.7303 0.2618  0.0624  0.0534  157 LYS   B N   
1535 N N   B LYS   B 148 ? 1.1784 1.3943 0.7303 0.2618  0.0624  0.0534  157 LYS   B N   
1536 N N   C LYS   B 148 ? 1.1764 1.3927 0.7284 0.2618  0.0625  0.0536  157 LYS   B N   
1537 N N   D LYS   B 148 ? 1.1764 1.3927 0.7284 0.2618  0.0625  0.0536  157 LYS   B N   
1538 C CA  A LYS   B 148 ? 1.2057 1.4496 0.7558 0.2697  0.0650  0.0586  157 LYS   B CA  
1539 C CA  B LYS   B 148 ? 1.2057 1.4496 0.7558 0.2697  0.0650  0.0586  157 LYS   B CA  
1540 C CA  C LYS   B 148 ? 1.2010 1.4457 0.7525 0.2682  0.0656  0.0593  157 LYS   B CA  
1541 C CA  D LYS   B 148 ? 1.2010 1.4457 0.7525 0.2682  0.0656  0.0593  157 LYS   B CA  
1542 C C   A LYS   B 148 ? 1.2013 1.4607 0.7597 0.2662  0.0698  0.0663  157 LYS   B C   
1543 C C   B LYS   B 148 ? 1.2013 1.4607 0.7597 0.2662  0.0698  0.0663  157 LYS   B C   
1544 C C   C LYS   B 148 ? 1.1999 1.4598 0.7586 0.2660  0.0700  0.0666  157 LYS   B C   
1545 C C   D LYS   B 148 ? 1.1999 1.4598 0.7586 0.2660  0.0700  0.0666  157 LYS   B C   
1546 O O   A LYS   B 148 ? 1.1954 1.4744 0.7617 0.2602  0.0748  0.0734  157 LYS   B O   
1547 O O   B LYS   B 148 ? 1.1954 1.4744 0.7617 0.2602  0.0748  0.0734  157 LYS   B O   
1548 O O   C LYS   B 148 ? 1.1965 1.4769 0.7628 0.2606  0.0749  0.0738  157 LYS   B O   
1549 O O   D LYS   B 148 ? 1.1965 1.4769 0.7628 0.2606  0.0749  0.0738  157 LYS   B O   
1550 C CB  A LYS   B 148 ? 1.2333 1.4806 0.7684 0.2878  0.0595  0.0540  157 LYS   B CB  
1551 C CB  B LYS   B 148 ? 1.2333 1.4806 0.7684 0.2878  0.0595  0.0540  157 LYS   B CB  
1552 C CB  C LYS   B 148 ? 1.2261 1.4763 0.7628 0.2858  0.0605  0.0549  157 LYS   B CB  
1553 C CB  D LYS   B 148 ? 1.2261 1.4763 0.7628 0.2858  0.0605  0.0549  157 LYS   B CB  
1554 C CG  A LYS   B 148 ? 1.2547 1.4923 0.7795 0.2943  0.0543  0.0473  157 LYS   B CG  
1555 C CG  B LYS   B 148 ? 1.2547 1.4923 0.7795 0.2943  0.0543  0.0473  157 LYS   B CG  
1556 C CG  C LYS   B 148 ? 1.2395 1.4780 0.7678 0.2894  0.0558  0.0483  157 LYS   B CG  
1557 C CG  D LYS   B 148 ? 1.2395 1.4780 0.7678 0.2894  0.0558  0.0483  157 LYS   B CG  
1558 C CD  A LYS   B 148 ? 1.2708 1.5169 0.7810 0.3130  0.0494  0.0438  157 LYS   B CD  
1559 C CD  B LYS   B 148 ? 1.2708 1.5169 0.7810 0.3130  0.0494  0.0438  157 LYS   B CD  
1560 C CD  C LYS   B 148 ? 1.2357 1.4926 0.7667 0.2879  0.0588  0.0516  157 LYS   B CD  
1561 C CD  D LYS   B 148 ? 1.2357 1.4926 0.7667 0.2879  0.0588  0.0516  157 LYS   B CD  
1562 C CE  A LYS   B 148 ? 1.2733 1.5518 0.7850 0.3196  0.0537  0.0502  157 LYS   B CE  
1563 C CE  B LYS   B 148 ? 1.2733 1.5518 0.7850 0.3196  0.0537  0.0502  157 LYS   B CE  
1564 C CE  C LYS   B 148 ? 1.2307 1.5187 0.7622 0.2952  0.0624  0.0580  157 LYS   B CE  
1565 C CE  D LYS   B 148 ? 1.2307 1.5187 0.7622 0.2952  0.0624  0.0580  157 LYS   B CE  
1566 N NZ  A LYS   B 148 ? 1.2734 1.5675 0.7933 0.3112  0.0586  0.0551  157 LYS   B NZ  
1567 N NZ  B LYS   B 148 ? 1.2734 1.5675 0.7933 0.3112  0.0586  0.0551  157 LYS   B NZ  
1568 N NZ  C LYS   B 148 ? 1.2228 1.5271 0.7500 0.3012  0.0623  0.0582  157 LYS   B NZ  
1569 N NZ  D LYS   B 148 ? 1.2228 1.5271 0.7500 0.3012  0.0623  0.0582  157 LYS   B NZ  
1570 N N   . ASN   B 149 ? 1.2180 1.4680 0.7743 0.2697  0.0679  0.0650  158 ASN   B N   
1571 C CA  . ASN   B 149 ? 1.2032 1.4665 0.7648 0.2692  0.0711  0.0715  158 ASN   B CA  
1572 C C   . ASN   B 149 ? 1.1527 1.4166 0.7290 0.2529  0.0764  0.0778  158 ASN   B C   
1573 O O   . ASN   B 149 ? 1.1565 1.4369 0.7380 0.2513  0.0797  0.0851  158 ASN   B O   
1574 C CB  . ASN   B 149 ? 1.2341 1.4827 0.7895 0.2762  0.0671  0.0673  158 ASN   B CB  
1575 C CG  . ASN   B 149 ? 1.2724 1.5096 0.8130 0.2899  0.0603  0.0590  158 ASN   B CG  
1576 O OD1 . ASN   B 149 ? 1.3032 1.5387 0.8380 0.2933  0.0580  0.0552  158 ASN   B OD1 
1577 N ND2 . ASN   B 149 ? 1.2909 1.5196 0.8247 0.2978  0.0566  0.0561  158 ASN   B ND2 
1578 N N   . GLY   B 150 ? 1.1049 1.3509 0.6874 0.2415  0.0768  0.0751  159 GLY   B N   
1579 C CA  . GLY   B 150 ? 1.0390 1.2795 0.6345 0.2267  0.0806  0.0793  159 GLY   B CA  
1580 C C   . GLY   B 150 ? 1.0096 1.2279 0.6067 0.2238  0.0785  0.0753  159 GLY   B C   
1581 O O   . GLY   B 150 ? 0.9744 1.1851 0.5819 0.2118  0.0811  0.0775  159 GLY   B O   
1582 N N   A SER   B 151 ? 1.0080 1.2163 0.5951 0.2345  0.0738  0.0696  160 SER   B N   
1583 N N   B SER   B 151 ? 1.0045 1.2129 0.5915 0.2346  0.0738  0.0695  160 SER   B N   
1584 N N   C SER   B 151 ? 1.0080 1.2163 0.5951 0.2345  0.0738  0.0696  160 SER   B N   
1585 N N   D SER   B 151 ? 1.0045 1.2129 0.5915 0.2346  0.0738  0.0695  160 SER   B N   
1586 C CA  A SER   B 151 ? 0.9950 1.1823 0.5819 0.2333  0.0710  0.0651  160 SER   B CA  
1587 C CA  B SER   B 151 ? 0.9899 1.1771 0.5762 0.2338  0.0708  0.0649  160 SER   B CA  
1588 C CA  C SER   B 151 ? 0.9950 1.1823 0.5819 0.2333  0.0710  0.0651  160 SER   B CA  
1589 C CA  D SER   B 151 ? 0.9899 1.1771 0.5762 0.2338  0.0708  0.0649  160 SER   B CA  
1590 C C   A SER   B 151 ? 0.9806 1.1463 0.5678 0.2268  0.0687  0.0585  160 SER   B C   
1591 C C   B SER   B 151 ? 0.9768 1.1427 0.5644 0.2264  0.0689  0.0587  160 SER   B C   
1592 C C   C SER   B 151 ? 0.9806 1.1463 0.5678 0.2268  0.0687  0.0585  160 SER   B C   
1593 C C   D SER   B 151 ? 0.9768 1.1427 0.5644 0.2264  0.0689  0.0587  160 SER   B C   
1594 O O   A SER   B 151 ? 0.9731 1.1393 0.5568 0.2271  0.0678  0.0562  160 SER   B O   
1595 O O   B SER   B 151 ? 0.9686 1.1352 0.5537 0.2256  0.0684  0.0567  160 SER   B O   
1596 O O   C SER   B 151 ? 0.9731 1.1393 0.5568 0.2271  0.0678  0.0562  160 SER   B O   
1597 O O   D SER   B 151 ? 0.9686 1.1352 0.5537 0.2256  0.0684  0.0567  160 SER   B O   
1598 C CB  A SER   B 151 ? 1.0039 1.1901 0.5794 0.2473  0.0665  0.0621  160 SER   B CB  
1599 C CB  B SER   B 151 ? 0.9950 1.1807 0.5692 0.2482  0.0660  0.0613  160 SER   B CB  
1600 C CB  C SER   B 151 ? 1.0039 1.1901 0.5794 0.2473  0.0665  0.0621  160 SER   B CB  
1601 C CB  D SER   B 151 ? 0.9950 1.1807 0.5692 0.2482  0.0660  0.0613  160 SER   B CB  
1602 O OG  A SER   B 151 ? 1.0016 1.1723 0.5787 0.2456  0.0648  0.0600  160 SER   B OG  
1603 O OG  B SER   B 151 ? 0.9922 1.1828 0.5557 0.2581  0.0630  0.0579  160 SER   B OG  
1604 O OG  C SER   B 151 ? 1.0016 1.1723 0.5787 0.2456  0.0648  0.0600  160 SER   B OG  
1605 O OG  D SER   B 151 ? 0.9922 1.1828 0.5557 0.2581  0.0630  0.0579  160 SER   B OG  
1606 N N   . TYR   B 152 ? 0.9655 1.1137 0.5566 0.2212  0.0676  0.0558  161 TYR   B N   
1607 C CA  . TYR   B 152 ? 0.9547 1.0825 0.5473 0.2138  0.0656  0.0499  161 TYR   B CA  
1608 C C   . TYR   B 152 ? 0.9115 1.0229 0.4929 0.2218  0.0591  0.0430  161 TYR   B C   
1609 O O   . TYR   B 152 ? 0.8602 0.9680 0.4387 0.2271  0.0571  0.0426  161 TYR   B O   
1610 C CB  . TYR   B 152 ? 0.9769 1.0972 0.5815 0.2022  0.0687  0.0517  161 TYR   B CB  
1611 C CG  . TYR   B 152 ? 0.9818 1.0843 0.5901 0.1931  0.0678  0.0465  161 TYR   B CG  
1612 C CD1 . TYR   B 152 ? 0.9867 1.0898 0.6000 0.1846  0.0702  0.0465  161 TYR   B CD1 
1613 C CD2 . TYR   B 152 ? 0.9850 1.0707 0.5919 0.1928  0.0645  0.0419  161 TYR   B CD2 
1614 C CE1 . TYR   B 152 ? 0.9760 1.0640 0.5927 0.1761  0.0695  0.0419  161 TYR   B CE1 
1615 C CE2 . TYR   B 152 ? 1.0174 1.0885 0.6278 0.1843  0.0637  0.0375  161 TYR   B CE2 
1616 C CZ  . TYR   B 152 ? 0.9916 1.0640 0.6068 0.1761  0.0662  0.0374  161 TYR   B CZ  
1617 O OH  . TYR   B 152 ? 1.0604 1.1196 0.6791 0.1676  0.0656  0.0331  161 TYR   B OH  
1618 N N   . VAL   B 153 ? 0.8586 0.9593 0.4342 0.2215  0.0556  0.0377  162 VAL   B N   
1619 C CA  . VAL   B 153 ? 0.8432 0.9246 0.4090 0.2259  0.0488  0.0309  162 VAL   B CA  
1620 C C   . VAL   B 153 ? 0.8033 0.8688 0.3754 0.2135  0.0488  0.0277  162 VAL   B C   
1621 O O   . VAL   B 153 ? 0.7767 0.8441 0.3523 0.2071  0.0508  0.0278  162 VAL   B O   
1622 C CB  . VAL   B 153 ? 0.8617 0.9438 0.4140 0.2364  0.0439  0.0275  162 VAL   B CB  
1623 C CG1 . VAL   B 153 ? 0.8690 0.9333 0.4090 0.2438  0.0360  0.0214  162 VAL   B CG1 
1624 C CG2 . VAL   B 153 ? 0.8929 0.9962 0.4417 0.2466  0.0458  0.0316  162 VAL   B CG2 
1625 N N   . SER   B 154 ? 0.7762 0.8273 0.3492 0.2108  0.0463  0.0249  163 SER   B N   
1626 C CA  . SER   B 154 ? 0.7559 0.7919 0.3341 0.2000  0.0457  0.0215  163 SER   B CA  
1627 C C   . SER   B 154 ? 0.7592 0.7791 0.3257 0.2032  0.0383  0.0156  163 SER   B C   
1628 O O   . SER   B 154 ? 0.7587 0.7734 0.3150 0.2128  0.0330  0.0136  163 SER   B O   
1629 C CB  . SER   B 154 ? 0.7461 0.7775 0.3323 0.1953  0.0474  0.0225  163 SER   B CB  
1630 O OG  . SER   B 154 ? 0.7229 0.7402 0.3131 0.1859  0.0463  0.0187  163 SER   B OG  
1631 N N   . ALA   B 155 ? 0.7419 0.7529 0.3101 0.1946  0.0375  0.0128  164 ALA   B N   
1632 C CA  . ALA   B 155 ? 0.7423 0.7354 0.3018 0.1940  0.0304  0.0075  164 ALA   B CA  
1633 C C   . ALA   B 155 ? 0.7433 0.7274 0.3059 0.1918  0.0291  0.0065  164 ALA   B C   
1634 O O   . ALA   B 155 ? 0.7471 0.7375 0.3210 0.1874  0.0345  0.0095  164 ALA   B O   
1635 C CB  . ALA   B 155 ? 0.7462 0.7336 0.3090 0.1836  0.0308  0.0054  164 ALA   B CB  
1636 N N   . ILE   B 156 ? 0.7476 0.7179 0.2993 0.1963  0.0215  0.0027  165 ILE   B N   
1637 C CA  . ILE   B 156 ? 0.7464 0.7040 0.3000 0.1908  0.0187  0.0005  165 ILE   B CA  
1638 C C   . ILE   B 156 ? 0.7376 0.6874 0.2950 0.1790  0.0184  -0.0018 165 ILE   B C   
1639 O O   . ILE   B 156 ? 0.7234 0.6623 0.2707 0.1795  0.0120  -0.0049 165 ILE   B O   
1640 C CB  . ILE   B 156 ? 0.7626 0.7080 0.3021 0.1998  0.0102  -0.0023 165 ILE   B CB  
1641 C CG1 . ILE   B 156 ? 0.7847 0.7388 0.3182 0.2130  0.0099  -0.0004 165 ILE   B CG1 
1642 C CG2 . ILE   B 156 ? 0.7611 0.6956 0.3038 0.1938  0.0078  -0.0039 165 ILE   B CG2 
1643 C CD1 . ILE   B 156 ? 0.8095 0.7521 0.3268 0.2234  0.0009  -0.0038 165 ILE   B CD1 
1644 N N   . THR   B 157 ? 0.7244 0.6801 0.2955 0.1690  0.0251  -0.0002 166 THR   B N   
1645 C CA  . THR   B 157 ? 0.7186 0.6699 0.2959 0.1569  0.0263  -0.0020 166 THR   B CA  
1646 C C   . THR   B 157 ? 0.7199 0.6601 0.2983 0.1515  0.0230  -0.0046 166 THR   B C   
1647 O O   . THR   B 157 ? 0.7069 0.6502 0.2943 0.1496  0.0265  -0.0033 166 THR   B O   
1648 C CB  . THR   B 157 ? 0.7070 0.6701 0.2981 0.1498  0.0348  0.0006  166 THR   B CB  
1649 O OG1 . THR   B 157 ? 0.6924 0.6663 0.2815 0.1549  0.0373  0.0033  166 THR   B OG1 
1650 C CG2 . THR   B 157 ? 0.6999 0.6594 0.2974 0.1377  0.0363  -0.0014 166 THR   B CG2 
1651 N N   . GLN   B 158 ? 0.7208 0.6490 0.2908 0.1488  0.0164  -0.0077 167 GLN   B N   
1652 C CA  . GLN   B 158 ? 0.7315 0.6493 0.3019 0.1421  0.0126  -0.0101 167 GLN   B CA  
1653 C C   . GLN   B 158 ? 0.7488 0.6642 0.3232 0.1303  0.0131  -0.0118 167 GLN   B C   
1654 O O   . GLN   B 158 ? 0.7300 0.6446 0.2994 0.1295  0.0118  -0.0123 167 GLN   B O   
1655 C CB  . GLN   B 158 ? 0.7328 0.6379 0.2884 0.1492  0.0032  -0.0119 167 GLN   B CB  
1656 C CG  . GLN   B 158 ? 0.7341 0.6289 0.2891 0.1435  -0.0014 -0.0137 167 GLN   B CG  
1657 C CD  . GLN   B 158 ? 0.7265 0.6267 0.2930 0.1409  0.0033  -0.0125 167 GLN   B CD  
1658 O OE1 . GLN   B 158 ? 0.7105 0.6201 0.2900 0.1348  0.0106  -0.0115 167 GLN   B OE1 
1659 N NE2 . GLN   B 158 ? 0.7243 0.6182 0.2859 0.1456  -0.0012 -0.0129 167 GLN   B NE2 
1660 N N   . GLY   B 159 ? 0.7799 0.6944 0.3627 0.1216  0.0147  -0.0127 168 GLY   B N   
1661 C CA  . GLY   B 159 ? 0.8367 0.7492 0.4232 0.1101  0.0148  -0.0146 168 GLY   B CA  
1662 C C   . GLY   B 159 ? 0.9007 0.7999 0.4760 0.1080  0.0058  -0.0166 168 GLY   B C   
1663 O O   . GLY   B 159 ? 0.9187 0.8100 0.4834 0.1159  -0.0004 -0.0167 168 GLY   B O   
1664 N N   . LYS   B 160 ? 1.0110 0.9081 0.5879 0.0976  0.0048  -0.0180 169 LYS   B N   
1665 C CA  . LYS   B 160 ? 1.0998 0.9851 0.6680 0.0924  -0.0035 -0.0196 169 LYS   B CA  
1666 C C   . LYS   B 160 ? 1.1527 1.0407 0.7302 0.0843  -0.0018 -0.0202 169 LYS   B C   
1667 O O   . LYS   B 160 ? 1.1755 1.0738 0.7659 0.0782  0.0056  -0.0203 169 LYS   B O   
1668 C CB  . LYS   B 160 ? 1.1423 1.0247 0.7059 0.0863  -0.0058 -0.0203 169 LYS   B CB  
1669 C CG  . LYS   B 160 ? 1.1867 1.0546 0.7369 0.0836  -0.0163 -0.0213 169 LYS   B CG  
1670 C CD  . LYS   B 160 ? 1.1948 1.0596 0.7409 0.0762  -0.0189 -0.0219 169 LYS   B CD  
1671 C CE  . LYS   B 160 ? 1.2215 1.0791 0.7646 0.0654  -0.0249 -0.0224 169 LYS   B CE  
1672 N NZ  . LYS   B 160 ? 1.2429 1.1079 0.7939 0.0540  -0.0206 -0.0227 169 LYS   B NZ  
1673 N N   . ARG   B 161 ? 1.1939 1.0731 0.7651 0.0846  -0.0086 -0.0205 170 ARG   B N   
1674 C CA  . ARG   B 161 ? 1.2371 1.1179 0.8151 0.0764  -0.0088 -0.0211 170 ARG   B CA  
1675 C C   . ARG   B 161 ? 1.3065 1.1818 0.8795 0.0658  -0.0143 -0.0219 170 ARG   B C   
1676 O O   . ARG   B 161 ? 1.3692 1.2331 0.9287 0.0678  -0.0220 -0.0219 170 ARG   B O   
1677 C CB  . ARG   B 161 ? 1.2226 1.0974 0.7959 0.0828  -0.0133 -0.0207 170 ARG   B CB  
1678 C CG  . ARG   B 161 ? 1.2097 1.0889 0.7921 0.0769  -0.0118 -0.0210 170 ARG   B CG  
1679 C CD  . ARG   B 161 ? 1.2206 1.0917 0.7960 0.0821  -0.0182 -0.0205 170 ARG   B CD  
1680 N NE  . ARG   B 161 ? 1.2314 1.1054 0.8132 0.0745  -0.0189 -0.0208 170 ARG   B NE  
1681 C CZ  . ARG   B 161 ? 1.2298 1.1095 0.8200 0.0765  -0.0155 -0.0205 170 ARG   B CZ  
1682 N NH1 . ARG   B 161 ? 1.1746 1.0576 0.7681 0.0858  -0.0112 -0.0198 170 ARG   B NH1 
1683 N NH2 . ARG   B 161 ? 1.2502 1.1331 0.8456 0.0689  -0.0166 -0.0209 170 ARG   B NH2 
1684 N N   . GLU   B 162 ? 1.3433 1.2263 0.9263 0.0553  -0.0108 -0.0227 171 GLU   B N   
1685 C CA  . GLU   B 162 ? 1.3834 1.2639 0.9633 0.0439  -0.0150 -0.0231 171 GLU   B CA  
1686 C C   . GLU   B 162 ? 1.3313 1.2103 0.9115 0.0379  -0.0195 -0.0230 171 GLU   B C   
1687 O O   . GLU   B 162 ? 1.2970 1.1643 0.8656 0.0383  -0.0286 -0.0222 171 GLU   B O   
1688 C CB  . GLU   B 162 ? 1.4145 1.3066 1.0054 0.0359  -0.0075 -0.0241 171 GLU   B CB  
1689 C CG  . GLU   B 162 ? 1.4539 1.3522 1.0498 0.0415  -0.0001 -0.0241 171 GLU   B CG  
1690 C CD  . GLU   B 162 ? 1.5218 1.4152 1.1092 0.0422  -0.0024 -0.0238 171 GLU   B CD  
1691 O OE1 . GLU   B 162 ? 1.5664 1.4573 1.1503 0.0335  -0.0058 -0.0241 171 GLU   B OE1 
1692 O OE2 . GLU   B 162 ? 1.5377 1.4306 1.1224 0.0513  -0.0007 -0.0230 171 GLU   B OE2 
1693 S S   A DMS   C .   ? 1.5321 1.6253 1.1808 0.1571  0.0799  0.0545  201 DMS   B S   
1694 S S   B DMS   C .   ? 1.5321 1.6253 1.1808 0.1571  0.0799  0.0545  201 DMS   B S   
1695 O O   A DMS   C .   ? 1.5330 1.6409 1.1746 0.1640  0.0799  0.0573  201 DMS   B O   
1696 O O   B DMS   C .   ? 1.5330 1.6409 1.1746 0.1640  0.0799  0.0573  201 DMS   B O   
1697 C C1  A DMS   C .   ? 1.5301 1.6119 1.1821 0.1477  0.0802  0.0490  201 DMS   B C1  
1698 C C1  B DMS   C .   ? 1.5301 1.6119 1.1821 0.1477  0.0802  0.0490  201 DMS   B C1  
1699 C C2  A DMS   C .   ? 1.5349 1.6142 1.1750 0.1652  0.0745  0.0482  201 DMS   B C2  
1700 C C2  B DMS   C .   ? 1.5349 1.6142 1.1750 0.1652  0.0745  0.0482  201 DMS   B C2  
1701 S S   . DMS   D .   ? 1.1893 1.1857 0.9296 0.0361  0.0974  -0.0141 202 DMS   B S   
1702 O O   . DMS   D .   ? 1.1163 1.1116 0.8498 0.0386  0.0944  -0.0155 202 DMS   B O   
1703 C C1  . DMS   D .   ? 1.1497 1.1428 0.8969 0.0393  0.0973  -0.0152 202 DMS   B C1  
1704 C C2  . DMS   D .   ? 1.1325 1.1317 0.8697 0.0406  0.0976  -0.0064 202 DMS   B C2  
1705 S S   A DMS   E .   ? 1.0730 1.1447 0.7120 0.1460  0.0759  0.0386  203 DMS   B S   
1706 S S   B DMS   E .   ? 1.0730 1.1447 0.7120 0.1460  0.0759  0.0386  203 DMS   B S   
1707 O O   A DMS   E .   ? 1.0566 1.1250 0.6834 0.1543  0.0712  0.0349  203 DMS   B O   
1708 O O   B DMS   E .   ? 1.0566 1.1250 0.6834 0.1543  0.0712  0.0349  203 DMS   B O   
1709 C C1  A DMS   E .   ? 1.0703 1.1284 0.7166 0.1338  0.0768  0.0338  203 DMS   B C1  
1710 C C1  B DMS   E .   ? 1.0703 1.1284 0.7166 0.1338  0.0768  0.0338  203 DMS   B C1  
1711 C C2  A DMS   E .   ? 1.0688 1.1568 0.7130 0.1413  0.0806  0.0444  203 DMS   B C2  
1712 C C2  B DMS   E .   ? 1.0688 1.1568 0.7130 0.1413  0.0806  0.0444  203 DMS   B C2  
1713 N N1  C A1BXG F .   ? 1.1284 1.2061 0.7958 0.1247  0.0861  0.0476  204 A1BXG B N1  
1714 N N1  D A1BXG F .   ? 1.1284 1.2061 0.7958 0.1247  0.0861  0.0476  204 A1BXG B N1  
1715 N N3  C A1BXG F .   ? 1.1015 1.2085 0.7438 0.1647  0.0797  0.0577  204 A1BXG B N3  
1716 N N3  D A1BXG F .   ? 1.1015 1.2085 0.7438 0.1647  0.0797  0.0577  204 A1BXG B N3  
1717 C C4  C A1BXG F .   ? 1.1390 1.2024 0.7942 0.1304  0.0803  0.0382  204 A1BXG B C4  
1718 C C4  D A1BXG F .   ? 1.1390 1.2024 0.7942 0.1304  0.0803  0.0382  204 A1BXG B C4  
1719 C C5  C A1BXG F .   ? 1.1189 1.1933 0.7720 0.1426  0.0800  0.0452  204 A1BXG B C5  
1720 C C5  D A1BXG F .   ? 1.1189 1.1933 0.7720 0.1426  0.0800  0.0452  204 A1BXG B C5  
1721 C C6  C A1BXG F .   ? 1.1103 1.1725 0.7609 0.1453  0.0767  0.0408  204 A1BXG B C6  
1722 C C6  D A1BXG F .   ? 1.1103 1.1725 0.7609 0.1453  0.0767  0.0408  204 A1BXG B C6  
1723 C C7  C A1BXG F .   ? 1.1018 1.1653 0.7470 0.1543  0.0744  0.0419  204 A1BXG B C7  
1724 C C7  D A1BXG F .   ? 1.1018 1.1653 0.7470 0.1543  0.0744  0.0419  204 A1BXG B C7  
1725 C C8  C A1BXG F .   ? 1.1067 1.1841 0.7491 0.1610  0.0754  0.0473  204 A1BXG B C8  
1726 C C8  D A1BXG F .   ? 1.1067 1.1841 0.7491 0.1610  0.0754  0.0473  204 A1BXG B C8  
1727 C C10 C A1BXG F .   ? 1.0947 1.2155 0.7396 0.1618  0.0827  0.0625  204 A1BXG B C10 
1728 C C10 D A1BXG F .   ? 1.0947 1.2155 0.7396 0.1618  0.0827  0.0625  204 A1BXG B C10 
1729 C C13 C A1BXG F .   ? 1.1075 1.1970 0.7579 0.1490  0.0810  0.0511  204 A1BXG B C13 
1730 C C13 D A1BXG F .   ? 1.1075 1.1970 0.7579 0.1490  0.0810  0.0511  204 A1BXG B C13 
1731 C C1  C A1BXG F .   ? 1.1196 1.1956 0.7976 0.1078  0.0905  0.0466  204 A1BXG B C1  
1732 C C1  D A1BXG F .   ? 1.1196 1.1956 0.7976 0.1078  0.0905  0.0466  204 A1BXG B C1  
1733 C C2  C A1BXG F .   ? 1.1335 1.2065 0.8030 0.1178  0.0869  0.0443  204 A1BXG B C2  
1734 C C2  D A1BXG F .   ? 1.1335 1.2065 0.8030 0.1178  0.0869  0.0443  204 A1BXG B C2  
1735 C C3  C A1BXG F .   ? 1.1220 1.1939 0.7803 0.1330  0.0821  0.0436  204 A1BXG B C3  
1736 C C3  D A1BXG F .   ? 1.1220 1.1939 0.7803 0.1330  0.0821  0.0436  204 A1BXG B C3  
1737 N N2  C A1BXG F .   ? 1.1373 1.2019 0.7996 0.1209  0.0835  0.0387  204 A1BXG B N2  
1738 N N2  D A1BXG F .   ? 1.1373 1.2019 0.7996 0.1209  0.0835  0.0387  204 A1BXG B N2  
1739 C C9  C A1BXG F .   ? 1.1105 1.2019 0.7556 0.1583  0.0787  0.0521  204 A1BXG B C9  
1740 C C9  D A1BXG F .   ? 1.1105 1.2019 0.7556 0.1583  0.0787  0.0521  204 A1BXG B C9  
1741 C C11 C A1BXG F .   ? 1.0931 1.2127 0.7433 0.1526  0.0850  0.0620  204 A1BXG B C11 
1742 C C11 D A1BXG F .   ? 1.0931 1.2127 0.7433 0.1526  0.0850  0.0620  204 A1BXG B C11 
1743 C C12 C A1BXG F .   ? 1.1017 1.2055 0.7545 0.1464  0.0841  0.0562  204 A1BXG B C12 
1744 C C12 D A1BXG F .   ? 1.1017 1.2055 0.7545 0.1464  0.0841  0.0562  204 A1BXG B C12 
1745 C C14 C A1BXG F .   ? 1.1239 1.2027 0.7604 0.1707  0.0728  0.0481  204 A1BXG B C14 
1746 C C14 D A1BXG F .   ? 1.1239 1.2027 0.7604 0.1707  0.0728  0.0481  204 A1BXG B C14 
1747 S S   C DMS   G .   ? 2.7718 2.6853 2.3669 0.0374  0.0150  -0.0234 205 DMS   B S   
1748 S S   D DMS   G .   ? 2.7718 2.6853 2.3669 0.0374  0.0150  -0.0234 205 DMS   B S   
1749 O O   C DMS   G .   ? 2.7343 2.6546 2.3379 0.0254  0.0187  -0.0248 205 DMS   B O   
1750 O O   D DMS   G .   ? 2.7343 2.6546 2.3379 0.0254  0.0187  -0.0248 205 DMS   B O   
1751 C C1  C DMS   G .   ? 2.7540 2.6780 2.3603 0.0447  0.0239  -0.0224 205 DMS   B C1  
1752 C C1  D DMS   G .   ? 2.7540 2.6780 2.3603 0.0447  0.0239  -0.0224 205 DMS   B C1  
1753 C C2  C DMS   G .   ? 2.7724 2.6788 2.3641 0.0390  0.0094  -0.0237 205 DMS   B C2  
1754 C C2  D DMS   G .   ? 2.7724 2.6788 2.3641 0.0390  0.0094  -0.0237 205 DMS   B C2  
# 
