data_7HOL
# 
_entry.id   7HOL 
# 
_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   7HOL         pdb_00007hol 10.2210/pdb7hol/pdb 
WWPDB D_1001407735 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7HOL 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                5067.486  1   ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                         18117.629 1   3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                          78.133    2   ?                           ?    ? ? 
4 non-polymer syn '3-fluoro-N-(2-hydroxy-6-methylphenyl)pyridine-4-carboxamide' 246.237   1   ?                           ?    ? ? 
5 water       nat water                                                         18.015    140 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                          DMS 
4 '3-fluoro-N-(2-hydroxy-6-methylphenyl)pyridine-4-carboxamide' ZUC 
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 
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 
ZUC non-polymer         . '3-fluoro-N-(2-hydroxy-6-methylphenyl)pyridine-4-carboxamide' ? 'C13 H11 F N2 O2' 246.237 
# 
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        ZUC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZUC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS 1   201 202 DMS DMS B . 
D 3 DMS 1   202 203 DMS DMS B . 
E 4 ZUC 1   203 301 ZUC LIG B . 
F 5 HOH 1   101 109 HOH HOH A . 
F 5 HOH 2   102 82  HOH HOH A . 
F 5 HOH 3   103 121 HOH HOH A . 
F 5 HOH 4   104 35  HOH HOH A . 
F 5 HOH 5   105 66  HOH HOH A . 
F 5 HOH 6   106 140 HOH HOH A . 
F 5 HOH 7   107 48  HOH HOH A . 
F 5 HOH 8   108 112 HOH HOH A . 
F 5 HOH 9   109 79  HOH HOH A . 
F 5 HOH 10  110 123 HOH HOH A . 
F 5 HOH 11  111 78  HOH HOH A . 
F 5 HOH 12  112 26  HOH HOH A . 
F 5 HOH 13  113 21  HOH HOH A . 
F 5 HOH 14  114 12  HOH HOH A . 
F 5 HOH 15  115 36  HOH HOH A . 
F 5 HOH 16  116 139 HOH HOH A . 
F 5 HOH 17  117 28  HOH HOH A . 
F 5 HOH 18  118 15  HOH HOH A . 
F 5 HOH 19  119 100 HOH HOH A . 
F 5 HOH 20  120 37  HOH HOH A . 
F 5 HOH 21  121 92  HOH HOH A . 
F 5 HOH 22  122 81  HOH HOH A . 
F 5 HOH 23  123 53  HOH HOH A . 
F 5 HOH 24  124 74  HOH HOH A . 
F 5 HOH 25  125 98  HOH HOH A . 
F 5 HOH 26  126 22  HOH HOH A . 
F 5 HOH 27  127 118 HOH HOH A . 
F 5 HOH 28  128 80  HOH HOH A . 
F 5 HOH 29  129 69  HOH HOH A . 
F 5 HOH 30  130 119 HOH HOH A . 
F 5 HOH 31  131 30  HOH HOH A . 
F 5 HOH 32  132 108 HOH HOH A . 
F 5 HOH 33  133 20  HOH HOH A . 
F 5 HOH 34  134 61  HOH HOH A . 
F 5 HOH 35  135 130 HOH HOH A . 
G 5 HOH 1   301 137 HOH HOH B . 
G 5 HOH 2   302 38  HOH HOH B . 
G 5 HOH 3   303 62  HOH HOH B . 
G 5 HOH 4   304 8   HOH HOH B . 
G 5 HOH 5   305 95  HOH HOH B . 
G 5 HOH 6   306 90  HOH HOH B . 
G 5 HOH 7   307 96  HOH HOH B . 
G 5 HOH 8   308 93  HOH HOH B . 
G 5 HOH 9   309 85  HOH HOH B . 
G 5 HOH 10  310 67  HOH HOH B . 
G 5 HOH 11  311 6   HOH HOH B . 
G 5 HOH 12  312 29  HOH HOH B . 
G 5 HOH 13  313 18  HOH HOH B . 
G 5 HOH 14  314 122 HOH HOH B . 
G 5 HOH 15  315 51  HOH HOH B . 
G 5 HOH 16  316 63  HOH HOH B . 
G 5 HOH 17  317 52  HOH HOH B . 
G 5 HOH 18  318 113 HOH HOH B . 
G 5 HOH 19  319 126 HOH HOH B . 
G 5 HOH 20  320 4   HOH HOH B . 
G 5 HOH 21  321 106 HOH HOH B . 
G 5 HOH 22  322 59  HOH HOH B . 
G 5 HOH 23  323 116 HOH HOH B . 
G 5 HOH 24  324 39  HOH HOH B . 
G 5 HOH 25  325 11  HOH HOH B . 
G 5 HOH 26  326 94  HOH HOH B . 
G 5 HOH 27  327 83  HOH HOH B . 
G 5 HOH 28  328 46  HOH HOH B . 
G 5 HOH 29  329 2   HOH HOH B . 
G 5 HOH 30  330 72  HOH HOH B . 
G 5 HOH 31  331 54  HOH HOH B . 
G 5 HOH 32  332 49  HOH HOH B . 
G 5 HOH 33  333 1   HOH HOH B . 
G 5 HOH 34  334 24  HOH HOH B . 
G 5 HOH 35  335 7   HOH HOH B . 
G 5 HOH 36  336 31  HOH HOH B . 
G 5 HOH 37  337 87  HOH HOH B . 
G 5 HOH 38  338 55  HOH HOH B . 
G 5 HOH 39  339 34  HOH HOH B . 
G 5 HOH 40  340 25  HOH HOH B . 
G 5 HOH 41  341 70  HOH HOH B . 
G 5 HOH 42  342 10  HOH HOH B . 
G 5 HOH 43  343 64  HOH HOH B . 
G 5 HOH 44  344 41  HOH HOH B . 
G 5 HOH 45  345 5   HOH HOH B . 
G 5 HOH 46  346 138 HOH HOH B . 
G 5 HOH 47  347 105 HOH HOH B . 
G 5 HOH 48  348 89  HOH HOH B . 
G 5 HOH 49  349 91  HOH HOH B . 
G 5 HOH 50  350 86  HOH HOH B . 
G 5 HOH 51  351 103 HOH HOH B . 
G 5 HOH 52  352 76  HOH HOH B . 
G 5 HOH 53  353 110 HOH HOH B . 
G 5 HOH 54  354 9   HOH HOH B . 
G 5 HOH 55  355 84  HOH HOH B . 
G 5 HOH 56  356 120 HOH HOH B . 
G 5 HOH 57  357 23  HOH HOH B . 
G 5 HOH 58  358 77  HOH HOH B . 
G 5 HOH 59  359 115 HOH HOH B . 
G 5 HOH 60  360 16  HOH HOH B . 
G 5 HOH 61  361 43  HOH HOH B . 
G 5 HOH 62  362 58  HOH HOH B . 
G 5 HOH 63  363 65  HOH HOH B . 
G 5 HOH 64  364 88  HOH HOH B . 
G 5 HOH 65  365 117 HOH HOH B . 
G 5 HOH 66  366 17  HOH HOH B . 
G 5 HOH 67  367 27  HOH HOH B . 
G 5 HOH 68  368 127 HOH HOH B . 
G 5 HOH 69  369 60  HOH HOH B . 
G 5 HOH 70  370 71  HOH HOH B . 
G 5 HOH 71  371 134 HOH HOH B . 
G 5 HOH 72  372 104 HOH HOH B . 
G 5 HOH 73  373 3   HOH HOH B . 
G 5 HOH 74  374 50  HOH HOH B . 
G 5 HOH 75  375 45  HOH HOH B . 
G 5 HOH 76  376 32  HOH HOH B . 
G 5 HOH 77  377 14  HOH HOH B . 
G 5 HOH 78  378 128 HOH HOH B . 
G 5 HOH 79  379 102 HOH HOH B . 
G 5 HOH 80  380 131 HOH HOH B . 
G 5 HOH 81  381 99  HOH HOH B . 
G 5 HOH 82  382 129 HOH HOH B . 
G 5 HOH 83  383 68  HOH HOH B . 
G 5 HOH 84  384 125 HOH HOH B . 
G 5 HOH 85  385 57  HOH HOH B . 
G 5 HOH 86  386 47  HOH HOH B . 
G 5 HOH 87  387 13  HOH HOH B . 
G 5 HOH 88  388 107 HOH HOH B . 
G 5 HOH 89  389 97  HOH HOH B . 
G 5 HOH 90  390 111 HOH HOH B . 
G 5 HOH 91  391 135 HOH HOH B . 
G 5 HOH 92  392 132 HOH HOH B . 
G 5 HOH 93  393 44  HOH HOH B . 
G 5 HOH 94  394 75  HOH HOH B . 
G 5 HOH 95  395 19  HOH HOH B . 
G 5 HOH 96  396 124 HOH HOH B . 
G 5 HOH 97  397 136 HOH HOH B . 
G 5 HOH 98  398 101 HOH HOH B . 
G 5 HOH 99  399 133 HOH HOH B . 
G 5 HOH 100 400 114 HOH HOH B . 
G 5 HOH 101 401 56  HOH HOH B . 
G 5 HOH 102 402 42  HOH HOH B . 
G 5 HOH 103 403 73  HOH HOH B . 
G 5 HOH 104 404 40  HOH HOH B . 
G 5 HOH 105 405 33  HOH HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (26-JUL-2023)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
'data reduction' XDS     .                      ? 5 
'data reduction' XDS     .                      ? 6 
'data reduction' XDS     .                      ? 7 
'data reduction' XDS     .                      ? 8 
# 
_cell.entry_id           7HOL 
_cell.length_a           42.551 
_cell.length_b           42.551 
_cell.length_c           216.797 
_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                         7HOL 
_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          7HOL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_percent_sol   41.88 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-03-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HOL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.67 
_reflns.d_resolution_high            1.32 
_reflns.number_obs                   47939 
_reflns.percent_possible_obs         98.9 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_netI_over_sigmaI        16.3 
_reflns.pdbx_redundancy              21.8 
_reflns.pdbx_Rrim_I_all              0.066 
_reflns.pdbx_Rpim_I_all              0.013 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     1044637 
_reflns.pdbx_chi_squared             0.46 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.32 
_reflns_shell.d_res_low                   1.34 
_reflns_shell.number_measured_all         20054 
_reflns_shell.number_unique_obs           2030 
_reflns_shell.Rmerge_I_obs                6.208 
_reflns_shell.pdbx_chi_squared            0.16 
_reflns_shell.pdbx_redundancy             9.9 
_reflns_shell.percent_possible_obs        86.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             6.542 
_reflns_shell.pdbx_Rpim_I_all             1.978 
_reflns_shell.pdbx_CC_half                0.319 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HOL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     45958 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.67 
_refine.ls_d_res_high                            1.320 
_refine.ls_percent_reflns_obs                    95.0 
_refine.ls_R_factor_obs                          0.2195 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2186 
_refine.ls_R_factor_R_free                       0.2368 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.070 
_refine.ls_number_reflns_R_free                  2329 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               40.92 
_refine.aniso_B[1][1]                            -4.19620 
_refine.aniso_B[2][2]                            -4.19620 
_refine.aniso_B[3][3]                            8.39230 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.061 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.061 
_refine.pdbx_overall_SU_R_Blow_DPI               0.064 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.063 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HOL 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             140 
_refine_hist.number_atoms_total               1642 
_refine_hist.d_res_high                       1.320 
_refine_hist.d_res_low                        36.67 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  1580 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.13  ? 2.00  2148 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  529  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  284  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1580 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.48  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.94 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  192  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1334 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.32 
_refine_ls_shell.d_res_low                        1.34 
_refine_ls_shell.number_reflns_R_work             873 
_refine_ls_shell.R_factor_R_work                  0.5769 
_refine_ls_shell.percent_reflns_obs               37.11 
_refine_ls_shell.R_factor_R_free                  0.5862 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.11 
_refine_ls_shell.number_reflns_R_free             47 
_refine_ls_shell.number_reflns_all                920 
_refine_ls_shell.R_factor_all                     0.5773 
# 
_struct.entry_id                  7HOL 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with Z1619958679' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOL 
_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 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HOL A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOL 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 7HOL SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOL MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOL MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOL LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4480 ? 
1 MORE         -24  ? 
1 'SSA (A^2)'  9700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 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   ? 
# 
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 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N 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 ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N 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                   7HOL 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU B 30 ? ? -88.76 -158.30 
2 1 CYS B 80 ? ? 75.25  -11.63  
# 
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 -13.5066 -1.4508 -19.2917 0.0484 0.0367  -0.1202 0.1646 0.0782 0.0842 2.3321 2.2291 2.1248 -1.5829 
0.6401 0.4592 0.4608 0.3650 0.3059 -0.4234 -0.3805 -0.2315 0.0195 0.4136 -0.0804 
'X-RAY DIFFRACTION' 2 ? refined -18.3722 1.1905  -15.4359 0.0827 -0.0019 -0.0233 0.1141 0.0243 0.0244 1.1858 0.8401 1.5211 -0.8601 
0.3868 0.0215 0.2906 0.1053 0.0725 -0.1497 -0.2585 0.0428  0.0505 0.1361 -0.0321 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
DMS S    S N N 88  
DMS O    O N N 89  
DMS C1   C N N 90  
DMS C2   C N N 91  
DMS H11  H N N 92  
DMS H12  H N N 93  
DMS H13  H N N 94  
DMS H21  H N N 95  
DMS H22  H N N 96  
DMS H23  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
THR N    N N N 314 
THR CA   C N S 315 
THR C    C N N 316 
THR O    O N N 317 
THR CB   C N R 318 
THR OG1  O N N 319 
THR CG2  C N N 320 
THR OXT  O N N 321 
THR H    H N N 322 
THR H2   H N N 323 
THR HA   H N N 324 
THR HB   H N N 325 
THR HG1  H N N 326 
THR HG21 H N N 327 
THR HG22 H N N 328 
THR HG23 H N N 329 
THR HXT  H N N 330 
TRP N    N N N 331 
TRP CA   C N S 332 
TRP C    C N N 333 
TRP O    O N N 334 
TRP CB   C N N 335 
TRP CG   C Y N 336 
TRP CD1  C Y N 337 
TRP CD2  C Y N 338 
TRP NE1  N Y N 339 
TRP CE2  C Y N 340 
TRP CE3  C Y N 341 
TRP CZ2  C Y N 342 
TRP CZ3  C Y N 343 
TRP CH2  C Y N 344 
TRP OXT  O N N 345 
TRP H    H N N 346 
TRP H2   H N N 347 
TRP HA   H N N 348 
TRP HB2  H N N 349 
TRP HB3  H N N 350 
TRP HD1  H N N 351 
TRP HE1  H N N 352 
TRP HE3  H N N 353 
TRP HZ2  H N N 354 
TRP HZ3  H N N 355 
TRP HH2  H N N 356 
TRP HXT  H N N 357 
TYR N    N N N 358 
TYR CA   C N S 359 
TYR C    C N N 360 
TYR O    O N N 361 
TYR CB   C N N 362 
TYR CG   C Y N 363 
TYR CD1  C Y N 364 
TYR CD2  C Y N 365 
TYR CE1  C Y N 366 
TYR CE2  C Y N 367 
TYR CZ   C Y N 368 
TYR OH   O N N 369 
TYR OXT  O N N 370 
TYR H    H N N 371 
TYR H2   H N N 372 
TYR HA   H N N 373 
TYR HB2  H N N 374 
TYR HB3  H N N 375 
TYR HD1  H N N 376 
TYR HD2  H N N 377 
TYR HE1  H N N 378 
TYR HE2  H N N 379 
TYR HH   H N N 380 
TYR HXT  H N N 381 
VAL N    N N N 382 
VAL CA   C N S 383 
VAL C    C N N 384 
VAL O    O N N 385 
VAL CB   C N N 386 
VAL CG1  C N N 387 
VAL CG2  C N N 388 
VAL OXT  O N N 389 
VAL H    H N N 390 
VAL H2   H N N 391 
VAL HA   H N N 392 
VAL HB   H N N 393 
VAL HG11 H N N 394 
VAL HG12 H N N 395 
VAL HG13 H N N 396 
VAL HG21 H N N 397 
VAL HG22 H N N 398 
VAL HG23 H N N 399 
VAL HXT  H N N 400 
ZUC N1   N N N 401 
ZUC C4   C Y N 402 
ZUC C5   C Y N 403 
ZUC C6   C Y N 404 
ZUC C7   C Y N 405 
ZUC C8   C N N 406 
ZUC C10  C Y N 407 
ZUC C13  C Y N 408 
ZUC C1   C N N 409 
ZUC C2   C Y N 410 
ZUC C3   C Y N 411 
ZUC O1   O N N 412 
ZUC O2   O N N 413 
ZUC C9   C Y N 414 
ZUC C11  C Y N 415 
ZUC N2   N Y N 416 
ZUC C12  C Y N 417 
ZUC F1   F N N 418 
ZUC H1   H N N 419 
ZUC H2   H N N 420 
ZUC H3   H N N 421 
ZUC H4   H N N 422 
ZUC H5   H N N 423 
ZUC H6   H N N 424 
ZUC H7   H N N 425 
ZUC H8   H N N 426 
ZUC H9   H N N 427 
ZUC H10  H N N 428 
ZUC H11  H N N 429 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
ZUC C4  C5   doub Y N 385 
ZUC C4  C3   sing Y N 386 
ZUC C5  C6   sing Y N 387 
ZUC C3  C2   doub Y N 388 
ZUC C6  O1   sing N N 389 
ZUC C6  C7   doub Y N 390 
ZUC C2  C7   sing Y N 391 
ZUC C2  C1   sing N N 392 
ZUC C7  N1   sing N N 393 
ZUC N1  C8   sing N N 394 
ZUC O2  C8   doub N N 395 
ZUC C8  C9   sing N N 396 
ZUC C9  C10  doub Y N 397 
ZUC C9  C13  sing Y N 398 
ZUC C10 C11  sing Y N 399 
ZUC F1  C13  sing N N 400 
ZUC C13 C12  doub Y N 401 
ZUC C11 N2   doub Y N 402 
ZUC C12 N2   sing Y N 403 
ZUC N1  H1   sing N N 404 
ZUC C4  H2   sing N N 405 
ZUC C5  H3   sing N N 406 
ZUC C10 H4   sing N N 407 
ZUC C1  H5   sing N N 408 
ZUC C1  H6   sing N N 409 
ZUC C1  H7   sing N N 410 
ZUC C3  H8   sing N N 411 
ZUC O1  H9   sing N N 412 
ZUC C11 H10  sing N N 413 
ZUC C12 H11  sing N N 414 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002322 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HOL 
_atom_sites.fract_transf_matrix[1][1]   0.023501 
_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]   0.023501 
_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]   0.004613 
_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 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 7   ? -21.037 19.419  -7.553  1.00 49.64 ? 50  ASP A N   1 
ATOM   2    C CA  . ASP A 1 7   ? -22.326 18.749  -7.675  1.00 48.67 ? 50  ASP A CA  1 
ATOM   3    C C   . ASP A 1 7   ? -22.429 17.972  -8.999  1.00 44.96 ? 50  ASP A C   1 
ATOM   4    O O   . ASP A 1 7   ? -22.393 18.539  -10.111 1.00 45.59 ? 50  ASP A O   1 
ATOM   5    C CB  . ASP A 1 7   ? -23.487 19.696  -7.502  1.00 52.97 ? 50  ASP A CB  1 
ATOM   6    C CG  . ASP A 1 7   ? -24.768 18.971  -7.169  1.00 60.29 ? 50  ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 7   ? -24.853 18.393  -6.059  1.00 62.17 ? 50  ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 7   ? -25.689 18.978  -8.016  1.00 63.43 ? 50  ASP A OD2 1 
ATOM   9    N N   . MET A 1 8   ? -22.575 16.678  -8.863  1.00 39.84 ? 51  MET A N   1 
ATOM   10   C CA  . MET A 1 8   ? -22.574 15.796  -10.017 1.00 35.77 ? 51  MET A CA  1 
ATOM   11   C C   . MET A 1 8   ? -23.959 15.511  -10.568 1.00 34.57 ? 51  MET A C   1 
ATOM   12   O O   . MET A 1 8   ? -24.938 15.436  -9.814  1.00 35.03 ? 51  MET A O   1 
ATOM   13   C CB  . MET A 1 8   ? -21.821 14.507  -9.670  1.00 34.85 ? 51  MET A CB  1 
ATOM   14   C CG  . MET A 1 8   ? -20.352 14.703  -9.586  1.00 36.01 ? 51  MET A CG  1 
ATOM   15   S SD  . MET A 1 8   ? -19.575 13.100  -9.152  1.00 38.90 ? 51  MET A SD  1 
ATOM   16   C CE  . MET A 1 8   ? -17.965 13.563  -9.123  1.00 41.86 ? 51  MET A CE  1 
ATOM   17   N N   . TYR A 1 9   ? -24.063 15.436  -11.895 1.00 32.14 ? 52  TYR A N   1 
ATOM   18   C CA  . TYR A 1 9   ? -25.342 15.188  -12.545 1.00 31.62 ? 52  TYR A CA  1 
ATOM   19   C C   . TYR A 1 9   ? -25.175 14.202  -13.690 1.00 31.58 ? 52  TYR A C   1 
ATOM   20   O O   . TYR A 1 9   ? -24.068 14.065  -14.230 1.00 32.31 ? 52  TYR A O   1 
ATOM   21   C CB  . TYR A 1 9   ? -26.021 16.486  -13.025 1.00 31.85 ? 52  TYR A CB  1 
ATOM   22   C CG  . TYR A 1 9   ? -25.236 17.241  -14.065 1.00 34.06 ? 52  TYR A CG  1 
ATOM   23   C CD1 . TYR A 1 9   ? -24.274 18.171  -13.695 1.00 35.82 ? 52  TYR A CD1 1 
ATOM   24   C CD2 . TYR A 1 9   ? -25.553 17.135  -15.416 1.00 35.99 ? 52  TYR A CD2 1 
ATOM   25   C CE1 . TYR A 1 9   ? -23.576 18.906  -14.646 1.00 38.26 ? 52  TYR A CE1 1 
ATOM   26   C CE2 . TYR A 1 9   ? -24.874 17.885  -16.378 1.00 38.04 ? 52  TYR A CE2 1 
ATOM   27   C CZ  . TYR A 1 9   ? -23.871 18.754  -15.987 1.00 39.61 ? 52  TYR A CZ  1 
ATOM   28   O OH  . TYR A 1 9   ? -23.134 19.458  -16.926 1.00 41.23 ? 52  TYR A OH  1 
ATOM   29   N N   . ILE A 1 10  ? -26.260 13.518  -14.073 1.00 30.32 ? 53  ILE A N   1 
ATOM   30   C CA  . ILE A 1 10  ? -26.171 12.526  -15.158 1.00 30.02 ? 53  ILE A CA  1 
ATOM   31   C C   . ILE A 1 10  ? -26.976 12.975  -16.381 1.00 31.05 ? 53  ILE A C   1 
ATOM   32   O O   . ILE A 1 10  ? -27.960 13.730  -16.257 1.00 31.18 ? 53  ILE A O   1 
ATOM   33   C CB  . ILE A 1 10  ? -26.620 11.143  -14.670 1.00 29.99 ? 53  ILE A CB  1 
ATOM   34   C CG1 . ILE A 1 10  ? -28.161 11.093  -14.303 1.00 31.26 ? 53  ILE A CG1 1 
ATOM   35   C CG2 . ILE A 1 10  ? -25.744 10.734  -13.455 1.00 29.78 ? 53  ILE A CG2 1 
ATOM   36   C CD1 . ILE A 1 10  ? -28.567 9.632   -13.917 1.00 32.32 ? 53  ILE A CD1 1 
ATOM   37   N N   . GLU A 1 11  ? -26.515 12.543  -17.572 1.00 31.51 ? 54  GLU A N   1 
ATOM   38   C CA  . GLU A 1 11  ? -27.164 12.918  -18.841 1.00 31.75 ? 54  GLU A CA  1 
ATOM   39   C C   . GLU A 1 11  ? -27.215 11.691  -19.721 1.00 31.53 ? 54  GLU A C   1 
ATOM   40   O O   . GLU A 1 11  ? -26.163 11.041  -19.908 1.00 31.68 ? 54  GLU A O   1 
ATOM   41   C CB  . GLU A 1 11  ? -26.298 13.934  -19.626 1.00 34.85 ? 54  GLU A CB  1 
ATOM   42   C CG  . GLU A 1 11  ? -26.125 15.309  -19.041 1.00 43.51 ? 54  GLU A CG  1 
ATOM   43   C CD  . GLU A 1 11  ? -25.366 16.225  -19.992 1.00 50.08 ? 54  GLU A CD  1 
ATOM   44   O OE1 . GLU A 1 11  ? -24.533 15.734  -20.800 1.00 52.01 ? 54  GLU A OE1 1 
ATOM   45   O OE2 . GLU A 1 11  ? -25.596 17.448  -19.906 1.00 55.78 ? 54  GLU A OE2 1 
ATOM   46   N N   . ARG A 1 12  ? -28.384 11.358  -20.308 1.00 32.25 ? 55  ARG A N   1 
ATOM   47   C CA  . ARG A 1 12  ? -28.459 10.126  -21.117 1.00 34.06 ? 55  ARG A CA  1 
ATOM   48   C C   . ARG A 1 12  ? -27.557 10.211  -22.334 1.00 33.14 ? 55  ARG A C   1 
ATOM   49   O O   . ARG A 1 12  ? -27.515 11.290  -22.957 1.00 35.30 ? 55  ARG A O   1 
ATOM   50   C CB  . ARG A 1 12  ? -29.902 9.803   -21.544 1.00 38.03 ? 55  ARG A CB  1 
ATOM   51   C CG  . ARG A 1 12  ? -30.092 8.303   -21.830 1.00 41.45 ? 55  ARG A CG  1 
ATOM   52   C CD  . ARG A 1 12  ? -31.571 7.952   -21.955 1.00 46.78 ? 55  ARG A CD  1 
ATOM   53   N NE  . ARG A 1 12  ? -31.759 6.518   -22.192 1.00 47.02 ? 55  ARG A NE  1 
ATOM   54   C CZ  . ARG A 1 12  ? -31.895 5.983   -23.404 1.00 46.52 ? 55  ARG A CZ  1 
ATOM   55   N NH1 . ARG A 1 12  ? -31.915 6.759   -24.483 1.00 49.39 ? 55  ARG A NH1 1 
ATOM   56   N NH2 . ARG A 1 12  ? -32.012 4.668   -23.547 1.00 44.00 ? 55  ARG A NH2 1 
ATOM   57   N N   . ALA A 1 13  ? -26.838 9.096   -22.666 1.00 32.28 ? 56  ALA A N   1 
ATOM   58   C CA  . ALA A 1 13  ? -25.982 9.075   -23.851 1.00 33.67 ? 56  ALA A CA  1 
ATOM   59   C C   . ALA A 1 13  ? -26.375 8.007   -24.875 1.00 35.65 ? 56  ALA A C   1 
ATOM   60   O O   . ALA A 1 13  ? -25.875 8.087   -25.996 1.00 37.56 ? 56  ALA A O   1 
ATOM   61   C CB  . ALA A 1 13  ? -24.521 8.881   -23.464 1.00 36.04 ? 56  ALA A CB  1 
ATOM   62   N N   . GLY A 1 14  ? -27.249 7.071   -24.528 1.00 34.58 ? 57  GLY A N   1 
ATOM   63   C CA  . GLY A 1 14  ? -27.676 6.061   -25.481 1.00 35.73 ? 57  GLY A CA  1 
ATOM   64   C C   . GLY A 1 14  ? -28.332 4.830   -24.908 1.00 35.94 ? 57  GLY A C   1 
ATOM   65   O O   . GLY A 1 14  ? -28.466 4.702   -23.684 1.00 35.78 ? 57  GLY A O   1 
ATOM   66   N N   . ASP A 1 15  ? -28.769 3.931   -25.786 1.00 36.71 ? 58  ASP A N   1 
ATOM   67   C CA  . ASP A 1 15  ? -29.289 2.622   -25.415 1.00 37.90 ? 58  ASP A CA  1 
ATOM   68   C C   . ASP A 1 15  ? -28.098 1.653   -25.285 1.00 39.52 ? 58  ASP A C   1 
ATOM   69   O O   . ASP A 1 15  ? -27.068 1.804   -25.971 1.00 41.01 ? 58  ASP A O   1 
ATOM   70   C CB  . ASP A 1 15  ? -30.216 2.039   -26.512 1.00 40.42 ? 58  ASP A CB  1 
ATOM   71   C CG  . ASP A 1 15  ? -31.592 2.696   -26.660 1.00 45.92 ? 58  ASP A CG  1 
ATOM   72   O OD1 . ASP A 1 15  ? -31.833 3.710   -26.011 1.00 44.52 ? 58  ASP A OD1 1 
ATOM   73   O OD2 . ASP A 1 15  ? -32.394 2.239   -27.537 1.00 51.40 ? 58  ASP A OD2 1 
ATOM   74   N N   . ILE A 1 16  ? -28.299 0.572   -24.530 1.00 39.48 ? 59  ILE A N   1 
ATOM   75   C CA  . ILE A 1 16  ? -27.267 -0.460  -24.438 1.00 38.89 ? 59  ILE A CA  1 
ATOM   76   C C   . ILE A 1 16  ? -27.675 -1.607  -25.350 1.00 41.05 ? 59  ILE A C   1 
ATOM   77   O O   . ILE A 1 16  ? -28.599 -2.363  -25.038 1.00 41.49 ? 59  ILE A O   1 
ATOM   78   C CB  . ILE A 1 16  ? -27.083 -0.873  -23.006 1.00 39.20 ? 59  ILE A CB  1 
ATOM   79   C CG1 . ILE A 1 16  ? -26.651 0.354   -22.179 1.00 39.92 ? 59  ILE A CG1 1 
ATOM   80   C CG2 . ILE A 1 16  ? -26.081 -2.015  -22.906 1.00 40.26 ? 59  ILE A CG2 1 
ATOM   81   C CD1 . ILE A 1 16  ? -26.588 0.103   -20.698 1.00 40.37 ? 59  ILE A CD1 1 
ATOM   82   N N   . THR A 1 17  ? -27.027 -1.674  -26.501 1.00 41.84 ? 60  THR A N   1 
ATOM   83   C CA  . THR A 1 17  ? -27.333 -2.671  -27.517 1.00 44.47 ? 60  THR A CA  1 
ATOM   84   C C   . THR A 1 17  ? -26.046 -3.098  -28.212 1.00 47.77 ? 60  THR A C   1 
ATOM   85   O O   . THR A 1 17  ? -25.175 -2.255  -28.442 1.00 49.61 ? 60  THR A O   1 
ATOM   86   C CB  . THR A 1 17  ? -28.313 -2.048  -28.570 1.00 46.86 ? 60  THR A CB  1 
ATOM   87   O OG1 . THR A 1 17  ? -29.538 -1.667  -27.924 1.00 47.21 ? 60  THR A OG1 1 
ATOM   88   C CG2 . THR A 1 17  ? -28.676 -2.979  -29.649 1.00 49.99 ? 60  THR A CG2 1 
ATOM   89   N N   . TRP A 1 18  ? -25.968 -4.377  -28.633 1.00 47.48 ? 61  TRP A N   1 
ATOM   90   C CA  . TRP A 1 18  ? -24.832 -4.882  -29.416 1.00 49.39 ? 61  TRP A CA  1 
ATOM   91   C C   . TRP A 1 18  ? -24.946 -4.322  -30.849 1.00 51.15 ? 61  TRP A C   1 
ATOM   92   O O   . TRP A 1 18  ? -26.059 -4.274  -31.380 1.00 53.95 ? 61  TRP A O   1 
ATOM   93   C CB  . TRP A 1 18  ? -24.910 -6.405  -29.473 1.00 49.16 ? 61  TRP A CB  1 
ATOM   94   C CG  . TRP A 1 18  ? -23.833 -7.041  -30.294 1.00 49.36 ? 61  TRP A CG  1 
ATOM   95   C CD1 . TRP A 1 18  ? -23.880 -7.339  -31.632 1.00 50.38 ? 61  TRP A CD1 1 
ATOM   96   C CD2 . TRP A 1 18  ? -22.592 -7.563  -29.809 1.00 49.39 ? 61  TRP A CD2 1 
ATOM   97   N NE1 . TRP A 1 18  ? -22.721 -7.977  -32.012 1.00 50.88 ? 61  TRP A NE1 1 
ATOM   98   C CE2 . TRP A 1 18  ? -21.909 -8.119  -30.914 1.00 49.92 ? 61  TRP A CE2 1 
ATOM   99   C CE3 . TRP A 1 18  ? -21.949 -7.536  -28.568 1.00 50.00 ? 61  TRP A CE3 1 
ATOM   100  C CZ2 . TRP A 1 18  ? -20.649 -8.700  -30.788 1.00 49.99 ? 61  TRP A CZ2 1 
ATOM   101  C CZ3 . TRP A 1 18  ? -20.709 -8.114  -28.447 1.00 49.97 ? 61  TRP A CZ3 1 
ATOM   102  C CH2 . TRP A 1 18  ? -20.067 -8.684  -29.549 1.00 50.08 ? 61  TRP A CH2 1 
ATOM   103  N N   . GLU A 1 19  ? -23.840 -3.833  -31.458 1.00 50.44 ? 62  GLU A N   1 
ATOM   104  C CA  . GLU A 1 19  ? -23.929 -3.256  -32.809 1.00 52.52 ? 62  GLU A CA  1 
ATOM   105  C C   . GLU A 1 19  ? -23.312 -4.220  -33.760 1.00 55.04 ? 62  GLU A C   1 
ATOM   106  O O   . GLU A 1 19  ? -22.131 -4.495  -33.628 1.00 53.29 ? 62  GLU A O   1 
ATOM   107  C CB  . GLU A 1 19  ? -23.195 -1.897  -32.925 1.00 55.01 ? 62  GLU A CB  1 
ATOM   108  C CG  . GLU A 1 19  ? -23.227 -1.332  -34.350 1.00 62.33 ? 62  GLU A CG  1 
ATOM   109  C CD  . GLU A 1 19  ? -22.281 -0.199  -34.714 1.00 71.29 ? 62  GLU A CD  1 
ATOM   110  O OE1 . GLU A 1 19  ? -21.602 0.334   -33.807 1.00 74.30 ? 62  GLU A OE1 1 
ATOM   111  O OE2 . GLU A 1 19  ? -22.233 0.165   -35.913 1.00 74.05 ? 62  GLU A OE2 1 
ATOM   112  N N   . LYS A 1 20  ? -24.067 -4.672  -34.773 1.00 59.14 ? 63  LYS A N   1 
ATOM   113  C CA  . LYS A 1 20  ? -23.503 -5.606  -35.753 1.00 63.86 ? 63  LYS A CA  1 
ATOM   114  C C   . LYS A 1 20  ? -22.469 -4.876  -36.627 1.00 66.20 ? 63  LYS A C   1 
ATOM   115  O O   . LYS A 1 20  ? -22.636 -3.691  -36.886 1.00 65.68 ? 63  LYS A O   1 
ATOM   116  C CB  . LYS A 1 20  ? -24.622 -6.220  -36.614 1.00 68.04 ? 63  LYS A CB  1 
ATOM   117  C CG  . LYS A 1 20  ? -25.188 -7.511  -36.000 1.00 75.64 ? 63  LYS A CG  1 
ATOM   118  C CD  . LYS A 1 20  ? -25.770 -8.434  -37.083 1.00 82.86 ? 63  LYS A CD  1 
ATOM   119  C CE  . LYS A 1 20  ? -27.178 -8.895  -36.769 1.00 87.27 ? 63  LYS A CE  1 
ATOM   120  N NZ  . LYS A 1 20  ? -28.127 -7.754  -36.690 1.00 89.16 ? 63  LYS A NZ  1 
ATOM   121  N N   . ASP A 1 21  ? -21.340 -5.527  -36.946 1.00 68.98 ? 64  ASP A N   1 
ATOM   122  C CA  . ASP A 1 21  ? -20.285 -4.861  -37.734 1.00 71.08 ? 64  ASP A CA  1 
ATOM   123  C C   . ASP A 1 21  ? -19.802 -3.540  -37.077 1.00 69.54 ? 64  ASP A C   1 
ATOM   124  O O   . ASP A 1 21  ? -19.735 -2.498  -37.709 1.00 69.99 ? 64  ASP A O   1 
ATOM   125  C CB  . ASP A 1 21  ? -20.700 -4.657  -39.196 1.00 76.24 ? 64  ASP A CB  1 
ATOM   126  C CG  . ASP A 1 21  ? -20.986 -5.966  -39.895 1.00 84.34 ? 64  ASP A CG  1 
ATOM   127  O OD1 . ASP A 1 21  ? -20.102 -6.863  -39.866 1.00 87.25 ? 64  ASP A OD1 1 
ATOM   128  O OD2 . ASP A 1 21  ? -22.098 -6.107  -40.459 1.00 86.78 ? 64  ASP A OD2 1 
ATOM   129  N N   . ALA A 1 22  ? -19.512 -3.598  -35.770 1.00 66.26 ? 65  ALA A N   1 
ATOM   130  C CA  . ALA A 1 22  ? -18.926 -2.471  -35.060 1.00 63.19 ? 65  ALA A CA  1 
ATOM   131  C C   . ALA A 1 22  ? -17.420 -2.495  -35.432 1.00 61.57 ? 65  ALA A C   1 
ATOM   132  O O   . ALA A 1 22  ? -16.915 -3.534  -35.869 1.00 61.75 ? 65  ALA A O   1 
ATOM   133  C CB  . ALA A 1 22  ? -19.047 -2.724  -33.552 1.00 62.29 ? 65  ALA A CB  1 
ATOM   134  N N   . GLU A 1 23  ? -16.665 -1.410  -35.146 1.00 60.55 ? 66  GLU A N   1 
ATOM   135  C CA  . GLU A 1 23  ? -15.208 -1.423  -35.361 1.00 60.75 ? 66  GLU A CA  1 
ATOM   136  C C   . GLU A 1 23  ? -14.595 -2.483  -34.423 1.00 57.98 ? 66  GLU A C   1 
ATOM   137  O O   . GLU A 1 23  ? -14.985 -2.537  -33.264 1.00 54.65 ? 66  GLU A O   1 
ATOM   138  C CB  . GLU A 1 23  ? -14.605 -0.060  -35.008 1.00 66.84 ? 66  GLU A CB  1 
ATOM   139  C CG  . GLU A 1 23  ? -13.105 0.012   -35.253 1.00 77.27 ? 66  GLU A CG  1 
ATOM   140  C CD  . GLU A 1 23  ? -12.387 1.019   -34.372 1.00 89.86 ? 66  GLU A CD  1 
ATOM   141  O OE1 . GLU A 1 23  ? -12.998 2.062   -34.037 1.00 92.35 ? 66  GLU A OE1 1 
ATOM   142  O OE2 . GLU A 1 23  ? -11.212 0.763   -34.018 1.00 93.69 ? 66  GLU A OE2 1 
ATOM   143  N N   . VAL A 1 24  ? -13.772 -3.384  -34.936 1.00 58.31 ? 67  VAL A N   1 
ATOM   144  C CA  . VAL A 1 24  ? -13.146 -4.455  -34.141 1.00 59.00 ? 67  VAL A CA  1 
ATOM   145  C C   . VAL A 1 24  ? -11.657 -4.159  -33.887 1.00 58.95 ? 67  VAL A C   1 
ATOM   146  O O   . VAL A 1 24  ? -10.886 -4.105  -34.839 1.00 61.45 ? 67  VAL A O   1 
ATOM   147  C CB  . VAL A 1 24  ? -13.316 -5.833  -34.827 1.00 61.05 ? 67  VAL A CB  1 
ATOM   148  C CG1 . VAL A 1 24  ? -12.783 -6.949  -33.965 1.00 61.54 ? 67  VAL A CG1 1 
ATOM   149  C CG2 . VAL A 1 24  ? -14.760 -6.098  -35.224 1.00 62.27 ? 67  VAL A CG2 1 
ATOM   150  N N   . THR A 1 25  ? -11.233 -4.015  -32.594 1.00 57.12 ? 68  THR A N   1 
ATOM   151  C CA  . THR A 1 25  ? -9.838  -3.697  -32.281 1.00 57.03 ? 68  THR A CA  1 
ATOM   152  C C   . THR A 1 25  ? -9.403  -4.177  -30.871 1.00 55.52 ? 68  THR A C   1 
ATOM   153  O O   . THR A 1 25  ? -10.226 -4.671  -30.108 1.00 54.75 ? 68  THR A O   1 
ATOM   154  C CB  . THR A 1 25  ? -9.555  -2.194  -32.494 1.00 59.92 ? 68  THR A CB  1 
ATOM   155  O OG1 . THR A 1 25  ? -8.130  -2.065  -32.643 1.00 62.57 ? 68  THR A OG1 1 
ATOM   156  C CG2 . THR A 1 25  ? -10.054 -1.348  -31.326 1.00 60.42 ? 68  THR A CG2 1 
ATOM   157  N N   . GLY A 1 26  ? -8.127  -4.027  -30.538 1.00 55.17 ? 69  GLY A N   1 
ATOM   158  C CA  . GLY A 1 26  ? -7.615  -4.413  -29.233 1.00 55.36 ? 69  GLY A CA  1 
ATOM   159  C C   . GLY A 1 26  ? -7.037  -5.810  -29.217 1.00 55.88 ? 69  GLY A C   1 
ATOM   160  O O   . GLY A 1 26  ? -7.526  -6.691  -29.926 1.00 56.80 ? 69  GLY A O   1 
ATOM   161  N N   . ASN A 1 27  ? -5.982  -6.013  -28.415 1.00 53.88 ? 70  ASN A N   1 
ATOM   162  C CA  . ASN A 1 27  ? -5.389  -7.332  -28.279 1.00 53.36 ? 70  ASN A CA  1 
ATOM   163  C C   . ASN A 1 27  ? -5.973  -8.024  -27.018 1.00 50.94 ? 70  ASN A C   1 
ATOM   164  O O   . ASN A 1 27  ? -6.900  -7.479  -26.388 1.00 49.81 ? 70  ASN A O   1 
ATOM   165  C CB  . ASN A 1 27  ? -3.836  -7.293  -28.370 1.00 55.82 ? 70  ASN A CB  1 
ATOM   166  C CG  . ASN A 1 27  ? -3.170  -6.621  -27.190 1.00 60.23 ? 70  ASN A CG  1 
ATOM   167  O OD1 . ASN A 1 27  ? -3.598  -5.560  -26.726 1.00 61.31 ? 70  ASN A OD1 1 
ATOM   168  N ND2 . ASN A 1 27  ? -2.077  -7.207  -26.706 1.00 61.92 ? 70  ASN A ND2 1 
ATOM   169  N N   . SER A 1 28  ? -5.490  -9.235  -26.669 1.00 49.57 ? 71  SER A N   1 
ATOM   170  C CA  . SER A 1 28  ? -6.045  -10.030 -25.570 1.00 48.68 ? 71  SER A CA  1 
ATOM   171  C C   . SER A 1 28  ? -4.947  -10.505 -24.635 1.00 47.87 ? 71  SER A C   1 
ATOM   172  O O   . SER A 1 28  ? -4.620  -11.699 -24.580 1.00 48.82 ? 71  SER A O   1 
ATOM   173  C CB  . SER A 1 28  ? -6.838  -11.208 -26.136 1.00 49.98 ? 71  SER A CB  1 
ATOM   174  O OG  . SER A 1 28  ? -7.568  -10.819 -27.296 1.00 52.52 ? 71  SER A OG  1 
ATOM   175  N N   . PRO A 1 29  ? -4.339  -9.571  -23.883 1.00 46.95 ? 72  PRO A N   1 
ATOM   176  C CA  . PRO A 1 29  ? -3.184  -9.951  -23.069 1.00 46.91 ? 72  PRO A CA  1 
ATOM   177  C C   . PRO A 1 29  ? -3.556  -10.777 -21.858 1.00 45.79 ? 72  PRO A C   1 
ATOM   178  O O   . PRO A 1 29  ? -4.590  -10.506 -21.239 1.00 44.69 ? 72  PRO A O   1 
ATOM   179  C CB  . PRO A 1 29  ? -2.585  -8.601  -22.656 1.00 48.64 ? 72  PRO A CB  1 
ATOM   180  C CG  . PRO A 1 29  ? -3.779  -7.650  -22.633 1.00 48.66 ? 72  PRO A CG  1 
ATOM   181  C CD  . PRO A 1 29  ? -4.612  -8.110  -23.816 1.00 46.45 ? 72  PRO A CD  1 
ATOM   182  N N   . ARG A 1 30  ? -2.688  -11.741 -21.471 1.00 45.00 ? 73  ARG A N   1 
ATOM   183  C CA  . ARG A 1 30  ? -2.860  -12.557 -20.268 1.00 47.05 ? 73  ARG A CA  1 
ATOM   184  C C   . ARG A 1 30  ? -1.824  -12.050 -19.263 1.00 46.75 ? 73  ARG A C   1 
ATOM   185  O O   . ARG A 1 30  ? -0.623  -12.227 -19.462 1.00 47.85 ? 73  ARG A O   1 
ATOM   186  C CB  . ARG A 1 30  ? -2.684  -14.067 -20.576 1.00 50.28 ? 73  ARG A CB  1 
ATOM   187  C CG  . ARG A 1 30  ? -3.844  -14.616 -21.433 1.00 56.34 ? 73  ARG A CG  1 
ATOM   188  C CD  . ARG A 1 30  ? -3.928  -16.139 -21.479 1.00 62.54 ? 73  ARG A CD  1 
ATOM   189  N NE  . ARG A 1 30  ? -4.718  -16.611 -22.622 1.00 66.88 ? 73  ARG A NE  1 
ATOM   190  C CZ  . ARG A 1 30  ? -5.675  -17.534 -22.548 1.00 68.85 ? 73  ARG A CZ  1 
ATOM   191  N NH1 . ARG A 1 30  ? -5.965  -18.109 -21.385 1.00 71.32 ? 73  ARG A NH1 1 
ATOM   192  N NH2 . ARG A 1 30  ? -6.341  -17.899 -23.641 1.00 64.54 ? 73  ARG A NH2 1 
ATOM   193  N N   . LEU A 1 31  ? -2.294  -11.392 -18.178 1.00 44.34 ? 74  LEU A N   1 
ATOM   194  C CA  . LEU A 1 31  ? -1.438  -10.712 -17.212 1.00 44.25 ? 74  LEU A CA  1 
ATOM   195  C C   . LEU A 1 31  ? -1.608  -11.208 -15.795 1.00 43.59 ? 74  LEU A C   1 
ATOM   196  O O   . LEU A 1 31  ? -2.743  -11.357 -15.336 1.00 44.19 ? 74  LEU A O   1 
ATOM   197  C CB  . LEU A 1 31  ? -1.790  -9.194  -17.234 1.00 44.56 ? 74  LEU A CB  1 
ATOM   198  C CG  . LEU A 1 31  ? -1.642  -8.496  -18.596 1.00 46.58 ? 74  LEU A CG  1 
ATOM   199  C CD1 . LEU A 1 31  ? -2.341  -7.117  -18.609 1.00 46.80 ? 74  LEU A CD1 1 
ATOM   200  C CD2 . LEU A 1 31  ? -0.166  -8.386  -19.004 1.00 48.09 ? 74  LEU A CD2 1 
ATOM   201  N N   . ASP A 1 32  ? -0.507  -11.323 -15.033 1.00 43.42 ? 75  ASP A N   1 
ATOM   202  C CA  . ASP A 1 32  ? -0.610  -11.684 -13.624 1.00 43.15 ? 75  ASP A CA  1 
ATOM   203  C C   . ASP A 1 32  ? -0.746  -10.376 -12.865 1.00 41.62 ? 75  ASP A C   1 
ATOM   204  O O   . ASP A 1 32  ? 0.105   -9.485  -13.012 1.00 42.14 ? 75  ASP A O   1 
ATOM   205  C CB  . ASP A 1 32  ? 0.663   -12.418 -13.135 1.00 46.16 ? 75  ASP A CB  1 
ATOM   206  C CG  . ASP A 1 32  ? 0.831   -13.818 -13.715 1.00 56.21 ? 75  ASP A CG  1 
ATOM   207  O OD1 . ASP A 1 32  ? -0.184  -14.407 -14.158 1.00 57.37 ? 75  ASP A OD1 1 
ATOM   208  O OD2 . ASP A 1 32  ? 1.980   -14.326 -13.725 1.00 59.89 ? 75  ASP A OD2 1 
ATOM   209  N N   . VAL A 1 33  ? -1.828  -10.232 -12.093 1.00 39.67 ? 76  VAL A N   1 
ATOM   210  C CA  . VAL A 1 33  ? -2.053  -8.980  -11.403 1.00 38.51 ? 76  VAL A CA  1 
ATOM   211  C C   . VAL A 1 33  ? -2.418  -9.200  -9.942  1.00 38.52 ? 76  VAL A C   1 
ATOM   212  O O   . VAL A 1 33  ? -2.826  -10.295 -9.532  1.00 39.39 ? 76  VAL A O   1 
ATOM   213  C CB  . VAL A 1 33  ? -3.126  -8.093  -12.144 1.00 39.08 ? 76  VAL A CB  1 
ATOM   214  C CG1 . VAL A 1 33  ? -2.817  -7.925  -13.626 1.00 39.96 ? 76  VAL A CG1 1 
ATOM   215  C CG2 . VAL A 1 33  ? -4.513  -8.652  -11.942 1.00 38.62 ? 76  VAL A CG2 1 
ATOM   216  N N   . ALA A 1 34  ? -2.260  -8.135  -9.153  1.00 36.67 ? 77  ALA A N   1 
ATOM   217  C CA  . ALA A 1 34  ? -2.598  -8.106  -7.742  1.00 35.88 ? 77  ALA A CA  1 
ATOM   218  C C   . ALA A 1 34  ? -3.623  -6.970  -7.523  1.00 35.04 ? 77  ALA A C   1 
ATOM   219  O O   . ALA A 1 34  ? -3.576  -5.971  -8.237  1.00 35.32 ? 77  ALA A O   1 
ATOM   220  C CB  . ALA A 1 34  ? -1.339  -7.846  -6.911  1.00 35.73 ? 77  ALA A CB  1 
ATOM   221  N N   . LEU A 1 35  ? -4.549  -7.140  -6.576  1.00 34.41 ? 78  LEU A N   1 
ATOM   222  C CA  . LEU A 1 35  ? -5.574  -6.117  -6.315  1.00 34.81 ? 78  LEU A CA  1 
ATOM   223  C C   . LEU A 1 35  ? -5.440  -5.749  -4.850  1.00 35.09 ? 78  LEU A C   1 
ATOM   224  O O   . LEU A 1 35  ? -5.510  -6.647  -4.005  1.00 36.22 ? 78  LEU A O   1 
ATOM   225  C CB  . LEU A 1 35  ? -6.974  -6.693  -6.599  1.00 34.46 ? 78  LEU A CB  1 
ATOM   226  C CG  . LEU A 1 35  ? -8.129  -5.783  -6.203  1.00 35.62 ? 78  LEU A CG  1 
ATOM   227  C CD1 . LEU A 1 35  ? -8.113  -4.508  -7.030  1.00 35.05 ? 78  LEU A CD1 1 
ATOM   228  C CD2 . LEU A 1 35  ? -9.468  -6.492  -6.383  1.00 37.05 ? 78  LEU A CD2 1 
ATOM   229  N N   . ASP A 1 36  ? -5.164  -4.469  -4.550  1.00 33.51 ? 79  ASP A N   1 
ATOM   230  C CA  . ASP A 1 36  ? -4.948  -4.080  -3.162  1.00 33.41 ? 79  ASP A CA  1 
ATOM   231  C C   . ASP A 1 36  ? -6.252  -3.628  -2.478  1.00 33.12 ? 79  ASP A C   1 
ATOM   232  O O   . ASP A 1 36  ? -7.312  -3.566  -3.117  1.00 32.90 ? 79  ASP A O   1 
ATOM   233  C CB  . ASP A 1 36  ? -3.791  -3.066  -3.027  1.00 34.84 ? 79  ASP A CB  1 
ATOM   234  C CG  . ASP A 1 36  ? -4.012  -1.655  -3.536  1.00 37.00 ? 79  ASP A CG  1 
ATOM   235  O OD1 . ASP A 1 36  ? -5.177  -1.286  -3.798  1.00 36.53 ? 79  ASP A OD1 1 
ATOM   236  O OD2 . ASP A 1 36  ? -3.022  -0.892  -3.615  1.00 43.09 ? 79  ASP A OD2 1 
ATOM   237  N N   . GLU A 1 37  ? -6.184  -3.361  -1.183  1.00 34.02 ? 80  GLU A N   1 
ATOM   238  C CA  . GLU A 1 37  ? -7.349  -2.959  -0.423  1.00 33.70 ? 80  GLU A CA  1 
ATOM   239  C C   . GLU A 1 37  ? -7.959  -1.643  -0.922  1.00 33.80 ? 80  GLU A C   1 
ATOM   240  O O   . GLU A 1 37  ? -9.159  -1.433  -0.751  1.00 34.55 ? 80  GLU A O   1 
ATOM   241  C CB  . GLU A 1 37  ? -6.930  -2.851  1.041   1.00 36.19 ? 80  GLU A CB  1 
ATOM   242  C CG  . GLU A 1 37  ? -8.119  -2.696  1.964   1.00 39.46 ? 80  GLU A CG  1 
ATOM   243  C CD  . GLU A 1 37  ? -7.768  -2.792  3.435   1.00 44.99 ? 80  GLU A CD  1 
ATOM   244  O OE1 . GLU A 1 37  ? -7.536  -1.734  4.059   1.00 44.15 ? 80  GLU A OE1 1 
ATOM   245  O OE2 . GLU A 1 37  ? -7.680  -3.931  3.950   1.00 49.31 ? 80  GLU A OE2 1 
ATOM   246  N N   . SER A 1 38  ? -7.178  -0.788  -1.612  1.00 32.79 ? 81  SER A N   1 
ATOM   247  C CA  . SER A 1 38  ? -7.715  0.472   -2.138  1.00 33.85 ? 81  SER A CA  1 
ATOM   248  C C   . SER A 1 38  ? -8.338  0.296   -3.543  1.00 32.87 ? 81  SER A C   1 
ATOM   249  O O   . SER A 1 38  ? -8.743  1.282   -4.133  1.00 33.74 ? 81  SER A O   1 
ATOM   250  C CB  . SER A 1 38  ? -6.625  1.534   -2.192  1.00 37.30 ? 81  SER A CB  1 
ATOM   251  O OG  . SER A 1 38  ? -6.119  1.762   -0.888  1.00 42.90 ? 81  SER A OG  1 
ATOM   252  N N   . GLY A 1 39  ? -8.438  -0.940  -4.044  1.00 31.16 ? 82  GLY A N   1 
ATOM   253  C CA  . GLY A 1 39  ? -9.064  -1.179  -5.343  1.00 30.99 ? 82  GLY A CA  1 
ATOM   254  C C   . GLY A 1 39  ? -8.140  -0.886  -6.495  1.00 31.65 ? 82  GLY A C   1 
ATOM   255  O O   . GLY A 1 39  ? -8.615  -0.789  -7.625  1.00 31.52 ? 82  GLY A O   1 
ATOM   256  N N   . ASP A 1 40  ? -6.824  -0.804  -6.249  1.00 31.36 ? 83  ASP A N   1 
ATOM   257  C CA  . ASP A 1 40  ? -5.882  -0.556  -7.344  1.00 33.17 ? 83  ASP A CA  1 
ATOM   258  C C   . ASP A 1 40  ? -5.271  -1.880  -7.812  1.00 33.18 ? 83  ASP A C   1 
ATOM   259  O O   . ASP A 1 40  ? -4.762  -2.663  -6.994  1.00 33.40 ? 83  ASP A O   1 
ATOM   260  C CB  . ASP A 1 40  ? -4.761  0.405   -6.890  1.00 38.82 ? 83  ASP A CB  1 
ATOM   261  C CG  . ASP A 1 40  ? -5.294  1.770   -6.492  1.00 47.78 ? 83  ASP A CG  1 
ATOM   262  O OD1 . ASP A 1 40  ? -6.304  2.203   -7.076  1.00 51.39 ? 83  ASP A OD1 1 
ATOM   263  O OD2 . ASP A 1 40  ? -4.733  2.378   -5.563  1.00 51.56 ? 83  ASP A OD2 1 
ATOM   264  N N   . PHE A 1 41  ? -5.228  -2.087  -9.139  1.00 32.44 ? 84  PHE A N   1 
ATOM   265  C CA  . PHE A 1 41  ? -4.558  -3.252  -9.698  1.00 33.90 ? 84  PHE A CA  1 
ATOM   266  C C   . PHE A 1 41  ? -3.082  -2.921  -9.939  1.00 36.46 ? 84  PHE A C   1 
ATOM   267  O O   . PHE A 1 41  ? -2.731  -1.791  -10.298 1.00 37.45 ? 84  PHE A O   1 
ATOM   268  C CB  . PHE A 1 41  ? -5.217  -3.662  -11.034 1.00 32.50 ? 84  PHE A CB  1 
ATOM   269  C CG  . PHE A 1 41  ? -6.539  -4.388  -10.902 1.00 31.76 ? 84  PHE A CG  1 
ATOM   270  C CD1 . PHE A 1 41  ? -6.579  -5.734  -10.544 1.00 32.51 ? 84  PHE A CD1 1 
ATOM   271  C CD2 . PHE A 1 41  ? -7.739  -3.759  -11.249 1.00 31.97 ? 84  PHE A CD2 1 
ATOM   272  C CE1 . PHE A 1 41  ? -7.801  -6.407  -10.450 1.00 33.85 ? 84  PHE A CE1 1 
ATOM   273  C CE2 . PHE A 1 41  ? -8.956  -4.431  -11.145 1.00 32.50 ? 84  PHE A CE2 1 
ATOM   274  C CZ  . PHE A 1 41  ? -8.985  -5.754  -10.782 1.00 33.50 ? 84  PHE A CZ  1 
ATOM   275  N N   . SER A 1 42  ? -2.223  -3.922  -9.789  1.00 37.63 ? 85  SER A N   1 
ATOM   276  C CA  . SER A 1 42  ? -0.808  -3.746  -10.119 1.00 39.54 ? 85  SER A CA  1 
ATOM   277  C C   . SER A 1 42  ? -0.307  -4.976  -10.854 1.00 41.64 ? 85  SER A C   1 
ATOM   278  O O   . SER A 1 42  ? -0.824  -6.071  -10.636 1.00 40.34 ? 85  SER A O   1 
ATOM   279  C CB  . SER A 1 42  ? 0.023   -3.494  -8.864  1.00 42.63 ? 85  SER A CB  1 
ATOM   280  O OG  . SER A 1 42  ? -0.088  -4.570  -7.943  1.00 44.44 ? 85  SER A OG  1 
ATOM   281  N N   . LEU A 1 43  ? 0.739   -4.817  -11.694 1.00 44.40 ? 86  LEU A N   1 
ATOM   282  C CA  . LEU A 1 43  ? 1.302   -5.977  -12.383 1.00 47.66 ? 86  LEU A CA  1 
ATOM   283  C C   . LEU A 1 43  ? 2.241   -6.747  -11.450 1.00 50.15 ? 86  LEU A C   1 
ATOM   284  O O   . LEU A 1 43  ? 3.061   -6.141  -10.765 1.00 50.04 ? 86  LEU A O   1 
ATOM   285  C CB  . LEU A 1 43  ? 2.126   -5.550  -13.597 1.00 49.12 ? 86  LEU A CB  1 
ATOM   286  C CG  . LEU A 1 43  ? 1.384   -5.102  -14.836 1.00 52.33 ? 86  LEU A CG  1 
ATOM   287  C CD1 . LEU A 1 43  ? 2.388   -4.787  -15.931 1.00 53.32 ? 86  LEU A CD1 1 
ATOM   288  C CD2 . LEU A 1 43  ? 0.464   -6.193  -15.348 1.00 53.54 ? 86  LEU A CD2 1 
ATOM   289  N N   . VAL A 1 44  ? 2.143   -8.070  -11.446 1.00 52.48 ? 87  VAL A N   1 
ATOM   290  C CA  . VAL A 1 44  ? 3.050   -8.935  -10.686 1.00 55.41 ? 87  VAL A CA  1 
ATOM   291  C C   . VAL A 1 44  ? 4.013   -9.529  -11.724 1.00 59.59 ? 87  VAL A C   1 
ATOM   292  O O   . VAL A 1 44  ? 3.546   -10.048 -12.745 1.00 60.08 ? 87  VAL A O   1 
ATOM   293  C CB  . VAL A 1 44  ? 2.271   -10.079 -10.003 1.00 55.84 ? 87  VAL A CB  1 
ATOM   294  C CG1 . VAL A 1 44  ? 3.225   -11.070 -9.326  1.00 56.71 ? 87  VAL A CG1 1 
ATOM   295  C CG2 . VAL A 1 44  ? 1.247   -9.532  -9.020  1.00 55.83 ? 87  VAL A CG2 1 
ATOM   296  N N   . GLU A 1 45  ? 5.324   -9.440  -11.507 1.00 62.69 ? 88  GLU A N   1 
ATOM   297  C CA  . GLU A 1 45  ? 6.284   -10.004 -12.481 1.00 65.46 ? 88  GLU A CA  1 
ATOM   298  C C   . GLU A 1 45  ? 7.136   -11.136 -11.916 1.00 66.73 ? 88  GLU A C   1 
ATOM   299  O O   . GLU A 1 45  ? 7.282   -11.272 -10.699 1.00 67.56 ? 88  GLU A O   1 
ATOM   300  C CB  . GLU A 1 45  ? 7.159   -8.907  -13.103 1.00 69.61 ? 88  GLU A CB  1 
ATOM   301  C CG  . GLU A 1 45  ? 6.353   -7.909  -13.929 1.00 76.52 ? 88  GLU A CG  1 
ATOM   302  C CD  . GLU A 1 45  ? 6.270   -8.214  -15.414 1.00 85.44 ? 88  GLU A CD  1 
ATOM   303  O OE1 . GLU A 1 45  ? 6.722   -9.309  -15.827 1.00 87.49 ? 88  GLU A OE1 1 
ATOM   304  O OE2 . GLU A 1 45  ? 5.763   -7.352  -16.167 1.00 88.28 ? 88  GLU A OE2 1 
ATOM   305  N N   . GLY B 2 7   ? -36.516 12.740  -12.235 1.00 53.55 ? 16  GLY B N   1 
ATOM   306  C CA  . GLY B 2 7   ? -35.447 12.672  -13.233 1.00 53.48 ? 16  GLY B CA  1 
ATOM   307  C C   . GLY B 2 7   ? -35.636 11.578  -14.270 1.00 52.81 ? 16  GLY B C   1 
ATOM   308  O O   . GLY B 2 7   ? -36.637 10.849  -14.234 1.00 53.71 ? 16  GLY B O   1 
ATOM   309  N N   . GLU B 2 8   ? -34.698 11.472  -15.228 1.00 50.21 ? 17  GLU B N   1 
ATOM   310  C CA  . GLU B 2 8   ? -34.780 10.428  -16.249 1.00 48.55 ? 17  GLU B CA  1 
ATOM   311  C C   . GLU B 2 8   ? -34.378 9.098   -15.629 1.00 46.70 ? 17  GLU B C   1 
ATOM   312  O O   . GLU B 2 8   ? -33.348 8.977   -14.963 1.00 46.95 ? 17  GLU B O   1 
ATOM   313  C CB  . GLU B 2 8   ? -33.908 10.747  -17.481 1.00 50.27 ? 17  GLU B CB  1 
ATOM   314  C CG  . GLU B 2 8   ? -34.069 9.747   -18.617 1.00 52.87 ? 17  GLU B CG  1 
ATOM   315  C CD  . GLU B 2 8   ? -33.578 10.246  -19.962 1.00 57.36 ? 17  GLU B CD  1 
ATOM   316  O OE1 . GLU B 2 8   ? -32.636 11.069  -19.972 1.00 59.08 ? 17  GLU B OE1 1 
ATOM   317  O OE2 . GLU B 2 8   ? -34.165 9.860   -21.002 1.00 57.79 ? 17  GLU B OE2 1 
ATOM   318  N N   . THR B 2 9   ? -35.241 8.119   -15.771 1.00 45.72 ? 18  THR B N   1 
ATOM   319  C CA  . THR B 2 9   ? -35.005 6.775   -15.228 1.00 45.74 ? 18  THR B CA  1 
ATOM   320  C C   . THR B 2 9   ? -35.002 5.714   -16.292 1.00 44.64 ? 18  THR B C   1 
ATOM   321  O O   . THR B 2 9   ? -34.872 4.535   -15.977 1.00 45.46 ? 18  THR B O   1 
ATOM   322  C CB  . THR B 2 9   ? -36.087 6.463   -14.179 1.00 48.38 ? 18  THR B CB  1 
ATOM   323  O OG1 . THR B 2 9   ? -37.358 6.439   -14.845 1.00 49.64 ? 18  THR B OG1 1 
ATOM   324  C CG2 . THR B 2 9   ? -36.126 7.505   -13.081 1.00 49.66 ? 18  THR B CG2 1 
ATOM   325  N N   . THR B 2 10  ? -35.084 6.101   -17.581 1.00 43.33 ? 19  THR B N   1 
ATOM   326  C CA  . THR B 2 10  ? -35.076 5.160   -18.674 1.00 42.19 ? 19  THR B CA  1 
ATOM   327  C C   . THR B 2 10  ? -33.784 4.374   -18.667 1.00 39.80 ? 19  THR B C   1 
ATOM   328  O O   . THR B 2 10  ? -32.704 4.951   -18.464 1.00 40.38 ? 19  THR B O   1 
ATOM   329  C CB  . THR B 2 10  ? -35.211 5.931   -20.004 1.00 43.81 ? 19  THR B CB  1 
ATOM   330  O OG1 . THR B 2 10  ? -36.317 6.839   -19.906 1.00 46.69 ? 19  THR B OG1 1 
ATOM   331  C CG2 . THR B 2 10  ? -35.427 5.016   -21.196 1.00 44.51 ? 19  THR B CG2 1 
ATOM   332  N N   . ASP B 2 11  ? -33.858 3.066   -18.875 1.00 38.34 ? 20  ASP B N   1 
ATOM   333  C CA  . ASP B 2 11  ? -32.685 2.217   -19.007 1.00 37.98 ? 20  ASP B CA  1 
ATOM   334  C C   . ASP B 2 11  ? -31.738 2.817   -20.074 1.00 37.44 ? 20  ASP B C   1 
ATOM   335  O O   . ASP B 2 11  ? -32.230 3.428   -21.043 1.00 39.12 ? 20  ASP B O   1 
ATOM   336  C CB  . ASP B 2 11  ? -33.075 0.797   -19.475 1.00 40.42 ? 20  ASP B CB  1 
ATOM   337  C CG  . ASP B 2 11  ? -33.542 -0.145  -18.385 1.00 46.06 ? 20  ASP B CG  1 
ATOM   338  O OD1 . ASP B 2 11  ? -33.841 0.344   -17.269 1.00 42.67 ? 20  ASP B OD1 1 
ATOM   339  O OD2 . ASP B 2 11  ? -33.585 -1.387  -18.644 1.00 49.72 ? 20  ASP B OD2 1 
ATOM   340  N N   . GLY B 2 12  ? -30.457 2.725   -19.866 1.00 33.44 ? 21  GLY B N   1 
ATOM   341  C CA  . GLY B 2 12  ? -29.481 3.179   -20.854 1.00 33.02 ? 21  GLY B CA  1 
ATOM   342  C C   . GLY B 2 12  ? -28.146 3.550   -20.250 1.00 31.52 ? 21  GLY B C   1 
ATOM   343  O O   . GLY B 2 12  ? -27.909 3.300   -19.048 1.00 29.71 ? 21  GLY B O   1 
ATOM   344  N N   . VAL B 2 13  ? -27.222 4.054   -21.068 1.00 29.89 ? 22  VAL B N   1 
ATOM   345  C CA  . VAL B 2 13  ? -25.904 4.517   -20.641 1.00 28.68 ? 22  VAL B CA  1 
ATOM   346  C C   . VAL B 2 13  ? -25.940 6.049   -20.483 1.00 28.32 ? 22  VAL B C   1 
ATOM   347  O O   . VAL B 2 13  ? -26.617 6.751   -21.286 1.00 30.10 ? 22  VAL B O   1 
ATOM   348  C CB  . VAL B 2 13  ? -24.807 4.052   -21.573 1.00 29.62 ? 22  VAL B CB  1 
ATOM   349  C CG1 . VAL B 2 13  ? -25.005 4.650   -22.997 1.00 30.35 ? 22  VAL B CG1 1 
ATOM   350  C CG2 . VAL B 2 13  ? -23.412 4.345   -21.038 1.00 31.87 ? 22  VAL B CG2 1 
ATOM   351  N N   . TYR B 2 14  ? -25.328 6.574   -19.415 1.00 27.19 ? 23  TYR B N   1 
ATOM   352  C CA  . TYR B 2 14  ? -25.361 7.993   -19.080 1.00 27.13 ? 23  TYR B CA  1 
ATOM   353  C C   . TYR B 2 14  ? -23.970 8.534   -18.795 1.00 27.99 ? 23  TYR B C   1 
ATOM   354  O O   . TYR B 2 14  ? -23.131 7.851   -18.204 1.00 29.07 ? 23  TYR B O   1 
ATOM   355  C CB  . TYR B 2 14  ? -26.176 8.198   -17.754 1.00 27.20 ? 23  TYR B CB  1 
ATOM   356  C CG  . TYR B 2 14  ? -27.687 8.013   -17.868 1.00 27.89 ? 23  TYR B CG  1 
ATOM   357  C CD1 . TYR B 2 14  ? -28.238 6.757   -18.148 1.00 29.04 ? 23  TYR B CD1 1 
ATOM   358  C CD2 . TYR B 2 14  ? -28.555 9.080   -17.670 1.00 30.86 ? 23  TYR B CD2 1 
ATOM   359  C CE1 . TYR B 2 14  ? -29.612 6.582   -18.256 1.00 31.08 ? 23  TYR B CE1 1 
ATOM   360  C CE2 . TYR B 2 14  ? -29.933 8.921   -17.804 1.00 33.32 ? 23  TYR B CE2 1 
ATOM   361  C CZ  . TYR B 2 14  ? -30.454 7.664   -18.081 1.00 34.63 ? 23  TYR B CZ  1 
ATOM   362  O OH  . TYR B 2 14  ? -31.823 7.507   -18.178 1.00 39.23 ? 23  TYR B OH  1 
ATOM   363  N N   . ARG B 2 15  ? -23.751 9.805   -19.096 1.00 28.10 ? 24  ARG B N   1 
ATOM   364  C CA  . ARG B 2 15  ? -22.518 10.505  -18.710 1.00 28.32 ? 24  ARG B CA  1 
ATOM   365  C C   . ARG B 2 15  ? -22.708 11.009  -17.283 1.00 28.34 ? 24  ARG B C   1 
ATOM   366  O O   . ARG B 2 15  ? -23.806 11.403  -16.898 1.00 28.21 ? 24  ARG B O   1 
ATOM   367  C CB  . ARG B 2 15  ? -22.305 11.772  -19.575 1.00 30.48 ? 24  ARG B CB  1 
ATOM   368  C CG  . ARG B 2 15  ? -22.303 11.459  -21.063 1.00 32.78 ? 24  ARG B CG  1 
ATOM   369  C CD  . ARG B 2 15  ? -22.110 12.765  -21.864 1.00 32.60 ? 24  ARG B CD  1 
ATOM   370  N NE  . ARG B 2 15  ? -22.364 12.520  -23.290 1.00 33.46 ? 24  ARG B NE  1 
ATOM   371  C CZ  . ARG B 2 15  ? -21.459 12.080  -24.171 1.00 35.61 ? 24  ARG B CZ  1 
ATOM   372  N NH1 . ARG B 2 15  ? -20.189 11.903  -23.808 1.00 31.89 ? 24  ARG B NH1 1 
ATOM   373  N NH2 . ARG B 2 15  ? -21.814 11.827  -25.428 1.00 36.62 ? 24  ARG B NH2 1 
ATOM   374  N N   . VAL B 2 16  ? -21.646 11.026  -16.485 1.00 28.15 ? 25  VAL B N   1 
ATOM   375  C CA  . VAL B 2 16  ? -21.606 11.608  -15.145 1.00 28.34 ? 25  VAL B CA  1 
ATOM   376  C C   . VAL B 2 16  ? -20.762 12.878  -15.242 1.00 29.07 ? 25  VAL B C   1 
ATOM   377  O O   . VAL B 2 16  ? -19.570 12.808  -15.636 1.00 29.93 ? 25  VAL B O   1 
ATOM   378  C CB  . VAL B 2 16  ? -20.968 10.640  -14.135 1.00 28.63 ? 25  VAL B CB  1 
ATOM   379  C CG1 . VAL B 2 16  ? -20.968 11.317  -12.762 1.00 28.92 ? 25  VAL B CG1 1 
ATOM   380  C CG2 . VAL B 2 16  ? -21.735 9.290   -14.118 1.00 28.46 ? 25  VAL B CG2 1 
ATOM   381  N N   . MET B 2 17  ? -21.389 14.030  -15.005 1.00 30.43 ? 26  MET B N   1 
ATOM   382  C CA  . MET B 2 17  ? -20.763 15.334  -15.188 1.00 31.56 ? 26  MET B CA  1 
ATOM   383  C C   . MET B 2 17  ? -20.605 16.103  -13.902 1.00 33.37 ? 26  MET B C   1 
ATOM   384  O O   . MET B 2 17  ? -21.398 15.912  -12.986 1.00 33.40 ? 26  MET B O   1 
ATOM   385  C CB  . MET B 2 17  ? -21.686 16.176  -16.094 1.00 33.28 ? 26  MET B CB  1 
ATOM   386  C CG  . MET B 2 17  ? -22.098 15.462  -17.388 1.00 33.96 ? 26  MET B CG  1 
ATOM   387  S SD  . MET B 2 17  ? -20.774 15.215  -18.567 1.00 33.13 ? 26  MET B SD  1 
ATOM   388  C CE  . MET B 2 17  ? -20.349 16.913  -18.938 1.00 34.85 ? 26  MET B CE  1 
ATOM   389  N N   . THR B 2 18  ? -19.658 17.070  -13.879 1.00 34.08 ? 27  THR B N   1 
ATOM   390  C CA  . THR B 2 18  ? -19.583 17.993  -12.730 1.00 36.33 ? 27  THR B CA  1 
ATOM   391  C C   . THR B 2 18  ? -19.393 19.420  -13.235 1.00 38.14 ? 27  THR B C   1 
ATOM   392  O O   . THR B 2 18  ? -18.828 19.628  -14.309 1.00 36.87 ? 27  THR B O   1 
ATOM   393  C CB  . THR B 2 18  ? -18.432 17.639  -11.740 1.00 38.84 ? 27  THR B CB  1 
ATOM   394  O OG1 . THR B 2 18  ? -18.463 18.642  -10.684 1.00 41.56 ? 27  THR B OG1 1 
ATOM   395  C CG2 . THR B 2 18  ? -17.053 17.689  -12.399 1.00 40.03 ? 27  THR B CG2 1 
ATOM   396  N N   . ARG B 2 19  ? -19.856 20.417  -12.452 1.00 41.23 ? 28  ARG B N   1 
ATOM   397  C CA  . ARG B 2 19  ? -19.576 21.814  -12.781 1.00 45.06 ? 28  ARG B CA  1 
ATOM   398  C C   . ARG B 2 19  ? -18.574 22.453  -11.799 1.00 47.10 ? 28  ARG B C   1 
ATOM   399  O O   . ARG B 2 19  ? -18.395 23.670  -11.840 1.00 47.49 ? 28  ARG B O   1 
ATOM   400  C CB  . ARG B 2 19  ? -20.854 22.649  -12.870 1.00 48.82 ? 28  ARG B CB  1 
ATOM   401  C CG  . ARG B 2 19  ? -21.787 22.097  -13.932 1.00 56.04 ? 28  ARG B CG  1 
ATOM   402  C CD  . ARG B 2 19  ? -22.347 23.159  -14.826 1.00 62.10 ? 28  ARG B CD  1 
ATOM   403  N NE  . ARG B 2 19  ? -23.261 22.604  -15.824 1.00 67.38 ? 28  ARG B NE  1 
ATOM   404  C CZ  . ARG B 2 19  ? -24.562 22.411  -15.623 1.00 72.26 ? 28  ARG B CZ  1 
ATOM   405  N NH1 . ARG B 2 19  ? -25.114 22.707  -14.449 1.00 73.23 ? 28  ARG B NH1 1 
ATOM   406  N NH2 . ARG B 2 19  ? -25.320 21.907  -16.589 1.00 72.75 ? 28  ARG B NH2 1 
ATOM   407  N N   . ARG B 2 20  ? -17.916 21.649  -10.942 1.00 49.02 ? 29  ARG B N   1 
ATOM   408  C CA  . ARG B 2 20  ? -16.955 22.127  -9.949  1.00 51.99 ? 29  ARG B CA  1 
ATOM   409  C C   . ARG B 2 20  ? -15.685 22.661  -10.603 1.00 53.63 ? 29  ARG B C   1 
ATOM   410  O O   . ARG B 2 20  ? -15.152 23.662  -10.136 1.00 54.99 ? 29  ARG B O   1 
ATOM   411  C CB  . ARG B 2 20  ? -16.630 21.007  -8.937  1.00 54.90 ? 29  ARG B CB  1 
ATOM   412  C CG  . ARG B 2 20  ? -15.537 21.362  -7.927  1.00 61.30 ? 29  ARG B CG  1 
ATOM   413  C CD  . ARG B 2 20  ? -15.220 20.206  -6.989  1.00 66.73 ? 29  ARG B CD  1 
ATOM   414  N NE  . ARG B 2 20  ? -14.674 19.037  -7.685  1.00 71.00 ? 29  ARG B NE  1 
ATOM   415  C CZ  . ARG B 2 20  ? -13.378 18.740  -7.752  1.00 74.62 ? 29  ARG B CZ  1 
ATOM   416  N NH1 . ARG B 2 20  ? -12.475 19.538  -7.191  1.00 74.66 ? 29  ARG B NH1 1 
ATOM   417  N NH2 . ARG B 2 20  ? -12.973 17.652  -8.398  1.00 75.05 ? 29  ARG B NH2 1 
ATOM   418  N N   . LEU B 2 21  ? -15.201 22.007  -11.682 1.00 53.07 ? 30  LEU B N   1 
ATOM   419  C CA  . LEU B 2 21  ? -13.981 22.439  -12.377 1.00 52.91 ? 30  LEU B CA  1 
ATOM   420  C C   . LEU B 2 21  ? -14.327 23.478  -13.493 1.00 51.68 ? 30  LEU B C   1 
ATOM   421  O O   . LEU B 2 21  ? -15.381 24.127  -13.431 1.00 52.12 ? 30  LEU B O   1 
ATOM   422  C CB  . LEU B 2 21  ? -13.240 21.195  -12.960 1.00 53.66 ? 30  LEU B CB  1 
ATOM   423  C CG  . LEU B 2 21  ? -12.456 20.208  -12.053 1.00 56.06 ? 30  LEU B CG  1 
ATOM   424  C CD1 . LEU B 2 21  ? -12.277 20.697  -10.596 1.00 57.11 ? 30  LEU B CD1 1 
ATOM   425  C CD2 . LEU B 2 21  ? -13.041 18.823  -12.128 1.00 56.12 ? 30  LEU B CD2 1 
ATOM   426  N N   . LEU B 2 22  ? -13.448 23.651  -14.505 1.00 49.81 ? 31  LEU B N   1 
ATOM   427  C CA  . LEU B 2 22  ? -13.712 24.577  -15.592 1.00 48.17 ? 31  LEU B CA  1 
ATOM   428  C C   . LEU B 2 22  ? -14.863 24.029  -16.446 1.00 46.75 ? 31  LEU B C   1 
ATOM   429  O O   . LEU B 2 22  ? -14.885 22.821  -16.722 1.00 46.92 ? 31  LEU B O   1 
ATOM   430  C CB  . LEU B 2 22  ? -12.441 24.732  -16.430 1.00 48.35 ? 31  LEU B CB  1 
ATOM   431  C CG  . LEU B 2 22  ? -12.463 25.812  -17.474 1.00 48.68 ? 31  LEU B CG  1 
ATOM   432  C CD1 . LEU B 2 22  ? -12.504 27.226  -16.842 1.00 47.89 ? 31  LEU B CD1 1 
ATOM   433  C CD2 . LEU B 2 22  ? -11.245 25.698  -18.384 1.00 48.98 ? 31  LEU B CD2 1 
ATOM   434  N N   . GLY B 2 23  ? -15.833 24.890  -16.786 1.00 44.40 ? 32  GLY B N   1 
ATOM   435  C CA  . GLY B 2 23  ? -17.014 24.538  -17.572 1.00 42.96 ? 32  GLY B CA  1 
ATOM   436  C C   . GLY B 2 23  ? -17.756 23.312  -17.040 1.00 41.81 ? 32  GLY B C   1 
ATOM   437  O O   . GLY B 2 23  ? -17.976 23.183  -15.837 1.00 40.79 ? 32  GLY B O   1 
ATOM   438  N N   . SER B 2 24  ? -18.165 22.419  -17.940 1.00 41.03 ? 33  SER B N   1 
ATOM   439  C CA  . SER B 2 24  ? -18.850 21.182  -17.550 1.00 40.87 ? 33  SER B CA  1 
ATOM   440  C C   . SER B 2 24  ? -17.927 20.074  -17.931 1.00 38.76 ? 33  SER B C   1 
ATOM   441  O O   . SER B 2 24  ? -17.516 19.986  -19.090 1.00 40.35 ? 33  SER B O   1 
ATOM   442  C CB  . SER B 2 24  ? -20.175 21.022  -18.291 1.00 44.88 ? 33  SER B CB  1 
ATOM   443  O OG  . SER B 2 24  ? -21.080 22.061  -17.937 1.00 48.59 ? 33  SER B OG  1 
ATOM   444  N N   . THR B 2 25  ? -17.517 19.273  -16.951 1.00 36.44 ? 34  THR B N   1 
ATOM   445  C CA  . THR B 2 25  ? -16.526 18.244  -17.161 1.00 35.57 ? 34  THR B CA  1 
ATOM   446  C C   . THR B 2 25  ? -17.105 16.850  -16.947 1.00 33.98 ? 34  THR B C   1 
ATOM   447  O O   . THR B 2 25  ? -17.816 16.624  -15.962 1.00 32.67 ? 34  THR B O   1 
ATOM   448  C CB  . THR B 2 25  ? -15.310 18.512  -16.225 1.00 38.46 ? 34  THR B CB  1 
ATOM   449  O OG1 . THR B 2 25  ? -14.817 19.865  -16.419 1.00 39.74 ? 34  THR B OG1 1 
ATOM   450  C CG2 . THR B 2 25  ? -14.158 17.522  -16.455 1.00 39.44 ? 34  THR B CG2 1 
ATOM   451  N N   . GLN B 2 26  ? -16.797 15.921  -17.878 1.00 31.72 ? 35  GLN B N   1 
ATOM   452  C CA  . GLN B 2 26  ? -17.283 14.551  -17.711 1.00 31.74 ? 35  GLN B CA  1 
ATOM   453  C C   . GLN B 2 26  ? -16.292 13.790  -16.856 1.00 32.84 ? 35  GLN B C   1 
ATOM   454  O O   . GLN B 2 26  ? -15.133 13.608  -17.276 1.00 34.48 ? 35  GLN B O   1 
ATOM   455  C CB  . GLN B 2 26  ? -17.496 13.863  -19.081 1.00 31.84 ? 35  GLN B CB  1 
ATOM   456  C CG  . GLN B 2 26  ? -18.012 12.405  -18.934 1.00 29.63 ? 35  GLN B CG  1 
ATOM   457  C CD  . GLN B 2 26  ? -18.290 11.803  -20.294 1.00 30.06 ? 35  GLN B CD  1 
ATOM   458  O OE1 . GLN B 2 26  ? -18.889 12.463  -21.175 1.00 31.25 ? 35  GLN B OE1 1 
ATOM   459  N NE2 . GLN B 2 26  ? -17.889 10.545  -20.485 1.00 30.19 ? 35  GLN B NE2 1 
ATOM   460  N N   . VAL B 2 27  ? -16.729 13.375  -15.680 1.00 31.93 ? 36  VAL B N   1 
ATOM   461  C CA  . VAL B 2 27  ? -15.836 12.594  -14.796 1.00 31.62 ? 36  VAL B CA  1 
ATOM   462  C C   . VAL B 2 27  ? -16.002 11.058  -14.988 1.00 30.64 ? 36  VAL B C   1 
ATOM   463  O O   . VAL B 2 27  ? -15.137 10.286  -14.536 1.00 31.47 ? 36  VAL B O   1 
ATOM   464  C CB  . VAL B 2 27  ? -15.974 13.022  -13.335 1.00 32.80 ? 36  VAL B CB  1 
ATOM   465  C CG1 . VAL B 2 27  ? -15.562 14.493  -13.177 1.00 34.85 ? 36  VAL B CG1 1 
ATOM   466  C CG2 . VAL B 2 27  ? -17.399 12.816  -12.862 1.00 33.94 ? 36  VAL B CG2 1 
ATOM   467  N N   . GLY B 2 28  ? -17.093 10.621  -15.604 1.00 28.88 ? 37  GLY B N   1 
ATOM   468  C CA  . GLY B 2 28  ? -17.272 9.192   -15.882 1.00 27.78 ? 37  GLY B CA  1 
ATOM   469  C C   . GLY B 2 28  ? -18.579 8.901   -16.580 1.00 29.20 ? 37  GLY B C   1 
ATOM   470  O O   . GLY B 2 28  ? -19.173 9.816   -17.179 1.00 28.28 ? 37  GLY B O   1 
ATOM   471  N N   . VAL B 2 29  ? -19.023 7.636   -16.502 1.00 26.63 ? 38  VAL B N   1 
ATOM   472  C CA  . VAL B 2 29  ? -20.151 7.059   -17.210 1.00 27.91 ? 38  VAL B CA  1 
ATOM   473  C C   . VAL B 2 29  ? -20.801 6.013   -16.303 1.00 27.36 ? 38  VAL B C   1 
ATOM   474  O O   . VAL B 2 29  ? -20.158 5.479   -15.382 1.00 25.80 ? 38  VAL B O   1 
ATOM   475  C CB  . VAL B 2 29  ? -19.614 6.343   -18.502 1.00 28.94 ? 38  VAL B CB  1 
ATOM   476  C CG1 . VAL B 2 29  ? -20.738 5.673   -19.304 1.00 28.17 ? 38  VAL B CG1 1 
ATOM   477  C CG2 . VAL B 2 29  ? -18.848 7.332   -19.380 1.00 29.74 ? 38  VAL B CG2 1 
ATOM   478  N N   . GLY B 2 30  ? -22.071 5.738   -16.548 1.00 27.40 ? 39  GLY B N   1 
ATOM   479  C CA  . GLY B 2 30  ? -22.769 4.693   -15.801 1.00 27.89 ? 39  GLY B CA  1 
ATOM   480  C C   . GLY B 2 30  ? -23.951 4.084   -16.528 1.00 27.62 ? 39  GLY B C   1 
ATOM   481  O O   . GLY B 2 30  ? -24.331 4.529   -17.623 1.00 28.03 ? 39  GLY B O   1 
ATOM   482  N N   . VAL B 2 31  ? -24.529 3.038   -15.941 1.00 25.83 ? 40  VAL B N   1 
ATOM   483  C CA  . VAL B 2 31  ? -25.650 2.281   -16.483 1.00 26.11 ? 40  VAL B CA  1 
ATOM   484  C C   . VAL B 2 31  ? -26.886 2.383   -15.643 1.00 26.86 ? 40  VAL B C   1 
ATOM   485  O O   . VAL B 2 31  ? -26.831 2.048   -14.439 1.00 25.85 ? 40  VAL B O   1 
ATOM   486  C CB  . VAL B 2 31  ? -25.263 0.779   -16.615 1.00 28.78 ? 40  VAL B CB  1 
ATOM   487  C CG1 . VAL B 2 31  ? -26.467 -0.073  -17.045 1.00 30.19 ? 40  VAL B CG1 1 
ATOM   488  C CG2 . VAL B 2 31  ? -24.079 0.618   -17.554 1.00 28.45 ? 40  VAL B CG2 1 
ATOM   489  N N   . MET B 2 32  ? -28.036 2.739   -16.242 1.00 26.17 ? 41  MET B N   1 
ATOM   490  C CA  . MET B 2 32  ? -29.335 2.741   -15.611 1.00 27.24 ? 41  MET B CA  1 
ATOM   491  C C   . MET B 2 32  ? -30.015 1.418   -16.012 1.00 28.60 ? 41  MET B C   1 
ATOM   492  O O   . MET B 2 32  ? -30.184 1.136   -17.203 1.00 29.02 ? 41  MET B O   1 
ATOM   493  C CB  . MET B 2 32  ? -30.165 3.988   -15.990 1.00 28.41 ? 41  MET B CB  1 
ATOM   494  C CG  . MET B 2 32  ? -31.425 4.163   -15.182 1.00 28.62 ? 41  MET B CG  1 
ATOM   495  S SD  . MET B 2 32  ? -31.008 4.794   -13.540 1.00 30.98 ? 41  MET B SD  1 
ATOM   496  C CE  . MET B 2 32  ? -30.672 6.515   -13.911 1.00 35.53 ? 41  MET B CE  1 
ATOM   497  N N   . GLN B 2 33  ? -30.377 0.596   -15.036 1.00 27.63 ? 42  GLN B N   1 
ATOM   498  C CA  . GLN B 2 33  ? -31.043 -0.655  -15.299 1.00 28.82 ? 42  GLN B CA  1 
ATOM   499  C C   . GLN B 2 33  ? -31.951 -0.974  -14.137 1.00 29.70 ? 42  GLN B C   1 
ATOM   500  O O   . GLN B 2 33  ? -31.507 -0.931  -12.973 1.00 28.97 ? 42  GLN B O   1 
ATOM   501  C CB  . GLN B 2 33  ? -30.067 -1.836  -15.575 1.00 30.72 ? 42  GLN B CB  1 
ATOM   502  C CG  . GLN B 2 33  ? -30.871 -3.110  -15.927 1.00 34.70 ? 42  GLN B CG  1 
ATOM   503  C CD  . GLN B 2 33  ? -30.015 -4.244  -16.419 1.00 39.24 ? 42  GLN B CD  1 
ATOM   504  O OE1 . GLN B 2 33  ? -30.151 -5.398  -15.971 1.00 44.86 ? 42  GLN B OE1 1 
ATOM   505  N NE2 . GLN B 2 33  ? -29.093 -3.921  -17.307 1.00 35.70 ? 42  GLN B NE2 1 
ATOM   506  N N   . GLU B 2 34  ? -33.233 -1.230  -14.424 1.00 30.44 ? 43  GLU B N   1 
ATOM   507  C CA  . GLU B 2 34  ? -34.236 -1.591  -13.418 1.00 31.99 ? 43  GLU B CA  1 
ATOM   508  C C   . GLU B 2 34  ? -34.347 -0.564  -12.292 1.00 33.47 ? 43  GLU B C   1 
ATOM   509  O O   . GLU B 2 34  ? -34.458 -0.930  -11.115 1.00 35.38 ? 43  GLU B O   1 
ATOM   510  C CB  . GLU B 2 34  ? -33.927 -2.984  -12.864 1.00 34.11 ? 43  GLU B CB  1 
ATOM   511  C CG  . GLU B 2 34  ? -33.953 -4.110  -13.897 1.00 37.04 ? 43  GLU B CG  1 
ATOM   512  C CD  . GLU B 2 34  ? -33.355 -5.415  -13.406 1.00 45.96 ? 43  GLU B CD  1 
ATOM   513  O OE1 . GLU B 2 34  ? -33.814 -5.910  -12.353 1.00 47.97 ? 43  GLU B OE1 1 
ATOM   514  O OE2 . GLU B 2 34  ? -32.427 -5.940  -14.063 1.00 47.36 ? 43  GLU B OE2 1 
ATOM   515  N N   . GLY B 2 35  ? -34.239 0.706   -12.662 1.00 32.59 ? 44  GLY B N   1 
ATOM   516  C CA  . GLY B 2 35  ? -34.377 1.841   -11.756 1.00 31.79 ? 44  GLY B CA  1 
ATOM   517  C C   . GLY B 2 35  ? -33.173 2.117   -10.862 1.00 31.28 ? 44  GLY B C   1 
ATOM   518  O O   . GLY B 2 35  ? -33.256 3.002   -9.982  1.00 32.67 ? 44  GLY B O   1 
ATOM   519  N N   . VAL B 2 36  ? -32.046 1.427   -11.133 1.00 27.75 ? 45  VAL B N   1 
ATOM   520  C CA  . VAL B 2 36  ? -30.784 1.559   -10.376 1.00 25.38 ? 45  VAL B CA  1 
ATOM   521  C C   . VAL B 2 36  ? -29.647 2.083   -11.287 1.00 25.57 ? 45  VAL B C   1 
ATOM   522  O O   . VAL B 2 36  ? -29.504 1.647   -12.434 1.00 25.78 ? 45  VAL B O   1 
ATOM   523  C CB  . VAL B 2 36  ? -30.449 0.185   -9.748  1.00 26.55 ? 45  VAL B CB  1 
ATOM   524  C CG1 . VAL B 2 36  ? -29.065 0.219   -9.072  1.00 26.50 ? 45  VAL B CG1 1 
ATOM   525  C CG2 . VAL B 2 36  ? -31.535 -0.183  -8.716  1.00 27.69 ? 45  VAL B CG2 1 
ATOM   526  N N   . PHE B 2 37  ? -28.900 3.066   -10.787 1.00 24.20 ? 46  PHE B N   1 
ATOM   527  C CA  . PHE B 2 37  ? -27.773 3.629   -11.509 1.00 24.29 ? 46  PHE B CA  1 
ATOM   528  C C   . PHE B 2 37  ? -26.476 3.012   -11.018 1.00 23.90 ? 46  PHE B C   1 
ATOM   529  O O   . PHE B 2 37  ? -26.275 2.919   -9.827  1.00 22.82 ? 46  PHE B O   1 
ATOM   530  C CB  . PHE B 2 37  ? -27.732 5.151   -11.452 1.00 25.07 ? 46  PHE B CB  1 
ATOM   531  C CG  . PHE B 2 37  ? -26.697 5.730   -12.377 1.00 26.72 ? 46  PHE B CG  1 
ATOM   532  C CD1 . PHE B 2 37  ? -26.847 5.636   -13.746 1.00 28.86 ? 46  PHE B CD1 1 
ATOM   533  C CD2 . PHE B 2 37  ? -25.575 6.374   -11.874 1.00 27.66 ? 46  PHE B CD2 1 
ATOM   534  C CE1 . PHE B 2 37  ? -25.878 6.177   -14.597 1.00 29.14 ? 46  PHE B CE1 1 
ATOM   535  C CE2 . PHE B 2 37  ? -24.619 6.917   -12.722 1.00 28.31 ? 46  PHE B CE2 1 
ATOM   536  C CZ  . PHE B 2 37  ? -24.790 6.829   -14.083 1.00 28.89 ? 46  PHE B CZ  1 
ATOM   537  N N   . HIS B 2 38  ? -25.680 2.500   -11.920 1.00 22.82 ? 47  HIS B N   1 
ATOM   538  C CA  . HIS B 2 38  ? -24.488 1.713   -11.642 1.00 22.89 ? 47  HIS B CA  1 
ATOM   539  C C   . HIS B 2 38  ? -23.261 2.409   -12.205 1.00 23.57 ? 47  HIS B C   1 
ATOM   540  O O   . HIS B 2 38  ? -23.257 2.730   -13.397 1.00 23.97 ? 47  HIS B O   1 
ATOM   541  C CB  . HIS B 2 38  ? -24.581 0.316   -12.323 1.00 23.52 ? 47  HIS B CB  1 
ATOM   542  C CG  . HIS B 2 38  ? -25.818 -0.490  -12.007 1.00 23.40 ? 47  HIS B CG  1 
ATOM   543  N ND1 . HIS B 2 38  ? -27.053 -0.181  -12.574 1.00 25.46 ? 47  HIS B ND1 1 
ATOM   544  C CD2 . HIS B 2 38  ? -25.958 -1.596  -11.214 1.00 24.56 ? 47  HIS B CD2 1 
ATOM   545  C CE1 . HIS B 2 38  ? -27.899 -1.107  -12.145 1.00 24.61 ? 47  HIS B CE1 1 
ATOM   546  N NE2 . HIS B 2 38  ? -27.287 -1.976  -11.300 1.00 25.28 ? 47  HIS B NE2 1 
ATOM   547  N N   . THR B 2 39  ? -22.231 2.627   -11.396 1.00 23.31 ? 48  THR B N   1 
ATOM   548  C CA  . THR B 2 39  ? -21.001 3.240   -11.920 1.00 23.71 ? 48  THR B CA  1 
ATOM   549  C C   . THR B 2 39  ? -19.804 2.776   -11.072 1.00 23.80 ? 48  THR B C   1 
ATOM   550  O O   . THR B 2 39  ? -19.948 1.818   -10.250 1.00 24.73 ? 48  THR B O   1 
ATOM   551  C CB  . THR B 2 39  ? -21.145 4.820   -12.052 1.00 25.26 ? 48  THR B CB  1 
ATOM   552  O OG1 . THR B 2 39  ? -19.974 5.346   -12.678 1.00 26.14 ? 48  THR B OG1 1 
ATOM   553  C CG2 . THR B 2 39  ? -21.294 5.524   -10.666 1.00 26.57 ? 48  THR B CG2 1 
ATOM   554  N N   . MET B 2 40  ? -18.604 3.272   -11.415 1.00 25.30 ? 49  MET B N   1 
ATOM   555  C CA  . MET B 2 40  ? -17.414 2.863   -10.635 1.00 25.75 ? 49  MET B CA  1 
ATOM   556  C C   . MET B 2 40  ? -17.265 3.821   -9.463  1.00 25.33 ? 49  MET B C   1 
ATOM   557  O O   . MET B 2 40  ? -17.526 5.020   -9.570  1.00 26.72 ? 49  MET B O   1 
ATOM   558  C CB  . MET B 2 40  ? -16.183 2.889   -11.552 1.00 27.53 ? 49  MET B CB  1 
ATOM   559  C CG  . MET B 2 40  ? -16.402 1.877   -12.783 1.00 26.16 ? 49  MET B CG  1 
ATOM   560  S SD  . MET B 2 40  ? -14.873 1.252   -13.464 1.00 32.72 ? 49  MET B SD  1 
ATOM   561  C CE  . MET B 2 40  ? -14.584 -0.046  -12.267 1.00 30.86 ? 49  MET B CE  1 
ATOM   562  N N   A TRP B 2 41  ? -16.842 3.294   -8.296  0.25 24.52 ? 50  TRP B N   1 
ATOM   563  N N   B TRP B 2 41  ? -16.830 3.292   -8.302  0.25 24.53 ? 50  TRP B N   1 
ATOM   564  N N   C TRP B 2 41  ? -16.842 3.294   -8.296  0.25 24.52 ? 50  TRP B N   1 
ATOM   565  N N   D TRP B 2 41  ? -16.830 3.292   -8.302  0.25 24.53 ? 50  TRP B N   1 
ATOM   566  C CA  A TRP B 2 41  ? -16.662 4.117   -7.105  0.25 25.64 ? 50  TRP B CA  1 
ATOM   567  C CA  B TRP B 2 41  ? -16.633 4.092   -7.099  0.25 25.64 ? 50  TRP B CA  1 
ATOM   568  C CA  C TRP B 2 41  ? -16.662 4.117   -7.105  0.25 25.64 ? 50  TRP B CA  1 
ATOM   569  C CA  D TRP B 2 41  ? -16.633 4.092   -7.099  0.25 25.64 ? 50  TRP B CA  1 
ATOM   570  C C   A TRP B 2 41  ? -15.750 5.317   -7.352  0.25 26.94 ? 50  TRP B C   1 
ATOM   571  C C   B TRP B 2 41  ? -15.731 5.301   -7.332  0.25 27.01 ? 50  TRP B C   1 
ATOM   572  C C   C TRP B 2 41  ? -15.750 5.317   -7.352  0.25 26.94 ? 50  TRP B C   1 
ATOM   573  C C   D TRP B 2 41  ? -15.731 5.301   -7.332  0.25 27.01 ? 50  TRP B C   1 
ATOM   574  O O   A TRP B 2 41  ? -16.090 6.414   -6.937  0.25 27.42 ? 50  TRP B O   1 
ATOM   575  O O   B TRP B 2 41  ? -16.027 6.374   -6.828  0.25 27.57 ? 50  TRP B O   1 
ATOM   576  O O   C TRP B 2 41  ? -16.090 6.414   -6.937  0.25 27.42 ? 50  TRP B O   1 
ATOM   577  O O   D TRP B 2 41  ? -16.027 6.374   -6.828  0.25 27.57 ? 50  TRP B O   1 
ATOM   578  C CB  A TRP B 2 41  ? -16.151 3.272   -5.921  0.25 25.75 ? 50  TRP B CB  1 
ATOM   579  C CB  B TRP B 2 41  ? -16.068 3.224   -5.950  0.25 25.67 ? 50  TRP B CB  1 
ATOM   580  C CB  C TRP B 2 41  ? -16.151 3.272   -5.921  0.25 25.75 ? 50  TRP B CB  1 
ATOM   581  C CB  D TRP B 2 41  ? -16.068 3.224   -5.950  0.25 25.67 ? 50  TRP B CB  1 
ATOM   582  C CG  A TRP B 2 41  ? -16.224 4.002   -4.618  0.25 27.10 ? 50  TRP B CG  1 
ATOM   583  C CG  B TRP B 2 41  ? -15.863 4.011   -4.696  0.25 26.87 ? 50  TRP B CG  1 
ATOM   584  C CG  C TRP B 2 41  ? -16.224 4.002   -4.618  0.25 27.10 ? 50  TRP B CG  1 
ATOM   585  C CG  D TRP B 2 41  ? -15.863 4.011   -4.696  0.25 26.87 ? 50  TRP B CG  1 
ATOM   586  C CD1 A TRP B 2 41  ? -17.241 3.964   -3.710  0.25 28.22 ? 50  TRP B CD1 1 
ATOM   587  C CD1 B TRP B 2 41  ? -14.766 4.750   -4.361  0.25 28.12 ? 50  TRP B CD1 1 
ATOM   588  C CD1 C TRP B 2 41  ? -17.241 3.964   -3.710  0.25 28.22 ? 50  TRP B CD1 1 
ATOM   589  C CD1 D TRP B 2 41  ? -14.766 4.750   -4.361  0.25 28.12 ? 50  TRP B CD1 1 
ATOM   590  C CD2 A TRP B 2 41  ? -15.256 4.923   -4.099  0.25 28.09 ? 50  TRP B CD2 1 
ATOM   591  C CD2 B TRP B 2 41  ? -16.833 4.246   -3.674  0.25 27.53 ? 50  TRP B CD2 1 
ATOM   592  C CD2 C TRP B 2 41  ? -15.256 4.923   -4.099  0.25 28.09 ? 50  TRP B CD2 1 
ATOM   593  C CD2 D TRP B 2 41  ? -16.833 4.246   -3.674  0.25 27.53 ? 50  TRP B CD2 1 
ATOM   594  N NE1 A TRP B 2 41  ? -16.972 4.819   -2.666  0.25 28.89 ? 50  TRP B NE1 1 
ATOM   595  N NE1 B TRP B 2 41  ? -15.000 5.435   -3.192  0.25 28.42 ? 50  TRP B NE1 1 
ATOM   596  N NE1 C TRP B 2 41  ? -16.972 4.819   -2.666  0.25 28.89 ? 50  TRP B NE1 1 
ATOM   597  N NE1 D TRP B 2 41  ? -15.000 5.435   -3.192  0.25 28.42 ? 50  TRP B NE1 1 
ATOM   598  C CE2 A TRP B 2 41  ? -15.755 5.413   -2.878  0.25 28.90 ? 50  TRP B CE2 1 
ATOM   599  C CE2 B TRP B 2 41  ? -16.255 5.130   -2.740  0.25 28.37 ? 50  TRP B CE2 1 
ATOM   600  C CE2 C TRP B 2 41  ? -15.755 5.413   -2.878  0.25 28.90 ? 50  TRP B CE2 1 
ATOM   601  C CE2 D TRP B 2 41  ? -16.255 5.130   -2.740  0.25 28.37 ? 50  TRP B CE2 1 
ATOM   602  C CE3 A TRP B 2 41  ? -14.001 5.362   -4.539  0.25 29.17 ? 50  TRP B CE3 1 
ATOM   603  C CE3 B TRP B 2 41  ? -18.128 3.776   -3.445  0.25 28.27 ? 50  TRP B CE3 1 
ATOM   604  C CE3 C TRP B 2 41  ? -14.001 5.362   -4.539  0.25 29.17 ? 50  TRP B CE3 1 
ATOM   605  C CE3 D TRP B 2 41  ? -18.128 3.776   -3.445  0.25 28.27 ? 50  TRP B CE3 1 
ATOM   606  C CZ2 A TRP B 2 41  ? -15.060 6.345   -2.113  0.25 30.64 ? 50  TRP B CZ2 1 
ATOM   607  C CZ2 B TRP B 2 41  ? -16.943 5.578   -1.615  0.25 29.83 ? 50  TRP B CZ2 1 
ATOM   608  C CZ2 C TRP B 2 41  ? -15.060 6.345   -2.113  0.25 30.64 ? 50  TRP B CZ2 1 
ATOM   609  C CZ2 D TRP B 2 41  ? -16.943 5.578   -1.615  0.25 29.83 ? 50  TRP B CZ2 1 
ATOM   610  C CZ3 A TRP B 2 41  ? -13.317 6.289   -3.781  0.25 30.50 ? 50  TRP B CZ3 1 
ATOM   611  C CZ3 B TRP B 2 41  ? -18.795 4.201   -2.314  0.25 29.78 ? 50  TRP B CZ3 1 
ATOM   612  C CZ3 C TRP B 2 41  ? -13.317 6.289   -3.781  0.25 30.50 ? 50  TRP B CZ3 1 
ATOM   613  C CZ3 D TRP B 2 41  ? -18.795 4.201   -2.314  0.25 29.78 ? 50  TRP B CZ3 1 
ATOM   614  C CH2 A TRP B 2 41  ? -13.834 6.755   -2.574  0.25 31.00 ? 50  TRP B CH2 1 
ATOM   615  C CH2 B TRP B 2 41  ? -18.201 5.085   -1.409  0.25 30.11 ? 50  TRP B CH2 1 
ATOM   616  C CH2 C TRP B 2 41  ? -13.834 6.755   -2.574  0.25 31.00 ? 50  TRP B CH2 1 
ATOM   617  C CH2 D TRP B 2 41  ? -18.201 5.085   -1.409  0.25 30.11 ? 50  TRP B CH2 1 
ATOM   618  N N   . HIS B 2 42  ? -14.627 5.133   -8.071  1.00 26.95 ? 51  HIS B N   1 
ATOM   619  C CA  . HIS B 2 42  ? -13.690 6.247   -8.279  1.00 28.31 ? 51  HIS B CA  1 
ATOM   620  C C   . HIS B 2 42  ? -14.267 7.419   -9.103  1.00 29.55 ? 51  HIS B C   1 
ATOM   621  O O   . HIS B 2 42  ? -13.694 8.519   -9.070  1.00 31.01 ? 51  HIS B O   1 
ATOM   622  C CB  . HIS B 2 42  ? -12.370 5.776   -8.841  1.00 27.99 ? 51  HIS B CB  1 
ATOM   623  C CG  . HIS B 2 42  ? -12.402 5.474   -10.309 1.00 29.17 ? 51  HIS B CG  1 
ATOM   624  N ND1 . HIS B 2 42  ? -12.564 4.183   -10.803 1.00 29.11 ? 51  HIS B ND1 1 
ATOM   625  C CD2 . HIS B 2 42  ? -12.276 6.333   -11.351 1.00 30.26 ? 51  HIS B CD2 1 
ATOM   626  C CE1 . HIS B 2 42  ? -12.491 4.301   -12.133 1.00 31.20 ? 51  HIS B CE1 1 
ATOM   627  N NE2 . HIS B 2 42  ? -12.348 5.582   -12.494 1.00 30.13 ? 51  HIS B NE2 1 
ATOM   628  N N   . VAL B 2 43  ? -15.386 7.181   -9.823  1.00 28.05 ? 52  VAL B N   1 
ATOM   629  C CA  . VAL B 2 43  ? -16.016 8.263   -10.601 1.00 27.92 ? 52  VAL B CA  1 
ATOM   630  C C   . VAL B 2 43  ? -16.718 9.254   -9.662  1.00 29.72 ? 52  VAL B C   1 
ATOM   631  O O   . VAL B 2 43  ? -16.544 10.472  -9.796  1.00 29.95 ? 52  VAL B O   1 
ATOM   632  C CB  . VAL B 2 43  ? -17.014 7.660   -11.604 1.00 27.78 ? 52  VAL B CB  1 
ATOM   633  C CG1 . VAL B 2 43  ? -17.936 8.746   -12.254 1.00 28.84 ? 52  VAL B CG1 1 
ATOM   634  C CG2 . VAL B 2 43  ? -16.254 6.862   -12.689 1.00 27.88 ? 52  VAL B CG2 1 
ATOM   635  N N   . THR B 2 44  ? -17.533 8.738   -8.729  1.00 27.84 ? 53  THR B N   1 
ATOM   636  C CA  . THR B 2 44  ? -18.323 9.605   -7.854  1.00 27.00 ? 53  THR B CA  1 
ATOM   637  C C   . THR B 2 44  ? -17.818 9.773   -6.435  1.00 28.39 ? 53  THR B C   1 
ATOM   638  O O   . THR B 2 44  ? -18.298 10.663  -5.690  1.00 29.89 ? 53  THR B O   1 
ATOM   639  C CB  . THR B 2 44  ? -19.779 9.108   -7.756  1.00 26.28 ? 53  THR B CB  1 
ATOM   640  O OG1 . THR B 2 44  ? -19.849 7.864   -7.035  1.00 26.33 ? 53  THR B OG1 1 
ATOM   641  C CG2 . THR B 2 44  ? -20.451 8.926   -9.147  1.00 27.89 ? 53  THR B CG2 1 
ATOM   642  N N   . LYS B 2 45  ? -16.936 8.864   -6.019  1.00 28.45 ? 54  LYS B N   1 
ATOM   643  C CA  . LYS B 2 45  ? -16.436 8.752   -4.630  1.00 29.64 ? 54  LYS B CA  1 
ATOM   644  C C   . LYS B 2 45  ? -17.628 8.539   -3.648  1.00 30.17 ? 54  LYS B C   1 
ATOM   645  O O   . LYS B 2 45  ? -17.515 8.857   -2.438  1.00 31.80 ? 54  LYS B O   1 
ATOM   646  C CB  . LYS B 2 45  ? -15.597 10.003  -4.209  1.00 33.79 ? 54  LYS B CB  1 
ATOM   647  C CG  . LYS B 2 45  ? -14.551 10.464  -5.227  1.00 40.70 ? 54  LYS B CG  1 
ATOM   648  C CD  . LYS B 2 45  ? -13.413 9.522   -5.399  1.00 46.82 ? 54  LYS B CD  1 
ATOM   649  C CE  . LYS B 2 45  ? -12.324 10.176  -6.239  1.00 53.22 ? 54  LYS B CE  1 
ATOM   650  N NZ  . LYS B 2 45  ? -11.746 9.243   -7.254  1.00 55.52 ? 54  LYS B NZ  1 
ATOM   651  N N   . GLY B 2 46  ? -18.764 8.028   -4.134  1.00 28.95 ? 55  GLY B N   1 
ATOM   652  C CA  . GLY B 2 46  ? -19.922 7.785   -3.279  1.00 30.27 ? 55  GLY B CA  1 
ATOM   653  C C   . GLY B 2 46  ? -20.808 8.997   -3.061  1.00 31.94 ? 55  GLY B C   1 
ATOM   654  O O   . GLY B 2 46  ? -21.733 8.937   -2.243  1.00 33.39 ? 55  GLY B O   1 
ATOM   655  N N   . ALA B 2 47  ? -20.584 10.105  -3.790  1.00 31.48 ? 56  ALA B N   1 
ATOM   656  C CA  . ALA B 2 47  ? -21.416 11.302  -3.616  1.00 31.65 ? 56  ALA B CA  1 
ATOM   657  C C   . ALA B 2 47  ? -22.809 11.128  -4.244  1.00 31.45 ? 56  ALA B C   1 
ATOM   658  O O   . ALA B 2 47  ? -22.978 10.347  -5.172  1.00 29.87 ? 56  ALA B O   1 
ATOM   659  C CB  . ALA B 2 47  ? -20.720 12.504  -4.249  1.00 32.81 ? 56  ALA B CB  1 
ATOM   660  N N   . ALA B 2 48  ? -23.790 11.892  -3.774  1.00 32.12 ? 57  ALA B N   1 
ATOM   661  C CA  . ALA B 2 48  ? -25.127 11.906  -4.379  1.00 32.86 ? 57  ALA B CA  1 
ATOM   662  C C   . ALA B 2 48  ? -25.076 12.517  -5.793  1.00 32.55 ? 57  ALA B C   1 
ATOM   663  O O   . ALA B 2 48  ? -24.137 13.240  -6.122  1.00 33.85 ? 57  ALA B O   1 
ATOM   664  C CB  . ALA B 2 48  ? -26.093 12.731  -3.504  1.00 34.65 ? 57  ALA B CB  1 
ATOM   665  N N   . LEU B 2 49  ? -26.014 12.131  -6.650  1.00 30.45 ? 58  LEU B N   1 
ATOM   666  C CA  . LEU B 2 49  ? -26.076 12.604  -8.028  1.00 31.20 ? 58  LEU B CA  1 
ATOM   667  C C   . LEU B 2 49  ? -27.417 13.272  -8.308  1.00 33.10 ? 58  LEU B C   1 
ATOM   668  O O   . LEU B 2 49  ? -28.408 13.012  -7.615  1.00 34.39 ? 58  LEU B O   1 
ATOM   669  C CB  . LEU B 2 49  ? -25.956 11.418  -9.016  1.00 30.42 ? 58  LEU B CB  1 
ATOM   670  C CG  . LEU B 2 49  ? -24.740 10.565  -8.864  1.00 31.08 ? 58  LEU B CG  1 
ATOM   671  C CD1 . LEU B 2 49  ? -24.828 9.313   -9.774  1.00 29.28 ? 58  LEU B CD1 1 
ATOM   672  C CD2 . LEU B 2 49  ? -23.486 11.329  -9.225  1.00 33.42 ? 58  LEU B CD2 1 
ATOM   673  N N   . ARG B 2 50  ? -27.438 14.139  -9.291  1.00 33.57 ? 59  ARG B N   1 
ATOM   674  C CA  . ARG B 2 50  ? -28.642 14.818  -9.727  1.00 35.54 ? 59  ARG B CA  1 
ATOM   675  C C   . ARG B 2 50  ? -29.059 14.240  -11.106 1.00 36.30 ? 59  ARG B C   1 
ATOM   676  O O   . ARG B 2 50  ? -28.197 13.970  -11.934 1.00 34.56 ? 59  ARG B O   1 
ATOM   677  C CB  . ARG B 2 50  ? -28.284 16.324  -9.875  1.00 38.51 ? 59  ARG B CB  1 
ATOM   678  C CG  . ARG B 2 50  ? -29.412 17.228  -10.181 1.00 45.96 ? 59  ARG B CG  1 
ATOM   679  C CD  . ARG B 2 50  ? -28.999 18.686  -9.948  1.00 49.89 ? 59  ARG B CD  1 
ATOM   680  N NE  . ARG B 2 50  ? -27.888 19.153  -10.795 1.00 51.49 ? 59  ARG B NE  1 
ATOM   681  C CZ  . ARG B 2 50  ? -28.007 19.446  -12.088 1.00 55.37 ? 59  ARG B CZ  1 
ATOM   682  N NH1 . ARG B 2 50  ? -29.151 19.218  -12.729 1.00 55.61 ? 59  ARG B NH1 1 
ATOM   683  N NH2 . ARG B 2 50  ? -26.968 19.914  -12.766 1.00 56.74 ? 59  ARG B NH2 1 
ATOM   684  N N   . SER B 2 51  ? -30.373 14.091  -11.352 1.00 38.11 ? 60  SER B N   1 
ATOM   685  C CA  . SER B 2 51  ? -30.920 13.740  -12.666 1.00 40.93 ? 60  SER B CA  1 
ATOM   686  C C   . SER B 2 51  ? -32.048 14.744  -12.889 1.00 42.96 ? 60  SER B C   1 
ATOM   687  O O   . SER B 2 51  ? -33.109 14.569  -12.303 1.00 42.95 ? 60  SER B O   1 
ATOM   688  C CB  . SER B 2 51  ? -31.492 12.329  -12.669 1.00 43.67 ? 60  SER B CB  1 
ATOM   689  O OG  . SER B 2 51  ? -31.910 12.009  -13.985 1.00 48.18 ? 60  SER B OG  1 
ATOM   690  N N   . GLY B 2 52  ? -31.803 15.836  -13.618 1.00 44.65 ? 61  GLY B N   1 
ATOM   691  C CA  . GLY B 2 52  ? -32.811 16.893  -13.765 1.00 46.09 ? 61  GLY B CA  1 
ATOM   692  C C   . GLY B 2 52  ? -33.032 17.539  -12.414 1.00 48.49 ? 61  GLY B C   1 
ATOM   693  O O   . GLY B 2 52  ? -32.060 17.890  -11.743 1.00 48.80 ? 61  GLY B O   1 
ATOM   694  N N   . GLU B 2 53  ? -34.286 17.569  -11.939 1.00 49.55 ? 62  GLU B N   1 
ATOM   695  C CA  . GLU B 2 53  ? -34.580 18.071  -10.600 1.00 51.09 ? 62  GLU B CA  1 
ATOM   696  C C   . GLU B 2 53  ? -34.617 16.963  -9.524  1.00 50.40 ? 62  GLU B C   1 
ATOM   697  O O   . GLU B 2 53  ? -34.955 17.264  -8.377  1.00 51.43 ? 62  GLU B O   1 
ATOM   698  C CB  . GLU B 2 53  ? -35.913 18.823  -10.588 1.00 56.33 ? 62  GLU B CB  1 
ATOM   699  C CG  . GLU B 2 53  ? -35.790 20.330  -10.706 1.00 65.55 ? 62  GLU B CG  1 
ATOM   700  C CD  . GLU B 2 53  ? -37.145 21.013  -10.651 1.00 78.19 ? 62  GLU B CD  1 
ATOM   701  O OE1 . GLU B 2 53  ? -38.119 20.427  -11.182 1.00 80.58 ? 62  GLU B OE1 1 
ATOM   702  O OE2 . GLU B 2 53  ? -37.237 22.128  -10.082 1.00 82.50 ? 62  GLU B OE2 1 
ATOM   703  N N   . GLY B 2 54  ? -34.279 15.720  -9.887  1.00 48.16 ? 63  GLY B N   1 
ATOM   704  C CA  . GLY B 2 54  ? -34.290 14.582  -8.974  1.00 46.44 ? 63  GLY B CA  1 
ATOM   705  C C   . GLY B 2 54  ? -32.926 14.275  -8.384  1.00 44.36 ? 63  GLY B C   1 
ATOM   706  O O   . GLY B 2 54  ? -31.899 14.694  -8.933  1.00 44.50 ? 63  GLY B O   1 
ATOM   707  N N   . ARG B 2 55  ? -32.911 13.610  -7.223  1.00 41.07 ? 64  ARG B N   1 
ATOM   708  C CA  . ARG B 2 55  ? -31.669 13.274  -6.547  1.00 40.43 ? 64  ARG B CA  1 
ATOM   709  C C   . ARG B 2 55  ? -31.528 11.752  -6.519  1.00 38.38 ? 64  ARG B C   1 
ATOM   710  O O   . ARG B 2 55  ? -32.503 11.059  -6.231  1.00 40.12 ? 64  ARG B O   1 
ATOM   711  C CB  . ARG B 2 55  ? -31.689 13.793  -5.102  1.00 42.51 ? 64  ARG B CB  1 
ATOM   712  C CG  . ARG B 2 55  ? -30.351 13.651  -4.366  1.00 45.31 ? 64  ARG B CG  1 
ATOM   713  C CD  . ARG B 2 55  ? -30.473 14.220  -2.958  1.00 48.67 ? 64  ARG B CD  1 
ATOM   714  N NE  . ARG B 2 55  ? -29.352 13.854  -2.096  1.00 52.99 ? 64  ARG B NE  1 
ATOM   715  C CZ  . ARG B 2 55  ? -28.610 14.725  -1.412  1.00 56.93 ? 64  ARG B CZ  1 
ATOM   716  N NH1 . ARG B 2 55  ? -28.854 16.029  -1.497  1.00 56.56 ? 64  ARG B NH1 1 
ATOM   717  N NH2 . ARG B 2 55  ? -27.622 14.298  -0.635  1.00 56.61 ? 64  ARG B NH2 1 
ATOM   718  N N   . LEU B 2 56  ? -30.323 11.235  -6.799  1.00 33.34 ? 65  LEU B N   1 
ATOM   719  C CA  . LEU B 2 56  ? -30.063 9.812   -6.696  1.00 31.94 ? 65  LEU B CA  1 
ATOM   720  C C   . LEU B 2 56  ? -29.110 9.658   -5.515  1.00 31.10 ? 65  LEU B C   1 
ATOM   721  O O   . LEU B 2 56  ? -28.018 10.248  -5.515  1.00 31.94 ? 65  LEU B O   1 
ATOM   722  C CB  . LEU B 2 56  ? -29.318 9.315   -7.965  1.00 31.50 ? 65  LEU B CB  1 
ATOM   723  C CG  . LEU B 2 56  ? -29.989 9.412   -9.318  1.00 35.56 ? 65  LEU B CG  1 
ATOM   724  C CD1 . LEU B 2 56  ? -29.263 8.467   -10.283 1.00 34.64 ? 65  LEU B CD1 1 
ATOM   725  C CD2 . LEU B 2 56  ? -31.411 8.946   -9.288  1.00 39.00 ? 65  LEU B CD2 1 
ATOM   726  N N   . ASP B 2 57  ? -29.503 8.887   -4.499  1.00 30.66 ? 66  ASP B N   1 
ATOM   727  C CA  . ASP B 2 57  ? -28.644 8.674   -3.345  1.00 29.99 ? 66  ASP B CA  1 
ATOM   728  C C   . ASP B 2 57  ? -27.925 7.309   -3.458  1.00 29.03 ? 66  ASP B C   1 
ATOM   729  O O   . ASP B 2 57  ? -28.493 6.361   -4.004  1.00 28.42 ? 66  ASP B O   1 
ATOM   730  C CB  . ASP B 2 57  ? -29.485 8.715   -2.059  1.00 34.03 ? 66  ASP B CB  1 
ATOM   731  C CG  . ASP B 2 57  ? -30.092 10.103  -1.858  1.00 40.82 ? 66  ASP B CG  1 
ATOM   732  O OD1 . ASP B 2 57  ? -29.428 11.090  -2.212  1.00 39.44 ? 66  ASP B OD1 1 
ATOM   733  O OD2 . ASP B 2 57  ? -31.251 10.183  -1.408  1.00 45.83 ? 66  ASP B OD2 1 
ATOM   734  N N   . PRO B 2 58  ? -26.685 7.209   -2.986  1.00 29.22 ? 67  PRO B N   1 
ATOM   735  C CA  . PRO B 2 58  ? -25.994 5.911   -3.005  1.00 28.48 ? 67  PRO B CA  1 
ATOM   736  C C   . PRO B 2 58  ? -26.727 4.908   -2.136  1.00 27.74 ? 67  PRO B C   1 
ATOM   737  O O   . PRO B 2 58  ? -27.348 5.249   -1.098  1.00 28.90 ? 67  PRO B O   1 
ATOM   738  C CB  . PRO B 2 58  ? -24.600 6.223   -2.446  1.00 29.53 ? 67  PRO B CB  1 
ATOM   739  C CG  . PRO B 2 58  ? -24.824 7.472   -1.615  1.00 31.90 ? 67  PRO B CG  1 
ATOM   740  C CD  . PRO B 2 58  ? -25.870 8.251   -2.318  1.00 30.69 ? 67  PRO B CD  1 
ATOM   741  N N   . TYR B 2 59  ? -26.694 3.675   -2.624  1.00 24.79 ? 68  TYR B N   1 
ATOM   742  C CA  . TYR B 2 59  ? -27.349 2.579   -1.909  1.00 24.08 ? 68  TYR B CA  1 
ATOM   743  C C   . TYR B 2 59  ? -26.328 1.507   -1.498  1.00 24.21 ? 68  TYR B C   1 
ATOM   744  O O   . TYR B 2 59  ? -26.437 0.962   -0.389  1.00 24.25 ? 68  TYR B O   1 
ATOM   745  C CB  . TYR B 2 59  ? -28.407 1.971   -2.841  1.00 25.11 ? 68  TYR B CB  1 
ATOM   746  C CG  . TYR B 2 59  ? -29.188 0.831   -2.247  1.00 24.90 ? 68  TYR B CG  1 
ATOM   747  C CD1 . TYR B 2 59  ? -28.641 -0.455  -2.176  1.00 26.07 ? 68  TYR B CD1 1 
ATOM   748  C CD2 . TYR B 2 59  ? -30.483 1.017   -1.783  1.00 25.41 ? 68  TYR B CD2 1 
ATOM   749  C CE1 . TYR B 2 59  ? -29.358 -1.514  -1.642  1.00 27.03 ? 68  TYR B CE1 1 
ATOM   750  C CE2 . TYR B 2 59  ? -31.206 -0.034  -1.231  1.00 27.71 ? 68  TYR B CE2 1 
ATOM   751  C CZ  . TYR B 2 59  ? -30.644 -1.297  -1.166  1.00 28.12 ? 68  TYR B CZ  1 
ATOM   752  O OH  . TYR B 2 59  ? -31.382 -2.325  -0.640  1.00 30.25 ? 68  TYR B OH  1 
ATOM   753  N N   . TRP B 2 60  ? -25.393 1.168   -2.324  1.00 23.76 ? 69  TRP B N   1 
ATOM   754  C CA  . TRP B 2 60  ? -24.383 0.142   -2.037  1.00 23.81 ? 69  TRP B CA  1 
ATOM   755  C C   . TRP B 2 60  ? -23.071 0.594   -2.683  1.00 24.10 ? 69  TRP B C   1 
ATOM   756  O O   . TRP B 2 60  ? -23.102 1.106   -3.784  1.00 24.01 ? 69  TRP B O   1 
ATOM   757  C CB  . TRP B 2 60  ? -24.778 -1.267  -2.551  1.00 24.94 ? 69  TRP B CB  1 
ATOM   758  C CG  . TRP B 2 60  ? -23.639 -2.260  -2.549  1.00 25.24 ? 69  TRP B CG  1 
ATOM   759  C CD1 . TRP B 2 60  ? -23.177 -2.968  -1.465  1.00 25.71 ? 69  TRP B CD1 1 
ATOM   760  C CD2 . TRP B 2 60  ? -22.712 -2.529  -3.632  1.00 24.27 ? 69  TRP B CD2 1 
ATOM   761  N NE1 . TRP B 2 60  ? -22.024 -3.665  -1.801  1.00 26.00 ? 69  TRP B NE1 1 
ATOM   762  C CE2 . TRP B 2 60  ? -21.732 -3.430  -3.136  1.00 24.97 ? 69  TRP B CE2 1 
ATOM   763  C CE3 . TRP B 2 60  ? -22.633 -2.114  -4.961  1.00 25.05 ? 69  TRP B CE3 1 
ATOM   764  C CZ2 . TRP B 2 60  ? -20.691 -3.921  -3.921  1.00 26.45 ? 69  TRP B CZ2 1 
ATOM   765  C CZ3 . TRP B 2 60  ? -21.579 -2.584  -5.712  1.00 26.05 ? 69  TRP B CZ3 1 
ATOM   766  C CH2 . TRP B 2 60  ? -20.625 -3.472  -5.202  1.00 26.30 ? 69  TRP B CH2 1 
ATOM   767  N N   . GLY B 2 61  ? -21.941 0.301   -2.043  1.00 24.34 ? 70  GLY B N   1 
ATOM   768  C CA  . GLY B 2 61  ? -20.650 0.600   -2.669  1.00 25.72 ? 70  GLY B CA  1 
ATOM   769  C C   . GLY B 2 61  ? -19.523 -0.165  -2.022  1.00 25.13 ? 70  GLY B C   1 
ATOM   770  O O   . GLY B 2 61  ? -19.649 -0.567  -0.870  1.00 24.82 ? 70  GLY B O   1 
ATOM   771  N N   . ASP B 2 62  ? -18.405 -0.283  -2.740  1.00 24.05 ? 71  ASP B N   1 
ATOM   772  C CA  . ASP B 2 62  ? -17.258 -1.017  -2.216  1.00 25.18 ? 71  ASP B CA  1 
ATOM   773  C C   . ASP B 2 62  ? -16.018 -0.518  -2.941  1.00 24.63 ? 71  ASP B C   1 
ATOM   774  O O   . ASP B 2 62  ? -15.896 -0.651  -4.152  1.00 24.69 ? 71  ASP B O   1 
ATOM   775  C CB  . ASP B 2 62  ? -17.461 -2.537  -2.395  1.00 26.06 ? 71  ASP B CB  1 
ATOM   776  C CG  . ASP B 2 62  ? -16.412 -3.347  -1.675  1.00 32.83 ? 71  ASP B CG  1 
ATOM   777  O OD1 . ASP B 2 62  ? -15.265 -3.342  -2.101  1.00 30.58 ? 71  ASP B OD1 1 
ATOM   778  O OD2 . ASP B 2 62  ? -16.717 -3.873  -0.609  1.00 37.79 ? 71  ASP B OD2 1 
ATOM   779  N N   . VAL B 2 63  ? -15.101 0.095   -2.198  1.00 24.01 ? 72  VAL B N   1 
ATOM   780  C CA  . VAL B 2 63  ? -13.853 0.646   -2.811  1.00 23.84 ? 72  VAL B CA  1 
ATOM   781  C C   . VAL B 2 63  ? -12.992 -0.409  -3.445  1.00 25.28 ? 72  VAL B C   1 
ATOM   782  O O   . VAL B 2 63  ? -12.357 -0.118  -4.477  1.00 27.22 ? 72  VAL B O   1 
ATOM   783  C CB  . VAL B 2 63  ? -13.081 1.456   -1.713  1.00 25.67 ? 72  VAL B CB  1 
ATOM   784  C CG1 . VAL B 2 63  ? -11.589 1.639   -2.044  1.00 27.52 ? 72  VAL B CG1 1 
ATOM   785  C CG2 . VAL B 2 63  ? -13.750 2.801   -1.484  1.00 25.87 ? 72  VAL B CG2 1 
ATOM   786  N N   . LYS B 2 64  ? -12.903 -1.603  -2.815  1.00 26.06 ? 73  LYS B N   1 
ATOM   787  C CA  . LYS B 2 64  ? -12.000 -2.627  -3.388  1.00 27.43 ? 73  LYS B CA  1 
ATOM   788  C C   . LYS B 2 64  ? -12.513 -3.163  -4.721  1.00 27.51 ? 73  LYS B C   1 
ATOM   789  O O   . LYS B 2 64  ? -11.742 -3.322  -5.667  1.00 29.27 ? 73  LYS B O   1 
ATOM   790  C CB  . LYS B 2 64  ? -11.757 -3.761  -2.374  1.00 27.76 ? 73  LYS B CB  1 
ATOM   791  C CG  . LYS B 2 64  ? -10.701 -4.729  -2.925  1.00 32.03 ? 73  LYS B CG  1 
ATOM   792  C CD  . LYS B 2 64  ? -10.373 -5.795  -1.889  1.00 33.43 ? 73  LYS B CD  1 
ATOM   793  C CE  . LYS B 2 64  ? -9.520  -6.871  -2.524  1.00 36.36 ? 73  LYS B CE  1 
ATOM   794  N NZ  . LYS B 2 64  ? -9.073  -7.886  -1.488  1.00 37.23 ? 73  LYS B NZ  1 
ATOM   795  N N   . GLN B 2 65  ? -13.828 -3.371  -4.819  1.00 25.32 ? 74  GLN B N   1 
ATOM   796  C CA  . GLN B 2 65  ? -14.441 -3.764  -6.093  1.00 25.25 ? 74  GLN B CA  1 
ATOM   797  C C   . GLN B 2 65  ? -14.470 -2.560  -7.032  1.00 25.92 ? 74  GLN B C   1 
ATOM   798  O O   . GLN B 2 65  ? -14.602 -2.773  -8.255  1.00 26.57 ? 74  GLN B O   1 
ATOM   799  C CB  . GLN B 2 65  ? -15.892 -4.234  -5.861  1.00 26.39 ? 74  GLN B CB  1 
ATOM   800  C CG  . GLN B 2 65  ? -16.018 -5.541  -5.045  1.00 30.39 ? 74  GLN B CG  1 
ATOM   801  C CD  . GLN B 2 65  ? -17.465 -5.997  -4.958  1.00 37.95 ? 74  GLN B CD  1 
ATOM   802  O OE1 . GLN B 2 65  ? -18.202 -6.005  -5.966  1.00 40.76 ? 74  GLN B OE1 1 
ATOM   803  N NE2 . GLN B 2 65  ? -17.910 -6.421  -3.767  1.00 38.67 ? 74  GLN B NE2 1 
ATOM   804  N N   . ASP B 2 66  ? -14.388 -1.331  -6.509  1.00 24.79 ? 75  ASP B N   1 
ATOM   805  C CA  . ASP B 2 66  ? -14.479 -0.086  -7.293  1.00 23.96 ? 75  ASP B CA  1 
ATOM   806  C C   . ASP B 2 66  ? -15.839 0.003   -7.953  1.00 24.57 ? 75  ASP B C   1 
ATOM   807  O O   . ASP B 2 66  ? -15.950 0.535   -9.088  1.00 23.91 ? 75  ASP B O   1 
ATOM   808  C CB  . ASP B 2 66  ? -13.333 0.109   -8.329  1.00 25.90 ? 75  ASP B CB  1 
ATOM   809  C CG  . ASP B 2 66  ? -13.218 1.532   -8.817  1.00 28.43 ? 75  ASP B CG  1 
ATOM   810  O OD1 . ASP B 2 66  ? -13.582 2.447   -8.090  1.00 27.12 ? 75  ASP B OD1 1 
ATOM   811  O OD2 . ASP B 2 66  ? -12.696 1.735   -9.915  1.00 28.56 ? 75  ASP B OD2 1 
ATOM   812  N N   . LEU B 2 67  ? -16.915 -0.257  -7.208  1.00 24.01 ? 76  LEU B N   1 
ATOM   813  C CA  . LEU B 2 67  ? -18.269 -0.156  -7.736  1.00 24.17 ? 76  LEU B CA  1 
ATOM   814  C C   . LEU B 2 67  ? -19.210 0.555   -6.794  1.00 24.36 ? 76  LEU B C   1 
ATOM   815  O O   . LEU B 2 67  ? -18.979 0.514   -5.605  1.00 24.24 ? 76  LEU B O   1 
ATOM   816  C CB  . LEU B 2 67  ? -18.850 -1.552  -7.991  1.00 25.01 ? 76  LEU B CB  1 
ATOM   817  C CG  . LEU B 2 67  ? -18.168 -2.352  -9.095  1.00 25.27 ? 76  LEU B CG  1 
ATOM   818  C CD1 . LEU B 2 67  ? -18.832 -3.747  -9.171  1.00 25.99 ? 76  LEU B CD1 1 
ATOM   819  C CD2 . LEU B 2 67  ? -18.303 -1.616  -10.477 1.00 27.13 ? 76  LEU B CD2 1 
ATOM   820  N N   . VAL B 2 68  ? -20.284 1.103   -7.320  1.00 23.95 ? 77  VAL B N   1 
ATOM   821  C CA  . VAL B 2 68  ? -21.310 1.804   -6.526  1.00 23.91 ? 77  VAL B CA  1 
ATOM   822  C C   . VAL B 2 68  ? -22.637 1.726   -7.282  1.00 23.68 ? 77  VAL B C   1 
ATOM   823  O O   . VAL B 2 68  ? -22.682 1.808   -8.511  1.00 23.23 ? 77  VAL B O   1 
ATOM   824  C CB  . VAL B 2 68  ? -20.912 3.270   -6.154  1.00 25.37 ? 77  VAL B CB  1 
ATOM   825  C CG1 . VAL B 2 68  ? -20.757 4.118   -7.400  1.00 25.82 ? 77  VAL B CG1 1 
ATOM   826  C CG2 . VAL B 2 68  ? -21.957 3.942   -5.232  1.00 25.22 ? 77  VAL B CG2 1 
ATOM   827  N N   . SER B 2 69  ? -23.731 1.573   -6.532  1.00 22.90 ? 78  SER B N   1 
ATOM   828  C CA  . SER B 2 69  ? -25.087 1.610   -7.081  1.00 22.80 ? 78  SER B CA  1 
ATOM   829  C C   . SER B 2 69  ? -25.894 2.681   -6.343  1.00 23.95 ? 78  SER B C   1 
ATOM   830  O O   . SER B 2 69  ? -25.655 2.966   -5.162  1.00 23.63 ? 78  SER B O   1 
ATOM   831  C CB  . SER B 2 69  ? -25.784 0.250   -7.008  1.00 24.47 ? 78  SER B CB  1 
ATOM   832  O OG  . SER B 2 69  ? -26.086 -0.174  -5.680  1.00 25.05 ? 78  SER B OG  1 
ATOM   833  N N   . TYR B 2 70  ? -26.854 3.254   -7.067  1.00 23.60 ? 79  TYR B N   1 
ATOM   834  C CA  . TYR B 2 70  ? -27.718 4.324   -6.543  1.00 24.13 ? 79  TYR B CA  1 
ATOM   835  C C   . TYR B 2 70  ? -29.197 3.907   -6.709  1.00 25.89 ? 79  TYR B C   1 
ATOM   836  O O   . TYR B 2 70  ? -29.560 3.352   -7.746  1.00 25.55 ? 79  TYR B O   1 
ATOM   837  C CB  . TYR B 2 70  ? -27.532 5.619   -7.423  1.00 24.00 ? 79  TYR B CB  1 
ATOM   838  C CG  . TYR B 2 70  ? -26.195 6.294   -7.175  1.00 23.49 ? 79  TYR B CG  1 
ATOM   839  C CD1 . TYR B 2 70  ? -25.024 5.805   -7.753  1.00 23.65 ? 79  TYR B CD1 1 
ATOM   840  C CD2 . TYR B 2 70  ? -26.104 7.429   -6.381  1.00 24.48 ? 79  TYR B CD2 1 
ATOM   841  C CE1 . TYR B 2 70  ? -23.788 6.379   -7.484  1.00 24.93 ? 79  TYR B CE1 1 
ATOM   842  C CE2 . TYR B 2 70  ? -24.870 7.991   -6.069  1.00 24.90 ? 79  TYR B CE2 1 
ATOM   843  C CZ  . TYR B 2 70  ? -23.715 7.474   -6.633  1.00 26.39 ? 79  TYR B CZ  1 
ATOM   844  O OH  . TYR B 2 70  ? -22.490 8.046   -6.325  1.00 27.42 ? 79  TYR B OH  1 
ATOM   845  N N   . CYS B 2 71  ? -30.054 4.258   -5.727  1.00 25.95 ? 80  CYS B N   1 
ATOM   846  C CA  . CYS B 2 71  ? -31.520 4.000   -5.711  1.00 28.32 ? 80  CYS B CA  1 
ATOM   847  C C   . CYS B 2 71  ? -31.913 2.564   -5.414  1.00 29.04 ? 80  CYS B C   1 
ATOM   848  O O   . CYS B 2 71  ? -33.104 2.314   -5.154  1.00 32.09 ? 80  CYS B O   1 
ATOM   849  C CB  . CYS B 2 71  ? -32.229 4.465   -6.972  1.00 29.90 ? 80  CYS B CB  1 
ATOM   850  S SG  . CYS B 2 71  ? -31.794 6.142   -7.502  1.00 34.75 ? 80  CYS B SG  1 
ATOM   851  N N   . GLY B 2 72  ? -30.965 1.650   -5.433  1.00 26.66 ? 81  GLY B N   1 
ATOM   852  C CA  . GLY B 2 72  ? -31.267 0.257   -5.137  1.00 25.94 ? 81  GLY B CA  1 
ATOM   853  C C   . GLY B 2 72  ? -30.026 -0.592  -5.255  1.00 25.51 ? 81  GLY B C   1 
ATOM   854  O O   . GLY B 2 72  ? -28.927 -0.088  -5.533  1.00 25.58 ? 81  GLY B O   1 
ATOM   855  N N   . PRO B 2 73  ? -30.190 -1.907  -5.008  1.00 26.28 ? 82  PRO B N   1 
ATOM   856  C CA  . PRO B 2 73  ? -29.042 -2.803  -5.070  1.00 26.45 ? 82  PRO B CA  1 
ATOM   857  C C   . PRO B 2 73  ? -28.510 -3.044  -6.465  1.00 27.02 ? 82  PRO B C   1 
ATOM   858  O O   . PRO B 2 73  ? -29.264 -2.918  -7.422  1.00 27.84 ? 82  PRO B O   1 
ATOM   859  C CB  . PRO B 2 73  ? -29.554 -4.105  -4.416  1.00 27.85 ? 82  PRO B CB  1 
ATOM   860  C CG  . PRO B 2 73  ? -31.029 -4.069  -4.725  1.00 29.30 ? 82  PRO B CG  1 
ATOM   861  C CD  . PRO B 2 73  ? -31.444 -2.606  -4.661  1.00 27.41 ? 82  PRO B CD  1 
ATOM   862  N N   . TRP B 2 74  ? -27.260 -3.488  -6.558  1.00 25.97 ? 83  TRP B N   1 
ATOM   863  C CA  . TRP B 2 74  ? -26.583 -3.757  -7.846  1.00 26.60 ? 83  TRP B CA  1 
ATOM   864  C C   . TRP B 2 74  ? -27.430 -4.774  -8.629  1.00 26.91 ? 83  TRP B C   1 
ATOM   865  O O   . TRP B 2 74  ? -27.736 -5.840  -8.097  1.00 28.54 ? 83  TRP B O   1 
ATOM   866  C CB  . TRP B 2 74  ? -25.158 -4.314  -7.556  1.00 26.34 ? 83  TRP B CB  1 
ATOM   867  C CG  . TRP B 2 74  ? -24.363 -4.514  -8.823  1.00 26.59 ? 83  TRP B CG  1 
ATOM   868  C CD1 . TRP B 2 74  ? -24.316 -5.644  -9.584  1.00 27.14 ? 83  TRP B CD1 1 
ATOM   869  C CD2 . TRP B 2 74  ? -23.501 -3.556  -9.459  1.00 26.53 ? 83  TRP B CD2 1 
ATOM   870  N NE1 . TRP B 2 74  ? -23.488 -5.447  -10.681 1.00 27.45 ? 83  TRP B NE1 1 
ATOM   871  C CE2 . TRP B 2 74  ? -23.015 -4.155  -10.651 1.00 26.94 ? 83  TRP B CE2 1 
ATOM   872  C CE3 . TRP B 2 74  ? -23.144 -2.227  -9.184  1.00 26.28 ? 83  TRP B CE3 1 
ATOM   873  C CZ2 . TRP B 2 74  ? -22.154 -3.487  -11.532 1.00 26.91 ? 83  TRP B CZ2 1 
ATOM   874  C CZ3 . TRP B 2 74  ? -22.289 -1.567  -10.050 1.00 25.76 ? 83  TRP B CZ3 1 
ATOM   875  C CH2 . TRP B 2 74  ? -21.845 -2.177  -11.240 1.00 25.73 ? 83  TRP B CH2 1 
ATOM   876  N N   . LYS B 2 75  ? -27.776 -4.455  -9.887  1.00 26.17 ? 84  LYS B N   1 
ATOM   877  C CA  . LYS B 2 75  ? -28.679 -5.326  -10.657 1.00 27.26 ? 84  LYS B CA  1 
ATOM   878  C C   . LYS B 2 75  ? -27.965 -6.127  -11.747 1.00 29.41 ? 84  LYS B C   1 
ATOM   879  O O   . LYS B 2 75  ? -28.601 -7.013  -12.330 1.00 32.09 ? 84  LYS B O   1 
ATOM   880  C CB  . LYS B 2 75  ? -29.729 -4.438  -11.360 1.00 27.80 ? 84  LYS B CB  1 
ATOM   881  C CG  . LYS B 2 75  ? -30.606 -3.561  -10.424 1.00 29.38 ? 84  LYS B CG  1 
ATOM   882  C CD  . LYS B 2 75  ? -31.618 -4.447  -9.693  1.00 32.56 ? 84  LYS B CD  1 
ATOM   883  C CE  . LYS B 2 75  ? -32.571 -3.621  -8.835  1.00 37.22 ? 84  LYS B CE  1 
ATOM   884  N NZ  . LYS B 2 75  ? -33.639 -4.457  -8.244  1.00 41.77 ? 84  LYS B NZ  1 
ATOM   885  N N   . LEU B 2 76  ? -26.743 -5.756  -12.120 1.00 28.39 ? 85  LEU B N   1 
ATOM   886  C CA  . LEU B 2 76  ? -26.038 -6.368  -13.274 1.00 28.71 ? 85  LEU B CA  1 
ATOM   887  C C   . LEU B 2 76  ? -25.392 -7.684  -12.887 1.00 30.81 ? 85  LEU B C   1 
ATOM   888  O O   . LEU B 2 76  ? -24.535 -7.720  -12.024 1.00 30.63 ? 85  LEU B O   1 
ATOM   889  C CB  . LEU B 2 76  ? -25.023 -5.420  -13.893 1.00 28.98 ? 85  LEU B CB  1 
ATOM   890  C CG  . LEU B 2 76  ? -25.503 -3.944  -14.068 1.00 28.99 ? 85  LEU B CG  1 
ATOM   891  C CD1 . LEU B 2 76  ? -24.418 -3.035  -14.636 1.00 30.42 ? 85  LEU B CD1 1 
ATOM   892  C CD2 . LEU B 2 76  ? -26.769 -3.840  -14.928 1.00 30.98 ? 85  LEU B CD2 1 
ATOM   893  N N   . ASP B 2 77  ? -25.785 -8.766  -13.585 1.00 33.21 ? 86  ASP B N   1 
ATOM   894  C CA  . ASP B 2 77  ? -25.289 -10.082 -13.205 1.00 36.01 ? 86  ASP B CA  1 
ATOM   895  C C   . ASP B 2 77  ? -24.739 -10.934 -14.344 1.00 35.29 ? 86  ASP B C   1 
ATOM   896  O O   . ASP B 2 77  ? -24.201 -12.024 -14.072 1.00 35.86 ? 86  ASP B O   1 
ATOM   897  C CB  . ASP B 2 77  ? -26.362 -10.860 -12.429 1.00 41.84 ? 86  ASP B CB  1 
ATOM   898  C CG  . ASP B 2 77  ? -27.676 -11.061 -13.160 1.00 50.80 ? 86  ASP B CG  1 
ATOM   899  O OD1 . ASP B 2 77  ? -27.881 -10.420 -14.218 1.00 53.87 ? 86  ASP B OD1 1 
ATOM   900  O OD2 . ASP B 2 77  ? -28.510 -11.839 -12.667 1.00 55.70 ? 86  ASP B OD2 1 
ATOM   901  N N   . ALA B 2 78  ? -24.782 -10.441 -15.569 1.00 34.00 ? 87  ALA B N   1 
ATOM   902  C CA  . ALA B 2 78  ? -24.200 -11.203 -16.684 1.00 33.92 ? 87  ALA B CA  1 
ATOM   903  C C   . ALA B 2 78  ? -22.683 -11.302 -16.549 1.00 34.01 ? 87  ALA B C   1 
ATOM   904  O O   . ALA B 2 78  ? -22.022 -10.418 -15.981 1.00 32.79 ? 87  ALA B O   1 
ATOM   905  C CB  . ALA B 2 78  ? -24.584 -10.578 -18.018 1.00 32.79 ? 87  ALA B CB  1 
ATOM   906  N N   . ALA B 2 79  ? -22.129 -12.400 -17.083 1.00 34.53 ? 88  ALA B N   1 
ATOM   907  C CA  . ALA B 2 79  ? -20.695 -12.652 -16.987 1.00 35.84 ? 88  ALA B CA  1 
ATOM   908  C C   . ALA B 2 79  ? -20.109 -12.971 -18.341 1.00 36.18 ? 88  ALA B C   1 
ATOM   909  O O   . ALA B 2 79  ? -20.773 -13.612 -19.155 1.00 37.80 ? 88  ALA B O   1 
ATOM   910  C CB  . ALA B 2 79  ? -20.437 -13.836 -16.054 1.00 38.11 ? 88  ALA B CB  1 
ATOM   911  N N   . TRP B 2 80  ? -18.848 -12.552 -18.589 1.00 35.12 ? 89  TRP B N   1 
ATOM   912  C CA  . TRP B 2 80  ? -18.126 -12.902 -19.822 1.00 35.98 ? 89  TRP B CA  1 
ATOM   913  C C   . TRP B 2 80  ? -18.008 -14.444 -19.861 1.00 37.24 ? 89  TRP B C   1 
ATOM   914  O O   . TRP B 2 80  ? -17.752 -15.065 -18.824 1.00 37.14 ? 89  TRP B O   1 
ATOM   915  C CB  . TRP B 2 80  ? -16.685 -12.322 -19.843 1.00 36.67 ? 89  TRP B CB  1 
ATOM   916  C CG  . TRP B 2 80  ? -15.897 -12.641 -21.107 1.00 37.28 ? 89  TRP B CG  1 
ATOM   917  C CD1 . TRP B 2 80  ? -16.343 -12.583 -22.403 1.00 39.26 ? 89  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 2 80  ? -14.520 -13.062 -21.173 1.00 38.29 ? 89  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 2 80  ? -15.343 -13.001 -23.266 1.00 39.57 ? 89  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 2 80  ? -14.211 -13.282 -22.537 1.00 39.53 ? 89  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 2 80  ? -13.527 -13.309 -20.209 1.00 38.63 ? 89  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 2 80  ? -12.940 -13.665 -22.957 1.00 40.85 ? 89  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 2 80  ? -12.273 -13.736 -20.637 1.00 39.85 ? 89  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 2 80  ? -11.984 -13.869 -22.000 1.00 40.25 ? 89  TRP B CH2 1 
ATOM   925  N N   . ASP B 2 81  ? -18.323 -15.033 -21.043 1.00 39.54 ? 90  ASP B N   1 
ATOM   926  C CA  . ASP B 2 81  ? -18.237 -16.492 -21.181 1.00 42.30 ? 90  ASP B CA  1 
ATOM   927  C C   . ASP B 2 81  ? -16.786 -17.023 -21.266 1.00 45.32 ? 90  ASP B C   1 
ATOM   928  O O   . ASP B 2 81  ? -16.602 -18.243 -21.373 1.00 46.26 ? 90  ASP B O   1 
ATOM   929  C CB  . ASP B 2 81  ? -19.090 -16.996 -22.374 1.00 43.09 ? 90  ASP B CB  1 
ATOM   930  C CG  . ASP B 2 81  ? -18.603 -16.584 -23.731 1.00 48.08 ? 90  ASP B CG  1 
ATOM   931  O OD1 . ASP B 2 81  ? -17.503 -15.999 -23.818 1.00 47.09 ? 90  ASP B OD1 1 
ATOM   932  O OD2 . ASP B 2 81  ? -19.352 -16.790 -24.722 1.00 53.29 ? 90  ASP B OD2 1 
ATOM   933  N N   . GLY B 2 82  ? -15.788 -16.148 -21.349 1.00 45.63 ? 91  GLY B N   1 
ATOM   934  C CA  . GLY B 2 82  ? -14.388 -16.592 -21.430 1.00 46.27 ? 91  GLY B CA  1 
ATOM   935  C C   . GLY B 2 82  ? -13.929 -17.023 -22.825 1.00 47.90 ? 91  GLY B C   1 
ATOM   936  O O   . GLY B 2 82  ? -12.783 -17.465 -22.988 1.00 49.38 ? 91  GLY B O   1 
ATOM   937  N N   . LEU B 2 83  ? -14.804 -16.941 -23.815 1.00 47.57 ? 92  LEU B N   1 
ATOM   938  C CA  . LEU B 2 83  ? -14.475 -17.385 -25.173 1.00 48.77 ? 92  LEU B CA  1 
ATOM   939  C C   . LEU B 2 83  ? -14.715 -16.352 -26.247 1.00 47.74 ? 92  LEU B C   1 
ATOM   940  O O   . LEU B 2 83  ? -14.000 -16.319 -27.252 1.00 48.25 ? 92  LEU B O   1 
ATOM   941  C CB  . LEU B 2 83  ? -15.381 -18.571 -25.561 1.00 50.80 ? 92  LEU B CB  1 
ATOM   942  C CG  . LEU B 2 83  ? -15.202 -19.902 -24.880 1.00 54.33 ? 92  LEU B CG  1 
ATOM   943  C CD1 . LEU B 2 83  ? -16.218 -20.886 -25.439 1.00 55.59 ? 92  LEU B CD1 1 
ATOM   944  C CD2 . LEU B 2 83  ? -13.792 -20.501 -25.175 1.00 54.65 ? 92  LEU B CD2 1 
ATOM   945  N N   . SER B 2 84  ? -15.829 -15.596 -26.130 1.00 46.00 ? 93  SER B N   1 
ATOM   946  C CA  . SER B 2 84  ? -16.317 -14.746 -27.213 1.00 46.18 ? 93  SER B CA  1 
ATOM   947  C C   . SER B 2 84  ? -15.895 -13.300 -27.181 1.00 44.66 ? 93  SER B C   1 
ATOM   948  O O   . SER B 2 84  ? -15.540 -12.802 -26.119 1.00 43.68 ? 93  SER B O   1 
ATOM   949  C CB  . SER B 2 84  ? -17.853 -14.773 -27.262 1.00 48.04 ? 93  SER B CB  1 
ATOM   950  O OG  . SER B 2 84  ? -18.352 -16.079 -27.012 1.00 52.85 ? 93  SER B OG  1 
ATOM   951  N N   . GLU B 2 85  ? -15.963 -12.624 -28.314 1.00 43.73 ? 94  GLU B N   1 
ATOM   952  C CA  . GLU B 2 85  ? -15.705 -11.191 -28.363 1.00 42.50 ? 94  GLU B CA  1 
ATOM   953  C C   . GLU B 2 85  ? -16.854 -10.462 -27.642 1.00 41.69 ? 94  GLU B C   1 
ATOM   954  O O   . GLU B 2 85  ? -17.943 -11.004 -27.434 1.00 41.08 ? 94  GLU B O   1 
ATOM   955  C CB  . GLU B 2 85  ? -15.473 -10.668 -29.801 1.00 42.74 ? 94  GLU B CB  1 
ATOM   956  C CG  . GLU B 2 85  ? -14.155 -11.233 -30.355 1.00 46.65 ? 94  GLU B CG  1 
ATOM   957  C CD  . GLU B 2 85  ? -13.626 -10.550 -31.609 1.00 52.55 ? 94  GLU B CD  1 
ATOM   958  O OE1 . GLU B 2 85  ? -14.413 -9.875  -32.300 1.00 51.12 ? 94  GLU B OE1 1 
ATOM   959  O OE2 . GLU B 2 85  ? -12.411 -10.681 -31.887 1.00 57.29 ? 94  GLU B OE2 1 
ATOM   960  N N   . VAL B 2 86  ? -16.519 -9.312  -27.113 1.00 40.42 ? 95  VAL B N   1 
ATOM   961  C CA  . VAL B 2 86  ? -17.481 -8.466  -26.418 1.00 36.55 ? 95  VAL B CA  1 
ATOM   962  C C   . VAL B 2 86  ? -17.418 -7.065  -27.047 1.00 36.91 ? 95  VAL B C   1 
ATOM   963  O O   . VAL B 2 86  ? -16.585 -6.809  -27.942 1.00 37.74 ? 95  VAL B O   1 
ATOM   964  C CB  . VAL B 2 86  ? -17.072 -8.374  -24.919 1.00 34.74 ? 95  VAL B CB  1 
ATOM   965  C CG1 . VAL B 2 86  ? -16.946 -9.749  -24.311 1.00 35.20 ? 95  VAL B CG1 1 
ATOM   966  C CG2 . VAL B 2 86  ? -15.776 -7.569  -24.758 1.00 35.43 ? 95  VAL B CG2 1 
ATOM   967  N N   . GLN B 2 87  ? -18.318 -6.142  -26.626 1.00 35.39 ? 96  GLN B N   1 
ATOM   968  C CA  . GLN B 2 87  ? -18.253 -4.789  -27.070 1.00 34.86 ? 96  GLN B CA  1 
ATOM   969  C C   . GLN B 2 87  ? -18.138 -3.857  -25.885 1.00 34.25 ? 96  GLN B C   1 
ATOM   970  O O   . GLN B 2 87  ? -18.909 -3.961  -24.948 1.00 35.76 ? 96  GLN B O   1 
ATOM   971  C CB  . GLN B 2 87  ? -19.479 -4.408  -27.963 1.00 35.26 ? 96  GLN B CB  1 
ATOM   972  C CG  . GLN B 2 87  ? -19.253 -4.986  -29.395 1.00 37.21 ? 96  GLN B CG  1 
ATOM   973  C CD  . GLN B 2 87  ? -20.369 -4.647  -30.342 1.00 39.06 ? 96  GLN B CD  1 
ATOM   974  O OE1 . GLN B 2 87  ? -21.324 -3.933  -30.052 1.00 37.67 ? 96  GLN B OE1 1 
ATOM   975  N NE2 . GLN B 2 87  ? -20.242 -5.231  -31.555 1.00 41.80 ? 96  GLN B NE2 1 
ATOM   976  N N   . LEU B 2 88  ? -17.227 -2.928  -25.980 1.00 34.00 ? 97  LEU B N   1 
ATOM   977  C CA  . LEU B 2 88  ? -17.188 -1.793  -25.073 1.00 33.42 ? 97  LEU B CA  1 
ATOM   978  C C   . LEU B 2 88  ? -18.093 -0.697  -25.673 1.00 33.59 ? 97  LEU B C   1 
ATOM   979  O O   . LEU B 2 88  ? -17.895 -0.276  -26.834 1.00 34.29 ? 97  LEU B O   1 
ATOM   980  C CB  . LEU B 2 88  ? -15.770 -1.255  -24.845 1.00 32.83 ? 97  LEU B CB  1 
ATOM   981  C CG  . LEU B 2 88  ? -15.692 0.084   -24.136 1.00 34.16 ? 97  LEU B CG  1 
ATOM   982  C CD1 . LEU B 2 88  ? -16.177 -0.055  -22.647 1.00 32.56 ? 97  LEU B CD1 1 
ATOM   983  C CD2 . LEU B 2 88  ? -14.306 0.637   -24.226 1.00 35.97 ? 97  LEU B CD2 1 
ATOM   984  N N   . LEU B 2 89  ? -19.095 -0.224  -24.919 1.00 33.03 ? 98  LEU B N   1 
ATOM   985  C CA  . LEU B 2 89  ? -19.925 0.856   -25.354 1.00 32.31 ? 98  LEU B CA  1 
ATOM   986  C C   . LEU B 2 89  ? -19.280 2.103   -24.756 1.00 33.45 ? 98  LEU B C   1 
ATOM   987  O O   . LEU B 2 89  ? -19.636 2.543   -23.638 1.00 30.73 ? 98  LEU B O   1 
ATOM   988  C CB  . LEU B 2 89  ? -21.376 0.655   -24.912 1.00 34.38 ? 98  LEU B CB  1 
ATOM   989  C CG  . LEU B 2 89  ? -22.408 1.735   -25.324 1.00 38.61 ? 98  LEU B CG  1 
ATOM   990  C CD1 . LEU B 2 89  ? -22.303 2.095   -26.807 1.00 42.11 ? 98  LEU B CD1 1 
ATOM   991  C CD2 . LEU B 2 89  ? -23.797 1.277   -24.930 1.00 40.18 ? 98  LEU B CD2 1 
ATOM   992  N N   . ALA B 2 90  ? -18.222 2.576   -25.430 1.00 33.27 ? 99  ALA B N   1 
ATOM   993  C CA  . ALA B 2 90  ? -17.432 3.720   -24.999 1.00 34.31 ? 99  ALA B CA  1 
ATOM   994  C C   . ALA B 2 90  ? -18.188 5.004   -25.104 1.00 33.33 ? 99  ALA B C   1 
ATOM   995  O O   . ALA B 2 90  ? -18.684 5.371   -26.176 1.00 33.07 ? 99  ALA B O   1 
ATOM   996  C CB  . ALA B 2 90  ? -16.143 3.827   -25.817 1.00 35.11 ? 99  ALA B CB  1 
ATOM   997  N N   . VAL B 2 91  ? -18.231 5.766   -24.013 1.00 32.55 ? 100 VAL B N   1 
ATOM   998  C CA  . VAL B 2 91  ? -18.846 7.066   -23.993 1.00 31.79 ? 100 VAL B CA  1 
ATOM   999  C C   . VAL B 2 91  ? -17.782 8.087   -23.619 1.00 33.54 ? 100 VAL B C   1 
ATOM   1000 O O   . VAL B 2 91  ? -17.690 8.466   -22.483 1.00 31.80 ? 100 VAL B O   1 
ATOM   1001 C CB  . VAL B 2 91  ? -20.101 7.158   -23.084 1.00 32.68 ? 100 VAL B CB  1 
ATOM   1002 C CG1 . VAL B 2 91  ? -20.796 8.526   -23.199 1.00 33.36 ? 100 VAL B CG1 1 
ATOM   1003 C CG2 . VAL B 2 91  ? -21.088 6.032   -23.377 1.00 33.38 ? 100 VAL B CG2 1 
ATOM   1004 N N   . PRO B 2 92  ? -16.923 8.530   -24.556 1.00 34.65 ? 101 PRO B N   1 
ATOM   1005 C CA  . PRO B 2 92  ? -15.846 9.475   -24.206 1.00 34.15 ? 101 PRO B CA  1 
ATOM   1006 C C   . PRO B 2 92  ? -16.308 10.899  -23.980 1.00 33.06 ? 101 PRO B C   1 
ATOM   1007 O O   . PRO B 2 92  ? -17.331 11.326  -24.553 1.00 33.72 ? 101 PRO B O   1 
ATOM   1008 C CB  . PRO B 2 92  ? -14.913 9.428   -25.444 1.00 37.00 ? 101 PRO B CB  1 
ATOM   1009 C CG  . PRO B 2 92  ? -15.405 8.278   -26.279 1.00 38.16 ? 101 PRO B CG  1 
ATOM   1010 C CD  . PRO B 2 92  ? -16.876 8.174   -25.979 1.00 36.40 ? 101 PRO B CD  1 
ATOM   1011 N N   . PRO B 2 93  ? -15.543 11.689  -23.216 1.00 33.04 ? 102 PRO B N   1 
ATOM   1012 C CA  . PRO B 2 93  ? -15.972 13.079  -22.952 1.00 33.65 ? 102 PRO B CA  1 
ATOM   1013 C C   . PRO B 2 93  ? -16.145 13.881  -24.255 1.00 35.48 ? 102 PRO B C   1 
ATOM   1014 O O   . PRO B 2 93  ? -15.294 13.766  -25.150 1.00 36.96 ? 102 PRO B O   1 
ATOM   1015 C CB  . PRO B 2 93  ? -14.817 13.636  -22.112 1.00 35.00 ? 102 PRO B CB  1 
ATOM   1016 C CG  . PRO B 2 93  ? -14.341 12.421  -21.321 1.00 35.18 ? 102 PRO B CG  1 
ATOM   1017 C CD  . PRO B 2 93  ? -14.387 11.307  -22.364 1.00 33.53 ? 102 PRO B CD  1 
ATOM   1018 N N   . GLY B 2 94  ? -17.300 14.518  -24.398 1.00 36.15 ? 103 GLY B N   1 
ATOM   1019 C CA  . GLY B 2 94  ? -17.630 15.349  -25.572 1.00 36.24 ? 103 GLY B CA  1 
ATOM   1020 C C   . GLY B 2 94  ? -17.864 14.612  -26.872 1.00 37.16 ? 103 GLY B C   1 
ATOM   1021 O O   . GLY B 2 94  ? -17.954 15.249  -27.931 1.00 37.77 ? 103 GLY B O   1 
ATOM   1022 N N   . GLU B 2 95  ? -17.904 13.263  -26.820 1.00 36.97 ? 104 GLU B N   1 
ATOM   1023 C CA  . GLU B 2 95  ? -18.009 12.429  -28.019 1.00 37.71 ? 104 GLU B CA  1 
ATOM   1024 C C   . GLU B 2 95  ? -19.181 11.466  -27.995 1.00 38.46 ? 104 GLU B C   1 
ATOM   1025 O O   . GLU B 2 95  ? -19.625 11.066  -26.929 1.00 35.88 ? 104 GLU B O   1 
ATOM   1026 C CB  . GLU B 2 95  ? -16.681 11.678  -28.295 1.00 40.26 ? 104 GLU B CB  1 
ATOM   1027 C CG  . GLU B 2 95  ? -15.479 12.604  -28.453 1.00 42.39 ? 104 GLU B CG  1 
ATOM   1028 C CD  . GLU B 2 95  ? -14.131 11.928  -28.658 1.00 44.09 ? 104 GLU B CD  1 
ATOM   1029 O OE1 . GLU B 2 95  ? -14.058 10.683  -28.527 1.00 42.22 ? 104 GLU B OE1 1 
ATOM   1030 O OE2 . GLU B 2 95  ? -13.157 12.641  -29.020 1.00 44.78 ? 104 GLU B OE2 1 
ATOM   1031 N N   . ARG B 2 96  ? -19.729 11.124  -29.171 1.00 39.06 ? 105 ARG B N   1 
ATOM   1032 C CA  . ARG B 2 96  ? -20.880 10.206  -29.245 1.00 40.72 ? 105 ARG B CA  1 
ATOM   1033 C C   . ARG B 2 96  ? -20.575 8.825   -28.691 1.00 39.38 ? 105 ARG B C   1 
ATOM   1034 O O   . ARG B 2 96  ? -19.440 8.353   -28.853 1.00 39.82 ? 105 ARG B O   1 
ATOM   1035 C CB  . ARG B 2 96  ? -21.268 9.997   -30.722 1.00 44.94 ? 105 ARG B CB  1 
ATOM   1036 C CG  . ARG B 2 96  ? -22.706 9.493   -30.891 1.00 52.51 ? 105 ARG B CG  1 
ATOM   1037 C CD  . ARG B 2 96  ? -23.449 10.137  -32.058 1.00 58.39 ? 105 ARG B CD  1 
ATOM   1038 N NE  . ARG B 2 96  ? -22.658 10.198  -33.286 1.00 65.44 ? 105 ARG B NE  1 
ATOM   1039 C CZ  . ARG B 2 96  ? -22.436 11.315  -33.978 1.00 69.32 ? 105 ARG B CZ  1 
ATOM   1040 N NH1 . ARG B 2 96  ? -22.939 12.472  -33.564 1.00 68.43 ? 105 ARG B NH1 1 
ATOM   1041 N NH2 . ARG B 2 96  ? -21.710 11.282  -35.090 1.00 70.50 ? 105 ARG B NH2 1 
ATOM   1042 N N   . ALA B 2 97  ? -21.601 8.129   -28.078 1.00 37.72 ? 106 ALA B N   1 
ATOM   1043 C CA  . ALA B 2 97  ? -21.428 6.720   -27.623 1.00 37.82 ? 106 ALA B CA  1 
ATOM   1044 C C   . ALA B 2 97  ? -21.065 5.868   -28.876 1.00 38.26 ? 106 ALA B C   1 
ATOM   1045 O O   . ALA B 2 97  ? -21.626 6.105   -29.969 1.00 39.56 ? 106 ALA B O   1 
ATOM   1046 C CB  . ALA B 2 97  ? -22.735 6.217   -27.015 1.00 38.55 ? 106 ALA B CB  1 
ATOM   1047 N N   . LYS B 2 98  ? -20.082 4.990   -28.743 1.00 37.04 ? 107 LYS B N   1 
ATOM   1048 C CA  . LYS B 2 98  ? -19.550 4.181   -29.854 1.00 39.76 ? 107 LYS B CA  1 
ATOM   1049 C C   . LYS B 2 98  ? -19.248 2.787   -29.385 1.00 39.67 ? 107 LYS B C   1 
ATOM   1050 O O   . LYS B 2 98  ? -18.577 2.608   -28.345 1.00 40.00 ? 107 LYS B O   1 
ATOM   1051 C CB  . LYS B 2 98  ? -18.246 4.842   -30.313 1.00 45.05 ? 107 LYS B CB  1 
ATOM   1052 C CG  . LYS B 2 98  ? -17.513 4.228   -31.507 1.00 53.71 ? 107 LYS B CG  1 
ATOM   1053 C CD  . LYS B 2 98  ? -16.182 4.988   -31.737 1.00 61.68 ? 107 LYS B CD  1 
ATOM   1054 C CE  . LYS B 2 98  ? -15.401 5.179   -30.432 1.00 67.15 ? 107 LYS B CE  1 
ATOM   1055 N NZ  . LYS B 2 98  ? -13.929 5.010   -30.599 1.00 70.37 ? 107 LYS B NZ  1 
ATOM   1056 N N   . ASN B 2 99  ? -19.744 1.781   -30.111 1.00 37.60 ? 108 ASN B N   1 
ATOM   1057 C CA  . ASN B 2 99  ? -19.466 0.383   -29.815 1.00 38.73 ? 108 ASN B CA  1 
ATOM   1058 C C   . ASN B 2 99  ? -18.140 -0.040  -30.414 1.00 39.43 ? 108 ASN B C   1 
ATOM   1059 O O   . ASN B 2 99  ? -17.912 0.164   -31.623 1.00 41.05 ? 108 ASN B O   1 
ATOM   1060 C CB  . ASN B 2 99  ? -20.551 -0.591  -30.302 1.00 40.85 ? 108 ASN B CB  1 
ATOM   1061 C CG  . ASN B 2 99  ? -21.909 -0.459  -29.673 1.00 44.04 ? 108 ASN B CG  1 
ATOM   1062 O OD1 . ASN B 2 99  ? -22.617 0.537   -29.888 1.00 47.68 ? 108 ASN B OD1 1 
ATOM   1063 N ND2 . ASN B 2 99  ? -22.329 -1.473  -28.913 1.00 40.49 ? 108 ASN B ND2 1 
ATOM   1064 N N   . ILE B 2 100 ? -17.284 -0.685  -29.604 1.00 38.59 ? 109 ILE B N   1 
ATOM   1065 C CA  . ILE B 2 100 ? -15.994 -1.196  -30.011 1.00 39.26 ? 109 ILE B CA  1 
ATOM   1066 C C   . ILE B 2 100 ? -15.939 -2.671  -29.665 1.00 38.93 ? 109 ILE B C   1 
ATOM   1067 O O   . ILE B 2 100 ? -15.983 -3.042  -28.484 1.00 38.75 ? 109 ILE B O   1 
ATOM   1068 C CB  . ILE B 2 100 ? -14.804 -0.446  -29.379 1.00 41.75 ? 109 ILE B CB  1 
ATOM   1069 C CG1 . ILE B 2 100 ? -14.945 1.068   -29.503 1.00 44.79 ? 109 ILE B CG1 1 
ATOM   1070 C CG2 . ILE B 2 100 ? -13.478 -0.952  -29.933 1.00 43.20 ? 109 ILE B CG2 1 
ATOM   1071 C CD1 . ILE B 2 100 ? -14.851 1.578   -30.913 1.00 46.82 ? 109 ILE B CD1 1 
ATOM   1072 N N   . GLN B 2 101 ? -15.739 -3.542  -30.663 1.00 39.32 ? 110 GLN B N   1 
ATOM   1073 C CA  . GLN B 2 101 ? -15.683 -4.979  -30.441 1.00 40.09 ? 110 GLN B CA  1 
ATOM   1074 C C   . GLN B 2 101 ? -14.249 -5.464  -30.209 1.00 42.25 ? 110 GLN B C   1 
ATOM   1075 O O   . GLN B 2 101 ? -13.321 -5.000  -30.882 1.00 44.43 ? 110 GLN B O   1 
ATOM   1076 C CB  . GLN B 2 101 ? -16.296 -5.680  -31.681 1.00 41.73 ? 110 GLN B CB  1 
ATOM   1077 C CG  . GLN B 2 101 ? -16.418 -7.184  -31.470 1.00 42.75 ? 110 GLN B CG  1 
ATOM   1078 C CD  . GLN B 2 101 ? -17.413 -7.759  -32.444 1.00 46.35 ? 110 GLN B CD  1 
ATOM   1079 O OE1 . GLN B 2 101 ? -18.428 -7.158  -32.786 1.00 45.68 ? 110 GLN B OE1 1 
ATOM   1080 N NE2 . GLN B 2 101 ? -17.102 -8.959  -32.919 1.00 48.09 ? 110 GLN B NE2 1 
ATOM   1081 N N   . THR B 2 102 ? -14.051 -6.412  -29.267 1.00 39.56 ? 111 THR B N   1 
ATOM   1082 C CA  . THR B 2 102 ? -12.730 -6.850  -28.929 1.00 39.87 ? 111 THR B CA  1 
ATOM   1083 C C   . THR B 2 102 ? -12.773 -8.236  -28.305 1.00 39.90 ? 111 THR B C   1 
ATOM   1084 O O   . THR B 2 102 ? -13.825 -8.612  -27.777 1.00 40.37 ? 111 THR B O   1 
ATOM   1085 C CB  . THR B 2 102 ? -12.051 -5.824  -27.976 1.00 40.47 ? 111 THR B CB  1 
ATOM   1086 O OG1 . THR B 2 102 ? -10.639 -6.061  -27.943 1.00 41.51 ? 111 THR B OG1 1 
ATOM   1087 C CG2 . THR B 2 102 ? -12.606 -5.878  -26.518 1.00 40.19 ? 111 THR B CG2 1 
ATOM   1088 N N   . LEU B 2 103 ? -11.654 -8.991  -28.329 1.00 39.29 ? 112 LEU B N   1 
ATOM   1089 C CA  . LEU B 2 103 ? -11.621 -10.257 -27.625 1.00 38.89 ? 112 LEU B CA  1 
ATOM   1090 C C   . LEU B 2 103 ? -10.882 -9.973  -26.332 1.00 39.79 ? 112 LEU B C   1 
ATOM   1091 O O   . LEU B 2 103 ? -9.695  -9.598  -26.340 1.00 41.04 ? 112 LEU B O   1 
ATOM   1092 C CB  . LEU B 2 103 ? -10.859 -11.395 -28.411 1.00 39.66 ? 112 LEU B CB  1 
ATOM   1093 C CG  . LEU B 2 103 ? -10.810 -12.669 -27.600 1.00 42.22 ? 112 LEU B CG  1 
ATOM   1094 C CD1 . LEU B 2 103 ? -12.131 -13.388 -27.644 1.00 42.28 ? 112 LEU B CD1 1 
ATOM   1095 C CD2 . LEU B 2 103 ? -9.665  -13.582 -28.083 1.00 45.30 ? 112 LEU B CD2 1 
ATOM   1096 N N   . PRO B 2 104 ? -11.528 -10.187 -25.135 1.00 38.12 ? 113 PRO B N   1 
ATOM   1097 C CA  . PRO B 2 104 ? -10.827 -9.876  -23.899 1.00 37.62 ? 113 PRO B CA  1 
ATOM   1098 C C   . PRO B 2 104 ? -9.642  -10.775 -23.687 1.00 39.90 ? 113 PRO B C   1 
ATOM   1099 O O   . PRO B 2 104 ? -9.646  -11.947 -24.110 1.00 41.34 ? 113 PRO B O   1 
ATOM   1100 C CB  . PRO B 2 104 ? -11.875 -10.163 -22.796 1.00 37.50 ? 113 PRO B CB  1 
ATOM   1101 C CG  . PRO B 2 104 ? -13.270 -10.023 -23.489 1.00 36.62 ? 113 PRO B CG  1 
ATOM   1102 C CD  . PRO B 2 104 ? -12.907 -10.656 -24.907 1.00 37.07 ? 113 PRO B CD  1 
ATOM   1103 N N   . GLY B 2 105 ? -8.672  -10.228 -22.963 1.00 37.75 ? 114 GLY B N   1 
ATOM   1104 C CA  . GLY B 2 105 ? -7.573  -10.960 -22.360 1.00 37.44 ? 114 GLY B CA  1 
ATOM   1105 C C   . GLY B 2 105 ? -8.024  -11.338 -20.962 1.00 38.76 ? 114 GLY B C   1 
ATOM   1106 O O   . GLY B 2 105 ? -9.232  -11.363 -20.650 1.00 39.11 ? 114 GLY B O   1 
ATOM   1107 N N   . ILE B 2 106 ? -7.063  -11.645 -20.126 1.00 38.33 ? 115 ILE B N   1 
ATOM   1108 C CA  . ILE B 2 106 ? -7.360  -12.129 -18.786 1.00 39.26 ? 115 ILE B CA  1 
ATOM   1109 C C   . ILE B 2 106 ? -6.434  -11.544 -17.754 1.00 38.38 ? 115 ILE B C   1 
ATOM   1110 O O   . ILE B 2 106 ? -5.219  -11.551 -17.925 1.00 41.16 ? 115 ILE B O   1 
ATOM   1111 C CB  . ILE B 2 106 ? -7.287  -13.704 -18.752 1.00 42.64 ? 115 ILE B CB  1 
ATOM   1112 C CG1 . ILE B 2 106 ? -8.391  -14.352 -19.630 1.00 44.97 ? 115 ILE B CG1 1 
ATOM   1113 C CG2 . ILE B 2 106 ? -7.274  -14.309 -17.354 1.00 44.05 ? 115 ILE B CG2 1 
ATOM   1114 C CD1 . ILE B 2 106 ? -8.135  -15.802 -19.913 1.00 48.12 ? 115 ILE B CD1 1 
ATOM   1115 N N   . PHE B 2 107 ? -6.981  -11.163 -16.601 1.00 36.24 ? 116 PHE B N   1 
ATOM   1116 C CA  . PHE B 2 107 ? -6.152  -10.807 -15.444 1.00 36.69 ? 116 PHE B CA  1 
ATOM   1117 C C   . PHE B 2 107 ? -6.141  -12.076 -14.600 1.00 38.37 ? 116 PHE B C   1 
ATOM   1118 O O   . PHE B 2 107 ? -7.206  -12.515 -14.161 1.00 38.79 ? 116 PHE B O   1 
ATOM   1119 C CB  . PHE B 2 107 ? -6.839  -9.708  -14.591 1.00 36.17 ? 116 PHE B CB  1 
ATOM   1120 C CG  . PHE B 2 107 ? -6.626  -8.267  -14.998 1.00 36.47 ? 116 PHE B CG  1 
ATOM   1121 C CD1 . PHE B 2 107 ? -5.876  -7.944  -16.118 1.00 36.83 ? 116 PHE B CD1 1 
ATOM   1122 C CD2 . PHE B 2 107 ? -7.184  -7.232  -14.260 1.00 36.51 ? 116 PHE B CD2 1 
ATOM   1123 C CE1 . PHE B 2 107 ? -5.718  -6.613  -16.508 1.00 36.48 ? 116 PHE B CE1 1 
ATOM   1124 C CE2 . PHE B 2 107 ? -7.010  -5.905  -14.644 1.00 36.67 ? 116 PHE B CE2 1 
ATOM   1125 C CZ  . PHE B 2 107 ? -6.258  -5.598  -15.737 1.00 36.60 ? 116 PHE B CZ  1 
ATOM   1126 N N   . LYS B 2 108 ? -4.952  -12.622 -14.276 1.00 38.66 ? 117 LYS B N   1 
ATOM   1127 C CA  . LYS B 2 108 ? -4.849  -13.780 -13.401 1.00 39.65 ? 117 LYS B CA  1 
ATOM   1128 C C   . LYS B 2 108 ? -4.473  -13.295 -12.014 1.00 40.23 ? 117 LYS B C   1 
ATOM   1129 O O   . LYS B 2 108 ? -3.455  -12.633 -11.868 1.00 40.51 ? 117 LYS B O   1 
ATOM   1130 C CB  . LYS B 2 108 ? -3.736  -14.718 -13.925 1.00 43.15 ? 117 LYS B CB  1 
ATOM   1131 C CG  . LYS B 2 108 ? -4.027  -15.257 -15.325 1.00 51.22 ? 117 LYS B CG  1 
ATOM   1132 C CD  . LYS B 2 108 ? -2.776  -15.848 -16.020 1.00 59.59 ? 117 LYS B CD  1 
ATOM   1133 C CE  . LYS B 2 108 ? -3.117  -17.077 -16.848 1.00 67.47 ? 117 LYS B CE  1 
ATOM   1134 N NZ  . LYS B 2 108 ? -2.098  -17.397 -17.907 1.00 71.86 ? 117 LYS B NZ  1 
ATOM   1135 N N   . THR B 2 109 ? -5.294  -13.585 -11.017 1.00 39.87 ? 118 THR B N   1 
ATOM   1136 C CA  . THR B 2 109 ? -5.016  -13.131 -9.649  1.00 40.86 ? 118 THR B CA  1 
ATOM   1137 C C   . THR B 2 109 ? -4.949  -14.324 -8.666  1.00 43.18 ? 118 THR B C   1 
ATOM   1138 O O   . THR B 2 109 ? -5.428  -15.411 -9.006  1.00 43.66 ? 118 THR B O   1 
ATOM   1139 C CB  . THR B 2 109 ? -6.077  -12.090 -9.158  1.00 41.80 ? 118 THR B CB  1 
ATOM   1140 O OG1 . THR B 2 109 ? -7.229  -12.777 -8.652  1.00 42.89 ? 118 THR B OG1 1 
ATOM   1141 C CG2 . THR B 2 109 ? -6.471  -11.050 -10.223 1.00 40.75 ? 118 THR B CG2 1 
ATOM   1142 N N   . LYS B 2 110 ? -4.517  -14.078 -7.417  1.00 44.24 ? 119 LYS B N   1 
ATOM   1143 C CA  . LYS B 2 110 ? -4.481  -15.151 -6.417  1.00 45.77 ? 119 LYS B CA  1 
ATOM   1144 C C   . LYS B 2 110 ? -5.900  -15.673 -6.078  1.00 48.12 ? 119 LYS B C   1 
ATOM   1145 O O   . LYS B 2 110 ? -6.037  -16.791 -5.559  1.00 49.78 ? 119 LYS B O   1 
ATOM   1146 C CB  . LYS B 2 110 ? -3.750  -14.687 -5.149  1.00 45.71 ? 119 LYS B CB  1 
ATOM   1147 C CG  . LYS B 2 110 ? -4.435  -13.510 -4.472  1.00 49.02 ? 119 LYS B CG  1 
ATOM   1148 C CD  . LYS B 2 110 ? -3.707  -13.097 -3.205  1.00 53.46 ? 119 LYS B CD  1 
ATOM   1149 C CE  . LYS B 2 110 ? -4.387  -11.976 -2.476  1.00 56.73 ? 119 LYS B CE  1 
ATOM   1150 N NZ  . LYS B 2 110 ? -5.680  -12.394 -1.887  1.00 58.54 ? 119 LYS B NZ  1 
ATOM   1151 N N   . ASP B 2 111 ? -6.937  -14.882 -6.380  1.00 47.26 ? 120 ASP B N   1 
ATOM   1152 C CA  . ASP B 2 111 ? -8.325  -15.222 -6.114  1.00 48.26 ? 120 ASP B CA  1 
ATOM   1153 C C   . ASP B 2 111 ? -9.134  -15.597 -7.335  1.00 49.00 ? 120 ASP B C   1 
ATOM   1154 O O   . ASP B 2 111 ? -10.360 -15.637 -7.240  1.00 50.73 ? 120 ASP B O   1 
ATOM   1155 C CB  . ASP B 2 111 ? -9.021  -14.061 -5.395  1.00 49.95 ? 120 ASP B CB  1 
ATOM   1156 C CG  . ASP B 2 111 ? -8.448  -13.820 -4.027  1.00 55.15 ? 120 ASP B CG  1 
ATOM   1157 O OD1 . ASP B 2 111 ? -8.243  -14.814 -3.286  1.00 56.67 ? 120 ASP B OD1 1 
ATOM   1158 O OD2 . ASP B 2 111 ? -8.181  -12.645 -3.697  1.00 56.42 ? 120 ASP B OD2 1 
ATOM   1159 N N   . GLY B 2 112 ? -8.484  -15.853 -8.461  1.00 47.40 ? 121 GLY B N   1 
ATOM   1160 C CA  . GLY B 2 112 ? -9.196  -16.218 -9.671  1.00 46.09 ? 121 GLY B CA  1 
ATOM   1161 C C   . GLY B 2 112 ? -8.892  -15.302 -10.832 1.00 44.84 ? 121 GLY B C   1 
ATOM   1162 O O   . GLY B 2 112 ? -8.233  -14.272 -10.677 1.00 44.20 ? 121 GLY B O   1 
ATOM   1163 N N   . ASP B 2 113 ? -9.357  -15.706 -12.004 1.00 43.31 ? 122 ASP B N   1 
ATOM   1164 C CA  . ASP B 2 113 ? -9.173  -14.980 -13.252 1.00 41.91 ? 122 ASP B CA  1 
ATOM   1165 C C   . ASP B 2 113 ? -10.380 -14.111 -13.575 1.00 41.09 ? 122 ASP B C   1 
ATOM   1166 O O   . ASP B 2 113 ? -11.508 -14.475 -13.260 1.00 41.73 ? 122 ASP B O   1 
ATOM   1167 C CB  . ASP B 2 113 ? -8.896  -15.958 -14.397 1.00 44.90 ? 122 ASP B CB  1 
ATOM   1168 C CG  . ASP B 2 113 ? -7.601  -16.757 -14.234 1.00 52.30 ? 122 ASP B CG  1 
ATOM   1169 O OD1 . ASP B 2 113 ? -6.899  -16.551 -13.230 1.00 54.25 ? 122 ASP B OD1 1 
ATOM   1170 O OD2 . ASP B 2 113 ? -7.296  -17.568 -15.116 1.00 57.77 ? 122 ASP B OD2 1 
ATOM   1171 N N   . ILE B 2 114 ? -10.105 -12.956 -14.194 1.00 38.11 ? 123 ILE B N   1 
ATOM   1172 C CA  . ILE B 2 114 ? -11.105 -11.968 -14.585 1.00 38.70 ? 123 ILE B CA  1 
ATOM   1173 C C   . ILE B 2 114 ? -10.826 -11.605 -16.059 1.00 37.46 ? 123 ILE B C   1 
ATOM   1174 O O   . ILE B 2 114 ? -9.669  -11.468 -16.423 1.00 37.32 ? 123 ILE B O   1 
ATOM   1175 C CB  . ILE B 2 114 ? -10.936 -10.673 -13.672 1.00 40.28 ? 123 ILE B CB  1 
ATOM   1176 C CG1 . ILE B 2 114 ? -10.602 -10.998 -12.164 1.00 43.26 ? 123 ILE B CG1 1 
ATOM   1177 C CG2 . ILE B 2 114 ? -12.131 -9.756  -13.788 1.00 43.34 ? 123 ILE B CG2 1 
ATOM   1178 C CD1 . ILE B 2 114 ? -10.298 -9.700  -11.308 1.00 45.85 ? 123 ILE B CD1 1 
ATOM   1179 N N   . GLY B 2 115 ? -11.862 -11.367 -16.880 1.00 35.71 ? 124 GLY B N   1 
ATOM   1180 C CA  . GLY B 2 115 ? -11.631 -10.877 -18.237 1.00 35.13 ? 124 GLY B CA  1 
ATOM   1181 C C   . GLY B 2 115 ? -11.075 -9.463  -18.187 1.00 34.90 ? 124 GLY B C   1 
ATOM   1182 O O   . GLY B 2 115 ? -11.261 -8.746  -17.194 1.00 33.56 ? 124 GLY B O   1 
ATOM   1183 N N   . ALA B 2 116 ? -10.375 -9.041  -19.232 1.00 34.49 ? 125 ALA B N   1 
ATOM   1184 C CA  . ALA B 2 116 ? -9.799  -7.701  -19.294 1.00 34.74 ? 125 ALA B CA  1 
ATOM   1185 C C   . ALA B 2 116 ? -9.828  -7.163  -20.716 1.00 35.85 ? 125 ALA B C   1 
ATOM   1186 O O   . ALA B 2 116 ? -9.610  -7.930  -21.651 1.00 38.98 ? 125 ALA B O   1 
ATOM   1187 C CB  . ALA B 2 116 ? -8.367  -7.738  -18.760 1.00 36.90 ? 125 ALA B CB  1 
ATOM   1188 N N   . VAL B 2 117 ? -10.038 -5.874  -20.903 1.00 35.33 ? 126 VAL B N   1 
ATOM   1189 C CA  . VAL B 2 117 ? -10.157 -5.276  -22.228 1.00 37.46 ? 126 VAL B CA  1 
ATOM   1190 C C   . VAL B 2 117 ? -9.019  -4.274  -22.487 1.00 38.15 ? 126 VAL B C   1 
ATOM   1191 O O   . VAL B 2 117 ? -8.759  -3.369  -21.678 1.00 36.68 ? 126 VAL B O   1 
ATOM   1192 C CB  . VAL B 2 117 ? -11.600 -4.702  -22.341 1.00 41.66 ? 126 VAL B CB  1 
ATOM   1193 C CG1 . VAL B 2 117 ? -11.704 -3.493  -23.242 1.00 44.86 ? 126 VAL B CG1 1 
ATOM   1194 C CG2 . VAL B 2 117 ? -12.582 -5.795  -22.750 1.00 41.54 ? 126 VAL B CG2 1 
ATOM   1195 N N   . ALA B 2 118 ? -8.255  -4.497  -23.612 1.00 37.47 ? 127 ALA B N   1 
ATOM   1196 C CA  . ALA B 2 118 ? -7.099  -3.669  -23.905 1.00 39.47 ? 127 ALA B CA  1 
ATOM   1197 C C   . ALA B 2 118 ? -7.476  -2.560  -24.875 1.00 40.82 ? 127 ALA B C   1 
ATOM   1198 O O   . ALA B 2 118 ? -7.178  -2.612  -26.091 1.00 41.41 ? 127 ALA B O   1 
ATOM   1199 C CB  . ALA B 2 118 ? -5.935  -4.535  -24.435 1.00 40.95 ? 127 ALA B CB  1 
ATOM   1200 N N   . LEU B 2 119 ? -8.234  -1.561  -24.356 1.00 39.39 ? 128 LEU B N   1 
ATOM   1201 C CA  . LEU B 2 119 ? -8.696  -0.436  -25.136 1.00 38.72 ? 128 LEU B CA  1 
ATOM   1202 C C   . LEU B 2 119 ? -8.365  0.820   -24.354 1.00 41.31 ? 128 LEU B C   1 
ATOM   1203 O O   . LEU B 2 119 ? -8.561  0.856   -23.124 1.00 40.47 ? 128 LEU B O   1 
ATOM   1204 C CB  . LEU B 2 119 ? -10.210 -0.537  -25.427 1.00 38.90 ? 128 LEU B CB  1 
ATOM   1205 C CG  . LEU B 2 119 ? -10.637 -1.766  -26.237 1.00 40.56 ? 128 LEU B CG  1 
ATOM   1206 C CD1 . LEU B 2 119 ? -12.139 -1.907  -26.278 1.00 41.70 ? 128 LEU B CD1 1 
ATOM   1207 C CD2 . LEU B 2 119 ? -10.115 -1.690  -27.657 1.00 40.04 ? 128 LEU B CD2 1 
ATOM   1208 N N   . ASP B 2 120 ? -7.886  1.857   -25.051 1.00 42.81 ? 129 ASP B N   1 
ATOM   1209 C CA  . ASP B 2 120 ? -7.450  3.095   -24.434 1.00 44.59 ? 129 ASP B CA  1 
ATOM   1210 C C   . ASP B 2 120 ? -8.374  4.284   -24.686 1.00 43.12 ? 129 ASP B C   1 
ATOM   1211 O O   . ASP B 2 120 ? -8.618  4.684   -25.826 1.00 42.59 ? 129 ASP B O   1 
ATOM   1212 C CB  . ASP B 2 120 ? -6.023  3.413   -24.899 1.00 51.27 ? 129 ASP B CB  1 
ATOM   1213 C CG  . ASP B 2 120 ? -5.015  2.386   -24.411 1.00 61.77 ? 129 ASP B CG  1 
ATOM   1214 O OD1 . ASP B 2 120 ? -4.054  2.778   -23.720 1.00 62.96 ? 129 ASP B OD1 1 
ATOM   1215 O OD2 . ASP B 2 120 ? -5.199  1.183   -24.699 1.00 67.40 ? 129 ASP B OD2 1 
ATOM   1216 N N   . TYR B 2 121 ? -8.877  4.881   -23.606 1.00 40.62 ? 130 TYR B N   1 
ATOM   1217 C CA  . TYR B 2 121 ? -9.755  6.040   -23.668 1.00 39.57 ? 130 TYR B CA  1 
ATOM   1218 C C   . TYR B 2 121 ? -9.420  7.054   -22.552 1.00 39.23 ? 130 TYR B C   1 
ATOM   1219 O O   . TYR B 2 121 ? -8.792  6.648   -21.557 1.00 39.91 ? 130 TYR B O   1 
ATOM   1220 C CB  . TYR B 2 121 ? -11.228 5.575   -23.520 1.00 39.77 ? 130 TYR B CB  1 
ATOM   1221 C CG  . TYR B 2 121 ? -11.811 5.025   -24.797 1.00 40.62 ? 130 TYR B CG  1 
ATOM   1222 C CD1 . TYR B 2 121 ? -12.332 5.873   -25.771 1.00 42.10 ? 130 TYR B CD1 1 
ATOM   1223 C CD2 . TYR B 2 121 ? -11.849 3.662   -25.034 1.00 41.98 ? 130 TYR B CD2 1 
ATOM   1224 C CE1 . TYR B 2 121 ? -12.890 5.370   -26.931 1.00 43.11 ? 130 TYR B CE1 1 
ATOM   1225 C CE2 . TYR B 2 121 ? -12.329 3.150   -26.228 1.00 43.48 ? 130 TYR B CE2 1 
ATOM   1226 C CZ  . TYR B 2 121 ? -12.836 4.011   -27.184 1.00 45.14 ? 130 TYR B CZ  1 
ATOM   1227 O OH  . TYR B 2 121 ? -13.336 3.530   -28.366 1.00 49.17 ? 130 TYR B OH  1 
ATOM   1228 N N   . PRO B 2 122 ? -9.900  8.320   -22.649 1.00 38.78 ? 131 PRO B N   1 
ATOM   1229 C CA  . PRO B 2 122 ? -9.685  9.283   -21.552 1.00 38.37 ? 131 PRO B CA  1 
ATOM   1230 C C   . PRO B 2 122 ? -10.313 8.770   -20.249 1.00 37.09 ? 131 PRO B C   1 
ATOM   1231 O O   . PRO B 2 122 ? -11.233 7.940   -20.278 1.00 35.69 ? 131 PRO B O   1 
ATOM   1232 C CB  . PRO B 2 122 ? -10.436 10.536  -22.020 1.00 39.65 ? 131 PRO B CB  1 
ATOM   1233 C CG  . PRO B 2 122 ? -10.487 10.422  -23.553 1.00 39.25 ? 131 PRO B CG  1 
ATOM   1234 C CD  . PRO B 2 122 ? -10.638 8.934   -23.786 1.00 37.59 ? 131 PRO B CD  1 
ATOM   1235 N N   . ALA B 2 123 ? -9.744  9.197   -19.110 1.00 36.77 ? 132 ALA B N   1 
ATOM   1236 C CA  . ALA B 2 123 ? -10.193 8.788   -17.783 1.00 35.60 ? 132 ALA B CA  1 
ATOM   1237 C C   . ALA B 2 123 ? -11.703 9.009   -17.524 1.00 33.94 ? 132 ALA B C   1 
ATOM   1238 O O   . ALA B 2 123 ? -12.324 8.197   -16.817 1.00 32.39 ? 132 ALA B O   1 
ATOM   1239 C CB  . ALA B 2 123 ? -9.362  9.510   -16.739 1.00 36.60 ? 132 ALA B CB  1 
ATOM   1240 N N   . GLY B 2 124 ? -12.282 10.065  -18.142 1.00 33.47 ? 133 GLY B N   1 
ATOM   1241 C CA  . GLY B 2 124 ? -13.709 10.349  -18.000 1.00 32.40 ? 133 GLY B CA  1 
ATOM   1242 C C   . GLY B 2 124 ? -14.613 9.347   -18.717 1.00 29.68 ? 133 GLY B C   1 
ATOM   1243 O O   . GLY B 2 124 ? -15.836 9.465   -18.632 1.00 30.53 ? 133 GLY B O   1 
ATOM   1244 N N   . THR B 2 125 ? -14.028 8.315   -19.373 1.00 29.25 ? 134 THR B N   1 
ATOM   1245 C CA  . THR B 2 125 ? -14.759 7.212   -20.001 1.00 28.83 ? 134 THR B CA  1 
ATOM   1246 C C   . THR B 2 125 ? -15.075 6.067   -18.969 1.00 30.05 ? 134 THR B C   1 
ATOM   1247 O O   . THR B 2 125 ? -15.801 5.127   -19.273 1.00 29.64 ? 134 THR B O   1 
ATOM   1248 C CB  . THR B 2 125 ? -13.966 6.695   -21.253 1.00 32.81 ? 134 THR B CB  1 
ATOM   1249 O OG1 . THR B 2 125 ? -13.541 7.838   -22.010 1.00 32.84 ? 134 THR B OG1 1 
ATOM   1250 C CG2 . THR B 2 125 ? -14.771 5.774   -22.170 1.00 34.28 ? 134 THR B CG2 1 
ATOM   1251 N N   . SER B 2 126 ? -14.456 6.136   -17.789 1.00 28.43 ? 135 SER B N   1 
ATOM   1252 C CA  . SER B 2 126 ? -14.638 5.104   -16.764 1.00 28.17 ? 135 SER B CA  1 
ATOM   1253 C C   . SER B 2 126 ? -16.105 4.902   -16.421 1.00 27.07 ? 135 SER B C   1 
ATOM   1254 O O   . SER B 2 126 ? -16.788 5.919   -16.246 1.00 27.34 ? 135 SER B O   1 
ATOM   1255 C CB  . SER B 2 126 ? -14.009 5.570   -15.460 1.00 30.78 ? 135 SER B CB  1 
ATOM   1256 O OG  . SER B 2 126 ? -12.615 5.392   -15.458 1.00 34.68 ? 135 SER B OG  1 
ATOM   1257 N N   . GLY B 2 127 ? -16.530 3.635   -16.260 1.00 25.26 ? 136 GLY B N   1 
ATOM   1258 C CA  . GLY B 2 127 ? -17.940 3.361   -16.031 1.00 26.37 ? 136 GLY B CA  1 
ATOM   1259 C C   . GLY B 2 127 ? -18.650 2.929   -17.294 1.00 27.13 ? 136 GLY B C   1 
ATOM   1260 O O   . GLY B 2 127 ? -19.817 2.528   -17.238 1.00 27.57 ? 136 GLY B O   1 
ATOM   1261 N N   . SER B 2 128 ? -17.979 3.095   -18.485 1.00 27.14 ? 137 SER B N   1 
ATOM   1262 C CA  . SER B 2 128 ? -18.637 2.685   -19.720 1.00 27.33 ? 137 SER B CA  1 
ATOM   1263 C C   . SER B 2 128 ? -18.881 1.146   -19.654 1.00 27.38 ? 137 SER B C   1 
ATOM   1264 O O   . SER B 2 128 ? -18.007 0.379   -19.220 1.00 28.30 ? 137 SER B O   1 
ATOM   1265 C CB  . SER B 2 128 ? -17.729 2.990   -20.932 1.00 27.73 ? 137 SER B CB  1 
ATOM   1266 O OG  . SER B 2 128 ? -17.742 4.391   -21.184 1.00 27.65 ? 137 SER B OG  1 
ATOM   1267 N N   . PRO B 2 129 ? -20.044 0.688   -20.138 1.00 27.01 ? 138 PRO B N   1 
ATOM   1268 C CA  . PRO B 2 129 ? -20.341 -0.741  -20.016 1.00 26.86 ? 138 PRO B CA  1 
ATOM   1269 C C   . PRO B 2 129 ? -19.718 -1.617  -21.082 1.00 28.61 ? 138 PRO B C   1 
ATOM   1270 O O   . PRO B 2 129 ? -19.647 -1.202  -22.253 1.00 28.96 ? 138 PRO B O   1 
ATOM   1271 C CB  . PRO B 2 129 ? -21.850 -0.828  -20.170 1.00 29.00 ? 138 PRO B CB  1 
ATOM   1272 C CG  . PRO B 2 129 ? -22.221 0.398   -20.992 1.00 29.64 ? 138 PRO B CG  1 
ATOM   1273 C CD  . PRO B 2 129 ? -21.209 1.474   -20.636 1.00 28.31 ? 138 PRO B CD  1 
ATOM   1274 N N   . ILE B 2 130 ? -19.425 -2.854  -20.699 1.00 28.82 ? 139 ILE B N   1 
ATOM   1275 C CA  . ILE B 2 130 ? -18.933 -3.889  -21.626 1.00 29.66 ? 139 ILE B CA  1 
ATOM   1276 C C   . ILE B 2 130 ? -20.116 -4.864  -21.766 1.00 31.27 ? 139 ILE B C   1 
ATOM   1277 O O   . ILE B 2 130 ? -20.769 -5.238  -20.776 1.00 30.63 ? 139 ILE B O   1 
ATOM   1278 C CB  . ILE B 2 130 ? -17.710 -4.579  -21.002 1.00 30.47 ? 139 ILE B CB  1 
ATOM   1279 C CG1 . ILE B 2 130 ? -16.574 -3.569  -20.821 1.00 33.51 ? 139 ILE B CG1 1 
ATOM   1280 C CG2 . ILE B 2 130 ? -17.264 -5.742  -21.934 1.00 32.04 ? 139 ILE B CG2 1 
ATOM   1281 C CD1 . ILE B 2 130 ? -15.545 -3.915  -19.747 1.00 36.49 ? 139 ILE B CD1 1 
ATOM   1282 N N   . LEU B 2 131 ? -20.444 -5.230  -23.001 1.00 32.71 ? 140 LEU B N   1 
ATOM   1283 C CA  . LEU B 2 131 ? -21.630 -6.022  -23.306 1.00 35.05 ? 140 LEU B CA  1 
ATOM   1284 C C   . LEU B 2 131 ? -21.337 -7.331  -24.005 1.00 35.37 ? 140 LEU B C   1 
ATOM   1285 O O   . LEU B 2 131 ? -20.362 -7.444  -24.766 1.00 36.92 ? 140 LEU B O   1 
ATOM   1286 C CB  . LEU B 2 131 ? -22.570 -5.236  -24.305 1.00 38.10 ? 140 LEU B CB  1 
ATOM   1287 C CG  . LEU B 2 131 ? -22.596 -3.746  -24.218 1.00 42.03 ? 140 LEU B CG  1 
ATOM   1288 C CD1 . LEU B 2 131 ? -23.431 -3.178  -25.342 1.00 43.81 ? 140 LEU B CD1 1 
ATOM   1289 C CD2 . LEU B 2 131 ? -23.096 -3.323  -22.854 1.00 43.79 ? 140 LEU B CD2 1 
ATOM   1290 N N   . ASP B 2 132 ? -22.206 -8.302  -23.774 1.00 34.60 ? 141 ASP B N   1 
ATOM   1291 C CA  . ASP B 2 132 ? -22.154 -9.537  -24.568 1.00 36.19 ? 141 ASP B CA  1 
ATOM   1292 C C   . ASP B 2 132 ? -23.056 -9.418  -25.806 1.00 38.88 ? 141 ASP B C   1 
ATOM   1293 O O   . ASP B 2 132 ? -23.697 -8.378  -26.020 1.00 39.73 ? 141 ASP B O   1 
ATOM   1294 C CB  . ASP B 2 132 ? -22.486 -10.784 -23.750 1.00 37.53 ? 141 ASP B CB  1 
ATOM   1295 C CG  . ASP B 2 132 ? -23.882 -10.881 -23.142 1.00 37.95 ? 141 ASP B CG  1 
ATOM   1296 O OD1 . ASP B 2 132 ? -24.816 -10.213 -23.653 1.00 39.52 ? 141 ASP B OD1 1 
ATOM   1297 O OD2 . ASP B 2 132 ? -24.042 -11.633 -22.190 1.00 39.29 ? 141 ASP B OD2 1 
ATOM   1298 N N   . LYS B 2 133 ? -23.149 -10.518 -26.597 1.00 41.26 ? 142 LYS B N   1 
ATOM   1299 C CA  . LYS B 2 133 ? -23.927 -10.516 -27.833 1.00 43.35 ? 142 LYS B CA  1 
ATOM   1300 C C   . LYS B 2 133 ? -25.429 -10.421 -27.653 1.00 45.92 ? 142 LYS B C   1 
ATOM   1301 O O   . LYS B 2 133 ? -26.147 -10.166 -28.645 1.00 47.49 ? 142 LYS B O   1 
ATOM   1302 C CB  . LYS B 2 133 ? -23.544 -11.755 -28.693 1.00 45.85 ? 142 LYS B CB  1 
ATOM   1303 C CG  . LYS B 2 133 ? -22.085 -11.684 -29.078 1.00 53.67 ? 142 LYS B CG  1 
ATOM   1304 C CD  . LYS B 2 133 ? -21.584 -12.919 -29.867 1.00 61.54 ? 142 LYS B CD  1 
ATOM   1305 C CE  . LYS B 2 133 ? -20.093 -13.098 -29.680 1.00 67.09 ? 142 LYS B CE  1 
ATOM   1306 N NZ  . LYS B 2 133 ? -19.635 -14.482 -30.032 1.00 71.26 ? 142 LYS B NZ  1 
ATOM   1307 N N   . CYS B 2 134 ? -25.929 -10.621 -26.418 1.00 45.99 ? 143 CYS B N   1 
ATOM   1308 C CA  . CYS B 2 134 ? -27.340 -10.420 -26.097 1.00 46.74 ? 143 CYS B CA  1 
ATOM   1309 C C   . CYS B 2 134 ? -27.627 -8.979  -25.622 1.00 45.52 ? 143 CYS B C   1 
ATOM   1310 O O   . CYS B 2 134 ? -28.761 -8.682  -25.237 1.00 46.66 ? 143 CYS B O   1 
ATOM   1311 C CB  . CYS B 2 134 ? -27.809 -11.424 -25.056 1.00 49.82 ? 143 CYS B CB  1 
ATOM   1312 S SG  . CYS B 2 134 ? -27.786 -13.139 -25.633 1.00 58.13 ? 143 CYS B SG  1 
ATOM   1313 N N   . GLY B 2 135 ? -26.606 -8.125  -25.592 1.00 43.02 ? 144 GLY B N   1 
ATOM   1314 C CA  . GLY B 2 135 ? -26.758 -6.759  -25.110 1.00 40.92 ? 144 GLY B CA  1 
ATOM   1315 C C   . GLY B 2 135 ? -26.728 -6.664  -23.597 1.00 39.18 ? 144 GLY B C   1 
ATOM   1316 O O   . GLY B 2 135 ? -27.026 -5.604  -23.053 1.00 38.98 ? 144 GLY B O   1 
ATOM   1317 N N   . ARG B 2 136 ? -26.361 -7.746  -22.897 1.00 36.01 ? 145 ARG B N   1 
ATOM   1318 C CA  . ARG B 2 136 ? -26.284 -7.728  -21.419 1.00 35.74 ? 145 ARG B CA  1 
ATOM   1319 C C   . ARG B 2 136 ? -24.987 -7.150  -20.927 1.00 33.13 ? 145 ARG B C   1 
ATOM   1320 O O   . ARG B 2 136 ? -23.927 -7.465  -21.454 1.00 33.31 ? 145 ARG B O   1 
ATOM   1321 C CB  . ARG B 2 136 ? -26.482 -9.130  -20.832 1.00 39.49 ? 145 ARG B CB  1 
ATOM   1322 C CG  . ARG B 2 136 ? -27.936 -9.616  -20.974 1.00 46.16 ? 145 ARG B CG  1 
ATOM   1323 C CD  . ARG B 2 136 ? -28.065 -11.052 -20.521 1.00 51.66 ? 145 ARG B CD  1 
ATOM   1324 N NE  . ARG B 2 136 ? -27.335 -11.930 -21.424 1.00 60.15 ? 145 ARG B NE  1 
ATOM   1325 C CZ  . ARG B 2 136 ? -26.903 -13.149 -21.121 1.00 64.09 ? 145 ARG B CZ  1 
ATOM   1326 N NH1 . ARG B 2 136 ? -27.080 -13.640 -19.897 1.00 64.24 ? 145 ARG B NH1 1 
ATOM   1327 N NH2 . ARG B 2 136 ? -26.259 -13.873 -22.027 1.00 64.58 ? 145 ARG B NH2 1 
ATOM   1328 N N   . VAL B 2 137 ? -25.048 -6.344  -19.827 1.00 29.87 ? 146 VAL B N   1 
ATOM   1329 C CA  . VAL B 2 137 ? -23.831 -5.727  -19.333 1.00 28.48 ? 146 VAL B CA  1 
ATOM   1330 C C   . VAL B 2 137 ? -23.044 -6.721  -18.497 1.00 29.48 ? 146 VAL B C   1 
ATOM   1331 O O   . VAL B 2 137 ? -23.564 -7.168  -17.498 1.00 30.01 ? 146 VAL B O   1 
ATOM   1332 C CB  . VAL B 2 137 ? -24.162 -4.445  -18.511 1.00 28.74 ? 146 VAL B CB  1 
ATOM   1333 C CG1 . VAL B 2 137 ? -22.887 -3.918  -17.862 1.00 30.17 ? 146 VAL B CG1 1 
ATOM   1334 C CG2 . VAL B 2 137 ? -24.770 -3.371  -19.430 1.00 30.22 ? 146 VAL B CG2 1 
ATOM   1335 N N   . ILE B 2 138 ? -21.841 -7.103  -18.953 1.00 30.68 ? 147 ILE B N   1 
ATOM   1336 C CA  . ILE B 2 138 ? -21.011 -8.082  -18.213 1.00 29.80 ? 147 ILE B CA  1 
ATOM   1337 C C   . ILE B 2 138 ? -20.010 -7.447  -17.280 1.00 28.89 ? 147 ILE B C   1 
ATOM   1338 O O   . ILE B 2 138 ? -19.286 -8.177  -16.574 1.00 29.88 ? 147 ILE B O   1 
ATOM   1339 C CB  . ILE B 2 138 ? -20.310 -9.060  -19.220 1.00 31.42 ? 147 ILE B CB  1 
ATOM   1340 C CG1 . ILE B 2 138 ? -19.508 -8.287  -20.276 1.00 31.71 ? 147 ILE B CG1 1 
ATOM   1341 C CG2 . ILE B 2 138 ? -21.386 -9.897  -19.872 1.00 32.43 ? 147 ILE B CG2 1 
ATOM   1342 C CD1 . ILE B 2 138 ? -18.700 -9.269  -21.290 1.00 32.84 ? 147 ILE B CD1 1 
ATOM   1343 N N   . GLY B 2 139 ? -19.965 -6.108  -17.263 1.00 28.52 ? 148 GLY B N   1 
ATOM   1344 C CA  . GLY B 2 139 ? -19.098 -5.353  -16.352 1.00 27.71 ? 148 GLY B CA  1 
ATOM   1345 C C   . GLY B 2 139 ? -18.885 -3.941  -16.860 1.00 26.27 ? 148 GLY B C   1 
ATOM   1346 O O   . GLY B 2 139 ? -19.386 -3.546  -17.930 1.00 27.24 ? 148 GLY B O   1 
ATOM   1347 N N   . LEU B 2 140 ? -18.141 -3.177  -16.061 1.00 26.50 ? 149 LEU B N   1 
ATOM   1348 C CA  . LEU B 2 140 ? -17.829 -1.781  -16.373 1.00 25.84 ? 149 LEU B CA  1 
ATOM   1349 C C   . LEU B 2 140 ? -16.292 -1.608  -16.618 1.00 26.20 ? 149 LEU B C   1 
ATOM   1350 O O   . LEU B 2 140 ? -15.459 -2.253  -16.001 1.00 26.70 ? 149 LEU B O   1 
ATOM   1351 C CB  . LEU B 2 140 ? -18.276 -0.830  -15.268 1.00 25.19 ? 149 LEU B CB  1 
ATOM   1352 C CG  . LEU B 2 140 ? -19.725 -0.931  -14.840 1.00 25.44 ? 149 LEU B CG  1 
ATOM   1353 C CD1 . LEU B 2 140 ? -20.001 0.193   -13.786 1.00 26.35 ? 149 LEU B CD1 1 
ATOM   1354 C CD2 . LEU B 2 140 ? -20.680 -0.776  -16.052 1.00 25.80 ? 149 LEU B CD2 1 
ATOM   1355 N N   . TYR B 2 141 ? -15.954 -0.691  -17.540 1.00 27.74 ? 150 TYR B N   1 
ATOM   1356 C CA  . TYR B 2 141 ? -14.589 -0.428  -17.922 1.00 28.72 ? 150 TYR B CA  1 
ATOM   1357 C C   . TYR B 2 141 ? -14.038 0.730   -17.115 1.00 28.06 ? 150 TYR B C   1 
ATOM   1358 O O   . TYR B 2 141 ? -14.757 1.712   -16.933 1.00 29.63 ? 150 TYR B O   1 
ATOM   1359 C CB  . TYR B 2 141 ? -14.716 0.018   -19.428 1.00 30.04 ? 150 TYR B CB  1 
ATOM   1360 C CG  . TYR B 2 141 ? -13.503 0.679   -20.063 1.00 31.28 ? 150 TYR B CG  1 
ATOM   1361 C CD1 . TYR B 2 141 ? -13.371 2.062   -20.079 1.00 32.89 ? 150 TYR B CD1 1 
ATOM   1362 C CD2 . TYR B 2 141 ? -12.488 -0.083  -20.636 1.00 32.69 ? 150 TYR B CD2 1 
ATOM   1363 C CE1 . TYR B 2 141 ? -12.240 2.674   -20.613 1.00 34.91 ? 150 TYR B CE1 1 
ATOM   1364 C CE2 . TYR B 2 141 ? -11.383 0.525   -21.227 1.00 34.46 ? 150 TYR B CE2 1 
ATOM   1365 C CZ  . TYR B 2 141 ? -11.240 1.901   -21.165 1.00 35.57 ? 150 TYR B CZ  1 
ATOM   1366 O OH  . TYR B 2 141 ? -10.167 2.533   -21.776 1.00 38.65 ? 150 TYR B OH  1 
ATOM   1367 N N   . GLY B 2 142 ? -12.768 0.680   -16.696 1.00 27.98 ? 151 GLY B N   1 
ATOM   1368 C CA  . GLY B 2 142 ? -12.168 1.873   -16.103 1.00 29.38 ? 151 GLY B CA  1 
ATOM   1369 C C   . GLY B 2 142 ? -11.326 1.621   -14.877 1.00 30.81 ? 151 GLY B C   1 
ATOM   1370 O O   . GLY B 2 142 ? -10.794 2.581   -14.306 1.00 32.20 ? 151 GLY B O   1 
ATOM   1371 N N   . ASN B 2 143 ? -11.188 0.331   -14.440 1.00 28.99 ? 152 ASN B N   1 
ATOM   1372 C CA  . ASN B 2 143 ? -10.250 0.032   -13.346 1.00 28.97 ? 152 ASN B CA  1 
ATOM   1373 C C   . ASN B 2 143 ? -9.288  -1.039  -13.867 1.00 31.38 ? 152 ASN B C   1 
ATOM   1374 O O   . ASN B 2 143 ? -9.710  -2.139  -14.234 1.00 30.36 ? 152 ASN B O   1 
ATOM   1375 C CB  . ASN B 2 143 ? -10.933 -0.489  -12.078 1.00 29.01 ? 152 ASN B CB  1 
ATOM   1376 C CG  . ASN B 2 143 ? -10.009 -0.451  -10.872 1.00 29.90 ? 152 ASN B CG  1 
ATOM   1377 O OD1 . ASN B 2 143 ? -9.027  0.334   -10.845 1.00 31.96 ? 152 ASN B OD1 1 
ATOM   1378 N ND2 . ASN B 2 143 ? -10.209 -1.369  -9.919  1.00 30.81 ? 152 ASN B ND2 1 
ATOM   1379 N N   . GLY B 2 144 ? -8.023  -0.677  -13.949 1.00 32.45 ? 153 GLY B N   1 
ATOM   1380 C CA  . GLY B 2 144 ? -7.052  -1.550  -14.601 1.00 34.69 ? 153 GLY B CA  1 
ATOM   1381 C C   . GLY B 2 144 ? -5.615  -1.196  -14.349 1.00 36.22 ? 153 GLY B C   1 
ATOM   1382 O O   . GLY B 2 144 ? -5.271  -0.666  -13.290 1.00 35.86 ? 153 GLY B O   1 
ATOM   1383 N N   . VAL B 2 145 ? -4.753  -1.508  -15.364 1.00 36.71 ? 154 VAL B N   1 
ATOM   1384 C CA  . VAL B 2 145 ? -3.336  -1.313  -15.183 1.00 39.35 ? 154 VAL B CA  1 
ATOM   1385 C C   . VAL B 2 145 ? -2.672  -0.776  -16.439 1.00 41.85 ? 154 VAL B C   1 
ATOM   1386 O O   . VAL B 2 145 ? -3.260  -0.828  -17.510 1.00 41.43 ? 154 VAL B O   1 
ATOM   1387 C CB  . VAL B 2 145 ? -2.761  -2.701  -14.781 1.00 41.78 ? 154 VAL B CB  1 
ATOM   1388 C CG1 . VAL B 2 145 ? -2.641  -3.653  -15.970 1.00 41.14 ? 154 VAL B CG1 1 
ATOM   1389 C CG2 . VAL B 2 145 ? -1.479  -2.579  -13.981 1.00 44.84 ? 154 VAL B CG2 1 
ATOM   1390 N N   . VAL B 2 146 ? -1.467  -0.223  -16.271 1.00 44.93 ? 155 VAL B N   1 
ATOM   1391 C CA  . VAL B 2 146 ? -0.638  0.269   -17.375 1.00 48.02 ? 155 VAL B CA  1 
ATOM   1392 C C   . VAL B 2 146 ? 0.443   -0.765  -17.590 1.00 50.90 ? 155 VAL B C   1 
ATOM   1393 O O   . VAL B 2 146 ? 1.130   -1.141  -16.645 1.00 50.09 ? 155 VAL B O   1 
ATOM   1394 C CB  . VAL B 2 146 ? -0.063  1.683   -17.110 1.00 49.86 ? 155 VAL B CB  1 
ATOM   1395 C CG1 . VAL B 2 146 ? 0.819   2.132   -18.276 1.00 51.26 ? 155 VAL B CG1 1 
ATOM   1396 C CG2 . VAL B 2 146 ? -1.192  2.688   -16.885 1.00 50.55 ? 155 VAL B CG2 1 
ATOM   1397 N N   . ILE B 2 147 ? 0.584   -1.265  -18.833 1.00 53.71 ? 156 ILE B N   1 
ATOM   1398 C CA  . ILE B 2 147 ? 1.551   -2.324  -19.108 1.00 57.00 ? 156 ILE B CA  1 
ATOM   1399 C C   . ILE B 2 147 ? 2.883   -1.781  -19.710 1.00 59.35 ? 156 ILE B C   1 
ATOM   1400 O O   . ILE B 2 147 ? 2.992   -0.587  -19.963 1.00 59.55 ? 156 ILE B O   1 
ATOM   1401 C CB  . ILE B 2 147 ? 0.876   -3.424  -19.971 1.00 58.32 ? 156 ILE B CB  1 
ATOM   1402 C CG1 . ILE B 2 147 ? 0.512   -2.901  -21.365 1.00 58.74 ? 156 ILE B CG1 1 
ATOM   1403 C CG2 . ILE B 2 147 ? -0.355  -3.990  -19.256 1.00 59.23 ? 156 ILE B CG2 1 
ATOM   1404 C CD1 . ILE B 2 147 ? 0.204   -3.992  -22.315 1.00 59.67 ? 156 ILE B CD1 1 
ATOM   1405 N N   . LYS B 2 148 ? 3.896   -2.654  -19.880 1.00 60.75 ? 157 LYS B N   1 
ATOM   1406 C CA  . LYS B 2 148 ? 5.243   -2.328  -20.375 1.00 63.19 ? 157 LYS B CA  1 
ATOM   1407 C C   . LYS B 2 148 ? 5.338   -1.185  -21.402 1.00 64.91 ? 157 LYS B C   1 
ATOM   1408 O O   . LYS B 2 148 ? 6.146   -0.274  -21.225 1.00 66.18 ? 157 LYS B O   1 
ATOM   1409 C CB  . LYS B 2 148 ? 5.934   -3.590  -20.932 1.00 65.41 ? 157 LYS B CB  1 
ATOM   1410 C CG  . LYS B 2 148 ? 6.299   -4.581  -19.824 1.00 70.61 ? 157 LYS B CG  1 
ATOM   1411 C CD  . LYS B 2 148 ? 6.863   -5.911  -20.344 1.00 76.33 ? 157 LYS B CD  1 
ATOM   1412 C CE  . LYS B 2 148 ? 8.125   -5.741  -21.159 1.00 80.90 ? 157 LYS B CE  1 
ATOM   1413 N NZ  . LYS B 2 148 ? 8.709   -7.050  -21.569 1.00 83.67 ? 157 LYS B NZ  1 
ATOM   1414 N N   . ASN B 2 149 ? 4.511   -1.205  -22.444 1.00 64.79 ? 158 ASN B N   1 
ATOM   1415 C CA  . ASN B 2 149 ? 4.548   -0.218  -23.521 1.00 65.19 ? 158 ASN B CA  1 
ATOM   1416 C C   . ASN B 2 149 ? 3.795   1.101   -23.253 1.00 63.99 ? 158 ASN B C   1 
ATOM   1417 O O   . ASN B 2 149 ? 3.662   1.927   -24.164 1.00 64.58 ? 158 ASN B O   1 
ATOM   1418 C CB  . ASN B 2 149 ? 4.055   -0.853  -24.847 1.00 68.20 ? 158 ASN B CB  1 
ATOM   1419 C CG  . ASN B 2 149 ? 3.057   -2.000  -24.697 1.00 73.51 ? 158 ASN B CG  1 
ATOM   1420 O OD1 . ASN B 2 149 ? 3.355   -3.064  -24.123 1.00 74.96 ? 158 ASN B OD1 1 
ATOM   1421 N ND2 . ASN B 2 149 ? 1.856   -1.811  -25.211 1.00 75.32 ? 158 ASN B ND2 1 
ATOM   1422 N N   . GLY B 2 150 ? 3.306   1.300   -22.036 1.00 61.77 ? 159 GLY B N   1 
ATOM   1423 C CA  . GLY B 2 150 ? 2.551   2.508   -21.691 1.00 59.80 ? 159 GLY B CA  1 
ATOM   1424 C C   . GLY B 2 150 ? 1.059   2.437   -21.986 1.00 57.36 ? 159 GLY B C   1 
ATOM   1425 O O   . GLY B 2 150 ? 0.322   3.389   -21.701 1.00 57.67 ? 159 GLY B O   1 
ATOM   1426 N N   . SER B 2 151 ? 0.595   1.306   -22.558 1.00 55.11 ? 160 SER B N   1 
ATOM   1427 C CA  . SER B 2 151 ? -0.812  1.106   -22.921 1.00 53.15 ? 160 SER B CA  1 
ATOM   1428 C C   . SER B 2 151 ? -1.672  0.678   -21.715 1.00 49.55 ? 160 SER B C   1 
ATOM   1429 O O   . SER B 2 151 ? -1.148  0.122   -20.767 1.00 50.58 ? 160 SER B O   1 
ATOM   1430 C CB  . SER B 2 151 ? -0.942  0.039   -23.996 1.00 55.29 ? 160 SER B CB  1 
ATOM   1431 O OG  . SER B 2 151 ? -2.097  0.372   -24.752 1.00 60.88 ? 160 SER B OG  1 
ATOM   1432 N N   . TYR B 2 152 ? -2.986  0.880   -21.823 1.00 46.69 ? 161 TYR B N   1 
ATOM   1433 C CA  . TYR B 2 152 ? -3.940  0.564   -20.739 1.00 44.32 ? 161 TYR B CA  1 
ATOM   1434 C C   . TYR B 2 152 ? -4.727  -0.729  -20.935 1.00 42.46 ? 161 TYR B C   1 
ATOM   1435 O O   . TYR B 2 152 ? -5.231  -0.991  -22.021 1.00 43.37 ? 161 TYR B O   1 
ATOM   1436 C CB  . TYR B 2 152 ? -4.930  1.711   -20.648 1.00 42.88 ? 161 TYR B CB  1 
ATOM   1437 C CG  . TYR B 2 152 ? -5.923  1.616   -19.496 1.00 41.21 ? 161 TYR B CG  1 
ATOM   1438 C CD1 . TYR B 2 152 ? -5.503  1.738   -18.180 1.00 41.63 ? 161 TYR B CD1 1 
ATOM   1439 C CD2 . TYR B 2 152 ? -7.285  1.481   -19.738 1.00 40.92 ? 161 TYR B CD2 1 
ATOM   1440 C CE1 . TYR B 2 152 ? -6.412  1.695   -17.125 1.00 41.41 ? 161 TYR B CE1 1 
ATOM   1441 C CE2 . TYR B 2 152 ? -8.205  1.438   -18.692 1.00 41.23 ? 161 TYR B CE2 1 
ATOM   1442 C CZ  . TYR B 2 152 ? -7.759  1.528   -17.387 1.00 41.53 ? 161 TYR B CZ  1 
ATOM   1443 O OH  . TYR B 2 152 ? -8.684  1.550   -16.370 1.00 42.02 ? 161 TYR B OH  1 
ATOM   1444 N N   . VAL B 2 153 ? -4.927  -1.493  -19.838 1.00 39.46 ? 162 VAL B N   1 
ATOM   1445 C CA  . VAL B 2 153 ? -5.764  -2.670  -19.904 1.00 37.19 ? 162 VAL B CA  1 
ATOM   1446 C C   . VAL B 2 153 ? -6.725  -2.583  -18.706 1.00 33.78 ? 162 VAL B C   1 
ATOM   1447 O O   . VAL B 2 153 ? -6.281  -2.524  -17.562 1.00 34.63 ? 162 VAL B O   1 
ATOM   1448 C CB  . VAL B 2 153 ? -4.959  -3.968  -19.888 1.00 38.55 ? 162 VAL B CB  1 
ATOM   1449 C CG1 . VAL B 2 153 ? -5.864  -5.203  -19.963 1.00 39.32 ? 162 VAL B CG1 1 
ATOM   1450 C CG2 . VAL B 2 153 ? -3.922  -3.981  -21.022 1.00 39.82 ? 162 VAL B CG2 1 
ATOM   1451 N N   . SER B 2 154 ? -8.001  -2.593  -19.019 1.00 32.25 ? 163 SER B N   1 
ATOM   1452 C CA  . SER B 2 154 ? -9.042  -2.500  -17.962 1.00 30.47 ? 163 SER B CA  1 
ATOM   1453 C C   . SER B 2 154 ? -9.564  -3.869  -17.558 1.00 30.83 ? 163 SER B C   1 
ATOM   1454 O O   . SER B 2 154 ? -9.824  -4.667  -18.439 1.00 32.70 ? 163 SER B O   1 
ATOM   1455 C CB  . SER B 2 154 ? -10.211 -1.700  -18.538 1.00 31.31 ? 163 SER B CB  1 
ATOM   1456 O OG  . SER B 2 154 ? -11.262 -1.685  -17.569 1.00 30.61 ? 163 SER B OG  1 
ATOM   1457 N N   . ALA B 2 155 ? -9.866  -4.115  -16.266 1.00 28.80 ? 164 ALA B N   1 
ATOM   1458 C CA  . ALA B 2 155 ? -10.566 -5.324  -15.889 1.00 29.49 ? 164 ALA B CA  1 
ATOM   1459 C C   . ALA B 2 155 ? -12.004 -5.196  -16.409 1.00 30.65 ? 164 ALA B C   1 
ATOM   1460 O O   . ALA B 2 155 ? -12.500 -4.068  -16.616 1.00 30.52 ? 164 ALA B O   1 
ATOM   1461 C CB  . ALA B 2 155 ? -10.622 -5.445  -14.340 1.00 29.45 ? 164 ALA B CB  1 
ATOM   1462 N N   . ILE B 2 156 ? -12.678 -6.325  -16.595 1.00 30.35 ? 165 ILE B N   1 
ATOM   1463 C CA  . ILE B 2 156 ? -14.123 -6.299  -16.836 1.00 30.31 ? 165 ILE B CA  1 
ATOM   1464 C C   . ILE B 2 156 ? -14.699 -6.397  -15.392 1.00 27.78 ? 165 ILE B C   1 
ATOM   1465 O O   . ILE B 2 156 ? -14.729 -7.488  -14.821 1.00 29.47 ? 165 ILE B O   1 
ATOM   1466 C CB  . ILE B 2 156 ? -14.591 -7.513  -17.673 1.00 32.67 ? 165 ILE B CB  1 
ATOM   1467 C CG1 . ILE B 2 156 ? -13.945 -7.380  -19.049 1.00 34.18 ? 165 ILE B CG1 1 
ATOM   1468 C CG2 . ILE B 2 156 ? -16.134 -7.447  -17.835 1.00 33.67 ? 165 ILE B CG2 1 
ATOM   1469 C CD1 . ILE B 2 156 ? -14.333 -8.536  -20.041 1.00 35.92 ? 165 ILE B CD1 1 
ATOM   1470 N N   . THR B 2 157 ? -15.068 -5.218  -14.779 1.00 27.64 ? 166 THR B N   1 
ATOM   1471 C CA  . THR B 2 157 ? -15.467 -5.278  -13.359 1.00 27.76 ? 166 THR B CA  1 
ATOM   1472 C C   . THR B 2 157 ? -16.967 -5.490  -13.242 1.00 27.47 ? 166 THR B C   1 
ATOM   1473 O O   . THR B 2 157 ? -17.720 -4.649  -13.668 1.00 26.74 ? 166 THR B O   1 
ATOM   1474 C CB  . THR B 2 157 ? -15.077 -3.985  -12.691 1.00 27.47 ? 166 THR B CB  1 
ATOM   1475 O OG1 . THR B 2 157 ? -13.645 -3.821  -12.727 1.00 28.56 ? 166 THR B OG1 1 
ATOM   1476 C CG2 . THR B 2 157 ? -15.580 -3.931  -11.217 1.00 26.14 ? 166 THR B CG2 1 
ATOM   1477 N N   . GLN B 2 158 ? -17.386 -6.603  -12.585 1.00 27.85 ? 167 GLN B N   1 
ATOM   1478 C CA  . GLN B 2 158 ? -18.813 -6.885  -12.402 1.00 27.50 ? 167 GLN B CA  1 
ATOM   1479 C C   . GLN B 2 158 ? -19.108 -6.999  -10.876 1.00 27.97 ? 167 GLN B C   1 
ATOM   1480 O O   . GLN B 2 158 ? -18.271 -7.519  -10.133 1.00 28.10 ? 167 GLN B O   1 
ATOM   1481 C CB  . GLN B 2 158 ? -19.182 -8.219  -13.135 1.00 29.39 ? 167 GLN B CB  1 
ATOM   1482 C CG  . GLN B 2 158 ? -20.691 -8.601  -13.092 1.00 29.92 ? 167 GLN B CG  1 
ATOM   1483 C CD  . GLN B 2 158 ? -21.585 -7.504  -13.680 1.00 30.13 ? 167 GLN B CD  1 
ATOM   1484 O OE1 . GLN B 2 158 ? -21.710 -6.402  -13.086 1.00 29.11 ? 167 GLN B OE1 1 
ATOM   1485 N NE2 . GLN B 2 158 ? -22.238 -7.791  -14.809 1.00 28.31 ? 167 GLN B NE2 1 
ATOM   1486 N N   . GLY B 2 159 ? -20.301 -6.579  -10.488 1.00 27.52 ? 168 GLY B N   1 
ATOM   1487 C CA  . GLY B 2 159 ? -20.781 -6.690  -9.112  1.00 30.98 ? 168 GLY B CA  1 
ATOM   1488 C C   . GLY B 2 159 ? -21.508 -8.004  -8.885  1.00 36.89 ? 168 GLY B C   1 
ATOM   1489 O O   . GLY B 2 159 ? -21.470 -8.930  -9.714  1.00 39.31 ? 168 GLY B O   1 
ATOM   1490 N N   . LYS B 2 160 ? -22.152 -8.120  -7.721  1.00 38.27 ? 169 LYS B N   1 
ATOM   1491 C CA  . LYS B 2 160 ? -22.915 -9.315  -7.393  1.00 40.40 ? 169 LYS B CA  1 
ATOM   1492 C C   . LYS B 2 160 ? -24.361 -8.886  -7.182  1.00 41.10 ? 169 LYS B C   1 
ATOM   1493 O O   . LYS B 2 160 ? -24.605 -7.885  -6.503  1.00 40.38 ? 169 LYS B O   1 
ATOM   1494 C CB  . LYS B 2 160 ? -22.344 -9.954  -6.107  1.00 44.39 ? 169 LYS B CB  1 
ATOM   1495 C CG  . LYS B 2 160 ? -23.035 -11.256 -5.736  1.00 53.76 ? 169 LYS B CG  1 
ATOM   1496 C CD  . LYS B 2 160 ? -22.415 -11.879 -4.494  1.00 60.99 ? 169 LYS B CD  1 
ATOM   1497 C CE  . LYS B 2 160 ? -22.901 -13.298 -4.287  1.00 67.22 ? 169 LYS B CE  1 
ATOM   1498 N NZ  . LYS B 2 160 ? -22.572 -13.804 -2.923  1.00 71.34 ? 169 LYS B NZ  1 
ATOM   1499 N N   . ARG B 2 161 ? -25.314 -9.587  -7.816  1.00 42.09 ? 170 ARG B N   1 
ATOM   1500 C CA  . ARG B 2 161 ? -26.722 -9.269  -7.629  1.00 44.84 ? 170 ARG B CA  1 
ATOM   1501 C C   . ARG B 2 161 ? -27.220 -10.128 -6.439  1.00 48.39 ? 170 ARG B C   1 
ATOM   1502 O O   . ARG B 2 161 ? -27.261 -11.355 -6.539  1.00 49.23 ? 170 ARG B O   1 
ATOM   1503 C CB  . ARG B 2 161 ? -27.525 -9.520  -8.926  1.00 45.91 ? 170 ARG B CB  1 
ATOM   1504 C CG  . ARG B 2 161 ? -29.003 -9.199  -8.820  1.00 48.07 ? 170 ARG B CG  1 
ATOM   1505 C CD  . ARG B 2 161 ? -29.793 -9.601  -10.057 1.00 50.72 ? 170 ARG B CD  1 
ATOM   1506 N NE  . ARG B 2 161 ? -31.203 -9.225  -9.911  1.00 53.15 ? 170 ARG B NE  1 
ATOM   1507 C CZ  . ARG B 2 161 ? -31.834 -8.345  -10.684 1.00 53.88 ? 170 ARG B CZ  1 
ATOM   1508 N NH1 . ARG B 2 161 ? -31.201 -7.763  -11.695 1.00 50.19 ? 170 ARG B NH1 1 
ATOM   1509 N NH2 . ARG B 2 161 ? -33.109 -8.054  -10.463 1.00 55.12 ? 170 ARG B NH2 1 
ATOM   1510 N N   . GLU B 2 162 ? -27.481 -9.486  -5.294  1.00 49.99 ? 171 GLU B N   1 
ATOM   1511 C CA  . GLU B 2 162 ? -27.935 -10.164 -4.079  1.00 53.33 ? 171 GLU B CA  1 
ATOM   1512 C C   . GLU B 2 162 ? -29.356 -10.709 -4.244  1.00 55.09 ? 171 GLU B C   1 
ATOM   1513 O O   . GLU B 2 162 ? -29.696 -11.723 -3.620  1.00 56.49 ? 171 GLU B O   1 
ATOM   1514 C CB  . GLU B 2 162 ? -27.873 -9.204  -2.875  1.00 56.99 ? 171 GLU B CB  1 
ATOM   1515 C CG  . GLU B 2 162 ? -26.537 -8.504  -2.713  1.00 64.78 ? 171 GLU B CG  1 
ATOM   1516 C CD  . GLU B 2 162 ? -25.464 -9.269  -1.963  1.00 76.00 ? 171 GLU B CD  1 
ATOM   1517 O OE1 . GLU B 2 162 ? -25.142 -8.861  -0.822  1.00 78.62 ? 171 GLU B OE1 1 
ATOM   1518 O OE2 . GLU B 2 162 ? -24.924 -10.253 -2.521  1.00 79.55 ? 171 GLU B OE2 1 
HETATM 1519 S S   . DMS C 3 .   ? -18.736 12.026  -0.209  1.00 72.67 ? 201 DMS B S   1 
HETATM 1520 O O   . DMS C 3 .   ? -19.388 10.670  -0.268  1.00 72.55 ? 201 DMS B O   1 
HETATM 1521 C C1  . DMS C 3 .   ? -19.789 13.277  -0.942  1.00 72.80 ? 201 DMS B C1  1 
HETATM 1522 C C2  . DMS C 3 .   ? -17.511 12.183  -1.534  1.00 72.38 ? 201 DMS B C2  1 
HETATM 1523 S S   . DMS D 3 .   ? -8.867  2.940   -8.240  1.00 82.83 ? 202 DMS B S   1 
HETATM 1524 O O   . DMS D 3 .   ? -9.895  1.854   -8.308  1.00 82.46 ? 202 DMS B O   1 
HETATM 1525 C C1  . DMS D 3 .   ? -9.267  4.020   -6.844  1.00 82.92 ? 202 DMS B C1  1 
HETATM 1526 C C2  . DMS D 3 .   ? -9.242  4.207   -9.466  1.00 82.80 ? 202 DMS B C2  1 
HETATM 1527 N N1  . ZUC E 4 .   ? -6.909  5.726   -19.034 0.69 59.80 ? 203 ZUC B N1  1 
HETATM 1528 C C4  . ZUC E 4 .   ? -10.079 4.874   -16.409 0.69 60.01 ? 203 ZUC B C4  1 
HETATM 1529 C C5  . ZUC E 4 .   ? -10.320 4.872   -17.767 0.69 59.97 ? 203 ZUC B C5  1 
HETATM 1530 C C6  . ZUC E 4 .   ? -9.293  5.151   -18.652 0.69 59.85 ? 203 ZUC B C6  1 
HETATM 1531 C C7  . ZUC E 4 .   ? -8.006  5.437   -18.157 0.69 59.59 ? 203 ZUC B C7  1 
HETATM 1532 C C8  . ZUC E 4 .   ? -6.643  5.152   -20.229 0.69 60.44 ? 203 ZUC B C8  1 
HETATM 1533 C C10 . ZUC E 4 .   ? -5.085  5.722   -22.085 0.69 61.52 ? 203 ZUC B C10 1 
HETATM 1534 C C13 . ZUC E 4 .   ? -4.100  5.226   -20.000 0.69 61.71 ? 203 ZUC B C13 1 
HETATM 1535 C C1  . ZUC E 4 .   ? -6.405  5.784   -16.217 0.69 59.98 ? 203 ZUC B C1  1 
HETATM 1536 C C2  . ZUC E 4 .   ? -7.764  5.456   -16.780 0.69 59.72 ? 203 ZUC B C2  1 
HETATM 1537 C C3  . ZUC E 4 .   ? -8.822  5.168   -15.924 0.69 59.97 ? 203 ZUC B C3  1 
HETATM 1538 O O1  . ZUC E 4 .   ? -9.493  4.841   -19.955 0.69 60.24 ? 203 ZUC B O1  1 
HETATM 1539 O O2  . ZUC E 4 .   ? -7.424  4.419   -20.826 0.69 60.24 ? 203 ZUC B O2  1 
HETATM 1540 C C9  . ZUC E 4 .   ? -5.255  5.379   -20.747 0.69 61.24 ? 203 ZUC B C9  1 
HETATM 1541 C C11 . ZUC E 4 .   ? -3.796  5.867   -22.568 0.69 61.61 ? 203 ZUC B C11 1 
HETATM 1542 N N2  . ZUC E 4 .   ? -2.693  5.697   -21.830 0.69 61.55 ? 203 ZUC B N2  1 
HETATM 1543 C C12 . ZUC E 4 .   ? -2.855  5.379   -20.543 0.69 61.59 ? 203 ZUC B C12 1 
HETATM 1544 F F1  . ZUC E 4 .   ? -4.192  4.928   -18.681 0.69 62.52 ? 203 ZUC B F1  1 
HETATM 1545 O O   . HOH F 5 .   ? -9.416  -8.301  -30.286 1.00 54.68 ? 101 HOH A O   1 
HETATM 1546 O O   . HOH F 5 .   ? -31.878 0.132   -28.902 1.00 50.94 ? 102 HOH A O   1 
HETATM 1547 O O   . HOH F 5 .   ? -25.926 3.322   -27.721 1.00 49.41 ? 103 HOH A O   1 
HETATM 1548 O O   . HOH F 5 .   ? -7.972  0.744   3.462   1.00 42.12 ? 104 HOH A O   1 
HETATM 1549 O O   . HOH F 5 .   ? -23.556 19.070  -19.564 1.00 46.92 ? 105 HOH A O   1 
HETATM 1550 O O   . HOH F 5 .   ? -28.043 17.958  -19.005 1.00 57.15 ? 106 HOH A O   1 
HETATM 1551 O O   . HOH F 5 .   ? -24.203 9.435   -27.566 1.00 34.71 ? 107 HOH A O   1 
HETATM 1552 O O   . HOH F 5 .   ? -8.648  -6.043  2.639   1.00 59.97 ? 108 HOH A O   1 
HETATM 1553 O O   . HOH F 5 .   ? -4.490  -14.256 -25.504 1.00 36.34 ? 109 HOH A O   1 
HETATM 1554 O O   . HOH F 5 .   ? -9.003  3.887   -3.365  1.00 53.78 ? 110 HOH A O   1 
HETATM 1555 O O   . HOH F 5 .   ? -9.255  -6.425  -25.429 1.00 36.75 ? 111 HOH A O   1 
HETATM 1556 O O   . HOH F 5 .   ? -2.127  -3.681  -6.297  1.00 42.76 ? 112 HOH A O   1 
HETATM 1557 O O   . HOH F 5 .   ? -2.995  -11.591 -7.090  1.00 37.45 ? 113 HOH A O   1 
HETATM 1558 O O   . HOH F 5 .   ? -29.232 15.874  -15.023 1.00 40.62 ? 114 HOH A O   1 
HETATM 1559 O O   . HOH F 5 .   ? -8.250  -1.681  6.747   1.00 44.87 ? 115 HOH A O   1 
HETATM 1560 O O   . HOH F 5 .   ? -25.581 20.148  -3.995  1.00 72.01 ? 116 HOH A O   1 
HETATM 1561 O O   . HOH F 5 .   ? -30.643 12.916  -16.487 1.00 43.99 ? 117 HOH A O   1 
HETATM 1562 O O   . HOH F 5 .   ? -6.999  -8.927  -3.166  1.00 40.24 ? 118 HOH A O   1 
HETATM 1563 O O   . HOH F 5 .   ? -8.203  1.955   1.047   1.00 44.12 ? 119 HOH A O   1 
HETATM 1564 O O   . HOH F 5 .   ? -30.675 0.444   -22.912 1.00 49.54 ? 120 HOH A O   1 
HETATM 1565 O O   . HOH F 5 .   ? -6.934  -15.798 -25.535 1.00 42.98 ? 121 HOH A O   1 
HETATM 1566 O O   . HOH F 5 .   ? -22.239 -9.268  -34.572 1.00 52.51 ? 122 HOH A O   1 
HETATM 1567 O O   . HOH F 5 .   ? -26.712 -3.526  -35.301 1.00 59.71 ? 123 HOH A O   1 
HETATM 1568 O O   . HOH F 5 .   ? -3.875  -4.310  0.384   1.00 45.88 ? 124 HOH A O   1 
HETATM 1569 O O   . HOH F 5 .   ? 1.598   -1.996  -12.034 1.00 53.67 ? 125 HOH A O   1 
HETATM 1570 O O   . HOH F 5 .   ? -4.671  -9.928  -5.491  1.00 36.67 ? 126 HOH A O   1 
HETATM 1571 O O   . HOH F 5 .   ? 2.128   -10.444 -16.161 1.00 59.95 ? 127 HOH A O   1 
HETATM 1572 O O   . HOH F 5 .   ? -3.981  -0.336  -0.437  1.00 46.33 ? 128 HOH A O   1 
HETATM 1573 O O   . HOH F 5 .   ? -28.437 -6.057  -28.074 1.00 47.48 ? 129 HOH A O   1 
HETATM 1574 O O   . HOH F 5 .   ? -12.736 -3.012  -37.845 1.00 54.36 ? 130 HOH A O   1 
HETATM 1575 O O   . HOH F 5 .   ? -4.902  2.269   -10.001 1.00 52.95 ? 131 HOH A O   1 
HETATM 1576 O O   . HOH F 5 .   ? -2.143  -15.382 -24.503 1.00 70.95 ? 132 HOH A O   1 
HETATM 1577 O O   . HOH F 5 .   ? -2.884  -8.846  -3.362  1.00 48.80 ? 133 HOH A O   1 
HETATM 1578 O O   . HOH F 5 .   ? -0.655  -13.086 -9.700  1.00 60.07 ? 134 HOH A O   1 
HETATM 1579 O O   . HOH F 5 .   ? -4.861  -7.077  -0.522  1.00 67.78 ? 135 HOH A O   1 
HETATM 1580 O O   . HOH G 5 .   ? -35.759 8.586   -21.911 1.00 64.42 ? 301 HOH B O   1 
HETATM 1581 O O   . HOH G 5 .   ? -30.946 12.487  -19.201 1.00 42.75 ? 302 HOH B O   1 
HETATM 1582 O O   . HOH G 5 .   ? -28.503 -4.277  -21.717 1.00 56.28 ? 303 HOH B O   1 
HETATM 1583 O O   . HOH G 5 .   ? -34.077 1.886   -15.444 1.00 40.83 ? 304 HOH B O   1 
HETATM 1584 O O   . HOH G 5 .   ? -18.210 0.782   -33.929 1.00 50.65 ? 305 HOH B O   1 
HETATM 1585 O O   . HOH G 5 .   ? -18.238 -20.032 -21.104 1.00 46.14 ? 306 HOH B O   1 
HETATM 1586 O O   . HOH G 5 .   ? -12.934 10.236  -13.459 1.00 46.32 ? 307 HOH B O   1 
HETATM 1587 O O   . HOH G 5 .   ? -20.401 -7.118  -5.499  1.00 51.88 ? 308 HOH B O   1 
HETATM 1588 O O   . HOH G 5 .   ? -9.187  3.475   -12.515 1.00 56.96 ? 309 HOH B O   1 
HETATM 1589 O O   . HOH G 5 .   ? -35.359 3.977   -8.844  1.00 55.34 ? 310 HOH B O   1 
HETATM 1590 O O   . HOH G 5 .   ? -15.370 -4.514  1.504   1.00 35.78 ? 311 HOH B O   1 
HETATM 1591 O O   . HOH G 5 .   ? -21.574 7.417   -0.113  0.50 32.69 ? 312 HOH B O   1 
HETATM 1592 O O   . HOH G 5 .   ? -16.609 -6.934  -8.180  1.00 46.90 ? 313 HOH B O   1 
HETATM 1593 O O   . HOH G 5 .   ? -32.947 8.937   -12.357 1.00 53.71 ? 314 HOH B O   1 
HETATM 1594 O O   . HOH G 5 .   ? -22.043 -13.281 -21.657 1.00 37.79 ? 315 HOH B O   1 
HETATM 1595 O O   . HOH G 5 .   ? -19.599 -11.849 -25.552 1.00 47.97 ? 316 HOH B O   1 
HETATM 1596 O O   . HOH G 5 .   ? -7.160  -10.770 -5.270  1.00 42.75 ? 317 HOH B O   1 
HETATM 1597 O O   . HOH G 5 .   ? -12.606 14.146  -17.918 1.00 63.09 ? 318 HOH B O   1 
HETATM 1598 O O   . HOH G 5 .   ? -22.341 -11.297 -10.567 1.00 59.68 ? 319 HOH B O   1 
HETATM 1599 O O   . HOH G 5 .   ? -18.073 -10.552 -16.430 1.00 34.46 ? 320 HOH B O   1 
HETATM 1600 O O   . HOH G 5 .   ? -12.227 20.520  -16.637 1.00 55.79 ? 321 HOH B O   1 
HETATM 1601 O O   . HOH G 5 .   ? -35.403 -5.223  -10.125 1.00 48.75 ? 322 HOH B O   1 
HETATM 1602 O O   . HOH G 5 .   ? -29.483 -8.389  -14.974 1.00 62.37 ? 323 HOH B O   1 
HETATM 1603 O O   . HOH G 5 .   ? -16.517 -14.736 -16.449 1.00 37.98 ? 324 HOH B O   1 
HETATM 1604 O O   . HOH G 5 .   ? -6.321  -0.053  -10.877 1.00 31.72 ? 325 HOH B O   1 
HETATM 1605 O O   . HOH G 5 .   ? -10.922 -16.446 -24.665 1.00 55.63 ? 326 HOH B O   1 
HETATM 1606 O O   . HOH G 5 .   ? -21.163 -16.297 -19.059 1.00 58.62 ? 327 HOH B O   1 
HETATM 1607 O O   . HOH G 5 .   ? -27.650 -6.666  -5.509  1.00 38.68 ? 328 HOH B O   1 
HETATM 1608 O O   . HOH G 5 .   ? -27.707 -5.951  -18.527 1.00 41.13 ? 329 HOH B O   1 
HETATM 1609 O O   . HOH G 5 .   ? -21.704 -12.167 -12.936 1.00 43.93 ? 330 HOH B O   1 
HETATM 1610 O O   . HOH G 5 .   ? -17.321 15.144  -30.602 1.00 57.93 ? 331 HOH B O   1 
HETATM 1611 O O   . HOH G 5 .   ? -11.832 -17.808 -28.069 1.00 39.29 ? 332 HOH B O   1 
HETATM 1612 O O   . HOH G 5 .   ? -12.986 -2.031  -14.762 1.00 26.60 ? 333 HOH B O   1 
HETATM 1613 O O   . HOH G 5 .   ? -12.206 2.415   -5.675  1.00 34.59 ? 334 HOH B O   1 
HETATM 1614 O O   . HOH G 5 .   ? -19.095 15.051  -22.178 1.00 31.48 ? 335 HOH B O   1 
HETATM 1615 O O   . HOH G 5 .   ? -20.203 -7.551  -2.666  1.00 54.50 ? 336 HOH B O   1 
HETATM 1616 O O   . HOH G 5 .   ? -25.097 12.778  -23.828 1.00 43.85 ? 337 HOH B O   1 
HETATM 1617 O O   . HOH G 5 .   ? -11.447 7.830   -14.182 1.00 38.61 ? 338 HOH B O   1 
HETATM 1618 O O   . HOH G 5 .   ? -16.457 21.124  -14.332 1.00 39.45 ? 339 HOH B O   1 
HETATM 1619 O O   . HOH G 5 .   ? -12.576 -3.201  -10.148 1.00 30.72 ? 340 HOH B O   1 
HETATM 1620 O O   . HOH G 5 .   ? -18.698 19.357  -21.557 1.00 52.37 ? 341 HOH B O   1 
HETATM 1621 O O   . HOH G 5 .   ? -29.876 -0.991  -19.009 1.00 54.04 ? 342 HOH B O   1 
HETATM 1622 O O   . HOH G 5 .   ? -15.671 -10.114 -15.159 1.00 37.76 ? 343 HOH B O   1 
HETATM 1623 O O   . HOH G 5 .   ? -17.195 13.238  -5.454  1.00 38.65 ? 344 HOH B O   1 
HETATM 1624 O O   . HOH G 5 .   ? -26.076 -7.848  -16.434 1.00 32.00 ? 345 HOH B O   1 
HETATM 1625 O O   . HOH G 5 .   ? -14.975 8.560   -30.130 1.00 69.37 ? 346 HOH B O   1 
HETATM 1626 O O   . HOH G 5 .   ? -16.699 26.273  -12.172 1.00 74.21 ? 347 HOH B O   1 
HETATM 1627 O O   . HOH G 5 .   ? -22.264 15.347  -6.108  1.00 40.36 ? 348 HOH B O   1 
HETATM 1628 O O   . HOH G 5 .   ? -21.468 14.701  -34.476 1.00 71.53 ? 349 HOH B O   1 
HETATM 1629 O O   . HOH G 5 .   ? -23.584 -5.913  -4.759  1.00 44.95 ? 350 HOH B O   1 
HETATM 1630 O O   . HOH G 5 .   ? -27.582 20.608  -15.441 1.00 70.92 ? 351 HOH B O   1 
HETATM 1631 O O   . HOH G 5 .   ? -15.298 9.467   -0.755  1.00 38.70 ? 352 HOH B O   1 
HETATM 1632 O O   . HOH G 5 .   ? -17.465 9.082   -30.777 1.00 42.36 ? 353 HOH B O   1 
HETATM 1633 O O   . HOH G 5 .   ? -7.385  -6.460  0.319   1.00 47.88 ? 354 HOH B O   1 
HETATM 1634 O O   . HOH G 5 .   ? -7.354  2.158   -13.910 1.00 39.27 ? 355 HOH B O   1 
HETATM 1635 O O   . HOH G 5 .   ? -11.163 -8.959  0.167   1.00 63.84 ? 356 HOH B O   1 
HETATM 1636 O O   . HOH G 5 .   ? -11.126 12.496  -19.171 1.00 38.08 ? 357 HOH B O   1 
HETATM 1637 O O   . HOH G 5 .   ? -14.601 -12.191 -16.521 1.00 39.66 ? 358 HOH B O   1 
HETATM 1638 O O   . HOH G 5 .   ? -35.647 -0.282  -8.562  1.00 62.31 ? 359 HOH B O   1 
HETATM 1639 O O   . HOH G 5 .   ? -15.063 16.748  -20.050 1.00 39.70 ? 360 HOH B O   1 
HETATM 1640 O O   . HOH G 5 .   ? -20.946 6.140   -32.795 1.00 52.96 ? 361 HOH B O   1 
HETATM 1641 O O   . HOH G 5 .   ? -32.575 -6.749  -6.804  1.00 43.57 ? 362 HOH B O   1 
HETATM 1642 O O   . HOH G 5 .   ? -10.513 -18.372 -12.147 1.00 55.80 ? 363 HOH B O   1 
HETATM 1643 O O   . HOH G 5 .   ? -15.264 -8.452  -11.833 1.00 43.97 ? 364 HOH B O   1 
HETATM 1644 O O   . HOH G 5 .   ? -6.029  -9.825  -0.553  1.00 64.30 ? 365 HOH B O   1 
HETATM 1645 O O   . HOH G 5 .   ? -31.977 7.345   -4.441  1.00 49.44 ? 366 HOH B O   1 
HETATM 1646 O O   . HOH G 5 .   ? -16.048 -14.146 -30.807 1.00 41.78 ? 367 HOH B O   1 
HETATM 1647 O O   . HOH G 5 .   ? -6.935  1.429   -27.781 1.00 50.13 ? 368 HOH B O   1 
HETATM 1648 O O   . HOH G 5 .   ? -11.701 -4.829  -8.207  1.00 37.93 ? 369 HOH B O   1 
HETATM 1649 O O   . HOH G 5 .   ? -8.684  -10.542 -7.353  1.00 58.16 ? 370 HOH B O   1 
HETATM 1650 O O   . HOH G 5 .   ? -6.313  -1.019  -28.460 1.00 66.01 ? 371 HOH B O   1 
HETATM 1651 O O   . HOH G 5 .   ? -7.132  10.641  -19.336 1.00 50.08 ? 372 HOH B O   1 
HETATM 1652 O O   . HOH G 5 .   ? -25.995 -4.392  -3.998  1.00 31.82 ? 373 HOH B O   1 
HETATM 1653 O O   . HOH G 5 .   ? -23.872 -14.635 -18.052 1.00 50.14 ? 374 HOH B O   1 
HETATM 1654 O O   . HOH G 5 .   ? -14.444 -6.172  -1.539  1.00 44.52 ? 375 HOH B O   1 
HETATM 1655 O O   . HOH G 5 .   ? -19.071 25.694  -14.607 1.00 52.09 ? 376 HOH B O   1 
HETATM 1656 O O   . HOH G 5 .   ? -19.555 -13.151 -23.071 1.00 35.49 ? 377 HOH B O   1 
HETATM 1657 O O   . HOH G 5 .   ? -24.358 21.336  -11.852 1.00 68.56 ? 378 HOH B O   1 
HETATM 1658 O O   . HOH G 5 .   ? -18.480 12.706  -31.440 1.00 48.19 ? 379 HOH B O   1 
HETATM 1659 O O   . HOH G 5 .   ? -35.037 4.538   -4.417  1.00 52.36 ? 380 HOH B O   1 
HETATM 1660 O O   . HOH G 5 .   ? -20.566 24.932  -17.054 1.00 59.16 ? 381 HOH B O   1 
HETATM 1661 O O   . HOH G 5 .   ? -8.882  -14.912 -24.002 1.00 50.65 ? 382 HOH B O   1 
HETATM 1662 O O   . HOH G 5 .   ? -30.689 4.784   -2.519  1.00 42.69 ? 383 HOH B O   1 
HETATM 1663 O O   . HOH G 5 .   ? -22.965 14.477  -2.287  1.00 70.73 ? 384 HOH B O   1 
HETATM 1664 O O   . HOH G 5 .   ? -23.118 -6.952  -2.287  1.00 59.29 ? 385 HOH B O   1 
HETATM 1665 O O   . HOH G 5 .   ? -19.648 -5.543  -0.793  1.00 37.97 ? 386 HOH B O   1 
HETATM 1666 O O   . HOH G 5 .   ? -0.546  0.688   -13.350 1.00 52.67 ? 387 HOH B O   1 
HETATM 1667 O O   . HOH G 5 .   ? -35.322 1.849   -7.409  1.00 56.83 ? 388 HOH B O   1 
HETATM 1668 O O   . HOH G 5 .   ? -36.832 1.921   -18.540 1.00 48.69 ? 389 HOH B O   1 
HETATM 1669 O O   . HOH G 5 .   ? -18.726 -10.698 -10.011 1.00 56.40 ? 390 HOH B O   1 
HETATM 1670 O O   . HOH G 5 .   ? -13.217 11.418  -10.542 1.00 63.88 ? 391 HOH B O   1 
HETATM 1671 O O   . HOH G 5 .   ? -16.689 -12.299 -32.626 1.00 59.77 ? 392 HOH B O   1 
HETATM 1672 O O   . HOH G 5 .   ? -29.790 -5.253  -0.912  1.00 39.97 ? 393 HOH B O   1 
HETATM 1673 O O   . HOH G 5 .   ? -30.314 -7.449  -5.094  1.00 50.74 ? 394 HOH B O   1 
HETATM 1674 O O   . HOH G 5 .   ? -17.245 17.059  -21.974 1.00 44.28 ? 395 HOH B O   1 
HETATM 1675 O O   . HOH G 5 .   ? -11.600 -12.705 -8.852  1.00 73.52 ? 396 HOH B O   1 
HETATM 1676 O O   . HOH G 5 .   ? -33.930 10.770  -10.679 1.00 60.08 ? 397 HOH B O   1 
HETATM 1677 O O   . HOH G 5 .   ? -22.740 -14.041 -25.528 1.00 55.09 ? 398 HOH B O   1 
HETATM 1678 O O   . HOH G 5 .   ? 3.247   -6.208  -19.022 1.00 60.09 ? 399 HOH B O   1 
HETATM 1679 O O   . HOH G 5 .   ? 5.512   -3.266  -16.495 1.00 72.23 ? 400 HOH B O   1 
HETATM 1680 O O   . HOH G 5 .   ? -11.647 12.254  -14.652 1.00 59.19 ? 401 HOH B O   1 
HETATM 1681 O O   . HOH G 5 .   ? -18.897 -11.772 -13.860 1.00 39.25 ? 402 HOH B O   1 
HETATM 1682 O O   . HOH G 5 .   ? -11.328 -6.961  2.131   1.00 46.57 ? 403 HOH B O   1 
HETATM 1683 O O   . HOH G 5 .   ? -17.528 28.121  -14.183 1.00 47.88 ? 404 HOH B O   1 
HETATM 1684 O O   . HOH G 5 .   ? -21.617 4.760   -0.438  0.50 39.43 ? 405 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   ? 0.6786 0.4584 0.7492 0.0426  0.0072  -0.0550 50  ASP A N   
2    C CA  . ASP A 7   ? 0.6708 0.4654 0.7130 0.0570  0.0088  -0.0583 50  ASP A CA  
3    C C   . ASP A 7   ? 0.6284 0.4246 0.6553 0.0596  0.0223  -0.0364 50  ASP A C   
4    O O   . ASP A 7   ? 0.6458 0.4164 0.6699 0.0625  0.0284  -0.0207 50  ASP A O   
5    C CB  . ASP A 7   ? 0.7340 0.5117 0.7670 0.0713  -0.0005 -0.0718 50  ASP A CB  
6    C CG  . ASP A 7   ? 0.8251 0.6287 0.8368 0.0843  -0.0013 -0.0821 50  ASP A CG  
7    O OD1 . ASP A 7   ? 0.8402 0.6712 0.8507 0.0836  -0.0046 -0.0956 50  ASP A OD1 
8    O OD2 . ASP A 7   ? 0.8720 0.6693 0.8690 0.0955  0.0016  -0.0764 50  ASP A OD2 
9    N N   . MET A 8   ? 0.5579 0.3826 0.5732 0.0601  0.0262  -0.0358 51  MET A N   
10   C CA  . MET A 8   ? 0.5095 0.3386 0.5109 0.0630  0.0367  -0.0180 51  MET A CA  
11   C C   . MET A 8   ? 0.5010 0.3317 0.4807 0.0781  0.0356  -0.0201 51  MET A C   
12   O O   . MET A 8   ? 0.5039 0.3479 0.4793 0.0840  0.0287  -0.0361 51  MET A O   
13   C CB  . MET A 8   ? 0.4885 0.3442 0.4914 0.0546  0.0407  -0.0151 51  MET A CB  
14   C CG  . MET A 8   ? 0.4964 0.3508 0.5211 0.0414  0.0441  -0.0081 51  MET A CG  
15   S SD  . MET A 8   ? 0.5231 0.4097 0.5454 0.0355  0.0468  -0.0066 51  MET A SD  
16   C CE  . MET A 8   ? 0.5510 0.4365 0.6030 0.0220  0.0498  -0.0002 51  MET A CE  
17   N N   . TYR A 9   ? 0.4791 0.2963 0.4460 0.0857  0.0420  -0.0045 52  TYR A N   
18   C CA  . TYR A 9   ? 0.4786 0.2966 0.4263 0.1016  0.0392  -0.0071 52  TYR A CA  
19   C C   . TYR A 9   ? 0.4815 0.3040 0.4143 0.1067  0.0460  0.0074  52  TYR A C   
20   O O   . TYR A 9   ? 0.4920 0.3088 0.4267 0.1010  0.0548  0.0231  52  TYR A O   
21   C CB  . TYR A 9   ? 0.4932 0.2822 0.4349 0.1141  0.0347  -0.0083 52  TYR A CB  
22   C CG  . TYR A 9   ? 0.5325 0.2899 0.4716 0.1145  0.0427  0.0121  52  TYR A CG  
23   C CD1 . TYR A 9   ? 0.5545 0.2932 0.5133 0.1020  0.0447  0.0165  52  TYR A CD1 
24   C CD2 . TYR A 9   ? 0.5687 0.3129 0.4857 0.1291  0.0473  0.0262  52  TYR A CD2 
25   C CE1 . TYR A 9   ? 0.5952 0.3043 0.5543 0.1010  0.0540  0.0375  52  TYR A CE1 
26   C CE2 . TYR A 9   ? 0.6066 0.3205 0.5183 0.1311  0.0567  0.0473  52  TYR A CE2 
27   C CZ  . TYR A 9   ? 0.6247 0.3216 0.5589 0.1158  0.0612  0.0542  52  TYR A CZ  
28   O OH  . TYR A 9   ? 0.6552 0.3235 0.5878 0.1151  0.0732  0.0779  52  TYR A OH  
29   N N   . ILE A 10  ? 0.4662 0.3002 0.3857 0.1182  0.0414  0.0015  53  ILE A N   
30   C CA  . ILE A 10  ? 0.4662 0.3041 0.3703 0.1255  0.0448  0.0121  53  ILE A CA  
31   C C   . ILE A 10  ? 0.4919 0.3116 0.3764 0.1457  0.0418  0.0158  53  ILE A C   
32   O O   . ILE A 10  ? 0.4963 0.3088 0.3797 0.1549  0.0344  0.0054  53  ILE A O   
33   C CB  . ILE A 10  ? 0.4556 0.3219 0.3618 0.1215  0.0406  0.0027  53  ILE A CB  
34   C CG1 . ILE A 10  ? 0.4667 0.3461 0.3750 0.1288  0.0313  -0.0144 53  ILE A CG1 
35   C CG2 . ILE A 10  ? 0.4429 0.3244 0.3642 0.1036  0.0437  0.0004  53  ILE A CG2 
36   C CD1 . ILE A 10  ? 0.4698 0.3756 0.3827 0.1228  0.0288  -0.0204 53  ILE A CD1 
37   N N   . GLU A 11  ? 0.5060 0.3179 0.3732 0.1548  0.0472  0.0305  54  GLU A N   
38   C CA  . GLU A 11  ? 0.5234 0.3165 0.3665 0.1771  0.0445  0.0358  54  GLU A CA  
39   C C   . GLU A 11  ? 0.5223 0.3268 0.3490 0.1878  0.0426  0.0381  54  GLU A C   
40   O O   . GLU A 11  ? 0.5225 0.3328 0.3483 0.1813  0.0510  0.0492  54  GLU A O   
41   C CB  . GLU A 11  ? 0.5761 0.3391 0.4088 0.1812  0.0562  0.0573  54  GLU A CB  
42   C CG  . GLU A 11  ? 0.6882 0.4300 0.5349 0.1730  0.0580  0.0585  54  GLU A CG  
43   C CD  . GLU A 11  ? 0.7858 0.4957 0.6212 0.1780  0.0704  0.0826  54  GLU A CD  
44   O OE1 . GLU A 11  ? 0.8132 0.5248 0.6381 0.1800  0.0822  0.1004  54  GLU A OE1 
45   O OE2 . GLU A 11  ? 0.8664 0.5491 0.7037 0.1800  0.0688  0.0842  54  GLU A OE2 
46   N N   . ARG A 12  ? 0.5344 0.3422 0.3487 0.2054  0.0307  0.0271  55  ARG A N   
47   C CA  . ARG A 12  ? 0.5586 0.3767 0.3590 0.2161  0.0257  0.0262  55  ARG A CA  
48   C C   . ARG A 12  ? 0.5616 0.3622 0.3354 0.2299  0.0354  0.0462  55  ARG A C   
49   O O   . ARG A 12  ? 0.6022 0.3787 0.3602 0.2418  0.0408  0.0577  55  ARG A O   
50   C CB  . ARG A 12  ? 0.6080 0.4334 0.4036 0.2330  0.0091  0.0087  55  ARG A CB  
51   C CG  . ARG A 12  ? 0.6450 0.4887 0.4412 0.2347  0.0002  0.0003  55  ARG A CG  
52   C CD  . ARG A 12  ? 0.7054 0.5623 0.5099 0.2449  -0.0173 -0.0205 55  ARG A CD  
53   N NE  . ARG A 12  ? 0.7016 0.5737 0.5111 0.2446  -0.0273 -0.0293 55  ARG A NE  
54   C CZ  . ARG A 12  ? 0.7049 0.5700 0.4927 0.2664  -0.0374 -0.0315 55  ARG A CZ  
55   N NH1 . ARG A 12  ? 0.7580 0.6029 0.5156 0.2912  -0.0379 -0.0249 55  ARG A NH1 
56   N NH2 . ARG A 12  ? 0.6669 0.5435 0.4615 0.2646  -0.0476 -0.0405 55  ARG A NH2 
57   N N   . ALA A 13  ? 0.5488 0.3608 0.3169 0.2294  0.0382  0.0509  56  ALA A N   
58   C CA  . ALA A 13  ? 0.5793 0.3795 0.3207 0.2450  0.0484  0.0695  56  ALA A CA  
59   C C   . ALA A 13  ? 0.6108 0.4159 0.3280 0.2675  0.0372  0.0628  56  ALA A C   
60   O O   . ALA A 13  ? 0.6483 0.4422 0.3366 0.2872  0.0442  0.0770  56  ALA A O   
61   C CB  . ALA A 13  ? 0.6026 0.4104 0.3563 0.2276  0.0641  0.0839  56  ALA A CB  
62   N N   . GLY A 14  ? 0.5883 0.4089 0.3169 0.2657  0.0204  0.0422  57  GLY A N   
63   C CA  . GLY A 14  ? 0.6083 0.4319 0.3173 0.2870  0.0064  0.0328  57  GLY A CA  
64   C C   . GLY A 14  ? 0.5975 0.4400 0.3282 0.2770  -0.0096 0.0125  57  GLY A C   
65   O O   . GLY A 14  ? 0.5812 0.4365 0.3417 0.2524  -0.0084 0.0067  57  GLY A O   
66   N N   . ASP A 15  ? 0.6120 0.4553 0.3276 0.2965  -0.0251 0.0016  58  ASP A N   
67   C CA  . ASP A 15  ? 0.6157 0.4734 0.3511 0.2881  -0.0411 -0.0161 58  ASP A CA  
68   C C   . ASP A 15  ? 0.6362 0.4971 0.3684 0.2805  -0.0347 -0.0080 58  ASP A C   
69   O O   . ASP A 15  ? 0.6660 0.5193 0.3728 0.2931  -0.0236 0.0070  58  ASP A O   
70   C CB  . ASP A 15  ? 0.6532 0.5083 0.3742 0.3146  -0.0635 -0.0332 58  ASP A CB  
71   C CG  . ASP A 15  ? 0.7197 0.5764 0.4486 0.3242  -0.0761 -0.0477 58  ASP A CG  
72   O OD1 . ASP A 15  ? 0.6977 0.5551 0.4386 0.3133  -0.0667 -0.0432 58  ASP A OD1 
73   O OD2 . ASP A 15  ? 0.7922 0.6485 0.5123 0.3464  -0.0967 -0.0642 58  ASP A OD2 
74   N N   . ILE A 16  ? 0.6241 0.4962 0.3800 0.2633  -0.0434 -0.0187 59  ILE A N   
75   C CA  . ILE A 16  ? 0.6175 0.4910 0.3690 0.2589  -0.0411 -0.0138 59  ILE A CA  
76   C C   . ILE A 16  ? 0.6503 0.5195 0.3898 0.2783  -0.0620 -0.0284 59  ILE A C   
77   O O   . ILE A 16  ? 0.6472 0.5208 0.4084 0.2706  -0.0784 -0.0447 59  ILE A O   
78   C CB  . ILE A 16  ? 0.6080 0.4924 0.3891 0.2287  -0.0360 -0.0135 59  ILE A CB  
79   C CG1 . ILE A 16  ? 0.6129 0.5005 0.4035 0.2132  -0.0174 -0.0011 59  ILE A CG1 
80   C CG2 . ILE A 16  ? 0.6231 0.5075 0.3990 0.2260  -0.0364 -0.0101 59  ILE A CG2 
81   C CD1 . ILE A 16  ? 0.6058 0.5049 0.4232 0.1859  -0.0129 -0.0021 59  ILE A CD1 
82   N N   . THR A 17  ? 0.6746 0.5352 0.3799 0.3046  -0.0613 -0.0227 60  THR A N   
83   C CA  . THR A 17  ? 0.7159 0.5704 0.4033 0.3291  -0.0823 -0.0375 60  THR A CA  
84   C C   . THR A 17  ? 0.7691 0.6201 0.4256 0.3467  -0.0747 -0.0267 60  THR A C   
85   O O   . THR A 17  ? 0.7980 0.6494 0.4376 0.3515  -0.0535 -0.0071 60  THR A O   
86   C CB  . THR A 17  ? 0.7548 0.6024 0.4232 0.3562  -0.0942 -0.0467 60  THR A CB  
87   O OG1 . THR A 17  ? 0.7467 0.6010 0.4463 0.3409  -0.1018 -0.0584 60  THR A OG1 
88   C CG2 . THR A 17  ? 0.8031 0.6442 0.4519 0.3844  -0.1180 -0.0644 60  THR A CG2 
89   N N   . TRP A 18  ? 0.7692 0.6166 0.4183 0.3587  -0.0926 -0.0400 61  TRP A N   
90   C CA  . TRP A 18  ? 0.8048 0.6502 0.4215 0.3813  -0.0885 -0.0333 61  TRP A CA  
91   C C   . TRP A 18  ? 0.8431 0.6820 0.4183 0.4192  -0.0896 -0.0315 61  TRP A C   
92   O O   . TRP A 18  ? 0.8821 0.7144 0.4535 0.4336  -0.1085 -0.0475 61  TRP A O   
93   C CB  . TRP A 18  ? 0.8024 0.6423 0.4230 0.3855  -0.1118 -0.0517 61  TRP A CB  
94   C CG  . TRP A 18  ? 0.8167 0.6552 0.4037 0.4119  -0.1113 -0.0489 61  TRP A CG  
95   C CD1 . TRP A 18  ? 0.8444 0.6762 0.3938 0.4508  -0.1244 -0.0582 61  TRP A CD1 
96   C CD2 . TRP A 18  ? 0.8145 0.6595 0.4025 0.4034  -0.0996 -0.0386 61  TRP A CD2 
97   N NE1 . TRP A 18  ? 0.8573 0.6922 0.3839 0.4671  -0.1197 -0.0534 61  TRP A NE1 
98   C CE2 . TRP A 18  ? 0.8342 0.6777 0.3850 0.4382  -0.1045 -0.0413 61  TRP A CE2 
99   C CE3 . TRP A 18  ? 0.8106 0.6641 0.4252 0.3721  -0.0846 -0.0271 61  TRP A CE3 
100  C CZ2 . TRP A 18  ? 0.8351 0.6863 0.3780 0.4413  -0.0955 -0.0338 61  TRP A CZ2 
101  C CZ3 . TRP A 18  ? 0.8107 0.6706 0.4174 0.3752  -0.0771 -0.0201 61  TRP A CZ3 
102  C CH2 . TRP A 18  ? 0.8237 0.6832 0.3960 0.4091  -0.0822 -0.0234 61  TRP A CH2 
103  N N   . GLU A 19  ? 0.8431 0.6849 0.3884 0.4356  -0.0686 -0.0115 62  GLU A N   
104  C CA  . GLU A 19  ? 0.8863 0.7212 0.3881 0.4730  -0.0667 -0.0065 62  GLU A CA  
105  C C   . GLU A 19  ? 0.9295 0.7645 0.3974 0.5047  -0.0753 -0.0125 62  GLU A C   
106  O O   . GLU A 19  ? 0.9052 0.7502 0.3695 0.5021  -0.0595 0.0003  62  GLU A O   
107  C CB  . GLU A 19  ? 0.9210 0.7580 0.4111 0.4712  -0.0346 0.0231  62  GLU A CB  
108  C CG  . GLU A 19  ? 1.0334 0.8614 0.4736 0.5118  -0.0304 0.0317  62  GLU A CG  
109  C CD  . GLU A 19  ? 1.1526 0.9817 0.5743 0.5160  0.0030  0.0641  62  GLU A CD  
110  O OE1 . GLU A 19  ? 1.1779 1.0148 0.6302 0.4845  0.0239  0.0804  62  GLU A OE1 
111  O OE2 . GLU A 19  ? 1.2050 1.0268 0.5819 0.5514  0.0081  0.0733  62  GLU A OE2 
112  N N   . LYS A 20  ? 0.9936 0.8189 0.4347 0.5377  -0.1000 -0.0322 63  LYS A N   
113  C CA  . LYS A 20  ? 1.0658 0.8904 0.4701 0.5731  -0.1106 -0.0405 63  LYS A CA  
114  C C   . LYS A 20  ? 1.1076 0.9387 0.4689 0.5992  -0.0824 -0.0143 63  LYS A C   
115  O O   . LYS A 20  ? 1.1060 0.9340 0.4557 0.6022  -0.0655 0.0030  63  LYS A O   
116  C CB  . LYS A 20  ? 1.1286 0.9406 0.5159 0.6030  -0.1466 -0.0704 63  LYS A CB  
117  C CG  . LYS A 20  ? 1.2145 1.0215 0.6379 0.5854  -0.1764 -0.0976 63  LYS A CG  
118  C CD  . LYS A 20  ? 1.3183 1.1139 0.7163 0.6238  -0.2121 -0.1273 63  LYS A CD  
119  C CE  . LYS A 20  ? 1.3639 1.1521 0.7999 0.6102  -0.2440 -0.1554 63  LYS A CE  
120  N NZ  . LYS A 20  ? 1.3834 1.1745 0.8297 0.6039  -0.2397 -0.1523 63  LYS A NZ  
121  N N   . ASP A 21  ? 1.1456 0.9870 0.4885 0.6136  -0.0742 -0.0087 64  ASP A N   
122  C CA  . ASP A 21  ? 1.1807 1.0330 0.4870 0.6366  -0.0438 0.0186  64  ASP A CA  
123  C C   . ASP A 21  ? 1.1511 1.0103 0.4806 0.6056  -0.0091 0.0496  64  ASP A C   
124  O O   . ASP A 21  ? 1.1662 1.0220 0.4710 0.6196  0.0102  0.0701  64  ASP A O   
125  C CB  . ASP A 21  ? 1.2681 1.1110 0.5176 0.6862  -0.0516 0.0153  64  ASP A CB  
126  C CG  . ASP A 21  ? 1.3807 1.2182 0.6055 0.7198  -0.0852 -0.0153 64  ASP A CG  
127  O OD1 . ASP A 21  ? 1.4150 1.2632 0.6369 0.7254  -0.0850 -0.0185 64  ASP A OD1 
128  O OD2 . ASP A 21  ? 1.4217 1.2441 0.6314 0.7409  -0.1134 -0.0377 64  ASP A OD2 
129  N N   . ALA A 22  ? 1.0910 0.9578 0.4688 0.5634  -0.0032 0.0517  65  ALA A N   
130  C CA  . ALA A 22  ? 1.0408 0.9153 0.4449 0.5330  0.0270  0.0779  65  ALA A CA  
131  C C   . ALA A 22  ? 1.0173 0.9130 0.4090 0.5429  0.0540  0.0995  65  ALA A C   
132  O O   . ALA A 22  ? 1.0227 0.9275 0.3961 0.5644  0.0455  0.0896  65  ALA A O   
133  C CB  . ALA A 22  ? 1.0108 0.8887 0.4671 0.4894  0.0211  0.0693  65  ALA A CB  
134  N N   . GLU A 23  ? 0.9959 0.9010 0.4038 0.5242  0.0856  0.1275  66  GLU A N   
135  C CA  . GLU A 23  ? 0.9904 0.9206 0.3974 0.5281  0.1125  0.1480  66  GLU A CA  
136  C C   . GLU A 23  ? 0.9395 0.8858 0.3777 0.5089  0.1028  0.1337  66  GLU A C   
137  O O   . GLU A 23  ? 0.8868 0.8275 0.3623 0.4761  0.0921  0.1234  66  GLU A O   
138  C CB  . GLU A 23  ? 1.0573 0.9932 0.4891 0.5032  0.1450  0.1780  66  GLU A CB  
139  C CG  . GLU A 23  ? 1.1780 1.1433 0.6147 0.5056  0.1747  0.2006  66  GLU A CG  
140  C CD  . GLU A 23  ? 1.3180 1.2936 0.8027 0.4669  0.1994  0.2213  66  GLU A CD  
141  O OE1 . GLU A 23  ? 1.3519 1.3073 0.8498 0.4486  0.2027  0.2288  66  GLU A OE1 
142  O OE2 . GLU A 23  ? 1.3486 1.3526 0.8585 0.4558  0.2140  0.2287  66  GLU A OE2 
143  N N   . VAL A 24  ? 0.9442 0.9077 0.3635 0.5323  0.1031  0.1306  67  VAL A N   
144  C CA  . VAL A 24  ? 0.9406 0.9175 0.3837 0.5194  0.0927  0.1169  67  VAL A CA  
145  C C   . VAL A 24  ? 0.9222 0.9313 0.3865 0.5090  0.1224  0.1380  67  VAL A C   
146  O O   . VAL A 24  ? 0.9563 0.9839 0.3948 0.5364  0.1407  0.1520  67  VAL A O   
147  C CB  . VAL A 24  ? 0.9795 0.9513 0.3888 0.5542  0.0663  0.0932  67  VAL A CB  
148  C CG1 . VAL A 24  ? 0.9754 0.9547 0.4081 0.5407  0.0528  0.0783  67  VAL A CG1 
149  C CG2 . VAL A 24  ? 1.0114 0.9539 0.4008 0.5676  0.0368  0.0718  67  VAL A CG2 
150  N N   . THR A 25  ? 0.8801 0.8983 0.3919 0.4708  0.1265  0.1393  68  THR A N   
151  C CA  . THR A 25  ? 0.8591 0.9099 0.3979 0.4585  0.1527  0.1572  68  THR A CA  
152  C C   . THR A 25  ? 0.8227 0.8824 0.4042 0.4271  0.1436  0.1461  68  THR A C   
153  O O   . THR A 25  ? 0.8172 0.8562 0.4069 0.4128  0.1195  0.1274  68  THR A O   
154  C CB  . THR A 25  ? 0.8894 0.9457 0.4415 0.4457  0.1839  0.1861  68  THR A CB  
155  O OG1 . THR A 25  ? 0.9054 0.9980 0.4738 0.4466  0.2103  0.2038  68  THR A OG1 
156  C CG2 . THR A 25  ? 0.8872 0.9290 0.4797 0.4053  0.1821  0.1865  68  THR A CG2 
157  N N   . GLY A 26  ? 0.7988 0.8902 0.4073 0.4173  0.1629  0.1579  69  GLY A N   
158  C CA  . GLY A 26  ? 0.7849 0.8869 0.4318 0.3905  0.1553  0.1483  69  GLY A CA  
159  C C   . GLY A 26  ? 0.7915 0.9050 0.4266 0.4092  0.1400  0.1322  69  GLY A C   
160  O O   . GLY A 26  ? 0.8206 0.9193 0.4182 0.4374  0.1225  0.1189  69  GLY A O   
161  N N   . ASN A 27  ? 0.7468 0.8863 0.4142 0.3950  0.1452  0.1322  70  ASN A N   
162  C CA  . ASN A 27  ? 0.7400 0.8892 0.3983 0.4117  0.1296  0.1164  70  ASN A CA  
163  C C   . ASN A 27  ? 0.7134 0.8379 0.3841 0.3907  0.1027  0.0974  70  ASN A C   
164  O O   . ASN A 27  ? 0.7027 0.8045 0.3856 0.3664  0.0973  0.0967  70  ASN A O   
165  C CB  . ASN A 27  ? 0.7487 0.9443 0.4279 0.4177  0.1507  0.1267  70  ASN A CB  
166  C CG  . ASN A 27  ? 0.7807 0.9957 0.5121 0.3826  0.1607  0.1326  70  ASN A CG  
167  O OD1 . ASN A 27  ? 0.7900 0.9950 0.5445 0.3554  0.1689  0.1417  70  ASN A OD1 
168  N ND2 . ASN A 27  ? 0.7859 1.0301 0.5368 0.3845  0.1596  0.1265  70  ASN A ND2 
169  N N   . SER A 28  ? 0.6970 0.8240 0.3623 0.4014  0.0856  0.0826  71  SER A N   
170  C CA  . SER A 28  ? 0.6928 0.7932 0.3634 0.3857  0.0602  0.0662  71  SER A CA  
171  C C   . SER A 28  ? 0.6681 0.7895 0.3612 0.3783  0.0584  0.0622  71  SER A C   
172  O O   . SER A 28  ? 0.6871 0.8034 0.3644 0.3957  0.0410  0.0490  71  SER A O   
173  C CB  . SER A 28  ? 0.7321 0.8012 0.3658 0.4092  0.0341  0.0492  71  SER A CB  
174  O OG  . SER A 28  ? 0.7762 0.8351 0.3843 0.4267  0.0372  0.0523  71  SER A OG  
175  N N   . PRO A 29  ? 0.6360 0.7810 0.3670 0.3535  0.0751  0.0725  72  PRO A N   
176  C CA  . PRO A 29  ? 0.6192 0.7899 0.3732 0.3495  0.0740  0.0683  72  PRO A CA  
177  C C   . PRO A 29  ? 0.6138 0.7588 0.3672 0.3374  0.0498  0.0540  72  PRO A C   
178  O O   . PRO A 29  ? 0.6084 0.7255 0.3639 0.3167  0.0424  0.0526  72  PRO A O   
179  C CB  . PRO A 29  ? 0.6172 0.8170 0.4139 0.3249  0.0974  0.0825  72  PRO A CB  
180  C CG  . PRO A 29  ? 0.6263 0.7992 0.4233 0.3056  0.1011  0.0894  72  PRO A CG  
181  C CD  . PRO A 29  ? 0.6200 0.7703 0.3748 0.3306  0.0952  0.0879  72  PRO A CD  
182  N N   . ARG A 30  ? 0.6007 0.7566 0.3524 0.3500  0.0387  0.0443  73  ARG A N   
183  C CA  . ARG A 30  ? 0.6349 0.7680 0.3849 0.3404  0.0172  0.0328  73  ARG A CA  
184  C C   . ARG A 30  ? 0.6083 0.7736 0.3945 0.3248  0.0250  0.0345  73  ARG A C   
185  O O   . ARG A 30  ? 0.6069 0.8072 0.4042 0.3392  0.0308  0.0334  73  ARG A O   
186  C CB  . ARG A 30  ? 0.6921 0.8083 0.4101 0.3686  -0.0043 0.0196  73  ARG A CB  
187  C CG  . ARG A 30  ? 0.7923 0.8712 0.4771 0.3815  -0.0172 0.0145  73  ARG A CG  
188  C CD  . ARG A 30  ? 0.8905 0.9396 0.5461 0.4027  -0.0439 -0.0005 73  ARG A CD  
189  N NE  . ARG A 30  ? 0.9633 0.9885 0.5894 0.4233  -0.0545 -0.0071 73  ARG A NE  
190  C CZ  . ARG A 30  ? 1.0090 0.9900 0.6169 0.4245  -0.0787 -0.0179 73  ARG A CZ  
191  N NH1 . ARG A 30  ? 1.0470 1.0018 0.6609 0.4062  -0.0928 -0.0208 73  ARG A NH1 
192  N NH2 . ARG A 30  ? 0.9687 0.9312 0.5523 0.4447  -0.0892 -0.0258 73  ARG A NH2 
193  N N   . LEU A 31  ? 0.5746 0.7298 0.3804 0.2962  0.0247  0.0362  74  LEU A N   
194  C CA  . LEU A 31  ? 0.5515 0.7357 0.3942 0.2792  0.0314  0.0367  74  LEU A CA  
195  C C   . LEU A 31  ? 0.5501 0.7153 0.3908 0.2680  0.0132  0.0274  74  LEU A C   
196  O O   . LEU A 31  ? 0.5750 0.7044 0.3997 0.2566  0.0041  0.0267  74  LEU A O   
197  C CB  . LEU A 31  ? 0.5433 0.7359 0.4140 0.2553  0.0502  0.0481  74  LEU A CB  
198  C CG  . LEU A 31  ? 0.5617 0.7723 0.4357 0.2638  0.0719  0.0613  74  LEU A CG  
199  C CD1 . LEU A 31  ? 0.5612 0.7641 0.4528 0.2408  0.0860  0.0722  74  LEU A CD1 
200  C CD2 . LEU A 31  ? 0.5565 0.8153 0.4553 0.2750  0.0861  0.0650  74  LEU A CD2 
201  N N   . ASP A 32  ? 0.5327 0.7242 0.3931 0.2691  0.0095  0.0212  75  ASP A N   
202  C CA  . ASP A 32  ? 0.5357 0.7109 0.3931 0.2595  -0.0066 0.0133  75  ASP A CA  
203  C C   . ASP A 32  ? 0.5017 0.6883 0.3915 0.2329  0.0027  0.0161  75  ASP A C   
204  O O   . ASP A 32  ? 0.4836 0.7076 0.4100 0.2270  0.0159  0.0182  75  ASP A O   
205  C CB  . ASP A 32  ? 0.5645 0.7629 0.4263 0.2761  -0.0174 0.0032  75  ASP A CB  
206  C CG  . ASP A 32  ? 0.7086 0.8914 0.5356 0.3044  -0.0309 -0.0021 75  ASP A CG  
207  O OD1 . ASP A 32  ? 0.7466 0.8906 0.5425 0.3083  -0.0378 -0.0002 75  ASP A OD1 
208  O OD2 . ASP A 32  ? 0.7445 0.9542 0.5770 0.3232  -0.0357 -0.0095 75  ASP A OD2 
209  N N   . VAL A 33  ? 0.4914 0.6465 0.3695 0.2171  -0.0035 0.0163  76  VAL A N   
210  C CA  . VAL A 33  ? 0.4649 0.6279 0.3706 0.1939  0.0040  0.0176  76  VAL A CA  
211  C C   . VAL A 33  ? 0.4741 0.6191 0.3702 0.1852  -0.0100 0.0105  76  VAL A C   
212  O O   . VAL A 33  ? 0.5050 0.6228 0.3690 0.1936  -0.0235 0.0084  76  VAL A O   
213  C CB  . VAL A 33  ? 0.4764 0.6252 0.3834 0.1816  0.0175  0.0275  76  VAL A CB  
214  C CG1 . VAL A 33  ? 0.4817 0.6454 0.3911 0.1934  0.0318  0.0361  76  VAL A CG1 
215  C CG2 . VAL A 33  ? 0.4947 0.6029 0.3699 0.1787  0.0084  0.0280  76  VAL A CG2 
216  N N   . ALA A 34  ? 0.4366 0.5962 0.3604 0.1688  -0.0068 0.0072  77  ALA A N   
217  C CA  . ALA A 34  ? 0.4334 0.5802 0.3496 0.1607  -0.0180 0.0003  77  ALA A CA  
218  C C   . ALA A 34  ? 0.4232 0.5588 0.3492 0.1407  -0.0097 0.0037  77  ALA A C   
219  O O   . ALA A 34  ? 0.4138 0.5626 0.3655 0.1319  0.0035  0.0084  77  ALA A O   
220  C CB  . ALA A 34  ? 0.4125 0.5906 0.3544 0.1630  -0.0253 -0.0112 77  ALA A CB  
221  N N   . LEU A 35  ? 0.4306 0.5417 0.3351 0.1348  -0.0166 0.0023  78  LEU A N   
222  C CA  . LEU A 35  ? 0.4367 0.5376 0.3481 0.1182  -0.0098 0.0041  78  LEU A CA  
223  C C   . LEU A 35  ? 0.4380 0.5432 0.3522 0.1135  -0.0188 -0.0060 78  LEU A C   
224  O O   . LEU A 35  ? 0.4655 0.5582 0.3526 0.1216  -0.0293 -0.0082 78  LEU A O   
225  C CB  . LEU A 35  ? 0.4528 0.5217 0.3347 0.1168  -0.0087 0.0119  78  LEU A CB  
226  C CG  . LEU A 35  ? 0.4700 0.5283 0.3553 0.1020  -0.0032 0.0126  78  LEU A CG  
227  C CD1 . LEU A 35  ? 0.4493 0.5197 0.3627 0.0936  0.0087  0.0150  78  LEU A CD1 
228  C CD2 . LEU A 35  ? 0.5061 0.5364 0.3653 0.1010  -0.0036 0.0192  78  LEU A CD2 
229  N N   . ASP A 36  ? 0.4016 0.5240 0.3477 0.1024  -0.0156 -0.0124 79  ASP A N   
230  C CA  . ASP A 36  ? 0.3973 0.5257 0.3464 0.1007  -0.0263 -0.0249 79  ASP A CA  
231  C C   . ASP A 36  ? 0.4060 0.5139 0.3384 0.0924  -0.0250 -0.0247 79  ASP A C   
232  O O   . ASP A 36  ? 0.4121 0.5028 0.3350 0.0865  -0.0156 -0.0151 79  ASP A O   
233  C CB  . ASP A 36  ? 0.3900 0.5494 0.3842 0.0955  -0.0283 -0.0358 79  ASP A CB  
234  C CG  . ASP A 36  ? 0.4043 0.5686 0.4329 0.0792  -0.0176 -0.0343 79  ASP A CG  
235  O OD1 . ASP A 36  ? 0.4097 0.5528 0.4255 0.0722  -0.0100 -0.0273 79  ASP A OD1 
236  O OD2 . ASP A 36  ? 0.4594 0.6485 0.5295 0.0734  -0.0175 -0.0407 79  ASP A OD2 
237  N N   . GLU A 37  ? 0.4181 0.5290 0.3455 0.0940  -0.0349 -0.0359 80  GLU A N   
238  C CA  . GLU A 37  ? 0.4248 0.5205 0.3350 0.0889  -0.0337 -0.0368 80  GLU A CA  
239  C C   . GLU A 37  ? 0.4178 0.5133 0.3532 0.0751  -0.0245 -0.0372 80  GLU A C   
240  O O   . GLU A 37  ? 0.4372 0.5178 0.3576 0.0708  -0.0193 -0.0337 80  GLU A O   
241  C CB  . GLU A 37  ? 0.4568 0.5602 0.3580 0.0969  -0.0473 -0.0509 80  GLU A CB  
242  C CG  . GLU A 37  ? 0.5122 0.6007 0.3863 0.0964  -0.0459 -0.0508 80  GLU A CG  
243  C CD  . GLU A 37  ? 0.5873 0.6808 0.4415 0.1089  -0.0592 -0.0630 80  GLU A CD  
244  O OE1 . GLU A 37  ? 0.5665 0.6724 0.4386 0.1081  -0.0665 -0.0789 80  GLU A OE1 
245  O OE2 . GLU A 37  ? 0.6564 0.7405 0.4768 0.1208  -0.0634 -0.0571 80  GLU A OE2 
246  N N   . SER A 38  ? 0.3869 0.4982 0.3606 0.0683  -0.0213 -0.0399 81  SER A N   
247  C CA  . SER A 38  ? 0.3940 0.5013 0.3908 0.0559  -0.0127 -0.0387 81  SER A CA  
248  C C   . SER A 38  ? 0.3871 0.4824 0.3793 0.0530  0.0014  -0.0225 81  SER A C   
249  O O   . SER A 38  ? 0.3942 0.4845 0.4032 0.0445  0.0093  -0.0193 81  SER A O   
250  C CB  . SER A 38  ? 0.4161 0.5432 0.4581 0.0485  -0.0152 -0.0477 81  SER A CB  
251  O OG  . SER A 38  ? 0.4819 0.6194 0.5287 0.0522  -0.0307 -0.0655 81  SER A OG  
252  N N   . GLY A 39  ? 0.3758 0.4645 0.3436 0.0615  0.0029  -0.0133 82  GLY A N   
253  C CA  . GLY A 39  ? 0.3802 0.4570 0.3403 0.0618  0.0135  -0.0004 82  GLY A CA  
254  C C   . GLY A 39  ? 0.3759 0.4670 0.3596 0.0625  0.0217  0.0059  82  GLY A C   
255  O O   . GLY A 39  ? 0.3783 0.4609 0.3584 0.0632  0.0313  0.0160  82  GLY A O   
256  N N   . ASP A 40  ? 0.3568 0.4710 0.3638 0.0638  0.0183  0.0003  83  ASP A N   
257  C CA  . ASP A 40  ? 0.3654 0.4978 0.3974 0.0646  0.0285  0.0077  83  ASP A CA  
258  C C   . ASP A 40  ? 0.3687 0.5087 0.3833 0.0801  0.0262  0.0110  83  ASP A C   
259  O O   . ASP A 40  ? 0.3727 0.5187 0.3777 0.0877  0.0141  0.0026  83  ASP A O   
260  C CB  . ASP A 40  ? 0.4137 0.5711 0.4900 0.0554  0.0271  -0.0006 83  ASP A CB  
261  C CG  . ASP A 40  ? 0.5239 0.6717 0.6197 0.0409  0.0280  -0.0049 83  ASP A CG  
262  O OD1 . ASP A 40  ? 0.5803 0.7078 0.6646 0.0373  0.0364  0.0037  83  ASP A OD1 
263  O OD2 . ASP A 40  ? 0.5595 0.7190 0.6805 0.0346  0.0184  -0.0184 83  ASP A OD2 
264  N N   . PHE A 41  ? 0.3603 0.5011 0.3711 0.0866  0.0376  0.0227  84  PHE A N   
265  C CA  . PHE A 41  ? 0.3804 0.5305 0.3772 0.1033  0.0357  0.0249  84  PHE A CA  
266  C C   . PHE A 41  ? 0.3885 0.5752 0.4216 0.1045  0.0414  0.0241  84  PHE A C   
267  O O   . PHE A 41  ? 0.3850 0.5859 0.4521 0.0930  0.0534  0.0289  84  PHE A O   
268  C CB  . PHE A 41  ? 0.3756 0.5105 0.3488 0.1129  0.0440  0.0362  84  PHE A CB  
269  C CG  . PHE A 41  ? 0.3889 0.4913 0.3264 0.1156  0.0357  0.0357  84  PHE A CG  
270  C CD1 . PHE A 41  ? 0.4112 0.5019 0.3220 0.1267  0.0228  0.0314  84  PHE A CD1 
271  C CD2 . PHE A 41  ? 0.3999 0.4832 0.3316 0.1078  0.0411  0.0403  84  PHE A CD2 
272  C CE1 . PHE A 41  ? 0.4473 0.5084 0.3303 0.1270  0.0159  0.0320  84  PHE A CE1 
273  C CE2 . PHE A 41  ? 0.4244 0.4815 0.3289 0.1093  0.0337  0.0394  84  PHE A CE2 
274  C CZ  . PHE A 41  ? 0.4483 0.4946 0.3300 0.1180  0.0218  0.0358  84  PHE A CZ  
275  N N   . SER A 42  ? 0.4003 0.6021 0.4273 0.1188  0.0333  0.0186  85  SER A N   
276  C CA  . SER A 42  ? 0.3997 0.6407 0.4619 0.1225  0.0392  0.0177  85  SER A CA  
277  C C   . SER A 42  ? 0.4310 0.6799 0.4713 0.1449  0.0381  0.0198  85  SER A C   
278  O O   . SER A 42  ? 0.4356 0.6602 0.4370 0.1568  0.0257  0.0165  85  SER A O   
279  C CB  . SER A 42  ? 0.4227 0.6844 0.5125 0.1168  0.0265  0.0025  85  SER A CB  
280  O OG  . SER A 42  ? 0.4610 0.7091 0.5184 0.1287  0.0080  -0.0076 85  SER A OG  
281  N N   . LEU A 43  ? 0.4456 0.7293 0.5122 0.1512  0.0509  0.0251  86  LEU A N   
282  C CA  . LEU A 43  ? 0.4900 0.7847 0.5362 0.1755  0.0492  0.0252  86  LEU A CA  
283  C C   . LEU A 43  ? 0.5140 0.8265 0.5648 0.1859  0.0319  0.0101  86  LEU A C   
284  O O   . LEU A 43  ? 0.4899 0.8311 0.5803 0.1762  0.0301  0.0023  86  LEU A O   
285  C CB  . LEU A 43  ? 0.4882 0.8180 0.5602 0.1809  0.0705  0.0365  86  LEU A CB  
286  C CG  . LEU A 43  ? 0.5388 0.8537 0.5959 0.1815  0.0883  0.0531  86  LEU A CG  
287  C CD1 . LEU A 43  ? 0.5296 0.8847 0.6116 0.1898  0.1101  0.0648  86  LEU A CD1 
288  C CD2 . LEU A 43  ? 0.5837 0.8640 0.5867 0.2002  0.0786  0.0526  86  LEU A CD2 
289  N N   . VAL A 44  ? 0.5624 0.8578 0.5739 0.2063  0.0183  0.0054  87  VAL A N   
290  C CA  . VAL A 44  ? 0.5954 0.9051 0.6047 0.2212  0.0011  -0.0081 87  VAL A CA  
291  C C   . VAL A 44  ? 0.6367 0.9773 0.6499 0.2436  0.0077  -0.0069 87  VAL A C   
292  O O   . VAL A 44  ? 0.6580 0.9824 0.6422 0.2566  0.0130  0.0007  87  VAL A O   
293  C CB  . VAL A 44  ? 0.6323 0.8975 0.5920 0.2305  -0.0187 -0.0128 87  VAL A CB  
294  C CG1 . VAL A 44  ? 0.6425 0.9187 0.5936 0.2501  -0.0369 -0.0255 87  VAL A CG1 
295  C CG2 . VAL A 44  ? 0.6441 0.8804 0.5968 0.2102  -0.0229 -0.0127 87  VAL A CG2 
296  N N   . GLU A 45  ? 0.6488 1.0350 0.6980 0.2493  0.0074  -0.0151 88  GLU A N   
297  C CA  . GLU A 45  ? 0.6706 1.0915 0.7251 0.2725  0.0148  -0.0144 88  GLU A CA  
298  C C   . GLU A 45  ? 0.6868 1.1191 0.7297 0.2962  -0.0057 -0.0300 88  GLU A C   
299  O O   . GLU A 45  ? 0.6990 1.1248 0.7430 0.2927  -0.0236 -0.0418 88  GLU A O   
300  C CB  . GLU A 45  ? 0.6869 1.1600 0.7981 0.2617  0.0385  -0.0068 88  GLU A CB  
301  C CG  . GLU A 45  ? 0.7775 1.2370 0.8928 0.2443  0.0606  0.0115  88  GLU A CG  
302  C CD  . GLU A 45  ? 0.8962 1.3601 0.9899 0.2627  0.0777  0.0249  88  GLU A CD  
303  O OE1 . GLU A 45  ? 0.9274 1.3998 0.9969 0.2905  0.0707  0.0189  88  GLU A OE1 
304  O OE2 . GLU A 45  ? 0.9322 1.3905 1.0314 0.2510  0.0975  0.0408  88  GLU A OE2 
305  N N   . GLY B 7   ? 0.7092 0.6698 0.6554 0.1437  0.0324  -0.0551 16  GLY B N   
306  C CA  . GLY B 7   ? 0.7175 0.6592 0.6554 0.1454  0.0321  -0.0490 16  GLY B CA  
307  C C   . GLY B 7   ? 0.7061 0.6528 0.6477 0.1477  0.0266  -0.0484 16  GLY B C   
308  O O   . GLY B 7   ? 0.7080 0.6725 0.6603 0.1468  0.0223  -0.0529 16  GLY B O   
309  N N   . GLU B 8   ? 0.6810 0.6127 0.6142 0.1513  0.0264  -0.0429 17  GLU B N   
310  C CA  . GLU B 8   ? 0.6585 0.5931 0.5930 0.1550  0.0203  -0.0428 17  GLU B CA  
311  C C   . GLU B 8   ? 0.6296 0.5717 0.5733 0.1415  0.0182  -0.0409 17  GLU B C   
312  O O   . GLU B 8   ? 0.6350 0.5714 0.5775 0.1323  0.0223  -0.0357 17  GLU B O   
313  C CB  . GLU B 8   ? 0.6905 0.6081 0.6115 0.1651  0.0212  -0.0372 17  GLU B CB  
314  C CG  . GLU B 8   ? 0.7228 0.6431 0.6427 0.1724  0.0139  -0.0385 17  GLU B CG  
315  C CD  . GLU B 8   ? 0.7892 0.6959 0.6941 0.1873  0.0147  -0.0343 17  GLU B CD  
316  O OE1 . GLU B 8   ? 0.8182 0.7117 0.7147 0.1873  0.0220  -0.0267 17  GLU B OE1 
317  O OE2 . GLU B 8   ? 0.7949 0.7046 0.6965 0.1993  0.0081  -0.0384 17  GLU B OE2 
318  N N   . THR B 9   ? 0.6093 0.5646 0.5632 0.1399  0.0117  -0.0454 18  THR B N   
319  C CA  . THR B 9   ? 0.6046 0.5658 0.5675 0.1273  0.0087  -0.0436 18  THR B CA  
320  C C   . THR B 9   ? 0.5916 0.5501 0.5545 0.1315  0.0001  -0.0449 18  THR B C   
321  O O   . THR B 9   ? 0.5988 0.5598 0.5685 0.1223  -0.0039 -0.0439 18  THR B O   
322  C CB  . THR B 9   ? 0.6265 0.6071 0.6045 0.1182  0.0087  -0.0471 18  THR B CB  
323  O OG1 . THR B 9   ? 0.6362 0.6286 0.6214 0.1257  0.0028  -0.0540 18  THR B OG1 
324  C CG2 . THR B 9   ? 0.6420 0.6261 0.6187 0.1157  0.0166  -0.0468 18  THR B CG2 
325  N N   . THR B 10  ? 0.5804 0.5319 0.5340 0.1464  -0.0031 -0.0470 19  THR B N   
326  C CA  . THR B 10  ? 0.5678 0.5161 0.5192 0.1532  -0.0122 -0.0494 19  THR B CA  
327  C C   . THR B 10  ? 0.5432 0.4807 0.4884 0.1485  -0.0121 -0.0432 19  THR B C   
328  O O   . THR B 10  ? 0.5566 0.4851 0.4928 0.1478  -0.0044 -0.0364 19  THR B O   
329  C CB  . THR B 10  ? 0.5949 0.5364 0.5334 0.1721  -0.0136 -0.0512 19  THR B CB  
330  O OG1 . THR B 10  ? 0.6271 0.5776 0.5695 0.1774  -0.0125 -0.0564 19  THR B OG1 
331  C CG2 . THR B 10  ? 0.6050 0.5453 0.5409 0.1821  -0.0246 -0.0560 19  THR B CG2 
332  N N   . ASP B 11  ? 0.5229 0.4609 0.4729 0.1450  -0.0207 -0.0456 20  ASP B N   
333  C CA  . ASP B 11  ? 0.5243 0.4518 0.4669 0.1433  -0.0224 -0.0409 20  ASP B CA  
334  C C   . ASP B 11  ? 0.5269 0.4437 0.4521 0.1581  -0.0193 -0.0368 20  ASP B C   
335  O O   . ASP B 11  ? 0.5502 0.4666 0.4695 0.1719  -0.0209 -0.0399 20  ASP B O   
336  C CB  . ASP B 11  ? 0.5540 0.4805 0.5014 0.1429  -0.0350 -0.0462 20  ASP B CB  
337  C CG  . ASP B 11  ? 0.6182 0.5509 0.5809 0.1258  -0.0377 -0.0465 20  ASP B CG  
338  O OD1 . ASP B 11  ? 0.5695 0.5113 0.5406 0.1152  -0.0299 -0.0439 20  ASP B OD1 
339  O OD2 . ASP B 11  ? 0.6653 0.5928 0.6309 0.1233  -0.0476 -0.0490 20  ASP B OD2 
340  N N   . GLY B 12  ? 0.4809 0.3908 0.3988 0.1555  -0.0143 -0.0296 21  GLY B N   
341  C CA  . GLY B 12  ? 0.4833 0.3852 0.3861 0.1685  -0.0108 -0.0243 21  GLY B CA  
342  C C   . GLY B 12  ? 0.4666 0.3652 0.3659 0.1617  -0.0015 -0.0153 21  GLY B C   
343  O O   . GLY B 12  ? 0.4399 0.3415 0.3473 0.1473  0.0010  -0.0140 21  GLY B O   
344  N N   . VAL B 13  ? 0.4514 0.3450 0.3392 0.1719  0.0034  -0.0089 22  VAL B N   
345  C CA  . VAL B 13  ? 0.4374 0.3295 0.3229 0.1663  0.0125  0.0000  22  VAL B CA  
346  C C   . VAL B 13  ? 0.4336 0.3228 0.3196 0.1653  0.0217  0.0040  22  VAL B C   
347  O O   . VAL B 13  ? 0.4590 0.3450 0.3397 0.1763  0.0219  0.0027  22  VAL B O   
348  C CB  . VAL B 13  ? 0.4537 0.3439 0.3278 0.1770  0.0124  0.0056  22  VAL B CB  
349  C CG1 . VAL B 13  ? 0.4679 0.3550 0.3303 0.1953  0.0132  0.0075  22  VAL B CG1 
350  C CG2 . VAL B 13  ? 0.4813 0.3733 0.3561 0.1695  0.0208  0.0144  22  VAL B CG2 
351  N N   . TYR B 14  ? 0.4170 0.3066 0.3093 0.1524  0.0283  0.0076  23  TYR B N   
352  C CA  . TYR B 14  ? 0.4173 0.3022 0.3112 0.1494  0.0358  0.0103  23  TYR B CA  
353  C C   . TYR B 14  ? 0.4289 0.3115 0.3231 0.1431  0.0435  0.0190  23  TYR B C   
354  O O   . TYR B 14  ? 0.4397 0.3274 0.3375 0.1352  0.0433  0.0207  23  TYR B O   
355  C CB  . TYR B 14  ? 0.4136 0.3023 0.3176 0.1377  0.0351  0.0037  23  TYR B CB  
356  C CG  . TYR B 14  ? 0.4199 0.3131 0.3269 0.1421  0.0292  -0.0048 23  TYR B CG  
357  C CD1 . TYR B 14  ? 0.4316 0.3308 0.3410 0.1439  0.0209  -0.0096 23  TYR B CD1 
358  C CD2 . TYR B 14  ? 0.4576 0.3493 0.3656 0.1443  0.0313  -0.0082 23  TYR B CD2 
359  C CE1 . TYR B 14  ? 0.4536 0.3591 0.3683 0.1469  0.0152  -0.0173 23  TYR B CE1 
360  C CE2 . TYR B 14  ? 0.4852 0.3839 0.3970 0.1491  0.0260  -0.0160 23  TYR B CE2 
361  C CZ  . TYR B 14  ? 0.4977 0.4043 0.4139 0.1496  0.0180  -0.0204 23  TYR B CZ  
362  O OH  . TYR B 14  ? 0.5508 0.4665 0.4733 0.1530  0.0125  -0.0282 23  TYR B OH  
363  N N   . ARG B 15  ? 0.4337 0.3085 0.3254 0.1453  0.0502  0.0242  24  ARG B N   
364  C CA  . ARG B 15  ? 0.4361 0.3086 0.3315 0.1368  0.0575  0.0321  24  ARG B CA  
365  C C   . ARG B 15  ? 0.4335 0.3051 0.3381 0.1231  0.0579  0.0270  24  ARG B C   
366  O O   . ARG B 15  ? 0.4325 0.3015 0.3380 0.1236  0.0557  0.0202  24  ARG B O   
367  C CB  . ARG B 15  ? 0.4689 0.3307 0.3585 0.1438  0.0643  0.0401  24  ARG B CB  
368  C CG  . ARG B 15  ? 0.5020 0.3638 0.3798 0.1605  0.0644  0.0451  24  ARG B CG  
369  C CD  . ARG B 15  ? 0.5056 0.3559 0.3771 0.1671  0.0721  0.0545  24  ARG B CD  
370  N NE  . ARG B 15  ? 0.5210 0.3712 0.3790 0.1857  0.0716  0.0579  24  ARG B NE  
371  C CZ  . ARG B 15  ? 0.5482 0.4046 0.4000 0.1937  0.0748  0.0666  24  ARG B CZ  
372  N NH1 . ARG B 15  ? 0.4964 0.3602 0.3553 0.1842  0.0795  0.0736  24  ARG B NH1 
373  N NH2 . ARG B 15  ? 0.5656 0.4221 0.4036 0.2123  0.0732  0.0680  24  ARG B NH2 
374  N N   . VAL B 16  ? 0.4277 0.3027 0.3390 0.1119  0.0605  0.0299  25  VAL B N   
375  C CA  . VAL B 16  ? 0.4280 0.3017 0.3471 0.0997  0.0611  0.0255  25  VAL B CA  
376  C C   . VAL B 16  ? 0.4395 0.3040 0.3612 0.0955  0.0672  0.0322  25  VAL B C   
377  O O   . VAL B 16  ? 0.4484 0.3164 0.3723 0.0935  0.0710  0.0404  25  VAL B O   
378  C CB  . VAL B 16  ? 0.4261 0.3108 0.3509 0.0901  0.0586  0.0234  25  VAL B CB  
379  C CG1 . VAL B 16  ? 0.4280 0.3115 0.3594 0.0793  0.0589  0.0183  25  VAL B CG1 
380  C CG2 . VAL B 16  ? 0.4223 0.3143 0.3446 0.0935  0.0525  0.0184  25  VAL B CG2 
381  N N   . MET B 17  ? 0.4607 0.3134 0.3819 0.0954  0.0682  0.0293  26  MET B N   
382  C CA  . MET B 17  ? 0.4788 0.3184 0.4018 0.0921  0.0733  0.0355  26  MET B CA  
383  C C   . MET B 17  ? 0.5012 0.3354 0.4314 0.0807  0.0720  0.0298  26  MET B C   
384  O O   . MET B 17  ? 0.5004 0.3379 0.4308 0.0794  0.0677  0.0200  26  MET B O   
385  C CB  . MET B 17  ? 0.5084 0.3340 0.4220 0.1038  0.0747  0.0368  26  MET B CB  
386  C CG  . MET B 17  ? 0.5185 0.3488 0.4228 0.1180  0.0745  0.0402  26  MET B CG  
387  S SD  . MET B 17  ? 0.5074 0.3416 0.4096 0.1217  0.0808  0.0545  26  MET B SD  
388  C CE  . MET B 17  ? 0.5359 0.3505 0.4378 0.1197  0.0883  0.0643  26  MET B CE  
389  N N   . THR B 18  ? 0.5113 0.3361 0.4473 0.0733  0.0757  0.0357  27  THR B N   
390  C CA  . THR B 18  ? 0.5410 0.3566 0.4828 0.0638  0.0733  0.0291  27  THR B CA  
391  C C   . THR B 18  ? 0.5712 0.3655 0.5125 0.0634  0.0767  0.0350  27  THR B C   
392  O O   . THR B 18  ? 0.5565 0.3473 0.4972 0.0657  0.0823  0.0467  27  THR B O   
393  C CB  . THR B 18  ? 0.5653 0.3921 0.5185 0.0507  0.0717  0.0277  27  THR B CB  
394  O OG1 . THR B 18  ? 0.6021 0.4177 0.5594 0.0434  0.0683  0.0201  27  THR B OG1 
395  C CG2 . THR B 18  ? 0.5763 0.4072 0.5375 0.0452  0.0768  0.0395  27  THR B CG2 
396  N N   . ARG B 19  ? 0.6155 0.3949 0.5562 0.0608  0.0732  0.0272  28  ARG B N   
397  C CA  . ARG B 19  ? 0.6716 0.4277 0.6128 0.0583  0.0754  0.0323  28  ARG B CA  
398  C C   . ARG B 19  ? 0.6950 0.4457 0.6488 0.0431  0.0728  0.0299  28  ARG B C   
399  O O   . ARG B 19  ? 0.7068 0.4357 0.6621 0.0393  0.0728  0.0319  28  ARG B O   
400  C CB  . ARG B 19  ? 0.7293 0.4672 0.6583 0.0692  0.0731  0.0263  28  ARG B CB  
401  C CG  . ARG B 19  ? 0.8228 0.5660 0.7404 0.0843  0.0753  0.0289  28  ARG B CG  
402  C CD  . ARG B 19  ? 0.9108 0.6315 0.8174 0.0946  0.0777  0.0337  28  ARG B CD  
403  N NE  . ARG B 19  ? 0.9791 0.7065 0.8746 0.1102  0.0788  0.0350  28  ARG B NE  
404  C CZ  . ARG B 19  ? 1.0418 0.7737 0.9301 0.1204  0.0743  0.0246  28  ARG B CZ  
405  N NH1 . ARG B 19  ? 1.0536 0.7851 0.9437 0.1175  0.0692  0.0128  28  ARG B NH1 
406  N NH2 . ARG B 19  ? 1.0486 0.7872 0.9284 0.1340  0.0746  0.0257  28  ARG B NH2 
407  N N   . ARG B 20  ? 0.7100 0.4797 0.6729 0.0346  0.0701  0.0255  29  ARG B N   
408  C CA  . ARG B 20  ? 0.7439 0.5122 0.7195 0.0207  0.0664  0.0215  29  ARG B CA  
409  C C   . ARG B 20  ? 0.7619 0.5260 0.7497 0.0108  0.0713  0.0343  29  ARG B C   
410  O O   . ARG B 20  ? 0.7809 0.5308 0.7777 0.0007  0.0686  0.0327  29  ARG B O   
411  C CB  . ARG B 20  ? 0.7714 0.5630 0.7515 0.0166  0.0626  0.0141  29  ARG B CB  
412  C CG  . ARG B 20  ? 0.8471 0.6413 0.8408 0.0029  0.0582  0.0096  29  ARG B CG  
413  C CD  . ARG B 20  ? 0.9073 0.7248 0.9033 0.0007  0.0548  0.0031  29  ARG B CD  
414  N NE  . ARG B 20  ? 0.9544 0.7911 0.9521 0.0023  0.0595  0.0123  29  ARG B NE  
415  C CZ  . ARG B 20  ? 0.9919 0.8418 1.0015 -0.0059 0.0610  0.0181  29  ARG B CZ  
416  N NH1 . ARG B 20  ? 0.9891 0.8356 1.0121 -0.0175 0.0581  0.0162  29  ARG B NH1 
417  N NH2 . ARG B 20  ? 0.9920 0.8588 1.0006 -0.0020 0.0649  0.0256  29  ARG B NH2 
418  N N   . LEU B 21  ? 0.7503 0.5270 0.7390 0.0138  0.0784  0.0468  30  LEU B N   
419  C CA  . LEU B 21  ? 0.7442 0.5211 0.7451 0.0051  0.0846  0.0608  30  LEU B CA  
420  C C   . LEU B 21  ? 0.7387 0.4922 0.7328 0.0104  0.0905  0.0717  30  LEU B C   
421  O O   . LEU B 21  ? 0.7548 0.4881 0.7375 0.0177  0.0876  0.0657  30  LEU B O   
422  C CB  . LEU B 21  ? 0.7436 0.5476 0.7475 0.0073  0.0895  0.0691  30  LEU B CB  
423  C CG  . LEU B 21  ? 0.7627 0.5911 0.7762 0.0003  0.0855  0.0630  30  LEU B CG  
424  C CD1 . LEU B 21  ? 0.7746 0.5986 0.7968 -0.0109 0.0773  0.0502  30  LEU B CD1 
425  C CD2 . LEU B 21  ? 0.7621 0.6060 0.7640 0.0115  0.0841  0.0589  30  LEU B CD2 
426  N N   . LEU B 22  ? 0.7117 0.4684 0.7124 0.0076  0.0989  0.0881  31  LEU B N   
427  C CA  . LEU B 22  ? 0.7005 0.4359 0.6939 0.0132  0.1054  0.1002  31  LEU B CA  
428  C C   . LEU B 22  ? 0.6893 0.4248 0.6622 0.0330  0.1073  0.1002  31  LEU B C   
429  O O   . LEU B 22  ? 0.6853 0.4432 0.6543 0.0403  0.1080  0.0996  31  LEU B O   
430  C CB  . LEU B 22  ? 0.6956 0.4399 0.7017 0.0056  0.1148  0.1186  31  LEU B CB  
431  C CG  . LEU B 22  ? 0.7087 0.4304 0.7106 0.0080  0.1226  0.1338  31  LEU B CG  
432  C CD1 . LEU B 22  ? 0.7069 0.3975 0.7153 -0.0038 0.1180  0.1304  31  LEU B CD1 
433  C CD2 . LEU B 22  ? 0.7033 0.4414 0.7165 0.0031  0.1334  0.1532  31  LEU B CD2 
434  N N   . GLY B 23  ? 0.6722 0.3827 0.6321 0.0417  0.1068  0.0992  32  GLY B N   
435  C CA  . GLY B 23  ? 0.6610 0.3696 0.6017 0.0609  0.1075  0.0979  32  GLY B CA  
436  C C   . GLY B 23  ? 0.6414 0.3698 0.5773 0.0676  0.1012  0.0842  32  GLY B C   
437  O O   . GLY B 23  ? 0.6259 0.3573 0.5668 0.0610  0.0943  0.0712  32  GLY B O   
438  N N   . SER B 24  ? 0.6306 0.3719 0.5564 0.0811  0.1035  0.0873  33  SER B N   
439  C CA  . SER B 24  ? 0.6237 0.3835 0.5458 0.0870  0.0977  0.0758  33  SER B CA  
440  C C   . SER B 24  ? 0.5878 0.3700 0.5151 0.0857  0.1006  0.0823  33  SER B C   
441  O O   . SER B 24  ? 0.6085 0.3934 0.5311 0.0931  0.1069  0.0945  33  SER B O   
442  C CB  . SER B 24  ? 0.6811 0.4368 0.5872 0.1048  0.0960  0.0722  33  SER B CB  
443  O OG  . SER B 24  ? 0.7368 0.4724 0.6370 0.1078  0.0931  0.0656  33  SER B OG  
444  N N   . THR B 25  ? 0.5500 0.3482 0.4865 0.0766  0.0963  0.0750  34  THR B N   
445  C CA  . THR B 25  ? 0.5301 0.3492 0.4721 0.0744  0.0983  0.0804  34  THR B CA  
446  C C   . THR B 25  ? 0.5069 0.3411 0.4433 0.0811  0.0925  0.0715  34  THR B C   
447  O O   . THR B 25  ? 0.4900 0.3243 0.4269 0.0780  0.0864  0.0597  34  THR B O   
448  C CB  . THR B 25  ? 0.5591 0.3842 0.5180 0.0571  0.0984  0.0811  34  THR B CB  
449  O OG1 . THR B 25  ? 0.5785 0.3872 0.5442 0.0496  0.1030  0.0893  34  THR B OG1 
450  C CG2 . THR B 25  ? 0.5616 0.4099 0.5271 0.0551  0.1010  0.0875  34  THR B CG2 
451  N N   . GLN B 26  ? 0.4758 0.3226 0.4066 0.0904  0.0945  0.0775  35  GLN B N   
452  C CA  . GLN B 26  ? 0.4736 0.3329 0.3995 0.0961  0.0883  0.0695  35  GLN B CA  
453  C C   . GLN B 26  ? 0.4793 0.3538 0.4148 0.0858  0.0865  0.0679  35  GLN B C   
454  O O   . GLN B 26  ? 0.4951 0.3799 0.4349 0.0846  0.0909  0.0769  35  GLN B O   
455  C CB  . GLN B 26  ? 0.4774 0.3412 0.3911 0.1125  0.0893  0.0746  35  GLN B CB  
456  C CG  . GLN B 26  ? 0.4475 0.3219 0.3565 0.1180  0.0815  0.0659  35  GLN B CG  
457  C CD  . GLN B 26  ? 0.4564 0.3331 0.3527 0.1352  0.0810  0.0692  35  GLN B CD  
458  O OE1 . GLN B 26  ? 0.4774 0.3445 0.3654 0.1455  0.0833  0.0723  35  GLN B OE1 
459  N NE2 . GLN B 26  ? 0.4549 0.3436 0.3484 0.1397  0.0771  0.0681  35  GLN B NE2 
460  N N   . VAL B 27  ? 0.4659 0.3429 0.4046 0.0793  0.0805  0.0571  36  VAL B N   
461  C CA  . VAL B 27  ? 0.4548 0.3459 0.4009 0.0706  0.0781  0.0549  36  VAL B CA  
462  C C   . VAL B 27  ? 0.4410 0.3432 0.3800 0.0782  0.0736  0.0522  36  VAL B C   
463  O O   . VAL B 27  ? 0.4462 0.3606 0.3888 0.0742  0.0722  0.0525  36  VAL B O   
464  C CB  . VAL B 27  ? 0.4681 0.3565 0.4216 0.0589  0.0746  0.0460  36  VAL B CB  
465  C CG1 . VAL B 27  ? 0.4952 0.3721 0.4566 0.0509  0.0781  0.0490  36  VAL B CG1 
466  C CG2 . VAL B 27  ? 0.4865 0.3694 0.4336 0.0627  0.0699  0.0363  36  VAL B CG2 
467  N N   . GLY B 28  ? 0.4235 0.3210 0.3529 0.0886  0.0706  0.0491  37  GLY B N   
468  C CA  . GLY B 28  ? 0.4093 0.3144 0.3320 0.0958  0.0654  0.0465  37  GLY B CA  
469  C C   . GLY B 28  ? 0.4322 0.3309 0.3463 0.1066  0.0615  0.0422  37  GLY B C   
470  O O   . GLY B 28  ? 0.4245 0.3143 0.3357 0.1118  0.0642  0.0436  37  GLY B O   
471  N N   . VAL B 29  ? 0.3994 0.3024 0.3099 0.1098  0.0547  0.0369  38  VAL B N   
472  C CA  . VAL B 29  ? 0.4191 0.3187 0.3226 0.1200  0.0491  0.0321  38  VAL B CA  
473  C C   . VAL B 29  ? 0.4101 0.3127 0.3167 0.1139  0.0422  0.0243  38  VAL B C   
474  O O   . VAL B 29  ? 0.3875 0.2951 0.2978 0.1054  0.0415  0.0242  38  VAL B O   
475  C CB  . VAL B 29  ? 0.4345 0.3368 0.3283 0.1337  0.0477  0.0368  38  VAL B CB  
476  C CG1 . VAL B 29  ? 0.4285 0.3271 0.3149 0.1453  0.0402  0.0308  38  VAL B CG1 
477  C CG2 . VAL B 29  ? 0.4459 0.3473 0.3368 0.1394  0.0561  0.0467  38  VAL B CG2 
478  N N   . GLY B 30  ? 0.4119 0.3119 0.3174 0.1182  0.0371  0.0183  39  GLY B N   
479  C CA  . GLY B 30  ? 0.4158 0.3189 0.3251 0.1124  0.0306  0.0121  39  GLY B CA  
480  C C   . GLY B 30  ? 0.4135 0.3151 0.3210 0.1202  0.0233  0.0065  39  GLY B C   
481  O O   . GLY B 30  ? 0.4216 0.3199 0.3237 0.1315  0.0230  0.0064  39  GLY B O   
482  N N   . VAL B 31  ? 0.3885 0.2925 0.3004 0.1143  0.0172  0.0021  40  VAL B N   
483  C CA  . VAL B 31  ? 0.3918 0.2953 0.3049 0.1190  0.0088  -0.0039 40  VAL B CA  
484  C C   . VAL B 31  ? 0.3958 0.3051 0.3197 0.1104  0.0080  -0.0088 40  VAL B C   
485  O O   . VAL B 31  ? 0.3797 0.2930 0.3095 0.0987  0.0095  -0.0081 40  VAL B O   
486  C CB  . VAL B 31  ? 0.4278 0.3282 0.3376 0.1194  0.0008  -0.0043 40  VAL B CB  
487  C CG1 . VAL B 31  ? 0.4448 0.3439 0.3584 0.1216  -0.0092 -0.0112 40  VAL B CG1 
488  C CG2 . VAL B 31  ? 0.4288 0.3255 0.3268 0.1306  0.0011  0.0001  40  VAL B CG2 
489  N N   . MET B 32  ? 0.3854 0.2968 0.3120 0.1166  0.0051  -0.0139 41  MET B N   
490  C CA  . MET B 32  ? 0.3924 0.3123 0.3302 0.1102  0.0034  -0.0190 41  MET B CA  
491  C C   . MET B 32  ? 0.4077 0.3286 0.3504 0.1101  -0.0070 -0.0233 41  MET B C   
492  O O   . MET B 32  ? 0.4162 0.3327 0.3537 0.1214  -0.0136 -0.0264 41  MET B O   
493  C CB  . MET B 32  ? 0.4062 0.3290 0.3444 0.1175  0.0064  -0.0223 41  MET B CB  
494  C CG  . MET B 32  ? 0.4009 0.3357 0.3510 0.1111  0.0064  -0.0271 41  MET B CG  
495  S SD  . MET B 32  ? 0.4283 0.3672 0.3815 0.0989  0.0155  -0.0239 41  MET B SD  
496  C CE  . MET B 32  ? 0.4918 0.4223 0.4361 0.1077  0.0221  -0.0230 41  MET B CE  
497  N N   . GLN B 33  ? 0.3907 0.3165 0.3428 0.0977  -0.0089 -0.0234 42  GLN B N   
498  C CA  . GLN B 33  ? 0.4036 0.3291 0.3624 0.0951  -0.0189 -0.0269 42  GLN B CA  
499  C C   . GLN B 33  ? 0.4060 0.3428 0.3795 0.0812  -0.0176 -0.0270 42  GLN B C   
500  O O   . GLN B 33  ? 0.3957 0.3349 0.3699 0.0718  -0.0109 -0.0220 42  GLN B O   
501  C CB  . GLN B 33  ? 0.4346 0.3477 0.3850 0.0959  -0.0248 -0.0245 42  GLN B CB  
502  C CG  . GLN B 33  ? 0.4835 0.3936 0.4414 0.0934  -0.0369 -0.0293 42  GLN B CG  
503  C CD  . GLN B 33  ? 0.5492 0.4449 0.4969 0.0978  -0.0449 -0.0287 42  GLN B CD  
504  O OE1 . GLN B 33  ? 0.6208 0.5106 0.5731 0.0890  -0.0512 -0.0282 42  GLN B OE1 
505  N NE2 . GLN B 33  ? 0.5113 0.4008 0.4444 0.1115  -0.0443 -0.0280 42  GLN B NE2 
506  N N   . GLU B 34  ? 0.4085 0.3539 0.3942 0.0802  -0.0234 -0.0324 43  GLU B N   
507  C CA  . GLU B 34  ? 0.4181 0.3773 0.4201 0.0671  -0.0223 -0.0319 43  GLU B CA  
508  C C   . GLU B 34  ? 0.4323 0.4032 0.4362 0.0626  -0.0109 -0.0291 43  GLU B C   
509  O O   . GLU B 34  ? 0.4520 0.4301 0.4623 0.0511  -0.0066 -0.0246 43  GLU B O   
510  C CB  . GLU B 34  ? 0.4462 0.3984 0.4513 0.0557  -0.0265 -0.0275 43  GLU B CB  
511  C CG  . GLU B 34  ? 0.4877 0.4275 0.4922 0.0594  -0.0396 -0.0315 43  GLU B CG  
512  C CD  . GLU B 34  ? 0.6056 0.5326 0.6079 0.0505  -0.0438 -0.0265 43  GLU B CD  
513  O OE1 . GLU B 34  ? 0.6253 0.5587 0.6387 0.0366  -0.0411 -0.0218 43  GLU B OE1 
514  O OE2 . GLU B 34  ? 0.6332 0.5440 0.6221 0.0582  -0.0494 -0.0268 43  GLU B OE2 
515  N N   . GLY B 35  ? 0.4235 0.3947 0.4201 0.0726  -0.0062 -0.0314 44  GLY B N   
516  C CA  . GLY B 35  ? 0.4104 0.3905 0.4070 0.0714  0.0032  -0.0306 44  GLY B CA  
517  C C   . GLY B 35  ? 0.4093 0.3825 0.3968 0.0669  0.0102  -0.0250 44  GLY B C   
518  O O   . GLY B 35  ? 0.4246 0.4046 0.4120 0.0653  0.0173  -0.0249 44  GLY B O   
519  N N   . VAL B 36  ? 0.3716 0.3316 0.3510 0.0663  0.0078  -0.0212 45  VAL B N   
520  C CA  . VAL B 36  ? 0.3465 0.3003 0.3176 0.0624  0.0132  -0.0161 45  VAL B CA  
521  C C   . VAL B 36  ? 0.3570 0.2983 0.3163 0.0715  0.0138  -0.0148 45  VAL B C   
522  O O   . VAL B 36  ? 0.3633 0.2976 0.3184 0.0790  0.0081  -0.0157 45  VAL B O   
523  C CB  . VAL B 36  ? 0.3614 0.3132 0.3342 0.0530  0.0103  -0.0118 45  VAL B CB  
524  C CG1 . VAL B 36  ? 0.3660 0.3116 0.3293 0.0506  0.0146  -0.0071 45  VAL B CG1 
525  C CG2 . VAL B 36  ? 0.3672 0.3330 0.3521 0.0431  0.0121  -0.0111 45  VAL B CG2 
526  N N   . PHE B 37  ? 0.3418 0.2815 0.2962 0.0713  0.0205  -0.0130 46  PHE B N   
527  C CA  . PHE B 37  ? 0.3493 0.2791 0.2946 0.0779  0.0224  -0.0103 46  PHE B CA  
528  C C   . PHE B 37  ? 0.3469 0.2734 0.2878 0.0729  0.0232  -0.0055 46  PHE B C   
529  O O   . PHE B 37  ? 0.3309 0.2621 0.2741 0.0646  0.0259  -0.0046 46  PHE B O   
530  C CB  . PHE B 37  ? 0.3604 0.2885 0.3038 0.0812  0.0284  -0.0112 46  PHE B CB  
531  C CG  . PHE B 37  ? 0.3871 0.3055 0.3227 0.0880  0.0306  -0.0072 46  PHE B CG  
532  C CD1 . PHE B 37  ? 0.4175 0.3310 0.3481 0.0988  0.0275  -0.0069 46  PHE B CD1 
533  C CD2 . PHE B 37  ? 0.4007 0.3158 0.3344 0.0839  0.0356  -0.0037 46  PHE B CD2 
534  C CE1 . PHE B 37  ? 0.4259 0.3320 0.3491 0.1055  0.0307  -0.0018 46  PHE B CE1 
535  C CE2 . PHE B 37  ? 0.4132 0.3211 0.3415 0.0892  0.0384  0.0012  46  PHE B CE2 
536  C CZ  . PHE B 37  ? 0.4237 0.3274 0.3466 0.1001  0.0365  0.0027  46  PHE B CZ  
537  N N   . HIS B 38  ? 0.3376 0.2575 0.2720 0.0789  0.0203  -0.0029 47  HIS B N   
538  C CA  . HIS B 38  ? 0.3409 0.2584 0.2704 0.0764  0.0194  0.0012  47  HIS B CA  
539  C C   . HIS B 38  ? 0.3524 0.2671 0.2761 0.0817  0.0236  0.0051  47  HIS B C   
540  O O   . HIS B 38  ? 0.3600 0.2710 0.2796 0.0914  0.0231  0.0058  47  HIS B O   
541  C CB  . HIS B 38  ? 0.3517 0.2641 0.2777 0.0804  0.0110  0.0008  47  HIS B CB  
542  C CG  . HIS B 38  ? 0.3473 0.2613 0.2806 0.0751  0.0057  -0.0025 47  HIS B CG  
543  N ND1 . HIS B 38  ? 0.3704 0.2873 0.3097 0.0782  0.0032  -0.0072 47  HIS B ND1 
544  C CD2 . HIS B 38  ? 0.3614 0.2748 0.2972 0.0668  0.0024  -0.0012 47  HIS B CD2 
545  C CE1 . HIS B 38  ? 0.3563 0.2756 0.3032 0.0712  -0.0016 -0.0087 47  HIS B CE1 
546  N NE2 . HIS B 38  ? 0.3663 0.2828 0.3113 0.0637  -0.0019 -0.0046 47  HIS B NE2 
547  N N   . THR B 39  ? 0.3482 0.2656 0.2719 0.0759  0.0275  0.0080  48  THR B N   
548  C CA  . THR B 39  ? 0.3544 0.2713 0.2750 0.0797  0.0315  0.0125  48  THR B CA  
549  C C   . THR B 39  ? 0.3542 0.2758 0.2743 0.0740  0.0322  0.0150  48  THR B C   
550  O O   . THR B 39  ? 0.3657 0.2886 0.2852 0.0693  0.0287  0.0136  48  THR B O   
551  C CB  . THR B 39  ? 0.3736 0.2886 0.2976 0.0796  0.0375  0.0127  48  THR B CB  
552  O OG1 . THR B 39  ? 0.3854 0.3000 0.3077 0.0827  0.0416  0.0185  48  THR B OG1 
553  C CG2 . THR B 39  ? 0.3872 0.3050 0.3172 0.0696  0.0404  0.0095  48  THR B CG2 
554  N N   . MET B 40  ? 0.3725 0.2968 0.2921 0.0758  0.0359  0.0194  49  MET B N   
555  C CA  . MET B 40  ? 0.3758 0.3068 0.2957 0.0712  0.0362  0.0213  49  MET B CA  
556  C C   . MET B 40  ? 0.3670 0.3014 0.2941 0.0614  0.0398  0.0190  49  MET B C   
557  O O   . MET B 40  ? 0.3839 0.3156 0.3157 0.0597  0.0435  0.0184  49  MET B O   
558  C CB  . MET B 40  ? 0.3977 0.3332 0.3152 0.0778  0.0382  0.0271  49  MET B CB  
559  C CG  . MET B 40  ? 0.3850 0.3163 0.2928 0.0902  0.0334  0.0282  49  MET B CG  
560  S SD  . MET B 40  ? 0.4672 0.4070 0.3689 0.0991  0.0334  0.0340  49  MET B SD  
561  C CE  . MET B 40  ? 0.4446 0.3850 0.3428 0.0944  0.0273  0.0308  49  MET B CE  
562  N N   A TRP B 41  ? 0.3550 0.2946 0.2821 0.0557  0.0382  0.0174  50  TRP B N   
563  N N   B TRP B 41  ? 0.3551 0.2947 0.2822 0.0557  0.0382  0.0174  50  TRP B N   
564  N N   C TRP B 41  ? 0.3550 0.2946 0.2821 0.0557  0.0382  0.0174  50  TRP B N   
565  N N   D TRP B 41  ? 0.3551 0.2947 0.2822 0.0557  0.0382  0.0174  50  TRP B N   
566  C CA  A TRP B 41  ? 0.3661 0.3094 0.2987 0.0476  0.0404  0.0141  50  TRP B CA  
567  C CA  B TRP B 41  ? 0.3661 0.3096 0.2987 0.0476  0.0404  0.0141  50  TRP B CA  
568  C CA  C TRP B 41  ? 0.3661 0.3094 0.2987 0.0476  0.0404  0.0141  50  TRP B CA  
569  C CA  D TRP B 41  ? 0.3661 0.3096 0.2987 0.0476  0.0404  0.0141  50  TRP B CA  
570  C C   A TRP B 41  ? 0.3796 0.3250 0.3191 0.0453  0.0443  0.0158  50  TRP B C   
571  C C   B TRP B 41  ? 0.3803 0.3259 0.3199 0.0452  0.0442  0.0158  50  TRP B C   
572  C C   C TRP B 41  ? 0.3796 0.3250 0.3191 0.0453  0.0443  0.0158  50  TRP B C   
573  C C   D TRP B 41  ? 0.3803 0.3259 0.3199 0.0452  0.0442  0.0158  50  TRP B C   
574  O O   A TRP B 41  ? 0.3851 0.3272 0.3295 0.0410  0.0462  0.0126  50  TRP B O   
575  O O   B TRP B 41  ? 0.3868 0.3296 0.3312 0.0405  0.0461  0.0123  50  TRP B O   
576  O O   C TRP B 41  ? 0.3851 0.3272 0.3295 0.0410  0.0462  0.0126  50  TRP B O   
577  O O   D TRP B 41  ? 0.3868 0.3296 0.3312 0.0405  0.0461  0.0123  50  TRP B O   
578  C CB  A TRP B 41  ? 0.3664 0.3160 0.2962 0.0439  0.0378  0.0128  50  TRP B CB  
579  C CB  B TRP B 41  ? 0.3653 0.3152 0.2949 0.0442  0.0377  0.0131  50  TRP B CB  
580  C CB  C TRP B 41  ? 0.3664 0.3160 0.2962 0.0439  0.0378  0.0128  50  TRP B CB  
581  C CB  D TRP B 41  ? 0.3653 0.3152 0.2949 0.0442  0.0377  0.0131  50  TRP B CB  
582  C CG  A TRP B 41  ? 0.3810 0.3342 0.3145 0.0372  0.0390  0.0080  50  TRP B CG  
583  C CG  B TRP B 41  ? 0.3775 0.3319 0.3114 0.0373  0.0390  0.0087  50  TRP B CG  
584  C CG  C TRP B 41  ? 0.3810 0.3342 0.3145 0.0372  0.0390  0.0080  50  TRP B CG  
585  C CG  D TRP B 41  ? 0.3775 0.3319 0.3114 0.0373  0.0390  0.0087  50  TRP B CG  
586  C CD1 A TRP B 41  ? 0.3959 0.3486 0.3279 0.0346  0.0388  0.0043  50  TRP B CD1 
587  C CD1 B TRP B 41  ? 0.3895 0.3498 0.3293 0.0337  0.0400  0.0080  50  TRP B CD1 
588  C CD1 C TRP B 41  ? 0.3959 0.3486 0.3279 0.0346  0.0388  0.0043  50  TRP B CD1 
589  C CD1 D TRP B 41  ? 0.3895 0.3498 0.3293 0.0337  0.0400  0.0080  50  TRP B CD1 
590  C CD2 A TRP B 41  ? 0.3898 0.3481 0.3293 0.0328  0.0402  0.0060  50  TRP B CD2 
591  C CD2 B TRP B 41  ? 0.3862 0.3402 0.3198 0.0338  0.0391  0.0041  50  TRP B CD2 
592  C CD2 C TRP B 41  ? 0.3898 0.3481 0.3293 0.0328  0.0402  0.0060  50  TRP B CD2 
593  C CD2 D TRP B 41  ? 0.3862 0.3402 0.3198 0.0338  0.0391  0.0041  50  TRP B CD2 
594  N NE1 A TRP B 41  ? 0.4020 0.3587 0.3370 0.0302  0.0396  -0.0003 50  TRP B NE1 
595  N NE1 B TRP B 41  ? 0.3920 0.3537 0.3342 0.0286  0.0399  0.0021  50  TRP B NE1 
596  N NE1 C TRP B 41  ? 0.4020 0.3587 0.3370 0.0302  0.0396  -0.0003 50  TRP B NE1 
597  N NE1 D TRP B 41  ? 0.3920 0.3537 0.3342 0.0286  0.0399  0.0021  50  TRP B NE1 
598  C CE2 A TRP B 41  ? 0.3996 0.3589 0.3395 0.0286  0.0399  0.0002  50  TRP B CE2 
599  C CE2 B TRP B 41  ? 0.3940 0.3523 0.3315 0.0293  0.0397  -0.0002 50  TRP B CE2 
600  C CE2 C TRP B 41  ? 0.3996 0.3589 0.3395 0.0286  0.0399  0.0002  50  TRP B CE2 
601  C CE2 D TRP B 41  ? 0.3940 0.3523 0.3315 0.0293  0.0397  -0.0002 50  TRP B CE2 
602  C CE3 A TRP B 41  ? 0.4000 0.3631 0.3452 0.0319  0.0413  0.0087  50  TRP B CE3 
603  C CE3 B TRP B 41  ? 0.3973 0.3489 0.3280 0.0343  0.0388  0.0031  50  TRP B CE3 
604  C CE3 C TRP B 41  ? 0.4000 0.3631 0.3452 0.0319  0.0413  0.0087  50  TRP B CE3 
605  C CE3 D TRP B 41  ? 0.3973 0.3489 0.3280 0.0343  0.0388  0.0031  50  TRP B CE3 
606  C CZ2 A TRP B 41  ? 0.4186 0.3815 0.3640 0.0240  0.0396  -0.0043 50  TRP B CZ2 
607  C CZ2 B TRP B 41  ? 0.4123 0.3721 0.3491 0.0269  0.0398  -0.0057 50  TRP B CZ2 
608  C CZ2 C TRP B 41  ? 0.4186 0.3815 0.3640 0.0240  0.0396  -0.0043 50  TRP B CZ2 
609  C CZ2 D TRP B 41  ? 0.4123 0.3721 0.3491 0.0269  0.0398  -0.0057 50  TRP B CZ2 
610  C CZ3 A TRP B 41  ? 0.4129 0.3804 0.3656 0.0257  0.0413  0.0050  50  TRP B CZ3 
611  C CZ3 B TRP B 41  ? 0.4151 0.3701 0.3462 0.0311  0.0399  -0.0013 50  TRP B CZ3 
612  C CZ3 C TRP B 41  ? 0.4129 0.3804 0.3656 0.0257  0.0413  0.0050  50  TRP B CZ3 
613  C CZ3 D TRP B 41  ? 0.4151 0.3701 0.3462 0.0311  0.0399  -0.0013 50  TRP B CZ3 
614  C CH2 A TRP B 41  ? 0.4197 0.3863 0.3720 0.0220  0.0399  -0.0020 50  TRP B CH2 
615  C CH2 B TRP B 41  ? 0.4174 0.3762 0.3504 0.0282  0.0404  -0.0058 50  TRP B CH2 
616  C CH2 C TRP B 41  ? 0.4197 0.3863 0.3720 0.0220  0.0399  -0.0020 50  TRP B CH2 
617  C CH2 D TRP B 41  ? 0.4174 0.3762 0.3504 0.0282  0.0404  -0.0058 50  TRP B CH2 
618  N N   . HIS B 42  ? 0.3778 0.3283 0.3179 0.0484  0.0453  0.0211  51  HIS B N   
619  C CA  . HIS B 42  ? 0.3909 0.3449 0.3398 0.0445  0.0494  0.0240  51  HIS B CA  
620  C C   . HIS B 42  ? 0.4089 0.3531 0.3607 0.0457  0.0534  0.0259  51  HIS B C   
621  O O   . HIS B 42  ? 0.4248 0.3684 0.3850 0.0402  0.0566  0.0276  51  HIS B O   
622  C CB  . HIS B 42  ? 0.3829 0.3478 0.3329 0.0477  0.0503  0.0300  51  HIS B CB  
623  C CG  . HIS B 42  ? 0.4002 0.3634 0.3447 0.0578  0.0522  0.0362  51  HIS B CG  
624  N ND1 . HIS B 42  ? 0.4029 0.3660 0.3369 0.0670  0.0483  0.0368  51  HIS B ND1 
625  C CD2 . HIS B 42  ? 0.4137 0.3747 0.3613 0.0605  0.0574  0.0422  51  HIS B CD2 
626  C CE1 . HIS B 42  ? 0.4309 0.3931 0.3616 0.0759  0.0509  0.0423  51  HIS B CE1 
627  N NE2 . HIS B 42  ? 0.4151 0.3763 0.3535 0.0724  0.0569  0.0462  51  HIS B NE2 
628  N N   . VAL B 43  ? 0.3948 0.3311 0.3399 0.0527  0.0528  0.0257  52  VAL B N   
629  C CA  . VAL B 43  ? 0.3963 0.3226 0.3420 0.0555  0.0562  0.0272  52  VAL B CA  
630  C C   . VAL B 43  ? 0.4200 0.3396 0.3696 0.0491  0.0561  0.0207  52  VAL B C   
631  O O   . VAL B 43  ? 0.4238 0.3363 0.3779 0.0463  0.0591  0.0220  52  VAL B O   
632  C CB  . VAL B 43  ? 0.3989 0.3203 0.3362 0.0659  0.0544  0.0276  52  VAL B CB  
633  C CG1 . VAL B 43  ? 0.4164 0.3269 0.3526 0.0700  0.0570  0.0274  52  VAL B CG1 
634  C CG2 . VAL B 43  ? 0.4003 0.3269 0.3323 0.0744  0.0545  0.0340  52  VAL B CG2 
635  N N   . THR B 44  ? 0.3965 0.3177 0.3436 0.0474  0.0526  0.0141  53  THR B N   
636  C CA  . THR B 44  ? 0.3869 0.3032 0.3357 0.0438  0.0523  0.0074  53  THR B CA  
637  C C   . THR B 44  ? 0.4016 0.3232 0.3540 0.0360  0.0506  0.0024  53  THR B C   
638  O O   . THR B 44  ? 0.4216 0.3387 0.3753 0.0337  0.0501  -0.0036 53  THR B O   
639  C CB  . THR B 44  ? 0.3793 0.2954 0.3236 0.0481  0.0503  0.0033  53  THR B CB  
640  O OG1 . THR B 44  ? 0.3778 0.3025 0.3201 0.0460  0.0474  0.0021  53  THR B OG1 
641  C CG2 . THR B 44  ? 0.4028 0.3139 0.3431 0.0570  0.0505  0.0064  53  THR B CG2 
642  N N   . LYS B 45  ? 0.3991 0.3303 0.3517 0.0336  0.0490  0.0039  54  LYS B N   
643  C CA  . LYS B 45  ? 0.4112 0.3496 0.3653 0.0278  0.0466  -0.0010 54  LYS B CA  
644  C C   . LYS B 45  ? 0.4193 0.3585 0.3684 0.0284  0.0451  -0.0070 54  LYS B C   
645  O O   . LYS B 45  ? 0.4388 0.3816 0.3881 0.0251  0.0435  -0.0127 54  LYS B O   
646  C CB  . LYS B 45  ? 0.4617 0.3981 0.4240 0.0215  0.0466  -0.0037 54  LYS B CB  
647  C CG  . LYS B 45  ? 0.5469 0.4827 0.5166 0.0198  0.0494  0.0033  54  LYS B CG  
648  C CD  . LYS B 45  ? 0.6198 0.5683 0.5908 0.0199  0.0491  0.0081  54  LYS B CD  
649  C CE  . LYS B 45  ? 0.6968 0.6476 0.6775 0.0170  0.0525  0.0150  54  LYS B CE  
650  N NZ  . LYS B 45  ? 0.7242 0.6835 0.7020 0.0233  0.0546  0.0231  54  LYS B NZ  
651  N N   . GLY B 46  ? 0.4058 0.3430 0.3511 0.0329  0.0455  -0.0059 55  GLY B N   
652  C CA  . GLY B 46  ? 0.4224 0.3630 0.3646 0.0333  0.0450  -0.0102 55  GLY B CA  
653  C C   . GLY B 46  ? 0.4448 0.3806 0.3881 0.0349  0.0462  -0.0158 55  GLY B C   
654  O O   . GLY B 46  ? 0.4621 0.4033 0.4033 0.0357  0.0463  -0.0197 55  GLY B O   
655  N N   . ALA B 47  ? 0.4414 0.3674 0.3874 0.0360  0.0473  -0.0158 56  ALA B N   
656  C CA  . ALA B 47  ? 0.4461 0.3649 0.3915 0.0388  0.0477  -0.0214 56  ALA B CA  
657  C C   . ALA B 47  ? 0.4443 0.3633 0.3874 0.0453  0.0486  -0.0215 56  ALA B C   
658  O O   . ALA B 47  ? 0.4240 0.3441 0.3669 0.0478  0.0488  -0.0166 56  ALA B O   
659  C CB  . ALA B 47  ? 0.4640 0.3699 0.4127 0.0377  0.0485  -0.0202 56  ALA B CB  
660  N N   . ALA B 48  ? 0.4537 0.3718 0.3950 0.0489  0.0487  -0.0276 57  ALA B N   
661  C CA  . ALA B 48  ? 0.4630 0.3824 0.4032 0.0557  0.0493  -0.0286 57  ALA B CA  
662  C C   . ALA B 48  ? 0.4636 0.3700 0.4030 0.0608  0.0500  -0.0252 57  ALA B C   
663  O O   . ALA B 48  ? 0.4838 0.3790 0.4234 0.0589  0.0508  -0.0228 57  ALA B O   
664  C CB  . ALA B 48  ? 0.4855 0.4076 0.4233 0.0597  0.0492  -0.0365 57  ALA B CB  
665  N N   . LEU B 49  ? 0.4364 0.3453 0.3752 0.0670  0.0498  -0.0241 58  LEU B N   
666  C CA  . LEU B 49  ? 0.4504 0.3484 0.3866 0.0739  0.0505  -0.0207 58  LEU B CA  
667  C C   . LEU B 49  ? 0.4757 0.3725 0.4093 0.0827  0.0500  -0.0258 58  LEU B C   
668  O O   . LEU B 49  ? 0.4874 0.3962 0.4230 0.0835  0.0491  -0.0309 58  LEU B O   
669  C CB  . LEU B 49  ? 0.4390 0.3413 0.3755 0.0757  0.0493  -0.0153 58  LEU B CB  
670  C CG  . LEU B 49  ? 0.4459 0.3511 0.3840 0.0691  0.0491  -0.0104 58  LEU B CG  
671  C CD1 . LEU B 49  ? 0.4221 0.3313 0.3591 0.0727  0.0465  -0.0068 58  LEU B CD1 
672  C CD2 . LEU B 49  ? 0.4789 0.3744 0.4165 0.0673  0.0518  -0.0057 58  LEU B CD2 
673  N N   . ARG B 50  ? 0.4877 0.3710 0.4168 0.0897  0.0510  -0.0239 59  ARG B N   
674  C CA  . ARG B 50  ? 0.5149 0.3955 0.4400 0.1001  0.0502  -0.0283 59  ARG B CA  
675  C C   . ARG B 50  ? 0.5245 0.4066 0.4479 0.1080  0.0491  -0.0248 59  ARG B C   
676  O O   . ARG B 50  ? 0.5052 0.3810 0.4268 0.1079  0.0502  -0.0179 59  ARG B O   
677  C CB  . ARG B 50  ? 0.5612 0.4216 0.4804 0.1032  0.0518  -0.0282 59  ARG B CB  
678  C CG  . ARG B 50  ? 0.6596 0.5140 0.5726 0.1147  0.0510  -0.0333 59  ARG B CG  
679  C CD  . ARG B 50  ? 0.7184 0.5514 0.6259 0.1155  0.0516  -0.0344 59  ARG B CD  
680  N NE  . ARG B 50  ? 0.7450 0.5604 0.6509 0.1129  0.0543  -0.0253 59  ARG B NE  
681  C CZ  . ARG B 50  ? 0.7996 0.6048 0.6994 0.1215  0.0562  -0.0193 59  ARG B CZ  
682  N NH1 . ARG B 50  ? 0.8020 0.6138 0.6972 0.1333  0.0548  -0.0221 59  ARG B NH1 
683  N NH2 . ARG B 50  ? 0.8222 0.6126 0.7211 0.1186  0.0596  -0.0100 59  ARG B NH2 
684  N N   . SER B 51  ? 0.5444 0.4355 0.4682 0.1157  0.0467  -0.0298 60  SER B N   
685  C CA  . SER B 51  ? 0.5807 0.4724 0.5020 0.1255  0.0444  -0.0286 60  SER B CA  
686  C C   . SER B 51  ? 0.6087 0.4979 0.5255 0.1368  0.0438  -0.0343 60  SER B C   
687  O O   . SER B 51  ? 0.6020 0.5061 0.5239 0.1378  0.0419  -0.0409 60  SER B O   
688  C CB  . SER B 51  ? 0.6070 0.5161 0.5362 0.1226  0.0404  -0.0304 60  SER B CB  
689  O OG  . SER B 51  ? 0.6654 0.5737 0.5916 0.1326  0.0371  -0.0300 60  SER B OG  
690  N N   . GLY B 52  ? 0.6395 0.5104 0.5466 0.1450  0.0457  -0.0316 61  GLY B N   
691  C CA  . GLY B 52  ? 0.6615 0.5273 0.5623 0.1567  0.0450  -0.0371 61  GLY B CA  
692  C C   . GLY B 52  ? 0.6910 0.5581 0.5934 0.1523  0.0456  -0.0432 61  GLY B C   
693  O O   . GLY B 52  ? 0.6982 0.5555 0.6007 0.1433  0.0477  -0.0408 61  GLY B O   
694  N N   . GLU B 53  ? 0.6985 0.5809 0.6034 0.1580  0.0434  -0.0513 62  GLU B N   
695  C CA  . GLU B 53  ? 0.7159 0.6034 0.6218 0.1553  0.0439  -0.0576 62  GLU B CA  
696  C C   . GLU B 53  ? 0.6960 0.6058 0.6131 0.1438  0.0442  -0.0587 62  GLU B C   
697  O O   . GLU B 53  ? 0.7061 0.6241 0.6239 0.1427  0.0448  -0.0640 62  GLU B O   
698  C CB  . GLU B 53  ? 0.7820 0.6749 0.6834 0.1692  0.0421  -0.0657 62  GLU B CB  
699  C CG  . GLU B 53  ? 0.9117 0.7793 0.7997 0.1784  0.0421  -0.0676 62  GLU B CG  
700  C CD  . GLU B 53  ? 1.0711 0.9458 0.9538 0.1936  0.0398  -0.0763 62  GLU B CD  
701  O OE1 . GLU B 53  ? 1.0932 0.9874 0.9810 0.2000  0.0381  -0.0785 62  GLU B OE1 
702  O OE2 . GLU B 53  ? 1.1333 0.9944 1.0069 0.1994  0.0391  -0.0813 62  GLU B OE2 
703  N N   . GLY B 54  ? 0.6622 0.5809 0.5867 0.1364  0.0437  -0.0536 63  GLY B N   
704  C CA  . GLY B 54  ? 0.6309 0.5684 0.5652 0.1255  0.0440  -0.0531 63  GLY B CA  
705  C C   . GLY B 54  ? 0.6071 0.5369 0.5414 0.1140  0.0459  -0.0482 63  GLY B C   
706  O O   . GLY B 54  ? 0.6166 0.5284 0.5457 0.1132  0.0466  -0.0438 63  GLY B O   
707  N N   . ARG B 55  ? 0.5588 0.5029 0.4986 0.1056  0.0468  -0.0488 64  ARG B N   
708  C CA  . ARG B 55  ? 0.5524 0.4917 0.4920 0.0955  0.0480  -0.0451 64  ARG B CA  
709  C C   . ARG B 55  ? 0.5201 0.4713 0.4667 0.0874  0.0473  -0.0402 64  ARG B C   
710  O O   . ARG B 55  ? 0.5343 0.5025 0.4875 0.0866  0.0469  -0.0414 64  ARG B O   
711  C CB  . ARG B 55  ? 0.5777 0.5221 0.5154 0.0935  0.0494  -0.0500 64  ARG B CB  
712  C CG  . ARG B 55  ? 0.6157 0.5539 0.5521 0.0845  0.0499  -0.0476 64  ARG B CG  
713  C CD  . ARG B 55  ? 0.6575 0.6011 0.5906 0.0849  0.0503  -0.0539 64  ARG B CD  
714  N NE  . ARG B 55  ? 0.7124 0.6557 0.6452 0.0764  0.0503  -0.0524 64  ARG B NE  
715  C CZ  . ARG B 55  ? 0.7671 0.7003 0.6956 0.0756  0.0487  -0.0568 64  ARG B CZ  
716  N NH1 . ARG B 55  ? 0.7686 0.6885 0.6919 0.0824  0.0471  -0.0628 64  ARG B NH1 
717  N NH2 . ARG B 55  ? 0.7621 0.6977 0.6909 0.0685  0.0481  -0.0558 64  ARG B NH2 
718  N N   . LEU B 56  ? 0.4596 0.4022 0.4052 0.0816  0.0471  -0.0346 65  LEU B N   
719  C CA  . LEU B 56  ? 0.4376 0.3883 0.3878 0.0744  0.0458  -0.0302 65  LEU B CA  
720  C C   . LEU B 56  ? 0.4271 0.3787 0.3759 0.0665  0.0475  -0.0289 65  LEU B C   
721  O O   . LEU B 56  ? 0.4429 0.3831 0.3877 0.0652  0.0482  -0.0279 65  LEU B O   
722  C CB  . LEU B 56  ? 0.4362 0.3764 0.3843 0.0759  0.0437  -0.0251 65  LEU B CB  
723  C CG  . LEU B 56  ? 0.4890 0.4258 0.4364 0.0852  0.0412  -0.0258 65  LEU B CG  
724  C CD1 . LEU B 56  ? 0.4796 0.4111 0.4252 0.0855  0.0384  -0.0207 65  LEU B CD1 
725  C CD2 . LEU B 56  ? 0.5255 0.4766 0.4798 0.0871  0.0387  -0.0299 65  LEU B CD2 
726  N N   . ASP B 57  ? 0.4158 0.3812 0.3679 0.0613  0.0482  -0.0287 66  ASP B N   
727  C CA  . ASP B 57  ? 0.4076 0.3750 0.3571 0.0551  0.0496  -0.0276 66  ASP B CA  
728  C C   . ASP B 57  ? 0.3951 0.3626 0.3455 0.0489  0.0480  -0.0212 66  ASP B C   
729  O O   . ASP B 57  ? 0.3848 0.3559 0.3393 0.0480  0.0461  -0.0184 66  ASP B O   
730  C CB  . ASP B 57  ? 0.4533 0.4362 0.4037 0.0547  0.0520  -0.0306 66  ASP B CB  
731  C CG  . ASP B 57  ? 0.5405 0.5224 0.4880 0.0623  0.0529  -0.0379 66  ASP B CG  
732  O OD1 . ASP B 57  ? 0.5296 0.4963 0.4726 0.0651  0.0518  -0.0405 66  ASP B OD1 
733  O OD2 . ASP B 57  ? 0.5983 0.5945 0.5483 0.0658  0.0546  -0.0406 66  ASP B OD2 
734  N N   . PRO B 58  ? 0.4003 0.3631 0.3468 0.0451  0.0480  -0.0194 67  PRO B N   
735  C CA  . PRO B 58  ? 0.3912 0.3540 0.3368 0.0404  0.0462  -0.0137 67  PRO B CA  
736  C C   . PRO B 58  ? 0.3774 0.3518 0.3250 0.0362  0.0469  -0.0114 67  PRO B C   
737  O O   . PRO B 58  ? 0.3885 0.3732 0.3363 0.0358  0.0499  -0.0138 67  PRO B O   
738  C CB  . PRO B 58  ? 0.4072 0.3660 0.3487 0.0380  0.0464  -0.0137 67  PRO B CB  
739  C CG  . PRO B 58  ? 0.4370 0.3976 0.3775 0.0395  0.0483  -0.0200 67  PRO B CG  
740  C CD  . PRO B 58  ? 0.4217 0.3798 0.3645 0.0448  0.0489  -0.0231 67  PRO B CD  
741  N N   . TYR B 59  ? 0.3403 0.3126 0.2891 0.0337  0.0442  -0.0065 68  TYR B N   
742  C CA  . TYR B 59  ? 0.3275 0.3083 0.2790 0.0283  0.0446  -0.0026 68  TYR B CA  
743  C C   . TYR B 59  ? 0.3329 0.3087 0.2783 0.0246  0.0428  0.0027  68  TYR B C   
744  O O   . TYR B 59  ? 0.3318 0.3144 0.2752 0.0205  0.0451  0.0059  68  TYR B O   
745  C CB  . TYR B 59  ? 0.3377 0.3194 0.2971 0.0282  0.0415  -0.0017 68  TYR B CB  
746  C CG  . TYR B 59  ? 0.3304 0.3204 0.2954 0.0213  0.0416  0.0031  68  TYR B CG  
747  C CD1 . TYR B 59  ? 0.3488 0.3311 0.3107 0.0166  0.0384  0.0089  68  TYR B CD1 
748  C CD2 . TYR B 59  ? 0.3288 0.3341 0.3025 0.0194  0.0448  0.0025  68  TYR B CD2 
749  C CE1 . TYR B 59  ? 0.3573 0.3450 0.3248 0.0093  0.0385  0.0145  68  TYR B CE1 
750  C CE2 . TYR B 59  ? 0.3528 0.3668 0.3334 0.0119  0.0456  0.0083  68  TYR B CE2 
751  C CZ  . TYR B 59  ? 0.3622 0.3663 0.3399 0.0063  0.0424  0.0146  68  TYR B CZ  
752  O OH  . TYR B 59  ? 0.3845 0.3954 0.3696 -0.0021 0.0432  0.0214  68  TYR B OH  
753  N N   . TRP B 60  ? 0.3320 0.2970 0.2737 0.0266  0.0392  0.0040  69  TRP B N   
754  C CA  . TRP B 60  ? 0.3366 0.2964 0.2715 0.0248  0.0369  0.0085  69  TRP B CA  
755  C C   . TRP B 60  ? 0.3441 0.2972 0.2746 0.0291  0.0354  0.0073  69  TRP B C   
756  O O   . TRP B 60  ? 0.3437 0.2922 0.2765 0.0333  0.0345  0.0056  69  TRP B O   
757  C CB  . TRP B 60  ? 0.3528 0.3062 0.2885 0.0227  0.0321  0.0130  69  TRP B CB  
758  C CG  . TRP B 60  ? 0.3626 0.3072 0.2894 0.0235  0.0284  0.0168  69  TRP B CG  
759  C CD1 . TRP B 60  ? 0.3704 0.3157 0.2907 0.0204  0.0292  0.0209  69  TRP B CD1 
760  C CD2 . TRP B 60  ? 0.3550 0.2901 0.2770 0.0295  0.0239  0.0166  69  TRP B CD2 
761  N NE1 . TRP B 60  ? 0.3799 0.3163 0.2917 0.0241  0.0250  0.0228  69  TRP B NE1 
762  C CE2 . TRP B 60  ? 0.3683 0.2991 0.2813 0.0297  0.0217  0.0202  69  TRP B CE2 
763  C CE3 . TRP B 60  ? 0.3660 0.2966 0.2893 0.0356  0.0216  0.0140  69  TRP B CE3 
764  C CZ2 . TRP B 60  ? 0.3919 0.3151 0.2979 0.0359  0.0173  0.0209  69  TRP B CZ2 
765  C CZ3 . TRP B 60  ? 0.3833 0.3069 0.2996 0.0416  0.0179  0.0153  69  TRP B CZ3 
766  C CH2 . TRP B 60  ? 0.3903 0.3108 0.2983 0.0419  0.0157  0.0185  69  TRP B CH2 
767  N N   . GLY B 61  ? 0.3491 0.3024 0.2735 0.0285  0.0352  0.0089  70  GLY B N   
768  C CA  . GLY B 61  ? 0.3686 0.3181 0.2904 0.0321  0.0339  0.0087  70  GLY B CA  
769  C C   . GLY B 61  ? 0.3632 0.3137 0.2780 0.0319  0.0321  0.0112  70  GLY B C   
770  O O   . GLY B 61  ? 0.3591 0.3137 0.2703 0.0289  0.0330  0.0121  70  GLY B O   
771  N N   . ASP B 62  ? 0.3511 0.2993 0.2635 0.0359  0.0301  0.0124  71  ASP B N   
772  C CA  . ASP B 62  ? 0.3670 0.3173 0.2724 0.0372  0.0279  0.0145  71  ASP B CA  
773  C C   . ASP B 62  ? 0.3584 0.3119 0.2657 0.0409  0.0278  0.0143  71  ASP B C   
774  O O   . ASP B 62  ? 0.3605 0.3098 0.2679 0.0457  0.0266  0.0162  71  ASP B O   
775  C CB  . ASP B 62  ? 0.3835 0.3254 0.2812 0.0392  0.0234  0.0187  71  ASP B CB  
776  C CG  . ASP B 62  ? 0.4719 0.4151 0.3605 0.0412  0.0211  0.0209  71  ASP B CG  
777  O OD1 . ASP B 62  ? 0.4432 0.3892 0.3295 0.0460  0.0195  0.0208  71  ASP B OD1 
778  O OD2 . ASP B 62  ? 0.5363 0.4795 0.4201 0.0382  0.0215  0.0226  71  ASP B OD2 
779  N N   . VAL B 63  ? 0.3469 0.3090 0.2563 0.0388  0.0291  0.0120  72  VAL B N   
780  C CA  . VAL B 63  ? 0.3412 0.3094 0.2552 0.0408  0.0296  0.0124  72  VAL B CA  
781  C C   . VAL B 63  ? 0.3615 0.3302 0.2689 0.0475  0.0264  0.0164  72  VAL B C   
782  O O   . VAL B 63  ? 0.3839 0.3556 0.2947 0.0513  0.0274  0.0187  72  VAL B O   
783  C CB  . VAL B 63  ? 0.3596 0.3376 0.2783 0.0362  0.0303  0.0081  72  VAL B CB  
784  C CG1 . VAL B 63  ? 0.3781 0.3662 0.3015 0.0375  0.0297  0.0092  72  VAL B CG1 
785  C CG2 . VAL B 63  ? 0.3601 0.3363 0.2866 0.0312  0.0332  0.0037  72  VAL B CG2 
786  N N   . LYS B 64  ? 0.3754 0.3418 0.2729 0.0497  0.0228  0.0176  73  LYS B N   
787  C CA  . LYS B 64  ? 0.3955 0.3618 0.2850 0.0577  0.0189  0.0207  73  LYS B CA  
788  C C   . LYS B 64  ? 0.4011 0.3571 0.2872 0.0637  0.0168  0.0232  73  LYS B C   
789  O O   . LYS B 64  ? 0.4229 0.3822 0.3072 0.0711  0.0158  0.0251  73  LYS B O   
790  C CB  . LYS B 64  ? 0.4042 0.3683 0.2824 0.0593  0.0151  0.0215  73  LYS B CB  
791  C CG  . LYS B 64  ? 0.4610 0.4258 0.3302 0.0689  0.0107  0.0239  73  LYS B CG  
792  C CD  . LYS B 64  ? 0.4839 0.4456 0.3407 0.0714  0.0069  0.0249  73  LYS B CD  
793  C CE  . LYS B 64  ? 0.5257 0.4844 0.3714 0.0825  0.0015  0.0270  73  LYS B CE  
794  N NZ  . LYS B 64  ? 0.5423 0.4977 0.3744 0.0862  -0.0024 0.0281  73  LYS B NZ  
795  N N   . GLN B 65  ? 0.3769 0.3222 0.2629 0.0609  0.0161  0.0229  74  GLN B N   
796  C CA  . GLN B 65  ? 0.3799 0.3155 0.2640 0.0664  0.0133  0.0238  74  GLN B CA  
797  C C   . GLN B 65  ? 0.3840 0.3243 0.2764 0.0676  0.0177  0.0233  74  GLN B C   
798  O O   . GLN B 65  ? 0.3948 0.3303 0.2844 0.0752  0.0157  0.0243  74  GLN B O   
799  C CB  . GLN B 65  ? 0.3977 0.3229 0.2822 0.0617  0.0113  0.0231  74  GLN B CB  
800  C CG  . GLN B 65  ? 0.4539 0.3711 0.3298 0.0601  0.0069  0.0252  74  GLN B CG  
801  C CD  . GLN B 65  ? 0.5516 0.4597 0.4306 0.0545  0.0051  0.0255  74  GLN B CD  
802  O OE1 . GLN B 65  ? 0.5878 0.4904 0.4705 0.0566  0.0026  0.0240  74  GLN B OE1 
803  N NE2 . GLN B 65  ? 0.5612 0.4687 0.4392 0.0476  0.0064  0.0278  74  GLN B NE2 
804  N N   . ASP B 66  ? 0.3642 0.3122 0.2657 0.0611  0.0231  0.0218  75  ASP B N   
805  C CA  . ASP B 66  ? 0.3504 0.3004 0.2597 0.0611  0.0277  0.0219  75  ASP B CA  
806  C C   . ASP B 66  ? 0.3611 0.3017 0.2708 0.0625  0.0271  0.0207  75  ASP B C   
807  O O   . ASP B 66  ? 0.3528 0.2916 0.2639 0.0678  0.0287  0.0220  75  ASP B O   
808  C CB  . ASP B 66  ? 0.3726 0.3292 0.2822 0.0680  0.0293  0.0260  75  ASP B CB  
809  C CG  . ASP B 66  ? 0.4006 0.3603 0.3195 0.0655  0.0353  0.0273  75  ASP B CG  
810  O OD1 . ASP B 66  ? 0.3818 0.3410 0.3077 0.0576  0.0378  0.0244  75  ASP B OD1 
811  O OD2 . ASP B 66  ? 0.4013 0.3639 0.3201 0.0720  0.0374  0.0318  75  ASP B OD2 
812  N N   . LEU B 67  ? 0.3550 0.2918 0.2654 0.0573  0.0258  0.0180  76  LEU B N   
813  C CA  . LEU B 67  ? 0.3583 0.2890 0.2712 0.0579  0.0250  0.0162  76  LEU B CA  
814  C C   . LEU B 67  ? 0.3577 0.2912 0.2767 0.0506  0.0282  0.0130  76  LEU B C   
815  O O   . LEU B 67  ? 0.3547 0.2928 0.2736 0.0452  0.0294  0.0124  76  LEU B O   
816  C CB  . LEU B 67  ? 0.3733 0.2962 0.2807 0.0603  0.0185  0.0166  76  LEU B CB  
817  C CG  . LEU B 67  ? 0.3809 0.2988 0.2804 0.0701  0.0136  0.0184  76  LEU B CG  
818  C CD1 . LEU B 67  ? 0.3951 0.3026 0.2897 0.0709  0.0059  0.0178  76  LEU B CD1 
819  C CD2 . LEU B 67  ? 0.4044 0.3216 0.3049 0.0782  0.0150  0.0182  76  LEU B CD2 
820  N N   . VAL B 68  ? 0.3519 0.2830 0.2750 0.0518  0.0290  0.0108  77  VAL B N   
821  C CA  . VAL B 68  ? 0.3483 0.2831 0.2769 0.0467  0.0319  0.0073  77  VAL B CA  
822  C C   . VAL B 68  ? 0.3452 0.2775 0.2770 0.0496  0.0299  0.0054  77  VAL B C   
823  O O   . VAL B 68  ? 0.3416 0.2690 0.2720 0.0565  0.0281  0.0056  77  VAL B O   
824  C CB  . VAL B 68  ? 0.3649 0.3023 0.2969 0.0451  0.0367  0.0050  77  VAL B CB  
825  C CG1 . VAL B 68  ? 0.3720 0.3041 0.3050 0.0508  0.0382  0.0059  77  VAL B CG1 
826  C CG2 . VAL B 68  ? 0.3603 0.3019 0.2960 0.0415  0.0391  0.0006  77  VAL B CG2 
827  N N   . SER B 69  ? 0.3321 0.2695 0.2684 0.0449  0.0303  0.0035  78  SER B N   
828  C CA  . SER B 69  ? 0.3286 0.2673 0.2704 0.0467  0.0287  0.0009  78  SER B CA  
829  C C   . SER B 69  ? 0.3389 0.2856 0.2855 0.0447  0.0334  -0.0027 78  SER B C   
830  O O   . SER B 69  ? 0.3333 0.2854 0.2793 0.0403  0.0368  -0.0029 78  SER B O   
831  C CB  . SER B 69  ? 0.3488 0.2876 0.2932 0.0430  0.0239  0.0025  78  SER B CB  
832  O OG  . SER B 69  ? 0.3531 0.2989 0.2998 0.0350  0.0263  0.0045  78  SER B OG  
833  N N   . TYR B 70  ? 0.3329 0.2804 0.2834 0.0495  0.0330  -0.0060 79  TYR B N   
834  C CA  . TYR B 70  ? 0.3360 0.2906 0.2901 0.0502  0.0367  -0.0103 79  TYR B CA  
835  C C   . TYR B 70  ? 0.3526 0.3164 0.3148 0.0502  0.0347  -0.0124 79  TYR B C   
836  O O   . TYR B 70  ? 0.3486 0.3093 0.3129 0.0534  0.0299  -0.0127 79  TYR B O   
837  C CB  . TYR B 70  ? 0.3381 0.2846 0.2890 0.0580  0.0382  -0.0127 79  TYR B CB  
838  C CG  . TYR B 70  ? 0.3357 0.2751 0.2817 0.0568  0.0409  -0.0109 79  TYR B CG  
839  C CD1 . TYR B 70  ? 0.3409 0.2742 0.2833 0.0571  0.0397  -0.0064 79  TYR B CD1 
840  C CD2 . TYR B 70  ? 0.3484 0.2878 0.2940 0.0557  0.0442  -0.0142 79  TYR B CD2 
841  C CE1 . TYR B 70  ? 0.3591 0.2888 0.2995 0.0549  0.0421  -0.0046 79  TYR B CE1 
842  C CE2 . TYR B 70  ? 0.3564 0.2901 0.2996 0.0530  0.0457  -0.0131 79  TYR B CE2 
843  C CZ  . TYR B 70  ? 0.3772 0.3069 0.3188 0.0521  0.0449  -0.0081 79  TYR B CZ  
844  O OH  . TYR B 70  ? 0.3911 0.3178 0.3327 0.0488  0.0464  -0.0069 79  TYR B OH  
845  N N   . CYS B 71  ? 0.3475 0.3239 0.3144 0.0475  0.0381  -0.0145 80  CYS B N   
846  C CA  . CYS B 71  ? 0.3698 0.3597 0.3466 0.0469  0.0374  -0.0165 80  CYS B CA  
847  C C   . CYS B 71  ? 0.3745 0.3704 0.3585 0.0385  0.0349  -0.0120 80  CYS B C   
848  O O   . CYS B 71  ? 0.4049 0.4152 0.3993 0.0356  0.0352  -0.0126 80  CYS B O   
849  C CB  . CYS B 71  ? 0.3895 0.3776 0.3689 0.0552  0.0340  -0.0209 80  CYS B CB  
850  S SG  . CYS B 71  ? 0.4578 0.4349 0.4278 0.0656  0.0366  -0.0248 80  CYS B SG  
851  N N   . GLY B 72  ? 0.3494 0.3350 0.3285 0.0346  0.0324  -0.0075 81  GLY B N   
852  C CA  . GLY B 72  ? 0.3379 0.3254 0.3225 0.0264  0.0295  -0.0027 81  GLY B CA  
853  C C   . GLY B 72  ? 0.3402 0.3131 0.3158 0.0251  0.0262  0.0014  81  GLY B C   
854  O O   . GLY B 72  ? 0.3472 0.3113 0.3135 0.0301  0.0268  0.0007  81  GLY B O   
855  N N   . PRO B 73  ? 0.3498 0.3202 0.3284 0.0180  0.0228  0.0062  82  PRO B N   
856  C CA  . PRO B 73  ? 0.3601 0.3161 0.3289 0.0176  0.0192  0.0100  82  PRO B CA  
857  C C   . PRO B 73  ? 0.3735 0.3160 0.3373 0.0253  0.0120  0.0072  82  PRO B C   
858  O O   . PRO B 73  ? 0.3816 0.3246 0.3514 0.0290  0.0079  0.0030  82  PRO B O   
859  C CB  . PRO B 73  ? 0.3760 0.3322 0.3500 0.0079  0.0174  0.0161  82  PRO B CB  
860  C CG  . PRO B 73  ? 0.3855 0.3529 0.3749 0.0044  0.0162  0.0139  82  PRO B CG  
861  C CD  . PRO B 73  ? 0.3563 0.3371 0.3479 0.0100  0.0222  0.0086  82  PRO B CD  
862  N N   . TRP B 74  ? 0.3675 0.2991 0.3202 0.0282  0.0101  0.0095  83  TRP B N   
863  C CA  . TRP B 74  ? 0.3818 0.3015 0.3274 0.0373  0.0038  0.0075  83  TRP B CA  
864  C C   . TRP B 74  ? 0.3862 0.2991 0.3371 0.0369  -0.0053 0.0057  83  TRP B C   
865  O O   . TRP B 74  ? 0.4073 0.3162 0.3610 0.0293  -0.0086 0.0091  83  TRP B O   
866  C CB  . TRP B 74  ? 0.3852 0.2968 0.3188 0.0391  0.0031  0.0113  83  TRP B CB  
867  C CG  . TRP B 74  ? 0.3942 0.2965 0.3194 0.0499  -0.0022 0.0097  83  TRP B CG  
868  C CD1 . TRP B 74  ? 0.4068 0.2970 0.3272 0.0542  -0.0113 0.0091  83  TRP B CD1 
869  C CD2 . TRP B 74  ? 0.3944 0.2988 0.3147 0.0581  0.0014  0.0089  83  TRP B CD2 
870  N NE1 . TRP B 74  ? 0.4150 0.3013 0.3269 0.0661  -0.0134 0.0076  83  TRP B NE1 
871  C CE2 . TRP B 74  ? 0.4052 0.3007 0.3177 0.0681  -0.0052 0.0081  83  TRP B CE2 
872  C CE3 . TRP B 74  ? 0.3880 0.3005 0.3101 0.0580  0.0092  0.0087  83  TRP B CE3 
873  C CZ2 . TRP B 74  ? 0.4064 0.3031 0.3131 0.0780  -0.0030 0.0084  83  TRP B CZ2 
874  C CZ3 . TRP B 74  ? 0.3831 0.2949 0.3006 0.0662  0.0110  0.0091  83  TRP B CZ3 
875  C CH2 . TRP B 74  ? 0.3875 0.2925 0.2976 0.0762  0.0055  0.0094  83  TRP B CH2 
876  N N   . LYS B 75  ? 0.3773 0.2880 0.3291 0.0454  -0.0098 0.0005  84  LYS B N   
877  C CA  . LYS B 75  ? 0.3906 0.2962 0.3489 0.0455  -0.0196 -0.0029 84  LYS B CA  
878  C C   . LYS B 75  ? 0.4267 0.3167 0.3740 0.0553  -0.0290 -0.0049 84  LYS B C   
879  O O   . LYS B 75  ? 0.4617 0.3444 0.4132 0.0552  -0.0389 -0.0083 84  LYS B O   
880  C CB  . LYS B 75  ? 0.3913 0.3066 0.3582 0.0501  -0.0195 -0.0088 84  LYS B CB  
881  C CG  . LYS B 75  ? 0.4020 0.3344 0.3799 0.0430  -0.0111 -0.0084 84  LYS B CG  
882  C CD  . LYS B 75  ? 0.4355 0.3746 0.4271 0.0305  -0.0131 -0.0063 84  LYS B CD  
883  C CE  . LYS B 75  ? 0.4843 0.4430 0.4869 0.0251  -0.0050 -0.0061 84  LYS B CE  
884  N NZ  . LYS B 75  ? 0.5336 0.5017 0.5516 0.0132  -0.0065 -0.0033 84  LYS B NZ  
885  N N   . LEU B 76  ? 0.4194 0.3055 0.3539 0.0644  -0.0264 -0.0036 85  LEU B N   
886  C CA  . LEU B 76  ? 0.4314 0.3055 0.3540 0.0769  -0.0346 -0.0058 85  LEU B CA  
887  C C   . LEU B 76  ? 0.4648 0.3261 0.3798 0.0746  -0.0405 -0.0030 85  LEU B C   
888  O O   . LEU B 76  ? 0.4638 0.3262 0.3737 0.0710  -0.0351 0.0021  85  LEU B O   
889  C CB  . LEU B 76  ? 0.4370 0.3144 0.3499 0.0881  -0.0288 -0.0047 85  LEU B CB  
890  C CG  . LEU B 76  ? 0.4314 0.3199 0.3502 0.0895  -0.0208 -0.0058 85  LEU B CG  
891  C CD1 . LEU B 76  ? 0.4518 0.3422 0.3617 0.0990  -0.0146 -0.0030 85  LEU B CD1 
892  C CD2 . LEU B 76  ? 0.4542 0.3437 0.3794 0.0939  -0.0266 -0.0121 85  LEU B CD2 
893  N N   . ASP B 77  ? 0.4999 0.3484 0.4135 0.0779  -0.0527 -0.0069 86  ASP B N   
894  C CA  . ASP B 77  ? 0.5429 0.3762 0.4491 0.0755  -0.0596 -0.0044 86  ASP B CA  
895  C C   . ASP B 77  ? 0.5435 0.3613 0.4361 0.0897  -0.0714 -0.0089 86  ASP B C   
896  O O   . ASP B 77  ? 0.5586 0.3618 0.4423 0.0899  -0.0777 -0.0071 86  ASP B O   
897  C CB  . ASP B 77  ? 0.6138 0.4431 0.5329 0.0602  -0.0631 -0.0028 86  ASP B CB  
898  C CG  . ASP B 77  ? 0.7230 0.5520 0.6552 0.0583  -0.0716 -0.0092 86  ASP B CG  
899  O OD1 . ASP B 77  ? 0.7605 0.5943 0.6919 0.0691  -0.0736 -0.0155 86  ASP B OD1 
900  O OD2 . ASP B 77  ? 0.7828 0.6073 0.7262 0.0459  -0.0761 -0.0078 86  ASP B OD2 
901  N N   . ALA B 78  ? 0.5275 0.3480 0.4163 0.1029  -0.0742 -0.0144 87  ALA B N   
902  C CA  . ALA B 78  ? 0.5359 0.3431 0.4096 0.1191  -0.0852 -0.0190 87  ALA B CA  
903  C C   . ALA B 78  ? 0.5425 0.3492 0.4005 0.1276  -0.0811 -0.0142 87  ALA B C   
904  O O   . ALA B 78  ? 0.5224 0.3426 0.3811 0.1248  -0.0688 -0.0085 87  ALA B O   
905  C CB  . ALA B 78  ? 0.5205 0.3327 0.3925 0.1329  -0.0881 -0.0253 87  ALA B CB  
906  N N   . ALA B 79  ? 0.5590 0.3502 0.4028 0.1385  -0.0922 -0.0171 88  ALA B N   
907  C CA  . ALA B 79  ? 0.5808 0.3718 0.4091 0.1481  -0.0899 -0.0132 88  ALA B CA  
908  C C   . ALA B 79  ? 0.5920 0.3784 0.4042 0.1697  -0.0977 -0.0181 88  ALA B C   
909  O O   . ALA B 79  ? 0.6178 0.3912 0.4274 0.1764  -0.1105 -0.0256 88  ALA B O   
910  C CB  . ALA B 79  ? 0.6163 0.3917 0.4401 0.1407  -0.0954 -0.0106 88  ALA B CB  
911  N N   . TRP B 80  ? 0.5784 0.3763 0.3799 0.1812  -0.0907 -0.0140 89  TRP B N   
912  C CA  . TRP B 80  ? 0.5956 0.3917 0.3797 0.2037  -0.0971 -0.0174 89  TRP B CA  
913  C C   . TRP B 80  ? 0.6236 0.3965 0.3949 0.2099  -0.1127 -0.0225 89  TRP B C   
914  O O   . TRP B 80  ? 0.6250 0.3897 0.3963 0.1998  -0.1133 -0.0192 89  TRP B O   
915  C CB  . TRP B 80  ? 0.6009 0.4150 0.3774 0.2125  -0.0861 -0.0104 89  TRP B CB  
916  C CG  . TRP B 80  ? 0.6141 0.4301 0.3724 0.2369  -0.0911 -0.0127 89  TRP B CG  
917  C CD1 . TRP B 80  ? 0.6422 0.4559 0.3935 0.2522  -0.0973 -0.0183 89  TRP B CD1 
918  C CD2 . TRP B 80  ? 0.6295 0.4518 0.3736 0.2499  -0.0903 -0.0096 89  TRP B CD2 
919  N NE1 . TRP B 80  ? 0.6512 0.4683 0.3839 0.2744  -0.1007 -0.0188 89  TRP B NE1 
920  C CE2 . TRP B 80  ? 0.6500 0.4733 0.3786 0.2732  -0.0961 -0.0133 89  TRP B CE2 
921  C CE3 . TRP B 80  ? 0.6325 0.4603 0.3750 0.2450  -0.0858 -0.0044 89  TRP B CE3 
922  C CZ2 . TRP B 80  ? 0.6692 0.5011 0.3818 0.2913  -0.0962 -0.0112 89  TRP B CZ2 
923  C CZ3 . TRP B 80  ? 0.6506 0.4861 0.3775 0.2629  -0.0868 -0.0030 89  TRP B CZ3 
924  C CH2 . TRP B 80  ? 0.6593 0.4980 0.3721 0.2856  -0.0913 -0.0060 89  TRP B CH2 
925  N N   . ASP B 81  ? 0.6601 0.4211 0.4210 0.2257  -0.1260 -0.0310 90  ASP B N   
926  C CA  . ASP B 81  ? 0.7078 0.4439 0.4554 0.2330  -0.1425 -0.0370 90  ASP B CA  
927  C C   . ASP B 81  ? 0.7526 0.4891 0.4800 0.2493  -0.1433 -0.0347 90  ASP B C   
928  O O   . ASP B 81  ? 0.7765 0.4911 0.4902 0.2574  -0.1573 -0.0398 90  ASP B O   
929  C CB  . ASP B 81  ? 0.7241 0.4458 0.4674 0.2446  -0.1584 -0.0484 90  ASP B CB  
930  C CG  . ASP B 81  ? 0.7884 0.5210 0.5174 0.2691  -0.1590 -0.0519 90  ASP B CG  
931  O OD1 . ASP B 81  ? 0.7724 0.5231 0.4937 0.2783  -0.1474 -0.0450 90  ASP B OD1 
932  O OD2 . ASP B 81  ? 0.8579 0.5824 0.5844 0.2791  -0.1706 -0.0614 90  ASP B OD2 
933  N N   . GLY B 82  ? 0.7495 0.5100 0.4744 0.2561  -0.1297 -0.0281 91  GLY B N   
934  C CA  . GLY B 82  ? 0.7618 0.5272 0.4691 0.2719  -0.1295 -0.0256 91  GLY B CA  
935  C C   . GLY B 82  ? 0.7897 0.5534 0.4769 0.2995  -0.1387 -0.0318 91  GLY B C   
936  O O   . GLY B 82  ? 0.8122 0.5806 0.4835 0.3153  -0.1397 -0.0305 91  GLY B O   
937  N N   . LEU B 83  ? 0.7876 0.5451 0.4746 0.3067  -0.1461 -0.0389 92  LEU B N   
938  C CA  . LEU B 83  ? 0.8107 0.5653 0.4771 0.3344  -0.1563 -0.0460 92  LEU B CA  
939  C C   . LEU B 83  ? 0.7911 0.5640 0.4589 0.3450  -0.1493 -0.0455 92  LEU B C   
940  O O   . LEU B 83  ? 0.7995 0.5830 0.4506 0.3688  -0.1494 -0.0459 92  LEU B O   
941  C CB  . LEU B 83  ? 0.8492 0.5721 0.5090 0.3383  -0.1778 -0.0586 92  LEU B CB  
942  C CG  . LEU B 83  ? 0.9056 0.6019 0.5570 0.3351  -0.1907 -0.0619 92  LEU B CG  
943  C CD1 . LEU B 83  ? 0.9328 0.5989 0.5804 0.3384  -0.2120 -0.0747 92  LEU B CD1 
944  C CD2 . LEU B 83  ? 0.9169 0.6157 0.5438 0.3585  -0.1933 -0.0615 92  LEU B CD2 
945  N N   . SER B 84  ? 0.7624 0.5370 0.4483 0.3294  -0.1452 -0.0456 93  SER B N   
946  C CA  . SER B 84  ? 0.7609 0.5468 0.4469 0.3400  -0.1421 -0.0472 93  SER B CA  
947  C C   . SER B 84  ? 0.7297 0.5423 0.4247 0.3359  -0.1218 -0.0357 93  SER B C   
948  O O   . SER B 84  ? 0.7100 0.5318 0.4180 0.3179  -0.1099 -0.0273 93  SER B O   
949  C CB  . SER B 84  ? 0.7846 0.5568 0.4840 0.3285  -0.1511 -0.0555 93  SER B CB  
950  O OG  . SER B 84  ? 0.8550 0.6008 0.5522 0.3249  -0.1691 -0.0648 93  SER B OG  
951  N N   . GLU B 85  ? 0.7164 0.5404 0.4048 0.3521  -0.1183 -0.0352 94  GLU B N   
952  C CA  . GLU B 85  ? 0.6902 0.5366 0.3878 0.3474  -0.0995 -0.0241 94  GLU B CA  
953  C C   . GLU B 85  ? 0.6739 0.5172 0.3931 0.3239  -0.0952 -0.0241 94  GLU B C   
954  O O   . GLU B 85  ? 0.6695 0.4963 0.3951 0.3157  -0.1068 -0.0332 94  GLU B O   
955  C CB  . GLU B 85  ? 0.6941 0.5527 0.3771 0.3723  -0.0965 -0.0224 94  GLU B CB  
956  C CG  . GLU B 85  ? 0.7471 0.6150 0.4104 0.3943  -0.0968 -0.0196 94  GLU B CG  
957  C CD  . GLU B 85  ? 0.8199 0.7068 0.4700 0.4174  -0.0883 -0.0131 94  GLU B CD  
958  O OE1 . GLU B 85  ? 0.8014 0.6887 0.4522 0.4219  -0.0869 -0.0141 94  GLU B OE1 
959  O OE2 . GLU B 85  ? 0.8783 0.7809 0.5174 0.4313  -0.0825 -0.0064 94  GLU B OE2 
960  N N   . VAL B 86  ? 0.6484 0.5076 0.3798 0.3116  -0.0785 -0.0137 95  VAL B N   
961  C CA  . VAL B 86  ? 0.5930 0.4522 0.3436 0.2910  -0.0723 -0.0127 95  VAL B CA  
962  C C   . VAL B 86  ? 0.5919 0.4663 0.3444 0.2960  -0.0588 -0.0049 95  VAL B C   
963  O O   . VAL B 86  ? 0.6029 0.4882 0.3427 0.3137  -0.0536 0.0006  95  VAL B O   
964  C CB  . VAL B 86  ? 0.5645 0.4266 0.3288 0.2687  -0.0648 -0.0070 95  VAL B CB  
965  C CG1 . VAL B 86  ? 0.5768 0.4241 0.3367 0.2656  -0.0767 -0.0124 95  VAL B CG1 
966  C CG2 . VAL B 86  ? 0.5667 0.4481 0.3314 0.2693  -0.0497 0.0045  95  VAL B CG2 
967  N N   . GLN B 87  ? 0.5674 0.4423 0.3348 0.2814  -0.0529 -0.0042 96  GLN B N   
968  C CA  . GLN B 87  ? 0.5561 0.4425 0.3258 0.2839  -0.0399 0.0038  96  GLN B CA  
969  C C   . GLN B 87  ? 0.5406 0.4330 0.3276 0.2618  -0.0276 0.0108  96  GLN B C   
970  O O   . GLN B 87  ? 0.5579 0.4438 0.3572 0.2452  -0.0305 0.0062  96  GLN B O   
971  C CB  . GLN B 87  ? 0.5637 0.4449 0.3311 0.2931  -0.0451 -0.0026 96  GLN B CB  
972  C CG  . GLN B 87  ? 0.5958 0.4760 0.3421 0.3205  -0.0535 -0.0065 96  GLN B CG  
973  C CD  . GLN B 87  ? 0.6220 0.4982 0.3641 0.3323  -0.0594 -0.0132 96  GLN B CD  
974  O OE1 . GLN B 87  ? 0.6009 0.4758 0.3548 0.3218  -0.0569 -0.0148 96  GLN B OE1 
975  N NE2 . GLN B 87  ? 0.6636 0.5380 0.3865 0.3571  -0.0685 -0.0183 96  GLN B NE2 
976  N N   . LEU B 88  ? 0.5329 0.4381 0.3208 0.2623  -0.0141 0.0217  97  LEU B N   
977  C CA  . LEU B 88  ? 0.5188 0.4291 0.3221 0.2438  -0.0023 0.0280  97  LEU B CA  
978  C C   . LEU B 88  ? 0.5211 0.4291 0.3260 0.2469  0.0020  0.0287  97  LEU B C   
979  O O   . LEU B 88  ? 0.5324 0.4442 0.3263 0.2635  0.0055  0.0334  97  LEU B O   
980  C CB  . LEU B 88  ? 0.5056 0.4303 0.3116 0.2410  0.0097  0.0394  97  LEU B CB  
981  C CG  . LEU B 88  ? 0.5160 0.4452 0.3368 0.2246  0.0218  0.0462  97  LEU B CG  
982  C CD1 . LEU B 88  ? 0.4931 0.4165 0.3274 0.2039  0.0191  0.0405  97  LEU B CD1 
983  C CD2 . LEU B 88  ? 0.5332 0.4775 0.3562 0.2248  0.0330  0.0578  97  LEU B CD2 
984  N N   . LEU B 89  ? 0.5119 0.4141 0.3291 0.2324  0.0018  0.0244  98  LEU B N   
985  C CA  . LEU B 89  ? 0.5029 0.4029 0.3218 0.2346  0.0061  0.0250  98  LEU B CA  
986  C C   . LEU B 89  ? 0.5125 0.4179 0.3405 0.2226  0.0200  0.0351  98  LEU B C   
987  O O   . LEU B 89  ? 0.4744 0.3779 0.3153 0.2055  0.0225  0.0334  98  LEU B O   
988  C CB  . LEU B 89  ? 0.5289 0.4214 0.3559 0.2271  -0.0023 0.0144  98  LEU B CB  
989  C CG  . LEU B 89  ? 0.5827 0.4729 0.4114 0.2303  0.0005  0.0131  98  LEU B CG  
990  C CD1 . LEU B 89  ? 0.6321 0.5226 0.4453 0.2521  0.0017  0.0165  98  LEU B CD1 
991  C CD2 . LEU B 89  ? 0.6012 0.4873 0.4383 0.2242  -0.0095 0.0017  98  LEU B CD2 
992  N N   . ALA B 90  ? 0.5099 0.4228 0.3316 0.2311  0.0288  0.0456  99  ALA B N   
993  C CA  . ALA B 90  ? 0.5181 0.4366 0.3488 0.2205  0.0417  0.0563  99  ALA B CA  
994  C C   . ALA B 90  ? 0.5070 0.4182 0.3412 0.2176  0.0474  0.0583  99  ALA B C   
995  O O   . ALA B 90  ? 0.5084 0.4159 0.3322 0.2323  0.0478  0.0597  99  ALA B O   
996  C CB  . ALA B 90  ? 0.5268 0.4570 0.3503 0.2314  0.0495  0.0678  99  ALA B CB  
997  N N   . VAL B 91  ? 0.4934 0.4022 0.3410 0.1999  0.0521  0.0588  100 VAL B N   
998  C CA  . VAL B 91  ? 0.4854 0.3860 0.3364 0.1963  0.0578  0.0610  100 VAL B CA  
999  C C   . VAL B 91  ? 0.5039 0.4072 0.3634 0.1856  0.0690  0.0719  100 VAL B C   
1000 O O   . VAL B 91  ? 0.4783 0.3803 0.3497 0.1696  0.0702  0.0698  100 VAL B O   
1001 C CB  . VAL B 91  ? 0.4967 0.3899 0.3552 0.1865  0.0519  0.0500  100 VAL B CB  
1002 C CG1 . VAL B 91  ? 0.5081 0.3920 0.3673 0.1863  0.0571  0.0517  100 VAL B CG1 
1003 C CG2 . VAL B 91  ? 0.5075 0.3999 0.3609 0.1945  0.0402  0.0393  100 VAL B CG2 
1004 N N   . PRO B 92  ? 0.5181 0.4263 0.3723 0.1942  0.0772  0.0841  101 PRO B N   
1005 C CA  . PRO B 92  ? 0.5068 0.4189 0.3718 0.1824  0.0877  0.0952  101 PRO B CA  
1006 C C   . PRO B 92  ? 0.4959 0.3941 0.3661 0.1747  0.0932  0.0982  101 PRO B C   
1007 O O   . PRO B 92  ? 0.5111 0.3979 0.3723 0.1842  0.0918  0.0958  101 PRO B O   
1008 C CB  . PRO B 92  ? 0.5423 0.4649 0.3986 0.1965  0.0949  0.1080  101 PRO B CB  
1009 C CG  . PRO B 92  ? 0.5614 0.4865 0.4019 0.2155  0.0864  0.1015  101 PRO B CG  
1010 C CD  . PRO B 92  ? 0.5444 0.4559 0.3828 0.2153  0.0773  0.0885  101 PRO B CD  
1011 N N   . PRO B 93  ? 0.4909 0.3894 0.3749 0.1585  0.0992  0.1035  102 PRO B N   
1012 C CA  . PRO B 93  ? 0.5024 0.3849 0.3911 0.1509  0.1034  0.1056  102 PRO B CA  
1013 C C   . PRO B 93  ? 0.5323 0.4061 0.4097 0.1644  0.1105  0.1166  102 PRO B C   
1014 O O   . PRO B 93  ? 0.5490 0.4327 0.4225 0.1722  0.1171  0.1284  102 PRO B O   
1015 C CB  . PRO B 93  ? 0.5124 0.3996 0.4178 0.1328  0.1085  0.1112  102 PRO B CB  
1016 C CG  . PRO B 93  ? 0.5077 0.4105 0.4185 0.1275  0.1024  0.1037  102 PRO B CG  
1017 C CD  . PRO B 93  ? 0.4884 0.4005 0.3853 0.1454  0.1001  0.1047  102 PRO B CD  
1018 N N   . GLY B 94  ? 0.5486 0.4062 0.4190 0.1695  0.1083  0.1118  103 GLY B N   
1019 C CA  . GLY B 94  ? 0.5576 0.4039 0.4154 0.1833  0.1143  0.1213  103 GLY B CA  
1020 C C   . GLY B 94  ? 0.5725 0.4261 0.4134 0.2052  0.1131  0.1233  103 GLY B C   
1021 O O   . GLY B 94  ? 0.5864 0.4332 0.4156 0.2182  0.1193  0.1332  103 GLY B O   
1022 N N   . GLU B 95  ? 0.5663 0.4333 0.4052 0.2100  0.1052  0.1146  104 GLU B N   
1023 C CA  . GLU B 95  ? 0.5783 0.4533 0.4012 0.2312  0.1025  0.1152  104 GLU B CA  
1024 C C   . GLU B 95  ? 0.5902 0.4644 0.4069 0.2393  0.0894  0.0990  104 GLU B C   
1025 O O   . GLU B 95  ? 0.5542 0.4279 0.3811 0.2267  0.0825  0.0879  104 GLU B O   
1026 C CB  . GLU B 95  ? 0.6041 0.4973 0.4282 0.2330  0.1062  0.1231  104 GLU B CB  
1027 C CG  . GLU B 95  ? 0.6273 0.5247 0.4588 0.2256  0.1198  0.1407  104 GLU B CG  
1028 C CD  . GLU B 95  ? 0.6406 0.5593 0.4754 0.2266  0.1242  0.1489  104 GLU B CD  
1029 O OE1 . GLU B 95  ? 0.6146 0.5436 0.4461 0.2317  0.1159  0.1399  104 GLU B OE1 
1030 O OE2 . GLU B 95  ? 0.6453 0.5707 0.4854 0.2235  0.1360  0.1649  104 GLU B OE2 
1031 N N   . ARG B 96  ? 0.6033 0.4774 0.4036 0.2606  0.0857  0.0975  105 ARG B N   
1032 C CA  . ARG B 96  ? 0.6260 0.4996 0.4214 0.2688  0.0722  0.0817  105 ARG B CA  
1033 C C   . ARG B 96  ? 0.6039 0.4874 0.4050 0.2631  0.0637  0.0734  105 ARG B C   
1034 O O   . ARG B 96  ? 0.6066 0.4999 0.4066 0.2642  0.0672  0.0804  105 ARG B O   
1035 C CB  . ARG B 96  ? 0.6859 0.5599 0.4616 0.2946  0.0695  0.0825  105 ARG B CB  
1036 C CG  . ARG B 96  ? 0.7845 0.6545 0.5561 0.3032  0.0563  0.0665  105 ARG B CG  
1037 C CD  . ARG B 96  ? 0.8666 0.7301 0.6219 0.3241  0.0566  0.0679  105 ARG B CD  
1038 N NE  . ARG B 96  ? 0.9601 0.8277 0.6985 0.3429  0.0632  0.0800  105 ARG B NE  
1039 C CZ  . ARG B 96  ? 1.0147 0.8761 0.7431 0.3516  0.0744  0.0935  105 ARG B CZ  
1040 N NH1 . ARG B 96  ? 1.0060 0.8547 0.7392 0.3434  0.0794  0.0960  105 ARG B NH1 
1041 N NH2 . ARG B 96  ? 1.0327 0.9003 0.7458 0.3694  0.0806  0.1051  105 ARG B NH2 
1042 N N   . ALA B 97  ? 0.5818 0.4631 0.3884 0.2581  0.0522  0.0587  106 ALA B N   
1043 C CA  . ALA B 97  ? 0.5796 0.4676 0.3898 0.2541  0.0427  0.0505  106 ALA B CA  
1044 C C   . ALA B 97  ? 0.5889 0.4819 0.3829 0.2754  0.0381  0.0511  106 ALA B C   
1045 O O   . ALA B 97  ? 0.6107 0.5007 0.3917 0.2934  0.0363  0.0505  106 ALA B O   
1046 C CB  . ALA B 97  ? 0.5877 0.4720 0.4051 0.2480  0.0317  0.0361  106 ALA B CB  
1047 N N   . LYS B 98  ? 0.5711 0.4718 0.3644 0.2747  0.0369  0.0530  107 LYS B N   
1048 C CA  . LYS B 98  ? 0.6090 0.5156 0.3862 0.2952  0.0331  0.0542  107 LYS B CA  
1049 C C   . LYS B 98  ? 0.6066 0.5156 0.3851 0.2922  0.0229  0.0462  107 LYS B C   
1050 O O   . LYS B 98  ? 0.6057 0.5185 0.3955 0.2759  0.0259  0.0484  107 LYS B O   
1051 C CB  . LYS B 98  ? 0.6740 0.5904 0.4474 0.2994  0.0472  0.0706  107 LYS B CB  
1052 C CG  . LYS B 98  ? 0.7863 0.7122 0.5420 0.3223  0.0468  0.0753  107 LYS B CG  
1053 C CD  . LYS B 98  ? 0.8827 0.8211 0.6399 0.3214  0.0629  0.0934  107 LYS B CD  
1054 C CE  . LYS B 98  ? 0.9437 0.8872 0.7206 0.2970  0.0685  0.0971  107 LYS B CE  
1055 N NZ  . LYS B 98  ? 0.9782 0.9397 0.7556 0.2993  0.0768  0.1086  107 LYS B NZ  
1056 N N   . ASN B 99  ? 0.5854 0.4912 0.3521 0.3080  0.0101  0.0364  108 ASN B N   
1057 C CA  . ASN B 99  ? 0.6005 0.5055 0.3656 0.3081  -0.0010 0.0286  108 ASN B CA  
1058 C C   . ASN B 99  ? 0.6100 0.5252 0.3628 0.3218  0.0026  0.0363  108 ASN B C   
1059 O O   . ASN B 99  ? 0.6341 0.5541 0.3714 0.3428  0.0050  0.0407  108 ASN B O   
1060 C CB  . ASN B 99  ? 0.6325 0.5282 0.3913 0.3183  -0.0182 0.0137  108 ASN B CB  
1061 C CG  . ASN B 99  ? 0.6710 0.5590 0.4433 0.3048  -0.0242 0.0044  108 ASN B CG  
1062 O OD1 . ASN B 99  ? 0.7164 0.6040 0.4912 0.3053  -0.0195 0.0055  108 ASN B OD1 
1063 N ND2 . ASN B 99  ? 0.6251 0.5072 0.4060 0.2934  -0.0350 -0.0049 108 ASN B ND2 
1064 N N   . ILE B 100 ? 0.5962 0.5156 0.3544 0.3118  0.0025  0.0374  109 ILE B N   
1065 C CA  . ILE B 100 ? 0.6043 0.5352 0.3524 0.3237  0.0052  0.0437  109 ILE B CA  
1066 C C   . ILE B 100 ? 0.6038 0.5280 0.3472 0.3254  -0.0091 0.0330  109 ILE B C   
1067 O O   . ILE B 100 ? 0.5991 0.5186 0.3547 0.3069  -0.0118 0.0296  109 ILE B O   
1068 C CB  . ILE B 100 ? 0.6273 0.5724 0.3867 0.3107  0.0203  0.0572  109 ILE B CB  
1069 C CG1 . ILE B 100 ? 0.6624 0.6098 0.4295 0.3041  0.0339  0.0674  109 ILE B CG1 
1070 C CG2 . ILE B 100 ? 0.6440 0.6047 0.3926 0.3255  0.0236  0.0642  109 ILE B CG2 
1071 C CD1 . ILE B 100 ? 0.6914 0.6439 0.4435 0.3256  0.0396  0.0752  109 ILE B CD1 
1072 N N   . GLN B 101 ? 0.6151 0.5388 0.3399 0.3483  -0.0182 0.0284  110 GLN B N   
1073 C CA  . GLN B 101 ? 0.6303 0.5446 0.3484 0.3522  -0.0332 0.0178  110 GLN B CA  
1074 C C   . GLN B 101 ? 0.6552 0.5817 0.3683 0.3562  -0.0290 0.0243  110 GLN B C   
1075 O O   . GLN B 101 ? 0.6797 0.6231 0.3854 0.3690  -0.0188 0.0346  110 GLN B O   
1076 C CB  . GLN B 101 ? 0.6602 0.5656 0.3596 0.3766  -0.0474 0.0074  110 GLN B CB  
1077 C CG  . GLN B 101 ? 0.6804 0.5710 0.3730 0.3799  -0.0653 -0.0052 110 GLN B CG  
1078 C CD  . GLN B 101 ? 0.7342 0.6117 0.4151 0.3968  -0.0815 -0.0184 110 GLN B CD  
1079 O OE1 . GLN B 101 ? 0.7251 0.5998 0.4108 0.3959  -0.0823 -0.0217 110 GLN B OE1 
1080 N NE2 . GLN B 101 ? 0.7645 0.6338 0.4290 0.4136  -0.0956 -0.0269 110 GLN B NE2 
1081 N N   . THR B 102 ? 0.6225 0.5411 0.3393 0.3458  -0.0369 0.0187  111 THR B N   
1082 C CA  . THR B 102 ? 0.6237 0.5542 0.3369 0.3484  -0.0332 0.0242  111 THR B CA  
1083 C C   . THR B 102 ? 0.6308 0.5457 0.3393 0.3464  -0.0480 0.0142  111 THR B C   
1084 O O   . THR B 102 ? 0.6406 0.5372 0.3561 0.3341  -0.0572 0.0056  111 THR B O   
1085 C CB  . THR B 102 ? 0.6200 0.5658 0.3519 0.3281  -0.0170 0.0359  111 THR B CB  
1086 O OG1 . THR B 102 ? 0.6285 0.5923 0.3562 0.3350  -0.0113 0.0431  111 THR B OG1 
1087 C CG2 . THR B 102 ? 0.6145 0.5490 0.3634 0.3020  -0.0191 0.0317  111 THR B CG2 
1088 N N   . LEU B 103 ? 0.6245 0.5465 0.3218 0.3579  -0.0501 0.0155  112 LEU B N   
1089 C CA  . LEU B 103 ? 0.6264 0.5321 0.3191 0.3547  -0.0631 0.0073  112 LEU B CA  
1090 C C   . LEU B 103 ? 0.6296 0.5456 0.3366 0.3353  -0.0534 0.0145  112 LEU B C   
1091 O O   . LEU B 103 ? 0.6380 0.5761 0.3453 0.3396  -0.0429 0.0235  112 LEU B O   
1092 C CB  . LEU B 103 ? 0.6445 0.5490 0.3133 0.3815  -0.0738 0.0025  112 LEU B CB  
1093 C CG  . LEU B 103 ? 0.6850 0.5701 0.3492 0.3768  -0.0871 -0.0053 112 LEU B CG  
1094 C CD1 . LEU B 103 ? 0.6957 0.5518 0.3589 0.3728  -0.1034 -0.0175 112 LEU B CD1 
1095 C CD2 . LEU B 103 ? 0.7294 0.6198 0.3722 0.4009  -0.0930 -0.0066 112 LEU B CD2 
1096 N N   . PRO B 104 ? 0.6090 0.5106 0.3286 0.3134  -0.0569 0.0109  113 PRO B N   
1097 C CA  . PRO B 104 ? 0.5950 0.5071 0.3273 0.2962  -0.0479 0.0173  113 PRO B CA  
1098 C C   . PRO B 104 ? 0.6259 0.5434 0.3465 0.3067  -0.0515 0.0178  113 PRO B C   
1099 O O   . PRO B 104 ? 0.6548 0.5577 0.3582 0.3219  -0.0650 0.0104  113 PRO B O   
1100 C CB  . PRO B 104 ? 0.5962 0.4890 0.3396 0.2752  -0.0536 0.0119  113 PRO B CB  
1101 C CG  . PRO B 104 ? 0.5893 0.4683 0.3340 0.2762  -0.0599 0.0054  113 PRO B CG  
1102 C CD  . PRO B 104 ? 0.6024 0.4802 0.3259 0.3042  -0.0684 0.0015  113 PRO B CD  
1103 N N   . GLY B 105 ? 0.5889 0.5261 0.3195 0.2977  -0.0402 0.0257  114 GLY B N   
1104 C CA  . GLY B 105 ? 0.5847 0.5287 0.3091 0.3016  -0.0423 0.0265  114 GLY B CA  
1105 C C   . GLY B 105 ? 0.6039 0.5324 0.3364 0.2818  -0.0462 0.0233  114 GLY B C   
1106 O O   . GLY B 105 ? 0.6128 0.5221 0.3511 0.2696  -0.0507 0.0189  114 GLY B O   
1107 N N   . ILE B 106 ? 0.5954 0.5332 0.3280 0.2792  -0.0445 0.0257  115 ILE B N   
1108 C CA  . ILE B 106 ? 0.6104 0.5340 0.3472 0.2634  -0.0486 0.0232  115 ILE B CA  
1109 C C   . ILE B 106 ? 0.5883 0.5329 0.3371 0.2522  -0.0388 0.0289  115 ILE B C   
1110 O O   . ILE B 106 ? 0.6177 0.5831 0.3632 0.2626  -0.0352 0.0324  115 ILE B O   
1111 C CB  . ILE B 106 ? 0.6674 0.5688 0.3838 0.2760  -0.0639 0.0166  115 ILE B CB  
1112 C CG1 . ILE B 106 ? 0.7088 0.5846 0.4152 0.2839  -0.0762 0.0091  115 ILE B CG1 
1113 C CG2 . ILE B 106 ? 0.6890 0.5785 0.4062 0.2631  -0.0673 0.0160  115 ILE B CG2 
1114 C CD1 . ILE B 106 ? 0.7627 0.6185 0.4471 0.3009  -0.0914 0.0027  115 ILE B CD1 
1115 N N   . PHE B 107 ? 0.5588 0.4977 0.3205 0.2318  -0.0357 0.0291  116 PHE B N   
1116 C CA  . PHE B 107 ? 0.5560 0.5109 0.3270 0.2214  -0.0293 0.0324  116 PHE B CA  
1117 C C   . PHE B 107 ? 0.5876 0.5244 0.3458 0.2225  -0.0394 0.0286  116 PHE B C   
1118 O O   . PHE B 107 ? 0.6010 0.5146 0.3581 0.2136  -0.0450 0.0255  116 PHE B O   
1119 C CB  . PHE B 107 ? 0.5425 0.4992 0.3328 0.1994  -0.0213 0.0340  116 PHE B CB  
1120 C CG  . PHE B 107 ? 0.5344 0.5109 0.3404 0.1938  -0.0095 0.0391  116 PHE B CG  
1121 C CD1 . PHE B 107 ? 0.5339 0.5274 0.3381 0.2070  -0.0051 0.0434  116 PHE B CD1 
1122 C CD2 . PHE B 107 ? 0.5291 0.5068 0.3514 0.1756  -0.0028 0.0399  116 PHE B CD2 
1123 C CE1 . PHE B 107 ? 0.5192 0.5288 0.3381 0.2010  0.0060  0.0493  116 PHE B CE1 
1124 C CE2 . PHE B 107 ? 0.5216 0.5141 0.3578 0.1703  0.0073  0.0446  116 PHE B CE2 
1125 C CZ  . PHE B 107 ? 0.5158 0.5240 0.3508 0.1821  0.0119  0.0498  116 PHE B CZ  
1126 N N   . LYS B 108 ? 0.5904 0.5384 0.3401 0.2321  -0.0411 0.0293  117 LYS B N   
1127 C CA  . LYS B 108 ? 0.6130 0.5440 0.3496 0.2335  -0.0500 0.0266  117 LYS B CA  
1128 C C   . LYS B 108 ? 0.6126 0.5556 0.3605 0.2188  -0.0437 0.0289  117 LYS B C   
1129 O O   . LYS B 108 ? 0.6042 0.5744 0.3607 0.2193  -0.0365 0.0316  117 LYS B O   
1130 C CB  . LYS B 108 ? 0.6619 0.5979 0.3798 0.2561  -0.0567 0.0252  117 LYS B CB  
1131 C CG  . LYS B 108 ? 0.7725 0.6969 0.4765 0.2738  -0.0642 0.0219  117 LYS B CG  
1132 C CD  . LYS B 108 ? 0.8789 0.8181 0.5670 0.2982  -0.0676 0.0214  117 LYS B CD  
1133 C CE  . LYS B 108 ? 0.9955 0.9079 0.6602 0.3170  -0.0822 0.0149  117 LYS B CE  
1134 N NZ  . LYS B 108 ? 1.0502 0.9797 0.7003 0.3431  -0.0842 0.0143  117 LYS B NZ  
1135 N N   . THR B 109 ? 0.6141 0.5381 0.3626 0.2057  -0.0462 0.0279  118 THR B N   
1136 C CA  . THR B 109 ? 0.6202 0.5547 0.3778 0.1925  -0.0407 0.0296  118 THR B CA  
1137 C C   . THR B 109 ? 0.6607 0.5771 0.4028 0.1946  -0.0485 0.0288  118 THR B C   
1138 O O   . THR B 109 ? 0.6803 0.5712 0.4075 0.2017  -0.0578 0.0273  118 THR B O   
1139 C CB  . THR B 109 ? 0.6265 0.5599 0.4019 0.1729  -0.0335 0.0304  118 THR B CB  
1140 O OG1 . THR B 109 ? 0.6507 0.5580 0.4209 0.1655  -0.0388 0.0295  118 THR B OG1 
1141 C CG2 . THR B 109 ? 0.6061 0.5482 0.3939 0.1711  -0.0274 0.0311  118 THR B CG2 
1142 N N   . LYS B 110 ? 0.6694 0.5961 0.4155 0.1869  -0.0448 0.0299  119 LYS B N   
1143 C CA  . LYS B 110 ? 0.6996 0.6090 0.4303 0.1886  -0.0511 0.0303  119 LYS B CA  
1144 C C   . LYS B 110 ? 0.7403 0.6198 0.4683 0.1780  -0.0545 0.0315  119 LYS B C   
1145 O O   . LYS B 110 ? 0.7738 0.6314 0.4863 0.1812  -0.0616 0.0328  119 LYS B O   
1146 C CB  . LYS B 110 ? 0.6907 0.6195 0.4266 0.1831  -0.0462 0.0309  119 LYS B CB  
1147 C CG  . LYS B 110 ? 0.7235 0.6607 0.4784 0.1646  -0.0376 0.0314  119 LYS B CG  
1148 C CD  . LYS B 110 ? 0.7725 0.7277 0.5311 0.1606  -0.0343 0.0307  119 LYS B CD  
1149 C CE  . LYS B 110 ? 0.8062 0.7680 0.5812 0.1439  -0.0270 0.0303  119 LYS B CE  
1150 N NZ  . LYS B 110 ? 0.8385 0.7769 0.6088 0.1351  -0.0276 0.0326  119 LYS B NZ  
1151 N N   . ASP B 111 ? 0.7245 0.6033 0.4677 0.1657  -0.0496 0.0316  120 ASP B N   
1152 C CA  . ASP B 111 ? 0.7444 0.6001 0.4893 0.1543  -0.0517 0.0328  120 ASP B CA  
1153 C C   . ASP B 111 ? 0.7597 0.5985 0.5035 0.1580  -0.0579 0.0305  120 ASP B C   
1154 O O   . ASP B 111 ? 0.7840 0.6089 0.5346 0.1468  -0.0584 0.0311  120 ASP B O   
1155 C CB  . ASP B 111 ? 0.7557 0.6235 0.5188 0.1374  -0.0420 0.0340  120 ASP B CB  
1156 C CG  . ASP B 111 ? 0.8175 0.6974 0.5805 0.1328  -0.0375 0.0357  120 ASP B CG  
1157 O OD1 . ASP B 111 ? 0.8458 0.7129 0.5944 0.1363  -0.0421 0.0379  120 ASP B OD1 
1158 O OD2 . ASP B 111 ? 0.8219 0.7233 0.5985 0.1265  -0.0298 0.0345  120 ASP B OD2 
1159 N N   . GLY B 112 ? 0.7414 0.5826 0.4770 0.1737  -0.0625 0.0278  121 GLY B N   
1160 C CA  . GLY B 112 ? 0.7309 0.5566 0.4638 0.1795  -0.0695 0.0244  121 GLY B CA  
1161 C C   . GLY B 112 ? 0.7062 0.5513 0.4463 0.1868  -0.0648 0.0228  121 GLY B C   
1162 O O   . GLY B 112 ? 0.6862 0.5568 0.4365 0.1843  -0.0550 0.0249  121 GLY B O   
1163 N N   . ASP B 113 ? 0.6930 0.5255 0.4271 0.1963  -0.0721 0.0190  122 ASP B N   
1164 C CA  . ASP B 113 ? 0.6691 0.5165 0.4067 0.2058  -0.0688 0.0177  122 ASP B CA  
1165 C C   . ASP B 113 ? 0.6537 0.5006 0.4069 0.1940  -0.0644 0.0171  122 ASP B C   
1166 O O   . ASP B 113 ? 0.6667 0.4952 0.4236 0.1836  -0.0689 0.0155  122 ASP B O   
1167 C CB  . ASP B 113 ? 0.7174 0.5522 0.4364 0.2267  -0.0804 0.0132  122 ASP B CB  
1168 C CG  . ASP B 113 ? 0.8156 0.6539 0.5177 0.2422  -0.0847 0.0134  122 ASP B CG  
1169 O OD1 . ASP B 113 ? 0.8348 0.6861 0.5402 0.2363  -0.0787 0.0171  122 ASP B OD1 
1170 O OD2 . ASP B 113 ? 0.8938 0.7223 0.5790 0.2609  -0.0944 0.0093  122 ASP B OD2 
1171 N N   . ILE B 114 ? 0.6058 0.4739 0.3684 0.1956  -0.0553 0.0190  123 ILE B N   
1172 C CA  . ILE B 114 ? 0.6076 0.4784 0.3842 0.1868  -0.0499 0.0187  123 ILE B CA  
1173 C C   . ILE B 114 ? 0.5906 0.4701 0.3624 0.2028  -0.0494 0.0181  123 ILE B C   
1174 O O   . ILE B 114 ? 0.5850 0.4812 0.3518 0.2140  -0.0457 0.0211  123 ILE B O   
1175 C CB  . ILE B 114 ? 0.6156 0.5056 0.4093 0.1712  -0.0369 0.0232  123 ILE B CB  
1176 C CG1 . ILE B 114 ? 0.6532 0.5429 0.4478 0.1607  -0.0358 0.0248  123 ILE B CG1 
1177 C CG2 . ILE B 114 ? 0.6502 0.5388 0.4576 0.1601  -0.0323 0.0224  123 ILE B CG2 
1178 C CD1 . ILE B 114 ? 0.6740 0.5837 0.4844 0.1476  -0.0242 0.0278  123 ILE B CD1 
1179 N N   . GLY B 115 ? 0.5704 0.4416 0.3449 0.2040  -0.0520 0.0149  124 GLY B N   
1180 C CA  . GLY B 115 ? 0.5612 0.4424 0.3313 0.2191  -0.0499 0.0153  124 GLY B CA  
1181 C C   . GLY B 115 ? 0.5460 0.4511 0.3288 0.2135  -0.0352 0.0224  124 GLY B C   
1182 O O   . GLY B 115 ? 0.5227 0.4329 0.3196 0.1963  -0.0279 0.0248  124 GLY B O   
1183 N N   . ALA B 116 ? 0.5376 0.4574 0.3156 0.2279  -0.0306 0.0259  125 ALA B N   
1184 C CA  . ALA B 116 ? 0.5293 0.4711 0.3197 0.2227  -0.0166 0.0337  125 ALA B CA  
1185 C C   . ALA B 116 ? 0.5426 0.4914 0.3281 0.2373  -0.0131 0.0365  125 ALA B C   
1186 O O   . ALA B 116 ? 0.5885 0.5346 0.3580 0.2565  -0.0201 0.0341  125 ALA B O   
1187 C CB  . ALA B 116 ? 0.5498 0.5107 0.3415 0.2235  -0.0116 0.0386  125 ALA B CB  
1188 N N   . VAL B 117 ? 0.5291 0.4867 0.3265 0.2299  -0.0026 0.0419  126 VAL B N   
1189 C CA  . VAL B 117 ? 0.5559 0.5189 0.3483 0.2433  0.0017  0.0457  126 VAL B CA  
1190 C C   . VAL B 117 ? 0.5540 0.5414 0.3542 0.2437  0.0156  0.0571  126 VAL B C   
1191 O O   . VAL B 117 ? 0.5273 0.5226 0.3438 0.2267  0.0242  0.0616  126 VAL B O   
1192 C CB  . VAL B 117 ? 0.6122 0.5605 0.4103 0.2357  0.0005  0.0417  126 VAL B CB  
1193 C CG1 . VAL B 117 ? 0.6491 0.6055 0.4500 0.2402  0.0104  0.0485  126 VAL B CG1 
1194 C CG2 . VAL B 117 ? 0.6210 0.5496 0.4076 0.2444  -0.0140 0.0314  126 VAL B CG2 
1195 N N   . ALA B 118 ? 0.5451 0.5456 0.3332 0.2640  0.0173  0.0618  127 ALA B N   
1196 C CA  . ALA B 118 ? 0.5594 0.5853 0.3551 0.2651  0.0305  0.0736  127 ALA B CA  
1197 C C   . ALA B 118 ? 0.5749 0.6035 0.3725 0.2688  0.0397  0.0811  127 ALA B C   
1198 O O   . ALA B 118 ? 0.5837 0.6210 0.3688 0.2885  0.0420  0.0859  127 ALA B O   
1199 C CB  . ALA B 118 ? 0.5769 0.6195 0.3596 0.2844  0.0286  0.0758  127 ALA B CB  
1200 N N   . LEU B 119 ? 0.5554 0.5745 0.3668 0.2511  0.0442  0.0816  128 LEU B N   
1201 C CA  . LEU B 119 ? 0.5466 0.5645 0.3601 0.2526  0.0526  0.0884  128 LEU B CA  
1202 C C   . LEU B 119 ? 0.5703 0.5946 0.4046 0.2316  0.0636  0.0957  128 LEU B C   
1203 O O   . LEU B 119 ? 0.5580 0.5762 0.4037 0.2140  0.0609  0.0901  128 LEU B O   
1204 C CB  . LEU B 119 ? 0.5589 0.5541 0.3652 0.2553  0.0443  0.0792  128 LEU B CB  
1205 C CG  . LEU B 119 ? 0.5895 0.5758 0.3759 0.2758  0.0316  0.0705  128 LEU B CG  
1206 C CD1 . LEU B 119 ? 0.6117 0.5769 0.3958 0.2741  0.0222  0.0602  128 LEU B CD1 
1207 C CD2 . LEU B 119 ? 0.5837 0.5821 0.3556 0.2990  0.0359  0.0777  128 LEU B CD2 
1208 N N   . ASP B 120 ? 0.5839 0.6197 0.4230 0.2334  0.0757  0.1081  129 ASP B N   
1209 C CA  . ASP B 120 ? 0.5977 0.6396 0.4568 0.2143  0.0861  0.1161  129 ASP B CA  
1210 C C   . ASP B 120 ? 0.5831 0.6095 0.4458 0.2083  0.0911  0.1189  129 ASP B C   
1211 O O   . ASP B 120 ? 0.5800 0.6051 0.4330 0.2215  0.0959  0.1256  129 ASP B O   
1212 C CB  . ASP B 120 ? 0.6714 0.7399 0.5368 0.2179  0.0970  0.1298  129 ASP B CB  
1213 C CG  . ASP B 120 ? 0.7985 0.8843 0.6640 0.2207  0.0926  0.1268  129 ASP B CG  
1214 O OD1 . ASP B 120 ? 0.8025 0.9048 0.6851 0.2074  0.0981  0.1316  129 ASP B OD1 
1215 O OD2 . ASP B 120 ? 0.8769 0.9588 0.7253 0.2362  0.0829  0.1190  129 ASP B OD2 
1216 N N   . TYR B 121 ? 0.5510 0.5658 0.4266 0.1892  0.0901  0.1138  130 TYR B N   
1217 C CA  . TYR B 121 ? 0.5416 0.5407 0.4213 0.1823  0.0940  0.1153  130 TYR B CA  
1218 C C   . TYR B 121 ? 0.5308 0.5292 0.4305 0.1598  0.0989  0.1170  130 TYR B C   
1219 O O   . TYR B 121 ? 0.5334 0.5406 0.4424 0.1495  0.0960  0.1131  130 TYR B O   
1220 C CB  . TYR B 121 ? 0.5537 0.5331 0.4241 0.1855  0.0836  0.1022  130 TYR B CB  
1221 C CG  . TYR B 121 ? 0.5722 0.5475 0.4238 0.2071  0.0796  0.1010  130 TYR B CG  
1222 C CD1 . TYR B 121 ? 0.5953 0.5638 0.4404 0.2161  0.0849  0.1069  130 TYR B CD1 
1223 C CD2 . TYR B 121 ? 0.5929 0.5698 0.4325 0.2194  0.0697  0.0935  130 TYR B CD2 
1224 C CE1 . TYR B 121 ? 0.6152 0.5803 0.4425 0.2371  0.0803  0.1047  130 TYR B CE1 
1225 C CE2 . TYR B 121 ? 0.6188 0.5923 0.4410 0.2403  0.0649  0.0915  130 TYR B CE2 
1226 C CZ  . TYR B 121 ? 0.6436 0.6120 0.4595 0.2494  0.0703  0.0970  130 TYR B CZ  
1227 O OH  . TYR B 121 ? 0.7017 0.6670 0.4996 0.2712  0.0649  0.0942  130 TYR B OH  
1228 N N   . PRO B 122 ? 0.5274 0.5135 0.4326 0.1529  0.1047  0.1214  131 PRO B N   
1229 C CA  . PRO B 122 ? 0.5176 0.4996 0.4408 0.1322  0.1073  0.1210  131 PRO B CA  
1230 C C   . PRO B 122 ? 0.5031 0.4774 0.4289 0.1225  0.0975  0.1064  131 PRO B C   
1231 O O   . PRO B 122 ? 0.4918 0.4583 0.4061 0.1304  0.0897  0.0974  131 PRO B O   
1232 C CB  . PRO B 122 ? 0.5400 0.5043 0.4621 0.1314  0.1124  0.1255  131 PRO B CB  
1233 C CG  . PRO B 122 ? 0.5391 0.5061 0.4461 0.1512  0.1172  0.1348  131 PRO B CG  
1234 C CD  . PRO B 122 ? 0.5199 0.4945 0.4140 0.1650  0.1086  0.1267  131 PRO B CD  
1235 N N   . ALA B 123 ? 0.4925 0.4707 0.4338 0.1057  0.0979  0.1045  132 ALA B N   
1236 C CA  . ALA B 123 ? 0.4783 0.4516 0.4227 0.0961  0.0898  0.0921  132 ALA B CA  
1237 C C   . ALA B 123 ? 0.4660 0.4196 0.4039 0.0964  0.0851  0.0832  132 ALA B C   
1238 O O   . ALA B 123 ? 0.4488 0.3994 0.3826 0.0957  0.0776  0.0734  132 ALA B O   
1239 C CB  . ALA B 123 ? 0.4831 0.4624 0.4451 0.0791  0.0918  0.0923  132 ALA B CB  
1240 N N   . GLY B 124 ? 0.4647 0.4056 0.4012 0.0982  0.0897  0.0874  133 GLY B N   
1241 C CA  . GLY B 124 ? 0.4588 0.3831 0.3893 0.1001  0.0857  0.0795  133 GLY B CA  
1242 C C   . GLY B 124 ? 0.4298 0.3518 0.3459 0.1148  0.0801  0.0749  133 GLY B C   
1243 O O   . GLY B 124 ? 0.4457 0.3568 0.3575 0.1170  0.0762  0.0678  133 GLY B O   
1244 N N   . THR B 125 ? 0.4231 0.3562 0.3322 0.1250  0.0787  0.0778  134 THR B N   
1245 C CA  . THR B 125 ? 0.4227 0.3538 0.3187 0.1387  0.0715  0.0723  134 THR B CA  
1246 C C   . THR B 125 ? 0.4375 0.3696 0.3345 0.1329  0.0625  0.0620  134 THR B C   
1247 O O   . THR B 125 ? 0.4365 0.3648 0.3251 0.1411  0.0550  0.0559  134 THR B O   
1248 C CB  . THR B 125 ? 0.4731 0.4143 0.3593 0.1543  0.0740  0.0803  134 THR B CB  
1249 O OG1 . THR B 125 ? 0.4728 0.4145 0.3605 0.1566  0.0840  0.0918  134 THR B OG1 
1250 C CG2 . THR B 125 ? 0.4982 0.4348 0.3692 0.1713  0.0664  0.0750  134 THR B CG2 
1251 N N   . SER B 126 ? 0.4118 0.3494 0.3190 0.1194  0.0632  0.0608  135 SER B N   
1252 C CA  . SER B 126 ? 0.4080 0.3467 0.3155 0.1138  0.0560  0.0529  135 SER B CA  
1253 C C   . SER B 126 ? 0.3984 0.3262 0.3039 0.1126  0.0503  0.0443  135 SER B C   
1254 O O   . SER B 126 ? 0.4026 0.3238 0.3124 0.1082  0.0532  0.0430  135 SER B O   
1255 C CB  . SER B 126 ? 0.4355 0.3793 0.3546 0.0989  0.0582  0.0520  135 SER B CB  
1256 O OG  . SER B 126 ? 0.4792 0.4366 0.4019 0.0982  0.0611  0.0576  135 SER B OG  
1257 N N   . GLY B 127 ? 0.3778 0.3042 0.2777 0.1156  0.0425  0.0389  136 GLY B N   
1258 C CA  . GLY B 127 ? 0.3946 0.3130 0.2942 0.1145  0.0370  0.0315  136 GLY B CA  
1259 C C   . GLY B 127 ? 0.4090 0.3221 0.2998 0.1282  0.0323  0.0299  136 GLY B C   
1260 O O   . GLY B 127 ? 0.4161 0.3241 0.3071 0.1284  0.0264  0.0234  136 GLY B O   
1261 N N   . SER B 128 ? 0.4108 0.3264 0.2941 0.1405  0.0351  0.0359  137 SER B N   
1262 C CA  . SER B 128 ? 0.4181 0.3288 0.2914 0.1556  0.0299  0.0335  137 SER B CA  
1263 C C   . SER B 128 ? 0.4214 0.3293 0.2896 0.1588  0.0189  0.0271  137 SER B C   
1264 O O   . SER B 128 ? 0.4324 0.3439 0.2988 0.1568  0.0173  0.0284  137 SER B O   
1265 C CB  . SER B 128 ? 0.4244 0.3402 0.2891 0.1692  0.0351  0.0419  137 SER B CB  
1266 O OG  . SER B 128 ? 0.4225 0.3373 0.2908 0.1676  0.0442  0.0479  137 SER B OG  
1267 N N   . PRO B 129 ? 0.4200 0.3210 0.2853 0.1646  0.0109  0.0200  138 PRO B N   
1268 C CA  . PRO B 129 ? 0.4208 0.3167 0.2830 0.1656  -0.0002 0.0138  138 PRO B CA  
1269 C C   . PRO B 129 ? 0.4481 0.3425 0.2964 0.1822  -0.0063 0.0138  138 PRO B C   
1270 O O   . PRO B 129 ? 0.4549 0.3507 0.2948 0.1967  -0.0048 0.0158  138 PRO B O   
1271 C CB  . PRO B 129 ? 0.4483 0.3387 0.3149 0.1650  -0.0069 0.0060  138 PRO B CB  
1272 C CG  . PRO B 129 ? 0.4564 0.3484 0.3213 0.1731  -0.0011 0.0079  138 PRO B CG  
1273 C CD  . PRO B 129 ? 0.4371 0.3346 0.3041 0.1681  0.0111  0.0168  138 PRO B CD  
1274 N N   . ILE B 130 ? 0.4534 0.3434 0.2982 0.1810  -0.0141 0.0109  139 ILE B N   
1275 C CA  . ILE B 130 ? 0.4702 0.3562 0.3005 0.1974  -0.0226 0.0088  139 ILE B CA  
1276 C C   . ILE B 130 ? 0.4948 0.3681 0.3253 0.1978  -0.0362 -0.0011 139 ILE B C   
1277 O O   . ILE B 130 ? 0.4848 0.3533 0.3255 0.1828  -0.0392 -0.0041 139 ILE B O   
1278 C CB  . ILE B 130 ? 0.4807 0.3699 0.3072 0.1953  -0.0221 0.0124  139 ILE B CB  
1279 C CG1 . ILE B 130 ? 0.5132 0.4172 0.3430 0.1931  -0.0089 0.0219  139 ILE B CG1 
1280 C CG2 . ILE B 130 ? 0.5080 0.3914 0.3178 0.2137  -0.0324 0.0090  139 ILE B CG2 
1281 C CD1 . ILE B 130 ? 0.5480 0.4579 0.3807 0.1841  -0.0062 0.0252  139 ILE B CD1 
1282 N N   . LEU B 131 ? 0.5182 0.3867 0.3381 0.2146  -0.0445 -0.0061 140 LEU B N   
1283 C CA  . LEU B 131 ? 0.5511 0.4082 0.3726 0.2159  -0.0582 -0.0163 140 LEU B CA  
1284 C C   . LEU B 131 ? 0.5634 0.4096 0.3708 0.2301  -0.0719 -0.0222 140 LEU B C   
1285 O O   . LEU B 131 ? 0.5870 0.4365 0.3794 0.2467  -0.0711 -0.0195 140 LEU B O   
1286 C CB  . LEU B 131 ? 0.5888 0.4485 0.4103 0.2257  -0.0587 -0.0200 140 LEU B CB  
1287 C CG  . LEU B 131 ? 0.6332 0.5032 0.4603 0.2221  -0.0447 -0.0133 140 LEU B CG  
1288 C CD1 . LEU B 131 ? 0.6572 0.5276 0.4799 0.2358  -0.0472 -0.0174 140 LEU B CD1 
1289 C CD2 . LEU B 131 ? 0.6491 0.5215 0.4932 0.2004  -0.0390 -0.0120 140 LEU B CD2 
1290 N N   . ASP B 132 ? 0.5562 0.3897 0.3686 0.2240  -0.0847 -0.0304 141 ASP B N   
1291 C CA  . ASP B 132 ? 0.5855 0.4052 0.3846 0.2385  -0.1007 -0.0384 141 ASP B CA  
1292 C C   . ASP B 132 ? 0.6214 0.4392 0.4168 0.2529  -0.1097 -0.0472 141 ASP B C   
1293 O O   . ASP B 132 ? 0.6263 0.4538 0.4293 0.2516  -0.1028 -0.0463 141 ASP B O   
1294 C CB  . ASP B 132 ? 0.6059 0.4098 0.4104 0.2258  -0.1116 -0.0425 141 ASP B CB  
1295 C CG  . ASP B 132 ? 0.6059 0.4060 0.4299 0.2077  -0.1159 -0.0469 141 ASP B CG  
1296 O OD1 . ASP B 132 ? 0.6210 0.4279 0.4526 0.2092  -0.1159 -0.0509 141 ASP B OD1 
1297 O OD2 . ASP B 132 ? 0.6235 0.4146 0.4547 0.1930  -0.1192 -0.0460 141 ASP B OD2 
1298 N N   . LYS B 133 ? 0.6600 0.4641 0.4436 0.2671  -0.1262 -0.0566 142 LYS B N   
1299 C CA  . LYS B 133 ? 0.6891 0.4910 0.4670 0.2835  -0.1368 -0.0663 142 LYS B CA  
1300 C C   . LYS B 133 ? 0.7160 0.5164 0.5125 0.2709  -0.1433 -0.0738 142 LYS B C   
1301 O O   . LYS B 133 ? 0.7360 0.5384 0.5298 0.2839  -0.1500 -0.0815 142 LYS B O   
1302 C CB  . LYS B 133 ? 0.7321 0.5189 0.4912 0.3030  -0.1539 -0.0753 142 LYS B CB  
1303 C CG  . LYS B 133 ? 0.8355 0.6290 0.5749 0.3198  -0.1464 -0.0678 142 LYS B CG  
1304 C CD  . LYS B 133 ? 0.9470 0.7261 0.6653 0.3409  -0.1628 -0.0764 142 LYS B CD  
1305 C CE  . LYS B 133 ? 1.0198 0.8049 0.7243 0.3489  -0.1549 -0.0677 142 LYS B CE  
1306 N NZ  . LYS B 133 ? 1.0846 0.8518 0.7712 0.3638  -0.1717 -0.0760 142 LYS B NZ  
1307 N N   . CYS B 134 ? 0.7113 0.5097 0.5266 0.2468  -0.1413 -0.0717 143 CYS B N   
1308 C CA  . CYS B 134 ? 0.7128 0.5145 0.5486 0.2327  -0.1446 -0.0769 143 CYS B CA  
1309 C C   . CYS B 134 ? 0.6879 0.5075 0.5344 0.2241  -0.1276 -0.0695 143 CYS B C   
1310 O O   . CYS B 134 ? 0.6943 0.5201 0.5584 0.2120  -0.1280 -0.0726 143 CYS B O   
1311 C CB  . CYS B 134 ? 0.7505 0.5414 0.6011 0.2119  -0.1516 -0.0780 143 CYS B CB  
1312 S SG  . CYS B 134 ? 0.8672 0.6330 0.7083 0.2201  -0.1748 -0.0888 143 CYS B SG  
1313 N N   . GLY B 135 ? 0.6566 0.4844 0.4935 0.2294  -0.1132 -0.0599 144 GLY B N   
1314 C CA  . GLY B 135 ? 0.6225 0.4642 0.4680 0.2215  -0.0976 -0.0527 144 GLY B CA  
1315 C C   . GLY B 135 ? 0.5946 0.4394 0.4546 0.1986  -0.0890 -0.0464 144 GLY B C   
1316 O O   . GLY B 135 ? 0.5856 0.4408 0.4548 0.1900  -0.0778 -0.0421 144 GLY B O   
1317 N N   . ARG B 136 ? 0.5573 0.3927 0.4181 0.1895  -0.0942 -0.0458 145 ARG B N   
1318 C CA  . ARG B 136 ? 0.5489 0.3873 0.4217 0.1689  -0.0861 -0.0394 145 ARG B CA  
1319 C C   . ARG B 136 ? 0.5165 0.3605 0.3818 0.1686  -0.0732 -0.0299 145 ARG B C   
1320 O O   . ARG B 136 ? 0.5248 0.3655 0.3755 0.1810  -0.0742 -0.0279 145 ARG B O   
1321 C CB  . ARG B 136 ? 0.5996 0.4246 0.4764 0.1588  -0.0969 -0.0419 145 ARG B CB  
1322 C CG  . ARG B 136 ? 0.6800 0.5022 0.5716 0.1519  -0.1080 -0.0501 145 ARG B CG  
1323 C CD  . ARG B 136 ? 0.7541 0.5601 0.6487 0.1428  -0.1196 -0.0520 145 ARG B CD  
1324 N NE  . ARG B 136 ? 0.8730 0.6631 0.7493 0.1592  -0.1314 -0.0566 145 ARG B NE  
1325 C CZ  . ARG B 136 ? 0.9309 0.7032 0.8009 0.1568  -0.1402 -0.0566 145 ARG B CZ  
1326 N NH1 . ARG B 136 ? 0.9307 0.6988 0.8112 0.1378  -0.1377 -0.0509 145 ARG B NH1 
1327 N NH2 . ARG B 136 ? 0.9478 0.7063 0.7997 0.1744  -0.1514 -0.0620 145 ARG B NH2 
1328 N N   . VAL B 137 ? 0.4683 0.3219 0.3446 0.1540  -0.0614 -0.0242 146 VAL B N   
1329 C CA  . VAL B 137 ? 0.4504 0.3103 0.3216 0.1528  -0.0498 -0.0160 146 VAL B CA  
1330 C C   . VAL B 137 ? 0.4663 0.3200 0.3339 0.1463  -0.0519 -0.0130 146 VAL B C   
1331 O O   . VAL B 137 ? 0.4707 0.3219 0.3476 0.1322  -0.0531 -0.0129 146 VAL B O   
1332 C CB  . VAL B 137 ? 0.4461 0.3172 0.3288 0.1413  -0.0375 -0.0122 146 VAL B CB  
1333 C CG1 . VAL B 137 ? 0.4634 0.3402 0.3429 0.1378  -0.0271 -0.0045 146 VAL B CG1 
1334 C CG2 . VAL B 137 ? 0.4631 0.3392 0.3461 0.1505  -0.0347 -0.0143 146 VAL B CG2 
1335 N N   . ILE B 138 ? 0.4869 0.3383 0.3405 0.1578  -0.0528 -0.0105 147 ILE B N   
1336 C CA  . ILE B 138 ? 0.4797 0.3248 0.3276 0.1541  -0.0555 -0.0079 147 ILE B CA  
1337 C C   . ILE B 138 ? 0.4639 0.3201 0.3136 0.1470  -0.0437 -0.0005 147 ILE B C   
1338 O O   . ILE B 138 ? 0.4792 0.3318 0.3241 0.1440  -0.0451 0.0019  147 ILE B O   
1339 C CB  . ILE B 138 ? 0.5092 0.3449 0.3399 0.1721  -0.0657 -0.0109 147 ILE B CB  
1340 C CG1 . ILE B 138 ? 0.5124 0.3590 0.3336 0.1885  -0.0597 -0.0081 147 ILE B CG1 
1341 C CG2 . ILE B 138 ? 0.5266 0.3482 0.3573 0.1758  -0.0799 -0.0196 147 ILE B CG2 
1342 C CD1 . ILE B 138 ? 0.5354 0.3752 0.3372 0.2093  -0.0693 -0.0109 147 ILE B CD1 
1343 N N   . GLY B 139 ? 0.4530 0.3216 0.3092 0.1446  -0.0328 0.0028  148 GLY B N   
1344 C CA  . GLY B 139 ? 0.4377 0.3172 0.2981 0.1365  -0.0219 0.0089  148 GLY B CA  
1345 C C   . GLY B 139 ? 0.4149 0.3047 0.2786 0.1396  -0.0122 0.0123  148 GLY B C   
1346 O O   . GLY B 139 ? 0.4283 0.3171 0.2896 0.1491  -0.0133 0.0105  148 GLY B O   
1347 N N   . LEU B 140 ? 0.4128 0.3120 0.2820 0.1315  -0.0031 0.0171  149 LEU B N   
1348 C CA  . LEU B 140 ? 0.4001 0.3078 0.2739 0.1319  0.0066  0.0212  149 LEU B CA  
1349 C C   . LEU B 140 ? 0.4027 0.3204 0.2724 0.1373  0.0118  0.0277  149 LEU B C   
1350 O O   . LEU B 140 ? 0.4085 0.3297 0.2761 0.1352  0.0105  0.0288  149 LEU B O   
1351 C CB  . LEU B 140 ? 0.3870 0.2977 0.2726 0.1174  0.0128  0.0210  149 LEU B CB  
1352 C CG  . LEU B 140 ? 0.3900 0.2952 0.2815 0.1108  0.0092  0.0154  149 LEU B CG  
1353 C CD1 . LEU B 140 ? 0.3965 0.3067 0.2980 0.0989  0.0166  0.0156  149 LEU B CD1 
1354 C CD2 . LEU B 140 ? 0.3968 0.2973 0.2860 0.1208  0.0056  0.0122  149 LEU B CD2 
1355 N N   . TYR B 141 ? 0.4206 0.3438 0.2896 0.1445  0.0182  0.0325  150 TYR B N   
1356 C CA  . TYR B 141 ? 0.4297 0.3648 0.2968 0.1499  0.0242  0.0398  150 TYR B CA  
1357 C C   . TYR B 141 ? 0.4143 0.3576 0.2942 0.1368  0.0334  0.0441  150 TYR B C   
1358 O O   . TYR B 141 ? 0.4334 0.3721 0.3203 0.1299  0.0371  0.0434  150 TYR B O   
1359 C CB  . TYR B 141 ? 0.4488 0.3841 0.3086 0.1649  0.0265  0.0433  150 TYR B CB  
1360 C CG  . TYR B 141 ? 0.4599 0.4089 0.3196 0.1708  0.0357  0.0532  150 TYR B CG  
1361 C CD1 . TYR B 141 ? 0.4760 0.4285 0.3452 0.1639  0.0457  0.0596  150 TYR B CD1 
1362 C CD2 . TYR B 141 ? 0.4777 0.4362 0.3282 0.1832  0.0344  0.0564  150 TYR B CD2 
1363 C CE1 . TYR B 141 ? 0.4964 0.4622 0.3678 0.1673  0.0547  0.0699  150 TYR B CE1 
1364 C CE2 . TYR B 141 ? 0.4944 0.4684 0.3464 0.1884  0.0437  0.0665  150 TYR B CE2 
1365 C CZ  . TYR B 141 ? 0.5032 0.4813 0.3669 0.1791  0.0541  0.0736  150 TYR B CZ  
1366 O OH  . TYR B 141 ? 0.5360 0.5298 0.4029 0.1830  0.0639  0.0849  150 TYR B OH  
1367 N N   . GLY B 142 ? 0.4082 0.3637 0.2912 0.1341  0.0367  0.0483  151 GLY B N   
1368 C CA  . GLY B 142 ? 0.4188 0.3826 0.3150 0.1224  0.0450  0.0526  151 GLY B CA  
1369 C C   . GLY B 142 ? 0.4319 0.4045 0.3344 0.1126  0.0444  0.0513  151 GLY B C   
1370 O O   . GLY B 142 ? 0.4431 0.4227 0.3575 0.1023  0.0500  0.0536  151 GLY B O   
1371 N N   . ASN B 143 ? 0.4118 0.3834 0.3063 0.1160  0.0372  0.0474  152 ASN B N   
1372 C CA  . ASN B 143 ? 0.4069 0.3885 0.3054 0.1093  0.0366  0.0467  152 ASN B CA  
1373 C C   . ASN B 143 ? 0.4379 0.4279 0.3264 0.1220  0.0332  0.0489  152 ASN B C   
1374 O O   . ASN B 143 ? 0.4327 0.4126 0.3084 0.1314  0.0259  0.0459  152 ASN B O   
1375 C CB  . ASN B 143 ? 0.4107 0.3834 0.3084 0.1007  0.0314  0.0402  152 ASN B CB  
1376 C CG  . ASN B 143 ? 0.4163 0.4000 0.3197 0.0928  0.0321  0.0393  152 ASN B CG  
1377 O OD1 . ASN B 143 ? 0.4345 0.4322 0.3475 0.0894  0.0372  0.0427  152 ASN B OD1 
1378 N ND2 . ASN B 143 ? 0.4316 0.4102 0.3288 0.0907  0.0266  0.0354  152 ASN B ND2 
1379 N N   . GLY B 144 ? 0.4434 0.4516 0.3381 0.1227  0.0381  0.0540  153 GLY B N   
1380 C CA  . GLY B 144 ? 0.4711 0.4906 0.3565 0.1369  0.0361  0.0569  153 GLY B CA  
1381 C C   . GLY B 144 ? 0.4792 0.5224 0.3745 0.1348  0.0412  0.0618  153 GLY B C   
1382 O O   . GLY B 144 ? 0.4686 0.5181 0.3759 0.1217  0.0429  0.0602  153 GLY B O   
1383 N N   . VAL B 145 ? 0.4823 0.5402 0.3723 0.1488  0.0434  0.0675  154 VAL B N   
1384 C CA  . VAL B 145 ? 0.5039 0.5877 0.4035 0.1482  0.0478  0.0723  154 VAL B CA  
1385 C C   . VAL B 145 ? 0.5285 0.6298 0.4317 0.1569  0.0563  0.0823  154 VAL B C   
1386 O O   . VAL B 145 ? 0.5297 0.6220 0.4227 0.1676  0.0571  0.0847  154 VAL B O   
1387 C CB  . VAL B 145 ? 0.5379 0.6252 0.4242 0.1588  0.0395  0.0676  154 VAL B CB  
1388 C CG1 . VAL B 145 ? 0.5362 0.6228 0.4041 0.1802  0.0359  0.0691  154 VAL B CG1 
1389 C CG2 . VAL B 145 ? 0.5648 0.6761 0.4627 0.1535  0.0413  0.0686  154 VAL B CG2 
1390 N N   . VAL B 146 ? 0.5538 0.6807 0.4724 0.1516  0.0627  0.0883  155 VAL B N   
1391 C CA  . VAL B 146 ? 0.5837 0.7326 0.5081 0.1590  0.0721  0.0997  155 VAL B CA  
1392 C C   . VAL B 146 ? 0.6158 0.7863 0.5319 0.1744  0.0694  0.1004  155 VAL B C   
1393 O O   . VAL B 146 ? 0.6002 0.7818 0.5214 0.1700  0.0655  0.0961  155 VAL B O   
1394 C CB  . VAL B 146 ? 0.5937 0.7571 0.5435 0.1414  0.0817  0.1070  155 VAL B CB  
1395 C CG1 . VAL B 146 ? 0.6013 0.7890 0.5574 0.1490  0.0922  0.1206  155 VAL B CG1 
1396 C CG2 . VAL B 146 ? 0.6087 0.7479 0.5641 0.1278  0.0833  0.1053  155 VAL B CG2 
1397 N N   . ILE B 147 ? 0.6543 0.8304 0.5559 0.1943  0.0707  0.1052  156 ILE B N   
1398 C CA  . ILE B 147 ? 0.6933 0.8886 0.5837 0.2122  0.0672  0.1050  156 ILE B CA  
1399 C C   . ILE B 147 ? 0.7058 0.9391 0.6101 0.2158  0.0783  0.1172  156 ILE B C   
1400 O O   . ILE B 147 ? 0.6995 0.9414 0.6218 0.2038  0.0887  0.1263  156 ILE B O   
1401 C CB  . ILE B 147 ? 0.7255 0.9021 0.5884 0.2339  0.0589  0.1002  156 ILE B CB  
1402 C CG1 . ILE B 147 ? 0.7324 0.9091 0.5902 0.2444  0.0659  0.1082  156 ILE B CG1 
1403 C CG2 . ILE B 147 ? 0.7519 0.8939 0.6048 0.2279  0.0479  0.0887  156 ILE B CG2 
1404 C CD1 . ILE B 147 ? 0.7563 0.9232 0.5878 0.2691  0.0580  0.1040  156 ILE B CD1 
1405 N N   . LYS B 148 ? 0.7185 0.9746 0.6152 0.2316  0.0760  0.1174  157 LYS B N   
1406 C CA  . LYS B 148 ? 0.7315 1.0282 0.6412 0.2367  0.0857  0.1284  157 LYS B CA  
1407 C C   . LYS B 148 ? 0.7447 1.0545 0.6669 0.2339  0.0998  0.1430  157 LYS B C   
1408 O O   . LYS B 148 ? 0.7441 1.0791 0.6913 0.2201  0.1093  0.1519  157 LYS B O   
1409 C CB  . LYS B 148 ? 0.7614 1.0736 0.6505 0.2635  0.0806  0.1266  157 LYS B CB  
1410 C CG  . LYS B 148 ? 0.8300 1.1401 0.7126 0.2649  0.0692  0.1154  157 LYS B CG  
1411 C CD  . LYS B 148 ? 0.9075 1.2266 0.7659 0.2929  0.0620  0.1119  157 LYS B CD  
1412 C CE  . LYS B 148 ? 0.9485 1.3115 0.8139 0.3061  0.0717  0.1228  157 LYS B CE  
1413 N NZ  . LYS B 148 ? 0.9887 1.3609 0.8297 0.3345  0.0638  0.1182  157 LYS B NZ  
1414 N N   . ASN B 149 ? 0.7547 1.0469 0.6600 0.2463  0.1009  0.1454  158 ASN B N   
1415 C CA  . ASN B 149 ? 0.7540 1.0566 0.6663 0.2473  0.1142  0.1599  158 ASN B CA  
1416 C C   . ASN B 149 ? 0.7397 1.0232 0.6685 0.2246  0.1200  0.1635  158 ASN B C   
1417 O O   . ASN B 149 ? 0.7454 1.0312 0.6771 0.2258  0.1304  0.1753  158 ASN B O   
1418 C CB  . ASN B 149 ? 0.8041 1.0985 0.6887 0.2742  0.1125  0.1609  158 ASN B CB  
1419 C CG  . ASN B 149 ? 0.8908 1.1524 0.7498 0.2856  0.0968  0.1453  158 ASN B CG  
1420 O OD1 . ASN B 149 ? 0.9125 1.1734 0.7621 0.2923  0.0865  0.1356  158 ASN B OD1 
1421 N ND2 . ASN B 149 ? 0.9268 1.1605 0.7747 0.2880  0.0945  0.1427  158 ASN B ND2 
1422 N N   . GLY B 150 ? 0.7148 0.9793 0.6529 0.2054  0.1134  0.1536  159 GLY B N   
1423 C CA  . GLY B 150 ? 0.6919 0.9363 0.6439 0.1850  0.1173  0.1551  159 GLY B CA  
1424 C C   . GLY B 150 ? 0.6788 0.8873 0.6131 0.1892  0.1118  0.1485  159 GLY B C   
1425 O O   . GLY B 150 ? 0.6861 0.8758 0.6292 0.1742  0.1141  0.1485  159 GLY B O   
1426 N N   . SER B 151 ? 0.6620 0.8606 0.5712 0.2101  0.1039  0.1422  160 SER B N   
1427 C CA  . SER B 151 ? 0.6534 0.8203 0.5456 0.2160  0.0975  0.1352  160 SER B CA  
1428 C C   . SER B 151 ? 0.6165 0.7587 0.5075 0.2042  0.0862  0.1209  160 SER B C   
1429 O O   . SER B 151 ? 0.6261 0.7749 0.5209 0.1990  0.0810  0.1152  160 SER B O   
1430 C CB  . SER B 151 ? 0.6892 0.8553 0.5561 0.2429  0.0922  0.1332  160 SER B CB  
1431 O OG  . SER B 151 ? 0.7709 0.9152 0.6272 0.2484  0.0919  0.1327  160 SER B OG  
1432 N N   . TYR B 152 ? 0.5915 0.7068 0.4756 0.2021  0.0825  0.1157  161 TYR B N   
1433 C CA  . TYR B 152 ? 0.5694 0.6615 0.4529 0.1905  0.0731  0.1035  161 TYR B CA  
1434 C C   . TYR B 152 ? 0.5588 0.6328 0.4215 0.2042  0.0608  0.0933  161 TYR B C   
1435 O O   . TYR B 152 ? 0.5775 0.6443 0.4259 0.2197  0.0590  0.0937  161 TYR B O   
1436 C CB  . TYR B 152 ? 0.5541 0.6292 0.4460 0.1777  0.0771  0.1041  161 TYR B CB  
1437 C CG  . TYR B 152 ? 0.5390 0.5934 0.4333 0.1643  0.0695  0.0930  161 TYR B CG  
1438 C CD1 . TYR B 152 ? 0.5386 0.5977 0.4456 0.1487  0.0684  0.0893  161 TYR B CD1 
1439 C CD2 . TYR B 152 ? 0.5460 0.5781 0.4307 0.1673  0.0642  0.0868  161 TYR B CD2 
1440 C CE1 . TYR B 152 ? 0.5410 0.5828 0.4496 0.1373  0.0625  0.0802  161 TYR B CE1 
1441 C CE2 . TYR B 152 ? 0.5542 0.5702 0.4422 0.1549  0.0585  0.0778  161 TYR B CE2 
1442 C CZ  . TYR B 152 ? 0.5526 0.5735 0.4518 0.1404  0.0579  0.0748  161 TYR B CZ  
1443 O OH  . TYR B 152 ? 0.5628 0.5692 0.4647 0.1292  0.0533  0.0669  161 TYR B OH  
1444 N N   . VAL B 153 ? 0.5246 0.5889 0.3858 0.1973  0.0519  0.0840  162 VAL B N   
1445 C CA  . VAL B 153 ? 0.5083 0.5523 0.3524 0.2066  0.0399  0.0746  162 VAL B CA  
1446 C C   . VAL B 153 ? 0.4689 0.4945 0.3199 0.1890  0.0355  0.0671  162 VAL B C   
1447 O O   . VAL B 153 ? 0.4748 0.5058 0.3352 0.1767  0.0359  0.0657  162 VAL B O   
1448 C CB  . VAL B 153 ? 0.5277 0.5784 0.3586 0.2204  0.0326  0.0716  162 VAL B CB  
1449 C CG1 . VAL B 153 ? 0.5515 0.5775 0.3649 0.2291  0.0191  0.0618  162 VAL B CG1 
1450 C CG2 . VAL B 153 ? 0.5382 0.6116 0.3632 0.2383  0.0382  0.0797  162 VAL B CG2 
1451 N N   . SER B 154 ? 0.4578 0.4638 0.3038 0.1894  0.0314  0.0625  163 SER B N   
1452 C CA  . SER B 154 ? 0.4385 0.4283 0.2910 0.1738  0.0277  0.0559  163 SER B CA  
1453 C C   . SER B 154 ? 0.4520 0.4263 0.2930 0.1771  0.0158  0.0479  163 SER B C   
1454 O O   . SER B 154 ? 0.4829 0.4492 0.3103 0.1918  0.0089  0.0453  163 SER B O   
1455 C CB  . SER B 154 ? 0.4522 0.4306 0.3069 0.1722  0.0300  0.0555  163 SER B CB  
1456 O OG  . SER B 154 ? 0.4460 0.4106 0.3063 0.1589  0.0262  0.0490  163 SER B OG  
1457 N N   . ALA B 155 ? 0.4268 0.3943 0.2729 0.1637  0.0130  0.0438  164 ALA B N   
1458 C CA  . ALA B 155 ? 0.4446 0.3945 0.2813 0.1647  0.0024  0.0374  164 ALA B CA  
1459 C C   . ALA B 155 ? 0.4645 0.3990 0.3013 0.1640  -0.0009 0.0334  164 ALA B C   
1460 O O   . ALA B 155 ? 0.4588 0.3961 0.3049 0.1584  0.0058  0.0352  164 ALA B O   
1461 C CB  . ALA B 155 ? 0.4426 0.3904 0.2859 0.1495  0.0021  0.0354  164 ALA B CB  
1462 N N   . ILE B 156 ? 0.4693 0.3875 0.2965 0.1692  -0.0116 0.0279  165 ILE B N   
1463 C CA  . ILE B 156 ? 0.4724 0.3768 0.3025 0.1655  -0.0159 0.0232  165 ILE B CA  
1464 C C   . ILE B 156 ? 0.4391 0.3382 0.2783 0.1478  -0.0158 0.0217  165 ILE B C   
1465 O O   . ILE B 156 ? 0.4657 0.3548 0.2993 0.1461  -0.0229 0.0196  165 ILE B O   
1466 C CB  . ILE B 156 ? 0.5118 0.4008 0.3289 0.1783  -0.0286 0.0174  165 ILE B CB  
1467 C CG1 . ILE B 156 ? 0.5319 0.4283 0.3384 0.1975  -0.0281 0.0192  165 ILE B CG1 
1468 C CG2 . ILE B 156 ? 0.5263 0.4033 0.3497 0.1724  -0.0333 0.0121  165 ILE B CG2 
1469 C CD1 . ILE B 156 ? 0.5640 0.4453 0.3554 0.2138  -0.0418 0.0123  165 ILE B CD1 
1470 N N   . THR B 157 ? 0.4304 0.3368 0.2828 0.1353  -0.0071 0.0233  166 THR B N   
1471 C CA  . THR B 157 ? 0.4302 0.3347 0.2898 0.1204  -0.0061 0.0224  166 THR B CA  
1472 C C   . THR B 157 ? 0.4286 0.3222 0.2929 0.1141  -0.0103 0.0183  166 THR B C   
1473 O O   . THR B 157 ? 0.4165 0.3119 0.2875 0.1129  -0.0072 0.0170  166 THR B O   
1474 C CB  . THR B 157 ? 0.4188 0.3361 0.2890 0.1112  0.0039  0.0252  166 THR B CB  
1475 O OG1 . THR B 157 ? 0.4291 0.3587 0.2974 0.1155  0.0076  0.0291  166 THR B OG1 
1476 C CG2 . THR B 157 ? 0.3999 0.3165 0.2769 0.0971  0.0053  0.0237  166 THR B CG2 
1477 N N   . GLN B 158 ? 0.4378 0.3208 0.2995 0.1092  -0.0170 0.0168  167 GLN B N   
1478 C CA  . GLN B 158 ? 0.4339 0.3086 0.3025 0.1016  -0.0210 0.0136  167 GLN B CA  
1479 C C   . GLN B 158 ? 0.4373 0.3136 0.3118 0.0874  -0.0176 0.0158  167 GLN B C   
1480 O O   . GLN B 158 ? 0.4411 0.3170 0.3094 0.0864  -0.0176 0.0186  167 GLN B O   
1481 C CB  . GLN B 158 ? 0.4659 0.3245 0.3263 0.1089  -0.0334 0.0102  167 GLN B CB  
1482 C CG  . GLN B 158 ? 0.4722 0.3227 0.3418 0.1010  -0.0389 0.0067  167 GLN B CG  
1483 C CD  . GLN B 158 ? 0.4689 0.3277 0.3482 0.1011  -0.0351 0.0038  167 GLN B CD  
1484 O OE1 . GLN B 158 ? 0.4494 0.3200 0.3368 0.0942  -0.0254 0.0057  167 GLN B OE1 
1485 N NE2 . GLN B 158 ? 0.4483 0.3007 0.3265 0.1093  -0.0431 -0.0015 167 GLN B NE2 
1486 N N   . GLY B 159 ? 0.4273 0.3057 0.3127 0.0783  -0.0153 0.0144  168 GLY B N   
1487 C CA  . GLY B 159 ? 0.4683 0.3493 0.3594 0.0658  -0.0119 0.0166  168 GLY B CA  
1488 C C   . GLY B 159 ? 0.5475 0.4160 0.4383 0.0610  -0.0196 0.0173  168 GLY B C   
1489 O O   . GLY B 159 ? 0.5845 0.4401 0.4689 0.0676  -0.0287 0.0156  168 GLY B O   
1490 N N   . LYS B 160 ? 0.5618 0.4335 0.4589 0.0495  -0.0160 0.0203  169 LYS B N   
1491 C CA  . LYS B 160 ? 0.5918 0.4524 0.4910 0.0426  -0.0220 0.0226  169 LYS B CA  
1492 C C   . LYS B 160 ? 0.5925 0.4619 0.5073 0.0334  -0.0191 0.0217  169 LYS B C   
1493 O O   . LYS B 160 ? 0.5765 0.4606 0.4973 0.0293  -0.0103 0.0221  169 LYS B O   
1494 C CB  . LYS B 160 ? 0.6457 0.5034 0.5375 0.0374  -0.0195 0.0288  169 LYS B CB  
1495 C CG  . LYS B 160 ? 0.7687 0.6124 0.6615 0.0298  -0.0255 0.0330  169 LYS B CG  
1496 C CD  . LYS B 160 ? 0.8648 0.7045 0.7479 0.0264  -0.0227 0.0400  169 LYS B CD  
1497 C CE  . LYS B 160 ? 0.9507 0.7715 0.8318 0.0204  -0.0299 0.0450  169 LYS B CE  
1498 N NZ  . LYS B 160 ? 1.0061 0.8250 0.8795 0.0155  -0.0253 0.0533  169 LYS B NZ  
1499 N N   . ARG B 161 ? 0.6054 0.4667 0.5271 0.0310  -0.0270 0.0196  170 ARG B N   
1500 C CA  . ARG B 161 ? 0.6312 0.5030 0.5694 0.0222  -0.0249 0.0188  170 ARG B CA  
1501 C C   . ARG B 161 ? 0.6750 0.5453 0.6181 0.0092  -0.0233 0.0262  170 ARG B C   
1502 O O   . ARG B 161 ? 0.6919 0.5460 0.6327 0.0062  -0.0313 0.0287  170 ARG B O   
1503 C CB  . ARG B 161 ? 0.6443 0.5108 0.5894 0.0261  -0.0345 0.0122  170 ARG B CB  
1504 C CG  . ARG B 161 ? 0.6611 0.5406 0.6247 0.0177  -0.0331 0.0105  170 ARG B CG  
1505 C CD  . ARG B 161 ? 0.6942 0.5679 0.6650 0.0213  -0.0443 0.0034  170 ARG B CD  
1506 N NE  . ARG B 161 ? 0.7133 0.6032 0.7032 0.0134  -0.0425 0.0016  170 ARG B NE  
1507 C CZ  . ARG B 161 ? 0.7167 0.6175 0.7128 0.0200  -0.0427 -0.0052 170 ARG B CZ  
1508 N NH1 . ARG B 161 ? 0.6756 0.5716 0.6600 0.0343  -0.0445 -0.0103 170 ARG B NH1 
1509 N NH2 . ARG B 161 ? 0.7212 0.6383 0.7349 0.0128  -0.0410 -0.0066 170 ARG B NH2 
1510 N N   . GLU B 162 ? 0.6886 0.5745 0.6362 0.0027  -0.0129 0.0302  171 GLU B N   
1511 C CA  . GLU B 162 ? 0.7290 0.6167 0.6804 -0.0087 -0.0091 0.0387  171 GLU B CA  
1512 C C   . GLU B 162 ? 0.7445 0.6349 0.7135 -0.0189 -0.0126 0.0399  171 GLU B C   
1513 O O   . GLU B 162 ? 0.7636 0.6472 0.7356 -0.0285 -0.0137 0.0476  171 GLU B O   
1514 C CB  . GLU B 162 ? 0.7694 0.6757 0.7204 -0.0106 0.0029  0.0414  171 GLU B CB  
1515 C CG  . GLU B 162 ? 0.8726 0.7792 0.8096 -0.0015 0.0062  0.0389  171 GLU B CG  
1516 C CD  . GLU B 162 ? 1.0229 0.9195 0.9453 -0.0005 0.0059  0.0445  171 GLU B CD  
1517 O OE1 . GLU B 162 ? 1.0542 0.9607 0.9721 -0.0016 0.0132  0.0474  171 GLU B OE1 
1518 O OE2 . GLU B 162 ? 1.0764 0.9554 0.9909 0.0027  -0.0022 0.0453  171 GLU B OE2 
1519 S S   . DMS C .   ? 0.9605 0.8906 0.9100 0.0240  0.0400  -0.0350 201 DMS B S   
1520 O O   . DMS C .   ? 0.9575 0.8970 0.9021 0.0268  0.0419  -0.0304 201 DMS B O   
1521 C C1  . DMS C .   ? 0.9673 0.8824 0.9163 0.0287  0.0415  -0.0372 201 DMS B C1  
1522 C C2  . DMS C .   ? 0.9559 0.8804 0.9139 0.0198  0.0415  -0.0268 201 DMS B C2  
1523 S S   . DMS D .   ? 1.0663 1.0711 1.0097 0.0571  0.0433  0.0350  202 DMS B S   
1524 O O   . DMS D .   ? 1.0704 1.0627 1.0002 0.0633  0.0387  0.0328  202 DMS B O   
1525 C C1  . DMS D .   ? 1.0654 1.0669 1.0183 0.0438  0.0432  0.0280  202 DMS B C1  
1526 C C2  . DMS D .   ? 1.0655 1.0645 1.0160 0.0568  0.0500  0.0404  202 DMS B C2  
1527 N N1  . ZUC E .   ? 0.7682 0.8028 0.7010 0.1250  0.0898  0.1046  203 ZUC B N1  
1528 C C4  . ZUC E .   ? 0.7894 0.7768 0.7138 0.1076  0.0675  0.0718  203 ZUC B C4  
1529 C C5  . ZUC E .   ? 0.7928 0.7781 0.7077 0.1213  0.0699  0.0771  203 ZUC B C5  
1530 C C6  . ZUC E .   ? 0.7862 0.7855 0.7024 0.1278  0.0771  0.0876  203 ZUC B C6  
1531 C C7  . ZUC E .   ? 0.7727 0.7894 0.7019 0.1192  0.0816  0.0927  203 ZUC B C7  
1532 C C8  . ZUC E .   ? 0.7778 0.8204 0.6981 0.1428  0.0914  0.1103  203 ZUC B C8  
1533 C C10 . ZUC E .   ? 0.7806 0.8543 0.7025 0.1583  0.1080  0.1337  203 ZUC B C10 
1534 C C13 . ZUC E .   ? 0.7720 0.8595 0.7133 0.1370  0.1008  0.1232  203 ZUC B C13 
1535 C C1  . ZUC E .   ? 0.7620 0.8000 0.7169 0.0954  0.0820  0.0904  203 ZUC B C1  
1536 C C2  . ZUC E .   ? 0.7703 0.7888 0.7100 0.1049  0.0783  0.0863  203 ZUC B C2  
1537 C C3  . ZUC E .   ? 0.7799 0.7830 0.7158 0.0999  0.0713  0.0759  203 ZUC B C3  
1538 O O1  . ZUC E .   ? 0.7956 0.7944 0.6988 0.1446  0.0779  0.0917  203 ZUC B O1  
1539 O O2  . ZUC E .   ? 0.7842 0.8165 0.6881 0.1565  0.0857  0.1056  203 ZUC B O2  
1540 C C9  . ZUC E .   ? 0.7769 0.8446 0.7052 0.1454  0.1001  0.1223  203 ZUC B C9  
1541 C C11 . ZUC E .   ? 0.7705 0.8702 0.7000 0.1613  0.1166  0.1456  203 ZUC B C11 
1542 N N2  . ZUC E .   ? 0.7583 0.8784 0.7019 0.1524  0.1171  0.1462  203 ZUC B N2  
1543 C C12 . ZUC E .   ? 0.7593 0.8725 0.7084 0.1404  0.1088  0.1345  203 ZUC B C12 
1544 F F1  . ZUC E .   ? 0.7819 0.8648 0.7288 0.1253  0.0936  0.1128  203 ZUC B F1  
# 
