data_7HOX
# 
_entry.id   7HOX 
# 
_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   7HOX         pdb_00007hox 10.2210/pdb7hox/pdb 
WWPDB D_1001407747 ?            ?                   
# 
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                        7HOX 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                         5067.486  1  ?                           
?    ? ? 
2 polymer     man 'Serine protease NS3'                                                  18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 
None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                   78.133    3  ?                           
?    ? ? 
4 non-polymer syn '(2P)-2-(6-methoxypyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' 308.335   1  ?                           
?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                          96.063    1  ?                           
?    ? ? 
6 water       nat water                                                                  18.015    97 ?                           
?    ? ? 
# 
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 '(2P)-2-(6-methoxypyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' A1BGK 
5 'SULFATE ION'                                                          SO4   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BGK non-polymer         . '(2P)-2-(6-methoxypyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' ? 'C17 H16 N4 O2'  308.335 
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                          ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGK 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BGK 1  204 301 A1BGK LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 6 HOH   1  101 105 HOH   HOH A . 
H 6 HOH   2  102 65  HOH   HOH A . 
H 6 HOH   3  103 34  HOH   HOH A . 
H 6 HOH   4  104 54  HOH   HOH A . 
H 6 HOH   5  105 121 HOH   HOH A . 
H 6 HOH   6  106 118 HOH   HOH A . 
H 6 HOH   7  107 98  HOH   HOH A . 
H 6 HOH   8  108 117 HOH   HOH A . 
H 6 HOH   9  109 49  HOH   HOH A . 
H 6 HOH   10 110 120 HOH   HOH A . 
H 6 HOH   11 111 110 HOH   HOH A . 
H 6 HOH   12 112 16  HOH   HOH A . 
H 6 HOH   13 113 77  HOH   HOH A . 
H 6 HOH   14 114 50  HOH   HOH A . 
H 6 HOH   15 115 28  HOH   HOH A . 
H 6 HOH   16 116 127 HOH   HOH A . 
H 6 HOH   17 117 70  HOH   HOH A . 
H 6 HOH   18 118 29  HOH   HOH A . 
H 6 HOH   19 119 119 HOH   HOH A . 
H 6 HOH   20 120 128 HOH   HOH A . 
H 6 HOH   21 121 27  HOH   HOH A . 
H 6 HOH   22 122 85  HOH   HOH A . 
I 6 HOH   1  301 40  HOH   HOH B . 
I 6 HOH   2  302 51  HOH   HOH B . 
I 6 HOH   3  303 5   HOH   HOH B . 
I 6 HOH   4  304 11  HOH   HOH B . 
I 6 HOH   5  305 90  HOH   HOH B . 
I 6 HOH   6  306 123 HOH   HOH B . 
I 6 HOH   7  307 100 HOH   HOH B . 
I 6 HOH   8  308 58  HOH   HOH B . 
I 6 HOH   9  309 92  HOH   HOH B . 
I 6 HOH   10 310 57  HOH   HOH B . 
I 6 HOH   11 311 1   HOH   HOH B . 
I 6 HOH   12 312 23  HOH   HOH B . 
I 6 HOH   13 313 63  HOH   HOH B . 
I 6 HOH   14 314 108 HOH   HOH B . 
I 6 HOH   15 315 130 HOH   HOH B . 
I 6 HOH   16 316 42  HOH   HOH B . 
I 6 HOH   17 317 48  HOH   HOH B . 
I 6 HOH   18 318 115 HOH   HOH B . 
I 6 HOH   19 319 14  HOH   HOH B . 
I 6 HOH   20 320 4   HOH   HOH B . 
I 6 HOH   21 321 125 HOH   HOH B . 
I 6 HOH   22 322 32  HOH   HOH B . 
I 6 HOH   23 323 124 HOH   HOH B . 
I 6 HOH   24 324 20  HOH   HOH B . 
I 6 HOH   25 325 81  HOH   HOH B . 
I 6 HOH   26 326 89  HOH   HOH B . 
I 6 HOH   27 327 122 HOH   HOH B . 
I 6 HOH   28 328 30  HOH   HOH B . 
I 6 HOH   29 329 31  HOH   HOH B . 
I 6 HOH   30 330 129 HOH   HOH B . 
I 6 HOH   31 331 60  HOH   HOH B . 
I 6 HOH   32 332 68  HOH   HOH B . 
I 6 HOH   33 333 17  HOH   HOH B . 
I 6 HOH   34 334 46  HOH   HOH B . 
I 6 HOH   35 335 2   HOH   HOH B . 
I 6 HOH   36 336 21  HOH   HOH B . 
I 6 HOH   37 337 62  HOH   HOH B . 
I 6 HOH   38 338 39  HOH   HOH B . 
I 6 HOH   39 339 56  HOH   HOH B . 
I 6 HOH   40 340 36  HOH   HOH B . 
I 6 HOH   41 341 24  HOH   HOH B . 
I 6 HOH   42 342 106 HOH   HOH B . 
I 6 HOH   43 343 10  HOH   HOH B . 
I 6 HOH   44 344 35  HOH   HOH B . 
I 6 HOH   45 345 72  HOH   HOH B . 
I 6 HOH   46 346 67  HOH   HOH B . 
I 6 HOH   47 347 66  HOH   HOH B . 
I 6 HOH   48 348 116 HOH   HOH B . 
I 6 HOH   49 349 73  HOH   HOH B . 
I 6 HOH   50 350 9   HOH   HOH B . 
I 6 HOH   51 351 3   HOH   HOH B . 
I 6 HOH   52 352 107 HOH   HOH B . 
I 6 HOH   53 353 64  HOH   HOH B . 
I 6 HOH   54 354 82  HOH   HOH B . 
I 6 HOH   55 355 12  HOH   HOH B . 
I 6 HOH   56 356 13  HOH   HOH B . 
I 6 HOH   57 357 103 HOH   HOH B . 
I 6 HOH   58 358 102 HOH   HOH B . 
I 6 HOH   59 359 18  HOH   HOH B . 
I 6 HOH   60 360 43  HOH   HOH B . 
I 6 HOH   61 361 126 HOH   HOH B . 
I 6 HOH   62 362 112 HOH   HOH B . 
I 6 HOH   63 363 69  HOH   HOH B . 
I 6 HOH   64 364 80  HOH   HOH B . 
I 6 HOH   65 365 26  HOH   HOH B . 
I 6 HOH   66 366 94  HOH   HOH B . 
I 6 HOH   67 367 109 HOH   HOH B . 
I 6 HOH   68 368 87  HOH   HOH B . 
I 6 HOH   69 369 59  HOH   HOH B . 
I 6 HOH   70 370 44  HOH   HOH B . 
I 6 HOH   71 371 83  HOH   HOH B . 
I 6 HOH   72 372 45  HOH   HOH B . 
I 6 HOH   73 373 61  HOH   HOH B . 
I 6 HOH   74 374 79  HOH   HOH B . 
I 6 HOH   75 375 75  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HOX 
_cell.length_a           42.481 
_cell.length_b           42.481 
_cell.length_c           216.453 
_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                         7HOX 
_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          7HOX 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.59 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-09-27 
_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                     7HOX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.43 
_reflns.d_resolution_high            1.67 
_reflns.number_obs                   24396 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.201 
_reflns.pdbx_netI_over_sigmaI        7.2 
_reflns.pdbx_redundancy              25.5 
_reflns.pdbx_Rrim_I_all              0.205 
_reflns.pdbx_Rpim_I_all              0.040 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     621836 
_reflns.pdbx_chi_squared             0.22 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.67 
_reflns_shell.d_res_low                   1.70 
_reflns_shell.number_measured_all         33390 
_reflns_shell.number_unique_obs           1273 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.09 
_reflns_shell.pdbx_redundancy             26.2 
_reflns_shell.percent_possible_obs        99.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             16.480 
_reflns_shell.pdbx_Rpim_I_all             3.181 
_reflns_shell.pdbx_CC_half                0.487 
_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                                 7HOX 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     20309 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.11 
_refine.ls_d_res_high                            1.67 
_refine.ls_percent_reflns_obs                    87.97 
_refine.ls_R_factor_obs                          0.23672 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23437 
_refine.ls_R_factor_R_free                       0.28119 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1080 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.B_iso_mean                               55.224 
_refine.aniso_B[1][1]                            1.80 
_refine.aniso_B[2][2]                            1.80 
_refine.aniso_B[3][3]                            -3.60 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.159 
_refine.pdbx_overall_ESU_R_Free                  0.152 
_refine.overall_SU_ML                            0.204 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             14.125 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               1613 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        54.11 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.011  0.013  ? 2005 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1682 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.682  1.639  ? 2481 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.254  1.589  ? 3874 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.919  5.000  ? 238  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       31.340 22.500 ? 80   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.355 15.000 ? 283  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       17.550 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.066  0.200  ? 219  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2139 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 421  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.105  3.501  ? 990  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.135  3.373  ? 958  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.558  4.980  ? 1152 'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.558  4.985  ? 1153 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.618  4.415  ? 1015 'X-RAY DIFFRACTION' ? 
r_scbond_other               2.631  4.358  ? 1002 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              4.309  5.847  ? 1318 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       23.015 37.835 ? 1963 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         23.074 37.500 ? 1945 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.669 
_refine_ls_shell.d_res_low                        1.712 
_refine_ls_shell.number_reflns_R_work             386 
_refine_ls_shell.R_factor_R_work                  0.644 
_refine_ls_shell.percent_reflns_obs               23.48 
_refine_ls_shell.R_factor_R_free                  0.723 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             24 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HOX 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014821-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOX 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HOX A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOX 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 7HOX SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOX MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOX MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOX LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.460 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
# 
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 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? 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 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA2 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA2 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA2 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA2 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA2 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
AA3 1 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA3 2 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA3 3 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA3 4 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N GLN B 33  ? N GLN B 42  O VAL B 36  ? O VAL B 45  
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 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA2 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA2 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA2 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA2 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA3 1 2 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA3 2 3 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA3 3 4 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
# 
_pdbx_entry_details.entry_id                   7HOX 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B DMS 203 ? A O B HOH 301 ? ? 2.03 
2 1 O   B DMS 203 ? B O B HOH 301 ? ? 2.04 
3 1 OE1 B GLU 17  ? ? O B HOH 302 ? ? 2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP B 20  ? ? -49.13  151.47  
2 1 LEU B 30  ? ? -116.53 -165.43 
3 1 ASP B 71  ? ? -160.35 115.23  
4 1 CYS B 80  ? ? 82.95   -11.11  
5 1 LEU B 92  ? ? -129.59 -56.07  
6 1 ALA B 127 ? ? -101.33 65.06   
7 1 ALA B 127 ? ? -101.11 65.06   
8 1 ALA B 127 ? ? -101.33 65.06   
9 1 ALA B 127 ? ? -101.11 65.06   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 338 ? I HOH . 
2 1 B HOH 372 ? I HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.4835 -1.8719 -19.3211 0.2549 0.3167 0.0528 0.1811 0.0708 0.0633 1.0426 2.0234 0.7464 -0.4864 
-0.2402 0.0629  0.4047 0.2997 0.2213 -0.2897 -0.3672 -0.1623 -0.1260 0.2588 -0.0376 
'X-RAY DIFFRACTION' 2 ? refined -18.2466 0.7681  -15.8446 0.2459 0.2272 0.1340 0.1345 0.0601 0.0139 0.3104 0.3125 0.9225 -0.2061 
0.4151  -0.0831 0.2270 0.1780 0.0472 -0.1981 -0.2451 0.0174  0.1594  0.1278 0.0181  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 302 ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BGK N1   N N N 1   
A1BGK N3   N Y N 2   
A1BGK C4   C Y N 3   
A1BGK C5   C Y N 4   
A1BGK C6   C Y N 5   
A1BGK C7   C Y N 6   
A1BGK C8   C Y N 7   
A1BGK C10  C Y N 8   
A1BGK C13  C Y N 9   
A1BGK C15  C N N 10  
A1BGK C17  C Y N 11  
A1BGK C1   C N N 12  
A1BGK O1   O N N 13  
A1BGK C2   C Y N 14  
A1BGK C3   C Y N 15  
A1BGK C9   C Y N 16  
A1BGK C11  C Y N 17  
A1BGK C12  C N N 18  
A1BGK O2   O N N 19  
A1BGK C14  C Y N 20  
A1BGK N2   N Y N 21  
A1BGK C16  C Y N 22  
A1BGK N4   N Y N 23  
A1BGK H10  H N N 24  
A1BGK H5   H N N 25  
A1BGK H6   H N N 26  
A1BGK H7   H N N 27  
A1BGK H9   H N N 28  
A1BGK H12  H N N 29  
A1BGK H14  H N N 30  
A1BGK H13  H N N 31  
A1BGK H16  H N N 32  
A1BGK H2   H N N 33  
A1BGK H1   H N N 34  
A1BGK H3   H N N 35  
A1BGK H4   H N N 36  
A1BGK H8   H N N 37  
A1BGK H11  H N N 38  
A1BGK H15  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
DMS   S    S N N 127 
DMS   O    O N N 128 
DMS   C1   C N N 129 
DMS   C2   C N N 130 
DMS   H11  H N N 131 
DMS   H12  H N N 132 
DMS   H13  H N N 133 
DMS   H21  H N N 134 
DMS   H22  H N N 135 
DMS   H23  H N N 136 
GLN   N    N N N 137 
GLN   CA   C N S 138 
GLN   C    C N N 139 
GLN   O    O N N 140 
GLN   CB   C N N 141 
GLN   CG   C N N 142 
GLN   CD   C N N 143 
GLN   OE1  O N N 144 
GLN   NE2  N N N 145 
GLN   OXT  O N N 146 
GLN   H    H N N 147 
GLN   H2   H N N 148 
GLN   HA   H N N 149 
GLN   HB2  H N N 150 
GLN   HB3  H N N 151 
GLN   HG2  H N N 152 
GLN   HG3  H N N 153 
GLN   HE21 H N N 154 
GLN   HE22 H N N 155 
GLN   HXT  H N N 156 
GLU   N    N N N 157 
GLU   CA   C N S 158 
GLU   C    C N N 159 
GLU   O    O N N 160 
GLU   CB   C N N 161 
GLU   CG   C N N 162 
GLU   CD   C N N 163 
GLU   OE1  O N N 164 
GLU   OE2  O N N 165 
GLU   OXT  O N N 166 
GLU   H    H N N 167 
GLU   H2   H N N 168 
GLU   HA   H N N 169 
GLU   HB2  H N N 170 
GLU   HB3  H N N 171 
GLU   HG2  H N N 172 
GLU   HG3  H N N 173 
GLU   HE2  H N N 174 
GLU   HXT  H N N 175 
GLY   N    N N N 176 
GLY   CA   C N N 177 
GLY   C    C N N 178 
GLY   O    O N N 179 
GLY   OXT  O N N 180 
GLY   H    H N N 181 
GLY   H2   H N N 182 
GLY   HA2  H N N 183 
GLY   HA3  H N N 184 
GLY   HXT  H N N 185 
HIS   N    N N N 186 
HIS   CA   C N S 187 
HIS   C    C N N 188 
HIS   O    O N N 189 
HIS   CB   C N N 190 
HIS   CG   C Y N 191 
HIS   ND1  N Y N 192 
HIS   CD2  C Y N 193 
HIS   CE1  C Y N 194 
HIS   NE2  N Y N 195 
HIS   OXT  O N N 196 
HIS   H    H N N 197 
HIS   H2   H N N 198 
HIS   HA   H N N 199 
HIS   HB2  H N N 200 
HIS   HB3  H N N 201 
HIS   HD1  H N N 202 
HIS   HD2  H N N 203 
HIS   HE1  H N N 204 
HIS   HE2  H N N 205 
HIS   HXT  H N N 206 
HOH   O    O N N 207 
HOH   H1   H N N 208 
HOH   H2   H N N 209 
ILE   N    N N N 210 
ILE   CA   C N S 211 
ILE   C    C N N 212 
ILE   O    O N N 213 
ILE   CB   C N S 214 
ILE   CG1  C N N 215 
ILE   CG2  C N N 216 
ILE   CD1  C N N 217 
ILE   OXT  O N N 218 
ILE   H    H N N 219 
ILE   H2   H N N 220 
ILE   HA   H N N 221 
ILE   HB   H N N 222 
ILE   HG12 H N N 223 
ILE   HG13 H N N 224 
ILE   HG21 H N N 225 
ILE   HG22 H N N 226 
ILE   HG23 H N N 227 
ILE   HD11 H N N 228 
ILE   HD12 H N N 229 
ILE   HD13 H N N 230 
ILE   HXT  H N N 231 
LEU   N    N N N 232 
LEU   CA   C N S 233 
LEU   C    C N N 234 
LEU   O    O N N 235 
LEU   CB   C N N 236 
LEU   CG   C N N 237 
LEU   CD1  C N N 238 
LEU   CD2  C N N 239 
LEU   OXT  O N N 240 
LEU   H    H N N 241 
LEU   H2   H N N 242 
LEU   HA   H N N 243 
LEU   HB2  H N N 244 
LEU   HB3  H N N 245 
LEU   HG   H N N 246 
LEU   HD11 H N N 247 
LEU   HD12 H N N 248 
LEU   HD13 H N N 249 
LEU   HD21 H N N 250 
LEU   HD22 H N N 251 
LEU   HD23 H N N 252 
LEU   HXT  H N N 253 
LYS   N    N N N 254 
LYS   CA   C N S 255 
LYS   C    C N N 256 
LYS   O    O N N 257 
LYS   CB   C N N 258 
LYS   CG   C N N 259 
LYS   CD   C N N 260 
LYS   CE   C N N 261 
LYS   NZ   N N N 262 
LYS   OXT  O N N 263 
LYS   H    H N N 264 
LYS   H2   H N N 265 
LYS   HA   H N N 266 
LYS   HB2  H N N 267 
LYS   HB3  H N N 268 
LYS   HG2  H N N 269 
LYS   HG3  H N N 270 
LYS   HD2  H N N 271 
LYS   HD3  H N N 272 
LYS   HE2  H N N 273 
LYS   HE3  H N N 274 
LYS   HZ1  H N N 275 
LYS   HZ2  H N N 276 
LYS   HZ3  H N N 277 
LYS   HXT  H N N 278 
MET   N    N N N 279 
MET   CA   C N S 280 
MET   C    C N N 281 
MET   O    O N N 282 
MET   CB   C N N 283 
MET   CG   C N N 284 
MET   SD   S N N 285 
MET   CE   C N N 286 
MET   OXT  O N N 287 
MET   H    H N N 288 
MET   H2   H N N 289 
MET   HA   H N N 290 
MET   HB2  H N N 291 
MET   HB3  H N N 292 
MET   HG2  H N N 293 
MET   HG3  H N N 294 
MET   HE1  H N N 295 
MET   HE2  H N N 296 
MET   HE3  H N N 297 
MET   HXT  H N N 298 
PHE   N    N N N 299 
PHE   CA   C N S 300 
PHE   C    C N N 301 
PHE   O    O N N 302 
PHE   CB   C N N 303 
PHE   CG   C Y N 304 
PHE   CD1  C Y N 305 
PHE   CD2  C Y N 306 
PHE   CE1  C Y N 307 
PHE   CE2  C Y N 308 
PHE   CZ   C Y N 309 
PHE   OXT  O N N 310 
PHE   H    H N N 311 
PHE   H2   H N N 312 
PHE   HA   H N N 313 
PHE   HB2  H N N 314 
PHE   HB3  H N N 315 
PHE   HD1  H N N 316 
PHE   HD2  H N N 317 
PHE   HE1  H N N 318 
PHE   HE2  H N N 319 
PHE   HZ   H N N 320 
PHE   HXT  H N N 321 
PRO   N    N N N 322 
PRO   CA   C N S 323 
PRO   C    C N N 324 
PRO   O    O N N 325 
PRO   CB   C N N 326 
PRO   CG   C N N 327 
PRO   CD   C N N 328 
PRO   OXT  O N N 329 
PRO   H    H N N 330 
PRO   HA   H N N 331 
PRO   HB2  H N N 332 
PRO   HB3  H N N 333 
PRO   HG2  H N N 334 
PRO   HG3  H N N 335 
PRO   HD2  H N N 336 
PRO   HD3  H N N 337 
PRO   HXT  H N N 338 
SER   N    N N N 339 
SER   CA   C N S 340 
SER   C    C N N 341 
SER   O    O N N 342 
SER   CB   C N N 343 
SER   OG   O N N 344 
SER   OXT  O N N 345 
SER   H    H N N 346 
SER   H2   H N N 347 
SER   HA   H N N 348 
SER   HB2  H N N 349 
SER   HB3  H N N 350 
SER   HG   H N N 351 
SER   HXT  H N N 352 
SO4   S    S N N 353 
SO4   O1   O N N 354 
SO4   O2   O N N 355 
SO4   O3   O N N 356 
SO4   O4   O N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1BGK C1  O1   sing N N 1   
A1BGK O1  C2   sing N N 2   
A1BGK C2  C3   doub Y N 3   
A1BGK C3  C4   sing Y N 4   
A1BGK C4  C5   doub Y N 5   
A1BGK C5  C6   sing N N 6   
A1BGK C6  C7   doub Y N 7   
A1BGK C7  C8   sing Y N 8   
A1BGK C8  C9   doub Y N 9   
A1BGK C9  C10  sing Y N 10  
A1BGK C10 C11  doub Y N 11  
A1BGK C11 C12  sing N N 12  
A1BGK C12 O2   doub N N 13  
A1BGK C12 N1   sing N N 14  
A1BGK N1  C13  sing N N 15  
A1BGK C13 C14  sing Y N 16  
A1BGK C14 N2   doub Y N 17  
A1BGK N2  N3   sing Y N 18  
A1BGK N3  C15  sing N N 19  
A1BGK N3  C16  sing Y N 20  
A1BGK C5  C17  sing Y N 21  
A1BGK C17 N4   doub Y N 22  
A1BGK C2  N4   sing Y N 23  
A1BGK C6  C11  sing Y N 24  
A1BGK C13 C16  doub Y N 25  
A1BGK N1  H10  sing N N 26  
A1BGK C4  H5   sing N N 27  
A1BGK C7  H6   sing N N 28  
A1BGK C8  H7   sing N N 29  
A1BGK C10 H9   sing N N 30  
A1BGK C15 H12  sing N N 31  
A1BGK C15 H14  sing N N 32  
A1BGK C15 H13  sing N N 33  
A1BGK C17 H16  sing N N 34  
A1BGK C1  H2   sing N N 35  
A1BGK C1  H1   sing N N 36  
A1BGK C1  H3   sing N N 37  
A1BGK C3  H4   sing N N 38  
A1BGK C9  H8   sing N N 39  
A1BGK C14 H11  sing N N 40  
A1BGK C16 H15  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
SO4   S   O1   doub N N 340 
SO4   S   O2   doub N N 341 
SO4   S   O3   sing N N 342 
SO4   S   O4   sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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                    7HOX 
_atom_sites.fract_transf_matrix[1][1]   0.023540 
_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]   0.023540 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004620 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -20.662 19.018  -7.672  1.00 65.60  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -21.959 18.290  -7.586  1.00 65.34  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.221 17.575  -8.921  1.00 62.17  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.210 18.225  -9.988  1.00 67.57  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.076 19.250  -7.187  1.00 66.24  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.409 18.586  -6.912  1.00 66.44  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.619 18.096  -5.775  1.00 71.51  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.252 18.600  -7.828  1.00 69.21  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.423 16.270  -8.863  1.00 55.91  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.376 15.393  -10.052 1.00 53.84  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.801 15.168  -10.547 1.00 46.32  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.675 15.082  -9.716  1.00 45.94  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.708 14.053  -9.736  1.00 53.44  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.272 14.223  -9.377  1.00 56.82  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.437 12.639  -9.237  1.00 56.70  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.737 13.205  -9.192  1.00 57.98  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.969 15.145  -11.864 1.00 44.53  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.241 14.887  -12.571 1.00 43.33  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -24.977 13.889  -13.687 1.00 42.29  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.847 13.750  -14.189 1.00 41.76  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.883 16.202  -13.044 1.00 43.60  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.094 17.015  -14.031 1.00 43.78  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.110 17.882  -13.590 1.00 44.14  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.318 16.924  -15.405 1.00 44.26  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.360 18.648  -14.478 1.00 44.75  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.564 17.668  -16.309 1.00 45.40  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.587 18.543  -15.839 1.00 45.93  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.791 19.261  -16.704 1.00 49.22  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.034 13.199  -14.083 1.00 43.01  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.009 12.220  -15.205 1.00 42.14  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.821 12.721  -16.421 1.00 44.04  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.839 13.433  -16.229 1.00 41.79  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.492 10.849  -14.705 1.00 41.36  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -27.928 10.859  -14.220 1.00 42.83  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.575 10.317  -13.614 1.00 42.19  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.449 9.478   -14.046 1.00 44.00  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.395 12.320  -17.624 1.00 45.00  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.080 12.581  -18.924 1.00 47.32  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.102 11.285  -19.744 1.00 46.43  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.042 10.555  -19.826 1.00 43.44  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.363 13.614  -19.793 1.00 48.87  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.303 15.039  -19.272 1.00 52.28  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.346 15.906  -20.092 1.00 57.78  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.511 15.361  -20.868 1.00 59.07  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.416 17.137  -19.975 1.00 62.03  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.259 10.967  -20.330 1.00 47.61  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.381 9.734   -21.150 1.00 47.88  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.485 9.900   -22.376 1.00 47.01  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.399 11.020  -22.893 1.00 49.05  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.846 9.455   -21.440 1.00 48.83  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.112 8.075   -22.017 1.00 52.22  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.564 7.655   -21.843 1.00 55.62  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.795 6.252   -22.107 1.00 56.96  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.696 5.707   -23.320 1.00 61.53  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.359 6.452   -24.354 1.00 65.48  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.870 4.408   -23.502 1.00 62.35  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.725 8.862   -22.744 1.00 47.20  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.789 8.859   -23.907 1.00 45.53  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.136 7.756   -24.912 1.00 44.54  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.492 7.733   -26.000 1.00 46.80  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.335 8.731   -23.486 1.00 47.01  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.074 6.869   -24.606 1.00 41.54  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.482 5.857   -25.593 1.00 42.20  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.188 4.681   -24.963 1.00 43.46  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.254 4.648   -23.681 1.00 43.16  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.693 3.770   -25.819 1.00 45.99  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.212 2.409   -25.491 1.00 46.99  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.031 1.440   -25.340 1.00 49.09  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.970 1.690   -25.915 1.00 52.78  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.091 1.761   -26.566 1.00 47.62  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.430 2.430   -26.748 1.00 52.18  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.673 3.415   -26.045 1.00 47.36  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.191 2.001   -27.649 1.00 54.74  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.240 0.351   -24.619 1.00 49.02  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.206 -0.706  -24.472 1.00 50.93  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.614 -1.819  -25.434 1.00 52.22  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.567 -2.576  -25.136 1.00 51.61  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.066 -1.137  -23.018 1.00 51.34  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.476 0.014   -22.200 1.00 50.65  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.232 -2.406  -22.897 1.00 50.56  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.578 -0.204  -20.740 1.00 50.56  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.901 -1.888  -26.564 0.25 53.14  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.902 -1.927  -26.556 0.25 52.98  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.901 -1.888  -26.564 0.25 53.14  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.902 -1.927  -26.556 0.25 52.98  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.157 -2.777  -27.729 0.25 54.74  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.214 -2.879  -27.651 0.25 54.45  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.157 -2.777  -27.729 0.25 54.74  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.214 -2.879  -27.651 0.25 54.45  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.825 -3.362  -28.234 0.25 55.10  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -25.918 -3.330  -28.352 0.25 55.27  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.825 -3.362  -28.234 0.25 55.10  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -25.918 -3.330  -28.352 0.25 55.27  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.754 -2.586  -28.287 0.25 55.20  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -24.986 -2.425  -28.652 0.25 55.86  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.754 -2.586  -28.287 0.25 55.20  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -24.986 -2.425  -28.652 0.25 55.86  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -27.830 -2.015  -28.879 0.25 56.07  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.209 -2.249  -28.633 0.25 55.52  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -27.830 -2.015  -28.879 0.25 56.07  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.209 -2.249  -28.633 0.25 55.52  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -26.919 -1.046  -29.391 0.25 55.84  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.422 -2.070  -27.900 0.25 54.86  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -26.919 -1.046  -29.391 0.25 55.84  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.422 -2.070  -27.900 0.25 54.86  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.084 -1.288  -28.456 0.25 56.87  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.453 -3.093  -29.861 0.25 56.22  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.084 -1.288  -28.456 0.25 56.87  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.453 -3.093  -29.861 0.25 56.22  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.863 -4.659  -28.609 1.00 55.97  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.790 -5.252  -29.432 1.00 59.61  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.004 -4.689  -30.841 1.00 65.60  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.170 -4.621  -31.238 1.00 69.48  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.895 -6.768  -29.412 1.00 60.56  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.836 -7.411  -30.237 1.00 63.52  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.899 -7.682  -31.576 1.00 67.22  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.560 -7.895  -29.780 1.00 64.83  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.734 -8.271  -31.979 1.00 68.20  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.900 -8.432  -30.906 1.00 67.60  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.908 -7.931  -28.544 1.00 61.88  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.624 -8.994  -30.822 1.00 68.48  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.650 -8.480  -28.462 1.00 63.54  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.020 -9.014  -29.580 1.00 65.32  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -23.956 -4.232  -31.531 1.00 70.10  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -24.047 -3.679  -32.907 1.00 75.49  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.220 -4.544  -33.859 1.00 78.37  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -21.979 -4.547  -33.718 1.00 71.55  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -23.588 -2.226  -32.932 1.00 81.01  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -24.435 -1.328  -32.024 1.00 89.43  ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -25.860 -0.996  -32.469 1.00 96.12  ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -26.071 -0.719  -33.687 1.00 102.96 ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -26.760 -0.969  -31.592 1.00 95.67  ? 62  GLU   A OE2 1 
ATOM   133  N N   . LYS   A 1 20  ? -23.882 -5.229  -34.800 1.00 82.77  ? 63  LYS   A N   1 
ATOM   134  C CA  . LYS   A 1 20  ? -23.212 -6.103  -35.809 1.00 84.82  ? 63  LYS   A CA  1 
ATOM   135  C C   . LYS   A 1 20  ? -22.297 -5.220  -36.643 1.00 80.29  ? 63  LYS   A C   1 
ATOM   136  O O   . LYS   A 1 20  ? -22.691 -4.111  -36.940 1.00 82.76  ? 63  LYS   A O   1 
ATOM   137  C CB  . LYS   A 1 20  ? -24.220 -6.832  -36.696 1.00 89.25  ? 63  LYS   A CB  1 
ATOM   138  C CG  . LYS   A 1 20  ? -24.915 -8.010  -36.034 1.00 93.83  ? 63  LYS   A CG  1 
ATOM   139  C CD  . LYS   A 1 20  ? -26.352 -8.147  -36.478 1.00 99.82  ? 63  LYS   A CD  1 
ATOM   140  C CE  . LYS   A 1 20  ? -27.046 -9.355  -35.886 1.00 104.91 ? 63  LYS   A CE  1 
ATOM   141  N NZ  . LYS   A 1 20  ? -28.480 -9.365  -36.257 1.00 107.79 ? 63  LYS   A NZ  1 
ATOM   142  N N   . ASP   A 1 21  ? -21.099 -5.686  -36.963 1.00 83.54  ? 64  ASP   A N   1 
ATOM   143  C CA  . ASP   A 1 21  ? -20.116 -4.890  -37.749 1.00 89.18  ? 64  ASP   A CA  1 
ATOM   144  C C   . ASP   A 1 21  ? -19.794 -3.578  -36.995 1.00 85.06  ? 64  ASP   A C   1 
ATOM   145  O O   . ASP   A 1 21  ? -19.886 -2.514  -37.601 1.00 80.77  ? 64  ASP   A O   1 
ATOM   146  C CB  . ASP   A 1 21  ? -20.616 -4.596  -39.182 1.00 98.89  ? 64  ASP   A CB  1 
ATOM   147  C CG  . ASP   A 1 21  ? -20.959 -5.783  -40.085 1.00 103.85 ? 64  ASP   A CG  1 
ATOM   148  O OD1 . ASP   A 1 21  ? -20.011 -6.404  -40.654 1.00 108.57 ? 64  ASP   A OD1 1 
ATOM   149  O OD2 . ASP   A 1 21  ? -22.183 -6.056  -40.257 1.00 102.84 ? 64  ASP   A OD2 1 
ATOM   150  N N   . ALA   A 1 22  ? -19.402 -3.631  -35.712 1.00 82.30  ? 65  ALA   A N   1 
ATOM   151  C CA  . ALA   A 1 22  ? -18.626 -2.539  -35.066 1.00 75.18  ? 65  ALA   A CA  1 
ATOM   152  C C   . ALA   A 1 22  ? -17.114 -2.731  -35.459 1.00 72.90  ? 65  ALA   A C   1 
ATOM   153  O O   . ALA   A 1 22  ? -16.723 -3.843  -35.701 1.00 73.14  ? 65  ALA   A O   1 
ATOM   154  C CB  . ALA   A 1 22  ? -18.820 -2.552  -33.568 1.00 74.67  ? 65  ALA   A CB  1 
ATOM   155  N N   . GLU   A 1 23  ? -16.343 -1.635  -35.214 1.00 71.21  ? 66  GLU   A N   1 
ATOM   156  C CA  . GLU   A 1 23  ? -14.858 -1.590  -35.335 1.00 74.25  ? 66  GLU   A CA  1 
ATOM   157  C C   . GLU   A 1 23  ? -14.259 -2.640  -34.372 1.00 73.27  ? 66  GLU   A C   1 
ATOM   158  O O   . GLU   A 1 23  ? -14.530 -2.580  -33.150 1.00 67.53  ? 66  GLU   A O   1 
ATOM   159  C CB  . GLU   A 1 23  ? -14.398 -0.160  -35.045 1.00 80.51  ? 66  GLU   A CB  1 
ATOM   160  C CG  . GLU   A 1 23  ? -12.900 0.021   -34.865 1.00 87.60  ? 66  GLU   A CG  1 
ATOM   161  C CD  . GLU   A 1 23  ? -12.552 1.481   -34.599 1.00 96.97  ? 66  GLU   A CD  1 
ATOM   162  O OE1 . GLU   A 1 23  ? -12.829 2.352   -35.491 1.00 100.58 ? 66  GLU   A OE1 1 
ATOM   163  O OE2 . GLU   A 1 23  ? -12.033 1.758   -33.493 1.00 99.17  ? 66  GLU   A OE2 1 
ATOM   164  N N   . VAL   A 1 24  ? -13.532 -3.626  -34.905 1.00 73.23  ? 67  VAL   A N   1 
ATOM   165  C CA  . VAL   A 1 24  ? -12.984 -4.784  -34.138 1.00 71.30  ? 67  VAL   A CA  1 
ATOM   166  C C   . VAL   A 1 24  ? -11.488 -4.534  -33.955 1.00 71.52  ? 67  VAL   A C   1 
ATOM   167  O O   . VAL   A 1 24  ? -10.783 -4.498  -34.956 1.00 73.23  ? 67  VAL   A O   1 
ATOM   168  C CB  . VAL   A 1 24  ? -13.255 -6.122  -34.850 1.00 71.80  ? 67  VAL   A CB  1 
ATOM   169  C CG1 . VAL   A 1 24  ? -12.725 -7.284  -34.047 1.00 70.21  ? 67  VAL   A CG1 1 
ATOM   170  C CG2 . VAL   A 1 24  ? -14.731 -6.327  -35.196 1.00 72.02  ? 67  VAL   A CG2 1 
ATOM   171  N N   . THR   A 1 25  ? -11.024 -4.363  -32.718 1.00 69.73  ? 68  THR   A N   1 
ATOM   172  C CA  . THR   A 1 25  ? -9.645  -3.905  -32.402 1.00 66.52  ? 68  THR   A CA  1 
ATOM   173  C C   . THR   A 1 25  ? -9.286  -4.445  -31.018 1.00 65.18  ? 68  THR   A C   1 
ATOM   174  O O   . THR   A 1 25  ? -10.120 -5.173  -30.470 1.00 63.62  ? 68  THR   A O   1 
ATOM   175  C CB  . THR   A 1 25  ? -9.590  -2.379  -32.560 1.00 68.27  ? 68  THR   A CB  1 
ATOM   176  O OG1 . THR   A 1 25  ? -8.239  -1.936  -32.491 1.00 68.24  ? 68  THR   A OG1 1 
ATOM   177  C CG2 . THR   A 1 25  ? -10.413 -1.630  -31.531 1.00 67.99  ? 68  THR   A CG2 1 
ATOM   178  N N   . GLY   A 1 26  ? -8.120  -4.075  -30.482 1.00 62.00  ? 69  GLY   A N   1 
ATOM   179  C CA  . GLY   A 1 26  ? -7.572  -4.570  -29.218 1.00 62.00  ? 69  GLY   A CA  1 
ATOM   180  C C   . GLY   A 1 26  ? -6.962  -5.959  -29.339 1.00 62.69  ? 69  GLY   A C   1 
ATOM   181  O O   . GLY   A 1 26  ? -7.471  -6.775  -30.108 1.00 65.86  ? 69  GLY   A O   1 
ATOM   182  N N   . ASN   A 1 27  ? -5.941  -6.227  -28.534 1.00 64.19  ? 70  ASN   A N   1 
ATOM   183  C CA  . ASN   A 1 27  ? -5.344  -7.579  -28.327 1.00 66.52  ? 70  ASN   A CA  1 
ATOM   184  C C   . ASN   A 1 27  ? -5.997  -8.259  -27.092 1.00 61.70  ? 70  ASN   A C   1 
ATOM   185  O O   . ASN   A 1 27  ? -7.036  -7.695  -26.573 1.00 58.15  ? 70  ASN   A O   1 
ATOM   186  C CB  . ASN   A 1 27  ? -3.817  -7.432  -28.325 1.00 70.34  ? 70  ASN   A CB  1 
ATOM   187  C CG  . ASN   A 1 27  ? -3.306  -6.627  -27.144 1.00 72.97  ? 70  ASN   A CG  1 
ATOM   188  O OD1 . ASN   A 1 27  ? -3.849  -5.581  -26.799 1.00 75.45  ? 70  ASN   A OD1 1 
ATOM   189  N ND2 . ASN   A 1 27  ? -2.249  -7.102  -26.512 1.00 77.63  ? 70  ASN   A ND2 1 
ATOM   190  N N   . SER   A 1 28  ? -5.495  -9.450  -26.689 1.00 59.19  ? 71  SER   A N   1 
ATOM   191  C CA  . SER   A 1 28  ? -5.985  -10.316 -25.568 1.00 60.03  ? 71  SER   A CA  1 
ATOM   192  C C   . SER   A 1 28  ? -4.830  -10.753 -24.679 1.00 59.60  ? 71  SER   A C   1 
ATOM   193  O O   . SER   A 1 28  ? -4.542  -11.933 -24.616 1.00 61.73  ? 71  SER   A O   1 
ATOM   194  C CB  . SER   A 1 28  ? -6.690  -11.571 -26.039 1.00 60.94  ? 71  SER   A CB  1 
ATOM   195  O OG  . SER   A 1 28  ? -7.613  -11.305 -27.071 1.00 66.46  ? 71  SER   A OG  1 
ATOM   196  N N   . PRO   A 1 29  ? -4.174  -9.857  -23.918 1.00 62.25  ? 72  PRO   A N   1 
ATOM   197  C CA  . PRO   A 1 29  ? -2.995  -10.227 -23.144 1.00 62.65  ? 72  PRO   A CA  1 
ATOM   198  C C   . PRO   A 1 29  ? -3.335  -11.013 -21.872 1.00 60.28  ? 72  PRO   A C   1 
ATOM   199  O O   . PRO   A 1 29  ? -4.343  -10.723 -21.221 1.00 58.12  ? 72  PRO   A O   1 
ATOM   200  C CB  . PRO   A 1 29  ? -2.362  -8.857  -22.839 1.00 65.73  ? 72  PRO   A CB  1 
ATOM   201  C CG  . PRO   A 1 29  ? -3.563  -7.924  -22.692 1.00 64.00  ? 72  PRO   A CG  1 
ATOM   202  C CD  . PRO   A 1 29  ? -4.579  -8.457  -23.691 1.00 64.34  ? 72  PRO   A CD  1 
ATOM   203  N N   . ARG   A 1 30  ? -2.502  -12.001 -21.552 1.00 64.90  ? 73  ARG   A N   1 
ATOM   204  C CA  . ARG   A 1 30  ? -2.574  -12.776 -20.278 1.00 68.43  ? 73  ARG   A CA  1 
ATOM   205  C C   . ARG   A 1 30  ? -1.584  -12.148 -19.286 1.00 64.24  ? 73  ARG   A C   1 
ATOM   206  O O   . ARG   A 1 30  ? -0.397  -12.184 -19.560 1.00 60.55  ? 73  ARG   A O   1 
ATOM   207  C CB  . ARG   A 1 30  ? -2.360  -14.270 -20.548 1.00 74.37  ? 73  ARG   A CB  1 
ATOM   208  C CG  . ARG   A 1 30  ? -3.499  -14.893 -21.354 1.00 80.53  ? 73  ARG   A CG  1 
ATOM   209  C CD  . ARG   A 1 30  ? -3.154  -16.149 -22.159 1.00 88.91  ? 73  ARG   A CD  1 
ATOM   210  N NE  . ARG   A 1 30  ? -4.307  -16.663 -22.925 1.00 91.29  ? 73  ARG   A NE  1 
ATOM   211  C CZ  . ARG   A 1 30  ? -5.011  -17.771 -22.646 1.00 89.13  ? 73  ARG   A CZ  1 
ATOM   212  N NH1 . ARG   A 1 30  ? -4.670  -18.546 -21.624 1.00 91.83  ? 73  ARG   A NH1 1 
ATOM   213  N NH2 . ARG   A 1 30  ? -6.049  -18.109 -23.401 1.00 78.55  ? 73  ARG   A NH2 1 
ATOM   214  N N   . LEU   A 1 31  ? -2.087  -11.494 -18.230 1.00 61.54  ? 74  LEU   A N   1 
ATOM   215  C CA  . LEU   A 1 31  ? -1.268  -10.681 -17.292 1.00 62.10  ? 74  LEU   A CA  1 
ATOM   216  C C   . LEU   A 1 31  ? -1.455  -11.199 -15.856 1.00 59.95  ? 74  LEU   A C   1 
ATOM   217  O O   . LEU   A 1 31  ? -2.606  -11.434 -15.448 1.00 58.52  ? 74  LEU   A O   1 
ATOM   218  C CB  . LEU   A 1 31  ? -1.675  -9.210  -17.428 1.00 64.37  ? 74  LEU   A CB  1 
ATOM   219  C CG  . LEU   A 1 31  ? -1.341  -8.542  -18.767 1.00 64.65  ? 74  LEU   A CG  1 
ATOM   220  C CD1 . LEU   A 1 31  ? -1.878  -7.120  -18.780 1.00 62.98  ? 74  LEU   A CD1 1 
ATOM   221  C CD2 . LEU   A 1 31  ? 0.173   -8.562  -19.056 1.00 64.59  ? 74  LEU   A CD2 1 
ATOM   222  N N   . ASP   A 1 32  ? -0.351  -11.402 -15.138 1.00 57.42  ? 75  ASP   A N   1 
ATOM   223  C CA  . ASP   A 1 32  ? -0.335  -11.648 -13.676 1.00 58.31  ? 75  ASP   A CA  1 
ATOM   224  C C   . ASP   A 1 32  ? -0.499  -10.342 -12.904 1.00 52.56  ? 75  ASP   A C   1 
ATOM   225  O O   . ASP   A 1 32  ? 0.411   -9.476  -12.974 1.00 52.83  ? 75  ASP   A O   1 
ATOM   226  C CB  . ASP   A 1 32  ? 0.995   -12.251 -13.236 1.00 63.65  ? 75  ASP   A CB  1 
ATOM   227  C CG  . ASP   A 1 32  ? 1.153   -13.684 -13.682 1.00 67.43  ? 75  ASP   A CG  1 
ATOM   228  O OD1 . ASP   A 1 32  ? 0.123   -14.416 -13.707 1.00 69.08  ? 75  ASP   A OD1 1 
ATOM   229  O OD2 . ASP   A 1 32  ? 2.296   -14.050 -13.982 1.00 72.58  ? 75  ASP   A OD2 1 
ATOM   230  N N   . VAL   A 1 33  ? -1.572  -10.240 -12.135 1.00 49.42  ? 76  VAL   A N   1 
ATOM   231  C CA  . VAL   A 1 33  ? -1.932  -8.968  -11.443 1.00 51.21  ? 76  VAL   A CA  1 
ATOM   232  C C   . VAL   A 1 33  ? -2.242  -9.270  -9.967  1.00 50.69  ? 76  VAL   A C   1 
ATOM   233  O O   . VAL   A 1 33  ? -2.709  -10.412 -9.625  1.00 49.09  ? 76  VAL   A O   1 
ATOM   234  C CB  . VAL   A 1 33  ? -3.090  -8.220  -12.154 1.00 49.59  ? 76  VAL   A CB  1 
ATOM   235  C CG1 . VAL   A 1 33  ? -2.909  -8.114  -13.640 1.00 51.13  ? 76  VAL   A CG1 1 
ATOM   236  C CG2 . VAL   A 1 33  ? -4.432  -8.860  -11.874 1.00 49.54  ? 76  VAL   A CG2 1 
ATOM   237  N N   . ALA   A 1 34  ? -2.011  -8.273  -9.112  1.00 50.40  ? 77  ALA   A N   1 
ATOM   238  C CA  . ALA   A 1 34  ? -2.414  -8.256  -7.685  1.00 49.89  ? 77  ALA   A CA  1 
ATOM   239  C C   . ALA   A 1 34  ? -3.503  -7.185  -7.513  1.00 47.81  ? 77  ALA   A C   1 
ATOM   240  O O   . ALA   A 1 34  ? -3.476  -6.229  -8.260  1.00 48.03  ? 77  ALA   A O   1 
ATOM   241  C CB  . ALA   A 1 34  ? -1.213  -7.984  -6.811  1.00 49.18  ? 77  ALA   A CB  1 
ATOM   242  N N   . LEU   A 1 35  ? -4.450  -7.394  -6.613  1.00 47.15  ? 78  LEU   A N   1 
ATOM   243  C CA  . LEU   A 1 35  ? -5.520  -6.423  -6.261  1.00 47.92  ? 78  LEU   A CA  1 
ATOM   244  C C   . LEU   A 1 35  ? -5.350  -6.062  -4.773  1.00 49.65  ? 78  LEU   A C   1 
ATOM   245  O O   . LEU   A 1 35  ? -5.477  -6.987  -3.886  1.00 50.17  ? 78  LEU   A O   1 
ATOM   246  C CB  . LEU   A 1 35  ? -6.883  -7.058  -6.562  1.00 47.38  ? 78  LEU   A CB  1 
ATOM   247  C CG  . LEU   A 1 35  ? -8.119  -6.219  -6.201  1.00 46.88  ? 78  LEU   A CG  1 
ATOM   248  C CD1 . LEU   A 1 35  ? -8.130  -4.911  -6.961  1.00 46.50  ? 78  LEU   A CD1 1 
ATOM   249  C CD2 . LEU   A 1 35  ? -9.410  -6.986  -6.463  1.00 45.15  ? 78  LEU   A CD2 1 
ATOM   250  N N   . ASP   A 1 36  ? -4.956  -4.819  -4.496  1.00 47.30  ? 79  ASP   A N   1 
ATOM   251  C CA  . ASP   A 1 36  ? -4.719  -4.319  -3.116  1.00 47.78  ? 79  ASP   A CA  1 
ATOM   252  C C   . ASP   A 1 36  ? -6.057  -3.917  -2.450  1.00 46.64  ? 79  ASP   A C   1 
ATOM   253  O O   . ASP   A 1 36  ? -7.112  -3.985  -3.126  1.00 45.48  ? 79  ASP   A O   1 
ATOM   254  C CB  . ASP   A 1 36  ? -3.659  -3.210  -3.102  1.00 49.25  ? 79  ASP   A CB  1 
ATOM   255  C CG  . ASP   A 1 36  ? -4.091  -1.824  -3.562  1.00 50.74  ? 79  ASP   A CG  1 
ATOM   256  O OD1 . ASP   A 1 36  ? -5.282  -1.617  -3.833  1.00 51.57  ? 79  ASP   A OD1 1 
ATOM   257  O OD2 . ASP   A 1 36  ? -3.215  -0.955  -3.638  1.00 56.57  ? 79  ASP   A OD2 1 
ATOM   258  N N   . GLU   A 1 37  ? -5.995  -3.513  -1.172  1.00 47.59  ? 80  GLU   A N   1 
ATOM   259  C CA  . GLU   A 1 37  ? -7.175  -3.208  -0.336  1.00 47.48  ? 80  GLU   A CA  1 
ATOM   260  C C   . GLU   A 1 37  ? -7.859  -1.916  -0.830  1.00 45.16  ? 80  GLU   A C   1 
ATOM   261  O O   . GLU   A 1 37  ? -9.087  -1.822  -0.641  1.00 42.42  ? 80  GLU   A O   1 
ATOM   262  C CB  . GLU   A 1 37  ? -6.743  -3.170  1.128   1.00 51.17  ? 80  GLU   A CB  1 
ATOM   263  C CG  . GLU   A 1 37  ? -7.920  -3.217  2.076   1.00 54.49  ? 80  GLU   A CG  1 
ATOM   264  C CD  . GLU   A 1 37  ? -7.569  -3.115  3.553   1.00 57.54  ? 80  GLU   A CD  1 
ATOM   265  O OE1 . GLU   A 1 37  ? -7.277  -1.995  4.037   1.00 57.45  ? 80  GLU   A OE1 1 
ATOM   266  O OE2 . GLU   A 1 37  ? -7.572  -4.166  4.211   1.00 61.28  ? 80  GLU   A OE2 1 
ATOM   267  N N   . SER   A 1 38  ? -7.119  -1.000  -1.477  1.00 44.88  ? 81  SER   A N   1 
ATOM   268  C CA  . SER   A 1 38  ? -7.622  0.252   -2.098  1.00 45.53  ? 81  SER   A CA  1 
ATOM   269  C C   . SER   A 1 38  ? -8.285  -0.021  -3.441  1.00 44.41  ? 81  SER   A C   1 
ATOM   270  O O   . SER   A 1 38  ? -8.688  0.954   -4.047  1.00 46.24  ? 81  SER   A O   1 
ATOM   271  C CB  . SER   A 1 38  ? -6.535  1.271   -2.310  1.00 49.12  ? 81  SER   A CB  1 
ATOM   272  O OG  . SER   A 1 38  ? -5.969  1.680   -1.082  1.00 54.31  ? 81  SER   A OG  1 
ATOM   273  N N   . GLY   A 1 39  ? -8.346  -1.267  -3.931  1.00 44.91  ? 82  GLY   A N   1 
ATOM   274  C CA  . GLY   A 1 39  ? -8.929  -1.566  -5.264  1.00 44.49  ? 82  GLY   A CA  1 
ATOM   275  C C   . GLY   A 1 39  ? -8.046  -1.160  -6.453  1.00 43.66  ? 82  GLY   A C   1 
ATOM   276  O O   . GLY   A 1 39  ? -8.571  -1.024  -7.552  1.00 41.17  ? 82  GLY   A O   1 
ATOM   277  N N   . ASP   A 1 40  ? -6.740  -1.013  -6.273  1.00 46.44  ? 83  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 40  ? -5.760  -0.760  -7.359  1.00 49.83  ? 83  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 40  ? -5.159  -2.101  -7.793  1.00 48.22  ? 83  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 40  ? -4.559  -2.773  -6.957  1.00 48.44  ? 83  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 40  ? -4.718  0.273   -6.916  1.00 53.22  ? 83  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 40  ? -5.334  1.631   -6.622  1.00 57.92  ? 83  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 40  ? -6.371  1.971   -7.250  1.00 63.46  ? 83  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 40  ? -4.780  2.341   -5.790  1.00 65.38  ? 83  ASP   A OD2 1 
ATOM   285  N N   . PHE   A 1 41  ? -5.325  -2.479  -9.056  1.00 49.50  ? 84  PHE   A N   1 
ATOM   286  C CA  . PHE   A 1 41  ? -4.569  -3.597  -9.690  1.00 48.75  ? 84  PHE   A CA  1 
ATOM   287  C C   . PHE   A 1 41  ? -3.096  -3.228  -9.867  1.00 52.20  ? 84  PHE   A C   1 
ATOM   288  O O   . PHE   A 1 41  ? -2.789  -2.051  -10.000 1.00 56.07  ? 84  PHE   A O   1 
ATOM   289  C CB  . PHE   A 1 41  ? -5.204  -3.982  -11.013 1.00 45.69  ? 84  PHE   A CB  1 
ATOM   290  C CG  . PHE   A 1 41  ? -6.500  -4.735  -10.884 1.00 44.55  ? 84  PHE   A CG  1 
ATOM   291  C CD1 . PHE   A 1 41  ? -6.503  -6.033  -10.413 1.00 43.08  ? 84  PHE   A CD1 1 
ATOM   292  C CD2 . PHE   A 1 41  ? -7.711  -4.170  -11.274 1.00 43.80  ? 84  PHE   A CD2 1 
ATOM   293  C CE1 . PHE   A 1 41  ? -7.692  -6.740  -10.330 1.00 44.36  ? 84  PHE   A CE1 1 
ATOM   294  C CE2 . PHE   A 1 41  ? -8.896  -4.876  -11.170 1.00 41.57  ? 84  PHE   A CE2 1 
ATOM   295  C CZ  . PHE   A 1 41  ? -8.883  -6.177  -10.746 1.00 42.16  ? 84  PHE   A CZ  1 
ATOM   296  N N   . SER   A 1 42  ? -2.201  -4.215  -9.878  1.00 52.06  ? 85  SER   A N   1 
ATOM   297  C CA  . SER   A 1 42  ? -0.772  -4.019  -10.211 1.00 54.08  ? 85  SER   A CA  1 
ATOM   298  C C   . SER   A 1 42  ? -0.209  -5.286  -10.857 1.00 55.44  ? 85  SER   A C   1 
ATOM   299  O O   . SER   A 1 42  ? -0.771  -6.386  -10.635 1.00 52.31  ? 85  SER   A O   1 
ATOM   300  C CB  . SER   A 1 42  ? 0.006   -3.635  -8.997  1.00 56.66  ? 85  SER   A CB  1 
ATOM   301  O OG  . SER   A 1 42  ? -0.095  -4.636  -7.990  1.00 55.78  ? 85  SER   A OG  1 
ATOM   302  N N   . LEU   A 1 43  ? 0.837   -5.119  -11.667 1.00 61.07  ? 86  LEU   A N   1 
ATOM   303  C CA  . LEU   A 1 43  ? 1.525   -6.240  -12.350 1.00 62.98  ? 86  LEU   A CA  1 
ATOM   304  C C   . LEU   A 1 43  ? 2.454   -6.914  -11.347 1.00 65.26  ? 86  LEU   A C   1 
ATOM   305  O O   . LEU   A 1 43  ? 3.347   -6.238  -10.830 1.00 65.12  ? 86  LEU   A O   1 
ATOM   306  C CB  . LEU   A 1 43  ? 2.274   -5.685  -13.559 1.00 65.85  ? 86  LEU   A CB  1 
ATOM   307  C CG  . LEU   A 1 43  ? 1.332   -5.182  -14.648 1.00 67.56  ? 86  LEU   A CG  1 
ATOM   308  C CD1 . LEU   A 1 43  ? 2.011   -4.167  -15.546 1.00 71.28  ? 86  LEU   A CD1 1 
ATOM   309  C CD2 . LEU   A 1 43  ? 0.770   -6.341  -15.461 1.00 67.96  ? 86  LEU   A CD2 1 
ATOM   310  N N   . VAL   A 1 44  ? 2.181   -8.179  -11.052 1.00 67.55  ? 87  VAL   A N   1 
ATOM   311  C CA  . VAL   A 1 44  ? 3.110   -9.144  -10.393 1.00 72.67  ? 87  VAL   A CA  1 
ATOM   312  C C   . VAL   A 1 44  ? 4.058   -9.676  -11.475 1.00 80.34  ? 87  VAL   A C   1 
ATOM   313  O O   . VAL   A 1 44  ? 3.569   -10.362 -12.389 1.00 86.13  ? 87  VAL   A O   1 
ATOM   314  C CB  . VAL   A 1 44  ? 2.299   -10.301 -9.781  1.00 70.02  ? 87  VAL   A CB  1 
ATOM   315  C CG1 . VAL   A 1 44  ? 3.195   -11.436 -9.284  1.00 69.71  ? 87  VAL   A CG1 1 
ATOM   316  C CG2 . VAL   A 1 44  ? 1.350   -9.800  -8.702  1.00 67.26  ? 87  VAL   A CG2 1 
ATOM   317  N N   . GLU   A 1 45  ? 5.344   -9.364  -11.433 1.00 88.49  ? 88  GLU   A N   1 
ATOM   318  C CA  . GLU   A 1 45  ? 6.289   -9.904  -12.453 1.00 99.00  ? 88  GLU   A CA  1 
ATOM   319  C C   . GLU   A 1 45  ? 7.201   -10.956 -11.803 1.00 100.95 ? 88  GLU   A C   1 
ATOM   320  O O   . GLU   A 1 45  ? 6.729   -11.994 -11.314 1.00 97.34  ? 88  GLU   A O   1 
ATOM   321  C CB  . GLU   A 1 45  ? 7.053   -8.760  -13.121 1.00 105.28 ? 88  GLU   A CB  1 
ATOM   322  C CG  . GLU   A 1 45  ? 6.220   -7.952  -14.112 1.00 107.39 ? 88  GLU   A CG  1 
ATOM   323  C CD  . GLU   A 1 45  ? 5.956   -8.654  -15.431 1.00 108.15 ? 88  GLU   A CD  1 
ATOM   324  O OE1 . GLU   A 1 45  ? 5.261   -9.680  -15.399 1.00 109.31 ? 88  GLU   A OE1 1 
ATOM   325  O OE2 . GLU   A 1 45  ? 6.457   -8.183  -16.481 1.00 111.82 ? 88  GLU   A OE2 1 
ATOM   326  N N   . GLY   B 2 7   ? -36.833 12.341  -11.963 1.00 78.43  ? 16  GLY   B N   1 
ATOM   327  C CA  . GLY   B 2 7   ? -35.535 12.017  -12.682 1.00 79.26  ? 16  GLY   B CA  1 
ATOM   328  C C   . GLY   B 2 7   ? -35.709 11.002  -13.819 1.00 76.72  ? 16  GLY   B C   1 
ATOM   329  O O   . GLY   B 2 7   ? -36.663 10.180  -13.761 1.00 77.71  ? 16  GLY   B O   1 
ATOM   330  N N   . GLU   B 2 8   ? -34.815 11.041  -14.818 1.00 68.35  ? 17  GLU   B N   1 
ATOM   331  C CA  . GLU   B 2 8   ? -34.770 10.084  -15.963 1.00 64.13  ? 17  GLU   B CA  1 
ATOM   332  C C   . GLU   B 2 8   ? -34.331 8.702   -15.456 1.00 60.33  ? 17  GLU   B C   1 
ATOM   333  O O   . GLU   B 2 8   ? -33.206 8.550   -15.021 1.00 57.52  ? 17  GLU   B O   1 
ATOM   334  C CB  . GLU   B 2 8   ? -33.810 10.574  -17.054 1.00 62.85  ? 17  GLU   B CB  1 
ATOM   335  C CG  . GLU   B 2 8   ? -33.902 9.755   -18.328 1.00 62.42  ? 17  GLU   B CG  1 
ATOM   336  C CD  . GLU   B 2 8   ? -33.167 10.319  -19.538 1.00 64.72  ? 17  GLU   B CD  1 
ATOM   337  O OE1 . GLU   B 2 8   ? -32.243 11.172  -19.363 1.00 59.08  ? 17  GLU   B OE1 1 
ATOM   338  O OE2 . GLU   B 2 8   ? -33.554 9.931   -20.676 1.00 70.58  ? 17  GLU   B OE2 1 
ATOM   339  N N   A THR   B 2 9   ? -35.222 7.712   -15.515 0.25 60.88  ? 18  THR   B N   1 
ATOM   340  N N   B THR   B 2 9   ? -35.244 7.731   -15.538 0.25 60.38  ? 18  THR   B N   1 
ATOM   341  N N   C THR   B 2 9   ? -35.222 7.712   -15.515 0.25 60.88  ? 18  THR   B N   1 
ATOM   342  N N   D THR   B 2 9   ? -35.244 7.731   -15.538 0.25 60.38  ? 18  THR   B N   1 
ATOM   343  C CA  A THR   B 2 9   ? -34.975 6.347   -14.981 0.25 61.11  ? 18  THR   B CA  1 
ATOM   344  C CA  B THR   B 2 9   ? -35.107 6.363   -14.974 0.25 60.26  ? 18  THR   B CA  1 
ATOM   345  C CA  C THR   B 2 9   ? -34.975 6.347   -14.981 0.25 61.11  ? 18  THR   B CA  1 
ATOM   346  C CA  D THR   B 2 9   ? -35.107 6.363   -14.974 0.25 60.26  ? 18  THR   B CA  1 
ATOM   347  C C   A THR   B 2 9   ? -34.974 5.312   -16.109 0.25 60.05  ? 18  THR   B C   1 
ATOM   348  C C   B THR   B 2 9   ? -34.926 5.335   -16.100 0.25 59.56  ? 18  THR   B C   1 
ATOM   349  C C   C THR   B 2 9   ? -34.974 5.312   -16.109 0.25 60.05  ? 18  THR   B C   1 
ATOM   350  C C   D THR   B 2 9   ? -34.926 5.335   -16.100 0.25 59.56  ? 18  THR   B C   1 
ATOM   351  O O   A THR   B 2 9   ? -34.883 4.112   -15.785 0.25 61.66  ? 18  THR   B O   1 
ATOM   352  O O   B THR   B 2 9   ? -34.624 4.171   -15.769 0.25 61.03  ? 18  THR   B O   1 
ATOM   353  O O   C THR   B 2 9   ? -34.883 4.112   -15.785 0.25 61.66  ? 18  THR   B O   1 
ATOM   354  O O   D THR   B 2 9   ? -34.624 4.171   -15.769 0.25 61.03  ? 18  THR   B O   1 
ATOM   355  C CB  A THR   B 2 9   ? -36.018 5.969   -13.924 0.25 62.19  ? 18  THR   B CB  1 
ATOM   356  C CB  B THR   B 2 9   ? -36.314 6.041   -14.082 0.25 60.75  ? 18  THR   B CB  1 
ATOM   357  C CB  C THR   B 2 9   ? -36.018 5.969   -13.924 0.25 62.19  ? 18  THR   B CB  1 
ATOM   358  C CB  D THR   B 2 9   ? -36.314 6.041   -14.082 0.25 60.75  ? 18  THR   B CB  1 
ATOM   359  O OG1 A THR   B 2 9   ? -36.356 7.160   -13.213 0.25 63.22  ? 18  THR   B OG1 1 
ATOM   360  O OG1 B THR   B 2 9   ? -37.511 6.335   -14.801 0.25 59.96  ? 18  THR   B OG1 1 
ATOM   361  O OG1 C THR   B 2 9   ? -36.356 7.160   -13.213 0.25 63.22  ? 18  THR   B OG1 1 
ATOM   362  O OG1 D THR   B 2 9   ? -37.511 6.335   -14.801 0.25 59.96  ? 18  THR   B OG1 1 
ATOM   363  C CG2 A THR   B 2 9   ? -35.520 4.885   -12.993 0.25 62.07  ? 18  THR   B CG2 1 
ATOM   364  C CG2 B THR   B 2 9   ? -36.320 6.831   -12.792 0.25 61.48  ? 18  THR   B CG2 1 
ATOM   365  C CG2 C THR   B 2 9   ? -35.520 4.885   -12.993 0.25 62.07  ? 18  THR   B CG2 1 
ATOM   366  C CG2 D THR   B 2 9   ? -36.320 6.831   -12.792 0.25 61.48  ? 18  THR   B CG2 1 
ATOM   367  N N   . THR   B 2 10  ? -35.066 5.750   -17.368 1.00 58.30  ? 19  THR   B N   1 
ATOM   368  C CA  . THR   B 2 10  ? -35.022 4.847   -18.547 1.00 54.95  ? 19  THR   B CA  1 
ATOM   369  C C   . THR   B 2 10  ? -33.712 4.041   -18.549 1.00 48.10  ? 19  THR   B C   1 
ATOM   370  O O   . THR   B 2 10  ? -32.650 4.639   -18.385 1.00 45.52  ? 19  THR   B O   1 
ATOM   371  C CB  . THR   B 2 10  ? -35.166 5.619   -19.874 1.00 57.53  ? 19  THR   B CB  1 
ATOM   372  O OG1 . THR   B 2 10  ? -36.090 6.704   -19.778 1.00 65.75  ? 19  THR   B OG1 1 
ATOM   373  C CG2 . THR   B 2 10  ? -35.659 4.733   -20.994 1.00 57.84  ? 19  THR   B CG2 1 
ATOM   374  N N   . ASP   B 2 11  ? -33.789 2.741   -18.795 1.00 44.78  ? 20  ASP   B N   1 
ATOM   375  C CA  . ASP   B 2 11  ? -32.594 1.901   -19.033 1.00 45.78  ? 20  ASP   B CA  1 
ATOM   376  C C   . ASP   B 2 11  ? -31.675 2.554   -20.074 1.00 47.57  ? 20  ASP   B C   1 
ATOM   377  O O   . ASP   B 2 11  ? -32.178 3.310   -20.941 1.00 50.59  ? 20  ASP   B O   1 
ATOM   378  C CB  . ASP   B 2 11  ? -33.006 0.508   -19.469 1.00 48.40  ? 20  ASP   B CB  1 
ATOM   379  C CG  . ASP   B 2 11  ? -33.549 -0.372  -18.353 1.00 50.94  ? 20  ASP   B CG  1 
ATOM   380  O OD1 . ASP   B 2 11  ? -33.626 0.108   -17.214 1.00 47.16  ? 20  ASP   B OD1 1 
ATOM   381  O OD2 . ASP   B 2 11  ? -33.917 -1.539  -18.662 1.00 56.91  ? 20  ASP   B OD2 1 
ATOM   382  N N   . GLY   B 2 12  ? -30.369 2.290   -19.990 1.00 44.51  ? 21  GLY   B N   1 
ATOM   383  C CA  . GLY   B 2 12  ? -29.368 2.749   -20.963 1.00 42.81  ? 21  GLY   B CA  1 
ATOM   384  C C   . GLY   B 2 12  ? -28.090 3.179   -20.295 1.00 39.53  ? 21  GLY   B C   1 
ATOM   385  O O   . GLY   B 2 12  ? -27.984 2.989   -19.088 1.00 38.18  ? 21  GLY   B O   1 
ATOM   386  N N   . VAL   B 2 13  ? -27.168 3.749   -21.069 1.00 38.77  ? 22  VAL   B N   1 
ATOM   387  C CA  . VAL   B 2 13  ? -25.831 4.222   -20.618 1.00 37.88  ? 22  VAL   B CA  1 
ATOM   388  C C   . VAL   B 2 13  ? -25.906 5.728   -20.406 1.00 39.13  ? 22  VAL   B C   1 
ATOM   389  O O   . VAL   B 2 13  ? -26.671 6.407   -21.124 1.00 39.67  ? 22  VAL   B O   1 
ATOM   390  C CB  . VAL   B 2 13  ? -24.713 3.759   -21.560 1.00 39.12  ? 22  VAL   B CB  1 
ATOM   391  C CG1 . VAL   B 2 13  ? -24.842 4.289   -23.012 1.00 40.47  ? 22  VAL   B CG1 1 
ATOM   392  C CG2 . VAL   B 2 13  ? -23.329 4.055   -20.990 1.00 39.32  ? 22  VAL   B CG2 1 
ATOM   393  N N   . TYR   B 2 14  ? -25.189 6.236   -19.413 1.00 38.73  ? 23  TYR   B N   1 
ATOM   394  C CA  . TYR   B 2 14  ? -25.256 7.666   -19.033 1.00 38.84  ? 23  TYR   B CA  1 
ATOM   395  C C   . TYR   B 2 14  ? -23.855 8.159   -18.792 1.00 39.44  ? 23  TYR   B C   1 
ATOM   396  O O   . TYR   B 2 14  ? -22.998 7.370   -18.319 1.00 38.99  ? 23  TYR   B O   1 
ATOM   397  C CB  . TYR   B 2 14  ? -26.057 7.899   -17.759 1.00 39.44  ? 23  TYR   B CB  1 
ATOM   398  C CG  . TYR   B 2 14  ? -27.520 7.654   -17.895 1.00 37.91  ? 23  TYR   B CG  1 
ATOM   399  C CD1 . TYR   B 2 14  ? -28.015 6.413   -18.210 1.00 37.48  ? 23  TYR   B CD1 1 
ATOM   400  C CD2 . TYR   B 2 14  ? -28.404 8.706   -17.723 1.00 39.29  ? 23  TYR   B CD2 1 
ATOM   401  C CE1 . TYR   B 2 14  ? -29.377 6.198   -18.344 1.00 37.91  ? 23  TYR   B CE1 1 
ATOM   402  C CE2 . TYR   B 2 14  ? -29.773 8.512   -17.856 1.00 39.55  ? 23  TYR   B CE2 1 
ATOM   403  C CZ  . TYR   B 2 14  ? -30.258 7.253   -18.145 1.00 42.14  ? 23  TYR   B CZ  1 
ATOM   404  O OH  . TYR   B 2 14  ? -31.610 7.095   -18.274 1.00 42.35  ? 23  TYR   B OH  1 
ATOM   405  N N   . ARG   B 2 15  ? -23.674 9.435   -19.085 1.00 39.89  ? 24  ARG   B N   1 
ATOM   406  C CA  . ARG   B 2 15  ? -22.470 10.203  -18.718 1.00 40.55  ? 24  ARG   B CA  1 
ATOM   407  C C   . ARG   B 2 15  ? -22.627 10.667  -17.266 1.00 41.75  ? 24  ARG   B C   1 
ATOM   408  O O   . ARG   B 2 15  ? -23.728 11.097  -16.898 1.00 37.74  ? 24  ARG   B O   1 
ATOM   409  C CB  . ARG   B 2 15  ? -22.277 11.395  -19.668 1.00 42.16  ? 24  ARG   B CB  1 
ATOM   410  C CG  . ARG   B 2 15  ? -22.255 11.077  -21.161 1.00 43.26  ? 24  ARG   B CG  1 
ATOM   411  C CD  . ARG   B 2 15  ? -22.143 12.354  -22.001 1.00 44.90  ? 24  ARG   B CD  1 
ATOM   412  N NE  . ARG   B 2 15  ? -22.269 12.062  -23.438 1.00 45.63  ? 24  ARG   B NE  1 
ATOM   413  C CZ  . ARG   B 2 15  ? -21.265 11.747  -24.266 1.00 47.45  ? 24  ARG   B CZ  1 
ATOM   414  N NH1 . ARG   B 2 15  ? -20.012 11.758  -23.843 1.00 45.21  ? 24  ARG   B NH1 1 
ATOM   415  N NH2 . ARG   B 2 15  ? -21.529 11.390  -25.518 1.00 50.35  ? 24  ARG   B NH2 1 
ATOM   416  N N   . VAL   B 2 16  ? -21.533 10.640  -16.511 1.00 41.14  ? 25  VAL   B N   1 
ATOM   417  C CA  . VAL   B 2 16  ? -21.407 11.266  -15.181 1.00 43.65  ? 25  VAL   B CA  1 
ATOM   418  C C   . VAL   B 2 16  ? -20.523 12.509  -15.318 1.00 42.79  ? 25  VAL   B C   1 
ATOM   419  O O   . VAL   B 2 16  ? -19.365 12.384  -15.636 1.00 44.92  ? 25  VAL   B O   1 
ATOM   420  C CB  . VAL   B 2 16  ? -20.866 10.246  -14.146 1.00 45.69  ? 25  VAL   B CB  1 
ATOM   421  C CG1 . VAL   B 2 16  ? -20.832 10.877  -12.754 1.00 45.67  ? 25  VAL   B CG1 1 
ATOM   422  C CG2 . VAL   B 2 16  ? -21.669 8.935   -14.137 1.00 44.33  ? 25  VAL   B CG2 1 
ATOM   423  N N   . MET   B 2 17  ? -21.086 13.657  -14.979 1.00 45.47  ? 26  MET   B N   1 
ATOM   424  C CA  . MET   B 2 17  ? -20.566 15.023  -15.197 1.00 46.67  ? 26  MET   B CA  1 
ATOM   425  C C   . MET   B 2 17  ? -20.448 15.746  -13.850 1.00 46.36  ? 26  MET   B C   1 
ATOM   426  O O   . MET   B 2 17  ? -21.294 15.496  -12.974 1.00 44.43  ? 26  MET   B O   1 
ATOM   427  C CB  . MET   B 2 17  ? -21.566 15.814  -16.046 1.00 47.63  ? 26  MET   B CB  1 
ATOM   428  C CG  . MET   B 2 17  ? -22.006 15.104  -17.336 1.00 49.08  ? 26  MET   B CG  1 
ATOM   429  S SD  . MET   B 2 17  ? -20.718 14.905  -18.618 1.00 50.34  ? 26  MET   B SD  1 
ATOM   430  C CE  . MET   B 2 17  ? -20.219 16.613  -18.835 1.00 52.56  ? 26  MET   B CE  1 
ATOM   431  N N   . THR   B 2 18  ? -19.511 16.683  -13.766 1.00 48.38  ? 27  THR   B N   1 
ATOM   432  C CA  . THR   B 2 18  ? -19.354 17.683  -12.693 1.00 53.81  ? 27  THR   B CA  1 
ATOM   433  C C   . THR   B 2 18  ? -19.206 19.083  -13.322 1.00 57.64  ? 27  THR   B C   1 
ATOM   434  O O   . THR   B 2 18  ? -18.616 19.179  -14.438 1.00 52.03  ? 27  THR   B O   1 
ATOM   435  C CB  . THR   B 2 18  ? -18.184 17.285  -11.779 1.00 53.87  ? 27  THR   B CB  1 
ATOM   436  O OG1 . THR   B 2 18  ? -18.165 18.261  -10.726 1.00 55.45  ? 27  THR   B OG1 1 
ATOM   437  C CG2 . THR   B 2 18  ? -16.846 17.198  -12.491 1.00 53.62  ? 27  THR   B CG2 1 
ATOM   438  N N   . ARG   B 2 19  ? -19.704 20.121  -12.625 1.00 61.25  ? 28  ARG   B N   1 
ATOM   439  C CA  . ARG   B 2 19  ? -19.361 21.553  -12.862 1.00 67.71  ? 28  ARG   B CA  1 
ATOM   440  C C   . ARG   B 2 19  ? -18.414 22.110  -11.776 1.00 66.95  ? 28  ARG   B C   1 
ATOM   441  O O   . ARG   B 2 19  ? -18.205 23.329  -11.755 1.00 69.86  ? 28  ARG   B O   1 
ATOM   442  C CB  . ARG   B 2 19  ? -20.643 22.389  -12.959 1.00 69.76  ? 28  ARG   B CB  1 
ATOM   443  C CG  . ARG   B 2 19  ? -21.587 21.901  -14.049 1.00 74.09  ? 28  ARG   B CG  1 
ATOM   444  C CD  . ARG   B 2 19  ? -22.259 22.990  -14.861 1.00 74.85  ? 28  ARG   B CD  1 
ATOM   445  N NE  . ARG   B 2 19  ? -23.404 22.492  -15.612 1.00 76.99  ? 28  ARG   B NE  1 
ATOM   446  C CZ  . ARG   B 2 19  ? -24.593 22.194  -15.092 1.00 83.99  ? 28  ARG   B CZ  1 
ATOM   447  N NH1 . ARG   B 2 19  ? -24.821 22.325  -13.791 1.00 88.93  ? 28  ARG   B NH1 1 
ATOM   448  N NH2 . ARG   B 2 19  ? -25.556 21.738  -15.875 1.00 84.90  ? 28  ARG   B NH2 1 
ATOM   449  N N   . ARG   B 2 20  ? -17.792 21.265  -10.960 1.00 69.51  ? 29  ARG   B N   1 
ATOM   450  C CA  . ARG   B 2 20  ? -16.901 21.681  -9.836  1.00 77.71  ? 29  ARG   B CA  1 
ATOM   451  C C   . ARG   B 2 20  ? -15.518 22.081  -10.390 1.00 77.76  ? 29  ARG   B C   1 
ATOM   452  O O   . ARG   B 2 20  ? -14.669 22.561  -9.611  1.00 79.68  ? 29  ARG   B O   1 
ATOM   453  C CB  . ARG   B 2 20  ? -16.813 20.536  -8.815  1.00 81.33  ? 29  ARG   B CB  1 
ATOM   454  C CG  . ARG   B 2 20  ? -16.433 20.941  -7.398  1.00 88.13  ? 29  ARG   B CG  1 
ATOM   455  C CD  . ARG   B 2 20  ? -16.031 19.728  -6.562  1.00 99.45  ? 29  ARG   B CD  1 
ATOM   456  N NE  . ARG   B 2 20  ? -14.988 18.908  -7.194  1.00 106.62 ? 29  ARG   B NE  1 
ATOM   457  C CZ  . ARG   B 2 20  ? -13.703 18.814  -6.815  1.00 112.29 ? 29  ARG   B CZ  1 
ATOM   458  N NH1 . ARG   B 2 20  ? -13.240 19.483  -5.770  1.00 115.57 ? 29  ARG   B NH1 1 
ATOM   459  N NH2 . ARG   B 2 20  ? -12.874 18.040  -7.497  1.00 111.17 ? 29  ARG   B NH2 1 
ATOM   460  N N   . LEU   B 2 21  ? -15.269 21.839  -11.678 1.00 74.22  ? 30  LEU   B N   1 
ATOM   461  C CA  . LEU   B 2 21  ? -14.004 22.193  -12.376 1.00 70.80  ? 30  LEU   B CA  1 
ATOM   462  C C   . LEU   B 2 21  ? -14.337 23.218  -13.466 1.00 66.83  ? 30  LEU   B C   1 
ATOM   463  O O   . LEU   B 2 21  ? -15.447 23.797  -13.402 1.00 65.06  ? 30  LEU   B O   1 
ATOM   464  C CB  . LEU   B 2 21  ? -13.384 20.908  -12.925 1.00 70.89  ? 30  LEU   B CB  1 
ATOM   465  C CG  . LEU   B 2 21  ? -12.288 20.279  -12.075 1.00 73.76  ? 30  LEU   B CG  1 
ATOM   466  C CD1 . LEU   B 2 21  ? -12.573 20.428  -10.593 1.00 75.01  ? 30  LEU   B CD1 1 
ATOM   467  C CD2 . LEU   B 2 21  ? -12.090 18.812  -12.442 1.00 74.07  ? 30  LEU   B CD2 1 
ATOM   468  N N   . LEU   B 2 22  ? -13.420 23.460  -14.410 1.00 67.07  ? 31  LEU   B N   1 
ATOM   469  C CA  . LEU   B 2 22  ? -13.672 24.355  -15.573 1.00 64.10  ? 31  LEU   B CA  1 
ATOM   470  C C   . LEU   B 2 22  ? -14.794 23.762  -16.427 1.00 63.32  ? 31  LEU   B C   1 
ATOM   471  O O   . LEU   B 2 22  ? -14.780 22.536  -16.589 1.00 67.95  ? 31  LEU   B O   1 
ATOM   472  C CB  . LEU   B 2 22  ? -12.388 24.483  -16.376 1.00 63.09  ? 31  LEU   B CB  1 
ATOM   473  C CG  . LEU   B 2 22  ? -12.394 25.647  -17.358 1.00 63.47  ? 31  LEU   B CG  1 
ATOM   474  C CD1 . LEU   B 2 22  ? -12.198 26.975  -16.639 1.00 61.84  ? 31  LEU   B CD1 1 
ATOM   475  C CD2 . LEU   B 2 22  ? -11.334 25.425  -18.434 1.00 63.06  ? 31  LEU   B CD2 1 
ATOM   476  N N   . GLY   B 2 23  ? -15.730 24.572  -16.943 1.00 60.25  ? 32  GLY   B N   1 
ATOM   477  C CA  . GLY   B 2 23  ? -16.871 24.080  -17.751 1.00 57.22  ? 32  GLY   B CA  1 
ATOM   478  C C   . GLY   B 2 23  ? -17.593 22.870  -17.122 1.00 55.39  ? 32  GLY   B C   1 
ATOM   479  O O   . GLY   B 2 23  ? -17.568 22.693  -15.890 1.00 55.26  ? 32  GLY   B O   1 
ATOM   480  N N   . SER   B 2 24  ? -18.298 22.091  -17.937 1.00 54.08  ? 33  SER   B N   1 
ATOM   481  C CA  . SER   B 2 24  ? -18.888 20.786  -17.557 1.00 52.13  ? 33  SER   B CA  1 
ATOM   482  C C   . SER   B 2 24  ? -17.865 19.700  -17.902 1.00 51.29  ? 33  SER   B C   1 
ATOM   483  O O   . SER   B 2 24  ? -17.468 19.672  -19.052 1.00 48.66  ? 33  SER   B O   1 
ATOM   484  C CB  . SER   B 2 24  ? -20.178 20.605  -18.255 1.00 52.08  ? 33  SER   B CB  1 
ATOM   485  O OG  . SER   B 2 24  ? -21.078 21.643  -17.851 1.00 55.49  ? 33  SER   B OG  1 
ATOM   486  N N   . THR   B 2 25  ? -17.421 18.891  -16.932 1.00 49.40  ? 34  THR   B N   1 
ATOM   487  C CA  . THR   B 2 25  ? -16.337 17.887  -17.120 1.00 49.09  ? 34  THR   B CA  1 
ATOM   488  C C   . THR   B 2 25  ? -16.903 16.485  -16.915 1.00 49.01  ? 34  THR   B C   1 
ATOM   489  O O   . THR   B 2 25  ? -17.649 16.293  -15.928 1.00 49.37  ? 34  THR   B O   1 
ATOM   490  C CB  . THR   B 2 25  ? -15.139 18.123  -16.193 1.00 51.35  ? 34  THR   B CB  1 
ATOM   491  O OG1 . THR   B 2 25  ? -14.644 19.445  -16.433 1.00 54.09  ? 34  THR   B OG1 1 
ATOM   492  C CG2 . THR   B 2 25  ? -14.013 17.131  -16.421 1.00 51.46  ? 34  THR   B CG2 1 
ATOM   493  N N   . GLN   B 2 26  ? -16.582 15.551  -17.813 1.00 48.09  ? 35  GLN   B N   1 
ATOM   494  C CA  . GLN   B 2 26  ? -17.104 14.161  -17.718 1.00 47.59  ? 35  GLN   B CA  1 
ATOM   495  C C   . GLN   B 2 26  ? -16.108 13.354  -16.873 1.00 50.36  ? 35  GLN   B C   1 
ATOM   496  O O   . GLN   B 2 26  ? -14.966 13.166  -17.336 1.00 50.27  ? 35  GLN   B O   1 
ATOM   497  C CB  . GLN   B 2 26  ? -17.294 13.501  -19.079 1.00 45.50  ? 35  GLN   B CB  1 
ATOM   498  C CG  . GLN   B 2 26  ? -17.963 12.130  -18.991 1.00 45.15  ? 35  GLN   B CG  1 
ATOM   499  C CD  . GLN   B 2 26  ? -18.233 11.516  -20.345 1.00 44.50  ? 35  GLN   B CD  1 
ATOM   500  O OE1 . GLN   B 2 26  ? -18.859 12.131  -21.200 1.00 46.28  ? 35  GLN   B OE1 1 
ATOM   501  N NE2 . GLN   B 2 26  ? -17.819 10.272  -20.539 1.00 42.91  ? 35  GLN   B NE2 1 
ATOM   502  N N   . VAL   B 2 27  ? -16.517 12.896  -15.690 1.00 48.77  ? 36  VAL   B N   1 
ATOM   503  C CA  . VAL   B 2 27  ? -15.625 12.112  -14.775 1.00 47.79  ? 36  VAL   B CA  1 
ATOM   504  C C   . VAL   B 2 27  ? -15.872 10.619  -15.013 1.00 44.07  ? 36  VAL   B C   1 
ATOM   505  O O   . VAL   B 2 27  ? -15.033 9.823   -14.658 1.00 43.49  ? 36  VAL   B O   1 
ATOM   506  C CB  . VAL   B 2 27  ? -15.838 12.513  -13.302 1.00 49.93  ? 36  VAL   B CB  1 
ATOM   507  C CG1 . VAL   B 2 27  ? -15.156 13.838  -12.976 1.00 51.97  ? 36  VAL   B CG1 1 
ATOM   508  C CG2 . VAL   B 2 27  ? -17.305 12.561  -12.898 1.00 46.54  ? 36  VAL   B CG2 1 
ATOM   509  N N   . GLY   B 2 28  ? -16.988 10.226  -15.614 1.00 42.18  ? 37  GLY   B N   1 
ATOM   510  C CA  . GLY   B 2 28  ? -17.182 8.800   -15.949 1.00 39.39  ? 37  GLY   B CA  1 
ATOM   511  C C   . GLY   B 2 28  ? -18.524 8.551   -16.591 1.00 39.29  ? 37  GLY   B C   1 
ATOM   512  O O   . GLY   B 2 28  ? -19.134 9.489   -17.087 1.00 40.37  ? 37  GLY   B O   1 
ATOM   513  N N   . VAL   B 2 29  ? -18.992 7.303   -16.503 1.00 37.49  ? 38  VAL   B N   1 
ATOM   514  C CA  . VAL   B 2 29  ? -20.120 6.716   -17.291 1.00 36.55  ? 38  VAL   B CA  1 
ATOM   515  C C   . VAL   B 2 29  ? -20.808 5.724   -16.361 1.00 36.65  ? 38  VAL   B C   1 
ATOM   516  O O   . VAL   B 2 29  ? -20.125 5.229   -15.447 1.00 34.97  ? 38  VAL   B O   1 
ATOM   517  C CB  . VAL   B 2 29  ? -19.566 5.990   -18.538 1.00 38.20  ? 38  VAL   B CB  1 
ATOM   518  C CG1 . VAL   B 2 29  ? -20.638 5.287   -19.348 1.00 39.10  ? 38  VAL   B CG1 1 
ATOM   519  C CG2 . VAL   B 2 29  ? -18.713 6.858   -19.434 1.00 38.05  ? 38  VAL   B CG2 1 
ATOM   520  N N   . GLY   B 2 30  ? -22.080 5.398   -16.593 1.00 36.19  ? 39  GLY   B N   1 
ATOM   521  C CA  . GLY   B 2 30  ? -22.764 4.363   -15.824 1.00 33.89  ? 39  GLY   B CA  1 
ATOM   522  C C   . GLY   B 2 30  ? -23.902 3.760   -16.574 1.00 34.08  ? 39  GLY   B C   1 
ATOM   523  O O   . GLY   B 2 30  ? -24.211 4.257   -17.709 1.00 37.22  ? 39  GLY   B O   1 
ATOM   524  N N   . VAL   B 2 31  ? -24.500 2.730   -15.978 1.00 33.30  ? 40  VAL   B N   1 
ATOM   525  C CA  . VAL   B 2 31  ? -25.571 1.892   -16.569 1.00 33.76  ? 40  VAL   B CA  1 
ATOM   526  C C   . VAL   B 2 31  ? -26.792 1.992   -15.667 1.00 35.56  ? 40  VAL   B C   1 
ATOM   527  O O   . VAL   B 2 31  ? -26.683 1.718   -14.445 1.00 33.98  ? 40  VAL   B O   1 
ATOM   528  C CB  . VAL   B 2 31  ? -25.213 0.405   -16.663 1.00 35.58  ? 40  VAL   B CB  1 
ATOM   529  C CG1 . VAL   B 2 31  ? -26.404 -0.385  -17.162 1.00 36.90  ? 40  VAL   B CG1 1 
ATOM   530  C CG2 . VAL   B 2 31  ? -23.999 0.163   -17.506 1.00 36.74  ? 40  VAL   B CG2 1 
ATOM   531  N N   . MET   B 2 32  ? -27.898 2.477   -16.232 1.00 36.74  ? 41  MET   B N   1 
ATOM   532  C CA  . MET   B 2 32  ? -29.214 2.430   -15.611 1.00 37.72  ? 41  MET   B CA  1 
ATOM   533  C C   . MET   B 2 32  ? -29.904 1.127   -16.035 1.00 37.61  ? 41  MET   B C   1 
ATOM   534  O O   . MET   B 2 32  ? -30.136 0.916   -17.223 1.00 36.31  ? 41  MET   B O   1 
ATOM   535  C CB  . MET   B 2 32  ? -30.023 3.657   -16.038 1.00 40.37  ? 41  MET   B CB  1 
ATOM   536  C CG  . MET   B 2 32  ? -31.272 3.881   -15.210 1.00 43.42  ? 41  MET   B CG  1 
ATOM   537  S SD  . MET   B 2 32  ? -30.963 4.487   -13.502 1.00 44.20  ? 41  MET   B SD  1 
ATOM   538  C CE  . MET   B 2 32  ? -30.296 6.113   -13.812 1.00 46.51  ? 41  MET   B CE  1 
ATOM   539  N N   . GLN   B 2 33  ? -30.286 0.294   -15.077 1.00 39.68  ? 42  GLN   B N   1 
ATOM   540  C CA  . GLN   B 2 33  ? -31.053 -0.940  -15.355 1.00 41.26  ? 42  GLN   B CA  1 
ATOM   541  C C   . GLN   B 2 33  ? -31.991 -1.164  -14.191 1.00 42.48  ? 42  GLN   B C   1 
ATOM   542  O O   . GLN   B 2 33  ? -31.550 -1.051  -13.049 1.00 42.50  ? 42  GLN   B O   1 
ATOM   543  C CB  . GLN   B 2 33  ? -30.133 -2.160  -15.536 1.00 41.64  ? 42  GLN   B CB  1 
ATOM   544  C CG  . GLN   B 2 33  ? -30.921 -3.371  -16.028 1.00 44.88  ? 42  GLN   B CG  1 
ATOM   545  C CD  . GLN   B 2 33  ? -30.036 -4.484  -16.538 1.00 48.98  ? 42  GLN   B CD  1 
ATOM   546  O OE1 . GLN   B 2 33  ? -30.138 -5.637  -16.107 1.00 55.58  ? 42  GLN   B OE1 1 
ATOM   547  N NE2 . GLN   B 2 33  ? -29.088 -4.139  -17.387 1.00 46.92  ? 42  GLN   B NE2 1 
ATOM   548  N N   . GLU   B 2 34  ? -33.228 -1.511  -14.469 1.00 45.87  ? 43  GLU   B N   1 
ATOM   549  C CA  . GLU   B 2 34  ? -34.242 -1.786  -13.425 1.00 47.52  ? 43  GLU   B CA  1 
ATOM   550  C C   . GLU   B 2 34  ? -34.257 -0.676  -12.353 1.00 47.14  ? 43  GLU   B C   1 
ATOM   551  O O   . GLU   B 2 34  ? -34.398 -1.010  -11.190 1.00 47.04  ? 43  GLU   B O   1 
ATOM   552  C CB  . GLU   B 2 34  ? -33.928 -3.160  -12.829 1.00 51.55  ? 43  GLU   B CB  1 
ATOM   553  C CG  . GLU   B 2 34  ? -34.171 -4.326  -13.779 1.00 53.35  ? 43  GLU   B CG  1 
ATOM   554  C CD  . GLU   B 2 34  ? -33.537 -5.662  -13.397 1.00 55.44  ? 43  GLU   B CD  1 
ATOM   555  O OE1 . GLU   B 2 34  ? -33.987 -6.274  -12.424 1.00 59.06  ? 43  GLU   B OE1 1 
ATOM   556  O OE2 . GLU   B 2 34  ? -32.589 -6.088  -14.080 1.00 58.35  ? 43  GLU   B OE2 1 
ATOM   557  N N   . GLY   B 2 35  ? -34.110 0.608   -12.699 1.00 45.62  ? 44  GLY   B N   1 
ATOM   558  C CA  . GLY   B 2 35  ? -34.286 1.723   -11.744 1.00 41.36  ? 44  GLY   B CA  1 
ATOM   559  C C   . GLY   B 2 35  ? -33.057 1.956   -10.888 1.00 41.34  ? 44  GLY   B C   1 
ATOM   560  O O   . GLY   B 2 35  ? -33.064 2.883   -10.067 1.00 40.04  ? 44  GLY   B O   1 
ATOM   561  N N   . VAL   B 2 36  ? -32.007 1.165   -11.098 1.00 36.71  ? 45  VAL   B N   1 
ATOM   562  C CA  . VAL   B 2 36  ? -30.714 1.238   -10.373 1.00 35.78  ? 45  VAL   B CA  1 
ATOM   563  C C   . VAL   B 2 36  ? -29.665 1.759   -11.331 1.00 33.74  ? 45  VAL   B C   1 
ATOM   564  O O   . VAL   B 2 36  ? -29.569 1.218   -12.471 1.00 33.91  ? 45  VAL   B O   1 
ATOM   565  C CB  . VAL   B 2 36  ? -30.350 -0.131  -9.743  1.00 37.56  ? 45  VAL   B CB  1 
ATOM   566  C CG1 . VAL   B 2 36  ? -28.930 -0.185  -9.179  1.00 37.67  ? 45  VAL   B CG1 1 
ATOM   567  C CG2 . VAL   B 2 36  ? -31.332 -0.436  -8.626  1.00 39.66  ? 45  VAL   B CG2 1 
ATOM   568  N N   . PHE   B 2 37  ? -28.880 2.727   -10.865 1.00 32.37  ? 46  PHE   B N   1 
ATOM   569  C CA  . PHE   B 2 37  ? -27.729 3.281   -11.586 1.00 33.03  ? 46  PHE   B CA  1 
ATOM   570  C C   . PHE   B 2 37  ? -26.470 2.597   -11.040 1.00 31.81  ? 46  PHE   B C   1 
ATOM   571  O O   . PHE   B 2 37  ? -26.288 2.578   -9.824  1.00 31.57  ? 46  PHE   B O   1 
ATOM   572  C CB  . PHE   B 2 37  ? -27.683 4.792   -11.427 1.00 32.80  ? 46  PHE   B CB  1 
ATOM   573  C CG  . PHE   B 2 37  ? -26.655 5.408   -12.343 1.00 33.47  ? 46  PHE   B CG  1 
ATOM   574  C CD1 . PHE   B 2 37  ? -26.810 5.324   -13.704 1.00 34.38  ? 46  PHE   B CD1 1 
ATOM   575  C CD2 . PHE   B 2 37  ? -25.512 6.005   -11.849 1.00 34.34  ? 46  PHE   B CD2 1 
ATOM   576  C CE1 . PHE   B 2 37  ? -25.895 5.905   -14.575 1.00 35.68  ? 46  PHE   B CE1 1 
ATOM   577  C CE2 . PHE   B 2 37  ? -24.571 6.541   -12.721 1.00 33.65  ? 46  PHE   B CE2 1 
ATOM   578  C CZ  . PHE   B 2 37  ? -24.787 6.526   -14.074 1.00 34.81  ? 46  PHE   B CZ  1 
ATOM   579  N N   . HIS   B 2 38  ? -25.603 2.157   -11.923 1.00 32.79  ? 47  HIS   B N   1 
ATOM   580  C CA  . HIS   B 2 38  ? -24.395 1.342   -11.634 1.00 32.02  ? 47  HIS   B CA  1 
ATOM   581  C C   . HIS   B 2 38  ? -23.179 2.091   -12.167 1.00 31.25  ? 47  HIS   B C   1 
ATOM   582  O O   . HIS   B 2 38  ? -23.157 2.400   -13.377 1.00 30.90  ? 47  HIS   B O   1 
ATOM   583  C CB  . HIS   B 2 38  ? -24.514 0.030   -12.343 1.00 32.44  ? 47  HIS   B CB  1 
ATOM   584  C CG  . HIS   B 2 38  ? -25.713 -0.778  -12.041 1.00 34.52  ? 47  HIS   B CG  1 
ATOM   585  N ND1 . HIS   B 2 38  ? -26.945 -0.466  -12.528 1.00 37.01  ? 47  HIS   B ND1 1 
ATOM   586  C CD2 . HIS   B 2 38  ? -25.858 -1.915  -11.333 1.00 34.75  ? 47  HIS   B CD2 1 
ATOM   587  C CE1 . HIS   B 2 38  ? -27.835 -1.344  -12.079 1.00 37.11  ? 47  HIS   B CE1 1 
ATOM   588  N NE2 . HIS   B 2 38  ? -27.175 -2.231  -11.314 1.00 36.71  ? 47  HIS   B NE2 1 
ATOM   589  N N   . THR   B 2 39  ? -22.187 2.390   -11.336 1.00 32.82  ? 48  THR   B N   1 
ATOM   590  C CA  . THR   B 2 39  ? -20.939 2.958   -11.866 1.00 33.25  ? 48  THR   B CA  1 
ATOM   591  C C   . THR   B 2 39  ? -19.777 2.366   -11.087 1.00 34.95  ? 48  THR   B C   1 
ATOM   592  O O   . THR   B 2 39  ? -19.991 1.421   -10.256 1.00 33.87  ? 48  THR   B O   1 
ATOM   593  C CB  . THR   B 2 39  ? -21.055 4.484   -11.954 1.00 35.38  ? 48  THR   B CB  1 
ATOM   594  O OG1 . THR   B 2 39  ? -19.887 5.007   -12.591 1.00 35.06  ? 48  THR   B OG1 1 
ATOM   595  C CG2 . THR   B 2 39  ? -21.220 5.149   -10.602 1.00 36.36  ? 48  THR   B CG2 1 
ATOM   596  N N   . MET   B 2 40  ? -18.590 2.894   -11.355 1.00 36.13  ? 49  MET   B N   1 
ATOM   597  C CA  . MET   B 2 40  ? -17.378 2.528   -10.589 1.00 38.41  ? 49  MET   B CA  1 
ATOM   598  C C   . MET   B 2 40  ? -17.174 3.531   -9.448  1.00 37.47  ? 49  MET   B C   1 
ATOM   599  O O   . MET   B 2 40  ? -17.436 4.747   -9.627  1.00 37.27  ? 49  MET   B O   1 
ATOM   600  C CB  . MET   B 2 40  ? -16.159 2.481   -11.506 1.00 37.84  ? 49  MET   B CB  1 
ATOM   601  C CG  . MET   B 2 40  ? -16.441 1.693   -12.790 1.00 40.36  ? 49  MET   B CG  1 
ATOM   602  S SD  . MET   B 2 40  ? -14.970 0.845   -13.423 1.00 45.84  ? 49  MET   B SD  1 
ATOM   603  C CE  . MET   B 2 40  ? -14.955 -0.610  -12.373 1.00 44.22  ? 49  MET   B CE  1 
ATOM   604  N N   A TRP   B 2 41  ? -16.705 3.039   -8.296  0.19 38.18  ? 50  TRP   B N   1 
ATOM   605  N N   B TRP   B 2 41  ? -16.713 3.043   -8.297  0.15 36.88  ? 50  TRP   B N   1 
ATOM   606  N N   C TRP   B 2 41  ? -16.705 3.038   -8.298  0.34 38.03  ? 50  TRP   B N   1 
ATOM   607  N N   D TRP   B 2 41  ? -16.712 3.043   -8.299  0.32 36.71  ? 50  TRP   B N   1 
ATOM   608  C CA  A TRP   B 2 41  ? -16.505 3.838   -7.054  0.19 38.84  ? 50  TRP   B CA  1 
ATOM   609  C CA  B TRP   B 2 41  ? -16.554 3.869   -7.072  0.15 36.64  ? 50  TRP   B CA  1 
ATOM   610  C CA  C TRP   B 2 41  ? -16.504 3.837   -7.057  0.34 38.86  ? 50  TRP   B CA  1 
ATOM   611  C CA  D TRP   B 2 41  ? -16.554 3.869   -7.075  0.32 36.59  ? 50  TRP   B CA  1 
ATOM   612  C C   A TRP   B 2 41  ? -15.597 5.039   -7.341  0.19 38.61  ? 50  TRP   B C   1 
ATOM   613  C C   B TRP   B 2 41  ? -15.607 5.047   -7.349  0.15 37.31  ? 50  TRP   B C   1 
ATOM   614  C C   C TRP   B 2 41  ? -15.596 5.039   -7.344  0.34 38.71  ? 50  TRP   B C   1 
ATOM   615  C C   D TRP   B 2 41  ? -15.605 5.047   -7.353  0.32 37.38  ? 50  TRP   B C   1 
ATOM   616  O O   A TRP   B 2 41  ? -15.871 6.137   -6.811  0.19 38.01  ? 50  TRP   B O   1 
ATOM   617  O O   B TRP   B 2 41  ? -15.876 6.154   -6.836  0.15 36.84  ? 50  TRP   B O   1 
ATOM   618  O O   C TRP   B 2 41  ? -15.861 6.139   -6.810  0.34 37.95  ? 50  TRP   B O   1 
ATOM   619  O O   D TRP   B 2 41  ? -15.866 6.157   -6.836  0.32 36.75  ? 50  TRP   B O   1 
ATOM   620  C CB  A TRP   B 2 41  ? -15.923 2.995   -5.906  0.19 39.98  ? 50  TRP   B CB  1 
ATOM   621  C CB  B TRP   B 2 41  ? -16.080 3.035   -5.872  0.15 36.11  ? 50  TRP   B CB  1 
ATOM   622  C CB  C TRP   B 2 41  ? -15.919 2.993   -5.908  0.34 40.05  ? 50  TRP   B CB  1 
ATOM   623  C CB  D TRP   B 2 41  ? -16.077 3.033   -5.874  0.32 36.08  ? 50  TRP   B CB  1 
ATOM   624  C CG  A TRP   B 2 41  ? -15.971 3.696   -4.579  0.19 40.96  ? 50  TRP   B CG  1 
ATOM   625  C CG  B TRP   B 2 41  ? -15.935 3.879   -4.644  0.15 35.42  ? 50  TRP   B CG  1 
ATOM   626  C CG  C TRP   B 2 41  ? -15.967 3.695   -4.580  0.34 41.09  ? 50  TRP   B CG  1 
ATOM   627  C CG  D TRP   B 2 41  ? -15.935 3.876   -4.643  0.32 35.31  ? 50  TRP   B CG  1 
ATOM   628  C CD1 A TRP   B 2 41  ? -16.982 3.631   -3.666  0.19 41.17  ? 50  TRP   B CD1 1 
ATOM   629  C CD1 B TRP   B 2 41  ? -14.896 4.713   -4.361  0.15 34.87  ? 50  TRP   B CD1 1 
ATOM   630  C CD1 C TRP   B 2 41  ? -16.980 3.632   -3.669  0.34 41.24  ? 50  TRP   B CD1 1 
ATOM   631  C CD1 D TRP   B 2 41  ? -14.900 4.712   -4.361  0.32 34.49  ? 50  TRP   B CD1 1 
ATOM   632  C CD2 A TRP   B 2 41  ? -14.994 4.601   -4.025  0.19 41.51  ? 50  TRP   B CD2 1 
ATOM   633  C CD2 B TRP   B 2 41  ? -16.888 4.051   -3.578  0.15 35.06  ? 50  TRP   B CD2 1 
ATOM   634  C CD2 C TRP   B 2 41  ? -14.990 4.602   -4.027  0.34 41.47  ? 50  TRP   B CD2 1 
ATOM   635  C CD2 D TRP   B 2 41  ? -16.891 4.051   -3.580  0.32 34.96  ? 50  TRP   B CD2 1 
ATOM   636  N NE1 A TRP   B 2 41  ? -16.697 4.414   -2.579  0.19 41.73  ? 50  TRP   B NE1 1 
ATOM   637  N NE1 B TRP   B 2 41  ? -15.112 5.368   -3.184  0.15 34.64  ? 50  TRP   B NE1 1 
ATOM   638  N NE1 C TRP   B 2 41  ? -16.695 4.415   -2.583  0.34 41.99  ? 50  TRP   B NE1 1 
ATOM   639  N NE1 D TRP   B 2 41  ? -15.114 5.368   -3.189  0.32 34.33  ? 50  TRP   B NE1 1 
ATOM   640  C CE2 A TRP   B 2 41  ? -15.485 5.024   -2.772  0.19 42.29  ? 50  TRP   B CE2 1 
ATOM   641  C CE2 B TRP   B 2 41  ? -16.325 4.983   -2.678  0.15 34.81  ? 50  TRP   B CE2 1 
ATOM   642  C CE2 C TRP   B 2 41  ? -15.483 5.027   -2.775  0.34 42.68  ? 50  TRP   B CE2 1 
ATOM   643  C CE2 D TRP   B 2 41  ? -16.328 4.984   -2.682  0.32 34.70  ? 50  TRP   B CE2 1 
ATOM   644  C CE3 A TRP   B 2 41  ? -13.751 5.086   -4.452  0.19 43.32  ? 50  TRP   B CE3 1 
ATOM   645  C CE3 B TRP   B 2 41  ? -18.143 3.505   -3.277  0.15 35.46  ? 50  TRP   B CE3 1 
ATOM   646  C CE3 C TRP   B 2 41  ? -13.743 5.087   -4.453  0.34 44.13  ? 50  TRP   B CE3 1 
ATOM   647  C CE3 D TRP   B 2 41  ? -18.146 3.506   -3.277  0.32 35.67  ? 50  TRP   B CE3 1 
ATOM   648  C CZ2 A TRP   B 2 41  ? -14.774 5.902   -1.948  0.19 43.01  ? 50  TRP   B CZ2 1 
ATOM   649  C CZ2 B TRP   B 2 41  ? -16.968 5.369   -1.504  0.15 34.78  ? 50  TRP   B CZ2 1 
ATOM   650  C CZ2 C TRP   B 2 41  ? -14.772 5.905   -1.950  0.34 43.63  ? 50  TRP   B CZ2 1 
ATOM   651  C CZ2 D TRP   B 2 41  ? -16.971 5.371   -1.506  0.32 34.82  ? 50  TRP   B CZ2 1 
ATOM   652  C CZ3 A TRP   B 2 41  ? -13.050 5.956   -3.641  0.19 43.19  ? 50  TRP   B CZ3 1 
ATOM   653  C CZ3 B TRP   B 2 41  ? -18.773 3.879   -2.107  0.15 35.02  ? 50  TRP   B CZ3 1 
ATOM   654  C CZ3 C TRP   B 2 41  ? -13.043 5.957   -3.639  0.34 43.76  ? 50  TRP   B CZ3 1 
ATOM   655  C CZ3 D TRP   B 2 41  ? -18.773 3.877   -2.100  0.32 35.09  ? 50  TRP   B CZ3 1 
ATOM   656  C CH2 A TRP   B 2 41  ? -13.556 6.355   -2.403  0.19 43.48  ? 50  TRP   B CH2 1 
ATOM   657  C CH2 B TRP   B 2 41  ? -18.198 4.809   -1.241  0.15 34.79  ? 50  TRP   B CH2 1 
ATOM   658  C CH2 C TRP   B 2 41  ? -13.551 6.356   -2.402  0.34 44.19  ? 50  TRP   B CH2 1 
ATOM   659  C CH2 D TRP   B 2 41  ? -18.202 4.812   -1.240  0.32 34.85  ? 50  TRP   B CH2 1 
ATOM   660  N N   . HIS   B 2 42  ? -14.538 4.835   -8.121  1.00 37.56  ? 51  HIS   B N   1 
ATOM   661  C CA  . HIS   B 2 42  ? -13.506 5.904   -8.342  1.00 39.54  ? 51  HIS   B CA  1 
ATOM   662  C C   . HIS   B 2 42  ? -14.086 7.110   -9.121  1.00 41.23  ? 51  HIS   B C   1 
ATOM   663  O O   . HIS   B 2 42  ? -13.494 8.163   -9.048  1.00 42.94  ? 51  HIS   B O   1 
ATOM   664  C CB  . HIS   B 2 42  ? -12.212 5.346   -8.899  1.00 39.73  ? 51  HIS   B CB  1 
ATOM   665  C CG  . HIS   B 2 42  ? -12.249 5.083   -10.343 1.00 40.75  ? 51  HIS   B CG  1 
ATOM   666  N ND1 . HIS   B 2 42  ? -12.419 3.804   -10.853 1.00 40.83  ? 51  HIS   B ND1 1 
ATOM   667  C CD2 . HIS   B 2 42  ? -12.117 5.931   -11.395 1.00 42.66  ? 51  HIS   B CD2 1 
ATOM   668  C CE1 . HIS   B 2 42  ? -12.365 3.876   -12.173 1.00 41.08  ? 51  HIS   B CE1 1 
ATOM   669  N NE2 . HIS   B 2 42  ? -12.215 5.185   -12.527 1.00 42.19  ? 51  HIS   B NE2 1 
ATOM   670  N N   . VAL   B 2 43  ? -15.240 6.973   -9.760  1.00 38.09  ? 52  VAL   B N   1 
ATOM   671  C CA  . VAL   B 2 43  ? -15.900 8.045   -10.537 1.00 40.50  ? 52  VAL   B CA  1 
ATOM   672  C C   . VAL   B 2 43  ? -16.663 8.955   -9.566  1.00 39.84  ? 52  VAL   B C   1 
ATOM   673  O O   . VAL   B 2 43  ? -16.510 10.175  -9.724  1.00 40.40  ? 52  VAL   B O   1 
ATOM   674  C CB  . VAL   B 2 43  ? -16.836 7.399   -11.568 1.00 41.28  ? 52  VAL   B CB  1 
ATOM   675  C CG1 . VAL   B 2 43  ? -17.841 8.382   -12.159 1.00 43.41  ? 52  VAL   B CG1 1 
ATOM   676  C CG2 . VAL   B 2 43  ? -16.070 6.666   -12.645 1.00 41.99  ? 52  VAL   B CG2 1 
ATOM   677  N N   . THR   B 2 44  ? -17.485 8.409   -8.637  1.00 39.09  ? 53  THR   B N   1 
ATOM   678  C CA  . THR   B 2 44  ? -18.388 9.232   -7.761  1.00 39.66  ? 53  THR   B CA  1 
ATOM   679  C C   . THR   B 2 44  ? -17.787 9.445   -6.360  1.00 41.68  ? 53  THR   B C   1 
ATOM   680  O O   . THR   B 2 44  ? -18.172 10.454  -5.708  1.00 42.60  ? 53  THR   B O   1 
ATOM   681  C CB  . THR   B 2 44  ? -19.815 8.682   -7.717  1.00 38.79  ? 53  THR   B CB  1 
ATOM   682  O OG1 . THR   B 2 44  ? -19.782 7.414   -7.042  1.00 38.56  ? 53  THR   B OG1 1 
ATOM   683  C CG2 . THR   B 2 44  ? -20.393 8.571   -9.118  1.00 38.63  ? 53  THR   B CG2 1 
ATOM   684  N N   . LYS   B 2 45  ? -16.867 8.566   -5.943  1.00 42.56  ? 54  LYS   B N   1 
ATOM   685  C CA  . LYS   B 2 45  ? -16.371 8.386   -4.550  1.00 46.22  ? 54  LYS   B CA  1 
ATOM   686  C C   . LYS   B 2 45  ? -17.568 8.206   -3.595  1.00 43.99  ? 54  LYS   B C   1 
ATOM   687  O O   . LYS   B 2 45  ? -17.476 8.653   -2.440  1.00 46.13  ? 54  LYS   B O   1 
ATOM   688  C CB  . LYS   B 2 45  ? -15.511 9.569   -4.085  1.00 51.27  ? 54  LYS   B CB  1 
ATOM   689  C CG  . LYS   B 2 45  ? -14.436 10.054  -5.035  1.00 57.39  ? 54  LYS   B CG  1 
ATOM   690  C CD  . LYS   B 2 45  ? -13.233 9.169   -5.162  1.00 62.95  ? 54  LYS   B CD  1 
ATOM   691  C CE  . LYS   B 2 45  ? -12.212 9.778   -6.112  1.00 68.58  ? 54  LYS   B CE  1 
ATOM   692  N NZ  . LYS   B 2 45  ? -11.572 8.757   -6.989  1.00 70.26  ? 54  LYS   B NZ  1 
ATOM   693  N N   . GLY   B 2 46  ? -18.674 7.625   -4.055  1.00 42.14  ? 55  GLY   B N   1 
ATOM   694  C CA  . GLY   B 2 46  ? -19.874 7.395   -3.231  1.00 41.94  ? 55  GLY   B CA  1 
ATOM   695  C C   . GLY   B 2 46  ? -20.744 8.636   -3.025  1.00 42.28  ? 55  GLY   B C   1 
ATOM   696  O O   . GLY   B 2 46  ? -21.675 8.559   -2.286  1.00 43.05  ? 55  GLY   B O   1 
ATOM   697  N N   . ALA   B 2 47  ? -20.495 9.741   -3.706  1.00 45.17  ? 56  ALA   B N   1 
ATOM   698  C CA  . ALA   B 2 47  ? -21.333 10.968  -3.625  1.00 44.70  ? 56  ALA   B CA  1 
ATOM   699  C C   . ALA   B 2 47  ? -22.705 10.744  -4.289  1.00 44.67  ? 56  ALA   B C   1 
ATOM   700  O O   . ALA   B 2 47  ? -22.833 9.952   -5.225  1.00 44.41  ? 56  ALA   B O   1 
ATOM   701  C CB  . ALA   B 2 47  ? -20.583 12.124  -4.261  1.00 43.42  ? 56  ALA   B CB  1 
ATOM   702  N N   . ALA   B 2 48  ? -23.711 11.481  -3.852  1.00 44.08  ? 57  ALA   B N   1 
ATOM   703  C CA  . ALA   B 2 48  ? -25.037 11.516  -4.505  1.00 43.28  ? 57  ALA   B CA  1 
ATOM   704  C C   . ALA   B 2 48  ? -24.924 12.220  -5.861  1.00 43.41  ? 57  ALA   B C   1 
ATOM   705  O O   . ALA   B 2 48  ? -23.906 12.904  -6.163  1.00 43.67  ? 57  ALA   B O   1 
ATOM   706  C CB  . ALA   B 2 48  ? -26.074 12.178  -3.627  1.00 45.38  ? 57  ALA   B CB  1 
ATOM   707  N N   . LEU   B 2 49  ? -25.924 11.963  -6.684  1.00 40.42  ? 58  LEU   B N   1 
ATOM   708  C CA  . LEU   B 2 49  ? -25.971 12.322  -8.113  1.00 42.70  ? 58  LEU   B CA  1 
ATOM   709  C C   . LEU   B 2 49  ? -27.302 13.030  -8.357  1.00 44.70  ? 58  LEU   B C   1 
ATOM   710  O O   . LEU   B 2 49  ? -28.307 12.684  -7.679  1.00 48.67  ? 58  LEU   B O   1 
ATOM   711  C CB  . LEU   B 2 49  ? -25.880 11.052  -8.963  1.00 40.96  ? 58  LEU   B CB  1 
ATOM   712  C CG  . LEU   B 2 49  ? -24.582 10.237  -8.842  1.00 39.40  ? 58  LEU   B CG  1 
ATOM   713  C CD1 . LEU   B 2 49  ? -24.683 8.974   -9.659  1.00 37.37  ? 58  LEU   B CD1 1 
ATOM   714  C CD2 . LEU   B 2 49  ? -23.393 11.057  -9.279  1.00 39.84  ? 58  LEU   B CD2 1 
ATOM   715  N N   . ARG   B 2 50  ? -27.300 13.975  -9.279  1.00 46.76  ? 59  ARG   B N   1 
ATOM   716  C CA  . ARG   B 2 50  ? -28.536 14.612  -9.774  1.00 50.24  ? 59  ARG   B CA  1 
ATOM   717  C C   . ARG   B 2 50  ? -28.890 13.996  -11.137 1.00 50.85  ? 59  ARG   B C   1 
ATOM   718  O O   . ARG   B 2 50  ? -27.964 13.694  -11.928 1.00 48.61  ? 59  ARG   B O   1 
ATOM   719  C CB  . ARG   B 2 50  ? -28.255 16.110  -9.821  1.00 55.53  ? 59  ARG   B CB  1 
ATOM   720  C CG  . ARG   B 2 50  ? -29.427 16.951  -10.303 1.00 63.60  ? 59  ARG   B CG  1 
ATOM   721  C CD  . ARG   B 2 50  ? -29.146 18.427  -10.071 1.00 67.13  ? 59  ARG   B CD  1 
ATOM   722  N NE  . ARG   B 2 50  ? -27.737 18.774  -10.292 1.00 68.78  ? 59  ARG   B NE  1 
ATOM   723  C CZ  . ARG   B 2 50  ? -27.229 19.254  -11.429 1.00 73.19  ? 59  ARG   B CZ  1 
ATOM   724  N NH1 . ARG   B 2 50  ? -27.998 19.415  -12.500 1.00 73.47  ? 59  ARG   B NH1 1 
ATOM   725  N NH2 . ARG   B 2 50  ? -25.939 19.560  -11.493 1.00 75.55  ? 59  ARG   B NH2 1 
ATOM   726  N N   . SER   B 2 51  ? -30.172 13.736  -11.366 1.00 50.59  ? 60  SER   B N   1 
ATOM   727  C CA  . SER   B 2 51  ? -30.783 13.496  -12.700 1.00 56.08  ? 60  SER   B CA  1 
ATOM   728  C C   . SER   B 2 51  ? -31.912 14.517  -12.948 1.00 58.48  ? 60  SER   B C   1 
ATOM   729  O O   . SER   B 2 51  ? -33.044 14.258  -12.526 1.00 58.82  ? 60  SER   B O   1 
ATOM   730  C CB  . SER   B 2 51  ? -31.317 12.085  -12.787 1.00 53.37  ? 60  SER   B CB  1 
ATOM   731  O OG  . SER   B 2 51  ? -31.991 11.895  -14.013 1.00 51.22  ? 60  SER   B OG  1 
ATOM   732  N N   . GLY   B 2 52  ? -31.634 15.637  -13.616 1.00 63.03  ? 61  GLY   B N   1 
ATOM   733  C CA  . GLY   B 2 52  ? -32.602 16.750  -13.717 1.00 64.27  ? 61  GLY   B CA  1 
ATOM   734  C C   . GLY   B 2 52  ? -32.851 17.361  -12.349 1.00 66.53  ? 61  GLY   B C   1 
ATOM   735  O O   . GLY   B 2 52  ? -31.889 17.845  -11.738 1.00 69.48  ? 61  GLY   B O   1 
ATOM   736  N N   . GLU   B 2 53  ? -34.075 17.273  -11.838 1.00 69.16  ? 62  GLU   B N   1 
ATOM   737  C CA  . GLU   B 2 53  ? -34.404 17.734  -10.466 1.00 74.86  ? 62  GLU   B CA  1 
ATOM   738  C C   . GLU   B 2 53  ? -34.360 16.575  -9.461  1.00 70.68  ? 62  GLU   B C   1 
ATOM   739  O O   . GLU   B 2 53  ? -34.310 16.877  -8.271  1.00 68.19  ? 62  GLU   B O   1 
ATOM   740  C CB  . GLU   B 2 53  ? -35.774 18.397  -10.432 1.00 81.17  ? 62  GLU   B CB  1 
ATOM   741  C CG  . GLU   B 2 53  ? -35.693 19.902  -10.417 1.00 89.32  ? 62  GLU   B CG  1 
ATOM   742  C CD  . GLU   B 2 53  ? -37.042 20.575  -10.228 1.00 102.10 ? 62  GLU   B CD  1 
ATOM   743  O OE1 . GLU   B 2 53  ? -38.086 19.860  -10.242 1.00 103.01 ? 62  GLU   B OE1 1 
ATOM   744  O OE2 . GLU   B 2 53  ? -37.050 21.815  -10.047 1.00 113.67 ? 62  GLU   B OE2 1 
ATOM   745  N N   . GLY   B 2 54  ? -34.357 15.320  -9.920  1.00 66.56  ? 63  GLY   B N   1 
ATOM   746  C CA  . GLY   B 2 54  ? -34.272 14.112  -9.075  1.00 65.74  ? 63  GLY   B CA  1 
ATOM   747  C C   . GLY   B 2 54  ? -32.902 13.957  -8.426  1.00 65.08  ? 63  GLY   B C   1 
ATOM   748  O O   . GLY   B 2 54  ? -31.918 14.493  -8.979  1.00 62.12  ? 63  GLY   B O   1 
ATOM   749  N N   . ARG   B 2 55  ? -32.849 13.287  -7.271  1.00 59.88  ? 64  ARG   B N   1 
ATOM   750  C CA  . ARG   B 2 55  ? -31.605 12.927  -6.544  1.00 57.90  ? 64  ARG   B CA  1 
ATOM   751  C C   . ARG   B 2 55  ? -31.432 11.397  -6.583  1.00 55.43  ? 64  ARG   B C   1 
ATOM   752  O O   . ARG   B 2 55  ? -32.430 10.656  -6.457  1.00 56.89  ? 64  ARG   B O   1 
ATOM   753  C CB  . ARG   B 2 55  ? -31.656 13.464  -5.114  1.00 60.78  ? 64  ARG   B CB  1 
ATOM   754  C CG  . ARG   B 2 55  ? -30.323 13.455  -4.376  1.00 63.29  ? 64  ARG   B CG  1 
ATOM   755  C CD  . ARG   B 2 55  ? -30.555 13.687  -2.883  1.00 68.15  ? 64  ARG   B CD  1 
ATOM   756  N NE  . ARG   B 2 55  ? -29.409 13.391  -2.030  1.00 68.97  ? 64  ARG   B NE  1 
ATOM   757  C CZ  . ARG   B 2 55  ? -28.621 14.282  -1.415  1.00 70.02  ? 64  ARG   B CZ  1 
ATOM   758  N NH1 . ARG   B 2 55  ? -28.843 15.580  -1.535  1.00 68.08  ? 64  ARG   B NH1 1 
ATOM   759  N NH2 . ARG   B 2 55  ? -27.614 13.862  -0.658  1.00 69.31  ? 64  ARG   B NH2 1 
ATOM   760  N N   . LEU   B 2 56  ? -30.214 10.931  -6.821  1.00 48.09  ? 65  LEU   B N   1 
ATOM   761  C CA  . LEU   B 2 56  ? -29.870 9.493   -6.722  1.00 48.05  ? 65  LEU   B CA  1 
ATOM   762  C C   . LEU   B 2 56  ? -28.967 9.368   -5.502  1.00 44.01  ? 65  LEU   B C   1 
ATOM   763  O O   . LEU   B 2 56  ? -27.902 10.029  -5.497  1.00 42.62  ? 65  LEU   B O   1 
ATOM   764  C CB  . LEU   B 2 56  ? -29.133 9.011   -7.987  1.00 46.43  ? 65  LEU   B CB  1 
ATOM   765  C CG  . LEU   B 2 56  ? -29.808 9.172   -9.346  1.00 50.10  ? 65  LEU   B CG  1 
ATOM   766  C CD1 . LEU   B 2 56  ? -29.270 8.116   -10.318 1.00 51.41  ? 65  LEU   B CD1 1 
ATOM   767  C CD2 . LEU   B 2 56  ? -31.315 9.027   -9.256  1.00 51.91  ? 65  LEU   B CD2 1 
ATOM   768  N N   . ASP   B 2 57  ? -29.368 8.576   -4.507  1.00 41.55  ? 66  ASP   B N   1 
ATOM   769  C CA  . ASP   B 2 57  ? -28.508 8.301   -3.334  1.00 41.13  ? 66  ASP   B CA  1 
ATOM   770  C C   . ASP   B 2 57  ? -27.812 6.946   -3.469  1.00 38.20  ? 66  ASP   B C   1 
ATOM   771  O O   . ASP   B 2 57  ? -28.397 5.946   -3.918  1.00 36.65  ? 66  ASP   B O   1 
ATOM   772  C CB  . ASP   B 2 57  ? -29.362 8.344   -2.072  1.00 46.74  ? 66  ASP   B CB  1 
ATOM   773  C CG  . ASP   B 2 57  ? -29.933 9.738   -1.800  1.00 52.36  ? 66  ASP   B CG  1 
ATOM   774  O OD1 . ASP   B 2 57  ? -29.171 10.700  -1.832  1.00 58.88  ? 66  ASP   B OD1 1 
ATOM   775  O OD2 . ASP   B 2 57  ? -31.134 9.847   -1.618  1.00 55.37  ? 66  ASP   B OD2 1 
ATOM   776  N N   . PRO   B 2 58  ? -26.550 6.832   -3.022  1.00 38.52  ? 67  PRO   B N   1 
ATOM   777  C CA  . PRO   B 2 58  ? -25.865 5.534   -3.021  1.00 37.49  ? 67  PRO   B CA  1 
ATOM   778  C C   . PRO   B 2 58  ? -26.645 4.503   -2.187  1.00 37.46  ? 67  PRO   B C   1 
ATOM   779  O O   . PRO   B 2 58  ? -27.313 4.880   -1.187  1.00 39.88  ? 67  PRO   B O   1 
ATOM   780  C CB  . PRO   B 2 58  ? -24.505 5.860   -2.402  1.00 39.44  ? 67  PRO   B CB  1 
ATOM   781  C CG  . PRO   B 2 58  ? -24.731 7.134   -1.636  1.00 39.02  ? 67  PRO   B CG  1 
ATOM   782  C CD  . PRO   B 2 58  ? -25.741 7.909   -2.437  1.00 38.26  ? 67  PRO   B CD  1 
ATOM   783  N N   . TYR   B 2 59  ? -26.628 3.243   -2.603  1.00 33.71  ? 68  TYR   B N   1 
ATOM   784  C CA  . TYR   B 2 59  ? -27.306 2.144   -1.905  1.00 33.45  ? 68  TYR   B CA  1 
ATOM   785  C C   . TYR   B 2 59  ? -26.255 1.131   -1.463  1.00 31.22  ? 68  TYR   B C   1 
ATOM   786  O O   . TYR   B 2 59  ? -26.398 0.572   -0.392  1.00 32.68  ? 68  TYR   B O   1 
ATOM   787  C CB  . TYR   B 2 59  ? -28.395 1.562   -2.800  1.00 35.04  ? 68  TYR   B CB  1 
ATOM   788  C CG  . TYR   B 2 59  ? -29.223 0.457   -2.201  1.00 34.58  ? 68  TYR   B CG  1 
ATOM   789  C CD1 . TYR   B 2 59  ? -28.744 -0.837  -2.166  1.00 35.41  ? 68  TYR   B CD1 1 
ATOM   790  C CD2 . TYR   B 2 59  ? -30.508 0.699   -1.727  1.00 35.72  ? 68  TYR   B CD2 1 
ATOM   791  C CE1 . TYR   B 2 59  ? -29.529 -1.880  -1.663  1.00 36.56  ? 68  TYR   B CE1 1 
ATOM   792  C CE2 . TYR   B 2 59  ? -31.302 -0.330  -1.233  1.00 37.44  ? 68  TYR   B CE2 1 
ATOM   793  C CZ  . TYR   B 2 59  ? -30.795 -1.626  -1.150  1.00 37.43  ? 68  TYR   B CZ  1 
ATOM   794  O OH  . TYR   B 2 59  ? -31.569 -2.675  -0.674  1.00 41.01  ? 68  TYR   B OH  1 
ATOM   795  N N   . TRP   B 2 60  ? -25.305 0.846   -2.307  1.00 31.07  ? 69  TRP   B N   1 
ATOM   796  C CA  . TRP   B 2 60  ? -24.304 -0.246  -2.104  1.00 30.22  ? 69  TRP   B CA  1 
ATOM   797  C C   . TRP   B 2 60  ? -22.978 0.220   -2.680  1.00 30.09  ? 69  TRP   B C   1 
ATOM   798  O O   . TRP   B 2 60  ? -22.946 0.837   -3.785  1.00 31.16  ? 69  TRP   B O   1 
ATOM   799  C CB  . TRP   B 2 60  ? -24.761 -1.599  -2.610  1.00 29.98  ? 69  TRP   B CB  1 
ATOM   800  C CG  . TRP   B 2 60  ? -23.632 -2.594  -2.548  1.00 29.62  ? 69  TRP   B CG  1 
ATOM   801  C CD1 . TRP   B 2 60  ? -23.192 -3.308  -1.454  1.00 29.93  ? 69  TRP   B CD1 1 
ATOM   802  C CD2 . TRP   B 2 60  ? -22.713 -2.898  -3.613  1.00 31.21  ? 69  TRP   B CD2 1 
ATOM   803  N NE1 . TRP   B 2 60  ? -22.045 -4.000  -1.800  1.00 30.54  ? 69  TRP   B NE1 1 
ATOM   804  C CE2 . TRP   B 2 60  ? -21.731 -3.774  -3.104  1.00 29.57  ? 69  TRP   B CE2 1 
ATOM   805  C CE3 . TRP   B 2 60  ? -22.596 -2.466  -4.936  1.00 32.00  ? 69  TRP   B CE3 1 
ATOM   806  C CZ2 . TRP   B 2 60  ? -20.698 -4.273  -3.888  1.00 30.72  ? 69  TRP   B CZ2 1 
ATOM   807  C CZ3 . TRP   B 2 60  ? -21.571 -2.958  -5.721  1.00 32.93  ? 69  TRP   B CZ3 1 
ATOM   808  C CH2 . TRP   B 2 60  ? -20.636 -3.858  -5.205  1.00 32.49  ? 69  TRP   B CH2 1 
ATOM   809  N N   . GLY   B 2 61  ? -21.883 -0.049  -1.994  1.00 31.53  ? 70  GLY   B N   1 
ATOM   810  C CA  . GLY   B 2 61  ? -20.596 0.194   -2.663  1.00 32.41  ? 70  GLY   B CA  1 
ATOM   811  C C   . GLY   B 2 61  ? -19.481 -0.566  -2.009  1.00 31.93  ? 70  GLY   B C   1 
ATOM   812  O O   . GLY   B 2 61  ? -19.661 -0.891  -0.809  1.00 32.37  ? 70  GLY   B O   1 
ATOM   813  N N   . ASP   B 2 62  ? -18.345 -0.650  -2.685  1.00 33.89  ? 71  ASP   B N   1 
ATOM   814  C CA  . ASP   B 2 62  ? -17.136 -1.402  -2.239  1.00 34.36  ? 71  ASP   B CA  1 
ATOM   815  C C   . ASP   B 2 62  ? -15.953 -0.856  -3.012  1.00 34.29  ? 71  ASP   B C   1 
ATOM   816  O O   . ASP   B 2 62  ? -15.965 -1.049  -4.247  1.00 36.50  ? 71  ASP   B O   1 
ATOM   817  C CB  . ASP   B 2 62  ? -17.322 -2.890  -2.460  1.00 36.48  ? 71  ASP   B CB  1 
ATOM   818  C CG  . ASP   B 2 62  ? -16.291 -3.773  -1.784  1.00 40.63  ? 71  ASP   B CG  1 
ATOM   819  O OD1 . ASP   B 2 62  ? -15.116 -3.614  -2.014  1.00 47.17  ? 71  ASP   B OD1 1 
ATOM   820  O OD2 . ASP   B 2 62  ? -16.699 -4.630  -1.041  1.00 49.37  ? 71  ASP   B OD2 1 
ATOM   821  N N   . VAL   B 2 63  ? -14.995 -0.228  -2.310  1.00 33.27  ? 72  VAL   B N   1 
ATOM   822  C CA  . VAL   B 2 63  ? -13.765 0.390   -2.863  1.00 34.56  ? 72  VAL   B CA  1 
ATOM   823  C C   . VAL   B 2 63  ? -12.906 -0.737  -3.422  1.00 35.44  ? 72  VAL   B C   1 
ATOM   824  O O   . VAL   B 2 63  ? -12.166 -0.492  -4.402  1.00 35.29  ? 72  VAL   B O   1 
ATOM   825  C CB  . VAL   B 2 63  ? -13.001 1.206   -1.802  1.00 35.94  ? 72  VAL   B CB  1 
ATOM   826  C CG1 . VAL   B 2 63  ? -11.563 1.478   -2.134  1.00 37.89  ? 72  VAL   B CG1 1 
ATOM   827  C CG2 . VAL   B 2 63  ? -13.688 2.532   -1.520  1.00 35.69  ? 72  VAL   B CG2 1 
ATOM   828  N N   . LYS   B 2 64  ? -13.004 -1.952  -2.894  1.00 36.18  ? 73  LYS   B N   1 
ATOM   829  C CA  . LYS   B 2 64  ? -12.021 -2.957  -3.401  1.00 36.86  ? 73  LYS   B CA  1 
ATOM   830  C C   . LYS   B 2 64  ? -12.484 -3.482  -4.782  1.00 37.66  ? 73  LYS   B C   1 
ATOM   831  O O   . LYS   B 2 64  ? -11.643 -3.630  -5.666  1.00 38.98  ? 73  LYS   B O   1 
ATOM   832  C CB  . LYS   B 2 64  ? -11.809 -4.104  -2.418  1.00 36.41  ? 73  LYS   B CB  1 
ATOM   833  C CG  . LYS   B 2 64  ? -10.805 -5.115  -2.983  1.00 38.11  ? 73  LYS   B CG  1 
ATOM   834  C CD  . LYS   B 2 64  ? -10.328 -6.077  -1.966  1.00 38.86  ? 73  LYS   B CD  1 
ATOM   835  C CE  . LYS   B 2 64  ? -9.197  -6.951  -2.477  1.00 41.74  ? 73  LYS   B CE  1 
ATOM   836  N NZ  . LYS   B 2 64  ? -9.020  -8.076  -1.537  1.00 42.74  ? 73  LYS   B NZ  1 
ATOM   837  N N   . GLN   B 2 65  ? -13.764 -3.850  -4.914  1.00 38.89  ? 74  GLN   B N   1 
ATOM   838  C CA  . GLN   B 2 65  ? -14.437 -4.199  -6.184  1.00 39.69  ? 74  GLN   B CA  1 
ATOM   839  C C   . GLN   B 2 65  ? -14.468 -3.003  -7.146  1.00 38.43  ? 74  GLN   B C   1 
ATOM   840  O O   . GLN   B 2 65  ? -14.597 -3.268  -8.349  1.00 36.32  ? 74  GLN   B O   1 
ATOM   841  C CB  . GLN   B 2 65  ? -15.874 -4.648  -5.948  1.00 40.44  ? 74  GLN   B CB  1 
ATOM   842  C CG  . GLN   B 2 65  ? -15.952 -5.960  -5.185  1.00 43.21  ? 74  GLN   B CG  1 
ATOM   843  C CD  . GLN   B 2 65  ? -17.385 -6.444  -5.066  1.00 46.45  ? 74  GLN   B CD  1 
ATOM   844  O OE1 . GLN   B 2 65  ? -18.158 -6.556  -6.037  1.00 50.37  ? 74  GLN   B OE1 1 
ATOM   845  N NE2 . GLN   B 2 65  ? -17.768 -6.717  -3.843  1.00 50.41  ? 74  GLN   B NE2 1 
ATOM   846  N N   . ASP   B 2 66  ? -14.445 -1.797  -6.579  1.00 38.01  ? 75  ASP   B N   1 
ATOM   847  C CA  . ASP   B 2 66  ? -14.487 -0.440  -7.190  1.00 38.12  ? 75  ASP   B CA  1 
ATOM   848  C C   . ASP   B 2 66  ? -15.817 -0.237  -7.886  1.00 36.30  ? 75  ASP   B C   1 
ATOM   849  O O   . ASP   B 2 66  ? -15.735 0.310   -8.998  1.00 36.40  ? 75  ASP   B O   1 
ATOM   850  C CB  . ASP   B 2 66  ? -13.340 -0.198  -8.189  1.00 40.41  ? 75  ASP   B CB  1 
ATOM   851  C CG  . ASP   B 2 66  ? -13.262 1.215   -8.757  1.00 40.74  ? 75  ASP   B CG  1 
ATOM   852  O OD1 . ASP   B 2 66  ? -13.566 2.191   -8.027  1.00 41.08  ? 75  ASP   B OD1 1 
ATOM   853  O OD2 . ASP   B 2 66  ? -12.884 1.338   -9.967  1.00 42.95  ? 75  ASP   B OD2 1 
ATOM   854  N N   . LEU   B 2 67  ? -16.938 -0.683  -7.273  1.00 33.69  ? 76  LEU   B N   1 
ATOM   855  C CA  . LEU   B 2 67  ? -18.327 -0.595  -7.796  1.00 31.77  ? 76  LEU   B CA  1 
ATOM   856  C C   . LEU   B 2 67  ? -19.211 0.168   -6.817  1.00 33.46  ? 76  LEU   B C   1 
ATOM   857  O O   . LEU   B 2 67  ? -18.967 0.086   -5.574  1.00 33.58  ? 76  LEU   B O   1 
ATOM   858  C CB  . LEU   B 2 67  ? -18.839 -2.013  -8.009  1.00 32.30  ? 76  LEU   B CB  1 
ATOM   859  C CG  . LEU   B 2 67  ? -18.135 -2.790  -9.136  1.00 32.96  ? 76  LEU   B CG  1 
ATOM   860  C CD1 . LEU   B 2 67  ? -18.739 -4.182  -9.248  1.00 33.07  ? 76  LEU   B CD1 1 
ATOM   861  C CD2 . LEU   B 2 67  ? -18.276 -2.070  -10.488 1.00 35.05  ? 76  LEU   B CD2 1 
ATOM   862  N N   . VAL   B 2 68  ? -20.302 0.747   -7.337  1.00 32.93  ? 77  VAL   B N   1 
ATOM   863  C CA  . VAL   B 2 68  ? -21.320 1.433   -6.503  1.00 31.68  ? 77  VAL   B CA  1 
ATOM   864  C C   . VAL   B 2 68  ? -22.650 1.455   -7.245  1.00 30.59  ? 77  VAL   B C   1 
ATOM   865  O O   . VAL   B 2 68  ? -22.601 1.623   -8.504  1.00 31.01  ? 77  VAL   B O   1 
ATOM   866  C CB  . VAL   B 2 68  ? -20.822 2.844   -6.188  1.00 32.59  ? 77  VAL   B CB  1 
ATOM   867  C CG1 . VAL   B 2 68  ? -20.576 3.649   -7.451  1.00 33.29  ? 77  VAL   B CG1 1 
ATOM   868  C CG2 . VAL   B 2 68  ? -21.803 3.546   -5.259  1.00 31.83  ? 77  VAL   B CG2 1 
ATOM   869  N N   . SER   B 2 69  ? -23.764 1.273   -6.530  1.00 30.91  ? 78  SER   B N   1 
ATOM   870  C CA  . SER   B 2 69  ? -25.123 1.242   -7.078  1.00 31.77  ? 78  SER   B CA  1 
ATOM   871  C C   . SER   B 2 69  ? -25.911 2.360   -6.397  1.00 31.92  ? 78  SER   B C   1 
ATOM   872  O O   . SER   B 2 69  ? -25.588 2.659   -5.184  1.00 29.90  ? 78  SER   B O   1 
ATOM   873  C CB  . SER   B 2 69  ? -25.769 -0.150  -6.935  1.00 32.96  ? 78  SER   B CB  1 
ATOM   874  O OG  . SER   B 2 69  ? -26.278 -0.391  -5.613  1.00 35.11  ? 78  SER   B OG  1 
ATOM   875  N N   . TYR   B 2 70  ? -26.923 2.876   -7.096  1.00 32.62  ? 79  TYR   B N   1 
ATOM   876  C CA  . TYR   B 2 70  ? -27.730 4.061   -6.680  1.00 31.92  ? 79  TYR   B CA  1 
ATOM   877  C C   . TYR   B 2 70  ? -29.184 3.645   -6.807  1.00 33.52  ? 79  TYR   B C   1 
ATOM   878  O O   . TYR   B 2 70  ? -29.495 3.005   -7.836  1.00 31.08  ? 79  TYR   B O   1 
ATOM   879  C CB  . TYR   B 2 70  ? -27.382 5.274   -7.536  1.00 33.94  ? 79  TYR   B CB  1 
ATOM   880  C CG  . TYR   B 2 70  ? -26.045 5.930   -7.243  1.00 33.06  ? 79  TYR   B CG  1 
ATOM   881  C CD1 . TYR   B 2 70  ? -24.869 5.457   -7.772  1.00 33.63  ? 79  TYR   B CD1 1 
ATOM   882  C CD2 . TYR   B 2 70  ? -25.945 7.001   -6.362  1.00 35.35  ? 79  TYR   B CD2 1 
ATOM   883  C CE1 . TYR   B 2 70  ? -23.643 6.031   -7.462  1.00 32.42  ? 79  TYR   B CE1 1 
ATOM   884  C CE2 . TYR   B 2 70  ? -24.733 7.628   -6.065  1.00 34.06  ? 79  TYR   B CE2 1 
ATOM   885  C CZ  . TYR   B 2 70  ? -23.574 7.141   -6.641  1.00 32.02  ? 79  TYR   B CZ  1 
ATOM   886  O OH  . TYR   B 2 70  ? -22.358 7.716   -6.355  1.00 36.73  ? 79  TYR   B OH  1 
ATOM   887  N N   . CYS   B 2 71  ? -29.988 3.901   -5.763  1.00 34.18  ? 80  CYS   B N   1 
ATOM   888  C CA  . CYS   B 2 71  ? -31.456 3.704   -5.698  1.00 36.43  ? 80  CYS   B CA  1 
ATOM   889  C C   . CYS   B 2 71  ? -31.801 2.271   -5.367  1.00 37.22  ? 80  CYS   B C   1 
ATOM   890  O O   . CYS   B 2 71  ? -32.975 1.981   -5.066  1.00 37.98  ? 80  CYS   B O   1 
ATOM   891  C CB  . CYS   B 2 71  ? -32.130 4.106   -6.995  1.00 41.50  ? 80  CYS   B CB  1 
ATOM   892  S SG  . CYS   B 2 71  ? -31.673 5.812   -7.421  1.00 46.26  ? 80  CYS   B SG  1 
ATOM   893  N N   . GLY   B 2 72  ? -30.825 1.369   -5.407  1.00 36.58  ? 81  GLY   B N   1 
ATOM   894  C CA  . GLY   B 2 72  ? -31.207 -0.041  -5.272  1.00 35.86  ? 81  GLY   B CA  1 
ATOM   895  C C   . GLY   B 2 72  ? -29.960 -0.894  -5.315  1.00 34.49  ? 81  GLY   B C   1 
ATOM   896  O O   . GLY   B 2 72  ? -28.847 -0.374  -5.530  1.00 31.57  ? 81  GLY   B O   1 
ATOM   897  N N   . PRO   B 2 73  ? -30.102 -2.193  -5.020  1.00 34.53  ? 82  PRO   B N   1 
ATOM   898  C CA  . PRO   B 2 73  ? -28.947 -3.094  -5.060  1.00 37.03  ? 82  PRO   B CA  1 
ATOM   899  C C   . PRO   B 2 73  ? -28.443 -3.341  -6.498  1.00 37.98  ? 82  PRO   B C   1 
ATOM   900  O O   . PRO   B 2 73  ? -29.235 -3.212  -7.443  1.00 38.60  ? 82  PRO   B O   1 
ATOM   901  C CB  . PRO   B 2 73  ? -29.512 -4.398  -4.452  1.00 36.54  ? 82  PRO   B CB  1 
ATOM   902  C CG  . PRO   B 2 73  ? -31.006 -4.335  -4.742  1.00 37.19  ? 82  PRO   B CG  1 
ATOM   903  C CD  . PRO   B 2 73  ? -31.353 -2.870  -4.645  1.00 36.97  ? 82  PRO   B CD  1 
ATOM   904  N N   . TRP   B 2 74  ? -27.180 -3.751  -6.636  1.00 37.85  ? 83  TRP   B N   1 
ATOM   905  C CA  . TRP   B 2 74  ? -26.570 -4.190  -7.908  1.00 38.39  ? 83  TRP   B CA  1 
ATOM   906  C C   . TRP   B 2 74  ? -27.509 -5.158  -8.639  1.00 40.10  ? 83  TRP   B C   1 
ATOM   907  O O   . TRP   B 2 74  ? -27.808 -6.186  -8.060  1.00 39.69  ? 83  TRP   B O   1 
ATOM   908  C CB  . TRP   B 2 74  ? -25.199 -4.811  -7.650  1.00 38.47  ? 83  TRP   B CB  1 
ATOM   909  C CG  . TRP   B 2 74  ? -24.356 -4.956  -8.884  1.00 36.57  ? 83  TRP   B CG  1 
ATOM   910  C CD1 . TRP   B 2 74  ? -24.264 -6.064  -9.667  1.00 35.63  ? 83  TRP   B CD1 1 
ATOM   911  C CD2 . TRP   B 2 74  ? -23.518 -3.949  -9.498  1.00 36.29  ? 83  TRP   B CD2 1 
ATOM   912  N NE1 . TRP   B 2 74  ? -23.412 -5.824  -10.711 1.00 35.72  ? 83  TRP   B NE1 1 
ATOM   913  C CE2 . TRP   B 2 74  ? -22.936 -4.542  -10.640 1.00 35.16  ? 83  TRP   B CE2 1 
ATOM   914  C CE3 . TRP   B 2 74  ? -23.194 -2.609  -9.200  1.00 35.77  ? 83  TRP   B CE3 1 
ATOM   915  C CZ2 . TRP   B 2 74  ? -22.108 -3.844  -11.524 1.00 35.16  ? 83  TRP   B CZ2 1 
ATOM   916  C CZ3 . TRP   B 2 74  ? -22.346 -1.930  -10.049 1.00 34.97  ? 83  TRP   B CZ3 1 
ATOM   917  C CH2 . TRP   B 2 74  ? -21.793 -2.554  -11.188 1.00 34.74  ? 83  TRP   B CH2 1 
ATOM   918  N N   . LYS   B 2 75  ? -27.806 -4.896  -9.923  1.00 40.81  ? 84  LYS   B N   1 
ATOM   919  C CA  . LYS   B 2 75  ? -28.736 -5.691  -10.780 1.00 41.32  ? 84  LYS   B CA  1 
ATOM   920  C C   . LYS   B 2 75  ? -28.005 -6.514  -11.858 1.00 42.22  ? 84  LYS   B C   1 
ATOM   921  O O   . LYS   B 2 75  ? -28.643 -7.414  -12.374 1.00 45.74  ? 84  LYS   B O   1 
ATOM   922  C CB  . LYS   B 2 75  ? -29.692 -4.725  -11.468 1.00 42.13  ? 84  LYS   B CB  1 
ATOM   923  C CG  . LYS   B 2 75  ? -30.552 -3.936  -10.517 1.00 43.45  ? 84  LYS   B CG  1 
ATOM   924  C CD  . LYS   B 2 75  ? -31.596 -4.761  -9.842  1.00 45.64  ? 84  LYS   B CD  1 
ATOM   925  C CE  . LYS   B 2 75  ? -32.224 -3.968  -8.722  1.00 48.39  ? 84  LYS   B CE  1 
ATOM   926  N NZ  . LYS   B 2 75  ? -33.655 -4.308  -8.571  1.00 51.51  ? 84  LYS   B NZ  1 
ATOM   927  N N   . LEU   B 2 76  ? -26.744 -6.239  -12.191 1.00 42.58  ? 85  LEU   B N   1 
ATOM   928  C CA  . LEU   B 2 76  ? -26.049 -6.781  -13.393 1.00 44.10  ? 85  LEU   B CA  1 
ATOM   929  C C   . LEU   B 2 76  ? -25.325 -8.076  -13.008 1.00 45.86  ? 85  LEU   B C   1 
ATOM   930  O O   . LEU   B 2 76  ? -24.332 -7.996  -12.207 1.00 43.91  ? 85  LEU   B O   1 
ATOM   931  C CB  . LEU   B 2 76  ? -25.069 -5.728  -13.925 1.00 45.72  ? 85  LEU   B CB  1 
ATOM   932  C CG  . LEU   B 2 76  ? -25.645 -4.313  -14.078 1.00 44.71  ? 85  LEU   B CG  1 
ATOM   933  C CD1 . LEU   B 2 76  ? -24.628 -3.336  -14.643 1.00 45.23  ? 85  LEU   B CD1 1 
ATOM   934  C CD2 . LEU   B 2 76  ? -26.874 -4.315  -14.958 1.00 47.69  ? 85  LEU   B CD2 1 
ATOM   935  N N   . ASP   B 2 77  ? -25.807 -9.218  -13.509 1.00 48.31  ? 86  ASP   B N   1 
ATOM   936  C CA  . ASP   B 2 77  ? -25.265 -10.538 -13.088 1.00 56.32  ? 86  ASP   B CA  1 
ATOM   937  C C   . ASP   B 2 77  ? -24.698 -11.341 -14.273 1.00 55.32  ? 86  ASP   B C   1 
ATOM   938  O O   . ASP   B 2 77  ? -24.265 -12.470 -14.047 1.00 54.85  ? 86  ASP   B O   1 
ATOM   939  C CB  . ASP   B 2 77  ? -26.310 -11.359 -12.328 1.00 61.87  ? 86  ASP   B CB  1 
ATOM   940  C CG  . ASP   B 2 77  ? -27.586 -11.553 -13.113 1.00 68.32  ? 86  ASP   B CG  1 
ATOM   941  O OD1 . ASP   B 2 77  ? -27.657 -11.010 -14.223 1.00 76.93  ? 86  ASP   B OD1 1 
ATOM   942  O OD2 . ASP   B 2 77  ? -28.508 -12.207 -12.596 1.00 73.88  ? 86  ASP   B OD2 1 
ATOM   943  N N   . ALA   B 2 78  ? -24.640 -10.795 -15.482 1.00 52.28  ? 87  ALA   B N   1 
ATOM   944  C CA  . ALA   B 2 78  ? -24.133 -11.527 -16.650 1.00 50.09  ? 87  ALA   B CA  1 
ATOM   945  C C   . ALA   B 2 78  ? -22.604 -11.624 -16.531 1.00 48.70  ? 87  ALA   B C   1 
ATOM   946  O O   . ALA   B 2 78  ? -21.953 -10.663 -15.951 1.00 44.93  ? 87  ALA   B O   1 
ATOM   947  C CB  . ALA   B 2 78  ? -24.593 -10.862 -17.945 1.00 50.52  ? 87  ALA   B CB  1 
ATOM   948  N N   . ALA   B 2 79  ? -22.041 -12.701 -17.102 1.00 45.99  ? 88  ALA   B N   1 
ATOM   949  C CA  . ALA   B 2 79  ? -20.603 -13.041 -17.021 1.00 47.20  ? 88  ALA   B CA  1 
ATOM   950  C C   . ALA   B 2 79  ? -19.989 -13.283 -18.414 1.00 45.98  ? 88  ALA   B C   1 
ATOM   951  O O   . ALA   B 2 79  ? -20.645 -13.948 -19.226 1.00 46.01  ? 88  ALA   B O   1 
ATOM   952  C CB  . ALA   B 2 79  ? -20.475 -14.267 -16.131 1.00 47.83  ? 88  ALA   B CB  1 
ATOM   953  N N   . TRP   B 2 80  ? -18.767 -12.788 -18.681 1.00 46.46  ? 89  TRP   B N   1 
ATOM   954  C CA  . TRP   B 2 80  ? -17.916 -13.193 -19.835 1.00 50.63  ? 89  TRP   B CA  1 
ATOM   955  C C   . TRP   B 2 80  ? -17.848 -14.713 -19.813 1.00 51.48  ? 89  TRP   B C   1 
ATOM   956  O O   . TRP   B 2 80  ? -17.774 -15.255 -18.678 1.00 48.34  ? 89  TRP   B O   1 
ATOM   957  C CB  . TRP   B 2 80  ? -16.498 -12.589 -19.830 1.00 52.50  ? 89  TRP   B CB  1 
ATOM   958  C CG  . TRP   B 2 80  ? -15.671 -12.978 -21.029 1.00 52.83  ? 89  TRP   B CG  1 
ATOM   959  C CD1 . TRP   B 2 80  ? -16.093 -13.062 -22.326 1.00 53.81  ? 89  TRP   B CD1 1 
ATOM   960  C CD2 . TRP   B 2 80  ? -14.275 -13.346 -21.047 1.00 54.02  ? 89  TRP   B CD2 1 
ATOM   961  N NE1 . TRP   B 2 80  ? -15.066 -13.460 -23.140 1.00 54.37  ? 89  TRP   B NE1 1 
ATOM   962  C CE2 . TRP   B 2 80  ? -13.939 -13.652 -22.387 1.00 53.30  ? 89  TRP   B CE2 1 
ATOM   963  C CE3 . TRP   B 2 80  ? -13.283 -13.487 -20.065 1.00 52.96  ? 89  TRP   B CE3 1 
ATOM   964  C CZ2 . TRP   B 2 80  ? -12.663 -14.061 -22.774 1.00 52.67  ? 89  TRP   B CZ2 1 
ATOM   965  C CZ3 . TRP   B 2 80  ? -12.018 -13.901 -20.454 1.00 52.90  ? 89  TRP   B CZ3 1 
ATOM   966  C CH2 . TRP   B 2 80  ? -11.715 -14.181 -21.787 1.00 52.23  ? 89  TRP   B CH2 1 
ATOM   967  N N   . ASP   B 2 81  ? -18.019 -15.351 -20.978 1.00 53.60  ? 90  ASP   B N   1 
ATOM   968  C CA  . ASP   B 2 81  ? -18.093 -16.840 -21.054 1.00 55.88  ? 90  ASP   B CA  1 
ATOM   969  C C   . ASP   B 2 81  ? -16.672 -17.394 -21.159 1.00 55.91  ? 90  ASP   B C   1 
ATOM   970  O O   . ASP   B 2 81  ? -16.567 -18.594 -21.151 1.00 58.39  ? 90  ASP   B O   1 
ATOM   971  C CB  . ASP   B 2 81  ? -19.033 -17.336 -22.166 1.00 55.16  ? 90  ASP   B CB  1 
ATOM   972  C CG  . ASP   B 2 81  ? -18.561 -17.056 -23.557 1.00 55.53  ? 90  ASP   B CG  1 
ATOM   973  O OD1 . ASP   B 2 81  ? -17.543 -16.372 -23.712 1.00 59.54  ? 90  ASP   B OD1 1 
ATOM   974  O OD2 . ASP   B 2 81  ? -19.250 -17.470 -24.495 1.00 63.45  ? 90  ASP   B OD2 1 
ATOM   975  N N   . GLY   B 2 82  ? -15.656 -16.530 -21.268 1.00 57.43  ? 91  GLY   B N   1 
ATOM   976  C CA  . GLY   B 2 82  ? -14.225 -16.883 -21.356 1.00 57.96  ? 91  GLY   B CA  1 
ATOM   977  C C   . GLY   B 2 82  ? -13.778 -17.285 -22.764 1.00 60.06  ? 91  GLY   B C   1 
ATOM   978  O O   . GLY   B 2 82  ? -12.610 -17.709 -22.890 1.00 59.09  ? 91  GLY   B O   1 
ATOM   979  N N   . LEU   B 2 83  ? -14.657 -17.174 -23.778 1.00 60.92  ? 92  LEU   B N   1 
ATOM   980  C CA  . LEU   B 2 83  ? -14.416 -17.601 -25.191 1.00 63.27  ? 92  LEU   B CA  1 
ATOM   981  C C   . LEU   B 2 83  ? -14.763 -16.487 -26.197 1.00 65.90  ? 92  LEU   B C   1 
ATOM   982  O O   . LEU   B 2 83  ? -13.933 -16.174 -27.078 1.00 65.58  ? 92  LEU   B O   1 
ATOM   983  C CB  . LEU   B 2 83  ? -15.315 -18.799 -25.479 1.00 65.45  ? 92  LEU   B CB  1 
ATOM   984  C CG  . LEU   B 2 83  ? -14.847 -20.151 -24.951 1.00 68.30  ? 92  LEU   B CG  1 
ATOM   985  C CD1 . LEU   B 2 83  ? -15.836 -21.215 -25.392 1.00 70.71  ? 92  LEU   B CD1 1 
ATOM   986  C CD2 . LEU   B 2 83  ? -13.444 -20.502 -25.440 1.00 69.96  ? 92  LEU   B CD2 1 
ATOM   987  N N   . SER   B 2 84  ? -15.996 -15.991 -26.147 1.00 64.37  ? 93  SER   B N   1 
ATOM   988  C CA  . SER   B 2 84  ? -16.619 -15.150 -27.203 1.00 62.25  ? 93  SER   B CA  1 
ATOM   989  C C   . SER   B 2 84  ? -16.050 -13.722 -27.137 1.00 61.57  ? 93  SER   B C   1 
ATOM   990  O O   . SER   B 2 84  ? -15.525 -13.318 -26.062 1.00 62.12  ? 93  SER   B O   1 
ATOM   991  C CB  . SER   B 2 84  ? -18.110 -15.178 -27.054 1.00 62.03  ? 93  SER   B CB  1 
ATOM   992  O OG  . SER   B 2 84  ? -18.510 -16.233 -26.165 1.00 61.92  ? 93  SER   B OG  1 
ATOM   993  N N   . GLU   B 2 85  ? -16.053 -13.012 -28.265 1.00 59.54  ? 94  GLU   B N   1 
ATOM   994  C CA  . GLU   B 2 85  ? -15.664 -11.580 -28.308 1.00 57.78  ? 94  GLU   B CA  1 
ATOM   995  C C   . GLU   B 2 85  ? -16.768 -10.821 -27.552 1.00 51.52  ? 94  GLU   B C   1 
ATOM   996  O O   . GLU   B 2 85  ? -17.864 -11.365 -27.270 1.00 45.78  ? 94  GLU   B O   1 
ATOM   997  C CB  . GLU   B 2 85  ? -15.415 -11.073 -29.746 1.00 63.31  ? 94  GLU   B CB  1 
ATOM   998  C CG  . GLU   B 2 85  ? -14.005 -11.373 -30.321 1.00 63.96  ? 94  GLU   B CG  1 
ATOM   999  C CD  . GLU   B 2 85  ? -13.609 -10.831 -31.709 1.00 68.73  ? 94  GLU   B CD  1 
ATOM   1000 O OE1 . GLU   B 2 85  ? -14.284 -9.900  -32.253 1.00 64.01  ? 94  GLU   B OE1 1 
ATOM   1001 O OE2 . GLU   B 2 85  ? -12.598 -11.342 -32.281 1.00 69.26  ? 94  GLU   B OE2 1 
ATOM   1002 N N   . VAL   B 2 86  ? -16.459 -9.604  -27.167 1.00 49.45  ? 95  VAL   B N   1 
ATOM   1003 C CA  . VAL   B 2 86  ? -17.404 -8.736  -26.411 1.00 45.83  ? 95  VAL   B CA  1 
ATOM   1004 C C   . VAL   B 2 86  ? -17.390 -7.383  -27.084 1.00 43.99  ? 95  VAL   B C   1 
ATOM   1005 O O   . VAL   B 2 86  ? -16.473 -7.167  -27.888 1.00 46.36  ? 95  VAL   B O   1 
ATOM   1006 C CB  . VAL   B 2 86  ? -16.976 -8.591  -24.931 1.00 43.26  ? 95  VAL   B CB  1 
ATOM   1007 C CG1 . VAL   B 2 86  ? -16.781 -9.932  -24.282 1.00 43.14  ? 95  VAL   B CG1 1 
ATOM   1008 C CG2 . VAL   B 2 86  ? -15.700 -7.778  -24.806 1.00 44.03  ? 95  VAL   B CG2 1 
ATOM   1009 N N   . GLN   B 2 87  ? -18.249 -6.461  -26.637 1.00 44.26  ? 96  GLN   B N   1 
ATOM   1010 C CA  . GLN   B 2 87  ? -18.160 -5.035  -27.072 1.00 45.31  ? 96  GLN   B CA  1 
ATOM   1011 C C   . GLN   B 2 87  ? -18.069 -4.082  -25.872 1.00 43.32  ? 96  GLN   B C   1 
ATOM   1012 O O   . GLN   B 2 87  ? -18.923 -4.145  -25.014 1.00 45.13  ? 96  GLN   B O   1 
ATOM   1013 C CB  . GLN   B 2 87  ? -19.344 -4.683  -27.992 1.00 46.13  ? 96  GLN   B CB  1 
ATOM   1014 C CG  . GLN   B 2 87  ? -19.231 -5.334  -29.362 1.00 48.52  ? 96  GLN   B CG  1 
ATOM   1015 C CD  . GLN   B 2 87  ? -20.290 -4.935  -30.384 1.00 50.85  ? 96  GLN   B CD  1 
ATOM   1016 O OE1 . GLN   B 2 87  ? -21.090 -4.005  -30.193 1.00 47.15  ? 96  GLN   B OE1 1 
ATOM   1017 N NE2 . GLN   B 2 87  ? -20.303 -5.664  -31.488 1.00 50.97  ? 96  GLN   B NE2 1 
ATOM   1018 N N   . LEU   B 2 88  ? -17.050 -3.230  -25.855 1.00 42.02  ? 97  LEU   B N   1 
ATOM   1019 C CA  . LEU   B 2 88  ? -16.974 -2.020  -25.020 1.00 41.79  ? 97  LEU   B CA  1 
ATOM   1020 C C   . LEU   B 2 88  ? -17.870 -0.958  -25.680 1.00 42.34  ? 97  LEU   B C   1 
ATOM   1021 O O   . LEU   B 2 88  ? -17.530 -0.437  -26.767 1.00 42.82  ? 97  LEU   B O   1 
ATOM   1022 C CB  . LEU   B 2 88  ? -15.531 -1.504  -24.931 1.00 42.01  ? 97  LEU   B CB  1 
ATOM   1023 C CG  . LEU   B 2 88  ? -15.366 -0.185  -24.185 1.00 42.94  ? 97  LEU   B CG  1 
ATOM   1024 C CD1 . LEU   B 2 88  ? -15.782 -0.322  -22.717 1.00 45.06  ? 97  LEU   B CD1 1 
ATOM   1025 C CD2 . LEU   B 2 88  ? -13.941 0.340   -24.260 1.00 44.02  ? 97  LEU   B CD2 1 
ATOM   1026 N N   A LEU   B 2 89  ? -19.003 -0.654  -25.051 0.25 41.19  ? 98  LEU   B N   1 
ATOM   1027 N N   B LEU   B 2 89  ? -19.003 -0.654  -25.051 0.25 41.19  ? 98  LEU   B N   1 
ATOM   1028 N N   C LEU   B 2 89  ? -19.000 -0.655  -25.044 0.25 41.61  ? 98  LEU   B N   1 
ATOM   1029 N N   D LEU   B 2 89  ? -19.000 -0.655  -25.044 0.25 41.61  ? 98  LEU   B N   1 
ATOM   1030 C CA  A LEU   B 2 89  ? -19.843 0.508   -25.425 0.25 40.67  ? 98  LEU   B CA  1 
ATOM   1031 C CA  B LEU   B 2 89  ? -19.843 0.508   -25.425 0.25 40.67  ? 98  LEU   B CA  1 
ATOM   1032 C CA  C LEU   B 2 89  ? -19.851 0.506   -25.396 0.25 41.32  ? 98  LEU   B CA  1 
ATOM   1033 C CA  D LEU   B 2 89  ? -19.851 0.506   -25.396 0.25 41.32  ? 98  LEU   B CA  1 
ATOM   1034 C C   A LEU   B 2 89  ? -19.190 1.723   -24.774 0.25 41.44  ? 98  LEU   B C   1 
ATOM   1035 C C   B LEU   B 2 89  ? -19.190 1.723   -24.774 0.25 41.44  ? 98  LEU   B C   1 
ATOM   1036 C C   C LEU   B 2 89  ? -19.186 1.725   -24.764 0.25 41.84  ? 98  LEU   B C   1 
ATOM   1037 C C   D LEU   B 2 89  ? -19.186 1.725   -24.764 0.25 41.84  ? 98  LEU   B C   1 
ATOM   1038 O O   A LEU   B 2 89  ? -19.665 2.163   -23.706 0.25 41.80  ? 98  LEU   B O   1 
ATOM   1039 O O   B LEU   B 2 89  ? -19.665 2.163   -23.706 0.25 41.80  ? 98  LEU   B O   1 
ATOM   1040 O O   C LEU   B 2 89  ? -19.653 2.177   -23.697 0.25 42.19  ? 98  LEU   B O   1 
ATOM   1041 O O   D LEU   B 2 89  ? -19.653 2.177   -23.697 0.25 42.19  ? 98  LEU   B O   1 
ATOM   1042 C CB  A LEU   B 2 89  ? -21.279 0.246   -24.969 0.25 40.13  ? 98  LEU   B CB  1 
ATOM   1043 C CB  B LEU   B 2 89  ? -21.279 0.246   -24.969 0.25 40.13  ? 98  LEU   B CB  1 
ATOM   1044 C CB  C LEU   B 2 89  ? -21.268 0.243   -24.883 0.25 41.28  ? 98  LEU   B CB  1 
ATOM   1045 C CB  D LEU   B 2 89  ? -21.268 0.243   -24.883 0.25 41.28  ? 98  LEU   B CB  1 
ATOM   1046 C CG  A LEU   B 2 89  ? -22.294 1.379   -25.151 0.25 39.71  ? 98  LEU   B CG  1 
ATOM   1047 C CG  B LEU   B 2 89  ? -22.294 1.379   -25.151 0.25 39.71  ? 98  LEU   B CG  1 
ATOM   1048 C CG  C LEU   B 2 89  ? -22.302 1.360   -25.056 0.25 41.30  ? 98  LEU   B CG  1 
ATOM   1049 C CG  D LEU   B 2 89  ? -22.302 1.360   -25.056 0.25 41.30  ? 98  LEU   B CG  1 
ATOM   1050 C CD1 A LEU   B 2 89  ? -21.739 2.516   -25.982 0.25 39.82  ? 98  LEU   B CD1 1 
ATOM   1051 C CD1 B LEU   B 2 89  ? -21.739 2.516   -25.982 0.25 39.82  ? 98  LEU   B CD1 1 
ATOM   1052 C CD1 C LEU   B 2 89  ? -22.337 1.883   -26.477 0.25 41.73  ? 98  LEU   B CD1 1 
ATOM   1053 C CD1 D LEU   B 2 89  ? -22.337 1.883   -26.477 0.25 41.73  ? 98  LEU   B CD1 1 
ATOM   1054 C CD2 A LEU   B 2 89  ? -23.592 0.856   -25.748 0.25 39.57  ? 98  LEU   B CD2 1 
ATOM   1055 C CD2 B LEU   B 2 89  ? -23.592 0.856   -25.748 0.25 39.57  ? 98  LEU   B CD2 1 
ATOM   1056 C CD2 C LEU   B 2 89  ? -23.687 0.872   -24.643 0.25 41.07  ? 98  LEU   B CD2 1 
ATOM   1057 C CD2 D LEU   B 2 89  ? -23.687 0.872   -24.643 0.25 41.07  ? 98  LEU   B CD2 1 
ATOM   1058 N N   . ALA   B 2 90  ? -18.088 2.186   -25.373 1.00 42.62  ? 99  ALA   B N   1 
ATOM   1059 C CA  . ALA   B 2 90  ? -17.337 3.377   -24.908 1.00 43.11  ? 99  ALA   B CA  1 
ATOM   1060 C C   . ALA   B 2 90  ? -18.204 4.618   -25.065 1.00 45.44  ? 99  ALA   B C   1 
ATOM   1061 O O   . ALA   B 2 90  ? -18.820 4.754   -26.147 1.00 44.67  ? 99  ALA   B O   1 
ATOM   1062 C CB  . ALA   B 2 90  ? -16.067 3.590   -25.678 1.00 43.91  ? 99  ALA   B CB  1 
ATOM   1063 N N   . VAL   B 2 91  ? -18.213 5.460   -24.017 1.00 44.42  ? 100 VAL   B N   1 
ATOM   1064 C CA  . VAL   B 2 91  ? -18.772 6.834   -24.034 1.00 41.91  ? 100 VAL   B CA  1 
ATOM   1065 C C   . VAL   B 2 91  ? -17.663 7.802   -23.634 1.00 42.50  ? 100 VAL   B C   1 
ATOM   1066 O O   . VAL   B 2 91  ? -17.598 8.253   -22.502 1.00 39.89  ? 100 VAL   B O   1 
ATOM   1067 C CB  . VAL   B 2 91  ? -19.975 6.867   -23.107 1.00 41.93  ? 100 VAL   B CB  1 
ATOM   1068 C CG1 . VAL   B 2 91  ? -20.626 8.246   -23.067 1.00 43.24  ? 100 VAL   B CG1 1 
ATOM   1069 C CG2 . VAL   B 2 91  ? -20.969 5.781   -23.508 1.00 41.47  ? 100 VAL   B CG2 1 
ATOM   1070 N N   . PRO   B 2 92  ? -16.776 8.194   -24.575 1.00 44.21  ? 101 PRO   B N   1 
ATOM   1071 C CA  . PRO   B 2 92  ? -15.701 9.125   -24.257 1.00 44.64  ? 101 PRO   B CA  1 
ATOM   1072 C C   . PRO   B 2 92  ? -16.193 10.541  -24.026 1.00 44.68  ? 101 PRO   B C   1 
ATOM   1073 O O   . PRO   B 2 92  ? -17.265 10.909  -24.506 1.00 45.95  ? 101 PRO   B O   1 
ATOM   1074 C CB  . PRO   B 2 92  ? -14.723 9.028   -25.442 1.00 46.20  ? 101 PRO   B CB  1 
ATOM   1075 C CG  . PRO   B 2 92  ? -15.327 8.027   -26.433 1.00 46.59  ? 101 PRO   B CG  1 
ATOM   1076 C CD  . PRO   B 2 92  ? -16.717 7.689   -25.955 1.00 45.63  ? 101 PRO   B CD  1 
ATOM   1077 N N   . PRO   B 2 93  ? -15.414 11.374  -23.296 1.00 45.63  ? 102 PRO   B N   1 
ATOM   1078 C CA  . PRO   B 2 93  ? -15.783 12.766  -23.053 1.00 49.48  ? 102 PRO   B CA  1 
ATOM   1079 C C   . PRO   B 2 93  ? -15.961 13.531  -24.377 1.00 51.62  ? 102 PRO   B C   1 
ATOM   1080 O O   . PRO   B 2 93  ? -15.126 13.393  -25.246 1.00 56.52  ? 102 PRO   B O   1 
ATOM   1081 C CB  . PRO   B 2 93  ? -14.632 13.284  -22.165 1.00 48.27  ? 102 PRO   B CB  1 
ATOM   1082 C CG  . PRO   B 2 93  ? -14.162 12.018  -21.461 1.00 49.32  ? 102 PRO   B CG  1 
ATOM   1083 C CD  . PRO   B 2 93  ? -14.170 11.016  -22.596 1.00 48.83  ? 102 PRO   B CD  1 
ATOM   1084 N N   . GLY   B 2 94  ? -17.087 14.233  -24.512 1.00 51.41  ? 103 GLY   B N   1 
ATOM   1085 C CA  . GLY   B 2 94  ? -17.484 15.036  -25.687 1.00 51.94  ? 103 GLY   B CA  1 
ATOM   1086 C C   . GLY   B 2 94  ? -17.760 14.249  -26.972 1.00 50.96  ? 103 GLY   B C   1 
ATOM   1087 O O   . GLY   B 2 94  ? -17.928 14.877  -28.004 1.00 54.97  ? 103 GLY   B O   1 
ATOM   1088 N N   . GLU   B 2 95  ? -17.838 12.929  -26.957 1.00 49.64  ? 104 GLU   B N   1 
ATOM   1089 C CA  . GLU   B 2 95  ? -17.878 12.115  -28.202 1.00 50.26  ? 104 GLU   B CA  1 
ATOM   1090 C C   . GLU   B 2 95  ? -19.058 11.151  -28.105 1.00 51.08  ? 104 GLU   B C   1 
ATOM   1091 O O   . GLU   B 2 95  ? -19.480 10.830  -26.980 1.00 52.91  ? 104 GLU   B O   1 
ATOM   1092 C CB  . GLU   B 2 95  ? -16.535 11.383  -28.403 1.00 52.25  ? 104 GLU   B CB  1 
ATOM   1093 C CG  . GLU   B 2 95  ? -15.320 12.321  -28.586 1.00 55.18  ? 104 GLU   B CG  1 
ATOM   1094 C CD  . GLU   B 2 95  ? -13.929 11.663  -28.653 1.00 58.70  ? 104 GLU   B CD  1 
ATOM   1095 O OE1 . GLU   B 2 95  ? -13.869 10.435  -28.478 1.00 59.27  ? 104 GLU   B OE1 1 
ATOM   1096 O OE2 . GLU   B 2 95  ? -12.874 12.376  -28.887 1.00 61.74  ? 104 GLU   B OE2 1 
ATOM   1097 N N   . ARG   B 2 96  ? -19.627 10.725  -29.217 1.00 51.42  ? 105 ARG   B N   1 
ATOM   1098 C CA  . ARG   B 2 96  ? -20.873 9.923   -29.208 1.00 54.40  ? 105 ARG   B CA  1 
ATOM   1099 C C   . ARG   B 2 96  ? -20.555 8.556   -28.628 1.00 53.14  ? 105 ARG   B C   1 
ATOM   1100 O O   . ARG   B 2 96  ? -19.400 8.109   -28.804 1.00 53.42  ? 105 ARG   B O   1 
ATOM   1101 C CB  . ARG   B 2 96  ? -21.418 9.811   -30.635 1.00 62.11  ? 105 ARG   B CB  1 
ATOM   1102 C CG  . ARG   B 2 96  ? -22.788 9.156   -30.740 1.00 67.38  ? 105 ARG   B CG  1 
ATOM   1103 C CD  . ARG   B 2 96  ? -23.624 9.728   -31.887 1.00 71.50  ? 105 ARG   B CD  1 
ATOM   1104 N NE  . ARG   B 2 96  ? -22.929 9.761   -33.171 1.00 72.49  ? 105 ARG   B NE  1 
ATOM   1105 C CZ  . ARG   B 2 96  ? -22.343 10.825  -33.747 1.00 77.02  ? 105 ARG   B CZ  1 
ATOM   1106 N NH1 . ARG   B 2 96  ? -22.358 12.025  -33.191 1.00 76.65  ? 105 ARG   B NH1 1 
ATOM   1107 N NH2 . ARG   B 2 96  ? -21.740 10.681  -34.921 1.00 80.10  ? 105 ARG   B NH2 1 
ATOM   1108 N N   . ALA   B 2 97  ? -21.524 7.909   -27.982 1.00 50.69  ? 106 ALA   B N   1 
ATOM   1109 C CA  . ALA   B 2 97  ? -21.428 6.468   -27.671 1.00 50.41  ? 106 ALA   B CA  1 
ATOM   1110 C C   . ALA   B 2 97  ? -20.884 5.762   -28.908 1.00 52.34  ? 106 ALA   B C   1 
ATOM   1111 O O   . ALA   B 2 97  ? -21.436 5.969   -29.979 1.00 53.75  ? 106 ALA   B O   1 
ATOM   1112 C CB  . ALA   B 2 97  ? -22.770 5.911   -27.296 1.00 48.65  ? 106 ALA   B CB  1 
ATOM   1113 N N   . LYS   B 2 98  ? -19.895 4.886   -28.757 1.00 56.10  ? 107 LYS   B N   1 
ATOM   1114 C CA  . LYS   B 2 98  ? -19.360 4.052   -29.865 1.00 59.43  ? 107 LYS   B CA  1 
ATOM   1115 C C   . LYS   B 2 98  ? -19.003 2.649   -29.351 1.00 58.34  ? 107 LYS   B C   1 
ATOM   1116 O O   . LYS   B 2 98  ? -18.238 2.582   -28.363 1.00 55.92  ? 107 LYS   B O   1 
ATOM   1117 C CB  . LYS   B 2 98  ? -18.129 4.763   -30.424 1.00 66.30  ? 107 LYS   B CB  1 
ATOM   1118 C CG  . LYS   B 2 98  ? -17.386 4.052   -31.554 1.00 73.04  ? 107 LYS   B CG  1 
ATOM   1119 C CD  . LYS   B 2 98  ? -15.955 4.563   -31.747 1.00 79.55  ? 107 LYS   B CD  1 
ATOM   1120 C CE  . LYS   B 2 98  ? -15.312 5.016   -30.444 1.00 82.38  ? 107 LYS   B CE  1 
ATOM   1121 N NZ  . LYS   B 2 98  ? -13.862 5.270   -30.596 1.00 88.18  ? 107 LYS   B NZ  1 
ATOM   1122 N N   . ASN   B 2 99  ? -19.531 1.594   -29.994 1.00 53.69  ? 108 ASN   B N   1 
ATOM   1123 C CA  . ASN   B 2 99  ? -19.211 0.167   -29.720 1.00 53.40  ? 108 ASN   B CA  1 
ATOM   1124 C C   . ASN   B 2 99  ? -17.811 -0.147  -30.271 1.00 54.70  ? 108 ASN   B C   1 
ATOM   1125 O O   . ASN   B 2 99  ? -17.490 0.307   -31.375 1.00 57.49  ? 108 ASN   B O   1 
ATOM   1126 C CB  . ASN   B 2 99  ? -20.227 -0.823  -30.307 1.00 51.53  ? 108 ASN   B CB  1 
ATOM   1127 C CG  . ASN   B 2 99  ? -21.625 -0.659  -29.745 1.00 53.94  ? 108 ASN   B CG  1 
ATOM   1128 O OD1 . ASN   B 2 99  ? -22.206 0.418   -29.854 1.00 54.95  ? 108 ASN   B OD1 1 
ATOM   1129 N ND2 . ASN   B 2 99  ? -22.221 -1.719  -29.220 1.00 52.44  ? 108 ASN   B ND2 1 
ATOM   1130 N N   . ILE   B 2 100 ? -17.000 -0.913  -29.548 1.00 50.55  ? 109 ILE   B N   1 
ATOM   1131 C CA  . ILE   B 2 100 ? -15.666 -1.362  -30.006 1.00 50.14  ? 109 ILE   B CA  1 
ATOM   1132 C C   . ILE   B 2 100 ? -15.602 -2.834  -29.662 1.00 49.33  ? 109 ILE   B C   1 
ATOM   1133 O O   . ILE   B 2 100 ? -15.737 -3.190  -28.463 1.00 50.95  ? 109 ILE   B O   1 
ATOM   1134 C CB  . ILE   B 2 100 ? -14.534 -0.588  -29.320 1.00 51.65  ? 109 ILE   B CB  1 
ATOM   1135 C CG1 . ILE   B 2 100 ? -14.733 0.922   -29.379 1.00 51.48  ? 109 ILE   B CG1 1 
ATOM   1136 C CG2 . ILE   B 2 100 ? -13.187 -1.027  -29.879 1.00 53.21  ? 109 ILE   B CG2 1 
ATOM   1137 C CD1 . ILE   B 2 100 ? -14.445 1.503   -30.735 1.00 52.39  ? 109 ILE   B CD1 1 
ATOM   1138 N N   . GLN   B 2 101 ? -15.483 -3.690  -30.651 1.00 50.11  ? 110 GLN   B N   1 
ATOM   1139 C CA  . GLN   B 2 101 ? -15.582 -5.142  -30.424 1.00 51.90  ? 110 GLN   B CA  1 
ATOM   1140 C C   . GLN   B 2 101 ? -14.177 -5.675  -30.199 1.00 53.86  ? 110 GLN   B C   1 
ATOM   1141 O O   . GLN   B 2 101 ? -13.285 -5.160  -30.884 1.00 54.67  ? 110 GLN   B O   1 
ATOM   1142 C CB  . GLN   B 2 101 ? -16.230 -5.850  -31.585 1.00 54.18  ? 110 GLN   B CB  1 
ATOM   1143 C CG  . GLN   B 2 101 ? -16.156 -7.359  -31.470 1.00 52.54  ? 110 GLN   B CG  1 
ATOM   1144 C CD  . GLN   B 2 101 ? -17.199 -7.947  -32.386 1.00 55.07  ? 110 GLN   B CD  1 
ATOM   1145 O OE1 . GLN   B 2 101 ? -18.245 -7.351  -32.666 1.00 51.62  ? 110 GLN   B OE1 1 
ATOM   1146 N NE2 . GLN   B 2 101 ? -16.882 -9.099  -32.935 1.00 54.77  ? 110 GLN   B NE2 1 
ATOM   1147 N N   . THR   B 2 102 ? -13.993 -6.603  -29.233 1.00 53.59  ? 111 THR   B N   1 
ATOM   1148 C CA  . THR   B 2 102 ? -12.652 -7.148  -28.871 1.00 52.00  ? 111 THR   B CA  1 
ATOM   1149 C C   . THR   B 2 102 ? -12.805 -8.517  -28.227 1.00 52.41  ? 111 THR   B C   1 
ATOM   1150 O O   . THR   B 2 102 ? -13.928 -8.808  -27.782 1.00 56.63  ? 111 THR   B O   1 
ATOM   1151 C CB  . THR   B 2 102 ? -11.914 -6.127  -27.994 1.00 51.54  ? 111 THR   B CB  1 
ATOM   1152 O OG1 . THR   B 2 102 ? -10.541 -6.511  -27.934 1.00 50.32  ? 111 THR   B OG1 1 
ATOM   1153 C CG2 . THR   B 2 102 ? -12.526 -5.966  -26.614 1.00 51.98  ? 111 THR   B CG2 1 
ATOM   1154 N N   . LEU   B 2 103 ? -11.746 -9.338  -28.266 1.00 51.71  ? 112 LEU   B N   1 
ATOM   1155 C CA  . LEU   B 2 103 ? -11.594 -10.599 -27.483 1.00 52.54  ? 112 LEU   B CA  1 
ATOM   1156 C C   . LEU   B 2 103 ? -10.802 -10.264 -26.213 1.00 52.03  ? 112 LEU   B C   1 
ATOM   1157 O O   . LEU   B 2 103 ? -9.646  -9.810  -26.286 1.00 51.89  ? 112 LEU   B O   1 
ATOM   1158 C CB  . LEU   B 2 103 ? -10.836 -11.691 -28.261 1.00 53.14  ? 112 LEU   B CB  1 
ATOM   1159 C CG  . LEU   B 2 103 ? -10.714 -13.007 -27.488 1.00 52.56  ? 112 LEU   B CG  1 
ATOM   1160 C CD1 . LEU   B 2 103 ? -12.038 -13.747 -27.488 1.00 51.82  ? 112 LEU   B CD1 1 
ATOM   1161 C CD2 . LEU   B 2 103 ? -9.608  -13.911 -28.030 1.00 55.60  ? 112 LEU   B CD2 1 
ATOM   1162 N N   . PRO   B 2 104 ? -11.397 -10.437 -25.015 1.00 50.30  ? 113 PRO   B N   1 
ATOM   1163 C CA  . PRO   B 2 104 ? -10.704 -10.116 -23.774 1.00 50.99  ? 113 PRO   B CA  1 
ATOM   1164 C C   . PRO   B 2 104 ? -9.518  -11.066 -23.556 1.00 52.90  ? 113 PRO   B C   1 
ATOM   1165 O O   . PRO   B 2 104 ? -9.633  -12.225 -23.892 1.00 51.75  ? 113 PRO   B O   1 
ATOM   1166 C CB  . PRO   B 2 104 ? -11.724 -10.387 -22.653 1.00 50.51  ? 113 PRO   B CB  1 
ATOM   1167 C CG  . PRO   B 2 104 ? -13.069 -10.429 -23.368 1.00 50.33  ? 113 PRO   B CG  1 
ATOM   1168 C CD  . PRO   B 2 104 ? -12.773 -10.906 -24.786 1.00 51.68  ? 113 PRO   B CD  1 
ATOM   1169 N N   . GLY   B 2 105 ? -8.428  -10.526 -23.014 1.00 54.74  ? 114 GLY   B N   1 
ATOM   1170 C CA  . GLY   B 2 105 ? -7.384  -11.299 -22.337 1.00 55.91  ? 114 GLY   B CA  1 
ATOM   1171 C C   . GLY   B 2 105 ? -7.844  -11.660 -20.937 1.00 55.84  ? 114 GLY   B C   1 
ATOM   1172 O O   . GLY   B 2 105 ? -9.074  -11.683 -20.696 1.00 51.22  ? 114 GLY   B O   1 
ATOM   1173 N N   . ILE   B 2 106 ? -6.880  -11.880 -20.044 1.00 55.61  ? 115 ILE   B N   1 
ATOM   1174 C CA  . ILE   B 2 106 ? -7.064  -12.496 -18.698 1.00 55.27  ? 115 ILE   B CA  1 
ATOM   1175 C C   . ILE   B 2 106 ? -6.158  -11.794 -17.686 1.00 52.28  ? 115 ILE   B C   1 
ATOM   1176 O O   . ILE   B 2 106 ? -4.967  -11.719 -17.900 1.00 54.92  ? 115 ILE   B O   1 
ATOM   1177 C CB  . ILE   B 2 106 ? -6.717  -13.985 -18.772 1.00 58.33  ? 115 ILE   B CB  1 
ATOM   1178 C CG1 . ILE   B 2 106 ? -7.558  -14.727 -19.810 1.00 62.01  ? 115 ILE   B CG1 1 
ATOM   1179 C CG2 . ILE   B 2 106 ? -6.831  -14.615 -17.409 1.00 61.51  ? 115 ILE   B CG2 1 
ATOM   1180 C CD1 . ILE   B 2 106 ? -8.886  -15.180 -19.315 1.00 60.71  ? 115 ILE   B CD1 1 
ATOM   1181 N N   . PHE   B 2 107 ? -6.719  -11.315 -16.596 1.00 51.56  ? 116 PHE   B N   1 
ATOM   1182 C CA  . PHE   B 2 107 ? -5.993  -10.963 -15.360 1.00 49.90  ? 116 PHE   B CA  1 
ATOM   1183 C C   . PHE   B 2 107 ? -5.950  -12.222 -14.520 1.00 51.51  ? 116 PHE   B C   1 
ATOM   1184 O O   . PHE   B 2 107 ? -7.041  -12.686 -14.167 1.00 50.18  ? 116 PHE   B O   1 
ATOM   1185 C CB  . PHE   B 2 107 ? -6.751  -9.892  -14.594 1.00 49.92  ? 116 PHE   B CB  1 
ATOM   1186 C CG  . PHE   B 2 107 ? -6.489  -8.482  -15.015 1.00 49.44  ? 116 PHE   B CG  1 
ATOM   1187 C CD1 . PHE   B 2 107 ? -5.724  -8.193  -16.129 1.00 51.29  ? 116 PHE   B CD1 1 
ATOM   1188 C CD2 . PHE   B 2 107 ? -7.055  -7.449  -14.287 1.00 49.92  ? 116 PHE   B CD2 1 
ATOM   1189 C CE1 . PHE   B 2 107 ? -5.505  -6.881  -16.504 1.00 53.27  ? 116 PHE   B CE1 1 
ATOM   1190 C CE2 . PHE   B 2 107 ? -6.823  -6.134  -14.659 1.00 50.89  ? 116 PHE   B CE2 1 
ATOM   1191 C CZ  . PHE   B 2 107 ? -6.054  -5.852  -15.761 1.00 52.79  ? 116 PHE   B CZ  1 
ATOM   1192 N N   . LYS   B 2 108 ? -4.751  -12.771 -14.301 1.00 52.74  ? 117 LYS   B N   1 
ATOM   1193 C CA  . LYS   B 2 108 ? -4.481  -13.925 -13.398 1.00 55.63  ? 117 LYS   B CA  1 
ATOM   1194 C C   . LYS   B 2 108 ? -4.184  -13.363 -12.002 1.00 51.77  ? 117 LYS   B C   1 
ATOM   1195 O O   . LYS   B 2 108 ? -3.245  -12.532 -11.896 1.00 49.17  ? 117 LYS   B O   1 
ATOM   1196 C CB  . LYS   B 2 108 ? -3.286  -14.755 -13.893 1.00 60.82  ? 117 LYS   B CB  1 
ATOM   1197 C CG  . LYS   B 2 108 ? -3.632  -15.950 -14.775 1.00 69.56  ? 117 LYS   B CG  1 
ATOM   1198 C CD  . LYS   B 2 108 ? -2.585  -16.312 -15.828 1.00 74.95  ? 117 LYS   B CD  1 
ATOM   1199 C CE  . LYS   B 2 108 ? -3.089  -17.360 -16.816 1.00 85.47  ? 117 LYS   B CE  1 
ATOM   1200 N NZ  . LYS   B 2 108 ? -2.226  -17.558 -18.029 1.00 88.17  ? 117 LYS   B NZ  1 
ATOM   1201 N N   . THR   B 2 109 ? -4.987  -13.741 -11.001 1.00 49.85  ? 118 THR   B N   1 
ATOM   1202 C CA  . THR   B 2 109 ? -4.823  -13.335 -9.580  1.00 49.67  ? 118 THR   B CA  1 
ATOM   1203 C C   . THR   B 2 109 ? -4.891  -14.562 -8.665  1.00 50.60  ? 118 THR   B C   1 
ATOM   1204 O O   . THR   B 2 109 ? -5.479  -15.586 -9.052  1.00 48.43  ? 118 THR   B O   1 
ATOM   1205 C CB  . THR   B 2 109 ? -5.877  -12.321 -9.110  1.00 47.56  ? 118 THR   B CB  1 
ATOM   1206 O OG1 . THR   B 2 109 ? -7.042  -12.992 -8.610  1.00 45.72  ? 118 THR   B OG1 1 
ATOM   1207 C CG2 . THR   B 2 109 ? -6.223  -11.330 -10.191 1.00 47.10  ? 118 THR   B CG2 1 
ATOM   1208 N N   . LYS   B 2 110 ? -4.410  -14.393 -7.438  1.00 53.51  ? 119 LYS   B N   1 
ATOM   1209 C CA  . LYS   B 2 110 ? -4.382  -15.453 -6.392  1.00 56.29  ? 119 LYS   B CA  1 
ATOM   1210 C C   . LYS   B 2 110 ? -5.826  -15.894 -6.089  1.00 58.21  ? 119 LYS   B C   1 
ATOM   1211 O O   . LYS   B 2 110 ? -6.015  -17.083 -5.759  1.00 60.46  ? 119 LYS   B O   1 
ATOM   1212 C CB  . LYS   B 2 110 ? -3.610  -14.928 -5.173  1.00 57.80  ? 119 LYS   B CB  1 
ATOM   1213 C CG  . LYS   B 2 110 ? -4.300  -13.838 -4.371  1.00 61.07  ? 119 LYS   B CG  1 
ATOM   1214 C CD  . LYS   B 2 110 ? -3.403  -13.159 -3.342  1.00 63.30  ? 119 LYS   B CD  1 
ATOM   1215 C CE  . LYS   B 2 110 ? -4.046  -12.985 -1.985  1.00 65.33  ? 119 LYS   B CE  1 
ATOM   1216 N NZ  . LYS   B 2 110 ? -5.341  -12.275 -2.060  1.00 63.02  ? 119 LYS   B NZ  1 
ATOM   1217 N N   . ASP   B 2 111 ? -6.811  -15.003 -6.260  1.00 56.22  ? 120 ASP   B N   1 
ATOM   1218 C CA  . ASP   B 2 111 ? -8.244  -15.285 -5.980  1.00 58.59  ? 120 ASP   B CA  1 
ATOM   1219 C C   . ASP   B 2 111 ? -8.977  -15.784 -7.227  1.00 61.06  ? 120 ASP   B C   1 
ATOM   1220 O O   . ASP   B 2 111 ? -10.172 -16.080 -7.103  1.00 63.40  ? 120 ASP   B O   1 
ATOM   1221 C CB  . ASP   B 2 111 ? -8.935  -14.043 -5.422  1.00 60.07  ? 120 ASP   B CB  1 
ATOM   1222 C CG  . ASP   B 2 111 ? -8.513  -13.764 -3.998  1.00 61.40  ? 120 ASP   B CG  1 
ATOM   1223 O OD1 . ASP   B 2 111 ? -7.718  -14.551 -3.471  1.00 61.87  ? 120 ASP   B OD1 1 
ATOM   1224 O OD2 . ASP   B 2 111 ? -9.020  -12.801 -3.417  1.00 71.31  ? 120 ASP   B OD2 1 
ATOM   1225 N N   . GLY   B 2 112 ? -8.302  -15.869 -8.376  1.00 61.27  ? 121 GLY   B N   1 
ATOM   1226 C CA  . GLY   B 2 112 ? -8.914  -16.341 -9.626  1.00 61.45  ? 121 GLY   B CA  1 
ATOM   1227 C C   . GLY   B 2 112 ? -8.629  -15.439 -10.820 1.00 60.44  ? 121 GLY   B C   1 
ATOM   1228 O O   . GLY   B 2 112 ? -7.950  -14.408 -10.662 1.00 60.16  ? 121 GLY   B O   1 
ATOM   1229 N N   . ASP   B 2 113 ? -9.119  -15.857 -11.987 1.00 58.96  ? 122 ASP   B N   1 
ATOM   1230 C CA  . ASP   B 2 113 ? -8.905  -15.199 -13.306 1.00 58.97  ? 122 ASP   B CA  1 
ATOM   1231 C C   . ASP   B 2 113 ? -10.075 -14.253 -13.612 1.00 56.57  ? 122 ASP   B C   1 
ATOM   1232 O O   . ASP   B 2 113 ? -11.206 -14.551 -13.205 1.00 50.17  ? 122 ASP   B O   1 
ATOM   1233 C CB  . ASP   B 2 113 ? -8.741  -16.242 -14.406 1.00 60.80  ? 122 ASP   B CB  1 
ATOM   1234 C CG  . ASP   B 2 113 ? -7.429  -17.005 -14.345 1.00 63.56  ? 122 ASP   B CG  1 
ATOM   1235 O OD1 . ASP   B 2 113 ? -6.589  -16.686 -13.477 1.00 68.94  ? 122 ASP   B OD1 1 
ATOM   1236 O OD2 . ASP   B 2 113 ? -7.250  -17.889 -15.191 1.00 67.34  ? 122 ASP   B OD2 1 
ATOM   1237 N N   . ILE   B 2 114 ? -9.788  -13.140 -14.277 1.00 54.72  ? 123 ILE   B N   1 
ATOM   1238 C CA  . ILE   B 2 114 ? -10.800 -12.111 -14.643 1.00 56.33  ? 123 ILE   B CA  1 
ATOM   1239 C C   . ILE   B 2 114 ? -10.560 -11.766 -16.111 1.00 50.93  ? 123 ILE   B C   1 
ATOM   1240 O O   . ILE   B 2 114 ? -9.400  -11.655 -16.455 1.00 48.21  ? 123 ILE   B O   1 
ATOM   1241 C CB  . ILE   B 2 114 ? -10.667 -10.849 -13.761 1.00 57.10  ? 123 ILE   B CB  1 
ATOM   1242 C CG1 . ILE   B 2 114 ? -10.413 -11.162 -12.293 1.00 62.59  ? 123 ILE   B CG1 1 
ATOM   1243 C CG2 . ILE   B 2 114 ? -11.874 -9.951  -13.901 1.00 57.11  ? 123 ILE   B CG2 1 
ATOM   1244 C CD1 . ILE   B 2 114 ? -10.126 -9.918  -11.459 1.00 64.38  ? 123 ILE   B CD1 1 
ATOM   1245 N N   . GLY   B 2 115 ? -11.620 -11.550 -16.901 1.00 50.13  ? 124 GLY   B N   1 
ATOM   1246 C CA  . GLY   B 2 115 ? -11.521 -10.972 -18.260 1.00 47.22  ? 124 GLY   B CA  1 
ATOM   1247 C C   . GLY   B 2 115 ? -10.868 -9.603  -18.167 1.00 46.23  ? 124 GLY   B C   1 
ATOM   1248 O O   . GLY   B 2 115 ? -11.002 -8.923  -17.127 1.00 43.89  ? 124 GLY   B O   1 
ATOM   1249 N N   . ALA   B 2 116 ? -10.089 -9.249  -19.166 1.00 46.53  ? 125 ALA   B N   1 
ATOM   1250 C CA  . ALA   B 2 116 ? -9.476  -7.913  -19.311 1.00 48.95  ? 125 ALA   B CA  1 
ATOM   1251 C C   . ALA   B 2 116 ? -9.665  -7.474  -20.767 1.00 49.57  ? 125 ALA   B C   1 
ATOM   1252 O O   . ALA   B 2 116 ? -9.546  -8.314  -21.672 1.00 51.64  ? 125 ALA   B O   1 
ATOM   1253 C CB  . ALA   B 2 116 ? -8.013  -7.965  -18.910 1.00 50.17  ? 125 ALA   B CB  1 
ATOM   1254 N N   A VAL   B 2 117 ? -9.972  -6.191  -20.988 0.25 49.33  ? 126 VAL   B N   1 
ATOM   1255 N N   B VAL   B 2 117 ? -9.929  -6.179  -20.965 0.25 49.24  ? 126 VAL   B N   1 
ATOM   1256 N N   C VAL   B 2 117 ? -9.972  -6.191  -20.988 0.25 49.33  ? 126 VAL   B N   1 
ATOM   1257 N N   D VAL   B 2 117 ? -9.929  -6.179  -20.965 0.25 49.24  ? 126 VAL   B N   1 
ATOM   1258 C CA  A VAL   B 2 117 ? -10.049 -5.574  -22.348 0.25 50.97  ? 126 VAL   B CA  1 
ATOM   1259 C CA  B VAL   B 2 117 ? -10.066 -5.513  -22.295 0.25 50.71  ? 126 VAL   B CA  1 
ATOM   1260 C CA  C VAL   B 2 117 ? -10.049 -5.574  -22.348 0.25 50.97  ? 126 VAL   B CA  1 
ATOM   1261 C CA  D VAL   B 2 117 ? -10.066 -5.513  -22.295 0.25 50.71  ? 126 VAL   B CA  1 
ATOM   1262 C C   A VAL   B 2 117 ? -8.904  -4.564  -22.501 0.25 51.05  ? 126 VAL   B C   1 
ATOM   1263 C C   B VAL   B 2 117 ? -8.892  -4.542  -22.491 0.25 50.91  ? 126 VAL   B C   1 
ATOM   1264 C C   C VAL   B 2 117 ? -8.904  -4.564  -22.501 0.25 51.05  ? 126 VAL   B C   1 
ATOM   1265 C C   D VAL   B 2 117 ? -8.892  -4.542  -22.491 0.25 50.91  ? 126 VAL   B C   1 
ATOM   1266 O O   A VAL   B 2 117 ? -8.707  -3.746  -21.585 0.25 50.58  ? 126 VAL   B O   1 
ATOM   1267 O O   B VAL   B 2 117 ? -8.659  -3.718  -21.588 0.25 50.42  ? 126 VAL   B O   1 
ATOM   1268 O O   C VAL   B 2 117 ? -8.707  -3.746  -21.585 0.25 50.58  ? 126 VAL   B O   1 
ATOM   1269 O O   D VAL   B 2 117 ? -8.659  -3.718  -21.588 0.25 50.42  ? 126 VAL   B O   1 
ATOM   1270 C CB  A VAL   B 2 117 ? -11.426 -4.931  -22.591 0.25 51.10  ? 126 VAL   B CB  1 
ATOM   1271 C CB  B VAL   B 2 117 ? -11.428 -4.803  -22.386 0.25 50.62  ? 126 VAL   B CB  1 
ATOM   1272 C CB  C VAL   B 2 117 ? -11.426 -4.931  -22.591 0.25 51.10  ? 126 VAL   B CB  1 
ATOM   1273 C CB  D VAL   B 2 117 ? -11.428 -4.803  -22.386 0.25 50.62  ? 126 VAL   B CB  1 
ATOM   1274 C CG1 A VAL   B 2 117 ? -12.551 -5.915  -22.309 0.25 51.32  ? 126 VAL   B CG1 1 
ATOM   1275 C CG1 B VAL   B 2 117 ? -11.376 -3.579  -23.279 0.25 50.86  ? 126 VAL   B CG1 1 
ATOM   1276 C CG1 C VAL   B 2 117 ? -12.551 -5.915  -22.309 0.25 51.32  ? 126 VAL   B CG1 1 
ATOM   1277 C CG1 D VAL   B 2 117 ? -11.376 -3.579  -23.279 0.25 50.86  ? 126 VAL   B CG1 1 
ATOM   1278 C CG2 A VAL   B 2 117 ? -11.609 -3.662  -21.777 0.25 50.69  ? 126 VAL   B CG2 1 
ATOM   1279 C CG2 B VAL   B 2 117 ? -12.521 -5.758  -22.835 0.25 51.25  ? 126 VAL   B CG2 1 
ATOM   1280 C CG2 C VAL   B 2 117 ? -11.609 -3.662  -21.777 0.25 50.69  ? 126 VAL   B CG2 1 
ATOM   1281 C CG2 D VAL   B 2 117 ? -12.521 -5.758  -22.835 0.25 51.25  ? 126 VAL   B CG2 1 
ATOM   1282 N N   . ALA   B 2 118 ? -8.174  -4.634  -23.618 1.00 51.45  ? 127 ALA   B N   1 
ATOM   1283 C CA  . ALA   B 2 118 ? -6.965  -3.795  -23.869 1.00 53.70  ? 127 ALA   B CA  1 
ATOM   1284 C C   . ALA   B 2 118 ? -7.292  -2.624  -24.800 1.00 56.14  ? 127 ALA   B C   1 
ATOM   1285 O O   . ALA   B 2 118 ? -6.834  -2.636  -25.947 1.00 58.91  ? 127 ALA   B O   1 
ATOM   1286 C CB  . ALA   B 2 118 ? -5.841  -4.649  -24.445 1.00 53.94  ? 127 ALA   B CB  1 
ATOM   1287 N N   . LEU   B 2 119 ? -8.138  -1.690  -24.373 1.00 55.92  ? 128 LEU   B N   1 
ATOM   1288 C CA  . LEU   B 2 119 ? -8.563  -0.559  -25.213 1.00 56.58  ? 128 LEU   B CA  1 
ATOM   1289 C C   . LEU   B 2 119 ? -8.223  0.718   -24.445 1.00 60.11  ? 128 LEU   B C   1 
ATOM   1290 O O   . LEU   B 2 119 ? -8.326  0.711   -23.200 1.00 66.25  ? 128 LEU   B O   1 
ATOM   1291 C CB  . LEU   B 2 119 ? -10.053 -0.732  -25.498 1.00 56.04  ? 128 LEU   B CB  1 
ATOM   1292 C CG  . LEU   B 2 119 ? -10.446 -2.003  -26.250 1.00 54.16  ? 128 LEU   B CG  1 
ATOM   1293 C CD1 . LEU   B 2 119 ? -11.954 -2.226  -26.205 1.00 51.08  ? 128 LEU   B CD1 1 
ATOM   1294 C CD2 . LEU   B 2 119 ? -9.968  -1.938  -27.691 1.00 56.22  ? 128 LEU   B CD2 1 
ATOM   1295 N N   . ASP   B 2 120 ? -7.763  1.743   -25.148 1.00 61.87  ? 129 ASP   B N   1 
ATOM   1296 C CA  . ASP   B 2 120 ? -7.127  2.928   -24.532 1.00 65.24  ? 129 ASP   B CA  1 
ATOM   1297 C C   . ASP   B 2 120 ? -8.109  4.093   -24.688 1.00 61.18  ? 129 ASP   B C   1 
ATOM   1298 O O   . ASP   B 2 120 ? -8.348  4.508   -25.811 1.00 66.19  ? 129 ASP   B O   1 
ATOM   1299 C CB  . ASP   B 2 120 ? -5.752  3.159   -25.169 1.00 71.26  ? 129 ASP   B CB  1 
ATOM   1300 C CG  . ASP   B 2 120 ? -4.684  3.758   -24.256 1.00 77.51  ? 129 ASP   B CG  1 
ATOM   1301 O OD1 . ASP   B 2 120 ? -4.958  3.961   -23.048 1.00 75.58  ? 129 ASP   B OD1 1 
ATOM   1302 O OD2 . ASP   B 2 120 ? -3.574  4.039   -24.771 1.00 87.74  ? 129 ASP   B OD2 1 
ATOM   1303 N N   . TYR   B 2 121 ? -8.695  4.587   -23.611 1.00 55.53  ? 130 TYR   B N   1 
ATOM   1304 C CA  . TYR   B 2 121 ? -9.627  5.737   -23.690 1.00 55.28  ? 130 TYR   B CA  1 
ATOM   1305 C C   . TYR   B 2 121 ? -9.342  6.676   -22.540 1.00 53.01  ? 130 TYR   B C   1 
ATOM   1306 O O   . TYR   B 2 121 ? -8.714  6.286   -21.563 1.00 55.52  ? 130 TYR   B O   1 
ATOM   1307 C CB  . TYR   B 2 121 ? -11.073 5.268   -23.671 1.00 55.25  ? 130 TYR   B CB  1 
ATOM   1308 C CG  . TYR   B 2 121 ? -11.555 4.641   -24.948 1.00 60.04  ? 130 TYR   B CG  1 
ATOM   1309 C CD1 . TYR   B 2 121 ? -12.036 5.436   -25.979 1.00 60.58  ? 130 TYR   B CD1 1 
ATOM   1310 C CD2 . TYR   B 2 121 ? -11.558 3.261   -25.128 1.00 62.35  ? 130 TYR   B CD2 1 
ATOM   1311 C CE1 . TYR   B 2 121 ? -12.494 4.878   -27.159 1.00 64.26  ? 130 TYR   B CE1 1 
ATOM   1312 C CE2 . TYR   B 2 121 ? -12.017 2.688   -26.311 1.00 66.14  ? 130 TYR   B CE2 1 
ATOM   1313 C CZ  . TYR   B 2 121 ? -12.480 3.505   -27.331 1.00 67.42  ? 130 TYR   B CZ  1 
ATOM   1314 O OH  . TYR   B 2 121 ? -12.945 3.005   -28.512 1.00 77.55  ? 130 TYR   B OH  1 
ATOM   1315 N N   . PRO   B 2 122 ? -9.787  7.940   -22.593 1.00 52.37  ? 131 PRO   B N   1 
ATOM   1316 C CA  . PRO   B 2 122 ? -9.534  8.828   -21.474 1.00 53.40  ? 131 PRO   B CA  1 
ATOM   1317 C C   . PRO   B 2 122 ? -10.167 8.240   -20.201 1.00 48.94  ? 131 PRO   B C   1 
ATOM   1318 O O   . PRO   B 2 122 ? -11.072 7.375   -20.270 1.00 46.77  ? 131 PRO   B O   1 
ATOM   1319 C CB  . PRO   B 2 122 ? -10.143 10.170  -21.920 1.00 54.21  ? 131 PRO   B CB  1 
ATOM   1320 C CG  . PRO   B 2 122 ? -10.294 10.054  -23.431 1.00 55.46  ? 131 PRO   B CG  1 
ATOM   1321 C CD  . PRO   B 2 122 ? -10.568 8.584   -23.670 1.00 56.42  ? 131 PRO   B CD  1 
ATOM   1322 N N   . ALA   B 2 123 ? -9.650  8.706   -19.069 1.00 48.91  ? 132 ALA   B N   1 
ATOM   1323 C CA  . ALA   B 2 123 ? -10.050 8.316   -17.703 1.00 48.03  ? 132 ALA   B CA  1 
ATOM   1324 C C   . ALA   B 2 123 ? -11.553 8.528   -17.534 1.00 45.93  ? 132 ALA   B C   1 
ATOM   1325 O O   . ALA   B 2 123 ? -12.220 7.655   -16.877 1.00 43.22  ? 132 ALA   B O   1 
ATOM   1326 C CB  . ALA   B 2 123 ? -9.235  9.093   -16.709 1.00 49.70  ? 132 ALA   B CB  1 
ATOM   1327 N N   . GLY   B 2 124 ? -12.067 9.602   -18.142 1.00 45.00  ? 133 GLY   B N   1 
ATOM   1328 C CA  . GLY   B 2 124 ? -13.486 9.998   -18.051 1.00 41.84  ? 133 GLY   B CA  1 
ATOM   1329 C C   . GLY   B 2 124 ? -14.402 8.981   -18.721 1.00 40.85  ? 133 GLY   B C   1 
ATOM   1330 O O   . GLY   B 2 124 ? -15.633 9.116   -18.539 1.00 37.05  ? 133 GLY   B O   1 
ATOM   1331 N N   . THR   B 2 125 ? -13.868 7.989   -19.438 1.00 38.79  ? 134 THR   B N   1 
ATOM   1332 C CA  . THR   B 2 125 ? -14.660 6.844   -20.004 1.00 40.61  ? 134 THR   B CA  1 
ATOM   1333 C C   . THR   B 2 125 ? -14.936 5.729   -18.966 1.00 40.87  ? 134 THR   B C   1 
ATOM   1334 O O   . THR   B 2 125 ? -15.784 4.826   -19.277 1.00 41.42  ? 134 THR   B O   1 
ATOM   1335 C CB  . THR   B 2 125 ? -13.963 6.285   -21.260 1.00 42.65  ? 134 THR   B CB  1 
ATOM   1336 O OG1 . THR   B 2 125 ? -13.692 7.313   -22.212 1.00 43.03  ? 134 THR   B OG1 1 
ATOM   1337 C CG2 . THR   B 2 125 ? -14.772 5.280   -22.054 1.00 41.94  ? 134 THR   B CG2 1 
ATOM   1338 N N   . SER   B 2 126 ? -14.300 5.757   -17.773 1.00 39.74  ? 135 SER   B N   1 
ATOM   1339 C CA  . SER   B 2 126 ? -14.547 4.806   -16.644 1.00 39.12  ? 135 SER   B CA  1 
ATOM   1340 C C   . SER   B 2 126 ? -16.038 4.593   -16.384 1.00 38.02  ? 135 SER   B C   1 
ATOM   1341 O O   . SER   B 2 126 ? -16.776 5.626   -16.216 1.00 36.84  ? 135 SER   B O   1 
ATOM   1342 C CB  . SER   B 2 126 ? -13.909 5.296   -15.398 1.00 39.23  ? 135 SER   B CB  1 
ATOM   1343 O OG  . SER   B 2 126 ? -12.504 5.285   -15.510 1.00 38.44  ? 135 SER   B OG  1 
ATOM   1344 N N   . GLY   B 2 127 ? -16.493 3.345   -16.371 1.00 36.43  ? 136 GLY   B N   1 
ATOM   1345 C CA  . GLY   B 2 127 ? -17.917 3.044   -16.099 1.00 38.04  ? 136 GLY   B CA  1 
ATOM   1346 C C   . GLY   B 2 127 ? -18.692 2.604   -17.322 1.00 37.99  ? 136 GLY   B C   1 
ATOM   1347 O O   . GLY   B 2 127 ? -19.768 2.008   -17.141 1.00 38.00  ? 136 GLY   B O   1 
ATOM   1348 N N   . SER   B 2 128 ? -18.108 2.778   -18.510 1.00 39.45  ? 137 SER   B N   1 
ATOM   1349 C CA  . SER   B 2 128 ? -18.649 2.289   -19.796 1.00 39.52  ? 137 SER   B CA  1 
ATOM   1350 C C   . SER   B 2 128 ? -18.875 0.802   -19.673 1.00 37.07  ? 137 SER   B C   1 
ATOM   1351 O O   . SER   B 2 128 ? -17.978 0.060   -19.300 1.00 38.02  ? 137 SER   B O   1 
ATOM   1352 C CB  . SER   B 2 128 ? -17.740 2.645   -20.956 1.00 40.39  ? 137 SER   B CB  1 
ATOM   1353 O OG  . SER   B 2 128 ? -17.615 4.054   -21.115 1.00 39.84  ? 137 SER   B OG  1 
ATOM   1354 N N   . PRO   B 2 129 ? -20.049 0.309   -20.087 1.00 36.09  ? 138 PRO   B N   1 
ATOM   1355 C CA  . PRO   B 2 129 ? -20.338 -1.115  -20.000 1.00 37.13  ? 138 PRO   B CA  1 
ATOM   1356 C C   . PRO   B 2 129 ? -19.715 -1.964  -21.102 1.00 38.86  ? 138 PRO   B C   1 
ATOM   1357 O O   . PRO   B 2 129 ? -19.601 -1.527  -22.261 1.00 39.69  ? 138 PRO   B O   1 
ATOM   1358 C CB  . PRO   B 2 129 ? -21.858 -1.196  -20.150 1.00 36.63  ? 138 PRO   B CB  1 
ATOM   1359 C CG  . PRO   B 2 129 ? -22.211 0.021   -20.984 1.00 35.76  ? 138 PRO   B CG  1 
ATOM   1360 C CD  . PRO   B 2 129 ? -21.181 1.066   -20.640 1.00 35.92  ? 138 PRO   B CD  1 
ATOM   1361 N N   . ILE   B 2 130 ? -19.505 -3.218  -20.762 1.00 39.30  ? 139 ILE   B N   1 
ATOM   1362 C CA  . ILE   B 2 130 ? -18.999 -4.284  -21.650 1.00 41.79  ? 139 ILE   B CA  1 
ATOM   1363 C C   . ILE   B 2 130 ? -20.149 -5.262  -21.849 1.00 41.75  ? 139 ILE   B C   1 
ATOM   1364 O O   . ILE   B 2 130 ? -20.771 -5.588  -20.836 1.00 40.74  ? 139 ILE   B O   1 
ATOM   1365 C CB  . ILE   B 2 130 ? -17.775 -4.949  -21.026 1.00 42.47  ? 139 ILE   B CB  1 
ATOM   1366 C CG1 . ILE   B 2 130 ? -16.626 -3.968  -20.811 1.00 44.70  ? 139 ILE   B CG1 1 
ATOM   1367 C CG2 . ILE   B 2 130 ? -17.331 -6.156  -21.845 1.00 43.09  ? 139 ILE   B CG2 1 
ATOM   1368 C CD1 . ILE   B 2 130 ? -15.589 -4.528  -19.857 1.00 47.02  ? 139 ILE   B CD1 1 
ATOM   1369 N N   . LEU   B 2 131 ? -20.436 -5.640  -23.107 1.00 44.42  ? 140 LEU   B N   1 
ATOM   1370 C CA  . LEU   B 2 131 ? -21.628 -6.443  -23.476 1.00 48.45  ? 140 LEU   B CA  1 
ATOM   1371 C C   . LEU   B 2 131 ? -21.233 -7.800  -24.042 1.00 49.07  ? 140 LEU   B C   1 
ATOM   1372 O O   . LEU   B 2 131 ? -20.210 -7.886  -24.703 1.00 52.81  ? 140 LEU   B O   1 
ATOM   1373 C CB  . LEU   B 2 131 ? -22.421 -5.702  -24.552 1.00 52.88  ? 140 LEU   B CB  1 
ATOM   1374 C CG  . LEU   B 2 131 ? -22.635 -4.218  -24.328 1.00 55.07  ? 140 LEU   B CG  1 
ATOM   1375 C CD1 . LEU   B 2 131 ? -23.537 -3.639  -25.440 1.00 55.80  ? 140 LEU   B CD1 1 
ATOM   1376 C CD2 . LEU   B 2 131 ? -23.232 -3.991  -22.936 1.00 55.56  ? 140 LEU   B CD2 1 
ATOM   1377 N N   . ASP   B 2 132 ? -22.099 -8.785  -23.844 1.00 50.59  ? 141 ASP   B N   1 
ATOM   1378 C CA  . ASP   B 2 132 ? -22.106 -10.076 -24.563 1.00 52.26  ? 141 ASP   B CA  1 
ATOM   1379 C C   . ASP   B 2 132 ? -23.036 -9.939  -25.776 1.00 56.89  ? 141 ASP   B C   1 
ATOM   1380 O O   . ASP   B 2 132 ? -23.639 -8.842  -25.962 1.00 57.26  ? 141 ASP   B O   1 
ATOM   1381 C CB  . ASP   B 2 132 ? -22.543 -11.224 -23.656 1.00 51.57  ? 141 ASP   B CB  1 
ATOM   1382 C CG  . ASP   B 2 132 ? -24.004 -11.241 -23.259 1.00 52.30  ? 141 ASP   B CG  1 
ATOM   1383 O OD1 . ASP   B 2 132 ? -24.794 -10.430 -23.775 1.00 50.58  ? 141 ASP   B OD1 1 
ATOM   1384 O OD2 . ASP   B 2 132 ? -24.340 -12.065 -22.382 1.00 55.97  ? 141 ASP   B OD2 1 
ATOM   1385 N N   . LYS   B 2 133 ? -23.199 -11.041 -26.508 1.00 61.51  ? 142 LYS   B N   1 
ATOM   1386 C CA  . LYS   B 2 133 ? -23.765 -11.075 -27.884 1.00 65.78  ? 142 LYS   B CA  1 
ATOM   1387 C C   . LYS   B 2 133 ? -25.249 -10.753 -27.789 1.00 62.56  ? 142 LYS   B C   1 
ATOM   1388 O O   . LYS   B 2 133 ? -25.763 -10.250 -28.762 1.00 61.76  ? 142 LYS   B O   1 
ATOM   1389 C CB  . LYS   B 2 133 ? -23.470 -12.423 -28.564 1.00 68.37  ? 142 LYS   B CB  1 
ATOM   1390 C CG  . LYS   B 2 133 ? -22.115 -12.476 -29.270 1.00 74.40  ? 142 LYS   B CG  1 
ATOM   1391 C CD  . LYS   B 2 133 ? -21.388 -13.828 -29.253 1.00 79.34  ? 142 LYS   B CD  1 
ATOM   1392 C CE  . LYS   B 2 133 ? -19.933 -13.704 -29.679 1.00 82.30  ? 142 LYS   B CE  1 
ATOM   1393 N NZ  . LYS   B 2 133 ? -19.377 -14.960 -30.249 1.00 83.83  ? 142 LYS   B NZ  1 
ATOM   1394 N N   . CYS   B 2 134 ? -25.865 -10.978 -26.624 1.00 61.62  ? 143 CYS   B N   1 
ATOM   1395 C CA  . CYS   B 2 134 ? -27.310 -10.750 -26.389 1.00 60.06  ? 143 CYS   B CA  1 
ATOM   1396 C C   . CYS   B 2 134 ? -27.561 -9.346  -25.819 1.00 54.87  ? 143 CYS   B C   1 
ATOM   1397 O O   . CYS   B 2 134 ? -28.694 -9.065  -25.446 1.00 51.23  ? 143 CYS   B O   1 
ATOM   1398 C CB  . CYS   B 2 134 ? -27.862 -11.799 -25.443 1.00 64.98  ? 143 CYS   B CB  1 
ATOM   1399 S SG  . CYS   B 2 134 ? -27.868 -13.471 -26.129 1.00 70.16  ? 143 CYS   B SG  1 
ATOM   1400 N N   . GLY   B 2 135 ? -26.568 -8.464  -25.836 1.00 54.38  ? 144 GLY   B N   1 
ATOM   1401 C CA  . GLY   B 2 135 ? -26.676 -7.109  -25.257 1.00 54.18  ? 144 GLY   B CA  1 
ATOM   1402 C C   . GLY   B 2 135 ? -26.672 -7.071  -23.715 1.00 52.09  ? 144 GLY   B C   1 
ATOM   1403 O O   . GLY   B 2 135 ? -26.922 -6.007  -23.171 1.00 50.45  ? 144 GLY   B O   1 
ATOM   1404 N N   . ARG   B 2 136 ? -26.369 -8.161  -22.998 1.00 53.74  ? 145 ARG   B N   1 
ATOM   1405 C CA  . ARG   B 2 136 ? -26.353 -8.149  -21.497 1.00 51.81  ? 145 ARG   B CA  1 
ATOM   1406 C C   . ARG   B 2 136 ? -25.036 -7.548  -20.980 1.00 49.09  ? 145 ARG   B C   1 
ATOM   1407 O O   . ARG   B 2 136 ? -23.938 -7.829  -21.587 1.00 47.48  ? 145 ARG   B O   1 
ATOM   1408 C CB  . ARG   B 2 136 ? -26.633 -9.553  -20.986 1.00 54.87  ? 145 ARG   B CB  1 
ATOM   1409 C CG  . ARG   B 2 136 ? -28.107 -9.907  -21.045 1.00 58.59  ? 145 ARG   B CG  1 
ATOM   1410 C CD  . ARG   B 2 136 ? -28.288 -11.324 -20.600 1.00 63.84  ? 145 ARG   B CD  1 
ATOM   1411 N NE  . ARG   B 2 136 ? -27.438 -12.120 -21.466 1.00 72.36  ? 145 ARG   B NE  1 
ATOM   1412 C CZ  . ARG   B 2 136 ? -26.874 -13.281 -21.167 1.00 75.63  ? 145 ARG   B CZ  1 
ATOM   1413 N NH1 . ARG   B 2 136 ? -27.028 -13.833 -19.967 1.00 80.13  ? 145 ARG   B NH1 1 
ATOM   1414 N NH2 . ARG   B 2 136 ? -26.144 -13.882 -22.092 1.00 77.72  ? 145 ARG   B NH2 1 
ATOM   1415 N N   . VAL   B 2 137 ? -25.096 -6.720  -19.934 1.00 45.30  ? 146 VAL   B N   1 
ATOM   1416 C CA  . VAL   B 2 137 ? -23.860 -6.095  -19.359 1.00 43.51  ? 146 VAL   B CA  1 
ATOM   1417 C C   . VAL   B 2 137 ? -23.126 -7.170  -18.537 1.00 45.03  ? 146 VAL   B C   1 
ATOM   1418 O O   . VAL   B 2 137 ? -23.698 -7.703  -17.528 1.00 44.83  ? 146 VAL   B O   1 
ATOM   1419 C CB  . VAL   B 2 137 ? -24.105 -4.816  -18.542 1.00 41.54  ? 146 VAL   B CB  1 
ATOM   1420 C CG1 . VAL   B 2 137 ? -22.794 -4.220  -18.082 1.00 40.38  ? 146 VAL   B CG1 1 
ATOM   1421 C CG2 . VAL   B 2 137 ? -24.877 -3.781  -19.340 1.00 43.87  ? 146 VAL   B CG2 1 
ATOM   1422 N N   . ILE   B 2 138 ? -21.904 -7.470  -18.934 1.00 43.33  ? 147 ILE   B N   1 
ATOM   1423 C CA  . ILE   B 2 138 ? -21.044 -8.464  -18.225 1.00 44.02  ? 147 ILE   B CA  1 
ATOM   1424 C C   . ILE   B 2 138 ? -20.019 -7.745  -17.317 1.00 41.77  ? 147 ILE   B C   1 
ATOM   1425 O O   . ILE   B 2 138 ? -19.253 -8.448  -16.631 1.00 40.86  ? 147 ILE   B O   1 
ATOM   1426 C CB  . ILE   B 2 138 ? -20.360 -9.402  -19.248 1.00 44.05  ? 147 ILE   B CB  1 
ATOM   1427 C CG1 . ILE   B 2 138 ? -19.579 -8.607  -20.289 1.00 43.93  ? 147 ILE   B CG1 1 
ATOM   1428 C CG2 . ILE   B 2 138 ? -21.370 -10.333 -19.889 1.00 43.55  ? 147 ILE   B CG2 1 
ATOM   1429 C CD1 . ILE   B 2 138 ? -18.499 -9.417  -20.961 1.00 48.50  ? 147 ILE   B CD1 1 
ATOM   1430 N N   . GLY   B 2 139 ? -19.997 -6.413  -17.278 1.00 40.41  ? 148 GLY   B N   1 
ATOM   1431 C CA  . GLY   B 2 139 ? -19.082 -5.694  -16.378 1.00 39.69  ? 148 GLY   B CA  1 
ATOM   1432 C C   . GLY   B 2 139 ? -18.830 -4.278  -16.840 1.00 40.45  ? 148 GLY   B C   1 
ATOM   1433 O O   . GLY   B 2 139 ? -19.384 -3.870  -17.915 1.00 39.14  ? 148 GLY   B O   1 
ATOM   1434 N N   . LEU   B 2 140 ? -18.003 -3.556  -16.100 1.00 39.97  ? 149 LEU   B N   1 
ATOM   1435 C CA  . LEU   B 2 140 ? -17.716 -2.144  -16.397 1.00 40.27  ? 149 LEU   B CA  1 
ATOM   1436 C C   . LEU   B 2 140 ? -16.232 -1.997  -16.644 1.00 41.35  ? 149 LEU   B C   1 
ATOM   1437 O O   . LEU   B 2 140 ? -15.392 -2.734  -16.006 1.00 39.82  ? 149 LEU   B O   1 
ATOM   1438 C CB  . LEU   B 2 140 ? -18.175 -1.210  -15.268 1.00 40.91  ? 149 LEU   B CB  1 
ATOM   1439 C CG  . LEU   B 2 140 ? -19.638 -1.290  -14.842 1.00 41.25  ? 149 LEU   B CG  1 
ATOM   1440 C CD1 . LEU   B 2 140 ? -19.969 -0.137  -13.877 1.00 42.48  ? 149 LEU   B CD1 1 
ATOM   1441 C CD2 . LEU   B 2 140 ? -20.598 -1.320  -16.020 1.00 41.85  ? 149 LEU   B CD2 1 
ATOM   1442 N N   . TYR   B 2 141 ? -15.958 -1.080  -17.551 1.00 38.80  ? 150 TYR   B N   1 
ATOM   1443 C CA  . TYR   B 2 141 ? -14.615 -0.699  -18.008 1.00 40.56  ? 150 TYR   B CA  1 
ATOM   1444 C C   . TYR   B 2 141 ? -14.082 0.422   -17.148 1.00 40.96  ? 150 TYR   B C   1 
ATOM   1445 O O   . TYR   B 2 141 ? -14.779 1.417   -16.930 1.00 40.92  ? 150 TYR   B O   1 
ATOM   1446 C CB  . TYR   B 2 141 ? -14.681 -0.244  -19.471 1.00 42.95  ? 150 TYR   B CB  1 
ATOM   1447 C CG  . TYR   B 2 141 ? -13.430 0.390   -20.031 1.00 43.30  ? 150 TYR   B CG  1 
ATOM   1448 C CD1 . TYR   B 2 141 ? -13.264 1.769   -20.026 1.00 43.71  ? 150 TYR   B CD1 1 
ATOM   1449 C CD2 . TYR   B 2 141 ? -12.401 -0.398  -20.547 1.00 45.79  ? 150 TYR   B CD2 1 
ATOM   1450 C CE1 . TYR   B 2 141 ? -12.113 2.344   -20.560 1.00 46.04  ? 150 TYR   B CE1 1 
ATOM   1451 C CE2 . TYR   B 2 141 ? -11.263 0.163   -21.111 1.00 45.06  ? 150 TYR   B CE2 1 
ATOM   1452 C CZ  . TYR   B 2 141 ? -11.111 1.542   -21.120 1.00 48.24  ? 150 TYR   B CZ  1 
ATOM   1453 O OH  . TYR   B 2 141 ? -9.986  2.113   -21.684 1.00 50.64  ? 150 TYR   B OH  1 
ATOM   1454 N N   . GLY   B 2 142 ? -12.831 0.324   -16.749 1.00 40.93  ? 151 GLY   B N   1 
ATOM   1455 C CA  . GLY   B 2 142 ? -12.185 1.509   -16.151 1.00 42.80  ? 151 GLY   B CA  1 
ATOM   1456 C C   . GLY   B 2 142 ? -11.352 1.207   -14.909 1.00 42.81  ? 151 GLY   B C   1 
ATOM   1457 O O   . GLY   B 2 142 ? -10.747 2.179   -14.401 1.00 43.39  ? 151 GLY   B O   1 
ATOM   1458 N N   . ASN   B 2 143 ? -11.219 -0.064  -14.474 1.00 41.38  ? 152 ASN   B N   1 
ATOM   1459 C CA  . ASN   B 2 143 ? -10.237 -0.391  -13.406 1.00 40.51  ? 152 ASN   B CA  1 
ATOM   1460 C C   . ASN   B 2 143 ? -9.289  -1.490  -13.880 1.00 39.19  ? 152 ASN   B C   1 
ATOM   1461 O O   . ASN   B 2 143 ? -9.733  -2.594  -14.102 1.00 39.13  ? 152 ASN   B O   1 
ATOM   1462 C CB  . ASN   B 2 143 ? -10.903 -0.823  -12.106 1.00 39.52  ? 152 ASN   B CB  1 
ATOM   1463 C CG  . ASN   B 2 143 ? -9.992  -0.797  -10.894 1.00 40.74  ? 152 ASN   B CG  1 
ATOM   1464 O OD1 . ASN   B 2 143 ? -9.055  0.032   -10.773 1.00 44.28  ? 152 ASN   B OD1 1 
ATOM   1465 N ND2 . ASN   B 2 143 ? -10.271 -1.712  -9.985  1.00 38.63  ? 152 ASN   B ND2 1 
ATOM   1466 N N   . GLY   B 2 144 ? -8.015  -1.172  -13.950 1.00 39.71  ? 153 GLY   B N   1 
ATOM   1467 C CA  . GLY   B 2 144 ? -6.979  -2.125  -14.339 1.00 42.97  ? 153 GLY   B CA  1 
ATOM   1468 C C   . GLY   B 2 144 ? -5.613  -1.505  -14.199 1.00 45.87  ? 153 GLY   B C   1 
ATOM   1469 O O   . GLY   B 2 144 ? -5.334  -0.854  -13.138 1.00 46.60  ? 153 GLY   B O   1 
ATOM   1470 N N   . VAL   B 2 145 ? -4.777  -1.718  -15.214 1.00 50.41  ? 154 VAL   B N   1 
ATOM   1471 C CA  . VAL   B 2 145 ? -3.308  -1.620  -15.083 1.00 52.36  ? 154 VAL   B CA  1 
ATOM   1472 C C   . VAL   B 2 145 ? -2.714  -0.961  -16.341 1.00 58.79  ? 154 VAL   B C   1 
ATOM   1473 O O   . VAL   B 2 145 ? -3.268  -1.123  -17.448 1.00 56.95  ? 154 VAL   B O   1 
ATOM   1474 C CB  . VAL   B 2 145 ? -2.810  -3.041  -14.756 1.00 54.24  ? 154 VAL   B CB  1 
ATOM   1475 C CG1 . VAL   B 2 145 ? -2.546  -3.937  -15.967 1.00 51.64  ? 154 VAL   B CG1 1 
ATOM   1476 C CG2 . VAL   B 2 145 ? -1.636  -2.991  -13.804 1.00 58.48  ? 154 VAL   B CG2 1 
ATOM   1477 N N   . VAL   B 2 146 ? -1.625  -0.213  -16.162 1.00 62.91  ? 155 VAL   B N   1 
ATOM   1478 C CA  . VAL   B 2 146 ? -0.784  0.332   -17.268 1.00 67.67  ? 155 VAL   B CA  1 
ATOM   1479 C C   . VAL   B 2 146 ? 0.285   -0.715  -17.575 1.00 70.12  ? 155 VAL   B C   1 
ATOM   1480 O O   . VAL   B 2 146 ? 0.784   -1.290  -16.603 1.00 70.44  ? 155 VAL   B O   1 
ATOM   1481 C CB  . VAL   B 2 146 ? -0.230  1.706   -16.857 1.00 68.57  ? 155 VAL   B CB  1 
ATOM   1482 C CG1 . VAL   B 2 146 ? 0.862   2.190   -17.781 1.00 70.94  ? 155 VAL   B CG1 1 
ATOM   1483 C CG2 . VAL   B 2 146 ? -1.363  2.724   -16.781 1.00 67.79  ? 155 VAL   B CG2 1 
ATOM   1484 N N   . ILE   B 2 147 ? 0.552   -1.035  -18.855 1.00 74.54  ? 156 ILE   B N   1 
ATOM   1485 C CA  . ILE   B 2 147 ? 1.314   -2.277  -19.214 1.00 78.35  ? 156 ILE   B CA  1 
ATOM   1486 C C   . ILE   B 2 147 ? 2.702   -1.904  -19.733 1.00 83.26  ? 156 ILE   B C   1 
ATOM   1487 O O   . ILE   B 2 147 ? 2.954   -0.715  -19.951 1.00 78.51  ? 156 ILE   B O   1 
ATOM   1488 C CB  . ILE   B 2 147 ? 0.541   -3.191  -20.191 1.00 80.18  ? 156 ILE   B CB  1 
ATOM   1489 C CG1 . ILE   B 2 147 ? -0.130  -2.441  -21.351 1.00 80.39  ? 156 ILE   B CG1 1 
ATOM   1490 C CG2 . ILE   B 2 147 ? -0.456  -4.049  -19.426 1.00 78.01  ? 156 ILE   B CG2 1 
ATOM   1491 C CD1 . ILE   B 2 147 ? -0.407  -3.325  -22.544 1.00 77.67  ? 156 ILE   B CD1 1 
ATOM   1492 N N   A LYS   B 2 148 ? 3.571   -2.912  -19.909 0.25 86.58  ? 157 LYS   B N   1 
ATOM   1493 N N   B LYS   B 2 148 ? 3.571   -2.912  -19.909 0.25 86.58  ? 157 LYS   B N   1 
ATOM   1494 N N   C LYS   B 2 148 ? 3.570   -2.911  -19.906 0.25 86.13  ? 157 LYS   B N   1 
ATOM   1495 N N   D LYS   B 2 148 ? 3.570   -2.911  -19.906 0.25 86.13  ? 157 LYS   B N   1 
ATOM   1496 C CA  A LYS   B 2 148 ? 4.962   -2.774  -20.427 0.25 90.54  ? 157 LYS   B CA  1 
ATOM   1497 C CA  B LYS   B 2 148 ? 4.962   -2.774  -20.427 0.25 90.54  ? 157 LYS   B CA  1 
ATOM   1498 C CA  C LYS   B 2 148 ? 4.979   -2.773  -20.368 0.25 89.75  ? 157 LYS   B CA  1 
ATOM   1499 C CA  D LYS   B 2 148 ? 4.979   -2.773  -20.368 0.25 89.75  ? 157 LYS   B CA  1 
ATOM   1500 C C   A LYS   B 2 148 ? 5.034   -1.588  -21.393 0.25 91.87  ? 157 LYS   B C   1 
ATOM   1501 C C   B LYS   B 2 148 ? 5.034   -1.588  -21.393 0.25 91.87  ? 157 LYS   B C   1 
ATOM   1502 C C   C LYS   B 2 148 ? 5.096   -1.627  -21.378 0.25 91.30  ? 157 LYS   B C   1 
ATOM   1503 C C   D LYS   B 2 148 ? 5.096   -1.627  -21.378 0.25 91.30  ? 157 LYS   B C   1 
ATOM   1504 O O   A LYS   B 2 148 ? 5.895   -0.711  -21.189 0.25 93.84  ? 157 LYS   B O   1 
ATOM   1505 O O   B LYS   B 2 148 ? 5.895   -0.711  -21.189 0.25 93.84  ? 157 LYS   B O   1 
ATOM   1506 O O   C LYS   B 2 148 ? 6.047   -0.833  -21.258 0.25 93.34  ? 157 LYS   B O   1 
ATOM   1507 O O   D LYS   B 2 148 ? 6.047   -0.833  -21.258 0.25 93.34  ? 157 LYS   B O   1 
ATOM   1508 C CB  A LYS   B 2 148 ? 5.403   -4.054  -21.146 0.25 92.60  ? 157 LYS   B CB  1 
ATOM   1509 C CB  B LYS   B 2 148 ? 5.403   -4.054  -21.146 0.25 92.60  ? 157 LYS   B CB  1 
ATOM   1510 C CB  C LYS   B 2 148 ? 5.457   -4.082  -21.003 0.25 91.30  ? 157 LYS   B CB  1 
ATOM   1511 C CB  D LYS   B 2 148 ? 5.457   -4.082  -21.003 0.25 91.30  ? 157 LYS   B CB  1 
ATOM   1512 C CG  A LYS   B 2 148 ? 5.689   -5.248  -20.245 0.25 93.50  ? 157 LYS   B CG  1 
ATOM   1513 C CG  B LYS   B 2 148 ? 5.689   -5.248  -20.245 0.25 93.50  ? 157 LYS   B CG  1 
ATOM   1514 C CG  C LYS   B 2 148 ? 5.509   -5.274  -20.058 0.25 91.51  ? 157 LYS   B CG  1 
ATOM   1515 C CG  D LYS   B 2 148 ? 5.509   -5.274  -20.058 0.25 91.51  ? 157 LYS   B CG  1 
ATOM   1516 C CD  A LYS   B 2 148 ? 5.895   -6.547  -21.005 0.25 95.04  ? 157 LYS   B CD  1 
ATOM   1517 C CD  B LYS   B 2 148 ? 5.895   -6.547  -21.005 0.25 95.04  ? 157 LYS   B CD  1 
ATOM   1518 C CD  C LYS   B 2 148 ? 5.965   -6.553  -20.727 0.25 92.74  ? 157 LYS   B CD  1 
ATOM   1519 C CD  D LYS   B 2 148 ? 5.965   -6.553  -20.727 0.25 92.74  ? 157 LYS   B CD  1 
ATOM   1520 C CE  A LYS   B 2 148 ? 7.031   -6.494  -22.007 0.25 96.96  ? 157 LYS   B CE  1 
ATOM   1521 C CE  B LYS   B 2 148 ? 7.031   -6.494  -22.007 0.25 96.96  ? 157 LYS   B CE  1 
ATOM   1522 C CE  C LYS   B 2 148 ? 6.350   -7.636  -19.742 0.25 92.66  ? 157 LYS   B CE  1 
ATOM   1523 C CE  D LYS   B 2 148 ? 6.350   -7.636  -19.742 0.25 92.66  ? 157 LYS   B CE  1 
ATOM   1524 N NZ  A LYS   B 2 148 ? 8.352   -6.685  -21.359 0.25 97.56  ? 157 LYS   B NZ  1 
ATOM   1525 N NZ  B LYS   B 2 148 ? 8.352   -6.685  -21.359 0.25 97.56  ? 157 LYS   B NZ  1 
ATOM   1526 N NZ  C LYS   B 2 148 ? 7.117   -8.718  -20.404 0.25 93.72  ? 157 LYS   B NZ  1 
ATOM   1527 N NZ  D LYS   B 2 148 ? 7.117   -8.718  -20.404 0.25 93.72  ? 157 LYS   B NZ  1 
ATOM   1528 N N   A ASN   B 2 149 ? 4.139   -1.574  -22.386 0.25 92.29  ? 158 ASN   B N   1 
ATOM   1529 N N   B ASN   B 2 149 ? 4.139   -1.574  -22.386 0.25 92.29  ? 158 ASN   B N   1 
ATOM   1530 N N   C ASN   B 2 149 ? 4.154   -1.561  -22.325 0.25 91.91  ? 158 ASN   B N   1 
ATOM   1531 N N   D ASN   B 2 149 ? 4.154   -1.561  -22.325 0.25 91.91  ? 158 ASN   B N   1 
ATOM   1532 C CA  A ASN   B 2 149 ? 4.058   -0.570  -23.480 0.25 92.62  ? 158 ASN   B CA  1 
ATOM   1533 C CA  B ASN   B 2 149 ? 4.058   -0.570  -23.480 0.25 92.62  ? 158 ASN   B CA  1 
ATOM   1534 C CA  C ASN   B 2 149 ? 4.106   -0.575  -23.439 0.25 92.45  ? 158 ASN   B CA  1 
ATOM   1535 C CA  D ASN   B 2 149 ? 4.106   -0.575  -23.439 0.25 92.45  ? 158 ASN   B CA  1 
ATOM   1536 C C   A ASN   B 2 149 ? 3.828   0.830   -22.897 0.25 91.19  ? 158 ASN   B C   1 
ATOM   1537 C C   B ASN   B 2 149 ? 3.828   0.830   -22.897 0.25 91.19  ? 158 ASN   B C   1 
ATOM   1538 C C   C ASN   B 2 149 ? 3.836   0.832   -22.890 0.25 91.09  ? 158 ASN   B C   1 
ATOM   1539 C C   D ASN   B 2 149 ? 3.836   0.832   -22.890 0.25 91.09  ? 158 ASN   B C   1 
ATOM   1540 O O   A ASN   B 2 149 ? 4.627   1.737   -23.205 0.25 92.17  ? 158 ASN   B O   1 
ATOM   1541 O O   B ASN   B 2 149 ? 4.627   1.737   -23.205 0.25 92.17  ? 158 ASN   B O   1 
ATOM   1542 O O   C ASN   B 2 149 ? 4.613   1.751   -23.218 0.25 92.07  ? 158 ASN   B O   1 
ATOM   1543 O O   D ASN   B 2 149 ? 4.613   1.751   -23.218 0.25 92.07  ? 158 ASN   B O   1 
ATOM   1544 C CB  A ASN   B 2 149 ? 2.940   -0.921  -24.467 0.25 93.56  ? 158 ASN   B CB  1 
ATOM   1545 C CB  B ASN   B 2 149 ? 2.940   -0.921  -24.467 0.25 93.56  ? 158 ASN   B CB  1 
ATOM   1546 C CB  C ASN   B 2 149 ? 3.044   -0.964  -24.473 0.25 93.63  ? 158 ASN   B CB  1 
ATOM   1547 C CB  D ASN   B 2 149 ? 3.044   -0.964  -24.473 0.25 93.63  ? 158 ASN   B CB  1 
ATOM   1548 C CG  A ASN   B 2 149 ? 2.649   -2.407  -24.528 0.25 93.54  ? 158 ASN   B CG  1 
ATOM   1549 C CG  B ASN   B 2 149 ? 2.649   -2.407  -24.528 0.25 93.54  ? 158 ASN   B CG  1 
ATOM   1550 C CG  C ASN   B 2 149 ? 3.037   -2.446  -24.791 0.25 94.14  ? 158 ASN   B CG  1 
ATOM   1551 C CG  D ASN   B 2 149 ? 3.037   -2.446  -24.791 0.25 94.14  ? 158 ASN   B CG  1 
ATOM   1552 O OD1 A ASN   B 2 149 ? 3.422   -3.221  -24.027 0.25 94.18  ? 158 ASN   B OD1 1 
ATOM   1553 O OD1 B ASN   B 2 149 ? 3.422   -3.221  -24.027 0.25 94.18  ? 158 ASN   B OD1 1 
ATOM   1554 O OD1 C ASN   B 2 149 ? 4.046   -3.129  -24.627 0.25 95.37  ? 158 ASN   B OD1 1 
ATOM   1555 O OD1 D ASN   B 2 149 ? 4.046   -3.129  -24.627 0.25 95.37  ? 158 ASN   B OD1 1 
ATOM   1556 N ND2 A ASN   B 2 149 ? 1.532   -2.770  -25.137 0.25 93.61  ? 158 ASN   B ND2 1 
ATOM   1557 N ND2 B ASN   B 2 149 ? 1.532   -2.770  -25.137 0.25 93.61  ? 158 ASN   B ND2 1 
ATOM   1558 N ND2 C ASN   B 2 149 ? 1.903   -2.952  -25.248 0.25 94.00  ? 158 ASN   B ND2 1 
ATOM   1559 N ND2 D ASN   B 2 149 ? 1.903   -2.952  -25.248 0.25 94.00  ? 158 ASN   B ND2 1 
ATOM   1560 N N   . GLY   B 2 150 ? 2.774   0.986   -22.090 1.00 90.05  ? 159 GLY   B N   1 
ATOM   1561 C CA  . GLY   B 2 150 ? 2.282   2.304   -21.623 1.00 84.60  ? 159 GLY   B CA  1 
ATOM   1562 C C   . GLY   B 2 150 ? 0.784   2.465   -21.858 1.00 80.45  ? 159 GLY   B C   1 
ATOM   1563 O O   . GLY   B 2 150 ? 0.178   3.429   -21.328 1.00 74.81  ? 159 GLY   B O   1 
ATOM   1564 N N   A SER   B 2 151 ? 0.192   1.553   -22.642 0.25 79.86  ? 160 SER   B N   1 
ATOM   1565 N N   B SER   B 2 151 ? 0.202   1.549   -22.643 0.25 80.15  ? 160 SER   B N   1 
ATOM   1566 N N   C SER   B 2 151 ? 0.192   1.553   -22.642 0.25 79.86  ? 160 SER   B N   1 
ATOM   1567 N N   D SER   B 2 151 ? 0.202   1.549   -22.643 0.25 80.15  ? 160 SER   B N   1 
ATOM   1568 C CA  A SER   B 2 151 ? -1.271  1.460   -22.898 0.25 77.45  ? 160 SER   B CA  1 
ATOM   1569 C CA  B SER   B 2 151 ? -1.256  1.408   -22.906 0.25 77.93  ? 160 SER   B CA  1 
ATOM   1570 C CA  C SER   B 2 151 ? -1.271  1.460   -22.898 0.25 77.45  ? 160 SER   B CA  1 
ATOM   1571 C CA  D SER   B 2 151 ? -1.256  1.408   -22.906 0.25 77.93  ? 160 SER   B CA  1 
ATOM   1572 C C   A SER   B 2 151 ? -2.001  0.978   -21.634 0.25 74.96  ? 160 SER   B C   1 
ATOM   1573 C C   B SER   B 2 151 ? -1.998  0.974   -21.631 0.25 75.20  ? 160 SER   B C   1 
ATOM   1574 C C   C SER   B 2 151 ? -2.001  0.978   -21.634 0.25 74.96  ? 160 SER   B C   1 
ATOM   1575 C C   D SER   B 2 151 ? -1.998  0.974   -21.631 0.25 75.20  ? 160 SER   B C   1 
ATOM   1576 O O   A SER   B 2 151 ? -1.322  0.524   -20.685 0.25 73.12  ? 160 SER   B O   1 
ATOM   1577 O O   B SER   B 2 151 ? -1.325  0.547   -20.665 0.25 73.29  ? 160 SER   B O   1 
ATOM   1578 O O   C SER   B 2 151 ? -1.322  0.524   -20.685 0.25 73.12  ? 160 SER   B O   1 
ATOM   1579 O O   D SER   B 2 151 ? -1.325  0.547   -20.665 0.25 73.29  ? 160 SER   B O   1 
ATOM   1580 C CB  A SER   B 2 151 ? -1.561  0.557   -24.071 0.25 77.78  ? 160 SER   B CB  1 
ATOM   1581 C CB  B SER   B 2 151 ? -1.467  0.421   -24.022 0.25 78.54  ? 160 SER   B CB  1 
ATOM   1582 C CB  C SER   B 2 151 ? -1.561  0.557   -24.071 0.25 77.78  ? 160 SER   B CB  1 
ATOM   1583 C CB  D SER   B 2 151 ? -1.467  0.421   -24.022 0.25 78.54  ? 160 SER   B CB  1 
ATOM   1584 O OG  A SER   B 2 151 ? -2.883  0.765   -24.545 0.25 77.74  ? 160 SER   B OG  1 
ATOM   1585 O OG  B SER   B 2 151 ? -0.492  -0.612  -23.954 0.25 79.88  ? 160 SER   B OG  1 
ATOM   1586 O OG  C SER   B 2 151 ? -2.883  0.765   -24.545 0.25 77.74  ? 160 SER   B OG  1 
ATOM   1587 O OG  D SER   B 2 151 ? -0.492  -0.612  -23.954 0.25 79.88  ? 160 SER   B OG  1 
ATOM   1588 N N   . TYR   B 2 152 ? -3.335  1.066   -21.639 1.00 73.28  ? 161 TYR   B N   1 
ATOM   1589 C CA  . TYR   B 2 152 ? -4.210  0.685   -20.494 1.00 71.35  ? 161 TYR   B CA  1 
ATOM   1590 C C   . TYR   B 2 152 ? -4.931  -0.633  -20.780 1.00 65.46  ? 161 TYR   B C   1 
ATOM   1591 O O   . TYR   B 2 152 ? -5.526  -0.770  -21.816 1.00 61.07  ? 161 TYR   B O   1 
ATOM   1592 C CB  . TYR   B 2 152 ? -5.282  1.742   -20.204 1.00 71.90  ? 161 TYR   B CB  1 
ATOM   1593 C CG  . TYR   B 2 152 ? -5.909  1.614   -18.833 1.00 73.94  ? 161 TYR   B CG  1 
ATOM   1594 C CD1 . TYR   B 2 152 ? -5.187  1.964   -17.704 1.00 73.48  ? 161 TYR   B CD1 1 
ATOM   1595 C CD2 . TYR   B 2 152 ? -7.197  1.130   -18.642 1.00 74.21  ? 161 TYR   B CD2 1 
ATOM   1596 C CE1 . TYR   B 2 152 ? -5.708  1.836   -16.428 1.00 71.74  ? 161 TYR   B CE1 1 
ATOM   1597 C CE2 . TYR   B 2 152 ? -7.734  0.996   -17.363 1.00 74.00  ? 161 TYR   B CE2 1 
ATOM   1598 C CZ  . TYR   B 2 152 ? -6.988  1.346   -16.244 1.00 73.28  ? 161 TYR   B CZ  1 
ATOM   1599 O OH  . TYR   B 2 152 ? -7.453  1.249   -14.946 1.00 73.14  ? 161 TYR   B OH  1 
ATOM   1600 N N   . VAL   B 2 153 ? -4.951  -1.529  -19.799 1.00 59.80  ? 162 VAL   B N   1 
ATOM   1601 C CA  . VAL   B 2 153 ? -5.776  -2.770  -19.795 1.00 55.40  ? 162 VAL   B CA  1 
ATOM   1602 C C   . VAL   B 2 153 ? -6.728  -2.753  -18.589 1.00 51.03  ? 162 VAL   B C   1 
ATOM   1603 O O   . VAL   B 2 153 ? -6.263  -2.731  -17.466 1.00 46.78  ? 162 VAL   B O   1 
ATOM   1604 C CB  . VAL   B 2 153 ? -4.864  -4.008  -19.764 1.00 53.69  ? 162 VAL   B CB  1 
ATOM   1605 C CG1 . VAL   B 2 153 ? -5.637  -5.290  -20.021 1.00 51.95  ? 162 VAL   B CG1 1 
ATOM   1606 C CG2 . VAL   B 2 153 ? -3.696  -3.843  -20.715 1.00 59.73  ? 162 VAL   B CG2 1 
ATOM   1607 N N   . SER   B 2 154 ? -8.016  -2.896  -18.834 1.00 49.59  ? 163 SER   B N   1 
ATOM   1608 C CA  . SER   B 2 154 ? -9.091  -2.795  -17.831 1.00 47.44  ? 163 SER   B CA  1 
ATOM   1609 C C   . SER   B 2 154 ? -9.599  -4.203  -17.550 1.00 45.01  ? 163 SER   B C   1 
ATOM   1610 O O   . SER   B 2 154 ? -9.782  -4.958  -18.504 1.00 44.51  ? 163 SER   B O   1 
ATOM   1611 C CB  . SER   B 2 154 ? -10.211 -1.900  -18.281 1.00 45.68  ? 163 SER   B CB  1 
ATOM   1612 O OG  . SER   B 2 154 ? -11.384 -2.136  -17.470 1.00 44.05  ? 163 SER   B OG  1 
ATOM   1613 N N   . ALA   B 2 155 ? -9.886  -4.492  -16.286 1.00 40.93  ? 164 ALA   B N   1 
ATOM   1614 C CA  . ALA   B 2 155 ? -10.632 -5.690  -15.879 1.00 40.19  ? 164 ALA   B CA  1 
ATOM   1615 C C   . ALA   B 2 155 ? -12.008 -5.523  -16.500 1.00 41.59  ? 164 ALA   B C   1 
ATOM   1616 O O   . ALA   B 2 155 ? -12.472 -4.358  -16.637 1.00 43.15  ? 164 ALA   B O   1 
ATOM   1617 C CB  . ALA   B 2 155 ? -10.738 -5.804  -14.373 1.00 40.63  ? 164 ALA   B CB  1 
ATOM   1618 N N   . ILE   B 2 156 ? -12.653 -6.645  -16.776 1.00 41.56  ? 165 ILE   B N   1 
ATOM   1619 C CA  . ILE   B 2 156 ? -14.130 -6.744  -16.808 1.00 41.70  ? 165 ILE   B CA  1 
ATOM   1620 C C   . ILE   B 2 156 ? -14.636 -6.862  -15.359 1.00 40.59  ? 165 ILE   B C   1 
ATOM   1621 O O   . ILE   B 2 156 ? -14.822 -8.003  -14.840 1.00 40.78  ? 165 ILE   B O   1 
ATOM   1622 C CB  . ILE   B 2 156 ? -14.560 -7.921  -17.696 1.00 43.51  ? 165 ILE   B CB  1 
ATOM   1623 C CG1 . ILE   B 2 156 ? -13.799 -7.882  -19.029 1.00 45.81  ? 165 ILE   B CG1 1 
ATOM   1624 C CG2 . ILE   B 2 156 ? -16.085 -7.913  -17.864 1.00 42.44  ? 165 ILE   B CG2 1 
ATOM   1625 C CD1 . ILE   B 2 156 ? -14.166 -8.979  -19.985 1.00 47.99  ? 165 ILE   B CD1 1 
ATOM   1626 N N   . THR   B 2 157 ? -14.913 -5.721  -14.719 1.00 40.72  ? 166 THR   B N   1 
ATOM   1627 C CA  . THR   B 2 157 ? -15.395 -5.658  -13.320 1.00 38.83  ? 166 THR   B CA  1 
ATOM   1628 C C   . THR   B 2 157 ? -16.917 -5.821  -13.267 1.00 40.29  ? 166 THR   B C   1 
ATOM   1629 O O   . THR   B 2 157 ? -17.625 -4.853  -13.716 1.00 39.53  ? 166 THR   B O   1 
ATOM   1630 C CB  . THR   B 2 157 ? -14.992 -4.335  -12.693 1.00 41.07  ? 166 THR   B CB  1 
ATOM   1631 O OG1 . THR   B 2 157 ? -13.572 -4.294  -12.819 1.00 39.40  ? 166 THR   B OG1 1 
ATOM   1632 C CG2 . THR   B 2 157 ? -15.475 -4.232  -11.264 1.00 40.29  ? 166 THR   B CG2 1 
ATOM   1633 N N   . GLN   B 2 158 ? -17.397 -6.924  -12.679 1.00 38.10  ? 167 GLN   B N   1 
ATOM   1634 C CA  . GLN   B 2 158 ? -18.813 -7.244  -12.417 1.00 39.59  ? 167 GLN   B CA  1 
ATOM   1635 C C   . GLN   B 2 158 ? -19.084 -7.340  -10.901 1.00 42.12  ? 167 GLN   B C   1 
ATOM   1636 O O   . GLN   B 2 158 ? -18.185 -7.797  -10.163 1.00 41.47  ? 167 GLN   B O   1 
ATOM   1637 C CB  . GLN   B 2 158 ? -19.125 -8.548  -13.125 1.00 39.73  ? 167 GLN   B CB  1 
ATOM   1638 C CG  . GLN   B 2 158 ? -20.590 -8.912  -13.125 1.00 39.20  ? 167 GLN   B CG  1 
ATOM   1639 C CD  . GLN   B 2 158 ? -21.468 -7.794  -13.670 1.00 40.66  ? 167 GLN   B CD  1 
ATOM   1640 O OE1 . GLN   B 2 158 ? -21.529 -6.674  -13.125 1.00 38.78  ? 167 GLN   B OE1 1 
ATOM   1641 N NE2 . GLN   B 2 158 ? -22.219 -8.117  -14.721 1.00 40.23  ? 167 GLN   B NE2 1 
ATOM   1642 N N   . GLY   B 2 159 ? -20.270 -6.893  -10.465 1.00 45.03  ? 168 GLY   B N   1 
ATOM   1643 C CA  . GLY   B 2 159 ? -20.791 -7.045  -9.091  1.00 48.64  ? 168 GLY   B CA  1 
ATOM   1644 C C   . GLY   B 2 159 ? -21.577 -8.338  -8.930  1.00 53.14  ? 168 GLY   B C   1 
ATOM   1645 O O   . GLY   B 2 159 ? -21.818 -9.036  -9.909  1.00 57.61  ? 168 GLY   B O   1 
ATOM   1646 N N   . LYS   B 2 160 ? -21.909 -8.679  -7.693  1.00 61.60  ? 169 LYS   B N   1 
ATOM   1647 C CA  . LYS   B 2 160 ? -22.813 -9.793  -7.307  1.00 64.36  ? 169 LYS   B CA  1 
ATOM   1648 C C   . LYS   B 2 160 ? -24.247 -9.233  -7.237  1.00 67.36  ? 169 LYS   B C   1 
ATOM   1649 O O   . LYS   B 2 160 ? -24.429 -8.106  -6.723  1.00 62.52  ? 169 LYS   B O   1 
ATOM   1650 C CB  . LYS   B 2 160 ? -22.323 -10.384 -5.978  1.00 69.01  ? 169 LYS   B CB  1 
ATOM   1651 C CG  . LYS   B 2 160 ? -22.906 -11.748 -5.659  1.00 75.15  ? 169 LYS   B CG  1 
ATOM   1652 C CD  . LYS   B 2 160 ? -22.741 -12.200 -4.230  1.00 77.06  ? 169 LYS   B CD  1 
ATOM   1653 C CE  . LYS   B 2 160 ? -23.683 -13.335 -3.893  1.00 76.85  ? 169 LYS   B CE  1 
ATOM   1654 N NZ  . LYS   B 2 160 ? -23.596 -13.690 -2.459  1.00 81.24  ? 169 LYS   B NZ  1 
ATOM   1655 N N   . ARG   B 2 161 ? -25.233 -9.965  -7.761  1.00 69.95  ? 170 ARG   B N   1 
ATOM   1656 C CA  . ARG   B 2 161 ? -26.689 -9.707  -7.537  1.00 74.61  ? 170 ARG   B CA  1 
ATOM   1657 C C   . ARG   B 2 161 ? -27.167 -10.676 -6.434  1.00 79.40  ? 170 ARG   B C   1 
ATOM   1658 O O   . ARG   B 2 161 ? -26.799 -11.866 -6.533  1.00 79.77  ? 170 ARG   B O   1 
ATOM   1659 C CB  . ARG   B 2 161 ? -27.417 -9.862  -8.885  1.00 74.32  ? 170 ARG   B CB  1 
ATOM   1660 C CG  . ARG   B 2 161 ? -28.906 -9.530  -8.891  1.00 73.06  ? 170 ARG   B CG  1 
ATOM   1661 C CD  . ARG   B 2 161 ? -29.633 -9.931  -10.179 1.00 74.54  ? 170 ARG   B CD  1 
ATOM   1662 N NE  . ARG   B 2 161 ? -31.082 -9.701  -10.108 1.00 73.83  ? 170 ARG   B NE  1 
ATOM   1663 C CZ  . ARG   B 2 161 ? -31.801 -8.820  -10.827 1.00 71.74  ? 170 ARG   B CZ  1 
ATOM   1664 N NH1 . ARG   B 2 161 ? -31.247 -8.031  -11.733 1.00 65.82  ? 170 ARG   B NH1 1 
ATOM   1665 N NH2 . ARG   B 2 161 ? -33.106 -8.738  -10.626 1.00 73.95  ? 170 ARG   B NH2 1 
ATOM   1666 N N   . GLU   B 2 162 ? -27.917 -10.203 -5.420  1.00 83.88  ? 171 GLU   B N   1 
ATOM   1667 C CA  . GLU   B 2 162 ? -28.491 -11.035 -4.311  1.00 88.10  ? 171 GLU   B CA  1 
ATOM   1668 C C   . GLU   B 2 162 ? -29.996 -11.238 -4.542  1.00 84.82  ? 171 GLU   B C   1 
ATOM   1669 O O   . GLU   B 2 162 ? -30.599 -12.244 -4.152  1.00 88.16  ? 171 GLU   B O   1 
ATOM   1670 C CB  . GLU   B 2 162 ? -28.254 -10.379 -2.944  1.00 93.87  ? 171 GLU   B CB  1 
ATOM   1671 C CG  . GLU   B 2 162 ? -26.790 -10.046 -2.628  1.00 96.96  ? 171 GLU   B CG  1 
ATOM   1672 C CD  . GLU   B 2 162 ? -26.072 -10.986 -1.661  1.00 100.23 ? 171 GLU   B CD  1 
ATOM   1673 O OE1 . GLU   B 2 162 ? -25.435 -10.481 -0.719  1.00 96.88  ? 171 GLU   B OE1 1 
ATOM   1674 O OE2 . GLU   B 2 162 ? -26.144 -12.223 -1.848  1.00 101.23 ? 171 GLU   B OE2 1 
HETATM 1675 S S   A DMS   C 3 .   ? -8.089  5.645   -18.123 0.19 63.55  ? 201 DMS   B S   1 
HETATM 1676 S S   B DMS   C 3 .   ? -8.089  5.644   -18.123 0.15 63.51  ? 201 DMS   B S   1 
HETATM 1677 O O   A DMS   C 3 .   ? -6.675  5.295   -18.500 0.19 63.32  ? 201 DMS   B O   1 
HETATM 1678 O O   B DMS   C 3 .   ? -6.675  5.293   -18.500 0.15 63.39  ? 201 DMS   B O   1 
HETATM 1679 C C1  A DMS   C 3 .   ? -8.257  5.259   -16.398 0.19 63.48  ? 201 DMS   B C1  1 
HETATM 1680 C C1  B DMS   C 3 .   ? -8.255  5.259   -16.398 0.15 63.37  ? 201 DMS   B C1  1 
HETATM 1681 C C2  A DMS   C 3 .   ? -9.121  4.345   -18.755 0.19 62.64  ? 201 DMS   B C2  1 
HETATM 1682 C C2  B DMS   C 3 .   ? -9.120  4.345   -18.755 0.15 62.72  ? 201 DMS   B C2  1 
HETATM 1683 S S   A DMS   D 3 .   ? -17.687 11.598  -0.249  0.50 713.90 ? 202 DMS   B S   1 
HETATM 1684 S S   B DMS   D 3 .   ? -17.687 11.598  -0.249  0.50 713.90 ? 202 DMS   B S   1 
HETATM 1685 O O   A DMS   D 3 .   ? -17.878 10.110  -0.157  0.50 708.26 ? 202 DMS   B O   1 
HETATM 1686 O O   B DMS   D 3 .   ? -17.878 10.110  -0.157  0.50 708.26 ? 202 DMS   B O   1 
HETATM 1687 C C1  A DMS   D 3 .   ? -19.285 12.275  -0.620  0.50 713.10 ? 202 DMS   B C1  1 
HETATM 1688 C C1  B DMS   D 3 .   ? -19.285 12.275  -0.620  0.50 713.10 ? 202 DMS   B C1  1 
HETATM 1689 C C2  A DMS   D 3 .   ? -16.929 11.909  -1.822  0.50 693.86 ? 202 DMS   B C2  1 
HETATM 1690 C C2  B DMS   D 3 .   ? -16.929 11.909  -1.822  0.50 693.86 ? 202 DMS   B C2  1 
HETATM 1691 S S   A DMS   E 3 .   ? -6.382  2.643   -13.135 0.19 64.63  ? 203 DMS   B S   1 
HETATM 1692 S S   B DMS   E 3 .   ? -6.384  2.645   -13.135 0.15 64.67  ? 203 DMS   B S   1 
HETATM 1693 O O   A DMS   E 3 .   ? -5.657  1.901   -12.055 0.19 63.85  ? 203 DMS   B O   1 
HETATM 1694 O O   B DMS   E 3 .   ? -5.657  1.899   -12.058 0.15 63.94  ? 203 DMS   B O   1 
HETATM 1695 C C1  A DMS   E 3 .   ? -7.893  3.222   -12.395 0.19 64.63  ? 203 DMS   B C1  1 
HETATM 1696 C C1  B DMS   E 3 .   ? -7.893  3.223   -12.393 0.15 64.56  ? 203 DMS   B C1  1 
HETATM 1697 C C2  A DMS   E 3 .   ? -5.567  4.214   -13.280 0.19 65.31  ? 203 DMS   B C2  1 
HETATM 1698 C C2  B DMS   E 3 .   ? -5.568  4.215   -13.279 0.15 65.30  ? 203 DMS   B C2  1 
HETATM 1699 N N1  C A1BGK F 4 .   ? -8.698  4.501   -13.664 0.34 58.96  ? 204 A1BGK B N1  1 
HETATM 1700 N N1  D A1BGK F 4 .   ? -8.697  4.502   -13.665 0.32 59.06  ? 204 A1BGK B N1  1 
HETATM 1701 N N3  C A1BGK F 4 .   ? -8.388  5.523   -10.252 0.34 59.85  ? 204 A1BGK B N3  1 
HETATM 1702 N N3  D A1BGK F 4 .   ? -8.388  5.523   -10.252 0.32 59.82  ? 204 A1BGK B N3  1 
HETATM 1703 C C4  C A1BGK F 4 .   ? -5.766  7.162   -17.175 0.34 67.86  ? 204 A1BGK B C4  1 
HETATM 1704 C C4  D A1BGK F 4 .   ? -5.767  7.162   -17.174 0.32 67.83  ? 204 A1BGK B C4  1 
HETATM 1705 C C5  C A1BGK F 4 .   ? -6.153  5.930   -16.651 0.34 66.72  ? 204 A1BGK B C5  1 
HETATM 1706 C C5  D A1BGK F 4 .   ? -6.154  5.929   -16.650 0.32 66.67  ? 204 A1BGK B C5  1 
HETATM 1707 C C6  C A1BGK F 4 .   ? -7.475  5.309   -16.991 0.34 64.26  ? 204 A1BGK B C6  1 
HETATM 1708 C C6  D A1BGK F 4 .   ? -7.475  5.308   -16.991 0.32 64.24  ? 204 A1BGK B C6  1 
HETATM 1709 C C7  C A1BGK F 4 .   ? -7.703  4.893   -18.307 0.34 63.38  ? 204 A1BGK B C7  1 
HETATM 1710 C C7  D A1BGK F 4 .   ? -7.702  4.892   -18.307 0.32 63.40  ? 204 A1BGK B C7  1 
HETATM 1711 C C8  C A1BGK F 4 .   ? -8.887  4.288   -18.684 0.34 61.38  ? 204 A1BGK B C8  1 
HETATM 1712 C C8  D A1BGK F 4 .   ? -8.886  4.289   -18.684 0.32 61.48  ? 204 A1BGK B C8  1 
HETATM 1713 C C10 C A1BGK F 4 .   ? -9.679  4.453   -16.442 0.34 60.85  ? 204 A1BGK B C10 1 
HETATM 1714 C C10 D A1BGK F 4 .   ? -9.679  4.454   -16.443 0.32 60.90  ? 204 A1BGK B C10 1 
HETATM 1715 C C13 C A1BGK F 4 .   ? -8.614  4.673   -12.270 0.34 59.78  ? 204 A1BGK B C13 1 
HETATM 1716 C C13 D A1BGK F 4 .   ? -8.613  4.673   -12.270 0.32 59.79  ? 204 A1BGK B C13 1 
HETATM 1717 C C15 C A1BGK F 4 .   ? -8.192  6.410   -9.109  0.34 59.59  ? 204 A1BGK B C15 1 
HETATM 1718 C C15 D A1BGK F 4 .   ? -8.192  6.409   -9.108  0.32 59.57  ? 204 A1BGK B C15 1 
HETATM 1719 C C17 C A1BGK F 4 .   ? -5.227  5.287   -15.831 0.34 67.71  ? 204 A1BGK B C17 1 
HETATM 1720 C C17 D A1BGK F 4 .   ? -5.227  5.287   -15.830 0.32 67.66  ? 204 A1BGK B C17 1 
HETATM 1721 C C1  C A1BGK F 4 .   ? -2.168  7.641   -14.304 0.34 69.43  ? 204 A1BGK B C1  1 
HETATM 1722 C C1  D A1BGK F 4 .   ? -2.168  7.640   -14.305 0.32 69.41  ? 204 A1BGK B C1  1 
HETATM 1723 O O1  C A1BGK F 4 .   ? -2.492  7.496   -15.697 0.34 69.99  ? 204 A1BGK B O1  1 
HETATM 1724 O O1  D A1BGK F 4 .   ? -2.493  7.497   -15.697 0.32 69.95  ? 204 A1BGK B O1  1 
HETATM 1725 C C2  C A1BGK F 4 .   ? -3.704  6.978   -16.019 0.34 69.41  ? 204 A1BGK B C2  1 
HETATM 1726 C C2  D A1BGK F 4 .   ? -3.705  6.979   -16.019 0.32 69.36  ? 204 A1BGK B C2  1 
HETATM 1727 C C3  C A1BGK F 4 .   ? -4.544  7.707   -16.864 0.34 69.09  ? 204 A1BGK B C3  1 
HETATM 1728 C C3  D A1BGK F 4 .   ? -4.545  7.707   -16.864 0.32 69.03  ? 204 A1BGK B C3  1 
HETATM 1729 C C9  C A1BGK F 4 .   ? -9.875  4.070   -17.752 0.34 60.54  ? 204 A1BGK B C9  1 
HETATM 1730 C C9  D A1BGK F 4 .   ? -9.875  4.071   -17.753 0.32 60.63  ? 204 A1BGK B C9  1 
HETATM 1731 C C11 C A1BGK F 4 .   ? -8.487  5.064   -16.038 0.34 62.49  ? 204 A1BGK B C11 1 
HETATM 1732 C C11 D A1BGK F 4 .   ? -8.486  5.064   -16.039 0.32 62.47  ? 204 A1BGK B C11 1 
HETATM 1733 C C12 C A1BGK F 4 .   ? -8.400  5.459   -14.591 0.34 60.47  ? 204 A1BGK B C12 1 
HETATM 1734 C C12 D A1BGK F 4 .   ? -8.399  5.460   -14.591 0.32 60.52  ? 204 A1BGK B C12 1 
HETATM 1735 O O2  C A1BGK F 4 .   ? -8.098  6.600   -14.276 0.34 61.54  ? 204 A1BGK B O2  1 
HETATM 1736 O O2  D A1BGK F 4 .   ? -8.096  6.600   -14.277 0.32 61.53  ? 204 A1BGK B O2  1 
HETATM 1737 C C14 C A1BGK F 4 .   ? -8.757  3.689   -11.281 0.34 58.55  ? 204 A1BGK B C14 1 
HETATM 1738 C C14 D A1BGK F 4 .   ? -8.756  3.689   -11.282 0.32 58.61  ? 204 A1BGK B C14 1 
HETATM 1739 N N2  C A1BGK F 4 .   ? -8.623  4.186   -10.060 0.34 59.66  ? 204 A1BGK B N2  1 
HETATM 1740 N N2  D A1BGK F 4 .   ? -8.623  4.185   -10.061 0.32 59.63  ? 204 A1BGK B N2  1 
HETATM 1741 C C16 C A1BGK F 4 .   ? -8.376  5.853   -11.564 0.34 59.90  ? 204 A1BGK B C16 1 
HETATM 1742 C C16 D A1BGK F 4 .   ? -8.376  5.853   -11.564 0.32 59.89  ? 204 A1BGK B C16 1 
HETATM 1743 N N4  C A1BGK F 4 .   ? -4.019  5.800   -15.506 0.34 68.82  ? 204 A1BGK B N4  1 
HETATM 1744 N N4  D A1BGK F 4 .   ? -4.020  5.800   -15.505 0.32 68.76  ? 204 A1BGK B N4  1 
HETATM 1745 S S   C SO4   G 5 .   ? -18.736 11.618  -0.442  0.50 99.73  ? 205 SO4   B S   1 
HETATM 1746 S S   D SO4   G 5 .   ? -18.736 11.618  -0.442  0.50 99.73  ? 205 SO4   B S   1 
HETATM 1747 O O1  C SO4   G 5 .   ? -17.407 11.803  -0.980  0.50 99.48  ? 205 SO4   B O1  1 
HETATM 1748 O O1  D SO4   G 5 .   ? -17.407 11.803  -0.980  0.50 99.48  ? 205 SO4   B O1  1 
HETATM 1749 O O2  C SO4   G 5 .   ? -19.692 12.206  -1.333  0.50 101.51 ? 205 SO4   B O2  1 
HETATM 1750 O O2  D SO4   G 5 .   ? -19.692 12.206  -1.333  0.50 101.51 ? 205 SO4   B O2  1 
HETATM 1751 O O3  C SO4   G 5 .   ? -19.012 10.211  -0.280  0.50 96.93  ? 205 SO4   B O3  1 
HETATM 1752 O O3  D SO4   G 5 .   ? -19.012 10.211  -0.280  0.50 96.93  ? 205 SO4   B O3  1 
HETATM 1753 O O4  C SO4   G 5 .   ? -18.843 12.264  0.835   0.50 100.27 ? 205 SO4   B O4  1 
HETATM 1754 O O4  D SO4   G 5 .   ? -18.843 12.264  0.835   0.50 100.27 ? 205 SO4   B O4  1 
HETATM 1755 O O   . HOH   H 6 .   ? -27.822 -5.975  -28.158 1.00 46.41  ? 101 HOH   A O   1 
HETATM 1756 O O   . HOH   H 6 .   ? -24.115 9.124   -27.575 1.00 35.95  ? 102 HOH   A O   1 
HETATM 1757 O O   . HOH   H 6 .   ? -2.393  -4.047  -6.312  1.00 53.53  ? 103 HOH   A O   1 
HETATM 1758 O O   . HOH   H 6 .   ? 5.938   -5.671  -16.879 1.00 72.64  ? 104 HOH   A O   1 
HETATM 1759 O O   . HOH   H 6 .   ? -31.588 -0.078  -29.161 1.00 72.28  ? 105 HOH   A O   1 
HETATM 1760 O O   . HOH   H 6 .   ? -4.206  -14.436 -25.445 1.00 49.72  ? 106 HOH   A O   1 
HETATM 1761 O O   . HOH   H 6 .   ? -23.522 18.981  -19.287 1.00 56.81  ? 107 HOH   A O   1 
HETATM 1762 O O   A HOH   H 6 .   ? -9.305  -6.695  -25.468 0.50 59.34  ? 108 HOH   A O   1 
HETATM 1763 O O   B HOH   H 6 .   ? -9.305  -6.695  -25.468 0.50 59.34  ? 108 HOH   A O   1 
HETATM 1764 O O   . HOH   H 6 .   ? -7.959  -2.094  6.725   1.00 53.00  ? 109 HOH   A O   1 
HETATM 1765 O O   . HOH   H 6 .   ? -22.531 -9.397  -34.592 1.00 51.52  ? 110 HOH   A O   1 
HETATM 1766 O O   . HOH   H 6 .   ? -3.686  -4.416  0.241   1.00 53.67  ? 111 HOH   A O   1 
HETATM 1767 O O   . HOH   H 6 .   ? -28.913 15.766  -14.972 1.00 56.60  ? 112 HOH   A O   1 
HETATM 1768 O O   A HOH   H 6 .   ? -8.563  2.595   -9.015  0.19 24.81  ? 113 HOH   A O   1 
HETATM 1769 O O   B HOH   H 6 .   ? -8.562  2.597   -9.014  0.15 24.85  ? 113 HOH   A O   1 
HETATM 1770 O O   . HOH   H 6 .   ? -30.656 0.253   -23.014 1.00 46.84  ? 114 HOH   A O   1 
HETATM 1771 O O   . HOH   H 6 .   ? -2.843  -11.851 -7.061  1.00 38.76  ? 115 HOH   A O   1 
HETATM 1772 O O   C HOH   H 6 .   ? -9.474  1.738   -8.266  0.34 29.52  ? 116 HOH   A O   1 
HETATM 1773 O O   D HOH   H 6 .   ? -9.474  1.739   -8.268  0.32 29.72  ? 116 HOH   A O   1 
HETATM 1774 O O   . HOH   H 6 .   ? -26.414 -3.688  -35.225 1.00 57.93  ? 117 HOH   A O   1 
HETATM 1775 O O   . HOH   H 6 .   ? -4.389  -10.335 -5.578  1.00 48.11  ? 118 HOH   A O   1 
HETATM 1776 O O   . HOH   H 6 .   ? -4.111  -0.737  -0.193  1.00 48.93  ? 119 HOH   A O   1 
HETATM 1777 O O   C HOH   H 6 .   ? -5.374  5.133   -7.324  0.34 58.03  ? 120 HOH   A O   1 
HETATM 1778 O O   D HOH   H 6 .   ? -5.373  5.132   -7.324  0.32 58.07  ? 120 HOH   A O   1 
HETATM 1779 O O   . HOH   H 6 .   ? -2.934  -9.159  -3.336  1.00 56.70  ? 121 HOH   A O   1 
HETATM 1780 O O   A HOH   H 6 .   ? -8.233  5.346   -7.038  0.19 42.35  ? 122 HOH   A O   1 
HETATM 1781 O O   B HOH   H 6 .   ? -8.237  5.347   -7.041  0.15 42.43  ? 122 HOH   A O   1 
HETATM 1782 O O   . HOH   I 6 .   ? -5.284  3.038   -10.411 1.00 71.28  ? 301 HOH   B O   1 
HETATM 1783 O O   . HOH   I 6 .   ? -30.609 12.566  -19.503 1.00 49.68  ? 302 HOH   B O   1 
HETATM 1784 O O   . HOH   I 6 .   ? -25.780 -8.188  -16.750 1.00 39.07  ? 303 HOH   B O   1 
HETATM 1785 O O   . HOH   I 6 .   ? -33.865 1.621   -15.522 1.00 48.77  ? 304 HOH   B O   1 
HETATM 1786 O O   . HOH   I 6 .   ? -19.357 -12.077 -25.561 1.00 61.83  ? 305 HOH   B O   1 
HETATM 1787 O O   C HOH   I 6 .   ? -20.506 13.791  1.593   0.50 58.51  ? 306 HOH   B O   1 
HETATM 1788 O O   D HOH   I 6 .   ? -20.506 13.791  1.593   0.50 58.51  ? 306 HOH   B O   1 
HETATM 1789 O O   . HOH   I 6 .   ? -34.823 4.369   -9.372  1.00 61.15  ? 307 HOH   B O   1 
HETATM 1790 O O   . HOH   I 6 .   ? -17.236 12.666  -5.484  1.00 43.55  ? 308 HOH   B O   1 
HETATM 1791 O O   A HOH   I 6 .   ? -15.721 -10.221 -15.200 0.50 56.37  ? 309 HOH   B O   1 
HETATM 1792 O O   B HOH   I 6 .   ? -15.721 -10.221 -15.200 0.50 56.37  ? 309 HOH   B O   1 
HETATM 1793 O O   A HOH   I 6 .   ? -16.404 25.945  -12.540 0.50 68.66  ? 310 HOH   B O   1 
HETATM 1794 O O   B HOH   I 6 .   ? -16.404 25.945  -12.540 0.50 68.66  ? 310 HOH   B O   1 
HETATM 1795 O O   . HOH   I 6 .   ? -13.205 -2.375  -14.827 1.00 37.74  ? 311 HOH   B O   1 
HETATM 1796 O O   . HOH   I 6 .   ? -31.478 7.200   -4.625  1.00 63.85  ? 312 HOH   B O   1 
HETATM 1797 O O   . HOH   I 6 .   ? -27.707 -7.292  -5.770  1.00 57.67  ? 313 HOH   B O   1 
HETATM 1798 O O   A HOH   I 6 .   ? -21.936 -12.363 -13.008 0.50 56.46  ? 314 HOH   B O   1 
HETATM 1799 O O   B HOH   I 6 .   ? -21.936 -12.363 -13.008 0.50 56.46  ? 314 HOH   B O   1 
HETATM 1800 O O   C HOH   I 6 .   ? -23.753 -6.734  -4.644  0.50 50.93  ? 315 HOH   B O   1 
HETATM 1801 O O   D HOH   I 6 .   ? -23.753 -6.734  -4.644  0.50 50.93  ? 315 HOH   B O   1 
HETATM 1802 O O   A HOH   I 6 .   ? -19.811 -7.758  -2.646  0.50 56.73  ? 316 HOH   B O   1 
HETATM 1803 O O   B HOH   I 6 .   ? -19.811 -7.758  -2.646  0.50 56.73  ? 316 HOH   B O   1 
HETATM 1804 O O   . HOH   I 6 .   ? -34.385 0.461   -3.502  1.00 44.39  ? 317 HOH   B O   1 
HETATM 1805 O O   . HOH   I 6 .   ? -15.451 9.248   -0.572  1.00 46.51  ? 318 HOH   B O   1 
HETATM 1806 O O   A HOH   I 6 .   ? -6.488  -0.573  -10.808 0.19 7.52   ? 319 HOH   B O   1 
HETATM 1807 O O   B HOH   I 6 .   ? -6.488  -0.575  -10.808 0.15 7.61   ? 319 HOH   B O   1 
HETATM 1808 O O   . HOH   I 6 .   ? -17.936 -10.732 -16.559 1.00 43.00  ? 320 HOH   B O   1 
HETATM 1809 O O   C HOH   I 6 .   ? -22.110 14.839  -6.145  0.50 50.42  ? 321 HOH   B O   1 
HETATM 1810 O O   D HOH   I 6 .   ? -22.110 14.839  -6.145  0.50 50.42  ? 321 HOH   B O   1 
HETATM 1811 O O   . HOH   I 6 .   ? -12.213 -3.501  -10.078 1.00 34.73  ? 322 HOH   B O   1 
HETATM 1812 O O   C HOH   I 6 .   ? -7.544  10.269  -19.396 0.34 42.78  ? 323 HOH   B O   1 
HETATM 1813 O O   D HOH   I 6 .   ? -7.542  10.269  -19.395 0.32 42.93  ? 323 HOH   B O   1 
HETATM 1814 O O   . HOH   I 6 .   ? -7.071  -8.970  -3.084  1.00 41.83  ? 324 HOH   B O   1 
HETATM 1815 O O   . HOH   I 6 .   ? -35.401 -5.226  -10.337 1.00 51.26  ? 325 HOH   B O   1 
HETATM 1816 O O   A HOH   I 6 .   ? -28.648 -4.182  -22.332 0.50 59.92  ? 326 HOH   B O   1 
HETATM 1817 O O   B HOH   I 6 .   ? -28.648 -4.182  -22.332 0.50 59.92  ? 326 HOH   B O   1 
HETATM 1818 O O   A HOH   I 6 .   ? -20.386 -16.583 -18.997 0.50 92.52  ? 327 HOH   B O   1 
HETATM 1819 O O   B HOH   I 6 .   ? -20.386 -16.583 -18.997 0.50 92.52  ? 327 HOH   B O   1 
HETATM 1820 O O   . HOH   I 6 .   ? -10.825 11.746  -19.160 1.00 60.14  ? 328 HOH   B O   1 
HETATM 1821 O O   A HOH   I 6 .   ? -11.949 2.354   -5.861  0.19 24.01  ? 329 HOH   B O   1 
HETATM 1822 O O   B HOH   I 6 .   ? -11.946 2.368   -5.861  0.15 24.12  ? 329 HOH   B O   1 
HETATM 1823 O O   C HOH   I 6 .   ? -10.235 6.533   -6.162  0.34 35.60  ? 330 HOH   B O   1 
HETATM 1824 O O   D HOH   I 6 .   ? -10.235 6.534   -6.162  0.32 35.70  ? 330 HOH   B O   1 
HETATM 1825 O O   . HOH   I 6 .   ? -21.302 6.044   -32.701 1.00 60.66  ? 331 HOH   B O   1 
HETATM 1826 O O   . HOH   I 6 .   ? -21.779 -13.660 -21.732 1.00 54.92  ? 332 HOH   B O   1 
HETATM 1827 O O   A HOH   I 6 .   ? -0.674  0.170   -13.579 0.50 71.04  ? 333 HOH   B O   1 
HETATM 1828 O O   B HOH   I 6 .   ? -0.674  0.170   -13.579 0.50 71.04  ? 333 HOH   B O   1 
HETATM 1829 O O   . HOH   I 6 .   ? -16.303 20.707  -14.237 1.00 56.58  ? 334 HOH   B O   1 
HETATM 1830 O O   . HOH   I 6 .   ? -27.919 -6.365  -18.596 1.00 49.92  ? 335 HOH   B O   1 
HETATM 1831 O O   . HOH   I 6 .   ? -15.175 16.332  -20.106 1.00 57.75  ? 336 HOH   B O   1 
HETATM 1832 O O   . HOH   I 6 .   ? -14.471 -6.327  -1.704  1.00 63.56  ? 337 HOH   B O   1 
HETATM 1833 O O   . HOH   I 6 .   ? -21.240 6.981   0.000   0.50 39.56  ? 338 HOH   B O   1 
HETATM 1834 O O   . HOH   I 6 .   ? -15.942 -14.593 -16.644 1.00 46.98  ? 339 HOH   B O   1 
HETATM 1835 O O   A HOH   I 6 .   ? -30.593 12.300  -16.444 0.50 56.70  ? 340 HOH   B O   1 
HETATM 1836 O O   B HOH   I 6 .   ? -30.593 12.300  -16.444 0.50 56.70  ? 340 HOH   B O   1 
HETATM 1837 O O   . HOH   I 6 .   ? -16.251 -7.277  -8.140  1.00 57.26  ? 341 HOH   B O   1 
HETATM 1838 O O   . HOH   I 6 .   ? -18.187 19.035  -21.732 1.00 57.00  ? 342 HOH   B O   1 
HETATM 1839 O O   . HOH   I 6 .   ? -18.677 14.804  -22.180 1.00 41.59  ? 343 HOH   B O   1 
HETATM 1840 O O   . HOH   I 6 .   ? -15.686 -13.935 -30.944 1.00 56.18  ? 344 HOH   B O   1 
HETATM 1841 O O   . HOH   I 6 .   ? -17.082 14.824  -30.779 1.00 56.23  ? 345 HOH   B O   1 
HETATM 1842 O O   . HOH   I 6 .   ? -23.902 -14.889 -17.539 1.00 66.18  ? 346 HOH   B O   1 
HETATM 1843 O O   A HOH   I 6 .   ? -11.493 -17.688 -27.543 0.50 70.59  ? 347 HOH   B O   1 
HETATM 1844 O O   B HOH   I 6 .   ? -11.493 -17.688 -27.543 0.50 70.59  ? 347 HOH   B O   1 
HETATM 1845 O O   . HOH   I 6 .   ? -14.348 -12.482 -16.467 1.00 42.41  ? 348 HOH   B O   1 
HETATM 1846 O O   . HOH   I 6 .   ? -10.701 7.865   -13.835 1.00 44.86  ? 349 HOH   B O   1 
HETATM 1847 O O   . HOH   I 6 .   ? -15.160 -4.857  1.466   1.00 47.06  ? 350 HOH   B O   1 
HETATM 1848 O O   . HOH   I 6 .   ? -25.977 -4.661  -4.068  1.00 45.81  ? 351 HOH   B O   1 
HETATM 1849 O O   . HOH   I 6 .   ? -8.545  -10.808 -7.223  1.00 62.49  ? 352 HOH   B O   1 
HETATM 1850 O O   . HOH   I 6 .   ? -19.504 -5.761  -0.872  1.00 46.88  ? 353 HOH   B O   1 
HETATM 1851 O O   . HOH   I 6 .   ? -11.450 -5.261  -8.232  1.00 46.32  ? 354 HOH   B O   1 
HETATM 1852 O O   . HOH   I 6 .   ? -7.488  -6.511  0.619   1.00 55.18  ? 355 HOH   B O   1 
HETATM 1853 O O   . HOH   I 6 .   ? -29.433 -1.515  -19.017 1.00 48.31  ? 356 HOH   B O   1 
HETATM 1854 O O   A HOH   I 6 .   ? -20.706 2.749   -32.645 0.50 56.29  ? 357 HOH   B O   1 
HETATM 1855 O O   B HOH   I 6 .   ? -20.706 2.749   -32.645 0.50 56.29  ? 357 HOH   B O   1 
HETATM 1856 O O   . HOH   I 6 .   ? -30.964 4.590   -2.751  1.00 54.55  ? 358 HOH   B O   1 
HETATM 1857 O O   A HOH   I 6 .   ? -19.557 -13.415 -22.964 0.50 45.96  ? 359 HOH   B O   1 
HETATM 1858 O O   B HOH   I 6 .   ? -19.557 -13.415 -22.964 0.50 45.96  ? 359 HOH   B O   1 
HETATM 1859 O O   A HOH   I 6 .   ? -20.269 24.597  -16.767 0.50 63.26  ? 360 HOH   B O   1 
HETATM 1860 O O   B HOH   I 6 .   ? -20.269 24.597  -16.767 0.50 63.26  ? 360 HOH   B O   1 
HETATM 1861 O O   C HOH   I 6 .   ? -10.147 -16.145 -24.357 0.50 52.34  ? 361 HOH   B O   1 
HETATM 1862 O O   D HOH   I 6 .   ? -10.147 -16.145 -24.357 0.50 52.34  ? 361 HOH   B O   1 
HETATM 1863 O O   . HOH   I 6 .   ? -30.208 -7.808  -5.332  1.00 68.80  ? 362 HOH   B O   1 
HETATM 1864 O O   . HOH   I 6 .   ? -6.947  -11.054 -5.329  1.00 55.52  ? 363 HOH   B O   1 
HETATM 1865 O O   A HOH   I 6 .   ? -32.128 -6.896  -7.041  0.50 57.60  ? 364 HOH   B O   1 
HETATM 1866 O O   B HOH   I 6 .   ? -32.128 -6.896  -7.041  0.50 57.60  ? 364 HOH   B O   1 
HETATM 1867 O O   . HOH   I 6 .   ? -17.226 16.469  -21.835 1.00 50.63  ? 365 HOH   B O   1 
HETATM 1868 O O   A HOH   I 6 .   ? -10.572 -19.045 -11.755 0.50 84.20  ? 366 HOH   B O   1 
HETATM 1869 O O   B HOH   I 6 .   ? -10.572 -19.045 -11.755 0.50 84.20  ? 366 HOH   B O   1 
HETATM 1870 O O   . HOH   I 6 .   ? -12.091 -9.389  -0.053  1.00 62.20  ? 367 HOH   B O   1 
HETATM 1871 O O   . HOH   I 6 .   ? -1.032  -14.817 -9.997  1.00 57.38  ? 368 HOH   B O   1 
HETATM 1872 O O   A HOH   I 6 .   ? -19.633 -12.204 -13.499 0.50 61.15  ? 369 HOH   B O   1 
HETATM 1873 O O   B HOH   I 6 .   ? -19.633 -12.204 -13.499 0.50 61.15  ? 369 HOH   B O   1 
HETATM 1874 O O   A HOH   I 6 .   ? -19.314 3.336   -0.170  0.19 0.50   ? 370 HOH   B O   1 
HETATM 1875 O O   B HOH   I 6 .   ? -20.728 4.251   0.854   0.15 20.49  ? 370 HOH   B O   1 
HETATM 1876 O O   A HOH   I 6 .   ? -11.473 4.715   -5.912  0.19 2.32   ? 371 HOH   B O   1 
HETATM 1877 O O   B HOH   I 6 .   ? -11.317 4.999   -4.696  0.15 0.50   ? 371 HOH   B O   1 
HETATM 1878 O O   . HOH   I 6 .   ? -30.516 -11.965 -27.057 0.50 111.34 ? 372 HOH   B O   1 
HETATM 1879 O O   . HOH   I 6 .   ? -29.451 -5.813  -1.023  1.00 51.49  ? 373 HOH   B O   1 
HETATM 1880 O O   . HOH   I 6 .   ? -23.481 -7.518  -2.202  1.00 56.75  ? 374 HOH   B O   1 
HETATM 1881 O O   . HOH   I 6 .   ? -11.594 12.348  -14.546 1.00 67.89  ? 375 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   ? 0.9418 0.7119 0.8387 -0.0195 0.2072  0.0313  50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.9409 0.7107 0.8310 -0.0093 0.2030  0.0253  50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.8949 0.6821 0.7850 0.0105  0.1976  0.0347  50  ASP   A C   
4    O O   . ASP   A 7   ? 0.9621 0.7482 0.8567 0.0213  0.2039  0.0460  50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.9593 0.7056 0.8518 -0.0097 0.2134  0.0206  50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.9634 0.7081 0.8528 -0.0019 0.2105  0.0130  50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.0317 0.7714 0.9136 -0.0120 0.2080  0.0016  50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.9957 0.7431 0.8906 0.0142  0.2112  0.0185  50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.8127 0.6146 0.6968 0.0153  0.1864  0.0302  51  MET   A N   
10   C CA  . MET   A 8   ? 0.7809 0.6018 0.6628 0.0321  0.1787  0.0377  51  MET   A CA  
11   C C   . MET   A 8   ? 0.6863 0.5046 0.5691 0.0473  0.1767  0.0359  51  MET   A C   
12   O O   . MET   A 8   ? 0.6841 0.4930 0.5684 0.0425  0.1773  0.0261  51  MET   A O   
13   C CB  . MET   A 8   ? 0.7718 0.6106 0.6480 0.0288  0.1669  0.0337  51  MET   A CB  
14   C CG  . MET   A 8   ? 0.8120 0.6566 0.6901 0.0158  0.1672  0.0362  51  MET   A CG  
15   S SD  . MET   A 8   ? 0.8048 0.6721 0.6774 0.0156  0.1531  0.0340  51  MET   A SD  
16   C CE  . MET   A 8   ? 0.8154 0.6903 0.6970 0.0037  0.1562  0.0407  51  MET   A CE  
17   N N   . TYR   A 9   ? 0.6613 0.4869 0.5434 0.0648  0.1751  0.0453  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.6454 0.4717 0.5291 0.0821  0.1704  0.0448  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.6286 0.4734 0.5048 0.0974  0.1597  0.0499  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.6208 0.4749 0.4909 0.0980  0.1600  0.0577  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.6525 0.4625 0.5416 0.0891  0.1805  0.0511  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.6567 0.4648 0.5419 0.0956  0.1877  0.0656  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.6631 0.4626 0.5511 0.0812  0.1985  0.0695  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.6631 0.4769 0.5416 0.1160  0.1841  0.0754  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.6723 0.4692 0.5588 0.0862  0.2071  0.0835  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.6803 0.4909 0.5535 0.1222  0.1926  0.0898  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.6882 0.4902 0.5666 0.1070  0.2050  0.0942  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.7321 0.5307 0.6073 0.1121  0.2151  0.1089  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.6356 0.4854 0.5131 0.1101  0.1506  0.0451  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.6221 0.4875 0.4915 0.1269  0.1388  0.0481  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.6479 0.5095 0.5157 0.1471  0.1371  0.0547  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.6200 0.4699 0.4977 0.1489  0.1408  0.0524  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.6079 0.4835 0.4801 0.1254  0.1270  0.0362  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.6247 0.4928 0.5098 0.1261  0.1256  0.0268  53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.6178 0.4971 0.4879 0.1076  0.1278  0.0315  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.6347 0.5136 0.5233 0.1285  0.1137  0.0169  53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.6612 0.5323 0.5160 0.1624  0.1313  0.0624  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.6937 0.5629 0.5412 0.1845  0.1264  0.0689  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.6810 0.5654 0.5176 0.1986  0.1111  0.0658  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.6426 0.5379 0.4700 0.1955  0.1099  0.0674  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.7198 0.5811 0.5558 0.1918  0.1375  0.0848  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.7659 0.6098 0.6107 0.1814  0.1533  0.0903  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.8413 0.6788 0.6751 0.1865  0.1656  0.1067  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 0.8587 0.7066 0.6787 0.1942  0.1639  0.1134  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 0.8987 0.7201 0.7380 0.1830  0.1781  0.1132  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.6947 0.5805 0.5334 0.2137  0.0991  0.0609  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.6973 0.5962 0.5257 0.2279  0.0830  0.0564  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.6941 0.5938 0.4982 0.2422  0.0854  0.0694  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.7258 0.6144 0.5232 0.2486  0.0949  0.0811  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.7054 0.6049 0.5448 0.2397  0.0694  0.0474  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.7457 0.6582 0.5800 0.2505  0.0515  0.0387  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.7810 0.6960 0.6363 0.2545  0.0388  0.0260  55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.7937 0.7208 0.6495 0.2598  0.0226  0.0152  55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.8561 0.7885 0.6932 0.2781  0.0096  0.0161  55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.9154 0.8418 0.7307 0.2930  0.0118  0.0281  55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.8627 0.8052 0.7009 0.2817  -0.0047 0.0054  55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.6967 0.6083 0.4883 0.2454  0.0795  0.0684  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.6830 0.5964 0.4502 0.2593  0.0827  0.0803  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.6731 0.5945 0.4244 0.2784  0.0657  0.0748  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.7098 0.6310 0.4371 0.2931  0.0677  0.0843  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.7002 0.6198 0.4660 0.2460  0.0942  0.0858  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.6292 0.5567 0.3922 0.2786  0.0503  0.0604  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.6403 0.5740 0.3891 0.2971  0.0327  0.0539  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.6472 0.5900 0.4140 0.2907  0.0186  0.0371  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.6357 0.5795 0.4244 0.2709  0.0245  0.0315  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.6807 0.6284 0.4380 0.3069  0.0010  0.0292  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.6861 0.6430 0.4563 0.3042  -0.0140 0.0132  58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.7136 0.6784 0.4732 0.2986  -0.0113 0.0129  58  ASP   A C   
69   O O   . ASP   A 15  ? 0.7677 0.7320 0.5057 0.3043  -0.0025 0.0241  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.6959 0.6549 0.4585 0.3245  -0.0351 0.0043  58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.7503 0.7045 0.5278 0.3318  -0.0432 0.0010  58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.6859 0.6344 0.4790 0.3213  -0.0312 0.0061  58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.7840 0.7397 0.5561 0.3490  -0.0618 -0.0061 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.7051 0.6767 0.4804 0.2888  -0.0183 0.0008  59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.7297 0.7089 0.4964 0.2847  -0.0179 -0.0006 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.7483 0.7313 0.5043 0.3016  -0.0361 -0.0105 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.7339 0.7191 0.5079 0.2997  -0.0489 -0.0241 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.7267 0.7089 0.5149 0.2629  -0.0124 -0.0061 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.7179 0.6954 0.5111 0.2478  0.0053  0.0042  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.7163 0.7064 0.4984 0.2608  -0.0159 -0.0100 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.7103 0.6874 0.5233 0.2272  0.0101  -0.0015 59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.7697 0.7524 0.4969 0.3178  -0.0366 -0.0039 60  THR   A N   
83   N N   B THR   A 17  ? 0.7675 0.7504 0.4949 0.3177  -0.0369 -0.0042 60  THR   A N   
84   N N   C THR   A 17  ? 0.7697 0.7524 0.4969 0.3178  -0.0366 -0.0039 60  THR   A N   
85   N N   D THR   A 17  ? 0.7675 0.7504 0.4949 0.3177  -0.0369 -0.0042 60  THR   A N   
86   C CA  A THR   A 17  ? 0.7960 0.7795 0.5040 0.3378  -0.0532 -0.0115 60  THR   A CA  
87   C CA  B THR   A 17  ? 0.7914 0.7755 0.5018 0.3367  -0.0542 -0.0130 60  THR   A CA  
88   C CA  C THR   A 17  ? 0.7960 0.7795 0.5040 0.3378  -0.0532 -0.0115 60  THR   A CA  
89   C CA  D THR   A 17  ? 0.7914 0.7755 0.5018 0.3367  -0.0542 -0.0130 60  THR   A CA  
90   C C   A THR   A 17  ? 0.8075 0.7945 0.4914 0.3437  -0.0471 -0.0058 60  THR   A C   
91   C C   B THR   A 17  ? 0.8104 0.7967 0.4927 0.3458  -0.0484 -0.0061 60  THR   A C   
92   C C   C THR   A 17  ? 0.8075 0.7945 0.4914 0.3437  -0.0471 -0.0058 60  THR   A C   
93   C C   D THR   A 17  ? 0.8104 0.7967 0.4927 0.3458  -0.0484 -0.0061 60  THR   A C   
94   O O   A THR   A 17  ? 0.8130 0.7990 0.4853 0.3414  -0.0293 0.0093  60  THR   A O   
95   O O   B THR   A 17  ? 0.8241 0.8077 0.4906 0.3477  -0.0320 0.0097  60  THR   A O   
96   O O   C THR   A 17  ? 0.8130 0.7990 0.4853 0.3414  -0.0293 0.0093  60  THR   A O   
97   O O   D THR   A 17  ? 0.8241 0.8077 0.4906 0.3477  -0.0320 0.0097  60  THR   A O   
98   C CB  A THR   A 17  ? 0.8213 0.7971 0.5120 0.3576  -0.0604 -0.0079 60  THR   A CB  
99   C CB  B THR   A 17  ? 0.8104 0.7877 0.5114 0.3546  -0.0651 -0.0134 60  THR   A CB  
100  C CB  C THR   A 17  ? 0.8213 0.7971 0.5120 0.3576  -0.0604 -0.0079 60  THR   A CB  
101  C CB  D THR   A 17  ? 0.8104 0.7877 0.5114 0.3546  -0.0651 -0.0134 60  THR   A CB  
102  O OG1 A THR   A 17  ? 0.8277 0.7981 0.4956 0.3633  -0.0445 0.0091  60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.7915 0.7691 0.5238 0.3453  -0.0715 -0.0222 60  THR   A OG1 
104  O OG1 C THR   A 17  ? 0.8277 0.7981 0.4956 0.3633  -0.0445 0.0091  60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.7915 0.7691 0.5238 0.3453  -0.0715 -0.0222 60  THR   A OG1 
106  C CG2 A THR   A 17  ? 0.8245 0.7970 0.5392 0.3534  -0.0649 -0.0115 60  THR   A CG2 
107  C CG2 B THR   A 17  ? 0.8271 0.8037 0.5051 0.3759  -0.0831 -0.0216 60  THR   A CG2 
108  C CG2 C THR   A 17  ? 0.8245 0.7970 0.5392 0.3534  -0.0649 -0.0115 60  THR   A CG2 
109  C CG2 D THR   A 17  ? 0.8271 0.8037 0.5051 0.3759  -0.0831 -0.0216 60  THR   A CG2 
110  N N   . TRP   A 18  ? 0.8193 0.8100 0.4971 0.3512  -0.0605 -0.0173 61  TRP   A N   
111  C CA  . TRP   A 18  ? 0.8743 0.8663 0.5240 0.3636  -0.0578 -0.0134 61  TRP   A CA  
112  C C   . TRP   A 18  ? 0.9635 0.9470 0.5817 0.3868  -0.0620 -0.0081 61  TRP   A C   
113  O O   . TRP   A 18  ? 1.0134 0.9927 0.6337 0.3955  -0.0776 -0.0165 61  TRP   A O   
114  C CB  . TRP   A 18  ? 0.8839 0.8802 0.5369 0.3652  -0.0716 -0.0283 61  TRP   A CB  
115  C CG  . TRP   A 18  ? 0.9304 0.9275 0.5554 0.3783  -0.0686 -0.0252 61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 0.9898 0.9809 0.5834 0.4010  -0.0776 -0.0277 61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 0.9444 0.9485 0.5702 0.3701  -0.0561 -0.0197 61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 1.0078 1.0012 0.5823 0.4075  -0.0695 -0.0235 61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 0.9904 0.9925 0.5856 0.3889  -0.0567 -0.0186 61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 0.8970 0.9085 0.5456 0.3496  -0.0449 -0.0156 61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 1.0012 1.0095 0.5912 0.3875  -0.0458 -0.0135 61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 0.9176 0.9356 0.5609 0.3483  -0.0358 -0.0105 61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 0.9496 0.9667 0.5656 0.3668  -0.0359 -0.0095 61  TRP   A CH2 
124  N N   . GLU   A 19  ? 1.0303 1.0111 0.6221 0.3961  -0.0480 0.0058  62  GLU   A N   
125  C CA  . GLU   A 19  ? 1.1137 1.0842 0.6702 0.4194  -0.0496 0.0129  62  GLU   A CA  
126  C C   . GLU   A 19  ? 1.1611 1.1308 0.6859 0.4357  -0.0498 0.0124  62  GLU   A C   
127  O O   . GLU   A 19  ? 1.0745 1.0486 0.5953 0.4309  -0.0321 0.0226  62  GLU   A O   
128  C CB  . GLU   A 19  ? 1.1870 1.1520 0.7388 0.4172  -0.0299 0.0317  62  GLU   A CB  
129  C CG  . GLU   A 19  ? 1.2840 1.2481 0.8656 0.4023  -0.0292 0.0319  62  GLU   A CG  
130  C CD  . GLU   A 19  ? 1.3710 1.3281 0.9530 0.4135  -0.0465 0.0248  62  GLU   A CD  
131  O OE1 . GLU   A 19  ? 1.4710 1.4190 1.0217 0.4356  -0.0524 0.0288  62  GLU   A OE1 
132  O OE2 . GLU   A 19  ? 1.3536 1.3141 0.9671 0.4005  -0.0535 0.0158  62  GLU   A OE2 
133  N N   . LYS   A 20  ? 1.2257 1.1897 0.7292 0.4545  -0.0692 0.0006  63  LYS   A N   
134  C CA  . LYS   A 20  ? 1.2642 1.2249 0.7334 0.4726  -0.0714 -0.0018 63  LYS   A CA  
135  C C   . LYS   A 20  ? 1.2203 1.1733 0.6568 0.4854  -0.0518 0.0172  63  LYS   A C   
136  O O   . LYS   A 20  ? 1.2566 1.2019 0.6857 0.4903  -0.0482 0.0269  63  LYS   A O   
137  C CB  . LYS   A 20  ? 1.3287 1.2824 0.7798 0.4911  -0.0975 -0.0184 63  LYS   A CB  
138  C CG  . LYS   A 20  ? 1.3747 1.3356 0.8548 0.4807  -0.1159 -0.0385 63  LYS   A CG  
139  C CD  . LYS   A 20  ? 1.4511 1.4075 0.9339 0.4905  -0.1417 -0.0533 63  LYS   A CD  
140  C CE  . LYS   A 20  ? 1.5035 1.4662 1.0162 0.4807  -0.1594 -0.0735 63  LYS   A CE  
141  N NZ  . LYS   A 20  ? 1.5379 1.4979 1.0597 0.4886  -0.1840 -0.0872 63  LYS   A NZ  
142  N N   . ASP   A 21  ? 1.2663 1.2214 0.6863 0.4899  -0.0383 0.0231  64  ASP   A N   
143  C CA  . ASP   A 21  ? 1.3499 1.2980 0.7405 0.5016  -0.0163 0.0424  64  ASP   A CA  
144  C C   . ASP   A 21  ? 1.2888 1.2399 0.7031 0.4845  0.0029  0.0586  64  ASP   A C   
145  O O   . ASP   A 21  ? 1.2444 1.1845 0.6399 0.4943  0.0114  0.0715  64  ASP   A O   
146  C CB  . ASP   A 21  ? 1.4940 1.4251 0.8382 0.5294  -0.0244 0.0441  64  ASP   A CB  
147  C CG  . ASP   A 21  ? 1.5688 1.4938 0.8832 0.5492  -0.0444 0.0280  64  ASP   A CG  
148  O OD1 . ASP   A 21  ? 1.6371 1.5605 0.9273 0.5596  -0.0348 0.0301  64  ASP   A OD1 
149  O OD2 . ASP   A 21  ? 1.5570 1.4783 0.8721 0.5549  -0.0694 0.0132  64  ASP   A OD2 
150  N N   . ALA   A 22  ? 1.2365 1.2006 0.6897 0.4600  0.0100  0.0583  65  ALA   A N   
151  C CA  . ALA   A 22  ? 1.1387 1.1066 0.6109 0.4442  0.0328  0.0749  65  ALA   A CA  
152  C C   . ALA   A 22  ? 1.1123 1.0848 0.5726 0.4483  0.0534  0.0866  65  ALA   A C   
153  O O   . ALA   A 22  ? 1.1166 1.0939 0.5685 0.4547  0.0484  0.0788  65  ALA   A O   
154  C CB  . ALA   A 22  ? 1.1143 1.0932 0.6296 0.4178  0.0307  0.0688  65  ALA   A CB  
155  N N   . GLU   A 23  ? 1.0871 1.0605 0.5579 0.4391  0.0757  0.1038  66  GLU   A N   
156  C CA  . GLU   A 23  ? 1.1228 1.1034 0.5947 0.4374  0.0984  0.1168  66  GLU   A CA  
157  C C   . GLU   A 23  ? 1.0952 1.0932 0.5953 0.4218  0.0946  0.1074  66  GLU   A C   
158  O O   . GLU   A 23  ? 1.0089 1.0147 0.5421 0.4006  0.0888  0.1016  66  GLU   A O   
159  C CB  . GLU   A 23  ? 1.1981 1.1763 0.6843 0.4264  0.1192  0.1342  66  GLU   A CB  
160  C CG  . GLU   A 23  ? 1.2795 1.2683 0.7805 0.4182  0.1426  0.1471  66  GLU   A CG  
161  C CD  . GLU   A 23  ? 1.3943 1.3790 0.9108 0.4071  0.1618  0.1633  66  GLU   A CD  
162  O OE1 . GLU   A 23  ? 1.4540 1.4225 0.9450 0.4213  0.1704  0.1746  66  GLU   A OE1 
163  O OE2 . GLU   A 23  ? 1.4061 1.4025 0.9592 0.3843  0.1676  0.1643  66  GLU   A OE2 
164  N N   . VAL   A 24  ? 1.0980 1.1005 0.5838 0.4330  0.0968  0.1052  67  VAL   A N   
165  C CA  . VAL   A 24  ? 1.0611 1.0786 0.5691 0.4223  0.0915  0.0956  67  VAL   A CA  
166  C C   . VAL   A 24  ? 1.0549 1.0841 0.5782 0.4154  0.1144  0.1096  67  VAL   A C   
167  O O   . VAL   A 24  ? 1.0854 1.1111 0.5856 0.4317  0.1287  0.1190  67  VAL   A O   
168  C CB  . VAL   A 24  ? 1.0769 1.0908 0.5601 0.4400  0.0768  0.0819  67  VAL   A CB  
169  C CG1 . VAL   A 24  ? 1.0444 1.0721 0.5508 0.4292  0.0716  0.0728  67  VAL   A CG1 
170  C CG2 . VAL   A 24  ? 1.0891 1.0910 0.5563 0.4491  0.0539  0.0682  67  VAL   A CG2 
171  N N   . THR   A 25  ? 1.0152 1.0577 0.5763 0.3923  0.1176  0.1107  68  THR   A N   
172  C CA  . THR   A 25  ? 0.9630 1.0180 0.5462 0.3823  0.1386  0.1245  68  THR   A CA  
173  C C   . THR   A 25  ? 0.9286 0.9993 0.5484 0.3606  0.1313  0.1172  68  THR   A C   
174  O O   . THR   A 25  ? 0.9083 0.9778 0.5310 0.3563  0.1121  0.1028  68  THR   A O   
175  C CB  . THR   A 25  ? 0.9869 1.0345 0.5723 0.3781  0.1548  0.1395  68  THR   A CB  
176  O OG1 . THR   A 25  ? 0.9766 1.0351 0.5808 0.3716  0.1765  0.1534  68  THR   A OG1 
177  C CG2 . THR   A 25  ? 0.9772 1.0220 0.5839 0.3591  0.1463  0.1356  68  THR   A CG2 
178  N N   . GLY   A 26  ? 0.8748 0.9591 0.5217 0.3478  0.1458  0.1270  69  GLY   A N   
179  C CA  . GLY   A 26  ? 0.8584 0.9584 0.5388 0.3287  0.1401  0.1220  69  GLY   A CA  
180  C C   . GLY   A 26  ? 0.8641 0.9742 0.5435 0.3368  0.1354  0.1159  69  GLY   A C   
181  O O   . GLY   A 26  ? 0.9159 1.0179 0.5684 0.3541  0.1272  0.1081  69  GLY   A O   
182  N N   . ASN   A 27  ? 0.8676 0.9946 0.5768 0.3241  0.1390  0.1183  70  ASN   A N   
183  C CA  . ASN   A 27  ? 0.8910 1.0293 0.6069 0.3277  0.1324  0.1116  70  ASN   A CA  
184  C C   . ASN   A 27  ? 0.8254 0.9644 0.5545 0.3132  0.1119  0.0982  70  ASN   A C   
185  O O   . ASN   A 27  ? 0.7840 0.9130 0.5124 0.3032  0.1032  0.0933  70  ASN   A O   
186  C CB  . ASN   A 27  ? 0.9257 1.0816 0.6651 0.3251  0.1496  0.1237  70  ASN   A CB  
187  C CG  . ASN   A 27  ? 0.9430 1.1104 0.7189 0.3014  0.1519  0.1286  70  ASN   A CG  
188  O OD1 . ASN   A 27  ? 0.9761 1.1356 0.7550 0.2904  0.1526  0.1308  70  ASN   A OD1 
189  N ND2 . ASN   A 27  ? 0.9867 1.1722 0.7905 0.2936  0.1526  0.1302  70  ASN   A ND2 
190  N N   . SER   A 28  ? 0.7872 0.9359 0.5259 0.3136  0.1045  0.0922  71  SER   A N   
191  C CA  . SER   A 28  ? 0.7942 0.9431 0.5435 0.3023  0.0862  0.0801  71  SER   A CA  
192  C C   . SER   A 28  ? 0.7734 0.9399 0.5512 0.2917  0.0869  0.0832  71  SER   A C   
193  O O   . SER   A 28  ? 0.7989 0.9695 0.5769 0.2980  0.0802  0.0776  71  SER   A O   
194  C CB  . SER   A 28  ? 0.8158 0.9554 0.5440 0.3165  0.0733  0.0675  71  SER   A CB  
195  O OG  . SER   A 28  ? 0.9000 1.0249 0.6000 0.3304  0.0722  0.0645  71  SER   A OG  
196  N N   . PRO   A 29  ? 0.7951 0.9718 0.5982 0.2751  0.0933  0.0912  72  PRO   A N   
197  C CA  . PRO   A 29  ? 0.7848 0.9796 0.6160 0.2662  0.0935  0.0947  72  PRO   A CA  
198  C C   . PRO   A 29  ? 0.7522 0.9464 0.5917 0.2543  0.0755  0.0849  72  PRO   A C   
199  O O   . PRO   A 29  ? 0.7307 0.9129 0.5647 0.2439  0.0664  0.0784  72  PRO   A O   
200  C CB  . PRO   A 29  ? 0.8138 1.0166 0.6668 0.2525  0.1055  0.1055  72  PRO   A CB  
201  C CG  . PRO   A 29  ? 0.8020 0.9878 0.6418 0.2452  0.1028  0.1026  72  PRO   A CG  
202  C CD  . PRO   A 29  ? 0.8223 0.9929 0.6292 0.2634  0.0991  0.0963  72  PRO   A CD  
203  N N   . ARG   A 30  ? 0.8025 1.0087 0.6547 0.2566  0.0715  0.0843  73  ARG   A N   
204  C CA  . ARG   A 30  ? 0.8434 1.0507 0.7058 0.2454  0.0557  0.0773  73  ARG   A CA  
205  C C   . ARG   A 30  ? 0.7753 0.9980 0.6673 0.2287  0.0566  0.0841  73  ARG   A C   
206  O O   . ARG   A 30  ? 0.7167 0.9566 0.6272 0.2325  0.0647  0.0917  73  ARG   A O   
207  C CB  . ARG   A 30  ? 0.9202 1.1288 0.7764 0.2593  0.0495  0.0720  73  ARG   A CB  
208  C CG  . ARG   A 30  ? 1.0138 1.2048 0.8411 0.2732  0.0449  0.0626  73  ARG   A CG  
209  C CD  . ARG   A 30  ? 1.1230 1.3147 0.9402 0.2923  0.0449  0.0591  73  ARG   A CD  
210  N NE  . ARG   A 30  ? 1.1684 1.3421 0.9580 0.3045  0.0390  0.0488  73  ARG   A NE  
211  C CZ  . ARG   A 30  ? 1.1473 1.3102 0.9290 0.3069  0.0257  0.0375  73  ARG   A CZ  
212  N NH1 . ARG   A 30  ? 1.1752 1.3421 0.9718 0.2990  0.0174  0.0357  73  ARG   A NH1 
213  N NH2 . ARG   A 30  ? 1.0259 1.1735 0.7850 0.3175  0.0204  0.0280  73  ARG   A NH2 
214  N N   . LEU   A 31  ? 0.7419 0.9582 0.6381 0.2109  0.0495  0.0813  74  LEU   A N   
215  C CA  . LEU   A 31  ? 0.7363 0.9645 0.6584 0.1935  0.0497  0.0866  74  LEU   A CA  
216  C C   . LEU   A 31  ? 0.7093 0.9340 0.6345 0.1805  0.0330  0.0798  74  LEU   A C   
217  O O   . LEU   A 31  ? 0.7032 0.9104 0.6097 0.1775  0.0251  0.0717  74  LEU   A O   
218  C CB  . LEU   A 31  ? 0.7675 0.9888 0.6894 0.1844  0.0590  0.0902  74  LEU   A CB  
219  C CG  . LEU   A 31  ? 0.7703 0.9951 0.6910 0.1959  0.0772  0.0993  74  LEU   A CG  
220  C CD1 . LEU   A 31  ? 0.7531 0.9678 0.6719 0.1862  0.0847  0.1023  74  LEU   A CD1 
221  C CD2 . LEU   A 31  ? 0.7531 1.0003 0.7005 0.1987  0.0869  0.1089  74  LEU   A CD2 
222  N N   . ASP   A 32  ? 0.6643 0.9050 0.6123 0.1739  0.0280  0.0831  75  ASP   A N   
223  C CA  . ASP   A 32  ? 0.6749 0.9134 0.6272 0.1597  0.0127  0.0785  75  ASP   A CA  
224  C C   . ASP   A 32  ? 0.6014 0.8354 0.5599 0.1410  0.0126  0.0786  75  ASP   A C   
225  O O   . ASP   A 32  ? 0.5923 0.8407 0.5741 0.1346  0.0193  0.0851  75  ASP   A O   
226  C CB  . ASP   A 32  ? 0.7278 0.9865 0.7038 0.1601  0.0066  0.0827  75  ASP   A CB  
227  C CG  . ASP   A 32  ? 0.7770 1.0380 0.7468 0.1768  0.0035  0.0813  75  ASP   A CG  
228  O OD1 . ASP   A 32  ? 0.8119 1.0552 0.7575 0.1823  -0.0015 0.0742  75  ASP   A OD1 
229  O OD2 . ASP   A 32  ? 0.8289 1.1092 0.8195 0.1837  0.0062  0.0871  75  ASP   A OD2 
230  N N   . VAL   A 33  ? 0.5741 0.7890 0.5144 0.1322  0.0054  0.0712  76  VAL   A N   
231  C CA  . VAL   A 33  ? 0.5994 0.8055 0.5409 0.1153  0.0063  0.0698  76  VAL   A CA  
232  C C   . VAL   A 33  ? 0.5991 0.7946 0.5322 0.1027  -0.0081 0.0631  76  VAL   A C   
233  O O   . VAL   A 33  ? 0.5865 0.7737 0.5049 0.1082  -0.0167 0.0584  76  VAL   A O   
234  C CB  . VAL   A 33  ? 0.5894 0.7797 0.5148 0.1177  0.0165  0.0683  76  VAL   A CB  
235  C CG1 . VAL   A 33  ? 0.6065 0.8036 0.5325 0.1330  0.0297  0.0745  76  VAL   A CG1 
236  C CG2 . VAL   A 33  ? 0.6035 0.7740 0.5047 0.1201  0.0100  0.0596  76  VAL   A CG2 
237  N N   . ALA   A 34  ? 0.5932 0.7874 0.5343 0.0864  -0.0104 0.0625  77  ALA   A N   
238  C CA  . ALA   A 34  ? 0.5955 0.7755 0.5245 0.0728  -0.0222 0.0559  77  ALA   A CA  
239  C C   . ALA   A 34  ? 0.5799 0.7406 0.4960 0.0636  -0.0155 0.0517  77  ALA   A C   
240  O O   . ALA   A 34  ? 0.5787 0.7424 0.5038 0.0634  -0.0041 0.0554  77  ALA   A O   
241  C CB  . ALA   A 34  ? 0.5755 0.7692 0.5236 0.0619  -0.0318 0.0577  77  ALA   A CB  
242  N N   . LEU   A 35  ? 0.5851 0.7259 0.4803 0.0576  -0.0212 0.0446  78  LEU   A N   
243  C CA  . LEU   A 35  ? 0.6056 0.7266 0.4884 0.0480  -0.0155 0.0397  78  LEU   A CA  
244  C C   . LEU   A 35  ? 0.6328 0.7442 0.5094 0.0320  -0.0249 0.0350  78  LEU   A C   
245  O O   . LEU   A 35  ? 0.6467 0.7505 0.5089 0.0314  -0.0353 0.0314  78  LEU   A O   
246  C CB  . LEU   A 35  ? 0.6107 0.7154 0.4740 0.0565  -0.0128 0.0350  78  LEU   A CB  
247  C CG  . LEU   A 35  ? 0.6155 0.6993 0.4663 0.0485  -0.0068 0.0295  78  LEU   A CG  
248  C CD1 . LEU   A 35  ? 0.6064 0.6927 0.4676 0.0469  0.0044  0.0331  78  LEU   A CD1 
249  C CD2 . LEU   A 35  ? 0.6031 0.6733 0.4391 0.0570  -0.0055 0.0246  78  LEU   A CD2 
250  N N   . ASP   A 36  ? 0.5991 0.7115 0.4864 0.0198  -0.0221 0.0352  79  ASP   A N   
251  C CA  . ASP   A 36  ? 0.6103 0.7133 0.4917 0.0039  -0.0313 0.0299  79  ASP   A CA  
252  C C   . ASP   A 36  ? 0.6131 0.6887 0.4700 -0.0027 -0.0273 0.0225  79  ASP   A C   
253  O O   . ASP   A 36  ? 0.6040 0.6706 0.4532 0.0048  -0.0176 0.0221  79  ASP   A O   
254  C CB  . ASP   A 36  ? 0.6163 0.7326 0.5222 -0.0063 -0.0309 0.0325  79  ASP   A CB  
255  C CG  . ASP   A 36  ? 0.6357 0.7442 0.5478 -0.0125 -0.0173 0.0327  79  ASP   A CG  
256  O OD1 . ASP   A 36  ? 0.6571 0.7488 0.5533 -0.0095 -0.0085 0.0304  79  ASP   A OD1 
257  O OD2 . ASP   A 36  ? 0.6984 0.8179 0.6329 -0.0205 -0.0158 0.0354  79  ASP   A OD2 
258  N N   . GLU   A 37  ? 0.6333 0.6962 0.4787 -0.0160 -0.0348 0.0168  80  GLU   A N   
259  C CA  . GLU   A 37  ? 0.6493 0.6849 0.4696 -0.0230 -0.0315 0.0094  80  GLU   A CA  
260  C C   . GLU   A 37  ? 0.6212 0.6478 0.4465 -0.0273 -0.0175 0.0082  80  GLU   A C   
261  O O   . GLU   A 37  ? 0.5986 0.6056 0.4074 -0.0272 -0.0103 0.0038  80  GLU   A O   
262  C CB  . GLU   A 37  ? 0.7044 0.7298 0.5097 -0.0347 -0.0441 0.0040  80  GLU   A CB  
263  C CG  . GLU   A 37  ? 0.7661 0.7628 0.5412 -0.0393 -0.0412 -0.0029 80  GLU   A CG  
264  C CD  . GLU   A 37  ? 0.8163 0.7990 0.5708 -0.0505 -0.0529 -0.0087 80  GLU   A CD  
265  O OE1 . GLU   A 37  ? 0.8166 0.7937 0.5726 -0.0626 -0.0539 -0.0131 80  GLU   A OE1 
266  O OE2 . GLU   A 37  ? 0.8718 0.8485 0.6081 -0.0467 -0.0613 -0.0087 80  GLU   A OE2 
267  N N   . SER   A 38  ? 0.6055 0.6459 0.4538 -0.0302 -0.0130 0.0125  81  SER   A N   
268  C CA  . SER   A 38  ? 0.6133 0.6470 0.4694 -0.0330 0.0009  0.0134  81  SER   A CA  
269  C C   . SER   A 38  ? 0.5965 0.6348 0.4561 -0.0179 0.0115  0.0187  81  SER   A C   
270  O O   . SER   A 38  ? 0.6192 0.6527 0.4849 -0.0182 0.0228  0.0206  81  SER   A O   
271  C CB  . SER   A 38  ? 0.6464 0.6928 0.5269 -0.0412 0.0023  0.0169  81  SER   A CB  
272  O OG  . SER   A 38  ? 0.7148 0.7556 0.5928 -0.0560 -0.0081 0.0107  81  SER   A OG  
273  N N   . GLY   A 39  ? 0.6009 0.6482 0.4571 -0.0050 0.0077  0.0211  82  GLY   A N   
274  C CA  . GLY   A 39  ? 0.5933 0.6452 0.4517 0.0102  0.0162  0.0254  82  GLY   A CA  
275  C C   . GLY   A 39  ? 0.5697 0.6407 0.4485 0.0169  0.0229  0.0344  82  GLY   A C   
276  O O   . GLY   A 39  ? 0.5381 0.6093 0.4168 0.0278  0.0318  0.0380  82  GLY   A O   
277  N N   . ASP   A 40  ? 0.5937 0.6807 0.4899 0.0114  0.0187  0.0382  83  ASP   A N   
278  C CA  . ASP   A 40  ? 0.6227 0.7298 0.5407 0.0180  0.0258  0.0476  83  ASP   A CA  
279  C C   . ASP   A 40  ? 0.5957 0.7197 0.5167 0.0307  0.0196  0.0508  83  ASP   A C   
280  O O   . ASP   A 40  ? 0.5959 0.7260 0.5186 0.0264  0.0074  0.0483  83  ASP   A O   
281  C CB  . ASP   A 40  ? 0.6559 0.7705 0.5955 0.0037  0.0262  0.0495  83  ASP   A CB  
282  C CG  . ASP   A 40  ? 0.7224 0.8190 0.6593 -0.0075 0.0340  0.0466  83  ASP   A CG  
283  O OD1 . ASP   A 40  ? 0.8005 0.8844 0.7261 -0.0008 0.0440  0.0472  83  ASP   A OD1 
284  O OD2 . ASP   A 40  ? 0.8141 0.9092 0.7607 -0.0224 0.0299  0.0434  83  ASP   A OD2 
285  N N   . PHE   A 41  ? 0.6100 0.7402 0.5303 0.0464  0.0274  0.0560  84  PHE   A N   
286  C CA  . PHE   A 41  ? 0.5923 0.7405 0.5192 0.0596  0.0247  0.0604  84  PHE   A CA  
287  C C   . PHE   A 41  ? 0.6196 0.7892 0.5744 0.0563  0.0272  0.0678  84  PHE   A C   
288  O O   . PHE   A 41  ? 0.6638 0.8343 0.6323 0.0481  0.0358  0.0715  84  PHE   A O   
289  C CB  . PHE   A 41  ? 0.5578 0.7042 0.4739 0.0773  0.0329  0.0631  84  PHE   A CB  
290  C CG  . PHE   A 41  ? 0.5563 0.6866 0.4497 0.0830  0.0275  0.0553  84  PHE   A CG  
291  C CD1 . PHE   A 41  ? 0.5398 0.6709 0.4261 0.0868  0.0165  0.0510  84  PHE   A CD1 
292  C CD2 . PHE   A 41  ? 0.5563 0.6707 0.4370 0.0852  0.0336  0.0526  84  PHE   A CD2 
293  C CE1 . PHE   A 41  ? 0.5669 0.6833 0.4352 0.0918  0.0125  0.0439  84  PHE   A CE1 
294  C CE2 . PHE   A 41  ? 0.5380 0.6391 0.4021 0.0902  0.0286  0.0453  84  PHE   A CE2 
295  C CZ  . PHE   A 41  ? 0.5470 0.6493 0.4054 0.0937  0.0186  0.0410  84  PHE   A CZ  
296  N N   . SER   A 42  ? 0.6088 0.7954 0.5736 0.0625  0.0204  0.0701  85  SER   A N   
297  C CA  . SER   A 42  ? 0.6166 0.8266 0.6115 0.0622  0.0239  0.0779  85  SER   A CA  
298  C C   . SER   A 42  ? 0.6277 0.8528 0.6260 0.0785  0.0225  0.0815  85  SER   A C   
299  O O   . SER   A 42  ? 0.5968 0.8146 0.5760 0.0857  0.0137  0.0764  85  SER   A O   
300  C CB  . SER   A 42  ? 0.6415 0.8578 0.6533 0.0455  0.0127  0.0751  85  SER   A CB  
301  O OG  . SER   A 42  ? 0.6359 0.8485 0.6349 0.0441  -0.0039 0.0688  85  SER   A OG  
302  N N   . LEU   A 43  ? 0.6845 0.9291 0.7066 0.0843  0.0324  0.0902  86  LEU   A N   
303  C CA  . LEU   A 43  ? 0.7010 0.9617 0.7299 0.1002  0.0333  0.0944  86  LEU   A CA  
304  C C   . LEU   A 43  ? 0.7192 0.9945 0.7656 0.0944  0.0177  0.0927  86  LEU   A C   
305  O O   . LEU   A 43  ? 0.7042 0.9923 0.7774 0.0822  0.0155  0.0949  86  LEU   A O   
306  C CB  . LEU   A 43  ? 0.7264 1.0010 0.7744 0.1080  0.0518  0.1048  86  LEU   A CB  
307  C CG  . LEU   A 43  ? 0.7607 1.0197 0.7864 0.1173  0.0663  0.1071  86  LEU   A CG  
308  C CD1 . LEU   A 43  ? 0.7984 1.0664 0.8434 0.1185  0.0856  0.1179  86  LEU   A CD1 
309  C CD2 . LEU   A 43  ? 0.7758 1.0292 0.7769 0.1369  0.0662  0.1050  86  LEU   A CD2 
310  N N   . VAL   A 44  ? 0.7547 1.0262 0.7854 0.1026  0.0067  0.0883  87  VAL   A N   
311  C CA  . VAL   A 44  ? 0.8097 1.0963 0.8548 0.1040  -0.0068 0.0884  87  VAL   A CA  
312  C C   . VAL   A 44  ? 0.8934 1.2008 0.9583 0.1194  0.0030  0.0962  87  VAL   A C   
313  O O   . VAL   A 44  ? 0.9746 1.2758 1.0219 0.1351  0.0101  0.0963  87  VAL   A O   
314  C CB  . VAL   A 44  ? 0.7909 1.0613 0.8080 0.1084  -0.0197 0.0813  87  VAL   A CB  
315  C CG1 . VAL   A 44  ? 0.7785 1.0628 0.8073 0.1138  -0.0324 0.0824  87  VAL   A CG1 
316  C CG2 . VAL   A 44  ? 0.7700 1.0189 0.7667 0.0938  -0.0277 0.0738  87  VAL   A CG2 
317  N N   . GLU   A 45  ? 0.9769 1.3077 1.0775 0.1157  0.0044  0.1022  88  GLU   A N   
318  C CA  . GLU   A 45  ? 1.0963 1.4475 1.2175 0.1311  0.0154  0.1099  88  GLU   A CA  
319  C C   . GLU   A 45  ? 1.1096 1.4773 1.2485 0.1344  0.0006  0.1098  88  GLU   A C   
320  O O   . GLU   A 45  ? 1.0746 1.4318 1.1921 0.1395  -0.0120 0.1045  88  GLU   A O   
321  C CB  . GLU   A 45  ? 1.1610 1.5270 1.3119 0.1269  0.0324  0.1183  88  GLU   A CB  
322  C CG  . GLU   A 45  ? 1.1996 1.5499 1.3308 0.1306  0.0505  0.1208  88  GLU   A CG  
323  C CD  . GLU   A 45  ? 1.2166 1.5635 1.3290 0.1521  0.0638  0.1241  88  GLU   A CD  
324  O OE1 . GLU   A 45  ? 1.2441 1.5793 1.3299 0.1615  0.0550  0.1179  88  GLU   A OE1 
325  O OE2 . GLU   A 45  ? 1.2564 1.6116 1.3807 0.1597  0.0830  0.1328  88  GLU   A OE2 
326  N N   . GLY   B 7   ? 0.9841 1.0249 0.9710 0.0938  0.0317  -0.0568 16  GLY   B N   
327  C CA  . GLY   B 7   ? 1.0009 1.0303 0.9802 0.0963  0.0341  -0.0501 16  GLY   B CA  
328  C C   . GLY   B 7   ? 0.9723 0.9981 0.9444 0.1003  0.0309  -0.0508 16  GLY   B C   
329  O O   . GLY   B 7   ? 0.9820 1.0141 0.9562 0.0975  0.0269  -0.0559 16  GLY   B O   
330  N N   . GLU   B 8   ? 0.8723 0.8887 0.8360 0.1066  0.0324  -0.0456 17  GLU   B N   
331  C CA  . GLU   B 8   ? 0.8235 0.8346 0.7785 0.1117  0.0296  -0.0455 17  GLU   B CA  
332  C C   . GLU   B 8   ? 0.7757 0.7861 0.7302 0.1052  0.0291  -0.0451 17  GLU   B C   
333  O O   . GLU   B 8   ? 0.7414 0.7484 0.6954 0.1025  0.0330  -0.0402 17  GLU   B O   
334  C CB  . GLU   B 8   ? 0.8131 0.8155 0.7594 0.1202  0.0322  -0.0393 17  GLU   B CB  
335  C CG  . GLU   B 8   ? 0.8127 0.8098 0.7491 0.1274  0.0289  -0.0399 17  GLU   B CG  
336  C CD  . GLU   B 8   ? 0.8473 0.8373 0.7745 0.1371  0.0312  -0.0344 17  GLU   B CD  
337  O OE1 . GLU   B 8   ? 0.7761 0.7643 0.7042 0.1371  0.0361  -0.0282 17  GLU   B OE1 
338  O OE2 . GLU   B 8   ? 0.9254 0.9117 0.8445 0.1446  0.0277  -0.0362 17  GLU   B OE2 
339  N N   A THR   B 9   ? 0.7818 0.7949 0.7361 0.1026  0.0240  -0.0502 18  THR   B N   
340  N N   B THR   B 9   ? 0.7755 0.7887 0.7298 0.1027  0.0240  -0.0503 18  THR   B N   
341  N N   C THR   B 9   ? 0.7818 0.7949 0.7361 0.1026  0.0240  -0.0502 18  THR   B N   
342  N N   D THR   B 9   ? 0.7755 0.7887 0.7298 0.1027  0.0240  -0.0503 18  THR   B N   
343  C CA  A THR   B 9   ? 0.7857 0.7972 0.7389 0.0956  0.0223  -0.0505 18  THR   B CA  
344  C CA  B THR   B 9   ? 0.7745 0.7868 0.7282 0.0954  0.0219  -0.0511 18  THR   B CA  
345  C CA  C THR   B 9   ? 0.7857 0.7972 0.7389 0.0956  0.0223  -0.0505 18  THR   B CA  
346  C CA  D THR   B 9   ? 0.7745 0.7868 0.7282 0.0954  0.0219  -0.0511 18  THR   B CA  
347  C C   A THR   B 9   ? 0.7785 0.7820 0.7210 0.1010  0.0176  -0.0513 18  THR   B C   
348  C C   B THR   B 9   ? 0.7723 0.7757 0.7148 0.1011  0.0179  -0.0510 18  THR   B C   
349  C C   C THR   B 9   ? 0.7785 0.7820 0.7210 0.1010  0.0176  -0.0513 18  THR   B C   
350  C C   D THR   B 9   ? 0.7723 0.7757 0.7148 0.1011  0.0179  -0.0510 18  THR   B C   
351  O O   A THR   B 9   ? 0.8007 0.8012 0.7407 0.0959  0.0148  -0.0521 18  THR   B O   
352  O O   B THR   B 9   ? 0.7933 0.7929 0.7327 0.0964  0.0159  -0.0510 18  THR   B O   
353  O O   C THR   B 9   ? 0.8007 0.8012 0.7407 0.0959  0.0148  -0.0521 18  THR   B O   
354  O O   D THR   B 9   ? 0.7933 0.7929 0.7327 0.0964  0.0159  -0.0510 18  THR   B O   
355  C CB  A THR   B 9   ? 0.7931 0.8146 0.7553 0.0859  0.0197  -0.0556 18  THR   B CB  
356  C CB  B THR   B 9   ? 0.7743 0.7970 0.7368 0.0868  0.0187  -0.0568 18  THR   B CB  
357  C CB  C THR   B 9   ? 0.7931 0.8146 0.7553 0.0859  0.0197  -0.0556 18  THR   B CB  
358  C CB  D THR   B 9   ? 0.7743 0.7970 0.7368 0.0868  0.0187  -0.0568 18  THR   B CB  
359  O OG1 A THR   B 9   ? 0.8005 0.8302 0.7714 0.0844  0.0227  -0.0565 18  THR   B OG1 
360  O OG1 B THR   B 9   ? 0.7626 0.7900 0.7254 0.0913  0.0144  -0.0616 18  THR   B OG1 
361  O OG1 C THR   B 9   ? 0.8005 0.8302 0.7714 0.0844  0.0227  -0.0565 18  THR   B OG1 
362  O OG1 D THR   B 9   ? 0.7626 0.7900 0.7254 0.0913  0.0144  -0.0616 18  THR   B OG1 
363  C CG2 A THR   B 9   ? 0.7917 0.8117 0.7546 0.0769  0.0198  -0.0544 18  THR   B CG2 
364  C CG2 B THR   B 9   ? 0.7775 0.8084 0.7500 0.0806  0.0228  -0.0566 18  THR   B CG2 
365  C CG2 C THR   B 9   ? 0.7917 0.8117 0.7546 0.0769  0.0198  -0.0544 18  THR   B CG2 
366  C CG2 D THR   B 9   ? 0.7775 0.8084 0.7500 0.0806  0.0228  -0.0566 18  THR   B CG2 
367  N N   . THR   B 10  ? 0.7601 0.7594 0.6957 0.1112  0.0166  -0.0509 19  THR   B N   
368  C CA  . THR   B 10  ? 0.7244 0.7151 0.6483 0.1181  0.0121  -0.0516 19  THR   B CA  
369  C C   . THR   B 10  ? 0.6427 0.6253 0.5593 0.1189  0.0142  -0.0468 19  THR   B C   
370  O O   . THR   B 10  ? 0.6101 0.5921 0.5271 0.1206  0.0202  -0.0413 19  THR   B O   
371  C CB  . THR   B 10  ? 0.7603 0.7478 0.6778 0.1296  0.0118  -0.0510 19  THR   B CB  
372  O OG1 . THR   B 10  ? 0.8595 0.8544 0.7841 0.1300  0.0118  -0.0539 19  THR   B OG1 
373  C CG2 . THR   B 10  ? 0.7696 0.7507 0.6770 0.1358  0.0052  -0.0542 19  THR   B CG2 
374  N N   . ASP   B 11  ? 0.6052 0.5815 0.5144 0.1184  0.0089  -0.0490 20  ASP   B N   
375  C CA  . ASP   B 11  ? 0.6242 0.5916 0.5236 0.1218  0.0097  -0.0452 20  ASP   B CA  
376  C C   . ASP   B 11  ? 0.6504 0.6144 0.5425 0.1334  0.0141  -0.0400 20  ASP   B C   
377  O O   . ASP   B 11  ? 0.6888 0.6539 0.5794 0.1401  0.0137  -0.0408 20  ASP   B O   
378  C CB  . ASP   B 11  ? 0.6632 0.6222 0.5532 0.1223  0.0017  -0.0491 20  ASP   B CB  
379  C CG  . ASP   B 11  ? 0.6932 0.6536 0.5885 0.1099  -0.0021 -0.0524 20  ASP   B CG  
380  O OD1 . ASP   B 11  ? 0.6387 0.6077 0.5454 0.1012  0.0016  -0.0518 20  ASP   B OD1 
381  O OD2 . ASP   B 11  ? 0.7741 0.7267 0.6615 0.1092  -0.0095 -0.0555 20  ASP   B OD2 
382  N N   . GLY   B 12  ? 0.6141 0.5750 0.5017 0.1356  0.0182  -0.0348 21  GLY   B N   
383  C CA  . GLY   B 12  ? 0.5959 0.5547 0.4759 0.1463  0.0225  -0.0291 21  GLY   B CA  
384  C C   . GLY   B 12  ? 0.5515 0.5142 0.4360 0.1438  0.0298  -0.0224 21  GLY   B C   
385  O O   . GLY   B 12  ? 0.5308 0.4963 0.4232 0.1341  0.0308  -0.0229 21  GLY   B O   
386  N N   . VAL   B 13  ? 0.5434 0.5066 0.4230 0.1520  0.0345  -0.0163 22  VAL   B N   
387  C CA  . VAL   B 13  ? 0.5294 0.4971 0.4126 0.1507  0.0417  -0.0088 22  VAL   B CA  
388  C C   . VAL   B 13  ? 0.5403 0.5136 0.4326 0.1479  0.0462  -0.0055 22  VAL   B C   
389  O O   . VAL   B 13  ? 0.5479 0.5204 0.4389 0.1521  0.0447  -0.0071 22  VAL   B O   
390  C CB  . VAL   B 13  ? 0.5496 0.5154 0.4213 0.1612  0.0437  -0.0039 22  VAL   B CB  
391  C CG1 . VAL   B 13  ? 0.5700 0.5344 0.4332 0.1726  0.0440  -0.0019 22  VAL   B CG1 
392  C CG2 . VAL   B 13  ? 0.5487 0.5204 0.4247 0.1589  0.0505  0.0034  22  VAL   B CG2 
393  N N   . TYR   B 14  ? 0.5308 0.5088 0.4319 0.1407  0.0509  -0.0013 23  TYR   B N   
394  C CA  . TYR   B 14  ? 0.5278 0.5098 0.4377 0.1367  0.0544  0.0015  23  TYR   B CA  
395  C C   . TYR   B 14  ? 0.5335 0.5192 0.4458 0.1356  0.0606  0.0100  23  TYR   B C   
396  O O   . TYR   B 14  ? 0.5276 0.5145 0.4393 0.1337  0.0621  0.0120  23  TYR   B O   
397  C CB  . TYR   B 14  ? 0.5311 0.5156 0.4518 0.1263  0.0528  -0.0034 23  TYR   B CB  
398  C CG  . TYR   B 14  ? 0.5120 0.4954 0.4328 0.1261  0.0471  -0.0113 23  TYR   B CG  
399  C CD1 . TYR   B 14  ? 0.5096 0.4897 0.4244 0.1277  0.0421  -0.0162 23  TYR   B CD1 
400  C CD2 . TYR   B 14  ? 0.5266 0.5126 0.4535 0.1244  0.0465  -0.0139 23  TYR   B CD2 
401  C CE1 . TYR   B 14  ? 0.5148 0.4950 0.4303 0.1269  0.0366  -0.0232 23  TYR   B CE1 
402  C CE2 . TYR   B 14  ? 0.5294 0.5163 0.4571 0.1244  0.0412  -0.0212 23  TYR   B CE2 
403  C CZ  . TYR   B 14  ? 0.5646 0.5492 0.4871 0.1251  0.0364  -0.0257 23  TYR   B CZ  
404  O OH  . TYR   B 14  ? 0.5660 0.5526 0.4902 0.1245  0.0311  -0.0325 23  TYR   B OH  
405  N N   . ARG   B 15  ? 0.5378 0.5249 0.4526 0.1366  0.0637  0.0149  24  ARG   B N   
406  C CA  . ARG   B 15  ? 0.5433 0.5345 0.4628 0.1333  0.0692  0.0233  24  ARG   B CA  
407  C C   . ARG   B 15  ? 0.5541 0.5469 0.4850 0.1222  0.0695  0.0216  24  ARG   B C   
408  O O   . ARG   B 15  ? 0.5026 0.4937 0.4375 0.1193  0.0665  0.0159  24  ARG   B O   
409  C CB  . ARG   B 15  ? 0.5648 0.5555 0.4813 0.1384  0.0716  0.0294  24  ARG   B CB  
410  C CG  . ARG   B 15  ? 0.5833 0.5723 0.4880 0.1500  0.0712  0.0309  24  ARG   B CG  
411  C CD  . ARG   B 15  ? 0.6052 0.5933 0.5074 0.1539  0.0733  0.0369  24  ARG   B CD  
412  N NE  . ARG   B 15  ? 0.6191 0.6051 0.5094 0.1654  0.0725  0.0376  24  ARG   B NE  
413  C CZ  . ARG   B 15  ? 0.6434 0.6332 0.5264 0.1723  0.0760  0.0442  24  ARG   B CZ  
414  N NH1 . ARG   B 15  ? 0.6114 0.6081 0.4982 0.1689  0.0810  0.0515  24  ARG   B NH1 
415  N NH2 . ARG   B 15  ? 0.6847 0.6720 0.5563 0.1832  0.0745  0.0433  24  ARG   B NH2 
416  N N   . VAL   B 16  ? 0.5436 0.5400 0.4793 0.1170  0.0732  0.0266  25  VAL   B N   
417  C CA  . VAL   B 16  ? 0.5714 0.5694 0.5175 0.1070  0.0742  0.0269  25  VAL   B CA  
418  C C   . VAL   B 16  ? 0.5591 0.5585 0.5079 0.1059  0.0781  0.0357  25  VAL   B C   
419  O O   . VAL   B 16  ? 0.5853 0.5887 0.5325 0.1076  0.0817  0.0428  25  VAL   B O   
420  C CB  . VAL   B 16  ? 0.5953 0.5958 0.5448 0.1013  0.0747  0.0256  25  VAL   B CB  
421  C CG1 . VAL   B 16  ? 0.5912 0.5929 0.5509 0.0913  0.0754  0.0252  25  VAL   B CG1 
422  C CG2 . VAL   B 16  ? 0.5804 0.5783 0.5254 0.1026  0.0704  0.0179  25  VAL   B CG2 
423  N N   . MET   B 17  ? 0.5926 0.5891 0.5458 0.1024  0.0769  0.0348  26  MET   B N   
424  C CA  . MET   B 17  ? 0.6078 0.6028 0.5625 0.1014  0.0789  0.0421  26  MET   B CA  
425  C C   . MET   B 17  ? 0.6011 0.5952 0.5649 0.0919  0.0786  0.0420  26  MET   B C   
426  O O   . MET   B 17  ? 0.5756 0.5689 0.5435 0.0881  0.0759  0.0344  26  MET   B O   
427  C CB  . MET   B 17  ? 0.6235 0.6129 0.5734 0.1069  0.0761  0.0397  26  MET   B CB  
428  C CG  . MET   B 17  ? 0.6450 0.6341 0.5855 0.1167  0.0750  0.0376  26  MET   B CG  
429  S SD  . MET   B 17  ? 0.6624 0.6551 0.5949 0.1240  0.0796  0.0477  26  MET   B SD  
430  C CE  . MET   B 17  ? 0.6910 0.6809 0.6250 0.1214  0.0815  0.0567  26  MET   B CE  
431  N N   . THR   B 18  ? 0.6260 0.6198 0.5923 0.0885  0.0810  0.0503  27  THR   B N   
432  C CA  . THR   B 18  ? 0.6934 0.6841 0.6667 0.0804  0.0801  0.0516  27  THR   B CA  
433  C C   . THR   B 18  ? 0.7448 0.7297 0.7154 0.0814  0.0796  0.0578  27  THR   B C   
434  O O   . THR   B 18  ? 0.6750 0.6616 0.6402 0.0861  0.0820  0.0649  27  THR   B O   
435  C CB  . THR   B 18  ? 0.6903 0.6864 0.6699 0.0735  0.0829  0.0559  27  THR   B CB  
436  O OG1 . THR   B 18  ? 0.7098 0.7016 0.6954 0.0660  0.0813  0.0560  27  THR   B OG1 
437  C CG2 . THR   B 18  ? 0.6859 0.6878 0.6636 0.0751  0.0872  0.0660  27  THR   B CG2 
438  N N   . ARG   B 19  ? 0.7919 0.7699 0.7654 0.0773  0.0764  0.0555  28  ARG   B N   
439  C CA  . ARG   B 19  ? 0.8767 0.8473 0.8486 0.0754  0.0752  0.0623  28  ARG   B CA  
440  C C   . ARG   B 19  ? 0.8649 0.8348 0.8438 0.0659  0.0756  0.0674  28  ARG   B C   
441  O O   . ARG   B 19  ? 0.9048 0.8668 0.8827 0.0630  0.0735  0.0721  28  ARG   B O   
442  C CB  . ARG   B 19  ? 0.9069 0.8685 0.8752 0.0789  0.0704  0.0558  28  ARG   B CB  
443  C CG  . ARG   B 19  ? 0.9637 0.9261 0.9253 0.0882  0.0696  0.0508  28  ARG   B CG  
444  C CD  . ARG   B 19  ? 0.9786 0.9319 0.9332 0.0936  0.0663  0.0510  28  ARG   B CD  
445  N NE  . ARG   B 19  ? 1.0072 0.9613 0.9568 0.1019  0.0644  0.0436  28  ARG   B NE  
446  C CZ  . ARG   B 19  ? 1.0946 1.0500 1.0465 0.1032  0.0613  0.0332  28  ARG   B CZ  
447  N NH1 . ARG   B 19  ? 1.1547 1.1107 1.1134 0.0972  0.0598  0.0288  28  ARG   B NH1 
448  N NH2 . ARG   B 19  ? 1.1072 1.0639 1.0546 0.1106  0.0595  0.0275  28  ARG   B NH2 
449  N N   . ARG   B 20  ? 0.8930 0.8701 0.8779 0.0612  0.0780  0.0672  29  ARG   B N   
450  C CA  . ARG   B 20  ? 0.9945 0.9715 0.9865 0.0521  0.0781  0.0713  29  ARG   B CA  
451  C C   . ARG   B 20  ? 0.9938 0.9744 0.9862 0.0494  0.0812  0.0837  29  ARG   B C   
452  O O   . ARG   B 20  ? 1.0163 0.9966 1.0143 0.0416  0.0811  0.0888  29  ARG   B O   
453  C CB  . ARG   B 20  ? 1.0362 1.0199 1.0337 0.0489  0.0794  0.0659  29  ARG   B CB  
454  C CG  . ARG   B 20  ? 1.1208 1.1023 1.1252 0.0402  0.0779  0.0655  29  ARG   B CG  
455  C CD  . ARG   B 20  ? 1.2600 1.2493 1.2692 0.0372  0.0801  0.0628  29  ARG   B CD  
456  N NE  . ARG   B 20  ? 1.3480 1.3462 1.3567 0.0390  0.0844  0.0692  29  ARG   B NE  
457  C CZ  . ARG   B 20  ? 1.4164 1.4202 1.4298 0.0341  0.0869  0.0763  29  ARG   B CZ  
458  N NH1 . ARG   B 20  ? 1.4569 1.4579 1.4762 0.0262  0.0853  0.0782  29  ARG   B NH1 
459  N NH2 . ARG   B 20  ? 1.3998 1.4125 1.4117 0.0375  0.0907  0.0813  29  ARG   B NH2 
460  N N   . LEU   B 21  ? 0.9494 0.9342 0.9362 0.0556  0.0840  0.0886  30  LEU   B N   
461  C CA  . LEU   B 21  ? 0.9044 0.8947 0.8909 0.0541  0.0875  0.1010  30  LEU   B CA  
462  C C   . LEU   B 21  ? 0.8590 0.8419 0.8383 0.0578  0.0859  0.1054  30  LEU   B C   
463  O O   . LEU   B 21  ? 0.8413 0.8134 0.8171 0.0599  0.0815  0.0988  30  LEU   B O   
464  C CB  . LEU   B 21  ? 0.9015 0.9046 0.8872 0.0591  0.0924  0.1029  30  LEU   B CB  
465  C CG  . LEU   B 21  ? 0.9322 0.9448 0.9253 0.0534  0.0951  0.1060  30  LEU   B CG  
466  C CD1 . LEU   B 21  ? 0.9475 0.9548 0.9474 0.0458  0.0919  0.0999  30  LEU   B CD1 
467  C CD2 . LEU   B 21  ? 0.9338 0.9560 0.9244 0.0600  0.0983  0.1033  30  LEU   B CD2 
468  N N   . LEU   B 22  ? 0.8610 0.8494 0.8378 0.0587  0.0893  0.1163  31  LEU   B N   
469  C CA  . LEU   B 22  ? 0.8282 0.8102 0.7969 0.0628  0.0883  0.1214  31  LEU   B CA  
470  C C   . LEU   B 22  ? 0.8215 0.8016 0.7824 0.0736  0.0878  0.1134  31  LEU   B C   
471  O O   . LEU   B 22  ? 0.8773 0.8663 0.8381 0.0785  0.0906  0.1095  31  LEU   B O   
472  C CB  . LEU   B 22  ? 0.8122 0.8042 0.7805 0.0617  0.0930  0.1347  31  LEU   B CB  
473  C CG  . LEU   B 22  ? 0.8219 0.8064 0.7831 0.0624  0.0918  0.1427  31  LEU   B CG  
474  C CD1 . LEU   B 22  ? 0.8041 0.7771 0.7683 0.0523  0.0872  0.1469  31  LEU   B CD1 
475  C CD2 . LEU   B 22  ? 0.8131 0.8108 0.7720 0.0649  0.0976  0.1543  31  LEU   B CD2 
476  N N   . GLY   B 23  ? 0.7887 0.7573 0.7429 0.0774  0.0839  0.1106  32  GLY   B N   
477  C CA  . GLY   B 23  ? 0.7535 0.7199 0.7004 0.0876  0.0827  0.1026  32  GLY   B CA  
478  C C   . GLY   B 23  ? 0.7278 0.6985 0.6781 0.0900  0.0822  0.0911  32  GLY   B C   
479  O O   . GLY   B 23  ? 0.7234 0.6947 0.6812 0.0835  0.0812  0.0871  32  GLY   B O   
480  N N   . SER   B 24  ? 0.7126 0.6852 0.6569 0.0989  0.0823  0.0857  33  SER   B N   
481  C CA  . SER   B 24  ? 0.6857 0.6631 0.6318 0.1015  0.0820  0.0761  33  SER   B CA  
482  C C   . SER   B 24  ? 0.6716 0.6599 0.6173 0.1035  0.0868  0.0808  33  SER   B C   
483  O O   . SER   B 24  ? 0.6395 0.6306 0.5786 0.1098  0.0892  0.0866  33  SER   B O   
484  C CB  . SER   B 24  ? 0.6886 0.6616 0.6283 0.1096  0.0787  0.0681  33  SER   B CB  
485  O OG  . SER   B 24  ? 0.7347 0.6985 0.6749 0.1079  0.0742  0.0637  33  SER   B OG  
486  N N   . THR   B 25  ? 0.6435 0.6376 0.5958 0.0987  0.0880  0.0787  34  THR   B N   
487  C CA  . THR   B 25  ? 0.6362 0.6406 0.5884 0.1003  0.0924  0.0833  34  THR   B CA  
488  C C   . THR   B 25  ? 0.6350 0.6413 0.5857 0.1040  0.0911  0.0741  34  THR   B C   
489  O O   . THR   B 25  ? 0.6392 0.6418 0.5946 0.0994  0.0880  0.0662  34  THR   B O   
490  C CB  . THR   B 25  ? 0.6601 0.6701 0.6208 0.0913  0.0950  0.0900  34  THR   B CB  
491  O OG1 . THR   B 25  ? 0.6953 0.7028 0.6570 0.0874  0.0955  0.0989  34  THR   B OG1 
492  C CG2 . THR   B 25  ? 0.6577 0.6793 0.6181 0.0939  0.0994  0.0949  34  THR   B CG2 
493  N N   . GLN   B 26  ? 0.6241 0.6352 0.5678 0.1120  0.0930  0.0752  35  GLN   B N   
494  C CA  . GLN   B 26  ? 0.6187 0.6300 0.5593 0.1160  0.0909  0.0667  35  GLN   B CA  
495  C C   . GLN   B 26  ? 0.6500 0.6681 0.5953 0.1117  0.0933  0.0685  35  GLN   B C   
496  O O   . GLN   B 26  ? 0.6470 0.6727 0.5903 0.1147  0.0973  0.0761  35  GLN   B O   
497  C CB  . GLN   B 26  ? 0.5959 0.6075 0.5253 0.1274  0.0908  0.0661  35  GLN   B CB  
498  C CG  . GLN   B 26  ? 0.5937 0.6029 0.5189 0.1310  0.0874  0.0569  35  GLN   B CG  
499  C CD  . GLN   B 26  ? 0.5898 0.5977 0.5032 0.1427  0.0863  0.0556  35  GLN   B CD  
500  O OE1 . GLN   B 26  ? 0.6152 0.6192 0.5239 0.1475  0.0851  0.0554  35  GLN   B OE1 
501  N NE2 . GLN   B 26  ? 0.5707 0.5809 0.4785 0.1477  0.0862  0.0541  35  GLN   B NE2 
502  N N   . VAL   B 27  ? 0.6287 0.6445 0.5796 0.1052  0.0910  0.0619  36  VAL   B N   
503  C CA  . VAL   B 27  ? 0.6130 0.6342 0.5683 0.1008  0.0927  0.0629  36  VAL   B CA  
504  C C   . VAL   B 27  ? 0.5684 0.5890 0.5167 0.1067  0.0908  0.0569  36  VAL   B C   
505  O O   . VAL   B 27  ? 0.5596 0.5847 0.5079 0.1066  0.0924  0.0584  36  VAL   B O   
506  C CB  . VAL   B 27  ? 0.6377 0.6566 0.6028 0.0901  0.0913  0.0598  36  VAL   B CB  
507  C CG1 . VAL   B 27  ? 0.6608 0.6810 0.6325 0.0839  0.0934  0.0675  36  VAL   B CG1 
508  C CG2 . VAL   B 27  ? 0.5969 0.6087 0.5628 0.0882  0.0869  0.0503  36  VAL   B CG2 
509  N N   . GLY   B 28  ? 0.5485 0.5633 0.4905 0.1118  0.0872  0.0501  37  GLY   B N   
510  C CA  . GLY   B 28  ? 0.5166 0.5294 0.4504 0.1178  0.0847  0.0450  37  GLY   B CA  
511  C C   . GLY   B 28  ? 0.5196 0.5256 0.4474 0.1223  0.0800  0.0376  37  GLY   B C   
512  O O   . GLY   B 28  ? 0.5338 0.5379 0.4621 0.1236  0.0795  0.0379  37  GLY   B O   
513  N N   . VAL   B 29  ? 0.4998 0.5019 0.4226 0.1240  0.0760  0.0310  38  VAL   B N   
514  C CA  . VAL   B 29  ? 0.4928 0.4885 0.4074 0.1300  0.0709  0.0242  38  VAL   B CA  
515  C C   . VAL   B 29  ? 0.4947 0.4865 0.4111 0.1237  0.0663  0.0166  38  VAL   B C   
516  O O   . VAL   B 29  ? 0.4718 0.4652 0.3914 0.1186  0.0676  0.0176  38  VAL   B O   
517  C CB  . VAL   B 29  ? 0.5181 0.5132 0.4202 0.1418  0.0710  0.0265  38  VAL   B CB  
518  C CG1 . VAL   B 29  ? 0.5349 0.5227 0.4278 0.1481  0.0651  0.0195  38  VAL   B CG1 
519  C CG2 . VAL   B 29  ? 0.5149 0.5157 0.4149 0.1479  0.0761  0.0352  38  VAL   B CG2 
520  N N   . GLY   B 30  ? 0.4913 0.4782 0.4052 0.1241  0.0611  0.0095  39  GLY   B N   
521  C CA  . GLY   B 30  ? 0.4633 0.4465 0.3777 0.1182  0.0563  0.0027  39  GLY   B CA  
522  C C   . GLY   B 30  ? 0.4699 0.4475 0.3772 0.1224  0.0502  -0.0035 39  GLY   B C   
523  O O   . GLY   B 30  ? 0.5115 0.4883 0.4140 0.1304  0.0499  -0.0029 39  GLY   B O   
524  N N   . VAL   B 31  ? 0.4616 0.4355 0.3682 0.1171  0.0453  -0.0092 40  VAL   B N   
525  C CA  . VAL   B 31  ? 0.4718 0.4396 0.3713 0.1196  0.0382  -0.0156 40  VAL   B CA  
526  C C   . VAL   B 31  ? 0.4906 0.4611 0.3992 0.1095  0.0352  -0.0211 40  VAL   B C   
527  O O   . VAL   B 31  ? 0.4678 0.4404 0.3829 0.1001  0.0359  -0.0216 40  VAL   B O   
528  C CB  . VAL   B 31  ? 0.5011 0.4608 0.3899 0.1218  0.0337  -0.0174 40  VAL   B CB  
529  C CG1 . VAL   B 31  ? 0.5221 0.4751 0.4047 0.1225  0.0257  -0.0240 40  VAL   B CG1 
530  C CG2 . VAL   B 31  ? 0.5197 0.4774 0.3986 0.1325  0.0363  -0.0124 40  VAL   B CG2 
531  N N   . MET   B 32  ? 0.5046 0.4765 0.4145 0.1114  0.0325  -0.0247 41  MET   B N   
532  C CA  . MET   B 32  ? 0.5135 0.4889 0.4305 0.1035  0.0286  -0.0306 41  MET   B CA  
533  C C   . MET   B 32  ? 0.5171 0.4858 0.4259 0.1039  0.0209  -0.0356 41  MET   B C   
534  O O   . MET   B 32  ? 0.5054 0.4690 0.4053 0.1125  0.0175  -0.0367 41  MET   B O   
535  C CB  . MET   B 32  ? 0.5437 0.5244 0.4658 0.1062  0.0294  -0.0319 41  MET   B CB  
536  C CG  . MET   B 32  ? 0.5766 0.5644 0.5086 0.0979  0.0270  -0.0372 41  MET   B CG  
537  S SD  . MET   B 32  ? 0.5797 0.5752 0.5245 0.0869  0.0321  -0.0357 41  MET   B SD  
538  C CE  . MET   B 32  ? 0.6075 0.6045 0.5549 0.0926  0.0381  -0.0304 41  MET   B CE  
539  N N   . GLN   B 33  ? 0.5424 0.5109 0.4541 0.0943  0.0176  -0.0385 42  GLN   B N   
540  C CA  . GLN   B 33  ? 0.5670 0.5288 0.4718 0.0925  0.0094  -0.0432 42  GLN   B CA  
541  C C   . GLN   B 33  ? 0.5771 0.5453 0.4915 0.0797  0.0072  -0.0467 42  GLN   B C   
542  O O   . GLN   B 33  ? 0.5737 0.5459 0.4949 0.0724  0.0111  -0.0448 42  GLN   B O   
543  C CB  . GLN   B 33  ? 0.5797 0.5301 0.4723 0.0955  0.0068  -0.0417 42  GLN   B CB  
544  C CG  . GLN   B 33  ? 0.6269 0.5681 0.5102 0.0952  -0.0026 -0.0465 42  GLN   B CG  
545  C CD  . GLN   B 33  ? 0.6882 0.6162 0.5565 0.1019  -0.0061 -0.0455 42  GLN   B CD  
546  O OE1 . GLN   B 33  ? 0.7764 0.6961 0.6390 0.0965  -0.0119 -0.0475 42  GLN   B OE1 
547  N NE2 . GLN   B 33  ? 0.6650 0.5912 0.5264 0.1136  -0.0022 -0.0419 42  GLN   B NE2 
548  N N   . GLU   B 34  ? 0.6194 0.5891 0.5343 0.0771  0.0010  -0.0515 43  GLU   B N   
549  C CA  . GLU   B 34  ? 0.6345 0.6120 0.5587 0.0648  -0.0015 -0.0548 43  GLU   B CA  
550  C C   . GLU   B 34  ? 0.6211 0.6112 0.5587 0.0594  0.0053  -0.0536 43  GLU   B C   
551  O O   . GLU   B 34  ? 0.6164 0.6108 0.5599 0.0493  0.0057  -0.0539 43  GLU   B O   
552  C CB  . GLU   B 34  ? 0.6905 0.6594 0.6087 0.0577  -0.0058 -0.0547 43  GLU   B CB  
553  C CG  . GLU   B 34  ? 0.7220 0.6781 0.6269 0.0614  -0.0144 -0.0570 43  GLU   B CG  
554  C CD  . GLU   B 34  ? 0.7560 0.6993 0.6510 0.0578  -0.0186 -0.0561 43  GLU   B CD  
555  O OE1 . GLU   B 34  ? 0.8001 0.7448 0.6990 0.0461  -0.0214 -0.0571 43  GLU   B OE1 
556  O OE2 . GLU   B 34  ? 0.8006 0.7326 0.6837 0.0669  -0.0192 -0.0543 43  GLU   B OE2 
557  N N   . GLY   B 35  ? 0.5988 0.5940 0.5405 0.0658  0.0103  -0.0521 44  GLY   B N   
558  C CA  . GLY   B 35  ? 0.5371 0.5434 0.4907 0.0614  0.0156  -0.0518 44  GLY   B CA  
559  C C   . GLY   B 35  ? 0.5367 0.5415 0.4924 0.0588  0.0215  -0.0471 44  GLY   B C   
560  O O   . GLY   B 35  ? 0.5148 0.5272 0.4794 0.0555  0.0259  -0.0465 44  GLY   B O   
561  N N   . VAL   B 36  ? 0.4842 0.4791 0.4314 0.0610  0.0216  -0.0439 45  VAL   B N   
562  C CA  . VAL   B 36  ? 0.4729 0.4656 0.4208 0.0592  0.0267  -0.0391 45  VAL   B CA  
563  C C   . VAL   B 36  ? 0.4505 0.4387 0.3926 0.0696  0.0303  -0.0345 45  VAL   B C   
564  O O   . VAL   B 36  ? 0.4584 0.4396 0.3903 0.0774  0.0272  -0.0346 45  VAL   B O   
565  C CB  . VAL   B 36  ? 0.4991 0.4855 0.4422 0.0529  0.0237  -0.0392 45  VAL   B CB  
566  C CG1 . VAL   B 36  ? 0.5021 0.4851 0.4439 0.0528  0.0284  -0.0343 45  VAL   B CG1 
567  C CG2 . VAL   B 36  ? 0.5209 0.5141 0.4716 0.0414  0.0215  -0.0428 45  VAL   B CG2 
568  N N   . PHE   B 37  ? 0.4301 0.4219 0.3778 0.0694  0.0364  -0.0303 46  PHE   B N   
569  C CA  . PHE   B 37  ? 0.4407 0.4298 0.3842 0.0776  0.0407  -0.0245 46  PHE   B CA  
570  C C   . PHE   B 37  ? 0.4273 0.4130 0.3681 0.0757  0.0429  -0.0206 46  PHE   B C   
571  O O   . PHE   B 37  ? 0.4211 0.4097 0.3685 0.0674  0.0445  -0.0205 46  PHE   B O   
572  C CB  . PHE   B 37  ? 0.4334 0.4281 0.3847 0.0780  0.0452  -0.0222 46  PHE   B CB  
573  C CG  . PHE   B 37  ? 0.4441 0.4365 0.3908 0.0864  0.0490  -0.0160 46  PHE   B CG  
574  C CD1 . PHE   B 37  ? 0.4597 0.4485 0.3979 0.0957  0.0472  -0.0159 46  PHE   B CD1 
575  C CD2 . PHE   B 37  ? 0.4533 0.4475 0.4037 0.0847  0.0542  -0.0101 46  PHE   B CD2 
576  C CE1 . PHE   B 37  ? 0.4780 0.4657 0.4118 0.1034  0.0509  -0.0098 46  PHE   B CE1 
577  C CE2 . PHE   B 37  ? 0.4463 0.4395 0.3926 0.0919  0.0576  -0.0038 46  PHE   B CE2 
578  C CZ  . PHE   B 37  ? 0.4646 0.4550 0.4028 0.1012  0.0562  -0.0036 46  PHE   B CZ  
579  N N   . HIS   B 38  ? 0.4446 0.4251 0.3760 0.0838  0.0433  -0.0174 47  HIS   B N   
580  C CA  . HIS   B 38  ? 0.4377 0.4146 0.3641 0.0844  0.0445  -0.0141 47  HIS   B CA  
581  C C   . HIS   B 38  ? 0.4272 0.4070 0.3529 0.0912  0.0503  -0.0072 47  HIS   B C   
582  O O   . HIS   B 38  ? 0.4251 0.4041 0.3450 0.1002  0.0505  -0.0056 47  HIS   B O   
583  C CB  . HIS   B 38  ? 0.4501 0.4182 0.3640 0.0895  0.0388  -0.0168 47  HIS   B CB  
584  C CG  . HIS   B 38  ? 0.4780 0.4424 0.3910 0.0834  0.0322  -0.0231 47  HIS   B CG  
585  N ND1 . HIS   B 38  ? 0.5084 0.4746 0.4232 0.0835  0.0290  -0.0271 47  HIS   B ND1 
586  C CD2 . HIS   B 38  ? 0.4837 0.4428 0.3937 0.0769  0.0279  -0.0257 47  HIS   B CD2 
587  C CE1 . HIS   B 38  ? 0.5107 0.4741 0.4249 0.0765  0.0232  -0.0319 47  HIS   B CE1 
588  N NE2 . HIS   B 38  ? 0.5082 0.4669 0.4195 0.0720  0.0225  -0.0309 47  HIS   B NE2 
589  N N   . THR   B 39  ? 0.4441 0.4276 0.3753 0.0871  0.0547  -0.0028 48  THR   B N   
590  C CA  . THR   B 39  ? 0.4487 0.4358 0.3788 0.0933  0.0599  0.0043  48  THR   B CA  
591  C C   . THR   B 39  ? 0.4698 0.4578 0.4002 0.0907  0.0620  0.0073  48  THR   B C   
592  O O   . THR   B 39  ? 0.4578 0.4418 0.3872 0.0851  0.0588  0.0035  48  THR   B O   
593  C CB  . THR   B 39  ? 0.4712 0.4636 0.4093 0.0923  0.0637  0.0075  48  THR   B CB  
594  O OG1 . THR   B 39  ? 0.4665 0.4626 0.4029 0.0981  0.0683  0.0150  48  THR   B OG1 
595  C CG2 . THR   B 39  ? 0.4787 0.4745 0.4283 0.0819  0.0653  0.0069  48  THR   B CG2 
596  N N   . MET   B 40  ? 0.4826 0.4759 0.4139 0.0944  0.0670  0.0143  49  MET   B N   
597  C CA  . MET   B 40  ? 0.5099 0.5062 0.4431 0.0920  0.0696  0.0180  49  MET   B CA  
598  C C   . MET   B 40  ? 0.4921 0.4935 0.4380 0.0823  0.0730  0.0204  49  MET   B C   
599  O O   . MET   B 40  ? 0.4865 0.4910 0.4384 0.0811  0.0751  0.0226  49  MET   B O   
600  C CB  . MET   B 40  ? 0.5031 0.5039 0.4304 0.1015  0.0730  0.0245  49  MET   B CB  
601  C CG  . MET   B 40  ? 0.5412 0.5369 0.4553 0.1125  0.0697  0.0222  49  MET   B CG  
602  S SD  . MET   B 40  ? 0.6129 0.6119 0.5168 0.1235  0.0716  0.0269  49  MET   B SD  
603  C CE  . MET   B 40  ? 0.5967 0.5873 0.4961 0.1192  0.0665  0.0212  49  MET   B CE  
604  N N   A TRP   B 41  ? 0.5000 0.5014 0.4491 0.0759  0.0730  0.0199  50  TRP   B N   
605  N N   B TRP   B 41  ? 0.4835 0.4849 0.4327 0.0759  0.0730  0.0199  50  TRP   B N   
606  N N   C TRP   B 41  ? 0.4981 0.4995 0.4473 0.0759  0.0730  0.0199  50  TRP   B N   
607  N N   D TRP   B 41  ? 0.4813 0.4827 0.4305 0.0759  0.0730  0.0199  50  TRP   B N   
608  C CA  A TRP   B 41  ? 0.5033 0.5084 0.4637 0.0664  0.0754  0.0214  50  TRP   B CA  
609  C CA  B TRP   B 41  ? 0.4755 0.4806 0.4360 0.0664  0.0754  0.0213  50  TRP   B CA  
610  C CA  C TRP   B 41  ? 0.5036 0.5087 0.4640 0.0664  0.0754  0.0214  50  TRP   B CA  
611  C CA  D TRP   B 41  ? 0.4748 0.4799 0.4353 0.0664  0.0754  0.0213  50  TRP   B CA  
612  C C   A TRP   B 41  ? 0.4963 0.5083 0.4624 0.0676  0.0803  0.0290  50  TRP   B C   
613  C C   B TRP   B 41  ? 0.4797 0.4918 0.4458 0.0676  0.0803  0.0290  50  TRP   B C   
614  C C   C TRP   B 41  ? 0.4975 0.5096 0.4636 0.0676  0.0803  0.0290  50  TRP   B C   
615  C C   D TRP   B 41  ? 0.4807 0.4927 0.4467 0.0676  0.0803  0.0290  50  TRP   B C   
616  O O   A TRP   B 41  ? 0.4854 0.4989 0.4597 0.0618  0.0815  0.0298  50  TRP   B O   
617  O O   B TRP   B 41  ? 0.4705 0.4841 0.4449 0.0619  0.0815  0.0299  50  TRP   B O   
618  O O   C TRP   B 41  ? 0.4846 0.4982 0.4589 0.0618  0.0815  0.0299  50  TRP   B O   
619  O O   D TRP   B 41  ? 0.4694 0.4831 0.4438 0.0619  0.0816  0.0299  50  TRP   B O   
620  C CB  A TRP   B 41  ? 0.5179 0.5220 0.4791 0.0610  0.0749  0.0205  50  TRP   B CB  
621  C CB  B TRP   B 41  ? 0.4689 0.4726 0.4305 0.0604  0.0746  0.0199  50  TRP   B CB  
622  C CB  C TRP   B 41  ? 0.5188 0.5229 0.4800 0.0610  0.0749  0.0205  50  TRP   B CB  
623  C CB  D TRP   B 41  ? 0.4685 0.4722 0.4300 0.0604  0.0746  0.0199  50  TRP   B CB  
624  C CG  A TRP   B 41  ? 0.5260 0.5324 0.4977 0.0510  0.0762  0.0204  50  TRP   B CG  
625  C CG  B TRP   B 41  ? 0.4554 0.4624 0.4278 0.0512  0.0767  0.0210  50  TRP   B CG  
626  C CG  C TRP   B 41  ? 0.5276 0.5340 0.4993 0.0510  0.0762  0.0204  50  TRP   B CG  
627  C CG  D TRP   B 41  ? 0.4539 0.4610 0.4264 0.0512  0.0767  0.0210  50  TRP   B CG  
628  C CD1 A TRP   B 41  ? 0.5283 0.5321 0.5037 0.0435  0.0738  0.0147  50  TRP   B CD1 
629  C CD1 B TRP   B 41  ? 0.4444 0.4572 0.4233 0.0496  0.0807  0.0273  50  TRP   B CD1 
630  C CD1 C TRP   B 41  ? 0.5293 0.5330 0.5046 0.0436  0.0738  0.0148  50  TRP   B CD1 
631  C CD1 D TRP   B 41  ? 0.4395 0.4523 0.4184 0.0496  0.0807  0.0273  50  TRP   B CD1 
632  C CD2 A TRP   B 41  ? 0.5284 0.5405 0.5081 0.0476  0.0802  0.0261  50  TRP   B CD2 
633  C CD2 B TRP   B 41  ? 0.4495 0.4548 0.4276 0.0427  0.0748  0.0159  50  TRP   B CD2 
634  C CD2 C TRP   B 41  ? 0.5279 0.5400 0.5076 0.0476  0.0802  0.0261  50  TRP   B CD2 
635  C CD2 D TRP   B 41  ? 0.4483 0.4535 0.4264 0.0427  0.0748  0.0159  50  TRP   B CD2 
636  N NE1 A TRP   B 41  ? 0.5314 0.5383 0.5158 0.0364  0.0759  0.0163  50  TRP   B NE1 
637  N NE1 B TRP   B 41  ? 0.4384 0.4518 0.4259 0.0409  0.0810  0.0262  50  TRP   B NE1 
638  N NE1 C TRP   B 41  ? 0.5347 0.5416 0.5191 0.0364  0.0759  0.0163  50  TRP   B NE1 
639  N NE1 D TRP   B 41  ? 0.4345 0.4479 0.4219 0.0410  0.0810  0.0262  50  TRP   B NE1 
640  C CE2 A TRP   B 41  ? 0.5361 0.5474 0.5233 0.0385  0.0796  0.0231  50  TRP   B CE2 
641  C CE2 B TRP   B 41  ? 0.4420 0.4512 0.4291 0.0369  0.0777  0.0192  50  TRP   B CE2 
642  C CE2 C TRP   B 41  ? 0.5409 0.5523 0.5282 0.0385  0.0796  0.0232  50  TRP   B CE2 
643  C CE2 D TRP   B 41  ? 0.4407 0.4499 0.4278 0.0369  0.0777  0.0192  50  TRP   B CE2 
644  C CE3 A TRP   B 41  ? 0.5487 0.5669 0.5300 0.0510  0.0840  0.0336  50  TRP   B CE3 
645  C CE3 B TRP   B 41  ? 0.4564 0.4578 0.4329 0.0392  0.0709  0.0092  50  TRP   B CE3 
646  C CE3 C TRP   B 41  ? 0.5590 0.5772 0.5403 0.0511  0.0840  0.0337  50  TRP   B CE3 
647  C CE3 D TRP   B 41  ? 0.4591 0.4605 0.4356 0.0392  0.0709  0.0092  50  TRP   B CE3 
648  C CZ2 A TRP   B 41  ? 0.5411 0.5561 0.5366 0.0331  0.0821  0.0271  50  TRP   B CZ2 
649  C CZ2 B TRP   B 41  ? 0.4396 0.4485 0.4332 0.0287  0.0769  0.0156  50  TRP   B CZ2 
650  C CZ2 C TRP   B 41  ? 0.5489 0.5640 0.5445 0.0331  0.0821  0.0271  50  TRP   B CZ2 
651  C CZ2 D TRP   B 41  ? 0.4400 0.4490 0.4337 0.0287  0.0769  0.0156  50  TRP   B CZ2 
652  C CZ3 A TRP   B 41  ? 0.5427 0.5652 0.5330 0.0449  0.0865  0.0379  50  TRP   B CZ3 
653  C CZ3 B TRP   B 41  ? 0.4480 0.4508 0.4318 0.0307  0.0705  0.0060  50  TRP   B CZ3 
654  C CZ3 C TRP   B 41  ? 0.5499 0.5724 0.5402 0.0449  0.0865  0.0379  50  TRP   B CZ3 
655  C CZ3 D TRP   B 41  ? 0.4489 0.4516 0.4327 0.0307  0.0705  0.0060  50  TRP   B CZ3 
656  C CH2 A TRP   B 41  ? 0.5449 0.5651 0.5419 0.0361  0.0854  0.0345  50  TRP   B CH2 
657  C CH2 B TRP   B 41  ? 0.4412 0.4475 0.4331 0.0260  0.0735  0.0090  50  TRP   B CH2 
658  C CH2 C TRP   B 41  ? 0.5538 0.5740 0.5509 0.0361  0.0854  0.0345  50  TRP   B CH2 
659  C CH2 D TRP   B 41  ? 0.4420 0.4482 0.4339 0.0260  0.0735  0.0090  50  TRP   B CH2 
660  N N   . HIS   B 42  ? 0.4832 0.4993 0.4446 0.0748  0.0829  0.0346  51  HIS   B N   
661  C CA  . HIS   B 42  ? 0.5037 0.5278 0.4707 0.0750  0.0877  0.0432  51  HIS   B CA  
662  C C   . HIS   B 42  ? 0.5245 0.5486 0.4933 0.0766  0.0885  0.0451  51  HIS   B C   
663  O O   . HIS   B 42  ? 0.5426 0.5712 0.5176 0.0737  0.0915  0.0513  51  HIS   B O   
664  C CB  . HIS   B 42  ? 0.5056 0.5361 0.4678 0.0820  0.0904  0.0488  51  HIS   B CB  
665  C CG  . HIS   B 42  ? 0.5214 0.5526 0.4741 0.0929  0.0905  0.0501  51  HIS   B CG  
666  N ND1 . HIS   B 42  ? 0.5277 0.5542 0.4693 0.1005  0.0874  0.0458  51  HIS   B ND1 
667  C CD2 . HIS   B 42  ? 0.5445 0.5799 0.4964 0.0979  0.0932  0.0554  51  HIS   B CD2 
668  C CE1 . HIS   B 42  ? 0.5327 0.5610 0.4669 0.1102  0.0884  0.0482  51  HIS   B CE1 
669  N NE2 . HIS   B 42  ? 0.5428 0.5767 0.4833 0.1086  0.0920  0.0542  51  HIS   B NE2 
670  N N   . VAL   B 43  ? 0.4882 0.5068 0.4519 0.0802  0.0854  0.0398  52  VAL   B N   
671  C CA  . VAL   B 43  ? 0.5191 0.5366 0.4831 0.0825  0.0855  0.0407  52  VAL   B CA  
672  C C   . VAL   B 43  ? 0.5087 0.5237 0.4813 0.0739  0.0843  0.0376  52  VAL   B C   
673  O O   . VAL   B 43  ? 0.5141 0.5301 0.4907 0.0726  0.0860  0.0420  52  VAL   B O   
674  C CB  . VAL   B 43  ? 0.5336 0.5463 0.4882 0.0903  0.0822  0.0356  52  VAL   B CB  
675  C CG1 . VAL   B 43  ? 0.5614 0.5713 0.5165 0.0917  0.0810  0.0340  52  VAL   B CG1 
676  C CG2 . VAL   B 43  ? 0.5451 0.5599 0.4901 0.1002  0.0835  0.0390  52  VAL   B CG2 
677  N N   . THR   B 44  ? 0.4996 0.5113 0.4743 0.0686  0.0812  0.0303  53  THR   B N   
678  C CA  . THR   B 44  ? 0.5049 0.5149 0.4868 0.0617  0.0796  0.0263  53  THR   B CA  
679  C C   . THR   B 44  ? 0.5274 0.5391 0.5171 0.0530  0.0809  0.0276  53  THR   B C   
680  O O   . THR   B 44  ? 0.5372 0.5482 0.5331 0.0482  0.0806  0.0267  53  THR   B O   
681  C CB  . THR   B 44  ? 0.4957 0.5026 0.4754 0.0615  0.0755  0.0177  53  THR   B CB  
682  O OG1 . THR   B 44  ? 0.4936 0.4997 0.4717 0.0583  0.0739  0.0143  53  THR   B OG1 
683  C CG2 . THR   B 44  ? 0.4969 0.5018 0.4691 0.0702  0.0739  0.0166  53  THR   B CG2 
684  N N   . LYS   B 45  ? 0.5381 0.5519 0.5270 0.0518  0.0821  0.0295  54  LYS   B N   
685  C CA  . LYS   B 45  ? 0.5821 0.5969 0.5769 0.0439  0.0826  0.0293  54  LYS   B CA  
686  C C   . LYS   B 45  ? 0.5539 0.5659 0.5514 0.0381  0.0796  0.0215  54  LYS   B C   
687  O O   . LYS   B 45  ? 0.5787 0.5912 0.5826 0.0312  0.0799  0.0210  54  LYS   B O   
688  C CB  . LYS   B 45  ? 0.6428 0.6603 0.6449 0.0397  0.0852  0.0355  54  LYS   B CB  
689  C CG  . LYS   B 45  ? 0.7192 0.7409 0.7202 0.0443  0.0883  0.0441  54  LYS   B CG  
690  C CD  . LYS   B 45  ? 0.7887 0.8156 0.7873 0.0469  0.0905  0.0483  54  LYS   B CD  
691  C CE  . LYS   B 45  ? 0.8581 0.8912 0.8564 0.0512  0.0940  0.0574  54  LYS   B CE  
692  N NZ  . LYS   B 45  ? 0.8803 0.9180 0.8712 0.0596  0.0954  0.0595  54  LYS   B NZ  
693  N N   . GLY   B 46  ? 0.5328 0.5425 0.5257 0.0407  0.0767  0.0158  55  GLY   B N   
694  C CA  . GLY   B 46  ? 0.5297 0.5387 0.5252 0.0353  0.0738  0.0087  55  GLY   B CA  
695  C C   . GLY   B 46  ? 0.5318 0.5419 0.5327 0.0337  0.0734  0.0064  55  GLY   B C   
696  O O   . GLY   B 46  ? 0.5401 0.5515 0.5438 0.0294  0.0715  0.0010  55  GLY   B O   
697  N N   . ALA   B 47  ? 0.5683 0.5781 0.5698 0.0375  0.0747  0.0104  56  ALA   B N   
698  C CA  . ALA   B 47  ? 0.5613 0.5706 0.5663 0.0373  0.0737  0.0081  56  ALA   B CA  
699  C C   . ALA   B 47  ? 0.5618 0.5715 0.5637 0.0413  0.0707  0.0021  56  ALA   B C   
700  O O   . ALA   B 47  ? 0.5608 0.5696 0.5567 0.0462  0.0698  0.0016  56  ALA   B O   
701  C CB  . ALA   B 47  ? 0.5457 0.5532 0.5509 0.0404  0.0756  0.0149  56  ALA   B CB  
702  N N   . ALA   B 48  ? 0.5528 0.5638 0.5583 0.0399  0.0690  -0.0024 57  ALA   B N   
703  C CA  . ALA   B 48  ? 0.5429 0.5553 0.5463 0.0441  0.0661  -0.0079 57  ALA   B CA  
704  C C   . ALA   B 48  ? 0.5472 0.5561 0.5459 0.0519  0.0662  -0.0045 57  ALA   B C   
705  O O   . ALA   B 48  ? 0.5518 0.5575 0.5498 0.0533  0.0686  0.0020  57  ALA   B O   
706  C CB  . ALA   B 48  ? 0.5665 0.5825 0.5752 0.0411  0.0644  -0.0135 57  ALA   B CB  
707  N N   . LEU   B 49  ? 0.5103 0.5199 0.5054 0.0568  0.0637  -0.0087 58  LEU   B N   
708  C CA  . LEU   B 49  ? 0.5423 0.5486 0.5312 0.0651  0.0632  -0.0065 58  LEU   B CA  
709  C C   . LEU   B 49  ? 0.5670 0.5745 0.5566 0.0682  0.0602  -0.0121 58  LEU   B C   
710  O O   . LEU   B 49  ? 0.6143 0.6270 0.6077 0.0648  0.0580  -0.0186 58  LEU   B O   
711  C CB  . LEU   B 49  ? 0.5228 0.5283 0.5051 0.0689  0.0624  -0.0067 58  LEU   B CB  
712  C CG  . LEU   B 49  ? 0.5041 0.5086 0.4843 0.0674  0.0650  -0.0016 58  LEU   B CG  
713  C CD1 . LEU   B 49  ? 0.4816 0.4843 0.4541 0.0719  0.0630  -0.0032 58  LEU   B CD1 
714  C CD2 . LEU   B 49  ? 0.5105 0.5134 0.4899 0.0700  0.0687  0.0065  58  LEU   B CD2 
715  N N   . ARG   B 50  ? 0.5957 0.5992 0.5817 0.0745  0.0600  -0.0095 59  ARG   B N   
716  C CA  . ARG   B 50  ? 0.6400 0.6440 0.6248 0.0795  0.0568  -0.0147 59  ARG   B CA  
717  C C   . ARG   B 50  ? 0.6505 0.6533 0.6282 0.0866  0.0552  -0.0154 59  ARG   B C   
718  O O   . ARG   B 50  ? 0.6251 0.6243 0.5974 0.0899  0.0572  -0.0096 59  ARG   B O   
719  C CB  . ARG   B 50  ? 0.7088 0.7075 0.6934 0.0814  0.0572  -0.0112 59  ARG   B CB  
720  C CG  . ARG   B 50  ? 0.8119 0.8099 0.7947 0.0873  0.0538  -0.0160 59  ARG   B CG  
721  C CD  . ARG   B 50  ? 0.8588 0.8502 0.8415 0.0878  0.0535  -0.0130 59  ARG   B CD  
722  N NE  . ARG   B 50  ? 0.8824 0.8678 0.8631 0.0860  0.0566  -0.0037 59  ARG   B NE  
723  C CZ  . ARG   B 50  ? 0.9422 0.9218 0.9166 0.0910  0.0573  0.0022  59  ARG   B CZ  
724  N NH1 . ARG   B 50  ? 0.9483 0.9262 0.9170 0.0987  0.0551  -0.0001 59  ARG   B NH1 
725  N NH2 . ARG   B 50  ? 0.9733 0.9496 0.9474 0.0883  0.0603  0.0109  59  ARG   B NH2 
726  N N   . SER   B 51  ? 0.6459 0.6524 0.6236 0.0888  0.0515  -0.0223 60  SER   B N   
727  C CA  . SER   B 51  ? 0.7182 0.7231 0.6892 0.0968  0.0488  -0.0242 60  SER   B CA  
728  C C   . SER   B 51  ? 0.7480 0.7541 0.7197 0.1012  0.0459  -0.0288 60  SER   B C   
729  O O   . SER   B 51  ? 0.7485 0.7617 0.7244 0.0995  0.0430  -0.0357 60  SER   B O   
730  C CB  . SER   B 51  ? 0.6831 0.6915 0.6531 0.0952  0.0462  -0.0286 60  SER   B CB  
731  O OG  . SER   B 51  ? 0.6586 0.6653 0.6222 0.1027  0.0430  -0.0310 60  SER   B OG  
732  N N   . GLY   B 52  ? 0.8091 0.8090 0.7766 0.1069  0.0465  -0.0251 61  GLY   B N   
733  C CA  . GLY   B 52  ? 0.8248 0.8245 0.7926 0.1111  0.0436  -0.0292 61  GLY   B CA  
734  C C   . GLY   B 52  ? 0.8497 0.8531 0.8249 0.1055  0.0436  -0.0320 61  GLY   B C   
735  O O   . GLY   B 52  ? 0.8880 0.8872 0.8648 0.1014  0.0463  -0.0269 61  GLY   B O   
736  N N   . GLU   B 53  ? 0.8786 0.8904 0.8584 0.1050  0.0407  -0.0397 62  GLU   B N   
737  C CA  . GLU   B 53  ? 0.9467 0.9639 0.9336 0.0999  0.0407  -0.0432 62  GLU   B CA  
738  C C   . GLU   B 53  ? 0.8890 0.9144 0.8821 0.0912  0.0422  -0.0449 62  GLU   B C   
739  O O   . GLU   B 53  ? 0.8545 0.8832 0.8529 0.0862  0.0432  -0.0461 62  GLU   B O   
740  C CB  . GLU   B 53  ? 1.0243 1.0473 1.0124 0.1049  0.0369  -0.0506 62  GLU   B CB  
741  C CG  . GLU   B 53  ? 1.1312 1.1462 1.1161 0.1097  0.0358  -0.0496 62  GLU   B CG  
742  C CD  . GLU   B 53  ? 1.2904 1.3120 1.2767 0.1150  0.0318  -0.0575 62  GLU   B CD  
743  O OE1 . GLU   B 53  ? 1.2966 1.3303 1.2867 0.1152  0.0301  -0.0635 62  GLU   B OE1 
744  O OE2 . GLU   B 53  ? 1.4402 1.4549 1.4235 0.1189  0.0302  -0.0576 62  GLU   B OE2 
745  N N   . GLY   B 54  ? 0.8364 0.8641 0.8283 0.0897  0.0420  -0.0450 63  GLY   B N   
746  C CA  . GLY   B 54  ? 0.8225 0.8562 0.8188 0.0814  0.0429  -0.0460 63  GLY   B CA  
747  C C   . GLY   B 54  ? 0.8157 0.8442 0.8127 0.0760  0.0468  -0.0399 63  GLY   B C   
748  O O   . GLY   B 54  ? 0.7825 0.8024 0.7752 0.0792  0.0488  -0.0339 63  GLY   B O   
749  N N   . ARG   B 55  ? 0.7464 0.7802 0.7486 0.0680  0.0478  -0.0413 64  ARG   B N   
750  C CA  . ARG   B 55  ? 0.7221 0.7522 0.7254 0.0620  0.0511  -0.0362 64  ARG   B CA  
751  C C   . ARG   B 55  ? 0.6911 0.7221 0.6926 0.0580  0.0507  -0.0362 64  ARG   B C   
752  O O   . ARG   B 55  ? 0.7069 0.7445 0.7101 0.0556  0.0479  -0.0413 64  ARG   B O   
753  C CB  . ARG   B 55  ? 0.7550 0.7893 0.7649 0.0563  0.0523  -0.0379 64  ARG   B CB  
754  C CG  . ARG   B 55  ? 0.7881 0.8175 0.7991 0.0513  0.0556  -0.0323 64  ARG   B CG  
755  C CD  . ARG   B 55  ? 0.8457 0.8805 0.8630 0.0450  0.0561  -0.0352 64  ARG   B CD  
756  N NE  . ARG   B 55  ? 0.8567 0.8883 0.8755 0.0389  0.0588  -0.0310 64  ARG   B NE  
757  C CZ  . ARG   B 55  ? 0.8710 0.8980 0.8915 0.0375  0.0603  -0.0276 64  ARG   B CZ  
758  N NH1 . ARG   B 55  ? 0.8475 0.8713 0.8676 0.0416  0.0591  -0.0280 64  ARG   B NH1 
759  N NH2 . ARG   B 55  ? 0.8620 0.8872 0.8841 0.0317  0.0625  -0.0241 64  ARG   B NH2 
760  N N   . LEU   B 56  ? 0.6016 0.6262 0.5994 0.0577  0.0530  -0.0305 65  LEU   B N   
761  C CA  . LEU   B 56  ? 0.6023 0.6259 0.5974 0.0539  0.0525  -0.0301 65  LEU   B CA  
762  C C   . LEU   B 56  ? 0.5498 0.5733 0.5488 0.0469  0.0554  -0.0273 65  LEU   B C   
763  O O   . LEU   B 56  ? 0.5337 0.5531 0.5326 0.0482  0.0585  -0.0219 65  LEU   B O   
764  C CB  . LEU   B 56  ? 0.5870 0.6035 0.5736 0.0605  0.0526  -0.0260 65  LEU   B CB  
765  C CG  . LEU   B 56  ? 0.6358 0.6507 0.6170 0.0687  0.0499  -0.0278 65  LEU   B CG  
766  C CD1 . LEU   B 56  ? 0.6573 0.6664 0.6296 0.0732  0.0488  -0.0256 65  LEU   B CD1 
767  C CD2 . LEU   B 56  ? 0.6556 0.6769 0.6398 0.0675  0.0458  -0.0349 65  LEU   B CD2 
768  N N   . ASP   B 57  ? 0.5161 0.5441 0.5185 0.0395  0.0544  -0.0305 66  ASP   B N   
769  C CA  . ASP   B 57  ? 0.5100 0.5374 0.5152 0.0327  0.0569  -0.0280 66  ASP   B CA  
770  C C   . ASP   B 57  ? 0.4764 0.4989 0.4761 0.0310  0.0564  -0.0259 66  ASP   B C   
771  O O   . ASP   B 57  ? 0.4583 0.4802 0.4539 0.0309  0.0530  -0.0287 66  ASP   B O   
772  C CB  . ASP   B 57  ? 0.5762 0.6116 0.5881 0.0258  0.0563  -0.0327 66  ASP   B CB  
773  C CG  . ASP   B 57  ? 0.6443 0.6839 0.6610 0.0281  0.0568  -0.0348 66  ASP   B CG  
774  O OD1 . ASP   B 57  ? 0.7284 0.7634 0.7453 0.0307  0.0588  -0.0312 66  ASP   B OD1 
775  O OD2 . ASP   B 57  ? 0.6788 0.7262 0.6985 0.0277  0.0548  -0.0400 66  ASP   B OD2 
776  N N   . PRO   B 58  ? 0.4817 0.5006 0.4810 0.0292  0.0592  -0.0212 67  PRO   B N   
777  C CA  . PRO   B 58  ? 0.4721 0.4863 0.4659 0.0277  0.0585  -0.0196 67  PRO   B CA  
778  C C   . PRO   B 58  ? 0.4708 0.4871 0.4652 0.0201  0.0555  -0.0241 67  PRO   B C   
779  O O   . PRO   B 58  ? 0.4972 0.5199 0.4983 0.0142  0.0558  -0.0270 67  PRO   B O   
780  C CB  . PRO   B 58  ? 0.4967 0.5092 0.4925 0.0260  0.0623  -0.0143 67  PRO   B CB  
781  C CG  . PRO   B 58  ? 0.4873 0.5040 0.4910 0.0232  0.0641  -0.0147 67  PRO   B CG  
782  C CD  . PRO   B 58  ? 0.4769 0.4957 0.4809 0.0282  0.0627  -0.0174 67  PRO   B CD  
783  N N   . TYR   B 59  ? 0.4274 0.4386 0.4146 0.0203  0.0523  -0.0247 68  TYR   B N   
784  C CA  . TYR   B 59  ? 0.4242 0.4358 0.4106 0.0126  0.0488  -0.0283 68  TYR   B CA  
785  C C   . TYR   B 59  ? 0.4003 0.4046 0.3811 0.0102  0.0487  -0.0256 68  TYR   B C   
786  O O   . TYR   B 59  ? 0.4180 0.4231 0.4004 0.0022  0.0480  -0.0268 68  TYR   B O   
787  C CB  . TYR   B 59  ? 0.4460 0.4572 0.4282 0.0146  0.0439  -0.0320 68  TYR   B CB  
788  C CG  . TYR   B 59  ? 0.4401 0.4520 0.4214 0.0061  0.0395  -0.0354 68  TYR   B CG  
789  C CD1 . TYR   B 59  ? 0.4566 0.4592 0.4295 0.0040  0.0363  -0.0345 68  TYR   B CD1 
790  C CD2 . TYR   B 59  ? 0.4490 0.4710 0.4372 0.0007  0.0382  -0.0393 68  TYR   B CD2 
791  C CE1 . TYR   B 59  ? 0.4718 0.4740 0.4431 -0.0043 0.0316  -0.0372 68  TYR   B CE1 
792  C CE2 . TYR   B 59  ? 0.4704 0.4940 0.4579 -0.0076 0.0340  -0.0418 68  TYR   B CE2 
793  C CZ  . TYR   B 59  ? 0.4766 0.4898 0.4556 -0.0108 0.0306  -0.0406 68  TYR   B CZ  
794  O OH  . TYR   B 59  ? 0.5224 0.5358 0.4998 -0.0198 0.0259  -0.0425 68  TYR   B OH  
795  N N   . TRP   B 60  ? 0.4029 0.4006 0.3767 0.0173  0.0491  -0.0223 69  TRP   B N   
796  C CA  . TRP   B 60  ? 0.3973 0.3871 0.3636 0.0171  0.0481  -0.0201 69  TRP   B CA  
797  C C   . TRP   B 60  ? 0.3967 0.3852 0.3610 0.0248  0.0519  -0.0148 69  TRP   B C   
798  O O   . TRP   B 60  ? 0.4105 0.4000 0.3735 0.0326  0.0530  -0.0134 69  TRP   B O   
799  C CB  . TRP   B 60  ? 0.4003 0.3822 0.3566 0.0174  0.0420  -0.0228 69  TRP   B CB  
800  C CG  . TRP   B 60  ? 0.4015 0.3746 0.3490 0.0196  0.0409  -0.0204 69  TRP   B CG  
801  C CD1 . TRP   B 60  ? 0.4070 0.3766 0.3533 0.0129  0.0403  -0.0201 69  TRP   B CD1 
802  C CD2 . TRP   B 60  ? 0.4266 0.3939 0.3651 0.0299  0.0408  -0.0178 69  TRP   B CD2 
803  N NE1 . TRP   B 60  ? 0.4203 0.3823 0.3575 0.0189  0.0397  -0.0176 69  TRP   B NE1 
804  C CE2 . TRP   B 60  ? 0.4100 0.3710 0.3424 0.0294  0.0401  -0.0161 69  TRP   B CE2 
805  C CE3 . TRP   B 60  ? 0.4377 0.4053 0.3726 0.0399  0.0416  -0.0165 69  TRP   B CE3 
806  C CZ2 . TRP   B 60  ? 0.4296 0.3852 0.3524 0.0390  0.0399  -0.0136 69  TRP   B CZ2 
807  C CZ3 . TRP   B 60  ? 0.4545 0.4168 0.3799 0.0491  0.0415  -0.0137 69  TRP   B CZ3 
808  C CH2 . TRP   B 60  ? 0.4527 0.4095 0.3722 0.0488  0.0407  -0.0124 69  TRP   B CH2 
809  N N   . GLY   B 61  ? 0.4157 0.4026 0.3797 0.0231  0.0540  -0.0118 70  GLY   B N   
810  C CA  . GLY   B 61  ? 0.4280 0.4144 0.3890 0.0309  0.0572  -0.0065 70  GLY   B CA  
811  C C   . GLY   B 61  ? 0.4242 0.4072 0.3818 0.0296  0.0576  -0.0042 70  GLY   B C   
812  O O   . GLY   B 61  ? 0.4289 0.4114 0.3896 0.0212  0.0568  -0.0061 70  GLY   B O   
813  N N   . ASP   B 62  ? 0.4505 0.4333 0.4036 0.0374  0.0596  0.0000  71  ASP   B N   
814  C CA  . ASP   B 62  ? 0.4589 0.4391 0.4075 0.0384  0.0600  0.0026  71  ASP   B CA  
815  C C   . ASP   B 62  ? 0.4561 0.4417 0.4047 0.0467  0.0642  0.0085  71  ASP   B C   
816  O O   . ASP   B 62  ? 0.4870 0.4712 0.4284 0.0555  0.0633  0.0091  71  ASP   B O   
817  C CB  . ASP   B 62  ? 0.4932 0.4633 0.4295 0.0406  0.0542  -0.0008 71  ASP   B CB  
818  C CG  . ASP   B 62  ? 0.5488 0.5148 0.4800 0.0403  0.0535  0.0004  71  ASP   B CG  
819  O OD1 . ASP   B 62  ? 0.6305 0.6004 0.5613 0.0461  0.0567  0.0047  71  ASP   B OD1 
820  O OD2 . ASP   B 62  ? 0.6631 0.6221 0.5906 0.0342  0.0496  -0.0028 71  ASP   B OD2 
821  N N   . VAL   B 63  ? 0.4386 0.4305 0.3948 0.0438  0.0684  0.0129  72  VAL   B N   
822  C CA  . VAL   B 63  ? 0.4518 0.4510 0.4100 0.0497  0.0729  0.0197  72  VAL   B CA  
823  C C   . VAL   B 63  ? 0.4673 0.4642 0.4148 0.0582  0.0716  0.0208  72  VAL   B C   
824  O O   . VAL   B 63  ? 0.4644 0.4668 0.4094 0.0667  0.0742  0.0254  72  VAL   B O   
825  C CB  . VAL   B 63  ? 0.4636 0.4691 0.4326 0.0430  0.0766  0.0235  72  VAL   B CB  
826  C CG1 . VAL   B 63  ? 0.4853 0.4986 0.4557 0.0479  0.0804  0.0305  72  VAL   B CG1 
827  C CG2 . VAL   B 63  ? 0.4563 0.4648 0.4350 0.0373  0.0782  0.0235  72  VAL   B CG2 
828  N N   . LYS   B 64  ? 0.4819 0.4706 0.4220 0.0567  0.0674  0.0168  73  LYS   B N   
829  C CA  . LYS   B 64  ? 0.4948 0.4815 0.4241 0.0659  0.0661  0.0182  73  LYS   B CA  
830  C C   . LYS   B 64  ? 0.5104 0.4919 0.4283 0.0758  0.0630  0.0162  73  LYS   B C   
831  O O   . LYS   B 64  ? 0.5278 0.5132 0.4399 0.0860  0.0646  0.0196  73  LYS   B O   
832  C CB  . LYS   B 64  ? 0.4937 0.4723 0.4174 0.0622  0.0623  0.0151  73  LYS   B CB  
833  C CG  . LYS   B 64  ? 0.5201 0.4961 0.4316 0.0730  0.0606  0.0162  73  LYS   B CG  
834  C CD  . LYS   B 64  ? 0.5334 0.5029 0.4402 0.0699  0.0576  0.0143  73  LYS   B CD  
835  C CE  . LYS   B 64  ? 0.5738 0.5426 0.4693 0.0814  0.0564  0.0158  73  LYS   B CE  
836  N NZ  . LYS   B 64  ? 0.5927 0.5507 0.4805 0.0784  0.0516  0.0125  73  LYS   B NZ  
837  N N   . GLN   B 65  ? 0.5301 0.5031 0.4443 0.0728  0.0583  0.0107  74  GLN   B N   
838  C CA  . GLN   B 65  ? 0.5452 0.5128 0.4500 0.0807  0.0549  0.0081  74  GLN   B CA  
839  C C   . GLN   B 65  ? 0.5245 0.5010 0.4346 0.0854  0.0595  0.0119  74  GLN   B C   
840  O O   . GLN   B 65  ? 0.5016 0.4756 0.4028 0.0950  0.0578  0.0115  74  GLN   B O   
841  C CB  . GLN   B 65  ? 0.5583 0.5170 0.4612 0.0739  0.0492  0.0019  74  GLN   B CB  
842  C CG  . GLN   B 65  ? 0.5997 0.5473 0.4945 0.0698  0.0435  -0.0018 74  GLN   B CG  
843  C CD  . GLN   B 65  ? 0.6441 0.5838 0.5367 0.0631  0.0376  -0.0074 74  GLN   B CD  
844  O OE1 . GLN   B 65  ? 0.6968 0.6328 0.5843 0.0673  0.0343  -0.0098 74  GLN   B OE1 
845  N NE2 . GLN   B 65  ? 0.6936 0.6311 0.5904 0.0521  0.0361  -0.0093 74  GLN   B NE2 
846  N N   . ASP   B 66  ? 0.5119 0.4968 0.4352 0.0786  0.0642  0.0149  75  ASP   B N   
847  C CA  . ASP   B 66  ? 0.5080 0.5012 0.4389 0.0801  0.0687  0.0190  75  ASP   B CA  
848  C C   . ASP   B 66  ? 0.4871 0.4760 0.4159 0.0810  0.0658  0.0147  75  ASP   B C   
849  O O   . ASP   B 66  ? 0.4879 0.4801 0.4147 0.0885  0.0677  0.0175  75  ASP   B O   
850  C CB  . ASP   B 66  ? 0.5359 0.5363 0.4633 0.0903  0.0727  0.0254  75  ASP   B CB  
851  C CG  . ASP   B 66  ? 0.5347 0.5435 0.4697 0.0909  0.0774  0.0307  75  ASP   B CG  
852  O OD1 . ASP   B 66  ? 0.5345 0.5458 0.4803 0.0823  0.0792  0.0314  75  ASP   B OD1 
853  O OD2 . ASP   B 66  ? 0.5634 0.5757 0.4926 0.1006  0.0791  0.0342  75  ASP   B OD2 
854  N N   . LEU   B 67  ? 0.4560 0.4386 0.3853 0.0740  0.0614  0.0086  76  LEU   B N   
855  C CA  . LEU   B 67  ? 0.4333 0.4124 0.3613 0.0736  0.0577  0.0037  76  LEU   B CA  
856  C C   . LEU   B 67  ? 0.4497 0.4322 0.3891 0.0632  0.0584  0.0013  76  LEU   B C   
857  O O   . LEU   B 67  ? 0.4490 0.4326 0.3940 0.0551  0.0592  0.0012  76  LEU   B O   
858  C CB  . LEU   B 67  ? 0.4473 0.4160 0.3639 0.0752  0.0510  -0.0013 76  LEU   B CB  
859  C CG  . LEU   B 67  ? 0.4616 0.4256 0.3649 0.0873  0.0493  0.0000  76  LEU   B CG  
860  C CD1 . LEU   B 67  ? 0.4710 0.4228 0.3626 0.0877  0.0415  -0.0055 76  LEU   B CD1 
861  C CD2 . LEU   B 67  ? 0.4876 0.4551 0.3888 0.0964  0.0512  0.0019  76  LEU   B CD2 
862  N N   . VAL   B 68  ? 0.4420 0.4255 0.3835 0.0636  0.0571  -0.0013 77  VAL   B N   
863  C CA  . VAL   B 68  ? 0.4216 0.4088 0.3729 0.0550  0.0570  -0.0046 77  VAL   B CA  
864  C C   . VAL   B 68  ? 0.4090 0.3950 0.3582 0.0570  0.0532  -0.0093 77  VAL   B C   
865  O O   . VAL   B 68  ? 0.4167 0.4012 0.3601 0.0660  0.0530  -0.0080 77  VAL   B O   
866  C CB  . VAL   B 68  ? 0.4278 0.4217 0.3885 0.0536  0.0623  -0.0002 77  VAL   B CB  
867  C CG1 . VAL   B 68  ? 0.4369 0.4325 0.3954 0.0622  0.0645  0.0034  77  VAL   B CG1 
868  C CG2 . VAL   B 68  ? 0.4139 0.4115 0.3838 0.0456  0.0621  -0.0038 77  VAL   B CG2 
869  N N   . SER   B 69  ? 0.4112 0.3983 0.3647 0.0493  0.0503  -0.0143 78  SER   B N   
870  C CA  . SER   B 69  ? 0.4222 0.4097 0.3750 0.0498  0.0462  -0.0192 78  SER   B CA  
871  C C   . SER   B 69  ? 0.4177 0.4135 0.3816 0.0445  0.0481  -0.0210 78  SER   B C   
872  O O   . SER   B 69  ? 0.3886 0.3879 0.3594 0.0375  0.0509  -0.0201 78  SER   B O   
873  C CB  . SER   B 69  ? 0.4412 0.4230 0.3878 0.0458  0.0400  -0.0235 78  SER   B CB  
874  O OG  . SER   B 69  ? 0.4652 0.4503 0.4182 0.0349  0.0393  -0.0259 78  SER   B OG  
875  N N   . TYR   B 70  ? 0.4253 0.4238 0.3902 0.0477  0.0463  -0.0240 79  TYR   B N   
876  C CA  . TYR   B 70  ? 0.4108 0.4171 0.3849 0.0452  0.0478  -0.0260 79  TYR   B CA  
877  C C   . TYR   B 70  ? 0.4297 0.4394 0.4045 0.0429  0.0430  -0.0320 79  TYR   B C   
878  O O   . TYR   B 70  ? 0.4028 0.4079 0.3701 0.0478  0.0392  -0.0334 79  TYR   B O   
879  C CB  . TYR   B 70  ? 0.4363 0.4427 0.4104 0.0531  0.0507  -0.0227 79  TYR   B CB  
880  C CG  . TYR   B 70  ? 0.4248 0.4302 0.4008 0.0536  0.0557  -0.0165 79  TYR   B CG  
881  C CD1 . TYR   B 70  ? 0.4356 0.4368 0.4054 0.0580  0.0574  -0.0116 79  TYR   B CD1 
882  C CD2 . TYR   B 70  ? 0.4498 0.4592 0.4339 0.0494  0.0586  -0.0154 79  TYR   B CD2 
883  C CE1 . TYR   B 70  ? 0.4192 0.4210 0.3916 0.0577  0.0619  -0.0056 79  TYR   B CE1 
884  C CE2 . TYR   B 70  ? 0.4331 0.4416 0.4193 0.0491  0.0626  -0.0095 79  TYR   B CE2 
885  C CZ  . TYR   B 70  ? 0.4102 0.4155 0.3909 0.0531  0.0643  -0.0043 79  TYR   B CZ  
886  O OH  . TYR   B 70  ? 0.4687 0.4745 0.4521 0.0523  0.0682  0.0018  79  TYR   B OH  
887  N N   . CYS   B 71  ? 0.4327 0.4503 0.4156 0.0354  0.0429  -0.0353 80  CYS   B N   
888  C CA  . CYS   B 71  ? 0.4577 0.4823 0.4439 0.0321  0.0389  -0.0409 80  CYS   B CA  
889  C C   . CYS   B 71  ? 0.4696 0.4921 0.4525 0.0252  0.0346  -0.0428 80  CYS   B C   
890  O O   . CYS   B 71  ? 0.4754 0.5052 0.4622 0.0199  0.0314  -0.0469 80  CYS   B O   
891  C CB  . CYS   B 71  ? 0.5229 0.5475 0.5062 0.0402  0.0365  -0.0428 80  CYS   B CB  
892  S SG  . CYS   B 71  ? 0.5821 0.6073 0.5680 0.0481  0.0411  -0.0399 80  CYS   B SG  
893  N N   . GLY   B 72  ? 0.4670 0.4800 0.4427 0.0252  0.0341  -0.0399 81  GLY   B N   
894  C CA  . GLY   B 72  ? 0.4613 0.4696 0.4315 0.0195  0.0287  -0.0418 81  GLY   B CA  
895  C C   . GLY   B 72  ? 0.4507 0.4476 0.4121 0.0212  0.0287  -0.0384 81  GLY   B C   
896  O O   . GLY   B 72  ? 0.4151 0.4093 0.3751 0.0271  0.0330  -0.0344 81  GLY   B O   
897  N N   . PRO   B 73  ? 0.4553 0.4458 0.4107 0.0155  0.0238  -0.0395 82  PRO   B N   
898  C CA  . PRO   B 73  ? 0.4942 0.4729 0.4398 0.0178  0.0229  -0.0368 82  PRO   B CA  
899  C C   . PRO   B 73  ? 0.5127 0.4826 0.4476 0.0295  0.0209  -0.0358 82  PRO   B C   
900  O O   . PRO   B 73  ? 0.5210 0.4914 0.4541 0.0338  0.0179  -0.0383 82  PRO   B O   
901  C CB  . PRO   B 73  ? 0.4910 0.4647 0.4325 0.0083  0.0168  -0.0390 82  PRO   B CB  
902  C CG  . PRO   B 73  ? 0.4955 0.4762 0.4413 0.0047  0.0128  -0.0431 82  PRO   B CG  
903  C CD  . PRO   B 73  ? 0.4844 0.4785 0.4417 0.0068  0.0185  -0.0433 82  PRO   B CD  
904  N N   . TRP   B 74  ? 0.5161 0.4783 0.4436 0.0346  0.0223  -0.0325 83  TRP   B N   
905  C CA  . TRP   B 74  ? 0.5299 0.4832 0.4454 0.0460  0.0202  -0.0314 83  TRP   B CA  
906  C C   . TRP   B 74  ? 0.5573 0.5025 0.4638 0.0466  0.0118  -0.0356 83  TRP   B C   
907  O O   . TRP   B 74  ? 0.5555 0.4945 0.4581 0.0394  0.0067  -0.0375 83  TRP   B O   
908  C CB  . TRP   B 74  ? 0.5356 0.4821 0.4440 0.0490  0.0215  -0.0281 83  TRP   B CB  
909  C CG  . TRP   B 74  ? 0.5168 0.4578 0.4147 0.0621  0.0217  -0.0258 83  TRP   B CG  
910  C CD1 . TRP   B 74  ? 0.5136 0.4429 0.3973 0.0685  0.0154  -0.0276 83  TRP   B CD1 
911  C CD2 . TRP   B 74  ? 0.5102 0.4576 0.4107 0.0706  0.0282  -0.0214 83  TRP   B CD2 
912  N NE1 . TRP   B 74  ? 0.5171 0.4459 0.3942 0.0809  0.0180  -0.0247 83  TRP   B NE1 
913  C CE2 . TRP   B 74  ? 0.5027 0.4429 0.3901 0.0822  0.0259  -0.0205 83  TRP   B CE2 
914  C CE3 . TRP   B 74  ? 0.4963 0.4544 0.4082 0.0695  0.0353  -0.0178 83  TRP   B CE3 
915  C CZ2 . TRP   B 74  ? 0.5017 0.4465 0.3877 0.0924  0.0309  -0.0161 83  TRP   B CZ2 
916  C CZ3 . TRP   B 74  ? 0.4855 0.4470 0.3960 0.0789  0.0398  -0.0133 83  TRP   B CZ3 
917  C CH2 . TRP   B 74  ? 0.4888 0.4443 0.3866 0.0901  0.0379  -0.0122 83  TRP   B CH2 
918  N N   . LYS   B 75  ? 0.5683 0.5121 0.4701 0.0558  0.0102  -0.0366 84  LYS   B N   
919  C CA  . LYS   B 75  ? 0.5800 0.5164 0.4734 0.0577  0.0019  -0.0407 84  LYS   B CA  
920  C C   . LYS   B 75  ? 0.6013 0.5244 0.4784 0.0690  -0.0019 -0.0402 84  LYS   B C   
921  O O   . LYS   B 75  ? 0.6518 0.5657 0.5200 0.0693  -0.0100 -0.0437 84  LYS   B O   
922  C CB  . LYS   B 75  ? 0.5853 0.5302 0.4851 0.0605  0.0026  -0.0426 84  LYS   B CB  
923  C CG  . LYS   B 75  ? 0.5927 0.5508 0.5074 0.0508  0.0055  -0.0440 84  LYS   B CG  
924  C CD  . LYS   B 75  ? 0.6196 0.5781 0.5362 0.0395  -0.0004 -0.0475 84  LYS   B CD  
925  C CE  . LYS   B 75  ? 0.6448 0.6177 0.5761 0.0302  0.0037  -0.0481 84  LYS   B CE  
926  N NZ  . LYS   B 75  ? 0.6808 0.6598 0.6164 0.0225  -0.0017 -0.0522 84  LYS   B NZ  
927  N N   . LEU   B 76  ? 0.6074 0.5299 0.4806 0.0780  0.0031  -0.0361 85  LEU   B N   
928  C CA  . LEU   B 76  ? 0.6347 0.5477 0.4930 0.0913  0.0006  -0.0354 85  LEU   B CA  
929  C C   . LEU   B 76  ? 0.6648 0.5657 0.5116 0.0913  -0.0037 -0.0356 85  LEU   B C   
930  O O   . LEU   B 76  ? 0.6381 0.5420 0.4881 0.0894  0.0012  -0.0322 85  LEU   B O   
931  C CB  . LEU   B 76  ? 0.6516 0.5727 0.5126 0.1006  0.0089  -0.0304 85  LEU   B CB  
932  C CG  . LEU   B 76  ? 0.6307 0.5637 0.5041 0.0994  0.0140  -0.0295 85  LEU   B CG  
933  C CD1 . LEU   B 76  ? 0.6347 0.5743 0.5095 0.1082  0.0216  -0.0238 85  LEU   B CD1 
934  C CD2 . LEU   B 76  ? 0.6700 0.6009 0.5407 0.1018  0.0086  -0.0339 85  LEU   B CD2 
935  N N   . ASP   B 77  ? 0.7047 0.5920 0.5386 0.0930  -0.0131 -0.0394 86  ASP   B N   
936  C CA  . ASP   B 77  ? 0.8150 0.6883 0.6365 0.0921  -0.0189 -0.0403 86  ASP   B CA  
937  C C   . ASP   B 77  ? 0.8129 0.6731 0.6157 0.1066  -0.0242 -0.0413 86  ASP   B C   
938  O O   . ASP   B 77  ? 0.8156 0.6624 0.6060 0.1075  -0.0300 -0.0424 86  ASP   B O   
939  C CB  . ASP   B 77  ? 0.8874 0.7539 0.7093 0.0787  -0.0266 -0.0439 86  ASP   B CB  
940  C CG  . ASP   B 77  ? 0.9711 0.8341 0.7904 0.0779  -0.0338 -0.0480 86  ASP   B CG  
941  O OD1 . ASP   B 77  ? 1.0800 0.9456 0.8973 0.0881  -0.0325 -0.0482 86  ASP   B OD1 
942  O OD2 . ASP   B 77  ? 1.0429 0.9013 0.8626 0.0668  -0.0405 -0.0506 86  ASP   B OD2 
943  N N   . ALA   B 78  ? 0.7744 0.6378 0.5740 0.1182  -0.0223 -0.0407 87  ALA   B N   
944  C CA  . ALA   B 78  ? 0.7568 0.6083 0.5378 0.1329  -0.0273 -0.0419 87  ALA   B CA  
945  C C   . ALA   B 78  ? 0.7402 0.5936 0.5164 0.1414  -0.0219 -0.0377 87  ALA   B C   
946  O O   . ALA   B 78  ? 0.6832 0.5512 0.4725 0.1387  -0.0121 -0.0330 87  ALA   B O   
947  C CB  . ALA   B 78  ? 0.7614 0.6168 0.5412 0.1423  -0.0266 -0.0424 87  ALA   B CB  
948  N N   . ALA   B 79  ? 0.7168 0.5562 0.4743 0.1520  -0.0282 -0.0394 88  ALA   B N   
949  C CA  . ALA   B 79  ? 0.7346 0.5741 0.4845 0.1613  -0.0249 -0.0363 88  ALA   B CA  
950  C C   . ALA   B 79  ? 0.7256 0.5615 0.4598 0.1801  -0.0262 -0.0361 88  ALA   B C   
951  O O   . ALA   B 79  ? 0.7348 0.5573 0.4559 0.1853  -0.0350 -0.0406 88  ALA   B O   
952  C CB  . ALA   B 79  ? 0.7503 0.5753 0.4917 0.1552  -0.0322 -0.0389 88  ALA   B CB  
953  N N   . TRP   B 80  ? 0.7276 0.5752 0.4625 0.1899  -0.0179 -0.0311 89  TRP   B N   
954  C CA  . TRP   B 80  ? 0.7868 0.6318 0.5052 0.2087  -0.0187 -0.0304 89  TRP   B CA  
955  C C   . TRP   B 80  ? 0.8111 0.6351 0.5098 0.2133  -0.0300 -0.0356 89  TRP   B C   
956  O O   . TRP   B 80  ? 0.7725 0.5907 0.4734 0.2032  -0.0325 -0.0365 89  TRP   B O   
957  C CB  . TRP   B 80  ? 0.8033 0.6650 0.5263 0.2164  -0.0084 -0.0237 89  TRP   B CB  
958  C CG  . TRP   B 80  ? 0.8132 0.6743 0.5195 0.2359  -0.0088 -0.0229 89  TRP   B CG  
959  C CD1 . TRP   B 80  ? 0.8312 0.6871 0.5260 0.2473  -0.0125 -0.0251 89  TRP   B CD1 
960  C CD2 . TRP   B 80  ? 0.8289 0.6956 0.5278 0.2471  -0.0056 -0.0197 89  TRP   B CD2 
961  N NE1 . TRP   B 80  ? 0.8425 0.7002 0.5228 0.2649  -0.0117 -0.0235 89  TRP   B NE1 
962  C CE2 . TRP   B 80  ? 0.8258 0.6906 0.5084 0.2652  -0.0075 -0.0202 89  TRP   B CE2 
963  C CE3 . TRP   B 80  ? 0.8117 0.6848 0.5156 0.2439  -0.0016 -0.0168 89  TRP   B CE3 
964  C CZ2 . TRP   B 80  ? 0.8197 0.6900 0.4914 0.2804  -0.0052 -0.0178 89  TRP   B CZ2 
965  C CZ3 . TRP   B 80  ? 0.8127 0.6911 0.5060 0.2587  0.0003  -0.0144 89  TRP   B CZ3 
966  C CH2 . TRP   B 80  ? 0.8098 0.6873 0.4873 0.2767  -0.0013 -0.0149 89  TRP   B CH2 
967  N N   . ASP   B 81  ? 0.8479 0.6599 0.5285 0.2265  -0.0372 -0.0391 90  ASP   B N   
968  C CA  . ASP   B 81  ? 0.8915 0.6803 0.5512 0.2311  -0.0499 -0.0448 90  ASP   B CA  
969  C C   . ASP   B 81  ? 0.8961 0.6848 0.5431 0.2453  -0.0485 -0.0431 90  ASP   B C   
970  O O   . ASP   B 81  ? 0.9398 0.7096 0.5690 0.2501  -0.0584 -0.0473 90  ASP   B O   
971  C CB  . ASP   B 81  ? 0.8922 0.6658 0.5377 0.2375  -0.0600 -0.0501 90  ASP   B CB  
972  C CG  . ASP   B 81  ? 0.8987 0.6771 0.5340 0.2563  -0.0575 -0.0490 90  ASP   B CG  
973  O OD1 . ASP   B 81  ? 0.9419 0.7376 0.5827 0.2639  -0.0471 -0.0435 90  ASP   B OD1 
974  O OD2 . ASP   B 81  ? 1.0074 0.7732 0.6300 0.2628  -0.0657 -0.0534 90  ASP   B OD2 
975  N N   . GLY   B 82  ? 0.9056 0.7149 0.5616 0.2515  -0.0369 -0.0369 91  GLY   B N   
976  C CA  . GLY   B 82  ? 0.9134 0.7282 0.5604 0.2651  -0.0336 -0.0343 91  GLY   B CA  
977  C C   . GLY   B 82  ? 0.9477 0.7591 0.5752 0.2864  -0.0364 -0.0355 91  GLY   B C   
978  O O   . GLY   B 82  ? 0.9375 0.7525 0.5552 0.2992  -0.0348 -0.0340 91  GLY   B O   
979  N N   . LEU   B 83  ? 0.9626 0.7676 0.5842 0.2905  -0.0406 -0.0383 92  LEU   B N   
980  C CA  . LEU   B 83  ? 1.0011 0.8003 0.6024 0.3109  -0.0447 -0.0404 92  LEU   B CA  
981  C C   . LEU   B 83  ? 1.0272 0.8405 0.6360 0.3150  -0.0378 -0.0371 92  LEU   B C   
982  O O   . LEU   B 83  ? 1.0210 0.8465 0.6241 0.3305  -0.0319 -0.0334 92  LEU   B O   
983  C CB  . LEU   B 83  ? 1.0444 0.8155 0.6269 0.3121  -0.0601 -0.0486 92  LEU   B CB  
984  C CG  . LEU   B 83  ? 1.0925 0.8446 0.6578 0.3156  -0.0697 -0.0527 92  LEU   B CG  
985  C CD1 . LEU   B 83  ? 1.1387 0.8626 0.6853 0.3165  -0.0853 -0.0604 92  LEU   B CD1 
986  C CD2 . LEU   B 83  ? 1.1161 0.8743 0.6675 0.3357  -0.0668 -0.0509 92  LEU   B CD2 
987  N N   . SER   B 84  ? 1.0053 0.8157 0.6245 0.3026  -0.0395 -0.0388 93  SER   B N   
988  C CA  . SER   B 84  ? 0.9753 0.7923 0.5974 0.3067  -0.0367 -0.0378 93  SER   B CA  
989  C C   . SER   B 84  ? 0.9518 0.7946 0.5929 0.3041  -0.0222 -0.0295 93  SER   B C   
990  O O   . SER   B 84  ? 0.9502 0.8040 0.6061 0.2938  -0.0154 -0.0255 93  SER   B O   
991  C CB  . SER   B 84  ? 0.9749 0.7800 0.6017 0.2938  -0.0441 -0.0428 93  SER   B CB  
992  O OG  . SER   B 84  ? 0.9810 0.7684 0.6030 0.2842  -0.0538 -0.0478 93  SER   B OG  
993  N N   . GLU   B 85  ? 0.9237 0.7755 0.5631 0.3141  -0.0177 -0.0268 94  GLU   B N   
994  C CA  . GLU   B 85  ? 0.8880 0.7625 0.5449 0.3108  -0.0048 -0.0187 94  GLU   B CA  
995  C C   . GLU   B 85  ? 0.8021 0.6775 0.4778 0.2918  -0.0040 -0.0195 94  GLU   B C   
996  O O   . GLU   B 85  ? 0.7351 0.5952 0.4090 0.2838  -0.0130 -0.0260 94  GLU   B O   
997  C CB  . GLU   B 85  ? 0.9581 0.8407 0.6067 0.3266  -0.0009 -0.0155 94  GLU   B CB  
998  C CG  . GLU   B 85  ? 0.9669 0.8595 0.6037 0.3440  0.0035  -0.0112 94  GLU   B CG  
999  C CD  . GLU   B 85  ? 1.0262 0.9298 0.6551 0.3599  0.0088  -0.0068 94  GLU   B CD  
1000 O OE1 . GLU   B 85  ? 0.9628 0.8706 0.5985 0.3570  0.0117  -0.0049 94  GLU   B OE1 
1001 O OE2 . GLU   B 85  ? 1.0360 0.9445 0.6510 0.3762  0.0100  -0.0051 94  GLU   B OE2 
1002 N N   . VAL   B 86  ? 0.7640 0.6573 0.4577 0.2844  0.0064  -0.0129 95  VAL   B N   
1003 C CA  . VAL   B 86  ? 0.7106 0.6072 0.4231 0.2672  0.0084  -0.0130 95  VAL   B CA  
1004 C C   . VAL   B 86  ? 0.6797 0.5907 0.4009 0.2693  0.0168  -0.0071 95  VAL   B C   
1005 O O   . VAL   B 86  ? 0.7088 0.6290 0.4235 0.2819  0.0220  -0.0021 95  VAL   B O   
1006 C CB  . VAL   B 86  ? 0.6712 0.5741 0.3984 0.2533  0.0125  -0.0106 95  VAL   B CB  
1007 C CG1 . VAL   B 86  ? 0.6775 0.5668 0.3947 0.2525  0.0050  -0.0153 95  VAL   B CG1 
1008 C CG2 . VAL   B 86  ? 0.6718 0.5936 0.4074 0.2558  0.0236  -0.0019 95  VAL   B CG2 
1009 N N   . GLN   B 87  ? 0.6768 0.5915 0.4133 0.2566  0.0189  -0.0070 96  GLN   B N   
1010 C CA  . GLN   B 87  ? 0.6819 0.6108 0.4288 0.2564  0.0275  -0.0006 96  GLN   B CA  
1011 C C   . GLN   B 87  ? 0.6464 0.5857 0.4136 0.2411  0.0341  0.0032  96  GLN   B C   
1012 O O   . GLN   B 87  ? 0.6685 0.6024 0.4438 0.2289  0.0304  -0.0011 96  GLN   B O   
1013 C CB  . GLN   B 87  ? 0.6955 0.6182 0.4389 0.2592  0.0233  -0.0044 96  GLN   B CB  
1014 C CG  . GLN   B 87  ? 0.7348 0.6504 0.4584 0.2765  0.0190  -0.0063 96  GLN   B CG  
1015 C CD  . GLN   B 87  ? 0.7675 0.6779 0.4866 0.2810  0.0153  -0.0093 96  GLN   B CD  
1016 O OE1 . GLN   B 87  ? 0.7154 0.6293 0.4467 0.2721  0.0170  -0.0093 96  GLN   B OE1 
1017 N NE2 . GLN   B 87  ? 0.7781 0.6795 0.4788 0.2955  0.0098  -0.0124 96  GLN   B NE2 
1018 N N   . LEU   B 88  ? 0.6227 0.5768 0.3970 0.2421  0.0433  0.0115  97  LEU   B N   
1019 C CA  . LEU   B 88  ? 0.6100 0.5748 0.4027 0.2296  0.0501  0.0165  97  LEU   B CA  
1020 C C   . LEU   B 88  ? 0.6154 0.5810 0.4121 0.2288  0.0510  0.0168  97  LEU   B C   
1021 O O   . LEU   B 88  ? 0.6216 0.5926 0.4126 0.2387  0.0546  0.0215  97  LEU   B O   
1022 C CB  . LEU   B 88  ? 0.6062 0.5863 0.4035 0.2320  0.0589  0.0257  97  LEU   B CB  
1023 C CG  . LEU   B 88  ? 0.6086 0.5992 0.4237 0.2200  0.0657  0.0316  97  LEU   B CG  
1024 C CD1 . LEU   B 88  ? 0.6330 0.6196 0.4593 0.2054  0.0636  0.0276  97  LEU   B CD1 
1025 C CD2 . LEU   B 88  ? 0.6158 0.6220 0.4345 0.2230  0.0740  0.0414  97  LEU   B CD2 
1026 N N   A LEU   B 89  ? 0.5996 0.5602 0.4053 0.2178  0.0477  0.0120  98  LEU   B N   
1027 N N   B LEU   B 89  ? 0.5996 0.5602 0.4053 0.2178  0.0477  0.0120  98  LEU   B N   
1028 N N   C LEU   B 89  ? 0.6048 0.5655 0.4106 0.2178  0.0477  0.0120  98  LEU   B N   
1029 N N   D LEU   B 89  ? 0.6048 0.5655 0.4106 0.2178  0.0477  0.0120  98  LEU   B N   
1030 C CA  A LEU   B 89  ? 0.5901 0.5526 0.4024 0.2151  0.0490  0.0125  98  LEU   B CA  
1031 C CA  B LEU   B 89  ? 0.5901 0.5526 0.4024 0.2151  0.0490  0.0125  98  LEU   B CA  
1032 C CA  C LEU   B 89  ? 0.5982 0.5607 0.4108 0.2148  0.0490  0.0124  98  LEU   B CA  
1033 C CA  D LEU   B 89  ? 0.5982 0.5607 0.4108 0.2148  0.0490  0.0124  98  LEU   B CA  
1034 C C   A LEU   B 89  ? 0.5912 0.5655 0.4176 0.2072  0.0572  0.0200  98  LEU   B C   
1035 C C   B LEU   B 89  ? 0.5912 0.5655 0.4176 0.2072  0.0572  0.0200  98  LEU   B C   
1036 C C   C LEU   B 89  ? 0.5963 0.5706 0.4228 0.2071  0.0572  0.0200  98  LEU   B C   
1037 C C   D LEU   B 89  ? 0.5963 0.5706 0.4228 0.2071  0.0572  0.0200  98  LEU   B C   
1038 O O   A LEU   B 89  ? 0.5914 0.5662 0.4303 0.1949  0.0573  0.0183  98  LEU   B O   
1039 O O   B LEU   B 89  ? 0.5914 0.5662 0.4303 0.1949  0.0573  0.0183  98  LEU   B O   
1040 O O   C LEU   B 89  ? 0.5963 0.5713 0.4353 0.1948  0.0574  0.0184  98  LEU   B O   
1041 O O   D LEU   B 89  ? 0.5963 0.5713 0.4353 0.1948  0.0574  0.0184  98  LEU   B O   
1042 C CB  A LEU   B 89  ? 0.5850 0.5386 0.4009 0.2070  0.0419  0.0040  98  LEU   B CB  
1043 C CB  B LEU   B 89  ? 0.5850 0.5386 0.4009 0.2070  0.0419  0.0040  98  LEU   B CB  
1044 C CB  C LEU   B 89  ? 0.5993 0.5531 0.4159 0.2062  0.0420  0.0040  98  LEU   B CB  
1045 C CB  D LEU   B 89  ? 0.5993 0.5531 0.4159 0.2062  0.0420  0.0040  98  LEU   B CB  
1046 C CG  A LEU   B 89  ? 0.5766 0.5318 0.4004 0.2029  0.0422  0.0031  98  LEU   B CG  
1047 C CG  B LEU   B 89  ? 0.5766 0.5318 0.4004 0.2029  0.0422  0.0031  98  LEU   B CG  
1048 C CG  C LEU   B 89  ? 0.5964 0.5517 0.4209 0.2021  0.0422  0.0029  98  LEU   B CG  
1049 C CG  D LEU   B 89  ? 0.5964 0.5517 0.4209 0.2021  0.0422  0.0029  98  LEU   B CG  
1050 C CD1 A LEU   B 89  ? 0.5756 0.5383 0.3992 0.2094  0.0488  0.0106  98  LEU   B CD1 
1051 C CD1 B LEU   B 89  ? 0.5756 0.5383 0.3992 0.2094  0.0488  0.0106  98  LEU   B CD1 
1052 C CD1 C LEU   B 89  ? 0.6047 0.5603 0.4204 0.2139  0.0433  0.0055  98  LEU   B CD1 
1053 C CD1 D LEU   B 89  ? 0.6047 0.5603 0.4204 0.2139  0.0433  0.0055  98  LEU   B CD1 
1054 C CD2 A LEU   B 89  ? 0.5804 0.5259 0.3972 0.2058  0.0339  -0.0048 98  LEU   B CD2 
1055 C CD2 B LEU   B 89  ? 0.5804 0.5259 0.3972 0.2058  0.0339  -0.0048 98  LEU   B CD2 
1056 C CD2 C LEU   B 89  ? 0.5953 0.5429 0.4220 0.1952  0.0344  -0.0057 98  LEU   B CD2 
1057 C CD2 D LEU   B 89  ? 0.5953 0.5429 0.4220 0.1952  0.0344  -0.0057 98  LEU   B CD2 
1058 N N   . ALA   B 90  ? 0.6039 0.5875 0.4279 0.2142  0.0636  0.0282  99  ALA   B N   
1059 C CA  . ALA   B 90  ? 0.6022 0.5972 0.4384 0.2075  0.0713  0.0367  99  ALA   B CA  
1060 C C   . ALA   B 90  ? 0.6298 0.6238 0.4728 0.2027  0.0718  0.0370  99  ALA   B C   
1061 O O   . ALA   B 90  ? 0.6243 0.6140 0.4590 0.2108  0.0695  0.0353  99  ALA   B O   
1062 C CB  . ALA   B 90  ? 0.6106 0.6162 0.4416 0.2166  0.0775  0.0456  99  ALA   B CB  
1063 N N   . VAL   B 91  ? 0.6110 0.6086 0.4679 0.1907  0.0744  0.0390  100 VAL   B N   
1064 C CA  . VAL   B 91  ? 0.5766 0.5746 0.4409 0.1856  0.0760  0.0410  100 VAL   B CA  
1065 C C   . VAL   B 91  ? 0.5780 0.5856 0.4509 0.1804  0.0828  0.0508  100 VAL   B C   
1066 O O   . VAL   B 91  ? 0.5408 0.5498 0.4249 0.1696  0.0839  0.0512  100 VAL   B O   
1067 C CB  . VAL   B 91  ? 0.5763 0.5681 0.4484 0.1762  0.0712  0.0330  100 VAL   B CB  
1068 C CG1 . VAL   B 91  ? 0.5908 0.5821 0.4699 0.1716  0.0720  0.0340  100 VAL   B CG1 
1069 C CG2 . VAL   B 91  ? 0.5762 0.5594 0.4397 0.1809  0.0642  0.0240  100 VAL   B CG2 
1070 N N   . PRO   B 92  ? 0.5992 0.6137 0.4668 0.1877  0.0876  0.0592  101 PRO   B N   
1071 C CA  . PRO   B 92  ? 0.5986 0.6229 0.4743 0.1823  0.0938  0.0693  101 PRO   B CA  
1072 C C   . PRO   B 92  ? 0.5974 0.6190 0.4809 0.1746  0.0943  0.0716  101 PRO   B C   
1073 O O   . PRO   B 92  ? 0.6173 0.6312 0.4975 0.1769  0.0908  0.0671  101 PRO   B O   
1074 C CB  . PRO   B 92  ? 0.6186 0.6516 0.4851 0.1933  0.0982  0.0772  101 PRO   B CB  
1075 C CG  . PRO   B 92  ? 0.6305 0.6569 0.4828 0.2057  0.0939  0.0706  101 PRO   B CG  
1076 C CD  . PRO   B 92  ? 0.6220 0.6360 0.4755 0.2015  0.0870  0.0597  101 PRO   B CD  
1077 N N   . PRO   B 93  ? 0.6042 0.6317 0.4977 0.1656  0.0982  0.0787  102 PRO   B N   
1078 C CA  . PRO   B 93  ? 0.6520 0.6760 0.5521 0.1584  0.0983  0.0815  102 PRO   B CA  
1079 C C   . PRO   B 93  ? 0.6822 0.7047 0.5743 0.1657  0.0992  0.0864  102 PRO   B C   
1080 O O   . PRO   B 93  ? 0.7438 0.7739 0.6297 0.1726  0.1031  0.0934  102 PRO   B O   
1081 C CB  . PRO   B 93  ? 0.6305 0.6625 0.5409 0.1490  0.1024  0.0895  102 PRO   B CB  
1082 C CG  . PRO   B 93  ? 0.6420 0.6782 0.5538 0.1486  0.1024  0.0858  102 PRO   B CG  
1083 C CD  . PRO   B 93  ? 0.6396 0.6769 0.5388 0.1616  0.1021  0.0839  102 PRO   B CD  
1084 N N   . GLY   B 94  ? 0.6829 0.6960 0.5745 0.1648  0.0955  0.0818  103 GLY   B N   
1085 C CA  . GLY   B 94  ? 0.6935 0.7025 0.5773 0.1713  0.0952  0.0849  103 GLY   B CA  
1086 C C   . GLY   B 94  ? 0.6856 0.6941 0.5564 0.1845  0.0943  0.0825  103 GLY   B C   
1087 O O   . GLY   B 94  ? 0.7395 0.7457 0.6031 0.1904  0.0947  0.0862  103 GLY   B O   
1088 N N   . GLU   B 95  ? 0.6699 0.6792 0.5367 0.1894  0.0925  0.0763  104 GLU   B N   
1089 C CA  . GLU   B 95  ? 0.6823 0.6917 0.5356 0.2027  0.0918  0.0750  104 GLU   B CA  
1090 C C   . GLU   B 95  ? 0.6968 0.6973 0.5465 0.2055  0.0850  0.0628  104 GLU   B C   
1091 O O   . GLU   B 95  ? 0.7181 0.7161 0.5761 0.1970  0.0823  0.0568  104 GLU   B O   
1092 C CB  . GLU   B 95  ? 0.7049 0.7252 0.5549 0.2075  0.0965  0.0813  104 GLU   B CB  
1093 C CG  . GLU   B 95  ? 0.7372 0.7685 0.5909 0.2048  0.1035  0.0944  104 GLU   B CG  
1094 C CD  . GLU   B 95  ? 0.7776 0.8225 0.6300 0.2085  0.1086  0.1011  104 GLU   B CD  
1095 O OE1 . GLU   B 95  ? 0.7861 0.8310 0.6346 0.2132  0.1066  0.0952  104 GLU   B OE1 
1096 O OE2 . GLU   B 95  ? 0.8115 0.8676 0.6667 0.2067  0.1145  0.1126  104 GLU   B OE2 
1097 N N   . ARG   B 96  ? 0.7067 0.7024 0.5446 0.2163  0.0819  0.0592  105 ARG   B N   
1098 C CA  . ARG   B 96  ? 0.7486 0.7353 0.5831 0.2184  0.0746  0.0477  105 ARG   B CA  
1099 C C   . ARG   B 96  ? 0.7327 0.7199 0.5664 0.2179  0.0728  0.0434  105 ARG   B C   
1100 O O   . ARG   B 96  ? 0.7352 0.7292 0.5651 0.2221  0.0768  0.0490  105 ARG   B O   
1101 C CB  . ARG   B 96  ? 0.8523 0.8340 0.6733 0.2310  0.0719  0.0459  105 ARG   B CB  
1102 C CG  . ARG   B 96  ? 0.9233 0.8956 0.7409 0.2329  0.0639  0.0346  105 ARG   B CG  
1103 C CD  . ARG   B 96  ? 0.9801 0.9468 0.7896 0.2410  0.0611  0.0330  105 ARG   B CD  
1104 N NE  . ARG   B 96  ? 0.9961 0.9650 0.7931 0.2530  0.0643  0.0394  105 ARG   B NE  
1105 C CZ  . ARG   B 96  ? 1.0526 1.0256 0.8480 0.2552  0.0697  0.0486  105 ARG   B CZ  
1106 N NH1 . ARG   B 96  ? 1.0443 1.0184 0.8495 0.2462  0.0722  0.0528  105 ARG   B NH1 
1107 N NH2 . ARG   B 96  ? 1.0948 1.0705 0.8780 0.2667  0.0723  0.0539  105 ARG   B NH2 
1108 N N   . ALA   B 97  ? 0.7029 0.6836 0.5394 0.2132  0.0668  0.0340  106 ALA   B N   
1109 C CA  . ALA   B 97  ? 0.7018 0.6797 0.5338 0.2147  0.0632  0.0286  106 ALA   B CA  
1110 C C   . ALA   B 97  ? 0.7314 0.7089 0.5481 0.2289  0.0631  0.0305  106 ALA   B C   
1111 O O   . ALA   B 97  ? 0.7535 0.7269 0.5618 0.2372  0.0610  0.0293  106 ALA   B O   
1112 C CB  . ALA   B 97  ? 0.6817 0.6515 0.5150 0.2107  0.0557  0.0184  106 ALA   B CB  
1113 N N   . LYS   B 98  ? 0.7793 0.7602 0.5918 0.2321  0.0648  0.0326  107 LYS   B N   
1114 C CA  . LYS   B 98  ? 0.8269 0.8072 0.6237 0.2466  0.0640  0.0334  107 LYS   B CA  
1115 C C   . LYS   B 98  ? 0.8161 0.7927 0.6079 0.2478  0.0604  0.0289  107 LYS   B C   
1116 O O   . LYS   B 98  ? 0.7806 0.7633 0.5808 0.2405  0.0639  0.0320  107 LYS   B O   
1117 C CB  . LYS   B 98  ? 0.9103 0.9028 0.7060 0.2518  0.0724  0.0445  107 LYS   B CB  
1118 C CG  . LYS   B 98  ? 0.9999 0.9952 0.7800 0.2674  0.0733  0.0470  107 LYS   B CG  
1119 C CD  . LYS   B 98  ? 1.0765 1.0874 0.8584 0.2701  0.0822  0.0585  107 LYS   B CD  
1120 C CE  . LYS   B 98  ? 1.1044 1.1233 0.9022 0.2565  0.0866  0.0629  107 LYS   B CE  
1121 N NZ  . LYS   B 98  ? 1.1721 1.2069 0.9711 0.2595  0.0944  0.0734  107 LYS   B NZ  
1122 N N   . ASN   B 99  ? 0.7650 0.7313 0.5434 0.2565  0.0532  0.0220  108 ASN   B N   
1123 C CA  . ASN   B 99  ? 0.7663 0.7264 0.5360 0.2600  0.0484  0.0174  108 ASN   B CA  
1124 C C   . ASN   B 99  ? 0.7830 0.7516 0.5438 0.2715  0.0535  0.0240  108 ASN   B C   
1125 O O   . ASN   B 99  ? 0.8190 0.7927 0.5726 0.2819  0.0569  0.0287  108 ASN   B O   
1126 C CB  . ASN   B 99  ? 0.7519 0.6971 0.5089 0.2660  0.0384  0.0082  108 ASN   B CB  
1127 C CG  . ASN   B 99  ? 0.7819 0.7200 0.5475 0.2548  0.0328  0.0014  108 ASN   B CG  
1128 O OD1 . ASN   B 99  ? 0.7907 0.7325 0.5645 0.2507  0.0352  0.0027  108 ASN   B OD1 
1129 N ND2 . ASN   B 99  ? 0.7672 0.6949 0.5301 0.2504  0.0250  -0.0059 108 ASN   B ND2 
1130 N N   . ILE   B 100 ? 0.7298 0.7003 0.4905 0.2703  0.0539  0.0243  109 ILE   B N   
1131 C CA  . ILE   B 100 ? 0.7247 0.7038 0.4764 0.2819  0.0580  0.0296  109 ILE   B CA  
1132 C C   . ILE   B 100 ? 0.7215 0.6897 0.4628 0.2855  0.0508  0.0227  109 ILE   B C   
1133 O O   . ILE   B 100 ? 0.7406 0.7049 0.4902 0.2741  0.0486  0.0196  109 ILE   B O   
1134 C CB  . ILE   B 100 ? 0.7339 0.7296 0.4989 0.2752  0.0673  0.0389  109 ILE   B CB  
1135 C CG1 . ILE   B 100 ? 0.7249 0.7286 0.5023 0.2676  0.0733  0.0452  109 ILE   B CG1 
1136 C CG2 . ILE   B 100 ? 0.7531 0.7599 0.5088 0.2880  0.0717  0.0446  109 ILE   B CG2 
1137 C CD1 . ILE   B 100 ? 0.7370 0.7474 0.5061 0.2792  0.0773  0.0511  109 ILE   B CD1 
1138 N N   . GLN   B 101 ? 0.7396 0.7014 0.4627 0.3006  0.0464  0.0198  110 GLN   B N   
1139 C CA  . GLN   B 101 ? 0.7712 0.7187 0.4818 0.3048  0.0375  0.0122  110 GLN   B CA  
1140 C C   . GLN   B 101 ? 0.7946 0.7510 0.5008 0.3118  0.0414  0.0163  110 GLN   B C   
1141 O O   . GLN   B 101 ? 0.8005 0.7716 0.5049 0.3210  0.0488  0.0237  110 GLN   B O   
1142 C CB  . GLN   B 101 ? 0.8109 0.7447 0.5029 0.3177  0.0294  0.0060  110 GLN   B CB  
1143 C CG  . GLN   B 101 ? 0.8003 0.7190 0.4767 0.3241  0.0201  -0.0009 110 GLN   B CG  
1144 C CD  . GLN   B 101 ? 0.8430 0.7447 0.5047 0.3315  0.0101  -0.0084 110 GLN   B CD  
1145 O OE1 . GLN   B 101 ? 0.7985 0.6972 0.4656 0.3261  0.0084  -0.0104 110 GLN   B OE1 
1146 N NE2 . GLN   B 101 ? 0.8494 0.7402 0.4913 0.3450  0.0032  -0.0125 110 GLN   B NE2 
1147 N N   . THR   B 102 ? 0.7939 0.7428 0.4992 0.3070  0.0369  0.0122  111 THR   B N   
1148 C CA  . THR   B 102 ? 0.7722 0.7295 0.4741 0.3129  0.0402  0.0157  111 THR   B CA  
1149 C C   . THR   B 102 ? 0.7862 0.7266 0.4784 0.3123  0.0308  0.0079  111 THR   B C   
1150 O O   . THR   B 102 ? 0.8440 0.7695 0.5380 0.3025  0.0236  0.0014  111 THR   B O   
1151 C CB  . THR   B 102 ? 0.7537 0.7293 0.4753 0.3016  0.0503  0.0239  111 THR   B CB  
1152 O OG1 . THR   B 102 ? 0.7355 0.7229 0.4532 0.3101  0.0545  0.0285  111 THR   B OG1 
1153 C CG2 . THR   B 102 ? 0.7561 0.7261 0.4928 0.2829  0.0485  0.0210  111 THR   B CG2 
1154 N N   . LEU   B 103 ? 0.7804 0.7228 0.4614 0.3234  0.0304  0.0085  112 LEU   B N   
1155 C CA  . LEU   B 103 ? 0.7983 0.7268 0.4710 0.3226  0.0227  0.0026  112 LEU   B CA  
1156 C C   . LEU   B 103 ? 0.7824 0.7232 0.4710 0.3114  0.0293  0.0073  112 LEU   B C   
1157 O O   . LEU   B 103 ? 0.7728 0.7326 0.4660 0.3166  0.0378  0.0146  112 LEU   B O   
1158 C CB  . LEU   B 103 ? 0.8152 0.7386 0.4652 0.3426  0.0182  0.0002  112 LEU   B CB  
1159 C CG  . LEU   B 103 ? 0.8169 0.7235 0.4565 0.3422  0.0092  -0.0060 112 LEU   B CG  
1160 C CD1 . LEU   B 103 ? 0.8189 0.7002 0.4497 0.3370  -0.0029 -0.0149 112 LEU   B CD1 
1161 C CD2 . LEU   B 103 ? 0.8615 0.7689 0.4821 0.3618  0.0074  -0.0064 112 LEU   B CD2 
1162 N N   . PRO   B 104 ? 0.7605 0.6921 0.4585 0.2954  0.0257  0.0037  113 PRO   B N   
1163 C CA  . PRO   B 104 ? 0.7608 0.7029 0.4736 0.2844  0.0314  0.0078  113 PRO   B CA  
1164 C C   . PRO   B 104 ? 0.7882 0.7315 0.4902 0.2946  0.0303  0.0080  113 PRO   B C   
1165 O O   . PRO   B 104 ? 0.7850 0.7124 0.4686 0.3041  0.0215  0.0018  113 PRO   B O   
1166 C CB  . PRO   B 104 ? 0.7570 0.6848 0.4771 0.2676  0.0254  0.0022  113 PRO   B CB  
1167 C CG  . PRO   B 104 ? 0.7611 0.6757 0.4755 0.2672  0.0189  -0.0031 113 PRO   B CG  
1168 C CD  . PRO   B 104 ? 0.7855 0.6971 0.4808 0.2868  0.0162  -0.0040 113 PRO   B CD  
1169 N N   . GLY   B 105 ? 0.8014 0.7635 0.5150 0.2924  0.0389  0.0149  114 GLY   B N   
1170 C CA  . GLY   B 105 ? 0.8170 0.7810 0.5262 0.2962  0.0383  0.0150  114 GLY   B CA  
1171 C C   . GLY   B 105 ? 0.8176 0.7697 0.5342 0.2803  0.0340  0.0109  114 GLY   B C   
1172 O O   . GLY   B 105 ? 0.7632 0.7010 0.4819 0.2700  0.0286  0.0060  114 GLY   B O   
1173 N N   . ILE   B 106 ? 0.8108 0.7701 0.5318 0.2783  0.0366  0.0133  115 ILE   B N   
1174 C CA  . ILE   B 106 ? 0.8096 0.7568 0.5334 0.2664  0.0316  0.0092  115 ILE   B CA  
1175 C C   . ILE   B 106 ? 0.7599 0.7250 0.5013 0.2576  0.0400  0.0155  115 ILE   B C   
1176 O O   . ILE   B 106 ? 0.7882 0.7691 0.5292 0.2669  0.0453  0.0205  115 ILE   B O   
1177 C CB  . ILE   B 106 ? 0.8609 0.7920 0.5631 0.2782  0.0225  0.0032  115 ILE   B CB  
1178 C CG1 . ILE   B 106 ? 0.9202 0.8323 0.6033 0.2877  0.0133  -0.0031 115 ILE   B CG1 
1179 C CG2 . ILE   B 106 ? 0.9047 0.8235 0.6089 0.2664  0.0177  -0.0002 115 ILE   B CG2 
1180 C CD1 . ILE   B 106 ? 0.9115 0.8019 0.5931 0.2751  0.0044  -0.0096 115 ILE   B CD1 
1181 N N   . PHE   B 107 ? 0.7466 0.7095 0.5028 0.2402  0.0409  0.0153  116 PHE   B N   
1182 C CA  . PHE   B 107 ? 0.7174 0.6907 0.4877 0.2302  0.0458  0.0190  116 PHE   B CA  
1183 C C   . PHE   B 107 ? 0.7470 0.7035 0.5067 0.2291  0.0378  0.0131  116 PHE   B C   
1184 O O   . PHE   B 107 ? 0.7374 0.6757 0.4934 0.2210  0.0308  0.0072  116 PHE   B O   
1185 C CB  . PHE   B 107 ? 0.7103 0.6866 0.4997 0.2123  0.0495  0.0207  116 PHE   B CB  
1186 C CG  . PHE   B 107 ? 0.6929 0.6884 0.4968 0.2103  0.0587  0.0283  116 PHE   B CG  
1187 C CD1 . PHE   B 107 ? 0.7132 0.7225 0.5129 0.2235  0.0634  0.0335  116 PHE   B CD1 
1188 C CD2 . PHE   B 107 ? 0.6922 0.6912 0.5132 0.1950  0.0622  0.0301  116 PHE   B CD2 
1189 C CE1 . PHE   B 107 ? 0.7284 0.7545 0.5410 0.2206  0.0716  0.0410  116 PHE   B CE1 
1190 C CE2 . PHE   B 107 ? 0.6951 0.7099 0.5286 0.1927  0.0699  0.0371  116 PHE   B CE2 
1191 C CZ  . PHE   B 107 ? 0.7160 0.7441 0.5454 0.2050  0.0745  0.0427  116 PHE   B CZ  
1192 N N   . LYS   B 108 ? 0.7623 0.7250 0.5164 0.2377  0.0386  0.0146  117 LYS   B N   
1193 C CA  . LYS   B 108 ? 0.8068 0.7553 0.5512 0.2371  0.0317  0.0099  117 LYS   B CA  
1194 C C   . LYS   B 108 ? 0.7494 0.7060 0.5116 0.2219  0.0364  0.0130  117 LYS   B C   
1195 O O   . LYS   B 108 ? 0.7050 0.6831 0.4799 0.2222  0.0450  0.0199  117 LYS   B O   
1196 C CB  . LYS   B 108 ? 0.8764 0.8287 0.6054 0.2555  0.0303  0.0100  117 LYS   B CB  
1197 C CG  . LYS   B 108 ? 1.0019 0.9345 0.7064 0.2696  0.0204  0.0033  117 LYS   B CG  
1198 C CD  . LYS   B 108 ? 1.0712 1.0142 0.7622 0.2911  0.0218  0.0051  117 LYS   B CD  
1199 C CE  . LYS   B 108 ? 1.2195 1.1418 0.8861 0.3049  0.0118  -0.0017 117 LYS   B CE  
1200 N NZ  . LYS   B 108 ? 1.2542 1.1879 0.9078 0.3266  0.0137  0.0000  117 LYS   B NZ  
1201 N N   . THR   B 109 ? 0.7299 0.6705 0.4935 0.2088  0.0310  0.0084  118 THR   B N   
1202 C CA  . THR   B 109 ? 0.7212 0.6662 0.4998 0.1940  0.0341  0.0102  118 THR   B CA  
1203 C C   . THR   B 109 ? 0.7430 0.6690 0.5103 0.1910  0.0258  0.0046  118 THR   B C   
1204 O O   . THR   B 109 ? 0.7278 0.6341 0.4779 0.1958  0.0168  -0.0011 118 THR   B O   
1205 C CB  . THR   B 109 ? 0.6884 0.6350 0.4837 0.1776  0.0372  0.0109  118 THR   B CB  
1206 O OG1 . THR   B 109 ? 0.6738 0.6001 0.4632 0.1686  0.0293  0.0046  118 THR   B OG1 
1207 C CG2 . THR   B 109 ? 0.6769 0.6342 0.4782 0.1808  0.0422  0.0143  118 THR   B CG2 
1208 N N   . LYS   B 110 ? 0.7750 0.7057 0.5523 0.1818  0.0283  0.0064  119 LYS   B N   
1209 C CA  . LYS   B 110 ? 0.8187 0.7328 0.5870 0.1774  0.0213  0.0020  119 LYS   B CA  
1210 C C   . LYS   B 110 ? 0.8513 0.7449 0.6153 0.1663  0.0140  -0.0033 119 LYS   B C   
1211 O O   . LYS   B 110 ? 0.8915 0.7654 0.6401 0.1670  0.0051  -0.0082 119 LYS   B O   
1212 C CB  . LYS   B 110 ? 0.8288 0.7553 0.6119 0.1688  0.0270  0.0059  119 LYS   B CB  
1213 C CG  . LYS   B 110 ? 0.8616 0.7944 0.6643 0.1515  0.0320  0.0080  119 LYS   B CG  
1214 C CD  . LYS   B 110 ? 0.8797 0.8276 0.6976 0.1450  0.0384  0.0127  119 LYS   B CD  
1215 C CE  . LYS   B 110 ? 0.9047 0.8458 0.7316 0.1283  0.0375  0.0110  119 LYS   B CE  
1216 N NZ  . LYS   B 110 ? 0.8733 0.8122 0.7089 0.1178  0.0384  0.0100  119 LYS   B NZ  
1217 N N   . ASP   B 111 ? 0.8207 0.7186 0.5968 0.1570  0.0172  -0.0025 120 ASP   B N   
1218 C CA  . ASP   B 111 ? 0.8565 0.7386 0.6310 0.1455  0.0111  -0.0071 120 ASP   B CA  
1219 C C   . ASP   B 111 ? 0.8962 0.7669 0.6569 0.1538  0.0050  -0.0108 120 ASP   B C   
1220 O O   . ASP   B 111 ? 0.9309 0.7886 0.6894 0.1450  -0.0006 -0.0146 120 ASP   B O   
1221 C CB  . ASP   B 111 ? 0.8644 0.7580 0.6597 0.1311  0.0176  -0.0046 120 ASP   B CB  
1222 C CG  . ASP   B 111 ? 0.8758 0.7746 0.6824 0.1202  0.0210  -0.0027 120 ASP   B CG  
1223 O OD1 . ASP   B 111 ? 0.8862 0.7796 0.6846 0.1236  0.0183  -0.0033 120 ASP   B OD1 
1224 O OD2 . ASP   B 111 ? 0.9932 0.9004 0.8157 0.1086  0.0258  -0.0010 120 ASP   B OD2 
1225 N N   . GLY   B 112 ? 0.9001 0.7758 0.6518 0.1701  0.0060  -0.0096 121 GLY   B N   
1226 C CA  . GLY   B 112 ? 0.9107 0.7756 0.6482 0.1797  0.0000  -0.0131 121 GLY   B CA  
1227 C C   . GLY   B 112 ? 0.8909 0.7724 0.6330 0.1898  0.0070  -0.0091 121 GLY   B C   
1228 O O   . GLY   B 112 ? 0.8755 0.7774 0.6328 0.1885  0.0166  -0.0032 121 GLY   B O   
1229 N N   . ASP   B 113 ? 0.8798 0.7520 0.6083 0.1997  0.0017  -0.0122 122 ASP   B N   
1230 C CA  . ASP   B 113 ? 0.8758 0.7605 0.6041 0.2117  0.0067  -0.0092 122 ASP   B CA  
1231 C C   . ASP   B 113 ? 0.8402 0.7283 0.5806 0.2024  0.0092  -0.0089 122 ASP   B C   
1232 O O   . ASP   B 113 ? 0.7637 0.6383 0.5041 0.1916  0.0032  -0.0132 122 ASP   B O   
1233 C CB  . ASP   B 113 ? 0.9111 0.7829 0.6161 0.2291  -0.0008 -0.0131 122 ASP   B CB  
1234 C CG  . ASP   B 113 ? 0.9496 0.8226 0.6426 0.2422  -0.0017 -0.0127 122 ASP   B CG  
1235 O OD1 . ASP   B 113 ? 1.0100 0.8955 0.7137 0.2379  0.0040  -0.0088 122 ASP   B OD1 
1236 O OD2 . ASP   B 113 ? 1.0079 0.8698 0.6808 0.2572  -0.0084 -0.0163 122 ASP   B OD2 
1237 N N   . ILE   B 114 ? 0.8075 0.7137 0.5579 0.2062  0.0177  -0.0036 123 ILE   B N   
1238 C CA  . ILE   B 114 ? 0.8223 0.7334 0.5843 0.1988  0.0208  -0.0027 123 ILE   B CA  
1239 C C   . ILE   B 114 ? 0.7537 0.6721 0.5090 0.2135  0.0234  -0.0004 123 ILE   B C   
1240 O O   . ILE   B 114 ? 0.7159 0.6466 0.4692 0.2238  0.0285  0.0041  123 ILE   B O   
1241 C CB  . ILE   B 114 ? 0.8193 0.7466 0.6035 0.1858  0.0297  0.0024  123 ILE   B CB  
1242 C CG1 . ILE   B 114 ? 0.8877 0.8123 0.6781 0.1745  0.0291  0.0018  123 ILE   B CG1 
1243 C CG2 . ILE   B 114 ? 0.8155 0.7439 0.6104 0.1765  0.0309  0.0018  123 ILE   B CG2 
1244 C CD1 . ILE   B 114 ? 0.8981 0.8389 0.7091 0.1635  0.0378  0.0072  123 ILE   B CD1 
1245 N N   . GLY   B 115 ? 0.7465 0.6588 0.4993 0.2139  0.0204  -0.0030 124 GLY   B N   
1246 C CA  . GLY   B 115 ? 0.7080 0.6288 0.4573 0.2258  0.0241  -0.0002 124 GLY   B CA  
1247 C C   . GLY   B 115 ? 0.6823 0.6253 0.4489 0.2225  0.0355  0.0079  124 GLY   B C   
1248 O O   . GLY   B 115 ? 0.6453 0.5941 0.4282 0.2084  0.0394  0.0099  124 GLY   B O   
1249 N N   . ALA   B 116 ? 0.6833 0.6385 0.4458 0.2354  0.0406  0.0128  125 ALA   B N   
1250 C CA  . ALA   B 116 ? 0.7020 0.6783 0.4793 0.2335  0.0511  0.0214  125 ALA   B CA  
1251 C C   . ALA   B 116 ? 0.7108 0.6912 0.4813 0.2448  0.0528  0.0234  125 ALA   B C   
1252 O O   . ALA   B 116 ? 0.7450 0.7187 0.4981 0.2592  0.0483  0.0205  125 ALA   B O   
1253 C CB  . ALA   B 116 ? 0.7118 0.7025 0.4917 0.2375  0.0566  0.0270  125 ALA   B CB  
1254 N N   A VAL   B 117 ? 0.7002 0.6905 0.4834 0.2388  0.0589  0.0282  126 VAL   B N   
1255 N N   B VAL   B 117 ? 0.6987 0.6896 0.4823 0.2387  0.0591  0.0284  126 VAL   B N   
1256 N N   C VAL   B 117 ? 0.7002 0.6905 0.4834 0.2388  0.0589  0.0282  126 VAL   B N   
1257 N N   D VAL   B 117 ? 0.6987 0.6896 0.4823 0.2387  0.0591  0.0284  126 VAL   B N   
1258 C CA  A VAL   B 117 ? 0.7203 0.7172 0.4990 0.2488  0.0620  0.0317  126 VAL   B CA  
1259 C CA  B VAL   B 117 ? 0.7166 0.7138 0.4963 0.2478  0.0623  0.0319  126 VAL   B CA  
1260 C CA  C VAL   B 117 ? 0.7203 0.7172 0.4990 0.2488  0.0620  0.0317  126 VAL   B CA  
1261 C CA  D VAL   B 117 ? 0.7166 0.7138 0.4963 0.2478  0.0623  0.0319  126 VAL   B CA  
1262 C C   A VAL   B 117 ? 0.7106 0.7296 0.4993 0.2500  0.0722  0.0421  126 VAL   B C   
1263 C C   B VAL   B 117 ? 0.7086 0.7279 0.4976 0.2498  0.0724  0.0423  126 VAL   B C   
1264 C C   C VAL   B 117 ? 0.7106 0.7296 0.4993 0.2500  0.0722  0.0421  126 VAL   B C   
1265 C C   D VAL   B 117 ? 0.7086 0.7279 0.4976 0.2498  0.0724  0.0423  126 VAL   B C   
1266 O O   A VAL   B 117 ? 0.6965 0.7235 0.5016 0.2371  0.0769  0.0462  126 VAL   B O   
1267 O O   B VAL   B 117 ? 0.6942 0.7220 0.4995 0.2372  0.0773  0.0466  126 VAL   B O   
1268 O O   C VAL   B 117 ? 0.6965 0.7235 0.5016 0.2371  0.0769  0.0462  126 VAL   B O   
1269 O O   D VAL   B 117 ? 0.6942 0.7220 0.4995 0.2372  0.0773  0.0466  126 VAL   B O   
1270 C CB  A VAL   B 117 ? 0.7231 0.7119 0.5065 0.2415  0.0596  0.0285  126 VAL   B CB  
1271 C CB  B VAL   B 117 ? 0.7156 0.7054 0.5021 0.2388  0.0603  0.0290  126 VAL   B CB  
1272 C CB  C VAL   B 117 ? 0.7231 0.7119 0.5065 0.2415  0.0596  0.0285  126 VAL   B CB  
1273 C CB  D VAL   B 117 ? 0.7156 0.7054 0.5021 0.2388  0.0603  0.0290  126 VAL   B CB  
1274 C CG1 A VAL   B 117 ? 0.7352 0.7038 0.5108 0.2381  0.0495  0.0188  126 VAL   B CG1 
1275 C CG1 B VAL   B 117 ? 0.7131 0.7148 0.5046 0.2417  0.0669  0.0356  126 VAL   B CG1 
1276 C CG1 C VAL   B 117 ? 0.7352 0.7038 0.5108 0.2381  0.0495  0.0188  126 VAL   B CG1 
1277 C CG1 D VAL   B 117 ? 0.7131 0.7148 0.5046 0.2417  0.0669  0.0356  126 VAL   B CG1 
1278 C CG2 A VAL   B 117 ? 0.7084 0.7059 0.5116 0.2264  0.0654  0.0328  126 VAL   B CG2 
1279 C CG2 B VAL   B 117 ? 0.7346 0.7052 0.5074 0.2428  0.0504  0.0199  126 VAL   B CG2 
1280 C CG2 C VAL   B 117 ? 0.7084 0.7059 0.5116 0.2264  0.0654  0.0328  126 VAL   B CG2 
1281 C CG2 D VAL   B 117 ? 0.7346 0.7052 0.5074 0.2428  0.0504  0.0199  126 VAL   B CG2 
1282 N N   . ALA   B 118 ? 0.7158 0.7444 0.4946 0.2649  0.0753  0.0463  127 ALA   B N   
1283 C CA  . ALA   B 118 ? 0.7340 0.7855 0.5207 0.2675  0.0850  0.0570  127 ALA   B CA  
1284 C C   . ALA   B 118 ? 0.7613 0.8199 0.5518 0.2680  0.0897  0.0626  127 ALA   B C   
1285 O O   . ALA   B 118 ? 0.7969 0.8637 0.5775 0.2816  0.0924  0.0664  127 ALA   B O   
1286 C CB  . ALA   B 118 ? 0.7387 0.7986 0.5120 0.2840  0.0858  0.0587  127 ALA   B CB  
1287 N N   . LEU   B 119 ? 0.7559 0.8102 0.5586 0.2547  0.0902  0.0625  128 LEU   B N   
1288 C CA  . LEU   B 119 ? 0.7617 0.8203 0.5675 0.2545  0.0938  0.0672  128 LEU   B CA  
1289 C C   . LEU   B 119 ? 0.7965 0.8661 0.6211 0.2403  0.1001  0.0746  128 LEU   B C   
1290 O O   . LEU   B 119 ? 0.8720 0.9381 0.7069 0.2282  0.0988  0.0722  128 LEU   B O   
1291 C CB  . LEU   B 119 ? 0.7629 0.8029 0.5632 0.2532  0.0866  0.0585  128 LEU   B CB  
1292 C CG  . LEU   B 119 ? 0.7498 0.7770 0.5310 0.2666  0.0792  0.0508  128 LEU   B CG  
1293 C CD1 . LEU   B 119 ? 0.7177 0.7265 0.4966 0.2616  0.0713  0.0417  128 LEU   B CD1 
1294 C CD2 . LEU   B 119 ? 0.7773 0.8124 0.5463 0.2827  0.0822  0.0552  128 LEU   B CD2 
1295 N N   . ASP   B 120 ? 0.8133 0.8959 0.6415 0.2419  0.1065  0.0837  129 ASP   B N   
1296 C CA  . ASP   B 120 ? 0.8463 0.9418 0.6908 0.2302  0.1129  0.0928  129 ASP   B CA  
1297 C C   . ASP   B 120 ? 0.7951 0.8837 0.6458 0.2220  0.1127  0.0933  129 ASP   B C   
1298 O O   . ASP   B 120 ? 0.8604 0.9500 0.7043 0.2293  0.1139  0.0960  129 ASP   B O   
1299 C CB  . ASP   B 120 ? 0.9157 1.0322 0.7594 0.2378  0.1201  0.1035  129 ASP   B CB  
1300 C CG  . ASP   B 120 ? 0.9848 1.1165 0.8435 0.2275  0.1256  0.1117  129 ASP   B CG  
1301 O OD1 . ASP   B 120 ? 0.9588 1.0841 0.8285 0.2145  0.1236  0.1087  129 ASP   B OD1 
1302 O OD2 . ASP   B 120 ? 1.1078 1.2585 0.9673 0.2326  0.1317  0.1212  129 ASP   B OD2 
1303 N N   . TYR   B 121 ? 0.7220 0.8034 0.5844 0.2081  0.1108  0.0903  130 TYR   B N   
1304 C CA  . TYR   B 121 ? 0.7190 0.7938 0.5874 0.2006  0.1102  0.0905  130 TYR   B CA  
1305 C C   . TYR   B 121 ? 0.6836 0.7623 0.5680 0.1857  0.1127  0.0947  130 TYR   B C   
1306 O O   . TYR   B 121 ? 0.7121 0.7948 0.6026 0.1804  0.1134  0.0948  130 TYR   B O   
1307 C CB  . TYR   B 121 ? 0.7261 0.7836 0.5893 0.2006  0.1030  0.0794  130 TYR   B CB  
1308 C CG  . TYR   B 121 ? 0.7939 0.8456 0.6415 0.2144  0.1000  0.0757  130 TYR   B CG  
1309 C CD1 . TYR   B 121 ? 0.8024 0.8531 0.6461 0.2187  0.1009  0.0783  130 TYR   B CD1 
1310 C CD2 . TYR   B 121 ? 0.8289 0.8750 0.6649 0.2233  0.0956  0.0693  130 TYR   B CD2 
1311 C CE1 . TYR   B 121 ? 0.8558 0.9009 0.6849 0.2316  0.0979  0.0746  130 TYR   B CE1 
1312 C CE2 . TYR   B 121 ? 0.8841 0.9238 0.7050 0.2363  0.0921  0.0655  130 TYR   B CE2 
1313 C CZ  . TYR   B 121 ? 0.9014 0.9410 0.7190 0.2405  0.0934  0.0682  130 TYR   B CZ  
1314 O OH  . TYR   B 121 ? 1.0368 1.0700 0.8395 0.2534  0.0899  0.0647  130 TYR   B OH  
1315 N N   . PRO   B 122 ? 0.6740 0.7506 0.5649 0.1787  0.1138  0.0982  131 PRO   B N   
1316 C CA  . PRO   B 122 ? 0.6817 0.7604 0.5869 0.1648  0.1154  0.1017  131 PRO   B CA  
1317 C C   . PRO   B 122 ? 0.6268 0.6958 0.5369 0.1571  0.1107  0.0923  131 PRO   B C   
1318 O O   . PRO   B 122 ? 0.6051 0.6637 0.5082 0.1611  0.1057  0.0830  131 PRO   B O   
1319 C CB  . PRO   B 122 ? 0.6925 0.7668 0.6001 0.1610  0.1157  0.1051  131 PRO   B CB  
1320 C CG  . PRO   B 122 ? 0.7123 0.7876 0.6073 0.1738  0.1165  0.1068  131 PRO   B CG  
1321 C CD  . PRO   B 122 ? 0.7293 0.8004 0.6139 0.1836  0.1130  0.0985  131 PRO   B CD  
1322 N N   . ALA   B 123 ? 0.6211 0.6939 0.5431 0.1461  0.1123  0.0953  132 ALA   B N   
1323 C CA  . ALA   B 123 ? 0.6101 0.6760 0.5387 0.1371  0.1089  0.0883  132 ALA   B CA  
1324 C C   . ALA   B 123 ? 0.5882 0.6405 0.5164 0.1339  0.1039  0.0797  132 ALA   B C   
1325 O O   . ALA   B 123 ? 0.5568 0.6013 0.4838 0.1320  0.0997  0.0710  132 ALA   B O   
1326 C CB  . ALA   B 123 ? 0.6247 0.6975 0.5659 0.1263  0.1118  0.0945  132 ALA   B CB  
1327 N N   . GLY   B 124 ? 0.5771 0.6268 0.5056 0.1336  0.1043  0.0822  133 GLY   B N   
1328 C CA  . GLY   B 124 ? 0.5408 0.5792 0.4696 0.1309  0.0999  0.0749  133 GLY   B CA  
1329 C C   . GLY   B 124 ? 0.5342 0.5654 0.4524 0.1394  0.0956  0.0667  133 GLY   B C   
1330 O O   . GLY   B 124 ? 0.4886 0.5113 0.4075 0.1369  0.0914  0.0595  133 GLY   B O   
1331 N N   . THR   B 125 ? 0.5102 0.5446 0.4189 0.1491  0.0961  0.0673  134 THR   B N   
1332 C CA  . THR   B 125 ? 0.5395 0.5659 0.4372 0.1573  0.0911  0.0590  134 THR   B CA  
1333 C C   . THR   B 125 ? 0.5443 0.5653 0.4430 0.1526  0.0870  0.0515  134 THR   B C   
1334 O O   . THR   B 125 ? 0.5570 0.5693 0.4474 0.1569  0.0816  0.0438  134 THR   B O   
1335 C CB  . THR   B 125 ? 0.5679 0.5991 0.4535 0.1706  0.0930  0.0628  134 THR   B CB  
1336 O OG1 . THR   B 125 ? 0.5713 0.6080 0.4557 0.1746  0.0969  0.0704  134 THR   B OG1 
1337 C CG2 . THR   B 125 ? 0.5663 0.5883 0.4389 0.1802  0.0875  0.0552  134 THR   B CG2 
1338 N N   . SER   B 126 ? 0.5256 0.5506 0.4334 0.1438  0.0890  0.0533  135 SER   B N   
1339 C CA  . SER   B 126 ? 0.5190 0.5388 0.4286 0.1378  0.0853  0.0468  135 SER   B CA  
1340 C C   . SER   B 126 ? 0.5085 0.5181 0.4179 0.1339  0.0796  0.0378  135 SER   B C   
1341 O O   . SER   B 126 ? 0.4915 0.5002 0.4079 0.1285  0.0797  0.0372  135 SER   B O   
1342 C CB  . SER   B 126 ? 0.5147 0.5397 0.4362 0.1274  0.0883  0.0501  135 SER   B CB  
1343 O OG  . SER   B 126 ? 0.5011 0.5362 0.4230 0.1304  0.0929  0.0578  135 SER   B OG  
1344 N N   . GLY   B 127 ? 0.4934 0.4957 0.3950 0.1365  0.0745  0.0312  136 GLY   B N   
1345 C CA  . GLY   B 127 ? 0.5166 0.5104 0.4183 0.1321  0.0688  0.0228  136 GLY   B CA  
1346 C C   . GLY   B 127 ? 0.5217 0.5092 0.4123 0.1413  0.0644  0.0188  136 GLY   B C   
1347 O O   . GLY   B 127 ? 0.5249 0.5051 0.4135 0.1385  0.0587  0.0116  136 GLY   B O   
1348 N N   . SER   B 128 ? 0.5419 0.5322 0.4248 0.1520  0.0669  0.0235  137 SER   B N   
1349 C CA  . SER   B 128 ? 0.5489 0.5333 0.4192 0.1628  0.0629  0.0204  137 SER   B CA  
1350 C C   . SER   B 128 ? 0.5240 0.4994 0.3848 0.1650  0.0566  0.0141  137 SER   B C   
1351 O O   . SER   B 128 ? 0.5369 0.5130 0.3945 0.1663  0.0572  0.0155  137 SER   B O   
1352 C CB  . SER   B 128 ? 0.5602 0.5507 0.4236 0.1740  0.0675  0.0274  137 SER   B CB  
1353 O OG  . SER   B 128 ? 0.5483 0.5457 0.4197 0.1713  0.0726  0.0334  137 SER   B OG  
1354 N N   . PRO   B 129 ? 0.5165 0.4830 0.3716 0.1663  0.0499  0.0071  138 PRO   B N   
1355 C CA  . PRO   B 129 ? 0.5364 0.4925 0.3817 0.1678  0.0428  0.0011  138 PRO   B CA  
1356 C C   . PRO   B 129 ? 0.5653 0.5169 0.3942 0.1820  0.0407  0.0016  138 PRO   B C   
1357 O O   . PRO   B 129 ? 0.5770 0.5309 0.3999 0.1920  0.0425  0.0043  138 PRO   B O   
1358 C CB  . PRO   B 129 ? 0.5322 0.4816 0.3778 0.1641  0.0364  -0.0058 138 PRO   B CB  
1359 C CG  . PRO   B 129 ? 0.5184 0.4731 0.3670 0.1682  0.0397  -0.0032 138 PRO   B CG  
1360 C CD  . PRO   B 129 ? 0.5140 0.4793 0.3714 0.1663  0.0483  0.0046  138 PRO   B CD  
1361 N N   . ILE   B 130 ? 0.5763 0.5197 0.3970 0.1827  0.0357  -0.0018 139 ILE   B N   
1362 C CA  . ILE   B 130 ? 0.6162 0.5523 0.4193 0.1961  0.0317  -0.0030 139 ILE   B CA  
1363 C C   . ILE   B 130 ? 0.6237 0.5447 0.4177 0.1954  0.0214  -0.0112 139 ILE   B C   
1364 O O   . ILE   B 130 ? 0.6102 0.5269 0.4106 0.1834  0.0179  -0.0149 139 ILE   B O   
1365 C CB  . ILE   B 130 ? 0.6251 0.5630 0.4254 0.1974  0.0336  -0.0004 139 ILE   B CB  
1366 C CG1 . ILE   B 130 ? 0.6448 0.5987 0.4550 0.1973  0.0435  0.0080  139 ILE   B CG1 
1367 C CG2 . ILE   B 130 ? 0.6425 0.5711 0.4234 0.2113  0.0281  -0.0028 139 ILE   B CG2 
1368 C CD1 . ILE   B 130 ? 0.6727 0.6292 0.4843 0.1946  0.0452  0.0099  139 ILE   B CD1 
1369 N N   . LEU   B 131 ? 0.6645 0.5786 0.4446 0.2073  0.0169  -0.0136 140 LEU   B N   
1370 C CA  . LEU   B 131 ? 0.7231 0.6230 0.4946 0.2071  0.0066  -0.0212 140 LEU   B CA  
1371 C C   . LEU   B 131 ? 0.7419 0.6285 0.4938 0.2180  -0.0006 -0.0244 140 LEU   B C   
1372 O O   . LEU   B 131 ? 0.7913 0.6811 0.5341 0.2306  0.0026  -0.0208 140 LEU   B O   
1373 C CB  . LEU   B 131 ? 0.7789 0.6804 0.5498 0.2123  0.0064  -0.0219 140 LEU   B CB  
1374 C CG  . LEU   B 131 ? 0.7968 0.7116 0.5839 0.2060  0.0142  -0.0178 140 LEU   B CG  
1375 C CD1 . LEU   B 131 ? 0.8073 0.7211 0.5916 0.2119  0.0122  -0.0197 140 LEU   B CD1 
1376 C CD2 . LEU   B 131 ? 0.7971 0.7145 0.5994 0.1895  0.0143  -0.0197 140 LEU   B CD2 
1377 N N   . ASP   B 132 ? 0.7683 0.6404 0.5135 0.2135  -0.0107 -0.0310 141 ASP   B N   
1378 C CA  . ASP   B 132 ? 0.8019 0.6572 0.5265 0.2238  -0.0205 -0.0357 141 ASP   B CA  
1379 C C   . ASP   B 132 ? 0.8646 0.7147 0.5822 0.2308  -0.0255 -0.0391 141 ASP   B C   
1380 O O   . ASP   B 132 ? 0.8620 0.7220 0.5915 0.2270  -0.0209 -0.0377 141 ASP   B O   
1381 C CB  . ASP   B 132 ? 0.7989 0.6403 0.5200 0.2139  -0.0294 -0.0406 141 ASP   B CB  
1382 C CG  . ASP   B 132 ? 0.8070 0.6440 0.5360 0.2005  -0.0354 -0.0452 141 ASP   B CG  
1383 O OD1 . ASP   B 132 ? 0.7809 0.6242 0.5168 0.1998  -0.0340 -0.0457 141 ASP   B OD1 
1384 O OD2 . ASP   B 132 ? 0.8567 0.6846 0.5851 0.1902  -0.0416 -0.0482 141 ASP   B OD2 
1385 N N   . LYS   B 133 ? 0.9348 0.7686 0.6334 0.2401  -0.0353 -0.0439 142 LYS   B N   
1386 C CA  . LYS   B 133 ? 0.9950 0.8223 0.6818 0.2517  -0.0404 -0.0469 142 LYS   B CA  
1387 C C   . LYS   B 133 ? 0.9516 0.7774 0.6478 0.2406  -0.0451 -0.0510 142 LYS   B C   
1388 O O   . LYS   B 133 ? 0.9418 0.7690 0.6357 0.2472  -0.0456 -0.0518 142 LYS   B O   
1389 C CB  . LYS   B 133 ? 1.0419 0.8509 0.7050 0.2644  -0.0505 -0.0512 142 LYS   B CB  
1390 C CG  . LYS   B 133 ? 1.1206 0.9342 0.7717 0.2819  -0.0452 -0.0472 142 LYS   B CG  
1391 C CD  . LYS   B 133 ? 1.1946 0.9934 0.8266 0.2908  -0.0524 -0.0499 142 LYS   B CD  
1392 C CE  . LYS   B 133 ? 1.2308 1.0401 0.8559 0.3059  -0.0446 -0.0446 142 LYS   B CE  
1393 N NZ  . LYS   B 133 ? 1.2635 1.0572 0.8643 0.3213  -0.0530 -0.0484 142 LYS   B NZ  
1394 N N   . CYS   B 134 ? 0.9365 0.7611 0.6436 0.2243  -0.0478 -0.0530 143 CYS   B N   
1395 C CA  . CYS   B 134 ? 0.9134 0.7381 0.6304 0.2123  -0.0525 -0.0570 143 CYS   B CA  
1396 C C   . CYS   B 134 ? 0.8343 0.6777 0.5726 0.2034  -0.0425 -0.0533 143 CYS   B C   
1397 O O   . CYS   B 134 ? 0.7837 0.6302 0.5326 0.1927  -0.0451 -0.0562 143 CYS   B O   
1398 C CB  . CYS   B 134 ? 0.9794 0.7932 0.6960 0.1995  -0.0612 -0.0610 143 CYS   B CB  
1399 S SG  . CYS   B 134 ? 1.0621 0.8505 0.7530 0.2083  -0.0759 -0.0664 143 CYS   B SG  
1400 N N   . GLY   B 135 ? 0.8223 0.6778 0.5660 0.2084  -0.0318 -0.0472 144 GLY   B N   
1401 C CA  . GLY   B 135 ? 0.8079 0.6798 0.5706 0.2003  -0.0223 -0.0433 144 GLY   B CA  
1402 C C   . GLY   B 135 ? 0.7749 0.6522 0.5518 0.1848  -0.0196 -0.0425 144 GLY   B C   
1403 O O   . GLY   B 135 ? 0.7451 0.6344 0.5373 0.1773  -0.0133 -0.0403 144 GLY   B O   
1404 N N   . ARG   B 136 ? 0.8006 0.6691 0.5722 0.1801  -0.0241 -0.0441 145 ARG   B N   
1405 C CA  . ARG   B 136 ? 0.7701 0.6436 0.5547 0.1652  -0.0215 -0.0432 145 ARG   B CA  
1406 C C   . ARG   B 136 ? 0.7302 0.6138 0.5209 0.1667  -0.0114 -0.0368 145 ARG   B C   
1407 O O   . ARG   B 136 ? 0.7142 0.5958 0.4939 0.1788  -0.0094 -0.0339 145 ARG   B O   
1408 C CB  . ARG   B 136 ? 0.8166 0.6757 0.5924 0.1594  -0.0312 -0.0474 145 ARG   B CB  
1409 C CG  . ARG   B 136 ? 0.8651 0.7188 0.6421 0.1515  -0.0399 -0.0529 145 ARG   B CG  
1410 C CD  . ARG   B 136 ? 0.9402 0.7783 0.7068 0.1460  -0.0498 -0.0564 145 ARG   B CD  
1411 N NE  . ARG   B 136 ? 1.0591 0.8840 0.8062 0.1604  -0.0538 -0.0567 145 ARG   B NE  
1412 C CZ  . ARG   B 136 ? 1.1094 0.9203 0.8437 0.1616  -0.0596 -0.0577 145 ARG   B CZ  
1413 N NH1 . ARG   B 136 ? 1.1660 0.9735 0.9047 0.1482  -0.0621 -0.0582 145 ARG   B NH1 
1414 N NH2 . ARG   B 136 ? 1.1455 0.9457 0.8617 0.1768  -0.0630 -0.0583 145 ARG   B NH2 
1415 N N   . VAL   B 137 ? 0.6729 0.5679 0.4802 0.1555  -0.0051 -0.0344 146 VAL   B N   
1416 C CA  . VAL   B 137 ? 0.6446 0.5496 0.4590 0.1556  0.0042  -0.0281 146 VAL   B CA  
1417 C C   . VAL   B 137 ? 0.6680 0.5660 0.4768 0.1527  0.0019  -0.0283 146 VAL   B C   
1418 O O   . VAL   B 137 ? 0.6655 0.5593 0.4785 0.1408  -0.0021 -0.0314 146 VAL   B O   
1419 C CB  . VAL   B 137 ? 0.6090 0.5273 0.4419 0.1456  0.0114  -0.0255 146 VAL   B CB  
1420 C CG1 . VAL   B 137 ? 0.5895 0.5168 0.4280 0.1464  0.0200  -0.0189 146 VAL   B CG1 
1421 C CG2 . VAL   B 137 ? 0.6352 0.5589 0.4725 0.1486  0.0129  -0.0258 146 VAL   B CG2 
1422 N N   . ILE   B 138 ? 0.6497 0.5472 0.4495 0.1631  0.0044  -0.0249 147 ILE   B N   
1423 C CA  . ILE   B 138 ? 0.6626 0.5538 0.4558 0.1625  0.0025  -0.0247 147 ILE   B CA  
1424 C C   . ILE   B 138 ? 0.6258 0.5299 0.4312 0.1580  0.0118  -0.0188 147 ILE   B C   
1425 O O   . ILE   B 138 ? 0.6166 0.5174 0.4184 0.1570  0.0112  -0.0182 147 ILE   B O   
1426 C CB  . ILE   B 138 ? 0.6728 0.5543 0.4463 0.1781  -0.0018 -0.0255 147 ILE   B CB  
1427 C CG1 . ILE   B 138 ? 0.6683 0.5605 0.4402 0.1911  0.0053  -0.0203 147 ILE   B CG1 
1428 C CG2 . ILE   B 138 ? 0.6762 0.5415 0.4367 0.1804  -0.0128 -0.0320 147 ILE   B CG2 
1429 C CD1 . ILE   B 138 ? 0.7332 0.6210 0.4885 0.2061  0.0039  -0.0193 147 ILE   B CD1 
1430 N N   . GLY   B 139 ? 0.5996 0.5172 0.4186 0.1552  0.0196  -0.0147 148 GLY   B N   
1431 C CA  . GLY   B 139 ? 0.5825 0.5118 0.4136 0.1498  0.0277  -0.0092 148 GLY   B CA  
1432 C C   . GLY   B 139 ? 0.5846 0.5270 0.4251 0.1521  0.0357  -0.0037 148 GLY   B C   
1433 O O   . GLY   B 139 ? 0.5694 0.5115 0.4063 0.1586  0.0349  -0.0044 148 GLY   B O   
1434 N N   . LEU   B 140 ? 0.5714 0.5242 0.4228 0.1473  0.0426  0.0015  149 LEU   B N   
1435 C CA  . LEU   B 140 ? 0.5680 0.5327 0.4291 0.1476  0.0500  0.0074  149 LEU   B CA  
1436 C C   . LEU   B 140 ? 0.5793 0.5529 0.4388 0.1547  0.0559  0.0144  149 LEU   B C   
1437 O O   . LEU   B 140 ? 0.5607 0.5340 0.4179 0.1544  0.0558  0.0151  149 LEU   B O   
1438 C CB  . LEU   B 140 ? 0.5691 0.5390 0.4461 0.1342  0.0528  0.0076  149 LEU   B CB  
1439 C CG  . LEU   B 140 ? 0.5741 0.5382 0.4549 0.1259  0.0477  0.0009  149 LEU   B CG  
1440 C CD1 . LEU   B 140 ? 0.5821 0.5535 0.4784 0.1151  0.0517  0.0021  149 LEU   B CD1 
1441 C CD2 . LEU   B 140 ? 0.5858 0.5450 0.4593 0.1326  0.0435  -0.0025 149 LEU   B CD2 
1442 N N   . TYR   B 141 ? 0.5441 0.5254 0.4045 0.1608  0.0605  0.0196  150 TYR   B N   
1443 C CA  . TYR   B 141 ? 0.5628 0.5555 0.4228 0.1680  0.0670  0.0276  150 TYR   B CA  
1444 C C   . TYR   B 141 ? 0.5592 0.5624 0.4345 0.1582  0.0733  0.0335  150 TYR   B C   
1445 O O   . TYR   B 141 ? 0.5555 0.5593 0.4400 0.1510  0.0743  0.0336  150 TYR   B O   
1446 C CB  . TYR   B 141 ? 0.5946 0.5899 0.4473 0.1791  0.0685  0.0304  150 TYR   B CB  
1447 C CG  . TYR   B 141 ? 0.5941 0.6032 0.4478 0.1855  0.0759  0.0397  150 TYR   B CG  
1448 C CD1 . TYR   B 141 ? 0.5926 0.6108 0.4573 0.1802  0.0816  0.0462  150 TYR   B CD1 
1449 C CD2 . TYR   B 141 ? 0.6277 0.6410 0.4710 0.1967  0.0768  0.0421  150 TYR   B CD2 
1450 C CE1 . TYR   B 141 ? 0.6173 0.6489 0.4830 0.1853  0.0882  0.0555  150 TYR   B CE1 
1451 C CE2 . TYR   B 141 ? 0.6132 0.6412 0.4575 0.2028  0.0837  0.0511  150 TYR   B CE2 
1452 C CZ  . TYR   B 141 ? 0.6465 0.6840 0.5024 0.1966  0.0895  0.0581  150 TYR   B CZ  
1453 O OH  . TYR   B 141 ? 0.6713 0.7240 0.5284 0.2018  0.0963  0.0677  150 TYR   B OH  
1454 N N   . GLY   B 142 ? 0.5552 0.5669 0.4329 0.1588  0.0773  0.0388  151 GLY   B N   
1455 C CA  . GLY   B 142 ? 0.5706 0.5934 0.4622 0.1509  0.0836  0.0459  151 GLY   B CA  
1456 C C   . GLY   B 142 ? 0.5671 0.5938 0.4654 0.1440  0.0850  0.0472  151 GLY   B C   
1457 O O   . GLY   B 142 ? 0.5676 0.6035 0.4773 0.1374  0.0899  0.0534  151 GLY   B O   
1458 N N   . ASN   B 143 ? 0.5537 0.5739 0.4447 0.1459  0.0809  0.0424  152 ASN   B N   
1459 C CA  . ASN   B 143 ? 0.5393 0.5643 0.4353 0.1413  0.0826  0.0445  152 ASN   B CA  
1460 C C   . ASN   B 143 ? 0.5261 0.5529 0.4100 0.1531  0.0818  0.0451  152 ASN   B C   
1461 O O   . ASN   B 143 ? 0.5330 0.5485 0.4050 0.1584  0.0760  0.0389  152 ASN   B O   
1462 C CB  . ASN   B 143 ? 0.5285 0.5441 0.4287 0.1303  0.0785  0.0383  152 ASN   B CB  
1463 C CG  . ASN   B 143 ? 0.5393 0.5606 0.4478 0.1232  0.0810  0.0411  152 ASN   B CG  
1464 O OD1 . ASN   B 143 ? 0.5771 0.6108 0.4942 0.1217  0.0866  0.0483  152 ASN   B OD1 
1465 N ND2 . ASN   B 143 ? 0.5166 0.5288 0.4224 0.1186  0.0765  0.0355  152 ASN   B ND2 
1466 N N   . GLY   B 144 ? 0.5267 0.5677 0.4143 0.1564  0.0873  0.0525  153 GLY   B N   
1467 C CA  . GLY   B 144 ? 0.5698 0.6155 0.4471 0.1681  0.0873  0.0538  153 GLY   B CA  
1468 C C   . GLY   B 144 ? 0.5975 0.6619 0.4834 0.1683  0.0943  0.0629  153 GLY   B C   
1469 O O   . GLY   B 144 ? 0.6005 0.6697 0.5001 0.1566  0.0967  0.0657  153 GLY   B O   
1470 N N   . VAL   B 145 ? 0.6540 0.7291 0.5323 0.1813  0.0971  0.0674  154 VAL   B N   
1471 C CA  . VAL   B 145 ? 0.6710 0.7644 0.5538 0.1846  0.1024  0.0750  154 VAL   B CA  
1472 C C   . VAL   B 145 ? 0.7474 0.8568 0.6292 0.1934  0.1083  0.0833  154 VAL   B C   
1473 O O   . VAL   B 145 ? 0.7294 0.8338 0.6004 0.2026  0.1068  0.0814  154 VAL   B O   
1474 C CB  . VAL   B 145 ? 0.7003 0.7888 0.5718 0.1925  0.0982  0.0699  154 VAL   B CB  
1475 C CG1 . VAL   B 145 ? 0.6732 0.7617 0.5270 0.2105  0.0964  0.0684  154 VAL   B CG1 
1476 C CG2 . VAL   B 145 ? 0.7467 0.8479 0.6275 0.1882  0.1014  0.0744  154 VAL   B CG2 
1477 N N   . VAL   B 146 ? 0.7897 0.9180 0.6824 0.1902  0.1146  0.0926  155 VAL   B N   
1478 C CA  . VAL   B 146 ? 0.8437 0.9913 0.7360 0.1987  0.1209  0.1021  155 VAL   B CA  
1479 C C   . VAL   B 146 ? 0.8745 1.0327 0.7571 0.2126  0.1215  0.1027  155 VAL   B C   
1480 O O   . VAL   B 146 ? 0.8776 1.0358 0.7627 0.2098  0.1198  0.1004  155 VAL   B O   
1481 C CB  . VAL   B 146 ? 0.8446 1.0063 0.7543 0.1864  0.1267  0.1119  155 VAL   B CB  
1482 C CG1 . VAL   B 146 ? 0.8666 1.0511 0.7775 0.1935  0.1335  0.1229  155 VAL   B CG1 
1483 C CG2 . VAL   B 146 ? 0.8366 0.9865 0.7526 0.1757  0.1256  0.1108  155 VAL   B CG2 
1484 N N   . ILE   B 147 ? 0.9321 1.0974 0.8026 0.2277  0.1230  0.1047  156 ILE   B N   
1485 C CA  . ILE   B 147 ? 0.9833 1.1535 0.8399 0.2438  0.1215  0.1023  156 ILE   B CA  
1486 C C   . ILE   B 147 ? 1.0348 1.2332 0.8954 0.2507  0.1292  0.1131  156 ILE   B C   
1487 O O   . ILE   B 147 ? 0.9661 1.1781 0.8387 0.2434  0.1351  0.1223  156 ILE   B O   
1488 C CB  . ILE   B 147 ? 1.0184 1.1729 0.8552 0.2576  0.1158  0.0944  156 ILE   B CB  
1489 C CG1 . ILE   B 147 ? 1.0221 1.1760 0.8562 0.2603  0.1179  0.0971  156 ILE   B CG1 
1490 C CG2 . ILE   B 147 ? 1.0014 1.1303 0.8321 0.2528  0.1071  0.0831  156 ILE   B CG2 
1491 C CD1 . ILE   B 147 ? 0.9968 1.1437 0.8106 0.2782  0.1142  0.0923  156 ILE   B CD1 
1492 N N   A LYS   B 148 ? 1.0774 1.2842 0.9279 0.2645  0.1287  0.1120  157 LYS   B N   
1493 N N   B LYS   B 148 ? 1.0774 1.2842 0.9279 0.2645  0.1287  0.1120  157 LYS   B N   
1494 N N   C LYS   B 148 ? 1.0716 1.2784 0.9222 0.2645  0.1286  0.1120  157 LYS   B N   
1495 N N   D LYS   B 148 ? 1.0716 1.2784 0.9222 0.2645  0.1286  0.1120  157 LYS   B N   
1496 C CA  A LYS   B 148 ? 1.1172 1.3529 0.9697 0.2738  0.1356  0.1216  157 LYS   B CA  
1497 C CA  B LYS   B 148 ? 1.1172 1.3529 0.9697 0.2738  0.1356  0.1216  157 LYS   B CA  
1498 C CA  C LYS   B 148 ? 1.1070 1.3427 0.9601 0.2733  0.1356  0.1216  157 LYS   B CA  
1499 C CA  D LYS   B 148 ? 1.1070 1.3427 0.9601 0.2733  0.1356  0.1216  157 LYS   B CA  
1500 C C   A LYS   B 148 ? 1.1270 1.3778 0.9856 0.2724  0.1424  0.1317  157 LYS   B C   
1501 C C   B LYS   B 148 ? 1.1270 1.3778 0.9856 0.2724  0.1424  0.1317  157 LYS   B C   
1502 C C   C LYS   B 148 ? 1.1196 1.3712 0.9781 0.2728  0.1425  0.1317  157 LYS   B C   
1503 C C   D LYS   B 148 ? 1.1196 1.3712 0.9781 0.2728  0.1425  0.1317  157 LYS   B C   
1504 O O   A LYS   B 148 ? 1.1399 1.4122 1.0132 0.2650  0.1489  0.1421  157 LYS   B O   
1505 O O   B LYS   B 148 ? 1.1399 1.4122 1.0132 0.2650  0.1489  0.1421  157 LYS   B O   
1506 O O   C LYS   B 148 ? 1.1332 1.4079 1.0051 0.2673  0.1492  0.1423  157 LYS   B O   
1507 O O   D LYS   B 148 ? 1.1332 1.4079 1.0051 0.2673  0.1492  0.1423  157 LYS   B O   
1508 C CB  A LYS   B 148 ? 1.1494 1.3865 0.9823 0.2948  0.1329  0.1170  157 LYS   B CB  
1509 C CB  B LYS   B 148 ? 1.1494 1.3865 0.9823 0.2948  0.1329  0.1170  157 LYS   B CB  
1510 C CB  C LYS   B 148 ? 1.1326 1.3699 0.9665 0.2939  0.1328  0.1169  157 LYS   B CB  
1511 C CB  D LYS   B 148 ? 1.1326 1.3699 0.9665 0.2939  0.1328  0.1169  157 LYS   B CB  
1512 C CG  A LYS   B 148 ? 1.1662 1.3937 0.9924 0.2984  0.1270  0.1091  157 LYS   B CG  
1513 C CG  B LYS   B 148 ? 1.1662 1.3937 0.9924 0.2984  0.1270  0.1091  157 LYS   B CG  
1514 C CG  C LYS   B 148 ? 1.1423 1.3653 0.9692 0.2959  0.1258  0.1076  157 LYS   B CG  
1515 C CG  D LYS   B 148 ? 1.1423 1.3653 0.9692 0.2959  0.1258  0.1076  157 LYS   B CG  
1516 C CD  A LYS   B 148 ? 1.1948 1.4177 0.9987 0.3196  0.1225  0.1029  157 LYS   B CD  
1517 C CD  B LYS   B 148 ? 1.1948 1.4177 0.9987 0.3196  0.1225  0.1029  157 LYS   B CD  
1518 C CD  C LYS   B 148 ? 1.1648 1.3876 0.9711 0.3171  0.1223  0.1028  157 LYS   B CD  
1519 C CD  D LYS   B 148 ? 1.1648 1.3876 0.9711 0.3171  0.1223  0.1028  157 LYS   B CD  
1520 C CE  A LYS   B 148 ? 1.2110 1.4621 1.0108 0.3353  0.1291  0.1109  157 LYS   B CE  
1521 C CE  B LYS   B 148 ? 1.2110 1.4621 1.0108 0.3353  0.1291  0.1109  157 LYS   B CE  
1522 C CE  C LYS   B 148 ? 1.1685 1.3826 0.9694 0.3193  0.1166  0.0960  157 LYS   B CE  
1523 C CE  D LYS   B 148 ? 1.1685 1.3826 0.9694 0.3193  0.1166  0.0960  157 LYS   B CE  
1524 N NZ  A LYS   B 148 ? 1.2089 1.4816 1.0161 0.3370  0.1325  0.1155  157 LYS   B NZ  
1525 N NZ  B LYS   B 148 ? 1.2089 1.4816 1.0161 0.3370  0.1325  0.1155  157 LYS   B NZ  
1526 N NZ  C LYS   B 148 ? 1.1857 1.4066 0.9685 0.3410  0.1148  0.0936  157 LYS   B NZ  
1527 N NZ  D LYS   B 148 ? 1.1857 1.4066 0.9685 0.3410  0.1148  0.0936  157 LYS   B NZ  
1528 N N   A ASN   B 149 ? 1.1400 1.3789 0.9876 0.2789  0.1405  0.1285  158 ASN   B N   
1529 N N   B ASN   B 149 ? 1.1400 1.3789 0.9876 0.2789  0.1405  0.1285  158 ASN   B N   
1530 N N   C ASN   B 149 ? 1.1349 1.3739 0.9832 0.2782  0.1405  0.1286  158 ASN   B N   
1531 N N   D ASN   B 149 ? 1.1349 1.3739 0.9832 0.2782  0.1405  0.1286  158 ASN   B N   
1532 C CA  A ASN   B 149 ? 1.1399 1.3896 0.9892 0.2800  0.1461  0.1369  158 ASN   B CA  
1533 C CA  B ASN   B 149 ? 1.1399 1.3896 0.9892 0.2800  0.1461  0.1369  158 ASN   B CA  
1534 C CA  C ASN   B 149 ? 1.1374 1.3878 0.9872 0.2798  0.1462  0.1371  158 ASN   B CA  
1535 C CA  D ASN   B 149 ? 1.1374 1.3878 0.9872 0.2798  0.1462  0.1371  158 ASN   B CA  
1536 C C   A ASN   B 149 ? 1.1150 1.3664 0.9832 0.2604  0.1493  0.1435  158 ASN   B C   
1537 C C   B ASN   B 149 ? 1.1150 1.3664 0.9832 0.2604  0.1493  0.1435  158 ASN   B C   
1538 C C   C ASN   B 149 ? 1.1136 1.3651 0.9819 0.2603  0.1493  0.1436  158 ASN   B C   
1539 C C   D ASN   B 149 ? 1.1136 1.3651 0.9819 0.2603  0.1493  0.1436  158 ASN   B C   
1540 O O   A ASN   B 149 ? 1.1170 1.3901 0.9949 0.2570  0.1562  0.1552  158 ASN   B O   
1541 O O   B ASN   B 149 ? 1.1170 1.3901 0.9949 0.2570  0.1562  0.1552  158 ASN   B O   
1542 O O   C ASN   B 149 ? 1.1157 1.3887 0.9936 0.2570  0.1562  0.1553  158 ASN   B O   
1543 O O   D ASN   B 149 ? 1.1157 1.3887 0.9936 0.2570  0.1562  0.1553  158 ASN   B O   
1544 C CB  A ASN   B 149 ? 1.1635 1.3945 0.9968 0.2893  0.1415  0.1299  158 ASN   B CB  
1545 C CB  B ASN   B 149 ? 1.1635 1.3945 0.9968 0.2893  0.1415  0.1299  158 ASN   B CB  
1546 C CB  C ASN   B 149 ? 1.1639 1.3965 0.9970 0.2902  0.1418  0.1303  158 ASN   B CB  
1547 C CB  D ASN   B 149 ? 1.1639 1.3965 0.9970 0.2902  0.1418  0.1303  158 ASN   B CB  
1548 C CG  A ASN   B 149 ? 1.1746 1.3896 0.9899 0.3026  0.1340  0.1185  158 ASN   B CG  
1549 C CG  B ASN   B 149 ? 1.1746 1.3896 0.9899 0.3026  0.1340  0.1185  158 ASN   B CG  
1550 C CG  C ASN   B 149 ? 1.1800 1.4030 0.9937 0.3072  0.1359  0.1210  158 ASN   B CG  
1551 C CG  D ASN   B 149 ? 1.1800 1.4030 0.9937 0.3072  0.1359  0.1210  158 ASN   B CG  
1552 O OD1 A ASN   B 149 ? 1.1817 1.4023 0.9942 0.3081  0.1329  0.1167  158 ASN   B OD1 
1553 O OD1 B ASN   B 149 ? 1.1817 1.4023 0.9942 0.3081  0.1329  0.1167  158 ASN   B OD1 
1554 O OD1 C ASN   B 149 ? 1.1925 1.4284 1.0027 0.3160  0.1370  0.1220  158 ASN   B OD1 
1555 O OD1 D ASN   B 149 ? 1.1925 1.4284 1.0027 0.3160  0.1370  0.1220  158 ASN   B OD1 
1556 N ND2 A ASN   B 149 ? 1.1865 1.3809 0.9891 0.3078  0.1283  0.1108  158 ASN   B ND2 
1557 N ND2 B ASN   B 149 ? 1.1865 1.3809 0.9891 0.3078  0.1283  0.1108  158 ASN   B ND2 
1558 N ND2 C ASN   B 149 ? 1.1903 1.3904 0.9908 0.3121  0.1293  0.1119  158 ASN   B ND2 
1559 N ND2 D ASN   B 149 ? 1.1903 1.3904 0.9908 0.3121  0.1293  0.1119  158 ASN   B ND2 
1560 N N   . GLY   B 150 ? 1.1065 1.3357 0.9792 0.2482  0.1441  0.1363  159 GLY   B N   
1561 C CA  . GLY   B 150 ? 1.0337 1.2592 0.9214 0.2308  0.1456  0.1406  159 GLY   B CA  
1562 C C   . GLY   B 150 ? 0.9909 1.1926 0.8731 0.2279  0.1406  0.1329  159 GLY   B C   
1563 O O   . GLY   B 150 ? 0.9184 1.1124 0.8116 0.2137  0.1402  0.1337  159 GLY   B O   
1564 N N   A SER   B 151 ? 0.9928 1.1831 0.8582 0.2413  0.1364  0.1254  160 SER   B N   
1565 N N   B SER   B 151 ? 0.9964 1.1869 0.8618 0.2414  0.1364  0.1254  160 SER   B N   
1566 N N   C SER   B 151 ? 0.9928 1.1831 0.8582 0.2413  0.1364  0.1254  160 SER   B N   
1567 N N   D SER   B 151 ? 0.9964 1.1869 0.8618 0.2414  0.1364  0.1254  160 SER   B N   
1568 C CA  A SER   B 151 ? 0.9724 1.1395 0.8307 0.2404  0.1305  0.1165  160 SER   B CA  
1569 C CA  B SER   B 151 ? 0.9786 1.1458 0.8364 0.2410  0.1304  0.1163  160 SER   B CA  
1570 C CA  C SER   B 151 ? 0.9724 1.1395 0.8307 0.2404  0.1305  0.1165  160 SER   B CA  
1571 C CA  D SER   B 151 ? 0.9786 1.1458 0.8364 0.2410  0.1304  0.1163  160 SER   B CA  
1572 C C   A SER   B 151 ? 0.9457 1.0944 0.8078 0.2302  0.1242  0.1070  160 SER   B C   
1573 C C   B SER   B 151 ? 0.9487 1.0975 0.8108 0.2302  0.1241  0.1070  160 SER   B C   
1574 C C   C SER   B 151 ? 0.9457 1.0944 0.8078 0.2302  0.1242  0.1070  160 SER   B C   
1575 C C   D SER   B 151 ? 0.9487 1.0975 0.8108 0.2302  0.1241  0.1070  160 SER   B C   
1576 O O   A SER   B 151 ? 0.9193 1.0724 0.7863 0.2268  0.1240  0.1066  160 SER   B O   
1577 O O   B SER   B 151 ? 0.9213 1.0744 0.7887 0.2264  0.1241  0.1066  160 SER   B O   
1578 O O   C SER   B 151 ? 0.9193 1.0724 0.7863 0.2268  0.1240  0.1066  160 SER   B O   
1579 O O   D SER   B 151 ? 0.9213 1.0744 0.7887 0.2264  0.1241  0.1066  160 SER   B O   
1580 C CB  A SER   B 151 ? 0.9848 1.1463 0.8239 0.2580  0.1275  0.1116  160 SER   B CB  
1581 C CB  B SER   B 151 ? 0.9946 1.1566 0.8330 0.2589  0.1273  0.1113  160 SER   B CB  
1582 C CB  C SER   B 151 ? 0.9848 1.1463 0.8239 0.2580  0.1275  0.1116  160 SER   B CB  
1583 C CB  D SER   B 151 ? 0.9946 1.1566 0.8330 0.2589  0.1273  0.1113  160 SER   B CB  
1584 O OG  A SER   B 151 ? 0.9921 1.1358 0.8259 0.2570  0.1232  0.1059  160 SER   B OG  
1585 O OG  B SER   B 151 ? 1.0110 1.1819 0.8420 0.2698  0.1273  0.1106  160 SER   B OG  
1586 O OG  C SER   B 151 ? 0.9921 1.1358 0.8259 0.2570  0.1232  0.1059  160 SER   B OG  
1587 O OG  D SER   B 151 ? 1.0110 1.1819 0.8420 0.2698  0.1273  0.1106  160 SER   B OG  
1588 N N   . TYR   B 152 ? 0.9315 1.0612 0.7912 0.2258  0.1191  0.0998  161 TYR   B N   
1589 C CA  . TYR   B 152 ? 0.9118 1.0238 0.7752 0.2153  0.1131  0.0908  161 TYR   B CA  
1590 C C   . TYR   B 152 ? 0.8483 0.9432 0.6956 0.2245  0.1055  0.0803  161 TYR   B C   
1591 O O   . TYR   B 152 ? 0.7983 0.8870 0.6349 0.2332  0.1035  0.0779  161 TYR   B O   
1592 C CB  . TYR   B 152 ? 0.9187 1.0215 0.7916 0.2028  0.1123  0.0898  161 TYR   B CB  
1593 C CG  . TYR   B 152 ? 0.9458 1.0367 0.8268 0.1897  0.1082  0.0833  161 TYR   B CG  
1594 C CD1 . TYR   B 152 ? 0.9331 1.0317 0.8267 0.1796  0.1109  0.0871  161 TYR   B CD1 
1595 C CD2 . TYR   B 152 ? 0.9569 1.0296 0.8330 0.1874  0.1016  0.0736  161 TYR   B CD2 
1596 C CE1 . TYR   B 152 ? 0.9122 1.0006 0.8128 0.1681  0.1074  0.0814  161 TYR   B CE1 
1597 C CE2 . TYR   B 152 ? 0.9548 1.0182 0.8383 0.1755  0.0982  0.0682  161 TYR   B CE2 
1598 C CZ  . TYR   B 152 ? 0.9392 1.0102 0.8346 0.1660  0.1012  0.0720  161 TYR   B CZ  
1599 O OH  . TYR   B 152 ? 0.9378 1.0006 0.8406 0.1544  0.0983  0.0671  161 TYR   B OH  
1600 N N   . VAL   B 153 ? 0.7800 0.8659 0.6261 0.2211  0.1010  0.0741  162 VAL   B N   
1601 C CA  . VAL   B 153 ? 0.7354 0.8017 0.5678 0.2259  0.0924  0.0635  162 VAL   B CA  
1602 C C   . VAL   B 153 ? 0.6818 0.7342 0.5226 0.2108  0.0881  0.0574  162 VAL   B C   
1603 O O   . VAL   B 153 ? 0.6238 0.6795 0.4738 0.2021  0.0892  0.0583  162 VAL   B O   
1604 C CB  . VAL   B 153 ? 0.7171 0.7849 0.5379 0.2372  0.0903  0.0617  162 VAL   B CB  
1605 C CG1 . VAL   B 153 ? 0.7076 0.7549 0.5113 0.2445  0.0810  0.0516  162 VAL   B CG1 
1606 C CG2 . VAL   B 153 ? 0.7884 0.8758 0.6051 0.2503  0.0964  0.0695  162 VAL   B CG2 
1607 N N   . SER   B 154 ? 0.6702 0.7074 0.5063 0.2089  0.0826  0.0507  163 SER   B N   
1608 C CA  . SER   B 154 ? 0.6444 0.6695 0.4883 0.1950  0.0786  0.0449  163 SER   B CA  
1609 C C   . SER   B 154 ? 0.6233 0.6317 0.4549 0.1973  0.0701  0.0361  163 SER   B C   
1610 O O   . SER   B 154 ? 0.6245 0.6256 0.4409 0.2092  0.0659  0.0328  163 SER   B O   
1611 C CB  . SER   B 154 ? 0.6219 0.6432 0.4703 0.1905  0.0784  0.0440  163 SER   B CB  
1612 O OG  . SER   B 154 ? 0.6046 0.6126 0.4563 0.1800  0.0729  0.0366  163 SER   B OG  
1613 N N   . ALA   B 155 ? 0.5719 0.5735 0.4098 0.1858  0.0675  0.0325  164 ALA   B N   
1614 C CA  . ALA   B 155 ? 0.5716 0.5554 0.3998 0.1841  0.0588  0.0240  164 ALA   B CA  
1615 C C   . ALA   B 155 ? 0.5935 0.5677 0.4190 0.1829  0.0546  0.0194  164 ALA   B C   
1616 O O   . ALA   B 155 ? 0.6073 0.5882 0.4438 0.1774  0.0587  0.0221  164 ALA   B O   
1617 C CB  . ALA   B 155 ? 0.5751 0.5557 0.4128 0.1703  0.0578  0.0221  164 ALA   B CB  
1618 N N   . ILE   B 156 ? 0.6028 0.5614 0.4147 0.1869  0.0462  0.0125  165 ILE   B N   
1619 C CA  . ILE   B 156 ? 0.6087 0.5554 0.4202 0.1803  0.0402  0.0063  165 ILE   B CA  
1620 C C   . ILE   B 156 ? 0.5928 0.5350 0.4141 0.1647  0.0382  0.0034  165 ILE   B C   
1621 O O   . ILE   B 156 ? 0.6022 0.5318 0.4153 0.1625  0.0315  -0.0013 165 ILE   B O   
1622 C CB  . ILE   B 156 ? 0.6430 0.5746 0.4355 0.1907  0.0314  0.0005  165 ILE   B CB  
1623 C CG1 . ILE   B 156 ? 0.6738 0.6112 0.4555 0.2076  0.0340  0.0039  165 ILE   B CG1 
1624 C CG2 . ILE   B 156 ? 0.6326 0.5541 0.4256 0.1843  0.0255  -0.0051 165 ILE   B CG2 
1625 C CD1 . ILE   B 156 ? 0.7129 0.6354 0.4748 0.2194  0.0254  -0.0016 165 ILE   B CD1 
1626 N N   . THR   B 157 ? 0.5859 0.5374 0.4237 0.1540  0.0436  0.0061  166 THR   B N   
1627 C CA  . THR   B 157 ? 0.5590 0.5087 0.4075 0.1392  0.0428  0.0039  166 THR   B CA  
1628 C C   . THR   B 157 ? 0.5804 0.5210 0.4292 0.1322  0.0369  -0.0022 166 THR   B C   
1629 O O   . THR   B 157 ? 0.5668 0.5125 0.4226 0.1309  0.0391  -0.0018 166 THR   B O   
1630 C CB  . THR   B 157 ? 0.5773 0.5407 0.4423 0.1319  0.0508  0.0094  166 THR   B CB  
1631 O OG1 . THR   B 157 ? 0.5536 0.5258 0.4175 0.1387  0.0556  0.0152  166 THR   B OG1 
1632 C CG2 . THR   B 157 ? 0.5644 0.5265 0.4400 0.1175  0.0502  0.0071  166 THR   B CG2 
1633 N N   . GLN   B 158 ? 0.5587 0.4873 0.4012 0.1272  0.0298  -0.0073 167 GLN   B N   
1634 C CA  . GLN   B 158 ? 0.5802 0.5006 0.4234 0.1185  0.0236  -0.0131 167 GLN   B CA  
1635 C C   . GLN   B 158 ? 0.6090 0.5296 0.4617 0.1041  0.0235  -0.0142 167 GLN   B C   
1636 O O   . GLN   B 158 ? 0.6015 0.5211 0.4528 0.1029  0.0245  -0.0126 167 GLN   B O   
1637 C CB  . GLN   B 158 ? 0.5928 0.4979 0.4186 0.1254  0.0145  -0.0177 167 GLN   B CB  
1638 C CG  . GLN   B 158 ? 0.5891 0.4860 0.4141 0.1180  0.0073  -0.0233 167 GLN   B CG  
1639 C CD  . GLN   B 158 ? 0.6014 0.5072 0.4361 0.1170  0.0102  -0.0233 167 GLN   B CD  
1640 O OE1 . GLN   B 158 ? 0.5687 0.4866 0.4181 0.1107  0.0169  -0.0207 167 GLN   B OE1 
1641 N NE2 . GLN   B 158 ? 0.6013 0.5000 0.4271 0.1229  0.0044  -0.0268 167 GLN   B NE2 
1642 N N   . GLY   B 159 ? 0.6420 0.5648 0.5040 0.0941  0.0226  -0.0169 168 GLY   B N   
1643 C CA  . GLY   B 159 ? 0.6851 0.6079 0.5551 0.0802  0.0215  -0.0188 168 GLY   B CA  
1644 C C   . GLY   B 159 ? 0.7498 0.6591 0.6101 0.0756  0.0123  -0.0238 168 GLY   B C   
1645 O O   . GLY   B 159 ? 0.8137 0.7134 0.6616 0.0830  0.0064  -0.0262 168 GLY   B O   
1646 N N   . LYS   B 160 ? 0.8557 0.7639 0.7209 0.0636  0.0109  -0.0251 169 LYS   B N   
1647 C CA  . LYS   B 160 ? 0.8966 0.7935 0.7552 0.0555  0.0024  -0.0293 169 LYS   B CA  
1648 C C   . LYS   B 160 ? 0.9287 0.8329 0.7975 0.0473  0.0016  -0.0319 169 LYS   B C   
1649 O O   . LYS   B 160 ? 0.8583 0.7759 0.7412 0.0429  0.0082  -0.0304 169 LYS   B O   
1650 C CB  . LYS   B 160 ? 0.9566 0.8499 0.8154 0.0471  0.0021  -0.0285 169 LYS   B CB  
1651 C CG  . LYS   B 160 ? 1.0430 0.9214 0.8909 0.0407  -0.0073 -0.0318 169 LYS   B CG  
1652 C CD  . LYS   B 160 ? 1.0670 0.9433 0.9173 0.0295  -0.0075 -0.0312 169 LYS   B CD  
1653 C CE  . LYS   B 160 ? 1.0710 0.9351 0.9136 0.0200  -0.0168 -0.0342 169 LYS   B CE  
1654 N NZ  . LYS   B 160 ? 1.1258 0.9892 0.9717 0.0084  -0.0164 -0.0333 169 LYS   B NZ  
1655 N N   . ARG   B 161 ? 0.9666 0.8626 0.8283 0.0458  -0.0063 -0.0357 170 ARG   B N   
1656 C CA  . ARG   B 161 ? 1.0206 0.9230 0.8910 0.0361  -0.0087 -0.0386 170 ARG   B CA  
1657 C C   . ARG   B 161 ? 1.0836 0.9802 0.9527 0.0230  -0.0140 -0.0400 170 ARG   B C   
1658 O O   . ARG   B 161 ? 1.0982 0.9792 0.9532 0.0243  -0.0206 -0.0406 170 ARG   B O   
1659 C CB  . ARG   B 161 ? 1.0208 0.9186 0.8843 0.0432  -0.0143 -0.0415 170 ARG   B CB  
1660 C CG  . ARG   B 161 ? 0.9993 0.9050 0.8715 0.0355  -0.0168 -0.0446 170 ARG   B CG  
1661 C CD  . ARG   B 161 ? 1.0233 0.9219 0.8867 0.0417  -0.0241 -0.0478 170 ARG   B CD  
1662 N NE  . ARG   B 161 ? 1.0087 0.9156 0.8809 0.0334  -0.0272 -0.0508 170 ARG   B NE  
1663 C CZ  . ARG   B 161 ? 0.9769 0.8932 0.8555 0.0375  -0.0256 -0.0523 170 ARG   B CZ  
1664 N NH1 . ARG   B 161 ? 0.9018 0.8200 0.7790 0.0497  -0.0210 -0.0510 170 ARG   B NH1 
1665 N NH2 . ARG   B 161 ? 0.9996 0.9240 0.8861 0.0290  -0.0288 -0.0551 170 ARG   B NH2 
1666 N N   . GLU   B 162 ? 1.1323 1.0403 1.0144 0.0112  -0.0113 -0.0402 171 GLU   B N   
1667 C CA  . GLU   B 162 ? 1.1866 1.0916 1.0690 -0.0025 -0.0157 -0.0411 171 GLU   B CA  
1668 C C   . GLU   B 162 ? 1.1428 1.0514 1.0283 -0.0099 -0.0215 -0.0441 171 GLU   B C   
1669 O O   . GLU   B 162 ? 1.1893 1.0907 1.0698 -0.0193 -0.0286 -0.0452 171 GLU   B O   
1670 C CB  . GLU   B 162 ? 1.2516 1.1683 1.1464 -0.0106 -0.0084 -0.0389 171 GLU   B CB  
1671 C CG  . GLU   B 162 ? 1.2914 1.2069 1.1855 -0.0042 -0.0022 -0.0357 171 GLU   B CG  
1672 C CD  . GLU   B 162 ? 1.3384 1.2440 1.2255 -0.0094 -0.0042 -0.0343 171 GLU   B CD  
1673 O OE1 . GLU   B 162 ? 1.2915 1.2036 1.1858 -0.0121 0.0017  -0.0320 171 GLU   B OE1 
1674 O OE2 . GLU   B 162 ? 1.3606 1.2512 1.2345 -0.0105 -0.0123 -0.0355 171 GLU   B OE2 
1675 S S   A DMS   C .   ? 0.8069 0.8876 0.7198 0.1561  0.1109  0.0889  201 DMS   B S   
1676 S S   B DMS   C .   ? 0.8064 0.8872 0.7194 0.1562  0.1109  0.0889  201 DMS   B S   
1677 O O   A DMS   C .   ? 0.7995 0.8959 0.7102 0.1634  0.1155  0.0963  201 DMS   B O   
1678 O O   B DMS   C .   ? 0.8004 0.8968 0.7111 0.1634  0.1155  0.0963  201 DMS   B O   
1679 C C1  A DMS   C .   ? 0.8052 0.8794 0.7272 0.1440  0.1078  0.0829  201 DMS   B C1  
1680 C C1  B DMS   C .   ? 0.8038 0.8781 0.7258 0.1440  0.1078  0.0829  201 DMS   B C1  
1681 C C2  A DMS   C .   ? 0.8051 0.8719 0.7027 0.1665  0.1045  0.0781  201 DMS   B C2  
1682 C C2  B DMS   C .   ? 0.8062 0.8730 0.7037 0.1665  0.1045  0.0781  201 DMS   B C2  
1683 S S   A DMS   D .   ? 9.0309 9.0420 9.0518 0.0180  0.0798  0.0215  202 DMS   B S   
1684 S S   B DMS   D .   ? 9.0309 9.0420 9.0518 0.0180  0.0798  0.0215  202 DMS   B S   
1685 O O   A DMS   D .   ? 8.9604 8.9727 8.9774 0.0182  0.0793  0.0179  202 DMS   B O   
1686 O O   B DMS   D .   ? 8.9604 8.9727 8.9774 0.0182  0.0793  0.0179  202 DMS   B O   
1687 C C1  A DMS   D .   ? 9.0217 9.0310 9.0416 0.0209  0.0771  0.0152  202 DMS   B C1  
1688 C C1  B DMS   D .   ? 9.0217 9.0310 9.0416 0.0209  0.0771  0.0152  202 DMS   B C1  
1689 C C2  A DMS   D .   ? 8.7783 8.7901 8.7951 0.0252  0.0818  0.0289  202 DMS   B C2  
1690 C C2  B DMS   D .   ? 8.7783 8.7901 8.7951 0.0252  0.0818  0.0289  202 DMS   B C2  
1691 S S   A DMS   E .   ? 0.8171 0.8937 0.7448 0.1350  0.1043  0.0758  203 DMS   B S   
1692 S S   B DMS   E .   ? 0.8176 0.8942 0.7453 0.1349  0.1043  0.0758  203 DMS   B S   
1693 O O   A DMS   E .   ? 0.8059 0.8841 0.7358 0.1319  0.1035  0.0745  203 DMS   B O   
1694 O O   B DMS   E .   ? 0.8071 0.8853 0.7369 0.1320  0.1035  0.0745  203 DMS   B O   
1695 C C1  A DMS   E .   ? 0.8197 0.8821 0.7538 0.1231  0.1005  0.0691  203 DMS   B C1  
1696 C C1  B DMS   E .   ? 0.8188 0.8813 0.7529 0.1231  0.1005  0.0691  203 DMS   B C1  
1697 C C2  A DMS   E .   ? 0.8163 0.9082 0.7568 0.1293  0.1110  0.0874  203 DMS   B C2  
1698 C C2  B DMS   E .   ? 0.8162 0.9081 0.7566 0.1293  0.1110  0.0874  203 DMS   B C2  
1699 N N1  C A1BGK F .   ? 0.7480 0.8101 0.6820 0.1255  0.1022  0.0722  204 A1BGK B N1  
1700 N N1  D A1BGK F .   ? 0.7492 0.8114 0.6832 0.1255  0.1022  0.0722  204 A1BGK B N1  
1701 N N3  C A1BGK F .   ? 0.7503 0.8115 0.7119 0.0959  0.1022  0.0717  204 A1BGK B N3  
1702 N N3  D A1BGK F .   ? 0.7500 0.8112 0.7116 0.0959  0.1022  0.0717  204 A1BGK B N3  
1703 C C4  C A1BGK F .   ? 0.8450 0.9534 0.7799 0.1429  0.1210  0.1080  204 A1BGK B C4  
1704 C C4  D A1BGK F .   ? 0.8446 0.9530 0.7795 0.1429  0.1210  0.1080  204 A1BGK B C4  
1705 C C5  C A1BGK F .   ? 0.8353 0.9349 0.7646 0.1454  0.1167  0.0987  204 A1BGK B C5  
1706 C C5  D A1BGK F .   ? 0.8347 0.9343 0.7640 0.1454  0.1167  0.0987  204 A1BGK B C5  
1707 C C6  C A1BGK F .   ? 0.8126 0.8965 0.7324 0.1497  0.1111  0.0887  204 A1BGK B C6  
1708 C C6  D A1BGK F .   ? 0.8124 0.8963 0.7322 0.1497  0.1111  0.0887  204 A1BGK B C6  
1709 C C7  C A1BGK F .   ? 0.8060 0.8890 0.7131 0.1624  0.1106  0.0880  204 A1BGK B C7  
1710 C C7  D A1BGK F .   ? 0.8062 0.8892 0.7134 0.1624  0.1106  0.0880  204 A1BGK B C7  
1711 C C8  C A1BGK F .   ? 0.7884 0.8573 0.6864 0.1666  0.1051  0.0791  204 A1BGK B C8  
1712 C C8  D A1BGK F .   ? 0.7896 0.8585 0.6876 0.1666  0.1051  0.0791  204 A1BGK B C8  
1713 C C10 C A1BGK F .   ? 0.7801 0.8379 0.6939 0.1460  0.1010  0.0715  204 A1BGK B C10 
1714 C C10 D A1BGK F .   ? 0.7807 0.8385 0.6946 0.1460  0.1010  0.0715  204 A1BGK B C10 
1715 C C13 C A1BGK F .   ? 0.7555 0.8163 0.6994 0.1142  0.1016  0.0709  204 A1BGK B C13 
1716 C C13 D A1BGK F .   ? 0.7556 0.8164 0.6995 0.1142  0.1016  0.0709  204 A1BGK B C13 
1717 C C15 C A1BGK F .   ? 0.7425 0.8051 0.7163 0.0843  0.1031  0.0739  204 A1BGK B C15 
1718 C C15 D A1BGK F .   ? 0.7423 0.8049 0.7161 0.0843  0.1031  0.0739  204 A1BGK B C15 
1719 C C17 C A1BGK F .   ? 0.8446 0.9509 0.7772 0.1439  0.1174  0.0994  204 A1BGK B C17 
1720 C C17 D A1BGK F .   ? 0.8439 0.9502 0.7765 0.1439  0.1174  0.0994  204 A1BGK B C17 
1721 C C1  C A1BGK F .   ? 0.8419 0.9867 0.8093 0.1209  0.1294  0.1257  204 A1BGK B C1  
1722 C C1  D A1BGK F .   ? 0.8416 0.9865 0.8091 0.1209  0.1294  0.1257  204 A1BGK B C1  
1723 O O1  C A1BGK F .   ? 0.8524 0.9979 0.8089 0.1323  0.1304  0.1264  204 A1BGK B O1  
1724 O O1  D A1BGK F .   ? 0.8520 0.9974 0.8084 0.1323  0.1304  0.1264  204 A1BGK B O1  
1725 C C2  C A1BGK F .   ? 0.8534 0.9832 0.8006 0.1370  0.1261  0.1171  204 A1BGK B C2  
1726 C C2  D A1BGK F .   ? 0.8527 0.9825 0.7999 0.1370  0.1261  0.1171  204 A1BGK B C2  
1727 C C3  C A1BGK F .   ? 0.8525 0.9759 0.7964 0.1383  0.1257  0.1175  204 A1BGK B C3  
1728 C C3  D A1BGK F .   ? 0.8519 0.9752 0.7957 0.1383  0.1257  0.1175  204 A1BGK B C3  
1729 C C9  C A1BGK F .   ? 0.7806 0.8372 0.6823 0.1581  0.1003  0.0710  204 A1BGK B C9  
1730 C C9  D A1BGK F .   ? 0.7817 0.8383 0.6834 0.1581  0.1003  0.0710  204 A1BGK B C9  
1731 C C11 C A1BGK F .   ? 0.7936 0.8642 0.7163 0.1417  0.1062  0.0801  204 A1BGK B C11 
1732 C C11 D A1BGK F .   ? 0.7934 0.8640 0.7161 0.1417  0.1062  0.0801  204 A1BGK B C11 
1733 C C12 C A1BGK F .   ? 0.7642 0.8340 0.6993 0.1286  0.1061  0.0796  204 A1BGK B C12 
1734 C C12 D A1BGK F .   ? 0.7649 0.8346 0.6999 0.1286  0.1061  0.0796  204 A1BGK B C12 
1735 O O2  C A1BGK F .   ? 0.7727 0.8477 0.7177 0.1210  0.1090  0.0855  204 A1BGK B O2  
1736 O O2  D A1BGK F .   ? 0.7726 0.8475 0.7176 0.1210  0.1090  0.0855  204 A1BGK B O2  
1737 C C14 C A1BGK F .   ? 0.7425 0.7967 0.6852 0.1108  0.0981  0.0645  204 A1BGK B C14 
1738 C C14 D A1BGK F .   ? 0.7432 0.7975 0.6860 0.1108  0.0981  0.0645  204 A1BGK B C14 
1739 N N2  C A1BGK F .   ? 0.7527 0.8076 0.7062 0.0999  0.0987  0.0650  204 A1BGK B N2  
1740 N N2  D A1BGK F .   ? 0.7524 0.8073 0.7059 0.0999  0.0987  0.0650  204 A1BGK B N2  
1741 C C16 C A1BGK F .   ? 0.7515 0.8163 0.7078 0.1040  0.1041  0.0755  204 A1BGK B C16 
1742 C C16 D A1BGK F .   ? 0.7515 0.8163 0.7077 0.1040  0.1041  0.0755  204 A1BGK B C16 
1743 N N4  C A1BGK F .   ? 0.8506 0.9720 0.7921 0.1400  0.1221  0.1082  204 A1BGK B N4  
1744 N N4  D A1BGK F .   ? 0.8499 0.9712 0.7914 0.1400  0.1221  0.1082  204 A1BGK B N4  
1745 S S   C SO4   G .   ? 1.2530 1.2635 1.2725 0.0197  0.0780  0.0166  205 SO4   B S   
1746 S S   D SO4   G .   ? 1.2530 1.2635 1.2725 0.0197  0.0780  0.0166  205 SO4   B S   
1747 O O1  C SO4   G .   ? 1.2497 1.2609 1.2688 0.0214  0.0806  0.0246  205 SO4   B O1  
1748 O O1  D SO4   G .   ? 1.2497 1.2609 1.2688 0.0214  0.0806  0.0246  205 SO4   B O1  
1749 O O2  C SO4   G .   ? 1.2768 1.2860 1.2939 0.0247  0.0766  0.0144  205 SO4   B O2  
1750 O O2  D SO4   G .   ? 1.2768 1.2860 1.2939 0.0247  0.0766  0.0144  205 SO4   B O2  
1751 O O3  C SO4   G .   ? 1.2182 1.2300 1.2345 0.0191  0.0774  0.0128  205 SO4   B O3  
1752 O O3  D SO4   G .   ? 1.2182 1.2300 1.2345 0.0191  0.0774  0.0128  205 SO4   B O3  
1753 O O4  C SO4   G .   ? 1.2583 1.2681 1.2833 0.0136  0.0773  0.0147  205 SO4   B O4  
1754 O O4  D SO4   G .   ? 1.2583 1.2681 1.2833 0.0136  0.0773  0.0147  205 SO4   B O4  
# 
