data_7I1M
# 
_entry.id   7I1M 
# 
_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   7I1M         pdb_00007i1m 10.2210/pdb7i1m/pdb 
WWPDB D_1001408201 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7I1M 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-20 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Balaji, G.'          9  
'Phelps, J.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Balaji, G.'          ? 9  
primary 'Phelps, J.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'        5067.486  1  ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                 18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                  78.133    3  ?                           ?    ? ? 
4 non-polymer syn 7,8-dichloro-2-methylquinolin-4-amine 227.090   1  ?                           ?    ? ? 
5 non-polymer syn 'SULFATE ION'                         96.063    2  ?                           ?    ? ? 
6 water       nat water                                 18.015    81 ?                           ?    ? ? 
# 
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 7,8-dichloro-2-methylquinolin-4-amine A1BXF 
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 
A1BXF non-polymer         . 7,8-dichloro-2-methylquinolin-4-amine ? 'C10 H8 Cl2 N2'  227.090 
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        A1BXF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXF 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 3 DMS   1  202 203 DMS   DMS B . 
E 4 A1BXF 1  203 301 A1BXF LIG B . 
F 5 SO4   1  204 302 SO4   SO4 B . 
G 5 SO4   1  205 303 SO4   SO4 B . 
H 3 DMS   1  206 304 DMS   DMS B . 
I 6 HOH   1  101 9   HOH   HOH A . 
I 6 HOH   2  102 10  HOH   HOH A . 
I 6 HOH   3  103 43  HOH   HOH A . 
I 6 HOH   4  104 73  HOH   HOH A . 
I 6 HOH   5  105 22  HOH   HOH A . 
I 6 HOH   6  106 70  HOH   HOH A . 
I 6 HOH   7  107 67  HOH   HOH A . 
I 6 HOH   8  108 51  HOH   HOH A . 
I 6 HOH   9  109 52  HOH   HOH A . 
I 6 HOH   10 110 58  HOH   HOH A . 
I 6 HOH   11 111 18  HOH   HOH A . 
I 6 HOH   12 112 44  HOH   HOH A . 
I 6 HOH   13 113 35  HOH   HOH A . 
I 6 HOH   14 114 36  HOH   HOH A . 
I 6 HOH   15 115 79  HOH   HOH A . 
I 6 HOH   16 116 13  HOH   HOH A . 
I 6 HOH   17 117 69  HOH   HOH A . 
I 6 HOH   18 118 80  HOH   HOH A . 
I 6 HOH   19 119 77  HOH   HOH A . 
I 6 HOH   20 120 19  HOH   HOH A . 
I 6 HOH   21 121 53  HOH   HOH A . 
I 6 HOH   22 122 42  HOH   HOH A . 
I 6 HOH   23 123 17  HOH   HOH A . 
I 6 HOH   24 124 72  HOH   HOH A . 
J 6 HOH   1  301 4   HOH   HOH B . 
J 6 HOH   2  302 71  HOH   HOH B . 
J 6 HOH   3  303 3   HOH   HOH B . 
J 6 HOH   4  304 1   HOH   HOH B . 
J 6 HOH   5  305 74  HOH   HOH B . 
J 6 HOH   6  306 8   HOH   HOH B . 
J 6 HOH   7  307 21  HOH   HOH B . 
J 6 HOH   8  308 63  HOH   HOH B . 
J 6 HOH   9  309 6   HOH   HOH B . 
J 6 HOH   10 310 65  HOH   HOH B . 
J 6 HOH   11 311 32  HOH   HOH B . 
J 6 HOH   12 312 15  HOH   HOH B . 
J 6 HOH   13 313 26  HOH   HOH B . 
J 6 HOH   14 314 76  HOH   HOH B . 
J 6 HOH   15 315 61  HOH   HOH B . 
J 6 HOH   16 316 33  HOH   HOH B . 
J 6 HOH   17 317 7   HOH   HOH B . 
J 6 HOH   18 318 12  HOH   HOH B . 
J 6 HOH   19 319 5   HOH   HOH B . 
J 6 HOH   20 320 24  HOH   HOH B . 
J 6 HOH   21 321 30  HOH   HOH B . 
J 6 HOH   22 322 62  HOH   HOH B . 
J 6 HOH   23 323 64  HOH   HOH B . 
J 6 HOH   24 324 56  HOH   HOH B . 
J 6 HOH   25 325 57  HOH   HOH B . 
J 6 HOH   26 326 39  HOH   HOH B . 
J 6 HOH   27 327 48  HOH   HOH B . 
J 6 HOH   28 328 78  HOH   HOH B . 
J 6 HOH   29 329 23  HOH   HOH B . 
J 6 HOH   30 330 37  HOH   HOH B . 
J 6 HOH   31 331 31  HOH   HOH B . 
J 6 HOH   32 332 27  HOH   HOH B . 
J 6 HOH   33 333 28  HOH   HOH B . 
J 6 HOH   34 334 41  HOH   HOH B . 
J 6 HOH   35 335 20  HOH   HOH B . 
J 6 HOH   36 336 2   HOH   HOH B . 
J 6 HOH   37 337 59  HOH   HOH B . 
J 6 HOH   38 338 11  HOH   HOH B . 
J 6 HOH   39 339 34  HOH   HOH B . 
J 6 HOH   40 340 60  HOH   HOH B . 
J 6 HOH   41 341 14  HOH   HOH B . 
J 6 HOH   42 342 50  HOH   HOH B . 
J 6 HOH   43 343 16  HOH   HOH B . 
J 6 HOH   44 344 68  HOH   HOH B . 
J 6 HOH   45 345 47  HOH   HOH B . 
J 6 HOH   46 346 81  HOH   HOH B . 
J 6 HOH   47 347 38  HOH   HOH B . 
J 6 HOH   48 348 25  HOH   HOH B . 
J 6 HOH   49 349 54  HOH   HOH B . 
J 6 HOH   50 350 55  HOH   HOH B . 
J 6 HOH   51 351 49  HOH   HOH B . 
J 6 HOH   52 352 40  HOH   HOH B . 
J 6 HOH   53 353 29  HOH   HOH B . 
J 6 HOH   54 354 75  HOH   HOH B . 
J 6 HOH   55 355 66  HOH   HOH B . 
J 6 HOH   56 356 45  HOH   HOH B . 
J 6 HOH   57 357 46  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       BUSTER  '2.10.4 (26-JUL-2023)' ? 1 ? ? ? ? 
'data scaling'   Aimless .                      ? 2 ? ? ? ? 
phasing          PHASER  .                      ? 3 ? ? ? ? 
'data reduction' XDS     .                      ? 4 ? ? ? ? 
# 
_cell.entry_id           7I1M 
_cell.length_a           42.477 
_cell.length_b           42.477 
_cell.length_c           216.517 
_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                         7I1M 
_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          7I1M 
_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   41.60 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                               1 
_diffrn.ambient_temp                     100 
_diffrn.crystal_id                       1 
_diffrn.ambient_temp_details             ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-10-10 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I1M 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             54.129 
_reflns.d_resolution_high            2.013 
_reflns.number_obs                   7765 
_reflns.percent_possible_obs         55.0 
_reflns.pdbx_Rmerge_I_obs            0.131 
_reflns.pdbx_netI_over_sigmaI        11.5 
_reflns.pdbx_redundancy              15.6 
_reflns.pdbx_Rrim_I_all              0.135 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_number_measured_all     121166 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  2.013 
_reflns_shell.d_res_low                   2.217 
_reflns_shell.number_measured_all         8917 
_reflns_shell.number_unique_obs           388 
_reflns_shell.Rmerge_I_obs                1.992 
_reflns_shell.pdbx_redundancy             23.0 
_reflns_shell.percent_possible_obs        11.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.6 
_reflns_shell.pdbx_Rrim_I_all             2.037 
_reflns_shell.pdbx_Rpim_I_all             0.419 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1M 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     7765 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.13 
_refine.ls_d_res_high                            2.013 
_refine.ls_percent_reflns_obs                    55.0 
_refine.ls_R_factor_obs                          0.2188 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2156 
_refine.ls_R_factor_R_free                       0.2815 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.800 
_refine.ls_number_reflns_R_free                  373 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.933 
_refine.correlation_coeff_Fo_to_Fc_free          0.896 
_refine.B_iso_mean                               45.57 
_refine.aniso_B[1][1]                            3.51560 
_refine.aniso_B[2][2]                            3.51560 
_refine.aniso_B[3][3]                            -7.03130 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.987 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.333 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.347 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I1M 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             81 
_refine_hist.number_atoms_total               1593 
_refine_hist.d_res_high                       2.013 
_refine_hist.d_res_low                        54.13 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.008 ? 2.00  1781 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.95  ? 2.00  2456 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  607  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  312  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1766 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? 5.00  6    'X-RAY DIFFRACTION' SEMIHARMONIC 
t_omega_torsion           2.84  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.04 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  219  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1321 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   19 
_refine_ls_shell.d_res_high                       2.01 
_refine_ls_shell.d_res_low                        2.23 
_refine_ls_shell.number_reflns_R_work             411 
_refine_ls_shell.R_factor_R_work                  0.2775 
_refine_ls_shell.percent_reflns_obs               11.79 
_refine_ls_shell.R_factor_R_free                  0.3850 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.86 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                432 
_refine_ls_shell.R_factor_all                     0.2831 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7I1M 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with MFP-0011177-001-002' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1M 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I1M A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I1M 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 7I1M SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I1M MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I1M MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I1M 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,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O ILE B 106 ? O ILE B 115 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7I1M 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    122 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    326 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.94 
# 
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 71  ? ? -160.34 114.95 
2 1 CYS B 80  ? ? 82.81   -22.09 
3 1 PRO B 131 ? ? -45.41  151.71 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     320 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   J 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 -14.0978 -2.0265 -20.9643 0.0334 -0.0142 -0.3211 0.2131 0.1126 0.0973 5.0693 4.1713 4.8652 -1.5106 
0.0777 0.4618 0.2587 0.6255 0.1385 -0.5335 -0.2679 -0.2354 -0.2658 0.3509 0.0093  
'X-RAY DIFFRACTION' 2 ? refined -17.4059 0.7014  -15.8736 0.1818 0.1305  -0.1529 0.2501 0.0570 0.0550 1.7973 2.0195 2.2969 -0.6689 
0.6821 0.0695 0.4462 0.2525 0.1458 -0.2309 -0.3720 0.0027  -0.0367 0.2534 -0.0742 
# 
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|304 }' 
# 
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 
A1BXF N1   N  Y N 1   
A1BXF C4   C  Y N 2   
A1BXF C5   C  Y N 3   
A1BXF C6   C  Y N 4   
A1BXF C7   C  Y N 5   
A1BXF C8   C  Y N 6   
A1BXF C10  C  Y N 7   
A1BXF C1   C  N N 8   
A1BXF C2   C  Y N 9   
A1BXF C3   C  Y N 10  
A1BXF C9   C  Y N 11  
A1BXF CL1  CL N N 12  
A1BXF CL2  CL N N 13  
A1BXF N2   N  N N 14  
A1BXF H1   H  N N 15  
A1BXF H2   H  N N 16  
A1BXF H3   H  N N 17  
A1BXF H4   H  N N 18  
A1BXF H5   H  N N 19  
A1BXF H6   H  N N 20  
A1BXF H7   H  N N 21  
A1BXF H8   H  N N 22  
ALA   N    N  N N 23  
ALA   CA   C  N S 24  
ALA   C    C  N N 25  
ALA   O    O  N N 26  
ALA   CB   C  N N 27  
ALA   OXT  O  N N 28  
ALA   H    H  N N 29  
ALA   H2   H  N N 30  
ALA   HA   H  N N 31  
ALA   HB1  H  N N 32  
ALA   HB2  H  N N 33  
ALA   HB3  H  N N 34  
ALA   HXT  H  N N 35  
ARG   N    N  N N 36  
ARG   CA   C  N S 37  
ARG   C    C  N N 38  
ARG   O    O  N N 39  
ARG   CB   C  N N 40  
ARG   CG   C  N N 41  
ARG   CD   C  N N 42  
ARG   NE   N  N N 43  
ARG   CZ   C  N N 44  
ARG   NH1  N  N N 45  
ARG   NH2  N  N N 46  
ARG   OXT  O  N N 47  
ARG   H    H  N N 48  
ARG   H2   H  N N 49  
ARG   HA   H  N N 50  
ARG   HB2  H  N N 51  
ARG   HB3  H  N N 52  
ARG   HG2  H  N N 53  
ARG   HG3  H  N N 54  
ARG   HD2  H  N N 55  
ARG   HD3  H  N N 56  
ARG   HE   H  N N 57  
ARG   HH11 H  N N 58  
ARG   HH12 H  N N 59  
ARG   HH21 H  N N 60  
ARG   HH22 H  N N 61  
ARG   HXT  H  N N 62  
ASN   N    N  N N 63  
ASN   CA   C  N S 64  
ASN   C    C  N N 65  
ASN   O    O  N N 66  
ASN   CB   C  N N 67  
ASN   CG   C  N N 68  
ASN   OD1  O  N N 69  
ASN   ND2  N  N N 70  
ASN   OXT  O  N N 71  
ASN   H    H  N N 72  
ASN   H2   H  N N 73  
ASN   HA   H  N N 74  
ASN   HB2  H  N N 75  
ASN   HB3  H  N N 76  
ASN   HD21 H  N N 77  
ASN   HD22 H  N N 78  
ASN   HXT  H  N N 79  
ASP   N    N  N N 80  
ASP   CA   C  N S 81  
ASP   C    C  N N 82  
ASP   O    O  N N 83  
ASP   CB   C  N N 84  
ASP   CG   C  N N 85  
ASP   OD1  O  N N 86  
ASP   OD2  O  N N 87  
ASP   OXT  O  N N 88  
ASP   H    H  N N 89  
ASP   H2   H  N N 90  
ASP   HA   H  N N 91  
ASP   HB2  H  N N 92  
ASP   HB3  H  N N 93  
ASP   HD2  H  N N 94  
ASP   HXT  H  N N 95  
CYS   N    N  N N 96  
CYS   CA   C  N R 97  
CYS   C    C  N N 98  
CYS   O    O  N N 99  
CYS   CB   C  N N 100 
CYS   SG   S  N N 101 
CYS   OXT  O  N N 102 
CYS   H    H  N N 103 
CYS   H2   H  N N 104 
CYS   HA   H  N N 105 
CYS   HB2  H  N N 106 
CYS   HB3  H  N N 107 
CYS   HG   H  N N 108 
CYS   HXT  H  N N 109 
DMS   S    S  N N 110 
DMS   O    O  N N 111 
DMS   C1   C  N N 112 
DMS   C2   C  N N 113 
DMS   H11  H  N N 114 
DMS   H12  H  N N 115 
DMS   H13  H  N N 116 
DMS   H21  H  N N 117 
DMS   H22  H  N N 118 
DMS   H23  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
SO4   S    S  N N 336 
SO4   O1   O  N N 337 
SO4   O2   O  N N 338 
SO4   O3   O  N N 339 
SO4   O4   O  N N 340 
THR   N    N  N N 341 
THR   CA   C  N S 342 
THR   C    C  N N 343 
THR   O    O  N N 344 
THR   CB   C  N R 345 
THR   OG1  O  N N 346 
THR   CG2  C  N N 347 
THR   OXT  O  N N 348 
THR   H    H  N N 349 
THR   H2   H  N N 350 
THR   HA   H  N N 351 
THR   HB   H  N N 352 
THR   HG1  H  N N 353 
THR   HG21 H  N N 354 
THR   HG22 H  N N 355 
THR   HG23 H  N N 356 
THR   HXT  H  N N 357 
TRP   N    N  N N 358 
TRP   CA   C  N S 359 
TRP   C    C  N N 360 
TRP   O    O  N N 361 
TRP   CB   C  N N 362 
TRP   CG   C  Y N 363 
TRP   CD1  C  Y N 364 
TRP   CD2  C  Y N 365 
TRP   NE1  N  Y N 366 
TRP   CE2  C  Y N 367 
TRP   CE3  C  Y N 368 
TRP   CZ2  C  Y N 369 
TRP   CZ3  C  Y N 370 
TRP   CH2  C  Y N 371 
TRP   OXT  O  N N 372 
TRP   H    H  N N 373 
TRP   H2   H  N N 374 
TRP   HA   H  N N 375 
TRP   HB2  H  N N 376 
TRP   HB3  H  N N 377 
TRP   HD1  H  N N 378 
TRP   HE1  H  N N 379 
TRP   HE3  H  N N 380 
TRP   HZ2  H  N N 381 
TRP   HZ3  H  N N 382 
TRP   HH2  H  N N 383 
TRP   HXT  H  N N 384 
TYR   N    N  N N 385 
TYR   CA   C  N S 386 
TYR   C    C  N N 387 
TYR   O    O  N N 388 
TYR   CB   C  N N 389 
TYR   CG   C  Y N 390 
TYR   CD1  C  Y N 391 
TYR   CD2  C  Y N 392 
TYR   CE1  C  Y N 393 
TYR   CE2  C  Y N 394 
TYR   CZ   C  Y N 395 
TYR   OH   O  N N 396 
TYR   OXT  O  N N 397 
TYR   H    H  N N 398 
TYR   H2   H  N N 399 
TYR   HA   H  N N 400 
TYR   HB2  H  N N 401 
TYR   HB3  H  N N 402 
TYR   HD1  H  N N 403 
TYR   HD2  H  N N 404 
TYR   HE1  H  N N 405 
TYR   HE2  H  N N 406 
TYR   HH   H  N N 407 
TYR   HXT  H  N N 408 
VAL   N    N  N N 409 
VAL   CA   C  N S 410 
VAL   C    C  N N 411 
VAL   O    O  N N 412 
VAL   CB   C  N N 413 
VAL   CG1  C  N N 414 
VAL   CG2  C  N N 415 
VAL   OXT  O  N N 416 
VAL   H    H  N N 417 
VAL   H2   H  N N 418 
VAL   HA   H  N N 419 
VAL   HB   H  N N 420 
VAL   HG11 H  N N 421 
VAL   HG12 H  N N 422 
VAL   HG13 H  N N 423 
VAL   HG21 H  N N 424 
VAL   HG22 H  N N 425 
VAL   HG23 H  N N 426 
VAL   HXT  H  N N 427 
# 
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 
A1BXF N2  C4   sing N N 1   
A1BXF C4  C3   doub Y N 2   
A1BXF C4  C5   sing Y N 3   
A1BXF C3  C2   sing Y N 4   
A1BXF C6  C5   doub Y N 5   
A1BXF C6  C7   sing Y N 6   
A1BXF C5  C10  sing Y N 7   
A1BXF C2  C1   sing N N 8   
A1BXF C2  N1   doub Y N 9   
A1BXF C7  C8   doub Y N 10  
A1BXF C10 N1   sing Y N 11  
A1BXF C10 C9   doub Y N 12  
A1BXF C8  C9   sing Y N 13  
A1BXF C8  CL2  sing N N 14  
A1BXF C9  CL1  sing N N 15  
A1BXF C6  H1   sing N N 16  
A1BXF C7  H2   sing N N 17  
A1BXF C1  H3   sing N N 18  
A1BXF C1  H4   sing N N 19  
A1BXF C1  H5   sing N N 20  
A1BXF C3  H6   sing N N 21  
A1BXF N2  H7   sing N N 22  
A1BXF N2  H8   sing N N 23  
ALA   N   CA   sing N N 24  
ALA   N   H    sing N N 25  
ALA   N   H2   sing N N 26  
ALA   CA  C    sing N N 27  
ALA   CA  CB   sing N N 28  
ALA   CA  HA   sing N N 29  
ALA   C   O    doub N N 30  
ALA   C   OXT  sing N N 31  
ALA   CB  HB1  sing N N 32  
ALA   CB  HB2  sing N N 33  
ALA   CB  HB3  sing N N 34  
ALA   OXT HXT  sing N N 35  
ARG   N   CA   sing N N 36  
ARG   N   H    sing N N 37  
ARG   N   H2   sing N N 38  
ARG   CA  C    sing N N 39  
ARG   CA  CB   sing N N 40  
ARG   CA  HA   sing N N 41  
ARG   C   O    doub N N 42  
ARG   C   OXT  sing N N 43  
ARG   CB  CG   sing N N 44  
ARG   CB  HB2  sing N N 45  
ARG   CB  HB3  sing N N 46  
ARG   CG  CD   sing N N 47  
ARG   CG  HG2  sing N N 48  
ARG   CG  HG3  sing N N 49  
ARG   CD  NE   sing N N 50  
ARG   CD  HD2  sing N N 51  
ARG   CD  HD3  sing N N 52  
ARG   NE  CZ   sing N N 53  
ARG   NE  HE   sing N N 54  
ARG   CZ  NH1  sing N N 55  
ARG   CZ  NH2  doub N N 56  
ARG   NH1 HH11 sing N N 57  
ARG   NH1 HH12 sing N N 58  
ARG   NH2 HH21 sing N N 59  
ARG   NH2 HH22 sing N N 60  
ARG   OXT HXT  sing N N 61  
ASN   N   CA   sing N N 62  
ASN   N   H    sing N N 63  
ASN   N   H2   sing N N 64  
ASN   CA  C    sing N N 65  
ASN   CA  CB   sing N N 66  
ASN   CA  HA   sing N N 67  
ASN   C   O    doub N N 68  
ASN   C   OXT  sing N N 69  
ASN   CB  CG   sing N N 70  
ASN   CB  HB2  sing N N 71  
ASN   CB  HB3  sing N N 72  
ASN   CG  OD1  doub N N 73  
ASN   CG  ND2  sing N N 74  
ASN   ND2 HD21 sing N N 75  
ASN   ND2 HD22 sing N N 76  
ASN   OXT HXT  sing N N 77  
ASP   N   CA   sing N N 78  
ASP   N   H    sing N N 79  
ASP   N   H2   sing N N 80  
ASP   CA  C    sing N N 81  
ASP   CA  CB   sing N N 82  
ASP   CA  HA   sing N N 83  
ASP   C   O    doub N N 84  
ASP   C   OXT  sing N N 85  
ASP   CB  CG   sing N N 86  
ASP   CB  HB2  sing N N 87  
ASP   CB  HB3  sing N N 88  
ASP   CG  OD1  doub N N 89  
ASP   CG  OD2  sing N N 90  
ASP   OD2 HD2  sing N N 91  
ASP   OXT HXT  sing N N 92  
CYS   N   CA   sing N N 93  
CYS   N   H    sing N N 94  
CYS   N   H2   sing N N 95  
CYS   CA  C    sing N N 96  
CYS   CA  CB   sing N N 97  
CYS   CA  HA   sing N N 98  
CYS   C   O    doub N N 99  
CYS   C   OXT  sing N N 100 
CYS   CB  SG   sing N N 101 
CYS   CB  HB2  sing N N 102 
CYS   CB  HB3  sing N N 103 
CYS   SG  HG   sing N N 104 
CYS   OXT HXT  sing N N 105 
DMS   S   O    doub N N 106 
DMS   S   C1   sing N N 107 
DMS   S   C2   sing N N 108 
DMS   C1  H11  sing N N 109 
DMS   C1  H12  sing N N 110 
DMS   C1  H13  sing N N 111 
DMS   C2  H21  sing N N 112 
DMS   C2  H22  sing N N 113 
DMS   C2  H23  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
SO4   S   O1   doub N N 322 
SO4   S   O2   doub N N 323 
SO4   S   O3   sing N N 324 
SO4   S   O4   sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TRP   N   CA   sing N N 342 
TRP   N   H    sing N N 343 
TRP   N   H2   sing N N 344 
TRP   CA  C    sing N N 345 
TRP   CA  CB   sing N N 346 
TRP   CA  HA   sing N N 347 
TRP   C   O    doub N N 348 
TRP   C   OXT  sing N N 349 
TRP   CB  CG   sing N N 350 
TRP   CB  HB2  sing N N 351 
TRP   CB  HB3  sing N N 352 
TRP   CG  CD1  doub Y N 353 
TRP   CG  CD2  sing Y N 354 
TRP   CD1 NE1  sing Y N 355 
TRP   CD1 HD1  sing N N 356 
TRP   CD2 CE2  doub Y N 357 
TRP   CD2 CE3  sing Y N 358 
TRP   NE1 CE2  sing Y N 359 
TRP   NE1 HE1  sing N N 360 
TRP   CE2 CZ2  sing Y N 361 
TRP   CE3 CZ3  doub Y N 362 
TRP   CE3 HE3  sing N N 363 
TRP   CZ2 CH2  doub Y N 364 
TRP   CZ2 HZ2  sing N N 365 
TRP   CZ3 CH2  sing Y N 366 
TRP   CZ3 HZ3  sing N N 367 
TRP   CH2 HH2  sing N N 368 
TRP   OXT HXT  sing N N 369 
TYR   N   CA   sing N N 370 
TYR   N   H    sing N N 371 
TYR   N   H2   sing N N 372 
TYR   CA  C    sing N N 373 
TYR   CA  CB   sing N N 374 
TYR   CA  HA   sing N N 375 
TYR   C   O    doub N N 376 
TYR   C   OXT  sing N N 377 
TYR   CB  CG   sing N N 378 
TYR   CB  HB2  sing N N 379 
TYR   CB  HB3  sing N N 380 
TYR   CG  CD1  doub Y N 381 
TYR   CG  CD2  sing Y N 382 
TYR   CD1 CE1  sing Y N 383 
TYR   CD1 HD1  sing N N 384 
TYR   CD2 CE2  doub Y N 385 
TYR   CD2 HD2  sing N N 386 
TYR   CE1 CZ   doub Y N 387 
TYR   CE1 HE1  sing N N 388 
TYR   CE2 CZ   sing Y N 389 
TYR   CE2 HE2  sing N N 390 
TYR   CZ  OH   sing N N 391 
TYR   OH  HH   sing N N 392 
TYR   OXT HXT  sing N N 393 
VAL   N   CA   sing N N 394 
VAL   N   H    sing N N 395 
VAL   N   H2   sing N N 396 
VAL   CA  C    sing N N 397 
VAL   CA  CB   sing N N 398 
VAL   CA  HA   sing N N 399 
VAL   C   O    doub N N 400 
VAL   C   OXT  sing N N 401 
VAL   CB  CG1  sing N N 402 
VAL   CB  CG2  sing N N 403 
VAL   CB  HB   sing N N 404 
VAL   CG1 HG11 sing N N 405 
VAL   CG1 HG12 sing N N 406 
VAL   CG1 HG13 sing N N 407 
VAL   CG2 HG21 sing N N 408 
VAL   CG2 HG22 sing N N 409 
VAL   CG2 HG23 sing N N 410 
VAL   OXT HXT  sing N N 411 
# 
_pdbx_audit_support.funding_organization   'Australian Research Council (ARC)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           IC180100021 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002340 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.accession_code   8PN6 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7I1M 
_atom_sites.fract_transf_matrix[1][1]   0.023542 
_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]   0.023542 
_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]   0.004619 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? -21.540 18.958  -7.251  1.00 49.34  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.514 17.879  -7.427  1.00 49.50  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.395 17.232  -8.801  1.00 47.65  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.322 17.914  -9.828  1.00 48.19  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.962 18.369  -7.181  1.00 52.94  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.614 17.836  -5.908  1.00 60.58  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.266 18.640  -5.190  1.00 62.48  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.491 16.612  -5.638  1.00 62.98  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.386 15.912  -8.809  1.00 45.35  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.312 15.152  -10.033 1.00 44.01  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.706 14.909  -10.601 1.00 42.44  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.675 14.820  -9.838  1.00 41.99  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.590 13.814  -9.799  1.00 44.62  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.100 13.956  -9.652  1.00 47.04  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.324 12.407  -9.145  1.00 52.58  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.647 12.952  -8.908  1.00 52.98  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.797 14.775  -11.951 1.00 41.19  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.051 14.503  -12.653 1.00 40.73  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.903 13.460  -13.770 1.00 40.33  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.804 13.237  -14.257 1.00 40.64  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.722 15.788  -13.165 1.00 40.71  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.958 16.533  -14.235 1.00 42.11  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.051 17.531  -13.902 1.00 43.48  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.220 16.319  -15.585 1.00 43.30  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.389 18.264  -14.883 1.00 45.07  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.566 17.046  -16.576 1.00 44.32  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.657 18.027  -16.221 1.00 45.86  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.987 18.736  -17.191 1.00 48.26  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.008 12.811  -14.169 1.00 39.67  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.971 11.811  -15.231 1.00 39.53  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.685 12.294  -16.509 1.00 40.07  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.685 13.025  -16.434 1.00 40.20  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.474 10.421  -14.762 1.00 39.33  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.901 10.485  -14.205 1.00 39.59  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.523 9.810   -13.748 1.00 39.77  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.542 9.118   -14.025 1.00 40.39  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.145 11.905  -17.677 1.00 40.00  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -26.686 12.241  -19.006 1.00 40.69  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -26.727 10.955  -19.873 1.00 40.68  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.711 10.286  -19.975 1.00 40.30  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -25.794 13.294  -19.696 1.00 43.23  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.138 14.743  -19.379 1.00 48.83  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.329 15.773  -20.154 1.00 56.98  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.548 15.377  -21.049 1.00 58.79  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.477 16.983  -19.865 1.00 59.70  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -27.872 10.612  -20.495 1.00 40.80  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -27.962 9.391   -21.311 1.00 40.87  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.029 9.417   -22.506 1.00 41.15  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -26.899 10.447  -23.159 1.00 41.37  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.397 9.122   -21.784 1.00 41.31  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -29.701 7.627   -21.840 1.00 42.74  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.147 7.334   -22.183 1.00 43.75  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.370 5.912   -22.448 1.00 44.75  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.216 5.345   -23.643 1.00 45.29  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -30.829 6.069   -24.684 1.00 46.13  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.422 4.043   -23.799 1.00 42.78  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.375 8.288   -22.791 1.00 40.77  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.456 8.195   -23.923 1.00 40.49  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -25.816 7.119   -24.956 1.00 40.07  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.137 7.021   -25.957 1.00 40.00  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.034 8.008   -23.435 1.00 40.57  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -26.878 6.349   -24.734 1.00 39.91  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.304 5.342   -25.702 1.00 39.98  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -27.921 4.088   -25.125 1.00 40.08  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.060 3.972   -23.914 1.00 40.46  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.326 3.155   -25.996 1.00 40.00  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -28.900 1.859   -25.618 1.00 40.58  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.795 0.840   -25.426 1.00 41.04  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.739 0.969   -26.044 1.00 40.87  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -29.780 1.309   -26.749 1.00 41.75  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.120 1.953   -26.912 1.00 46.64  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.375 2.959   -26.233 1.00 47.80  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -31.916 1.464   -27.750 1.00 48.39  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.068 -0.233  -24.666 1.00 41.33  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.088 -1.304  -24.508 1.00 41.99  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.429 -2.454  -25.448 1.00 43.41  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.211 -3.340  -25.099 1.00 43.69  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.981 -1.710  -23.053 1.00 41.81  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.458 -0.513  -22.251 1.00 42.20  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.097 -2.939  -22.906 1.00 41.98  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.601 -0.665  -20.851 1.00 42.77  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.863 -2.420  -26.661 0.25 43.53  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.860 -2.426  -26.658 0.25 43.54  ? 60  THR   A N   1 
ATOM   84   N  N   C THR   A 1 17  ? -26.863 -2.420  -26.661 0.25 43.53  ? 60  THR   A N   1 
ATOM   85   N  N   D THR   A 1 17  ? -26.860 -2.426  -26.658 0.25 43.54  ? 60  THR   A N   1 
ATOM   86   C  CA  A THR   A 1 17  ? -27.085 -3.445  -27.679 0.25 44.30  ? 60  THR   A CA  1 
ATOM   87   C  CA  B THR   A 1 17  ? -27.119 -3.430  -27.690 0.25 44.19  ? 60  THR   A CA  1 
ATOM   88   C  CA  C THR   A 1 17  ? -27.085 -3.445  -27.679 0.25 44.30  ? 60  THR   A CA  1 
ATOM   89   C  CA  D THR   A 1 17  ? -27.119 -3.430  -27.690 0.25 44.19  ? 60  THR   A CA  1 
ATOM   90   C  C   A THR   A 1 17  ? -25.760 -3.914  -28.286 0.25 44.60  ? 60  THR   A C   1 
ATOM   91   C  C   B THR   A 1 17  ? -25.797 -3.890  -28.340 0.25 44.60  ? 60  THR   A C   1 
ATOM   92   C  C   C THR   A 1 17  ? -25.760 -3.914  -28.286 0.25 44.60  ? 60  THR   A C   1 
ATOM   93   C  C   D THR   A 1 17  ? -25.797 -3.890  -28.340 0.25 44.60  ? 60  THR   A C   1 
ATOM   94   O  O   A THR   A 1 17  ? -24.800 -3.146  -28.354 0.25 44.43  ? 60  THR   A O   1 
ATOM   95   O  O   B THR   A 1 17  ? -24.857 -3.103  -28.446 0.25 44.45  ? 60  THR   A O   1 
ATOM   96   O  O   C THR   A 1 17  ? -24.800 -3.146  -28.354 0.25 44.43  ? 60  THR   A O   1 
ATOM   97   O  O   D THR   A 1 17  ? -24.857 -3.103  -28.446 0.25 44.45  ? 60  THR   A O   1 
ATOM   98   C  CB  A THR   A 1 17  ? -27.991 -2.908  -28.806 0.25 45.86  ? 60  THR   A CB  1 
ATOM   99   C  CB  B THR   A 1 17  ? -28.111 -2.838  -28.725 0.25 45.60  ? 60  THR   A CB  1 
ATOM   100  C  CB  C THR   A 1 17  ? -27.991 -2.908  -28.806 0.25 45.86  ? 60  THR   A CB  1 
ATOM   101  C  CB  D THR   A 1 17  ? -28.111 -2.838  -28.725 0.25 45.60  ? 60  THR   A CB  1 
ATOM   102  O  OG1 A THR   A 1 17  ? -27.341 -1.817  -29.465 0.25 46.96  ? 60  THR   A OG1 1 
ATOM   103  O  OG1 B THR   A 1 17  ? -29.252 -2.301  -28.049 0.25 46.52  ? 60  THR   A OG1 1 
ATOM   104  O  OG1 C THR   A 1 17  ? -27.341 -1.817  -29.465 0.25 46.96  ? 60  THR   A OG1 1 
ATOM   105  O  OG1 D THR   A 1 17  ? -29.252 -2.301  -28.049 0.25 46.52  ? 60  THR   A OG1 1 
ATOM   106  C  CG2 A THR   A 1 17  ? -29.375 -2.490  -28.314 0.25 46.29  ? 60  THR   A CG2 1 
ATOM   107  C  CG2 B THR   A 1 17  ? -28.570 -3.851  -29.768 0.25 45.94  ? 60  THR   A CG2 1 
ATOM   108  C  CG2 C THR   A 1 17  ? -29.375 -2.490  -28.314 0.25 46.29  ? 60  THR   A CG2 1 
ATOM   109  C  CG2 D THR   A 1 17  ? -28.570 -3.851  -29.768 0.25 45.94  ? 60  THR   A CG2 1 
ATOM   110  N  N   . TRP   A 1 18  ? -25.718 -5.161  -28.756 1.00 45.08  ? 61  TRP   A N   1 
ATOM   111  C  CA  . TRP   A 1 18  ? -24.525 -5.688  -29.416 1.00 48.48  ? 61  TRP   A CA  1 
ATOM   112  C  C   . TRP   A 1 18  ? -24.682 -5.210  -30.882 1.00 52.77  ? 61  TRP   A C   1 
ATOM   113  O  O   . TRP   A 1 18  ? -25.756 -5.380  -31.479 1.00 53.13  ? 61  TRP   A O   1 
ATOM   114  C  CB  . TRP   A 1 18  ? -24.503 -7.226  -29.375 1.00 48.28  ? 61  TRP   A CB  1 
ATOM   115  C  CG  . TRP   A 1 18  ? -23.471 -7.883  -30.259 1.00 48.63  ? 61  TRP   A CG  1 
ATOM   116  C  CD1 . TRP   A 1 18  ? -23.618 -8.237  -31.572 1.00 49.31  ? 61  TRP   A CD1 1 
ATOM   117  C  CD2 . TRP   A 1 18  ? -22.193 -8.398  -29.849 1.00 48.63  ? 61  TRP   A CD2 1 
ATOM   118  N  NE1 . TRP   A 1 18  ? -22.480 -8.869  -32.021 1.00 49.55  ? 61  TRP   A NE1 1 
ATOM   119  C  CE2 . TRP   A 1 18  ? -21.602 -9.003  -30.977 1.00 49.38  ? 61  TRP   A CE2 1 
ATOM   120  C  CE3 . TRP   A 1 18  ? -21.483 -8.391  -28.640 1.00 48.90  ? 61  TRP   A CE3 1 
ATOM   121  C  CZ2 . TRP   A 1 18  ? -20.337 -9.586  -30.929 1.00 50.08  ? 61  TRP   A CZ2 1 
ATOM   122  C  CZ3 . TRP   A 1 18  ? -20.234 -8.972  -28.592 1.00 49.52  ? 61  TRP   A CZ3 1 
ATOM   123  C  CH2 . TRP   A 1 18  ? -19.682 -9.579  -29.714 1.00 49.97  ? 61  TRP   A CH2 1 
ATOM   124  N  N   . GLU   A 1 19  ? -23.642 -4.587  -31.447 1.00 55.51  ? 62  GLU   A N   1 
ATOM   125  C  CA  . GLU   A 1 19  ? -23.727 -4.080  -32.811 1.00 58.56  ? 62  GLU   A CA  1 
ATOM   126  C  C   . GLU   A 1 19  ? -22.938 -4.895  -33.803 1.00 61.28  ? 62  GLU   A C   1 
ATOM   127  O  O   . GLU   A 1 19  ? -21.721 -5.006  -33.672 1.00 61.56  ? 62  GLU   A O   1 
ATOM   128  C  CB  . GLU   A 1 19  ? -23.340 -2.599  -32.869 1.00 62.02  ? 62  GLU   A CB  1 
ATOM   129  C  CG  . GLU   A 1 19  ? -24.399 -1.708  -32.226 1.00 68.79  ? 62  GLU   A CG  1 
ATOM   130  C  CD  . GLU   A 1 19  ? -25.762 -1.758  -32.896 1.00 75.83  ? 62  GLU   A CD  1 
ATOM   131  O  OE1 . GLU   A 1 19  ? -25.901 -1.220  -34.021 1.00 78.11  ? 62  GLU   A OE1 1 
ATOM   132  O  OE2 . GLU   A 1 19  ? -26.692 -2.344  -32.296 1.00 77.13  ? 62  GLU   A OE2 1 
ATOM   133  N  N   . LYS   A 1 20  ? -23.625 -5.469  -34.803 1.00 63.06  ? 63  LYS   A N   1 
ATOM   134  C  CA  . LYS   A 1 20  ? -22.942 -6.258  -35.819 1.00 65.52  ? 63  LYS   A CA  1 
ATOM   135  C  C   . LYS   A 1 20  ? -22.078 -5.348  -36.671 1.00 67.88  ? 63  LYS   A C   1 
ATOM   136  O  O   . LYS   A 1 20  ? -22.436 -4.185  -36.879 1.00 69.02  ? 63  LYS   A O   1 
ATOM   137  C  CB  . LYS   A 1 20  ? -23.933 -7.050  -36.689 1.00 67.67  ? 63  LYS   A CB  1 
ATOM   138  C  CG  . LYS   A 1 20  ? -24.705 -8.117  -35.922 1.00 72.33  ? 63  LYS   A CG  1 
ATOM   139  C  CD  . LYS   A 1 20  ? -25.593 -8.962  -36.842 1.00 76.98  ? 63  LYS   A CD  1 
ATOM   140  C  CE  . LYS   A 1 20  ? -24.804 -10.002 -37.612 1.00 81.57  ? 63  LYS   A CE  1 
ATOM   141  N  NZ  . LYS   A 1 20  ? -24.089 -10.947 -36.704 1.00 84.22  ? 63  LYS   A NZ  1 
ATOM   142  N  N   . ASP   A 1 21  ? -20.931 -5.848  -37.125 1.00 68.55  ? 64  ASP   A N   1 
ATOM   143  C  CA  . ASP   A 1 21  ? -20.022 -5.044  -37.937 1.00 70.13  ? 64  ASP   A CA  1 
ATOM   144  C  C   . ASP   A 1 21  ? -19.468 -3.849  -37.168 1.00 69.95  ? 64  ASP   A C   1 
ATOM   145  O  O   . ASP   A 1 21  ? -19.539 -2.712  -37.628 1.00 70.74  ? 64  ASP   A O   1 
ATOM   146  C  CB  . ASP   A 1 21  ? -20.667 -4.615  -39.266 1.00 73.88  ? 64  ASP   A CB  1 
ATOM   147  C  CG  . ASP   A 1 21  ? -20.739 -5.738  -40.283 1.00 82.93  ? 64  ASP   A CG  1 
ATOM   148  O  OD1 . ASP   A 1 21  ? -19.749 -6.494  -40.403 1.00 85.13  ? 64  ASP   A OD1 1 
ATOM   149  O  OD2 . ASP   A 1 21  ? -21.784 -5.859  -40.963 1.00 86.36  ? 64  ASP   A OD2 1 
ATOM   150  N  N   . ALA   A 1 22  ? -18.939 -4.113  -35.983 1.00 68.87  ? 65  ALA   A N   1 
ATOM   151  C  CA  . ALA   A 1 22  ? -18.302 -3.104  -35.143 1.00 67.83  ? 65  ALA   A CA  1 
ATOM   152  C  C   . ALA   A 1 22  ? -16.763 -3.139  -35.436 1.00 66.35  ? 65  ALA   A C   1 
ATOM   153  O  O   . ALA   A 1 22  ? -16.292 -4.068  -36.112 1.00 65.69  ? 65  ALA   A O   1 
ATOM   154  C  CB  . ALA   A 1 22  ? -18.592 -3.429  -33.679 1.00 68.00  ? 65  ALA   A CB  1 
ATOM   155  N  N   A GLU   A 1 23  ? -16.009 -2.131  -34.971 0.25 66.16  ? 66  GLU   A N   1 
ATOM   156  N  N   B GLU   A 1 23  ? -16.009 -2.131  -34.971 0.25 66.16  ? 66  GLU   A N   1 
ATOM   157  N  N   C GLU   A 1 23  ? -16.011 -2.139  -34.945 0.25 66.07  ? 66  GLU   A N   1 
ATOM   158  N  N   D GLU   A 1 23  ? -16.011 -2.139  -34.945 0.25 66.07  ? 66  GLU   A N   1 
ATOM   159  C  CA  A GLU   A 1 23  ? -14.565 -2.107  -35.203 0.25 66.42  ? 66  GLU   A CA  1 
ATOM   160  C  CA  B GLU   A 1 23  ? -14.565 -2.107  -35.203 0.25 66.42  ? 66  GLU   A CA  1 
ATOM   161  C  CA  C GLU   A 1 23  ? -14.562 -2.075  -35.122 0.25 66.23  ? 66  GLU   A CA  1 
ATOM   162  C  CA  D GLU   A 1 23  ? -14.562 -2.075  -35.122 0.25 66.23  ? 66  GLU   A CA  1 
ATOM   163  C  C   A GLU   A 1 23  ? -13.884 -3.144  -34.314 0.25 65.97  ? 66  GLU   A C   1 
ATOM   164  C  C   B GLU   A 1 23  ? -13.884 -3.144  -34.314 0.25 65.97  ? 66  GLU   A C   1 
ATOM   165  C  C   C GLU   A 1 23  ? -13.909 -3.172  -34.279 0.25 65.89  ? 66  GLU   A C   1 
ATOM   166  C  C   D GLU   A 1 23  ? -13.909 -3.172  -34.279 0.25 65.89  ? 66  GLU   A C   1 
ATOM   167  O  O   A GLU   A 1 23  ? -13.890 -3.009  -33.095 0.25 65.92  ? 66  GLU   A O   1 
ATOM   168  O  O   B GLU   A 1 23  ? -13.890 -3.009  -33.095 0.25 65.92  ? 66  GLU   A O   1 
ATOM   169  O  O   C GLU   A 1 23  ? -13.961 -3.105  -33.054 0.25 65.86  ? 66  GLU   A O   1 
ATOM   170  O  O   D GLU   A 1 23  ? -13.961 -3.105  -33.054 0.25 65.86  ? 66  GLU   A O   1 
ATOM   171  C  CB  A GLU   A 1 23  ? -13.979 -0.710  -34.954 0.25 69.05  ? 66  GLU   A CB  1 
ATOM   172  C  CB  B GLU   A 1 23  ? -13.979 -0.710  -34.954 0.25 69.05  ? 66  GLU   A CB  1 
ATOM   173  C  CB  C GLU   A 1 23  ? -14.036 -0.694  -34.682 0.25 68.52  ? 66  GLU   A CB  1 
ATOM   174  C  CB  D GLU   A 1 23  ? -14.036 -0.694  -34.682 0.25 68.52  ? 66  GLU   A CB  1 
ATOM   175  C  CG  A GLU   A 1 23  ? -12.484 -0.648  -35.208 0.25 74.18  ? 66  GLU   A CG  1 
ATOM   176  C  CG  B GLU   A 1 23  ? -12.484 -0.648  -35.208 0.25 74.18  ? 66  GLU   A CG  1 
ATOM   177  C  CG  C GLU   A 1 23  ? -12.522 -0.563  -34.716 0.25 72.99  ? 66  GLU   A CG  1 
ATOM   178  C  CG  D GLU   A 1 23  ? -12.522 -0.563  -34.716 0.25 72.99  ? 66  GLU   A CG  1 
ATOM   179  C  CD  A GLU   A 1 23  ? -11.855 0.706   -34.953 0.25 80.61  ? 66  GLU   A CD  1 
ATOM   180  C  CD  B GLU   A 1 23  ? -11.855 0.706   -34.953 0.25 80.61  ? 66  GLU   A CD  1 
ATOM   181  C  CD  C GLU   A 1 23  ? -11.973 0.652   -33.993 0.25 78.16  ? 66  GLU   A CD  1 
ATOM   182  C  CD  D GLU   A 1 23  ? -11.973 0.652   -33.993 0.25 78.16  ? 66  GLU   A CD  1 
ATOM   183  O  OE1 A GLU   A 1 23  ? -12.496 1.731   -35.283 0.25 81.99  ? 66  GLU   A OE1 1 
ATOM   184  O  OE1 B GLU   A 1 23  ? -12.496 1.731   -35.283 0.25 81.99  ? 66  GLU   A OE1 1 
ATOM   185  O  OE1 C GLU   A 1 23  ? -12.745 1.613   -33.771 0.25 78.85  ? 66  GLU   A OE1 1 
ATOM   186  O  OE1 D GLU   A 1 23  ? -12.745 1.613   -33.771 0.25 78.85  ? 66  GLU   A OE1 1 
ATOM   187  O  OE2 A GLU   A 1 23  ? -10.717 0.744   -34.431 0.25 82.52  ? 66  GLU   A OE2 1 
ATOM   188  O  OE2 B GLU   A 1 23  ? -10.717 0.744   -34.431 0.25 82.52  ? 66  GLU   A OE2 1 
ATOM   189  O  OE2 C GLU   A 1 23  ? -10.767 0.647   -33.654 0.25 79.85  ? 66  GLU   A OE2 1 
ATOM   190  O  OE2 D GLU   A 1 23  ? -10.767 0.647   -33.654 0.25 79.85  ? 66  GLU   A OE2 1 
ATOM   191  N  N   . VAL   A 1 24  ? -13.319 -4.189  -34.924 1.00 65.42  ? 67  VAL   A N   1 
ATOM   192  C  CA  . VAL   A 1 24  ? -12.668 -5.276  -34.184 1.00 63.80  ? 67  VAL   A CA  1 
ATOM   193  C  C   . VAL   A 1 24  ? -11.191 -4.972  -33.958 1.00 61.94  ? 67  VAL   A C   1 
ATOM   194  O  O   . VAL   A 1 24  ? -10.414 -5.002  -34.908 1.00 62.19  ? 67  VAL   A O   1 
ATOM   195  C  CB  . VAL   A 1 24  ? -12.895 -6.683  -34.801 1.00 64.21  ? 67  VAL   A CB  1 
ATOM   196  C  CG1 . VAL   A 1 24  ? -12.704 -7.752  -33.739 1.00 64.83  ? 67  VAL   A CG1 1 
ATOM   197  C  CG2 . VAL   A 1 24  ? -14.281 -6.819  -35.443 1.00 64.17  ? 67  VAL   A CG2 1 
ATOM   198  N  N   . THR   A 1 25  ? -10.806 -4.645  -32.720 1.00 60.18  ? 68  THR   A N   1 
ATOM   199  C  CA  . THR   A 1 25  ? -9.422  -4.279  -32.400 1.00 59.61  ? 68  THR   A CA  1 
ATOM   200  C  C   . THR   A 1 25  ? -8.993  -4.764  -30.990 1.00 59.47  ? 68  THR   A C   1 
ATOM   201  O  O   . THR   A 1 25  ? -9.817  -5.270  -30.237 1.00 59.32  ? 68  THR   A O   1 
ATOM   202  C  CB  . THR   A 1 25  ? -9.249  -2.753  -32.557 1.00 60.45  ? 68  THR   A CB  1 
ATOM   203  O  OG1 . THR   A 1 25  ? -7.854  -2.443  -32.563 1.00 61.25  ? 68  THR   A OG1 1 
ATOM   204  C  CG2 . THR   A 1 25  ? -9.919  -1.984  -31.437 1.00 60.49  ? 68  THR   A CG2 1 
ATOM   205  N  N   . GLY   A 1 26  ? -7.709  -4.628  -30.656 1.00 59.11  ? 69  GLY   A N   1 
ATOM   206  C  CA  . GLY   A 1 26  ? -7.200  -5.027  -29.356 1.00 59.15  ? 69  GLY   A CA  1 
ATOM   207  C  C   . GLY   A 1 26  ? -6.747  -6.471  -29.284 1.00 58.83  ? 69  GLY   A C   1 
ATOM   208  O  O   . GLY   A 1 26  ? -7.374  -7.357  -29.869 1.00 58.99  ? 69  GLY   A O   1 
ATOM   209  N  N   . ASN   A 1 27  ? -5.658  -6.711  -28.535 1.00 57.96  ? 70  ASN   A N   1 
ATOM   210  C  CA  . ASN   A 1 27  ? -5.084  -8.039  -28.315 1.00 57.43  ? 70  ASN   A CA  1 
ATOM   211  C  C   . ASN   A 1 27  ? -5.684  -8.738  -27.036 1.00 55.65  ? 70  ASN   A C   1 
ATOM   212  O  O   . ASN   A 1 27  ? -6.579  -8.167  -26.411 1.00 55.61  ? 70  ASN   A O   1 
ATOM   213  C  CB  . ASN   A 1 27  ? -3.545  -7.933  -28.285 1.00 59.28  ? 70  ASN   A CB  1 
ATOM   214  C  CG  . ASN   A 1 27  ? -3.005  -7.205  -27.078 1.00 63.42  ? 70  ASN   A CG  1 
ATOM   215  O  OD1 . ASN   A 1 27  ? -3.374  -6.058  -26.795 1.00 64.67  ? 70  ASN   A OD1 1 
ATOM   216  N  ND2 . ASN   A 1 27  ? -2.107  -7.855  -26.341 1.00 64.15  ? 70  ASN   A ND2 1 
ATOM   217  N  N   . SER   A 1 28  ? -5.240  -9.981  -26.683 1.00 53.99  ? 71  SER   A N   1 
ATOM   218  C  CA  . SER   A 1 28  ? -5.740  -10.744 -25.518 1.00 52.76  ? 71  SER   A CA  1 
ATOM   219  C  C   . SER   A 1 28  ? -4.583  -11.204 -24.606 1.00 51.58  ? 71  SER   A C   1 
ATOM   220  O  O   . SER   A 1 28  ? -4.262  -12.391 -24.553 1.00 51.84  ? 71  SER   A O   1 
ATOM   221  C  CB  . SER   A 1 28  ? -6.541  -11.967 -25.967 1.00 54.13  ? 71  SER   A CB  1 
ATOM   222  O  OG  . SER   A 1 28  ? -7.265  -11.792 -27.172 1.00 57.58  ? 71  SER   A OG  1 
ATOM   223  N  N   . PRO   A 1 29  ? -3.951  -10.292 -23.854 1.00 50.49  ? 72  PRO   A N   1 
ATOM   224  C  CA  . PRO   A 1 29  ? -2.799  -10.693 -23.029 1.00 49.85  ? 72  PRO   A CA  1 
ATOM   225  C  C   . PRO   A 1 29  ? -3.103  -11.514 -21.778 1.00 49.20  ? 72  PRO   A C   1 
ATOM   226  O  O   . PRO   A 1 29  ? -4.143  -11.338 -21.152 1.00 48.14  ? 72  PRO   A O   1 
ATOM   227  C  CB  . PRO   A 1 29  ? -2.180  -9.350  -22.650 1.00 50.83  ? 72  PRO   A CB  1 
ATOM   228  C  CG  . PRO   A 1 29  ? -3.368  -8.417  -22.574 1.00 51.45  ? 72  PRO   A CG  1 
ATOM   229  C  CD  . PRO   A 1 29  ? -4.204  -8.839  -23.755 1.00 49.99  ? 72  PRO   A CD  1 
ATOM   230  N  N   . ARG   A 1 30  ? -2.170  -12.402 -21.393 1.00 49.55  ? 73  ARG   A N   1 
ATOM   231  C  CA  . ARG   A 1 30  ? -2.309  -13.165 -20.141 1.00 50.20  ? 73  ARG   A CA  1 
ATOM   232  C  C   . ARG   A 1 30  ? -1.325  -12.587 -19.138 1.00 48.91  ? 73  ARG   A C   1 
ATOM   233  O  O   . ARG   A 1 30  ? -0.112  -12.727 -19.303 1.00 48.74  ? 73  ARG   A O   1 
ATOM   234  C  CB  . ARG   A 1 30  ? -2.129  -14.680 -20.340 1.00 53.01  ? 73  ARG   A CB  1 
ATOM   235  C  CG  . ARG   A 1 30  ? -3.358  -15.297 -21.000 1.00 58.51  ? 73  ARG   A CG  1 
ATOM   236  C  CD  . ARG   A 1 30  ? -3.268  -16.798 -21.175 1.00 63.89  ? 73  ARG   A CD  1 
ATOM   237  N  NE  . ARG   A 1 30  ? -4.110  -17.247 -22.290 1.00 68.51  ? 73  ARG   A NE  1 
ATOM   238  C  CZ  . ARG   A 1 30  ? -5.091  -18.138 -22.180 1.00 71.30  ? 73  ARG   A CZ  1 
ATOM   239  N  NH1 . ARG   A 1 30  ? -5.369  -18.690 -21.002 1.00 71.98  ? 73  ARG   A NH1 1 
ATOM   240  N  NH2 . ARG   A 1 30  ? -5.804  -18.483 -23.245 1.00 70.15  ? 73  ARG   A NH2 1 
ATOM   241  N  N   . LEU   A 1 31  ? -1.860  -11.851 -18.156 1.00 47.90  ? 74  LEU   A N   1 
ATOM   242  C  CA  . LEU   A 1 31  ? -1.095  -11.121 -17.153 1.00 47.50  ? 74  LEU   A CA  1 
ATOM   243  C  C   . LEU   A 1 31  ? -1.314  -11.590 -15.726 1.00 47.09  ? 74  LEU   A C   1 
ATOM   244  O  O   . LEU   A 1 31  ? -2.448  -11.594 -15.263 1.00 47.19  ? 74  LEU   A O   1 
ATOM   245  C  CB  . LEU   A 1 31  ? -1.498  -9.650  -17.210 1.00 47.45  ? 74  LEU   A CB  1 
ATOM   246  C  CG  . LEU   A 1 31  ? -1.287  -8.960  -18.532 1.00 48.81  ? 74  LEU   A CG  1 
ATOM   247  C  CD1 . LEU   A 1 31  ? -1.949  -7.600  -18.532 1.00 49.25  ? 74  LEU   A CD1 1 
ATOM   248  C  CD2 . LEU   A 1 31  ? 0.204   -8.886  -18.878 1.00 49.25  ? 74  LEU   A CD2 1 
ATOM   249  N  N   . ASP   A 1 32  ? -0.230  -11.872 -15.004 1.00 46.34  ? 75  ASP   A N   1 
ATOM   250  C  CA  . ASP   A 1 32  ? -0.282  -12.235 -13.590 1.00 46.67  ? 75  ASP   A CA  1 
ATOM   251  C  C   . ASP   A 1 32  ? -0.457  -10.943 -12.789 1.00 45.70  ? 75  ASP   A C   1 
ATOM   252  O  O   . ASP   A 1 32  ? 0.428   -10.081 -12.856 1.00 46.31  ? 75  ASP   A O   1 
ATOM   253  C  CB  . ASP   A 1 32  ? 1.047   -12.886 -13.177 1.00 49.54  ? 75  ASP   A CB  1 
ATOM   254  C  CG  . ASP   A 1 32  ? 0.990   -14.391 -13.049 1.00 56.84  ? 75  ASP   A CG  1 
ATOM   255  O  OD1 . ASP   A 1 32  ? 0.319   -14.883 -12.112 1.00 58.91  ? 75  ASP   A OD1 1 
ATOM   256  O  OD2 . ASP   A 1 32  ? 1.637   -15.078 -13.866 1.00 59.62  ? 75  ASP   A OD2 1 
ATOM   257  N  N   . VAL   A 1 33  ? -1.588  -10.774 -12.060 1.00 43.90  ? 76  VAL   A N   1 
ATOM   258  C  CA  . VAL   A 1 33  ? -1.793  -9.535  -11.307 1.00 43.19  ? 76  VAL   A CA  1 
ATOM   259  C  C   . VAL   A 1 33  ? -2.121  -9.776  -9.800  1.00 42.62  ? 76  VAL   A C   1 
ATOM   260  O  O   . VAL   A 1 33  ? -2.419  -10.898 -9.392  1.00 42.55  ? 76  VAL   A O   1 
ATOM   261  C  CB  . VAL   A 1 33  ? -2.830  -8.573  -11.980 1.00 43.18  ? 76  VAL   A CB  1 
ATOM   262  C  CG1 . VAL   A 1 33  ? -2.521  -8.335  -13.456 1.00 43.41  ? 76  VAL   A CG1 1 
ATOM   263  C  CG2 . VAL   A 1 33  ? -4.253  -9.064  -11.791 1.00 43.23  ? 76  VAL   A CG2 1 
ATOM   264  N  N   . ALA   A 1 34  ? -2.025  -8.704  -8.986  1.00 42.05  ? 77  ALA   A N   1 
ATOM   265  C  CA  . ALA   A 1 34  ? -2.344  -8.687  -7.562  1.00 42.11  ? 77  ALA   A CA  1 
ATOM   266  C  C   . ALA   A 1 34  ? -3.336  -7.560  -7.301  1.00 42.07  ? 77  ALA   A C   1 
ATOM   267  O  O   . ALA   A 1 34  ? -3.165  -6.467  -7.828  1.00 42.55  ? 77  ALA   A O   1 
ATOM   268  C  CB  . ALA   A 1 34  ? -1.088  -8.462  -6.735  1.00 42.00  ? 77  ALA   A CB  1 
ATOM   269  N  N   . LEU   A 1 35  ? -4.372  -7.823  -6.503  1.00 41.42  ? 78  LEU   A N   1 
ATOM   270  C  CA  . LEU   A 1 35  ? -5.380  -6.834  -6.145  1.00 41.17  ? 78  LEU   A CA  1 
ATOM   271  C  C   . LEU   A 1 35  ? -5.177  -6.455  -4.676  1.00 41.28  ? 78  LEU   A C   1 
ATOM   272  O  O   . LEU   A 1 35  ? -5.199  -7.322  -3.789  1.00 41.30  ? 78  LEU   A O   1 
ATOM   273  C  CB  . LEU   A 1 35  ? -6.786  -7.404  -6.377  1.00 41.22  ? 78  LEU   A CB  1 
ATOM   274  C  CG  . LEU   A 1 35  ? -7.953  -6.454  -6.120  1.00 42.76  ? 78  LEU   A CG  1 
ATOM   275  C  CD1 . LEU   A 1 35  ? -7.883  -5.237  -7.009  1.00 43.37  ? 78  LEU   A CD1 1 
ATOM   276  C  CD2 . LEU   A 1 35  ? -9.271  -7.157  -6.314  1.00 43.30  ? 78  LEU   A CD2 1 
ATOM   277  N  N   . ASP   A 1 36  ? -4.905  -5.175  -4.423  1.00 41.18  ? 79  ASP   A N   1 
ATOM   278  C  CA  . ASP   A 1 36  ? -4.668  -4.719  -3.058  1.00 41.54  ? 79  ASP   A CA  1 
ATOM   279  C  C   . ASP   A 1 36  ? -5.999  -4.318  -2.347  1.00 41.47  ? 79  ASP   A C   1 
ATOM   280  O  O   . ASP   A 1 36  ? -7.058  -4.293  -2.974  1.00 41.03  ? 79  ASP   A O   1 
ATOM   281  C  CB  . ASP   A 1 36  ? -3.568  -3.627  -3.020  1.00 43.08  ? 79  ASP   A CB  1 
ATOM   282  C  CG  . ASP   A 1 36  ? -3.961  -2.228  -3.452  1.00 48.71  ? 79  ASP   A CG  1 
ATOM   283  O  OD1 . ASP   A 1 36  ? -5.154  -2.005  -3.746  1.00 49.69  ? 79  ASP   A OD1 1 
ATOM   284  O  OD2 . ASP   A 1 36  ? -3.075  -1.348  -3.480  1.00 51.63  ? 79  ASP   A OD2 1 
ATOM   285  N  N   . GLU   A 1 37  ? -5.942  -4.044  -1.046  1.00 41.77  ? 80  GLU   A N   1 
ATOM   286  C  CA  . GLU   A 1 37  ? -7.108  -3.671  -0.256  1.00 42.86  ? 80  GLU   A CA  1 
ATOM   287  C  C   . GLU   A 1 37  ? -7.793  -2.395  -0.767  1.00 43.42  ? 80  GLU   A C   1 
ATOM   288  O  O   . GLU   A 1 37  ? -8.977  -2.217  -0.534  1.00 43.42  ? 80  GLU   A O   1 
ATOM   289  C  CB  . GLU   A 1 37  ? -6.710  -3.526  1.227   1.00 45.57  ? 80  GLU   A CB  1 
ATOM   290  C  CG  . GLU   A 1 37  ? -7.885  -3.555  2.191   1.00 51.92  ? 80  GLU   A CG  1 
ATOM   291  C  CD  . GLU   A 1 37  ? -7.529  -3.433  3.659   1.00 59.51  ? 80  GLU   A CD  1 
ATOM   292  O  OE1 . GLU   A 1 37  ? -7.222  -2.301  4.101   1.00 60.75  ? 80  GLU   A OE1 1 
ATOM   293  O  OE2 . GLU   A 1 37  ? -7.564  -4.467  4.368   1.00 61.85  ? 80  GLU   A OE2 1 
ATOM   294  N  N   . SER   A 1 38  ? -7.069  -1.520  -1.479  1.00 43.60  ? 81  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 38  ? -7.646  -0.281  -2.005  1.00 43.81  ? 81  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 38  ? -8.238  -0.386  -3.397  1.00 43.83  ? 81  SER   A C   1 
ATOM   297  O  O   . SER   A 1 38  ? -8.628  0.637   -3.956  1.00 44.49  ? 81  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 38  ? -6.624  0.847   -1.976  1.00 45.65  ? 81  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 38  ? -6.335  1.218   -0.637  1.00 49.20  ? 81  SER   A OG  1 
ATOM   300  N  N   . GLY   A 1 39  ? -8.304  -1.589  -3.956  1.00 43.20  ? 82  GLY   A N   1 
ATOM   301  C  CA  . GLY   A 1 39  ? -8.866  -1.797  -5.286  1.00 42.93  ? 82  GLY   A CA  1 
ATOM   302  C  C   . GLY   A 1 39  ? -7.906  -1.528  -6.428  1.00 42.42  ? 82  GLY   A C   1 
ATOM   303  O  O   . GLY   A 1 39  ? -8.334  -1.391  -7.573  1.00 42.43  ? 82  GLY   A O   1 
ATOM   304  N  N   . ASP   A 1 40  ? -6.599  -1.452  -6.137  1.00 41.56  ? 83  ASP   A N   1 
ATOM   305  C  CA  . ASP   A 1 40  ? -5.603  -1.200  -7.172  1.00 40.89  ? 83  ASP   A CA  1 
ATOM   306  C  C   . ASP   A 1 40  ? -4.943  -2.496  -7.638  1.00 39.79  ? 83  ASP   A C   1 
ATOM   307  O  O   . ASP   A 1 40  ? -4.389  -3.246  -6.831  1.00 39.49  ? 83  ASP   A O   1 
ATOM   308  C  CB  . ASP   A 1 40  ? -4.525  -0.226  -6.678  1.00 42.93  ? 83  ASP   A CB  1 
ATOM   309  C  CG  . ASP   A 1 40  ? -5.037  1.155   -6.329  1.00 49.67  ? 83  ASP   A CG  1 
ATOM   310  O  OD1 . ASP   A 1 40  ? -6.046  1.579   -6.922  1.00 51.03  ? 83  ASP   A OD1 1 
ATOM   311  O  OD2 . ASP   A 1 40  ? -4.425  1.814   -5.459  1.00 53.13  ? 83  ASP   A OD2 1 
ATOM   312  N  N   . PHE   A 1 41  ? -4.974  -2.739  -8.949  1.00 38.74  ? 84  PHE   A N   1 
ATOM   313  C  CA  . PHE   A 1 41  ? -4.312  -3.889  -9.543  1.00 37.95  ? 84  PHE   A CA  1 
ATOM   314  C  C   . PHE   A 1 41  ? -2.869  -3.520  -9.818  1.00 39.81  ? 84  PHE   A C   1 
ATOM   315  O  O   . PHE   A 1 41  ? -2.556  -2.384  -10.168 1.00 39.65  ? 84  PHE   A O   1 
ATOM   316  C  CB  . PHE   A 1 41  ? -4.972  -4.296  -10.867 1.00 35.76  ? 84  PHE   A CB  1 
ATOM   317  C  CG  . PHE   A 1 41  ? -6.337  -4.935  -10.777 1.00 34.25  ? 84  PHE   A CG  1 
ATOM   318  C  CD1 . PHE   A 1 41  ? -6.475  -6.263  -10.413 1.00 33.53  ? 84  PHE   A CD1 1 
ATOM   319  C  CD2 . PHE   A 1 41  ? -7.479  -4.226  -11.128 1.00 34.09  ? 84  PHE   A CD2 1 
ATOM   320  C  CE1 . PHE   A 1 41  ? -7.727  -6.861  -10.382 1.00 33.58  ? 84  PHE   A CE1 1 
ATOM   321  C  CE2 . PHE   A 1 41  ? -8.734  -4.822  -11.069 1.00 33.73  ? 84  PHE   A CE2 1 
ATOM   322  C  CZ  . PHE   A 1 41  ? -8.849  -6.135  -10.707 1.00 33.09  ? 84  PHE   A CZ  1 
ATOM   323  N  N   . SER   A 1 42  ? -1.991  -4.493  -9.691  1.00 41.74  ? 85  SER   A N   1 
ATOM   324  C  CA  . SER   A 1 42  ? -0.572  -4.305  -9.983  1.00 44.11  ? 85  SER   A CA  1 
ATOM   325  C  C   . SER   A 1 42  ? -0.042  -5.527  -10.721 1.00 46.35  ? 85  SER   A C   1 
ATOM   326  O  O   . SER   A 1 42  ? -0.573  -6.620  -10.539 1.00 46.36  ? 85  SER   A O   1 
ATOM   327  C  CB  . SER   A 1 42  ? 0.218   -4.092  -8.697  1.00 45.15  ? 85  SER   A CB  1 
ATOM   328  O  OG  . SER   A 1 42  ? -0.070  -5.118  -7.763  1.00 47.30  ? 85  SER   A OG  1 
ATOM   329  N  N   . LEU   A 1 43  ? 0.996   -5.355  -11.554 1.00 48.18  ? 86  LEU   A N   1 
ATOM   330  C  CA  . LEU   A 1 43  ? 1.568   -6.489  -12.280 1.00 50.24  ? 86  LEU   A CA  1 
ATOM   331  C  C   . LEU   A 1 43  ? 2.527   -7.237  -11.381 1.00 52.29  ? 86  LEU   A C   1 
ATOM   332  O  O   . LEU   A 1 43  ? 3.315   -6.620  -10.668 1.00 51.87  ? 86  LEU   A O   1 
ATOM   333  C  CB  . LEU   A 1 43  ? 2.340   -6.024  -13.521 1.00 50.66  ? 86  LEU   A CB  1 
ATOM   334  C  CG  . LEU   A 1 43  ? 1.543   -5.695  -14.772 1.00 52.65  ? 86  LEU   A CG  1 
ATOM   335  C  CD1 . LEU   A 1 43  ? 2.450   -5.139  -15.841 1.00 53.27  ? 86  LEU   A CD1 1 
ATOM   336  C  CD2 . LEU   A 1 43  ? 0.841   -6.924  -15.318 1.00 53.47  ? 86  LEU   A CD2 1 
ATOM   337  N  N   . VAL   A 1 44  ? 2.492   -8.565  -11.442 1.00 54.47  ? 87  VAL   A N   1 
ATOM   338  C  CA  . VAL   A 1 44  ? 3.435   -9.417  -10.718 1.00 57.12  ? 87  VAL   A CA  1 
ATOM   339  C  C   . VAL   A 1 44  ? 4.255   -10.073 -11.832 1.00 60.45  ? 87  VAL   A C   1 
ATOM   340  O  O   . VAL   A 1 44  ? 3.888   -11.157 -12.285 1.00 61.29  ? 87  VAL   A O   1 
ATOM   341  C  CB  . VAL   A 1 44  ? 2.690   -10.476 -9.867  1.00 57.44  ? 87  VAL   A CB  1 
ATOM   342  C  CG1 . VAL   A 1 44  ? 3.669   -11.374 -9.127  1.00 58.05  ? 87  VAL   A CG1 1 
ATOM   343  C  CG2 . VAL   A 1 44  ? 1.722   -9.812  -8.893  1.00 57.55  ? 87  VAL   A CG2 1 
ATOM   344  N  N   . GLU   A 1 45  ? 5.273   -9.369  -12.380 1.00 61.95  ? 88  GLU   A N   1 
ATOM   345  C  CA  . GLU   A 1 45  ? 6.044   -9.924  -13.506 1.00 63.89  ? 88  GLU   A CA  1 
ATOM   346  C  C   . GLU   A 1 45  ? 7.258   -10.756 -13.057 1.00 64.83  ? 88  GLU   A C   1 
ATOM   347  O  O   . GLU   A 1 45  ? 8.007   -11.275 -13.892 1.00 65.14  ? 88  GLU   A O   1 
ATOM   348  C  CB  . GLU   A 1 45  ? 6.459   -8.840  -14.535 1.00 66.79  ? 88  GLU   A CB  1 
ATOM   349  C  CG  . GLU   A 1 45  ? 5.340   -8.368  -15.456 1.00 72.67  ? 88  GLU   A CG  1 
ATOM   350  C  CD  . GLU   A 1 45  ? 5.793   -7.805  -16.795 1.00 81.21  ? 88  GLU   A CD  1 
ATOM   351  O  OE1 . GLU   A 1 45  ? 6.861   -8.233  -17.294 1.00 83.37  ? 88  GLU   A OE1 1 
ATOM   352  O  OE2 . GLU   A 1 45  ? 5.072   -6.945  -17.352 1.00 83.34  ? 88  GLU   A OE2 1 
ATOM   353  N  N   . GLY   B 2 7   ? -35.586 11.562  -11.955 1.00 52.17  ? 16  GLY   B N   1 
ATOM   354  C  CA  . GLY   B 2 7   ? -35.878 12.069  -13.291 1.00 52.65  ? 16  GLY   B CA  1 
ATOM   355  C  C   . GLY   B 2 7   ? -35.815 11.014  -14.387 1.00 53.02  ? 16  GLY   B C   1 
ATOM   356  O  O   . GLY   B 2 7   ? -36.826 10.363  -14.680 1.00 53.71  ? 16  GLY   B O   1 
ATOM   357  N  N   . GLU   B 2 8   ? -34.635 10.845  -15.027 1.00 51.92  ? 17  GLU   B N   1 
ATOM   358  C  CA  . GLU   B 2 8   ? -34.493 9.847   -16.084 1.00 51.23  ? 17  GLU   B CA  1 
ATOM   359  C  C   . GLU   B 2 8   ? -34.137 8.473   -15.506 1.00 50.08  ? 17  GLU   B C   1 
ATOM   360  O  O   . GLU   B 2 8   ? -33.064 8.300   -14.916 1.00 50.79  ? 17  GLU   B O   1 
ATOM   361  C  CB  . GLU   B 2 8   ? -33.472 10.279  -17.146 1.00 53.25  ? 17  GLU   B CB  1 
ATOM   362  C  CG  . GLU   B 2 8   ? -33.600 9.464   -18.422 1.00 57.24  ? 17  GLU   B CG  1 
ATOM   363  C  CD  . GLU   B 2 8   ? -32.784 9.969   -19.597 1.00 63.76  ? 17  GLU   B CD  1 
ATOM   364  O  OE1 . GLU   B 2 8   ? -31.805 10.717  -19.370 1.00 64.71  ? 17  GLU   B OE1 1 
ATOM   365  O  OE2 . GLU   B 2 8   ? -33.141 9.635   -20.750 1.00 66.54  ? 17  GLU   B OE2 1 
ATOM   366  N  N   A THR   B 2 9   ? -35.033 7.496   -15.670 0.25 49.57  ? 18  THR   B N   1 
ATOM   367  N  N   B THR   B 2 9   ? -35.038 7.500   -15.669 0.25 49.56  ? 18  THR   B N   1 
ATOM   368  N  N   C THR   B 2 9   ? -35.033 7.496   -15.670 0.25 49.57  ? 18  THR   B N   1 
ATOM   369  N  N   D THR   B 2 9   ? -35.038 7.500   -15.669 0.25 49.56  ? 18  THR   B N   1 
ATOM   370  C  CA  A THR   B 2 9   ? -34.792 6.147   -15.146 0.25 49.52  ? 18  THR   B CA  1 
ATOM   371  C  CA  B THR   B 2 9   ? -34.827 6.146   -15.158 0.25 49.49  ? 18  THR   B CA  1 
ATOM   372  C  CA  C THR   B 2 9   ? -34.792 6.147   -15.146 0.25 49.52  ? 18  THR   B CA  1 
ATOM   373  C  CA  D THR   B 2 9   ? -34.827 6.146   -15.158 0.25 49.49  ? 18  THR   B CA  1 
ATOM   374  C  C   A THR   B 2 9   ? -34.818 5.077   -16.260 0.25 49.07  ? 18  THR   B C   1 
ATOM   375  C  C   B THR   B 2 9   ? -34.815 5.080   -16.261 0.25 49.06  ? 18  THR   B C   1 
ATOM   376  C  C   C THR   B 2 9   ? -34.818 5.077   -16.260 0.25 49.07  ? 18  THR   B C   1 
ATOM   377  C  C   D THR   B 2 9   ? -34.815 5.080   -16.261 0.25 49.06  ? 18  THR   B C   1 
ATOM   378  O  O   A THR   B 2 9   ? -35.018 3.897   -15.972 0.25 49.36  ? 18  THR   B O   1 
ATOM   379  O  O   B THR   B 2 9   ? -34.998 3.901   -15.962 0.25 49.35  ? 18  THR   B O   1 
ATOM   380  O  O   C THR   B 2 9   ? -35.018 3.897   -15.972 0.25 49.36  ? 18  THR   B O   1 
ATOM   381  O  O   D THR   B 2 9   ? -34.998 3.901   -15.962 0.25 49.35  ? 18  THR   B O   1 
ATOM   382  C  CB  A THR   B 2 9   ? -35.745 5.798   -13.965 0.25 50.94  ? 18  THR   B CB  1 
ATOM   383  C  CB  B THR   B 2 9   ? -35.909 5.809   -14.130 0.25 50.85  ? 18  THR   B CB  1 
ATOM   384  C  CB  C THR   B 2 9   ? -35.745 5.798   -13.965 0.25 50.94  ? 18  THR   B CB  1 
ATOM   385  C  CB  D THR   B 2 9   ? -35.909 5.809   -14.130 0.25 50.85  ? 18  THR   B CB  1 
ATOM   386  O  OG1 A THR   B 2 9   ? -36.266 6.976   -13.333 0.25 51.95  ? 18  THR   B OG1 1 
ATOM   387  O  OG1 B THR   B 2 9   ? -37.189 5.923   -14.756 0.25 51.82  ? 18  THR   B OG1 1 
ATOM   388  O  OG1 C THR   B 2 9   ? -36.266 6.976   -13.333 0.25 51.95  ? 18  THR   B OG1 1 
ATOM   389  O  OG1 D THR   B 2 9   ? -37.189 5.923   -14.756 0.25 51.82  ? 18  THR   B OG1 1 
ATOM   390  C  CG2 A THR   B 2 9   ? -35.077 4.914   -12.912 0.25 51.36  ? 18  THR   B CG2 1 
ATOM   391  C  CG2 B THR   B 2 9   ? -35.846 6.705   -12.901 0.25 51.28  ? 18  THR   B CG2 1 
ATOM   392  C  CG2 C THR   B 2 9   ? -35.077 4.914   -12.912 0.25 51.36  ? 18  THR   B CG2 1 
ATOM   393  C  CG2 D THR   B 2 9   ? -35.846 6.705   -12.901 0.25 51.28  ? 18  THR   B CG2 1 
ATOM   394  N  N   . THR   B 2 10  ? -34.608 5.478   -17.523 1.00 48.22  ? 19  THR   B N   1 
ATOM   395  C  CA  . THR   B 2 10  ? -34.608 4.543   -18.638 1.00 45.33  ? 19  THR   B CA  1 
ATOM   396  C  C   . THR   B 2 10  ? -33.351 3.710   -18.628 1.00 42.02  ? 19  THR   B C   1 
ATOM   397  O  O   . THR   B 2 10  ? -32.278 4.237   -18.349 1.00 41.85  ? 19  THR   B O   1 
ATOM   398  C  CB  . THR   B 2 10  ? -34.687 5.322   -19.975 1.00 46.86  ? 19  THR   B CB  1 
ATOM   399  O  OG1 . THR   B 2 10  ? -35.727 6.303   -19.926 1.00 48.45  ? 19  THR   B OG1 1 
ATOM   400  C  CG2 . THR   B 2 10  ? -34.902 4.412   -21.174 1.00 47.15  ? 19  THR   B CG2 1 
ATOM   401  N  N   . ASP   B 2 11  ? -33.456 2.416   -18.976 1.00 39.48  ? 20  ASP   B N   1 
ATOM   402  C  CA  . ASP   B 2 11  ? -32.284 1.550   -19.106 1.00 38.11  ? 20  ASP   B CA  1 
ATOM   403  C  C   . ASP   B 2 11  ? -31.329 2.132   -20.177 1.00 36.49  ? 20  ASP   B C   1 
ATOM   404  O  O   . ASP   B 2 11  ? -31.771 2.870   -21.065 1.00 36.31  ? 20  ASP   B O   1 
ATOM   405  C  CB  . ASP   B 2 11  ? -32.708 0.145   -19.561 1.00 40.09  ? 20  ASP   B CB  1 
ATOM   406  C  CG  . ASP   B 2 11  ? -33.095 -0.815  -18.469 1.00 46.01  ? 20  ASP   B CG  1 
ATOM   407  O  OD1 . ASP   B 2 11  ? -33.612 -0.353  -17.427 1.00 46.80  ? 20  ASP   B OD1 1 
ATOM   408  O  OD2 . ASP   B 2 11  ? -32.890 -2.038  -18.658 1.00 49.01  ? 20  ASP   B OD2 1 
ATOM   409  N  N   . GLY   B 2 12  ? -30.054 1.793   -20.088 1.00 34.78  ? 21  GLY   B N   1 
ATOM   410  C  CA  . GLY   B 2 12  ? -29.076 2.283   -21.044 1.00 33.76  ? 21  GLY   B CA  1 
ATOM   411  C  C   . GLY   B 2 12  ? -27.772 2.677   -20.390 1.00 32.94  ? 21  GLY   B C   1 
ATOM   412  O  O   . GLY   B 2 12  ? -27.533 2.378   -19.212 1.00 31.83  ? 21  GLY   B O   1 
ATOM   413  N  N   . VAL   B 2 13  ? -26.892 3.302   -21.185 1.00 32.33  ? 22  VAL   B N   1 
ATOM   414  C  CA  . VAL   B 2 13  ? -25.583 3.766   -20.729 1.00 31.90  ? 22  VAL   B CA  1 
ATOM   415  C  C   . VAL   B 2 13  ? -25.656 5.280   -20.534 1.00 32.07  ? 22  VAL   B C   1 
ATOM   416  O  O   . VAL   B 2 13  ? -26.390 5.978   -21.260 1.00 32.71  ? 22  VAL   B O   1 
ATOM   417  C  CB  . VAL   B 2 13  ? -24.489 3.336   -21.727 1.00 32.62  ? 22  VAL   B CB  1 
ATOM   418  C  CG1 . VAL   B 2 13  ? -24.633 4.060   -23.077 1.00 33.16  ? 22  VAL   B CG1 1 
ATOM   419  C  CG2 . VAL   B 2 13  ? -23.102 3.509   -21.145 1.00 32.48  ? 22  VAL   B CG2 1 
ATOM   420  N  N   . TYR   B 2 14  ? -24.997 5.781   -19.483 1.00 31.18  ? 23  TYR   B N   1 
ATOM   421  C  CA  . TYR   B 2 14  ? -25.045 7.194   -19.125 1.00 30.83  ? 23  TYR   B CA  1 
ATOM   422  C  C   . TYR   B 2 14  ? -23.661 7.735   -18.840 1.00 31.63  ? 23  TYR   B C   1 
ATOM   423  O  O   . TYR   B 2 14  ? -22.817 7.015   -18.341 1.00 32.48  ? 23  TYR   B O   1 
ATOM   424  C  CB  . TYR   B 2 14  ? -25.889 7.396   -17.845 1.00 30.05  ? 23  TYR   B CB  1 
ATOM   425  C  CG  . TYR   B 2 14  ? -27.379 7.241   -18.026 1.00 29.93  ? 23  TYR   B CG  1 
ATOM   426  C  CD1 . TYR   B 2 14  ? -27.943 5.998   -18.276 1.00 30.34  ? 23  TYR   B CD1 1 
ATOM   427  C  CD2 . TYR   B 2 14  ? -28.233 8.319   -17.861 1.00 31.02  ? 23  TYR   B CD2 1 
ATOM   428  C  CE1 . TYR   B 2 14  ? -29.307 5.850   -18.464 1.00 31.53  ? 23  TYR   B CE1 1 
ATOM   429  C  CE2 . TYR   B 2 14  ? -29.602 8.188   -18.054 1.00 32.27  ? 23  TYR   B CE2 1 
ATOM   430  C  CZ  . TYR   B 2 14  ? -30.140 6.944   -18.337 1.00 33.32  ? 23  TYR   B CZ  1 
ATOM   431  O  OH  . TYR   B 2 14  ? -31.495 6.795   -18.521 1.00 35.54  ? 23  TYR   B OH  1 
ATOM   432  N  N   . ARG   B 2 15  ? -23.466 9.028   -19.036 1.00 31.35  ? 24  ARG   B N   1 
ATOM   433  C  CA  . ARG   B 2 15  ? -22.230 9.699   -18.680 1.00 31.58  ? 24  ARG   B CA  1 
ATOM   434  C  C   . ARG   B 2 15  ? -22.408 10.240  -17.272 1.00 32.24  ? 24  ARG   B C   1 
ATOM   435  O  O   . ARG   B 2 15  ? -23.503 10.689  -16.933 1.00 32.58  ? 24  ARG   B O   1 
ATOM   436  C  CB  . ARG   B 2 15  ? -21.991 10.904  -19.600 1.00 32.06  ? 24  ARG   B CB  1 
ATOM   437  C  CG  . ARG   B 2 15  ? -21.910 10.598  -21.086 1.00 33.21  ? 24  ARG   B CG  1 
ATOM   438  C  CD  . ARG   B 2 15  ? -21.477 11.854  -21.801 1.00 35.77  ? 24  ARG   B CD  1 
ATOM   439  N  NE  . ARG   B 2 15  ? -21.710 11.785  -23.242 1.00 38.59  ? 24  ARG   B NE  1 
ATOM   440  C  CZ  . ARG   B 2 15  ? -20.786 11.468  -24.137 1.00 39.78  ? 24  ARG   B CZ  1 
ATOM   441  N  NH1 . ARG   B 2 15  ? -19.541 11.207  -23.754 1.00 39.69  ? 24  ARG   B NH1 1 
ATOM   442  N  NH2 . ARG   B 2 15  ? -21.099 11.400  -25.424 1.00 38.64  ? 24  ARG   B NH2 1 
ATOM   443  N  N   . VAL   B 2 16  ? -21.325 10.245  -16.474 1.00 32.10  ? 25  VAL   B N   1 
ATOM   444  C  CA  . VAL   B 2 16  ? -21.247 10.808  -15.124 1.00 32.63  ? 25  VAL   B CA  1 
ATOM   445  C  C   . VAL   B 2 16  ? -20.429 12.107  -15.276 1.00 33.28  ? 25  VAL   B C   1 
ATOM   446  O  O   . VAL   B 2 16  ? -19.273 12.047  -15.693 1.00 33.23  ? 25  VAL   B O   1 
ATOM   447  C  CB  . VAL   B 2 16  ? -20.555 9.807   -14.157 1.00 33.34  ? 25  VAL   B CB  1 
ATOM   448  C  CG1 . VAL   B 2 16  ? -20.509 10.349  -12.733 1.00 34.14  ? 25  VAL   B CG1 1 
ATOM   449  C  CG2 . VAL   B 2 16  ? -21.250 8.455   -14.185 1.00 33.64  ? 25  VAL   B CG2 1 
ATOM   450  N  N   . MET   B 2 17  ? -21.049 13.270  -15.031 1.00 34.00  ? 26  MET   B N   1 
ATOM   451  C  CA  . MET   B 2 17  ? -20.428 14.580  -15.231 1.00 35.91  ? 26  MET   B CA  1 
ATOM   452  C  C   . MET   B 2 17  ? -20.212 15.372  -13.929 1.00 38.81  ? 26  MET   B C   1 
ATOM   453  O  O   . MET   B 2 17  ? -20.895 15.124  -12.945 1.00 38.21  ? 26  MET   B O   1 
ATOM   454  C  CB  . MET   B 2 17  ? -21.328 15.445  -16.139 1.00 35.99  ? 26  MET   B CB  1 
ATOM   455  C  CG  . MET   B 2 17  ? -21.802 14.776  -17.422 1.00 37.35  ? 26  MET   B CG  1 
ATOM   456  S  SD  . MET   B 2 17  ? -20.512 14.546  -18.669 1.00 37.49  ? 26  MET   B SD  1 
ATOM   457  C  CE  . MET   B 2 17  ? -20.187 16.222  -19.109 1.00 31.40  ? 26  MET   B CE  1 
ATOM   458  N  N   . THR   B 2 18  ? -19.332 16.401  -13.965 1.00 41.41  ? 27  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 18  ? -19.106 17.298  -12.831 1.00 44.19  ? 27  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 18  ? -18.908 18.766  -13.244 1.00 46.84  ? 27  THR   B C   1 
ATOM   461  O  O   . THR   B 2 18  ? -18.412 19.071  -14.329 1.00 46.24  ? 27  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 18  ? -17.970 16.825  -11.903 1.00 45.41  ? 27  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 18  ? -17.947 17.696  -10.762 1.00 47.31  ? 27  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 18  ? -16.607 16.831  -12.576 1.00 44.82  ? 27  THR   B CG2 1 
ATOM   465  N  N   . ARG   B 2 19  ? -19.284 19.680  -12.346 1.00 49.62  ? 28  ARG   B N   1 
ATOM   466  C  CA  . ARG   B 2 19  ? -19.108 21.114  -12.607 1.00 52.72  ? 28  ARG   B CA  1 
ATOM   467  C  C   . ARG   B 2 19  ? -18.044 21.778  -11.682 1.00 54.02  ? 28  ARG   B C   1 
ATOM   468  O  O   . ARG   B 2 19  ? -17.686 22.939  -11.900 1.00 54.04  ? 28  ARG   B O   1 
ATOM   469  C  CB  . ARG   B 2 19  ? -20.457 21.853  -12.579 1.00 55.58  ? 28  ARG   B CB  1 
ATOM   470  C  CG  . ARG   B 2 19  ? -21.365 21.433  -13.739 1.00 61.22  ? 28  ARG   B CG  1 
ATOM   471  C  CD  . ARG   B 2 19  ? -22.345 22.524  -14.131 1.00 66.84  ? 28  ARG   B CD  1 
ATOM   472  N  NE  . ARG   B 2 19  ? -23.197 22.133  -15.261 1.00 71.81  ? 28  ARG   B NE  1 
ATOM   473  C  CZ  . ARG   B 2 19  ? -24.476 21.777  -15.148 1.00 74.98  ? 28  ARG   B CZ  1 
ATOM   474  N  NH1 . ARG   B 2 19  ? -25.065 21.751  -13.954 1.00 74.80  ? 28  ARG   B NH1 1 
ATOM   475  N  NH2 . ARG   B 2 19  ? -25.176 21.442  -16.226 1.00 74.74  ? 28  ARG   B NH2 1 
ATOM   476  N  N   . ARG   B 2 20  ? -17.505 21.001  -10.709 1.00 54.75  ? 29  ARG   B N   1 
ATOM   477  C  CA  . ARG   B 2 20  ? -16.470 21.356  -9.728  1.00 56.12  ? 29  ARG   B CA  1 
ATOM   478  C  C   . ARG   B 2 20  ? -15.166 21.836  -10.413 1.00 56.24  ? 29  ARG   B C   1 
ATOM   479  O  O   . ARG   B 2 20  ? -14.454 22.702  -9.895  1.00 56.46  ? 29  ARG   B O   1 
ATOM   480  C  CB  . ARG   B 2 20  ? -16.170 20.103  -8.877  1.00 58.41  ? 29  ARG   B CB  1 
ATOM   481  C  CG  . ARG   B 2 20  ? -15.370 20.356  -7.608  1.00 63.36  ? 29  ARG   B CG  1 
ATOM   482  C  CD  . ARG   B 2 20  ? -14.948 19.041  -6.971  1.00 67.86  ? 29  ARG   B CD  1 
ATOM   483  N  NE  . ARG   B 2 20  ? -13.910 18.363  -7.755  1.00 71.58  ? 29  ARG   B NE  1 
ATOM   484  C  CZ  . ARG   B 2 20  ? -12.628 18.297  -7.404  1.00 73.95  ? 29  ARG   B CZ  1 
ATOM   485  N  NH1 . ARG   B 2 20  ? -12.213 18.846  -6.266  1.00 74.32  ? 29  ARG   B NH1 1 
ATOM   486  N  NH2 . ARG   B 2 20  ? -11.752 17.668  -8.179  1.00 73.09  ? 29  ARG   B NH2 1 
ATOM   487  N  N   . LEU   B 2 21  ? -14.857 21.238  -11.564 1.00 55.47  ? 30  LEU   B N   1 
ATOM   488  C  CA  . LEU   B 2 21  ? -13.680 21.532  -12.367 1.00 55.17  ? 30  LEU   B CA  1 
ATOM   489  C  C   . LEU   B 2 21  ? -14.065 22.643  -13.441 1.00 54.61  ? 30  LEU   B C   1 
ATOM   490  O  O   . LEU   B 2 21  ? -15.135 23.254  -13.332 1.00 54.69  ? 30  LEU   B O   1 
ATOM   491  C  CB  . LEU   B 2 21  ? -13.185 20.181  -12.986 1.00 55.48  ? 30  LEU   B CB  1 
ATOM   492  C  CG  . LEU   B 2 21  ? -12.511 19.147  -12.066 1.00 57.05  ? 30  LEU   B CG  1 
ATOM   493  C  CD1 . LEU   B 2 21  ? -11.403 19.764  -11.248 1.00 57.64  ? 30  LEU   B CD1 1 
ATOM   494  C  CD2 . LEU   B 2 21  ? -13.513 18.428  -11.182 1.00 57.88  ? 30  LEU   B CD2 1 
ATOM   495  N  N   A LEU   B 2 22  ? -13.190 22.896  -14.425 0.25 54.43  ? 31  LEU   B N   1 
ATOM   496  N  N   B LEU   B 2 22  ? -13.190 22.896  -14.425 0.25 54.43  ? 31  LEU   B N   1 
ATOM   497  N  N   C LEU   B 2 22  ? -13.190 22.896  -14.425 0.25 54.43  ? 31  LEU   B N   1 
ATOM   498  N  N   D LEU   B 2 22  ? -13.190 22.896  -14.425 0.25 54.43  ? 31  LEU   B N   1 
ATOM   499  C  CA  A LEU   B 2 22  ? -13.451 23.886  -15.464 0.25 54.73  ? 31  LEU   B CA  1 
ATOM   500  C  CA  B LEU   B 2 22  ? -13.451 23.886  -15.464 0.25 54.73  ? 31  LEU   B CA  1 
ATOM   501  C  CA  C LEU   B 2 22  ? -13.451 23.886  -15.464 0.25 54.74  ? 31  LEU   B CA  1 
ATOM   502  C  CA  D LEU   B 2 22  ? -13.451 23.886  -15.464 0.25 54.74  ? 31  LEU   B CA  1 
ATOM   503  C  C   A LEU   B 2 22  ? -14.494 23.347  -16.440 0.25 54.91  ? 31  LEU   B C   1 
ATOM   504  C  C   B LEU   B 2 22  ? -14.494 23.347  -16.440 0.25 54.91  ? 31  LEU   B C   1 
ATOM   505  C  C   C LEU   B 2 22  ? -14.494 23.347  -16.440 0.25 54.91  ? 31  LEU   B C   1 
ATOM   506  C  C   D LEU   B 2 22  ? -14.494 23.347  -16.440 0.25 54.91  ? 31  LEU   B C   1 
ATOM   507  O  O   A LEU   B 2 22  ? -14.310 22.266  -16.996 0.25 55.17  ? 31  LEU   B O   1 
ATOM   508  O  O   B LEU   B 2 22  ? -14.310 22.266  -16.996 0.25 55.17  ? 31  LEU   B O   1 
ATOM   509  O  O   C LEU   B 2 22  ? -14.310 22.267  -16.997 0.25 55.17  ? 31  LEU   B O   1 
ATOM   510  O  O   D LEU   B 2 22  ? -14.310 22.267  -16.997 0.25 55.17  ? 31  LEU   B O   1 
ATOM   511  C  CB  A LEU   B 2 22  ? -12.153 24.202  -16.212 0.25 54.94  ? 31  LEU   B CB  1 
ATOM   512  C  CB  B LEU   B 2 22  ? -12.153 24.202  -16.212 0.25 54.94  ? 31  LEU   B CB  1 
ATOM   513  C  CB  C LEU   B 2 22  ? -12.153 24.202  -16.212 0.25 54.95  ? 31  LEU   B CB  1 
ATOM   514  C  CB  D LEU   B 2 22  ? -12.153 24.202  -16.212 0.25 54.95  ? 31  LEU   B CB  1 
ATOM   515  C  CG  A LEU   B 2 22  ? -12.285 25.180  -17.361 0.25 56.44  ? 31  LEU   B CG  1 
ATOM   516  C  CG  B LEU   B 2 22  ? -12.285 25.180  -17.361 0.25 56.44  ? 31  LEU   B CG  1 
ATOM   517  C  CG  C LEU   B 2 22  ? -12.284 25.180  -17.360 0.25 56.47  ? 31  LEU   B CG  1 
ATOM   518  C  CG  D LEU   B 2 22  ? -12.284 25.180  -17.360 0.25 56.47  ? 31  LEU   B CG  1 
ATOM   519  C  CD1 A LEU   B 2 22  ? -12.036 26.602  -16.894 0.25 56.98  ? 31  LEU   B CD1 1 
ATOM   520  C  CD1 B LEU   B 2 22  ? -12.036 26.602  -16.894 0.25 56.98  ? 31  LEU   B CD1 1 
ATOM   521  C  CD1 C LEU   B 2 22  ? -12.036 26.602  -16.894 0.25 57.00  ? 31  LEU   B CD1 1 
ATOM   522  C  CD1 D LEU   B 2 22  ? -12.036 26.602  -16.894 0.25 57.00  ? 31  LEU   B CD1 1 
ATOM   523  C  CD2 A LEU   B 2 22  ? -11.351 24.809  -18.493 0.25 57.17  ? 31  LEU   B CD2 1 
ATOM   524  C  CD2 B LEU   B 2 22  ? -11.351 24.809  -18.493 0.25 57.17  ? 31  LEU   B CD2 1 
ATOM   525  C  CD2 C LEU   B 2 22  ? -11.351 24.809  -18.493 0.25 57.19  ? 31  LEU   B CD2 1 
ATOM   526  C  CD2 D LEU   B 2 22  ? -11.351 24.809  -18.493 0.25 57.19  ? 31  LEU   B CD2 1 
ATOM   527  N  N   . GLY   B 2 23  ? -15.574 24.097  -16.631 1.00 54.58  ? 32  GLY   B N   1 
ATOM   528  C  CA  . GLY   B 2 23  ? -16.660 23.705  -17.530 1.00 53.34  ? 32  GLY   B CA  1 
ATOM   529  C  C   . GLY   B 2 23  ? -17.422 22.482  -17.049 1.00 51.40  ? 32  GLY   B C   1 
ATOM   530  O  O   . GLY   B 2 23  ? -17.530 22.250  -15.844 1.00 51.58  ? 32  GLY   B O   1 
ATOM   531  N  N   . SER   B 2 24  ? -17.900 21.659  -17.983 1.00 49.51  ? 33  SER   B N   1 
ATOM   532  C  CA  . SER   B 2 24  ? -18.559 20.408  -17.635 1.00 48.33  ? 33  SER   B CA  1 
ATOM   533  C  C   . SER   B 2 24  ? -17.560 19.278  -17.931 1.00 46.35  ? 33  SER   B C   1 
ATOM   534  O  O   . SER   B 2 24  ? -17.315 18.976  -19.096 1.00 45.94  ? 33  SER   B O   1 
ATOM   535  C  CB  . SER   B 2 24  ? -19.824 20.224  -18.465 1.00 49.88  ? 33  SER   B CB  1 
ATOM   536  O  OG  . SER   B 2 24  ? -20.793 21.209  -18.152 1.00 52.52  ? 33  SER   B OG  1 
ATOM   537  N  N   . THR   B 2 25  ? -16.946 18.693  -16.896 1.00 44.79  ? 34  THR   B N   1 
ATOM   538  C  CA  . THR   B 2 25  ? -15.960 17.628  -17.102 1.00 43.97  ? 34  THR   B CA  1 
ATOM   539  C  C   . THR   B 2 25  ? -16.555 16.228  -16.881 1.00 42.16  ? 34  THR   B C   1 
ATOM   540  O  O   . THR   B 2 25  ? -17.155 15.986  -15.833 1.00 42.17  ? 34  THR   B O   1 
ATOM   541  C  CB  . THR   B 2 25  ? -14.707 17.863  -16.226 1.00 45.49  ? 34  THR   B CB  1 
ATOM   542  O  OG1 . THR   B 2 25  ? -14.113 19.136  -16.527 1.00 46.45  ? 34  THR   B OG1 1 
ATOM   543  C  CG2 . THR   B 2 25  ? -13.667 16.771  -16.412 1.00 45.98  ? 34  THR   B CG2 1 
ATOM   544  N  N   . GLN   B 2 26  ? -16.402 15.308  -17.854 1.00 40.32  ? 35  GLN   B N   1 
ATOM   545  C  CA  . GLN   B 2 26  ? -16.897 13.934  -17.673 1.00 39.07  ? 35  GLN   B CA  1 
ATOM   546  C  C   . GLN   B 2 26  ? -15.901 13.147  -16.811 1.00 37.89  ? 35  GLN   B C   1 
ATOM   547  O  O   . GLN   B 2 26  ? -14.726 13.074  -17.165 1.00 38.49  ? 35  GLN   B O   1 
ATOM   548  C  CB  . GLN   B 2 26  ? -17.099 13.219  -19.022 1.00 39.18  ? 35  GLN   B CB  1 
ATOM   549  C  CG  . GLN   B 2 26  ? -17.402 11.727  -18.887 1.00 40.42  ? 35  GLN   B CG  1 
ATOM   550  C  CD  . GLN   B 2 26  ? -17.795 11.130  -20.199 1.00 44.10  ? 35  GLN   B CD  1 
ATOM   551  O  OE1 . GLN   B 2 26  ? -18.503 11.752  -20.979 1.00 46.37  ? 35  GLN   B OE1 1 
ATOM   552  N  NE2 . GLN   B 2 26  ? -17.341 9.920   -20.483 1.00 43.93  ? 35  GLN   B NE2 1 
ATOM   553  N  N   . VAL   B 2 27  ? -16.367 12.540  -15.711 1.00 36.04  ? 36  VAL   B N   1 
ATOM   554  C  CA  . VAL   B 2 27  ? -15.507 11.762  -14.817 1.00 35.01  ? 36  VAL   B CA  1 
ATOM   555  C  C   . VAL   B 2 27  ? -15.622 10.236  -15.017 1.00 33.62  ? 36  VAL   B C   1 
ATOM   556  O  O   . VAL   B 2 27  ? -14.733 9.482   -14.613 1.00 34.01  ? 36  VAL   B O   1 
ATOM   557  C  CB  . VAL   B 2 27  ? -15.752 12.140  -13.330 1.00 36.19  ? 36  VAL   B CB  1 
ATOM   558  C  CG1 . VAL   B 2 27  ? -15.223 13.533  -13.019 1.00 37.12  ? 36  VAL   B CG1 1 
ATOM   559  C  CG2 . VAL   B 2 27  ? -17.224 12.037  -12.960 1.00 36.38  ? 36  VAL   B CG2 1 
ATOM   560  N  N   . GLY   B 2 28  ? -16.730 9.795   -15.590 1.00 31.80  ? 37  GLY   B N   1 
ATOM   561  C  CA  . GLY   B 2 28  ? -17.000 8.381   -15.786 1.00 30.68  ? 37  GLY   B CA  1 
ATOM   562  C  C   . GLY   B 2 28  ? -18.282 8.123   -16.550 1.00 29.49  ? 37  GLY   B C   1 
ATOM   563  O  O   . GLY   B 2 28  ? -18.887 9.043   -17.105 1.00 29.52  ? 37  GLY   B O   1 
ATOM   564  N  N   . VAL   B 2 29  ? -18.704 6.856   -16.565 1.00 27.99  ? 38  VAL   B N   1 
ATOM   565  C  CA  . VAL   B 2 29  ? -19.858 6.279   -17.260 1.00 26.21  ? 38  VAL   B CA  1 
ATOM   566  C  C   . VAL   B 2 29  ? -20.542 5.269   -16.306 1.00 25.50  ? 38  VAL   B C   1 
ATOM   567  O  O   . VAL   B 2 29  ? -19.912 4.770   -15.376 1.00 25.28  ? 38  VAL   B O   1 
ATOM   568  C  CB  . VAL   B 2 29  ? -19.351 5.564   -18.552 1.00 25.62  ? 38  VAL   B CB  1 
ATOM   569  C  CG1 . VAL   B 2 29  ? -20.464 4.856   -19.308 1.00 25.68  ? 38  VAL   B CG1 1 
ATOM   570  C  CG2 . VAL   B 2 29  ? -18.616 6.519   -19.475 1.00 25.80  ? 38  VAL   B CG2 1 
ATOM   571  N  N   . GLY   B 2 30  ? -21.798 4.941   -16.565 1.00 24.95  ? 39  GLY   B N   1 
ATOM   572  C  CA  . GLY   B 2 30  ? -22.514 3.943   -15.779 1.00 25.00  ? 39  GLY   B CA  1 
ATOM   573  C  C   . GLY   B 2 30  ? -23.673 3.314   -16.530 1.00 25.18  ? 39  GLY   B C   1 
ATOM   574  O  O   . GLY   B 2 30  ? -24.078 3.810   -17.582 1.00 24.74  ? 39  GLY   B O   1 
ATOM   575  N  N   . VAL   B 2 31  ? -24.261 2.258   -15.964 1.00 25.46  ? 40  VAL   B N   1 
ATOM   576  C  CA  . VAL   B 2 31  ? -25.379 1.551   -16.583 1.00 26.26  ? 40  VAL   B CA  1 
ATOM   577  C  C   . VAL   B 2 31  ? -26.655 1.622   -15.767 1.00 26.46  ? 40  VAL   B C   1 
ATOM   578  O  O   . VAL   B 2 31  ? -26.656 1.164   -14.621 1.00 27.48  ? 40  VAL   B O   1 
ATOM   579  C  CB  . VAL   B 2 31  ? -24.999 0.071   -16.817 1.00 27.61  ? 40  VAL   B CB  1 
ATOM   580  C  CG1 . VAL   B 2 31  ? -26.186 -0.723  -17.360 1.00 28.80  ? 40  VAL   B CG1 1 
ATOM   581  C  CG2 . VAL   B 2 31  ? -23.808 -0.038  -17.757 1.00 27.73  ? 40  VAL   B CG2 1 
ATOM   582  N  N   . MET   B 2 32  ? -27.750 2.142   -16.349 1.00 25.49  ? 41  MET   B N   1 
ATOM   583  C  CA  . MET   B 2 32  ? -29.053 2.123   -15.699 1.00 26.07  ? 41  MET   B CA  1 
ATOM   584  C  C   . MET   B 2 32  ? -29.712 0.809   -16.100 1.00 27.05  ? 41  MET   B C   1 
ATOM   585  O  O   . MET   B 2 32  ? -29.712 0.477   -17.275 1.00 27.76  ? 41  MET   B O   1 
ATOM   586  C  CB  . MET   B 2 32  ? -29.946 3.300   -16.140 1.00 26.58  ? 41  MET   B CB  1 
ATOM   587  C  CG  . MET   B 2 32  ? -31.229 3.492   -15.275 1.00 28.63  ? 41  MET   B CG  1 
ATOM   588  S  SD  . MET   B 2 32  ? -30.974 4.187   -13.593 1.00 33.59  ? 41  MET   B SD  1 
ATOM   589  C  CE  . MET   B 2 32  ? -30.025 5.667   -14.025 1.00 30.00  ? 41  MET   B CE  1 
ATOM   590  N  N   . GLN   B 2 33  ? -30.199 0.017   -15.132 1.00 27.08  ? 42  GLN   B N   1 
ATOM   591  C  CA  . GLN   B 2 33  ? -30.868 -1.244  -15.441 1.00 27.53  ? 42  GLN   B CA  1 
ATOM   592  C  C   . GLN   B 2 33  ? -31.803 -1.602  -14.304 1.00 28.25  ? 42  GLN   B C   1 
ATOM   593  O  O   . GLN   B 2 33  ? -31.396 -1.524  -13.148 1.00 28.18  ? 42  GLN   B O   1 
ATOM   594  C  CB  . GLN   B 2 33  ? -29.879 -2.393  -15.698 1.00 29.02  ? 42  GLN   B CB  1 
ATOM   595  C  CG  . GLN   B 2 33  ? -30.608 -3.593  -16.316 1.00 33.49  ? 42  GLN   B CG  1 
ATOM   596  C  CD  . GLN   B 2 33  ? -29.756 -4.791  -16.659 1.00 37.01  ? 42  GLN   B CD  1 
ATOM   597  O  OE1 . GLN   B 2 33  ? -29.957 -5.884  -16.128 1.00 37.98  ? 42  GLN   B OE1 1 
ATOM   598  N  NE2 . GLN   B 2 33  ? -28.826 -4.631  -17.593 1.00 37.71  ? 42  GLN   B NE2 1 
ATOM   599  N  N   . GLU   B 2 34  ? -33.072 -1.923  -14.607 1.00 28.49  ? 43  GLU   B N   1 
ATOM   600  C  CA  . GLU   B 2 34  ? -34.053 -2.257  -13.574 1.00 29.14  ? 43  GLU   B CA  1 
ATOM   601  C  C   . GLU   B 2 34  ? -34.172 -1.180  -12.472 1.00 28.78  ? 43  GLU   B C   1 
ATOM   602  O  O   . GLU   B 2 34  ? -34.332 -1.495  -11.292 1.00 29.20  ? 43  GLU   B O   1 
ATOM   603  C  CB  . GLU   B 2 34  ? -33.780 -3.649  -12.980 1.00 32.12  ? 43  GLU   B CB  1 
ATOM   604  C  CG  . GLU   B 2 34  ? -33.947 -4.764  -13.994 1.00 37.20  ? 43  GLU   B CG  1 
ATOM   605  C  CD  . GLU   B 2 34  ? -33.356 -6.100  -13.588 1.00 45.46  ? 43  GLU   B CD  1 
ATOM   606  O  OE1 . GLU   B 2 34  ? -33.915 -6.746  -12.672 1.00 48.81  ? 43  GLU   B OE1 1 
ATOM   607  O  OE2 . GLU   B 2 34  ? -32.338 -6.508  -14.193 1.00 47.34  ? 43  GLU   B OE2 1 
ATOM   608  N  N   . GLY   B 2 35  ? -34.084 0.079   -12.880 1.00 27.84  ? 44  GLY   B N   1 
ATOM   609  C  CA  . GLY   B 2 35  ? -34.182 1.214   -11.977 1.00 27.52  ? 44  GLY   B CA  1 
ATOM   610  C  C   . GLY   B 2 35  ? -32.961 1.431   -11.108 1.00 27.54  ? 44  GLY   B C   1 
ATOM   611  O  O   . GLY   B 2 35  ? -33.026 2.226   -10.176 1.00 27.94  ? 44  GLY   B O   1 
ATOM   612  N  N   . VAL   B 2 36  ? -31.837 0.725   -11.386 1.00 27.12  ? 45  VAL   B N   1 
ATOM   613  C  CA  . VAL   B 2 36  ? -30.600 0.811   -10.600 1.00 26.75  ? 45  VAL   B CA  1 
ATOM   614  C  C   . VAL   B 2 36  ? -29.417 1.362   -11.423 1.00 26.54  ? 45  VAL   B C   1 
ATOM   615  O  O   . VAL   B 2 36  ? -29.173 0.919   -12.563 1.00 26.19  ? 45  VAL   B O   1 
ATOM   616  C  CB  . VAL   B 2 36  ? -30.261 -0.539  -9.907  1.00 26.61  ? 45  VAL   B CB  1 
ATOM   617  C  CG1 . VAL   B 2 36  ? -28.884 -0.508  -9.251  1.00 26.34  ? 45  VAL   B CG1 1 
ATOM   618  C  CG2 . VAL   B 2 36  ? -31.329 -0.898  -8.884  1.00 27.03  ? 45  VAL   B CG2 1 
ATOM   619  N  N   . PHE   B 2 37  ? -28.709 2.371   -10.854 1.00 25.81  ? 46  PHE   B N   1 
ATOM   620  C  CA  . PHE   B 2 37  ? -27.556 2.915   -11.554 1.00 25.61  ? 46  PHE   B CA  1 
ATOM   621  C  C   . PHE   B 2 37  ? -26.325 2.158   -11.106 1.00 24.34  ? 46  PHE   B C   1 
ATOM   622  O  O   . PHE   B 2 37  ? -26.073 2.109   -9.924  1.00 24.33  ? 46  PHE   B O   1 
ATOM   623  C  CB  . PHE   B 2 37  ? -27.363 4.411   -11.290 1.00 25.53  ? 46  PHE   B CB  1 
ATOM   624  C  CG  . PHE   B 2 37  ? -26.415 5.007   -12.307 1.00 26.34  ? 46  PHE   B CG  1 
ATOM   625  C  CD1 . PHE   B 2 37  ? -26.605 4.797   -13.659 1.00 26.62  ? 46  PHE   B CD1 1 
ATOM   626  C  CD2 . PHE   B 2 37  ? -25.328 5.764   -11.908 1.00 27.43  ? 46  PHE   B CD2 1 
ATOM   627  C  CE1 . PHE   B 2 37  ? -25.773 5.388   -14.595 1.00 27.47  ? 46  PHE   B CE1 1 
ATOM   628  C  CE2 . PHE   B 2 37  ? -24.475 6.327   -12.848 1.00 27.69  ? 46  PHE   B CE2 1 
ATOM   629  C  CZ  . PHE   B 2 37  ? -24.713 6.146   -14.184 1.00 27.57  ? 46  PHE   B CZ  1 
ATOM   630  N  N   . HIS   B 2 38  ? -25.547 1.605   -12.028 1.00 23.13  ? 47  HIS   B N   1 
ATOM   631  C  CA  . HIS   B 2 38  ? -24.336 0.872   -11.690 1.00 22.87  ? 47  HIS   B CA  1 
ATOM   632  C  C   . HIS   B 2 38  ? -23.155 1.650   -12.202 1.00 23.55  ? 47  HIS   B C   1 
ATOM   633  O  O   . HIS   B 2 38  ? -23.179 2.037   -13.355 1.00 23.50  ? 47  HIS   B O   1 
ATOM   634  C  CB  . HIS   B 2 38  ? -24.340 -0.495  -12.383 1.00 22.21  ? 47  HIS   B CB  1 
ATOM   635  C  CG  . HIS   B 2 38  ? -25.565 -1.302  -12.107 1.00 22.92  ? 47  HIS   B CG  1 
ATOM   636  N  ND1 . HIS   B 2 38  ? -26.774 -1.002  -12.704 1.00 24.21  ? 47  HIS   B ND1 1 
ATOM   637  C  CD2 . HIS   B 2 38  ? -25.726 -2.386  -11.313 1.00 23.95  ? 47  HIS   B CD2 1 
ATOM   638  C  CE1 . HIS   B 2 38  ? -27.628 -1.914  -12.266 1.00 24.43  ? 47  HIS   B CE1 1 
ATOM   639  N  NE2 . HIS   B 2 38  ? -27.042 -2.771  -11.432 1.00 24.75  ? 47  HIS   B NE2 1 
ATOM   640  N  N   . THR   B 2 39  ? -22.129 1.906   -11.368 1.00 23.68  ? 48  THR   B N   1 
ATOM   641  C  CA  . THR   B 2 39  ? -20.920 2.590   -11.864 1.00 23.97  ? 48  THR   B CA  1 
ATOM   642  C  C   . THR   B 2 39  ? -19.681 2.046   -11.102 1.00 24.33  ? 48  THR   B C   1 
ATOM   643  O  O   . THR   B 2 39  ? -19.794 1.070   -10.359 1.00 23.94  ? 48  THR   B O   1 
ATOM   644  C  CB  . THR   B 2 39  ? -21.101 4.158   -11.871 1.00 24.89  ? 48  THR   B CB  1 
ATOM   645  O  OG1 . THR   B 2 39  ? -20.096 4.754   -12.682 1.00 24.96  ? 48  THR   B OG1 1 
ATOM   646  C  CG2 . THR   B 2 39  ? -20.997 4.771   -10.498 1.00 25.63  ? 48  THR   B CG2 1 
ATOM   647  N  N   . MET   B 2 40  ? -18.499 2.630   -11.327 1.00 24.58  ? 49  MET   B N   1 
ATOM   648  C  CA  . MET   B 2 40  ? -17.299 2.257   -10.603 1.00 24.95  ? 49  MET   B CA  1 
ATOM   649  C  C   . MET   B 2 40  ? -17.136 3.245   -9.415  1.00 25.73  ? 49  MET   B C   1 
ATOM   650  O  O   . MET   B 2 40  ? -17.465 4.423   -9.556  1.00 26.23  ? 49  MET   B O   1 
ATOM   651  C  CB  . MET   B 2 40  ? -16.102 2.216   -11.554 1.00 25.03  ? 49  MET   B CB  1 
ATOM   652  C  CG  . MET   B 2 40  ? -16.375 1.316   -12.746 1.00 27.42  ? 49  MET   B CG  1 
ATOM   653  S  SD  . MET   B 2 40  ? -14.958 0.364   -13.294 1.00 33.23  ? 49  MET   B SD  1 
ATOM   654  C  CE  . MET   B 2 40  ? -14.865 -0.849  -12.102 1.00 27.09  ? 49  MET   B CE  1 
ATOM   655  N  N   A TRP   B 2 41  ? -16.649 2.753   -8.268  0.25 25.80  ? 50  TRP   B N   1 
ATOM   656  N  N   B TRP   B 2 41  ? -16.653 2.753   -8.259  0.25 25.66  ? 50  TRP   B N   1 
ATOM   657  N  N   C TRP   B 2 41  ? -16.649 2.753   -8.268  0.25 25.80  ? 50  TRP   B N   1 
ATOM   658  N  N   D TRP   B 2 41  ? -16.653 2.753   -8.259  0.25 25.66  ? 50  TRP   B N   1 
ATOM   659  C  CA  A TRP   B 2 41  ? -16.471 3.558   -7.063  0.25 26.57  ? 50  TRP   B CA  1 
ATOM   660  C  CA  B TRP   B 2 41  ? -16.471 3.549   -7.042  0.25 26.31  ? 50  TRP   B CA  1 
ATOM   661  C  CA  C TRP   B 2 41  ? -16.471 3.558   -7.063  0.25 26.57  ? 50  TRP   B CA  1 
ATOM   662  C  CA  D TRP   B 2 41  ? -16.471 3.549   -7.042  0.25 26.31  ? 50  TRP   B CA  1 
ATOM   663  C  C   A TRP   B 2 41  ? -15.509 4.712   -7.267  0.25 27.10  ? 50  TRP   B C   1 
ATOM   664  C  C   B TRP   B 2 41  ? -15.479 4.695   -7.216  0.25 26.98  ? 50  TRP   B C   1 
ATOM   665  C  C   C TRP   B 2 41  ? -15.509 4.712   -7.267  0.25 27.10  ? 50  TRP   B C   1 
ATOM   666  C  C   D TRP   B 2 41  ? -15.479 4.695   -7.216  0.25 26.98  ? 50  TRP   B C   1 
ATOM   667  O  O   A TRP   B 2 41  ? -15.759 5.798   -6.757  0.25 27.45  ? 50  TRP   B O   1 
ATOM   668  O  O   B TRP   B 2 41  ? -15.694 5.765   -6.654  0.25 27.33  ? 50  TRP   B O   1 
ATOM   669  O  O   C TRP   B 2 41  ? -15.759 5.798   -6.757  0.25 27.45  ? 50  TRP   B O   1 
ATOM   670  O  O   D TRP   B 2 41  ? -15.694 5.765   -6.654  0.25 27.33  ? 50  TRP   B O   1 
ATOM   671  C  CB  A TRP   B 2 41  ? -16.012 2.697   -5.872  0.25 26.56  ? 50  TRP   B CB  1 
ATOM   672  C  CB  B TRP   B 2 41  ? -16.088 2.663   -5.836  0.25 26.09  ? 50  TRP   B CB  1 
ATOM   673  C  CB  C TRP   B 2 41  ? -16.012 2.697   -5.872  0.25 26.56  ? 50  TRP   B CB  1 
ATOM   674  C  CB  D TRP   B 2 41  ? -16.088 2.663   -5.836  0.25 26.09  ? 50  TRP   B CB  1 
ATOM   675  C  CG  A TRP   B 2 41  ? -16.080 3.413   -4.555  0.25 27.32  ? 50  TRP   B CG  1 
ATOM   676  C  CG  B TRP   B 2 41  ? -15.979 3.406   -4.532  0.25 26.60  ? 50  TRP   B CG  1 
ATOM   677  C  CG  C TRP   B 2 41  ? -16.080 3.413   -4.555  0.25 27.32  ? 50  TRP   B CG  1 
ATOM   678  C  CG  D TRP   B 2 41  ? -15.979 3.406   -4.532  0.25 26.60  ? 50  TRP   B CG  1 
ATOM   679  C  CD1 A TRP   B 2 41  ? -17.126 3.420   -3.682  0.25 28.21  ? 50  TRP   B CD1 1 
ATOM   680  C  CD1 B TRP   B 2 41  ? -14.905 4.113   -4.076  0.25 27.51  ? 50  TRP   B CD1 1 
ATOM   681  C  CD1 C TRP   B 2 41  ? -17.126 3.420   -3.682  0.25 28.21  ? 50  TRP   B CD1 1 
ATOM   682  C  CD1 D TRP   B 2 41  ? -14.905 4.113   -4.076  0.25 27.51  ? 50  TRP   B CD1 1 
ATOM   683  C  CD2 A TRP   B 2 41  ? -15.060 4.235   -3.966  0.25 27.55  ? 50  TRP   B CD2 1 
ATOM   684  C  CD2 B TRP   B 2 41  ? -16.975 3.482   -3.502  0.25 26.58  ? 50  TRP   B CD2 1 
ATOM   685  C  CD2 C TRP   B 2 41  ? -15.060 4.235   -3.966  0.25 27.55  ? 50  TRP   B CD2 1 
ATOM   686  C  CD2 D TRP   B 2 41  ? -16.975 3.482   -3.502  0.25 26.58  ? 50  TRP   B CD2 1 
ATOM   687  N  NE1 A TRP   B 2 41  ? -16.824 4.196   -2.588  0.25 28.60  ? 50  TRP   B NE1 1 
ATOM   688  N  NE1 B TRP   B 2 41  ? -15.185 4.657   -2.845  0.25 27.75  ? 50  TRP   B NE1 1 
ATOM   689  N  NE1 C TRP   B 2 41  ? -16.824 4.196   -2.588  0.25 28.60  ? 50  TRP   B NE1 1 
ATOM   690  N  NE1 D TRP   B 2 41  ? -15.185 4.657   -2.845  0.25 27.75  ? 50  TRP   B NE1 1 
ATOM   691  C  CE2 A TRP   B 2 41  ? -15.561 4.707   -2.736  0.25 28.36  ? 50  TRP   B CE2 1 
ATOM   692  C  CE2 B TRP   B 2 41  ? -16.447 4.279   -2.466  0.25 27.40  ? 50  TRP   B CE2 1 
ATOM   693  C  CE2 C TRP   B 2 41  ? -15.561 4.707   -2.736  0.25 28.36  ? 50  TRP   B CE2 1 
ATOM   694  C  CE2 D TRP   B 2 41  ? -16.447 4.279   -2.466  0.25 27.40  ? 50  TRP   B CE2 1 
ATOM   695  C  CE3 A TRP   B 2 41  ? -13.766 4.606   -4.351  0.25 28.08  ? 50  TRP   B CE3 1 
ATOM   696  C  CE3 B TRP   B 2 41  ? -18.267 2.966   -3.360  0.25 27.08  ? 50  TRP   B CE3 1 
ATOM   697  C  CE3 C TRP   B 2 41  ? -13.766 4.606   -4.351  0.25 28.08  ? 50  TRP   B CE3 1 
ATOM   698  C  CE3 D TRP   B 2 41  ? -18.267 2.966   -3.360  0.25 27.08  ? 50  TRP   B CE3 1 
ATOM   699  C  CZ2 A TRP   B 2 41  ? -14.819 5.538   -1.898  0.25 29.06  ? 50  TRP   B CZ2 1 
ATOM   700  C  CZ2 B TRP   B 2 41  ? -17.168 4.573   -1.309  0.25 27.95  ? 50  TRP   B CZ2 1 
ATOM   701  C  CZ2 C TRP   B 2 41  ? -14.819 5.538   -1.898  0.25 29.06  ? 50  TRP   B CZ2 1 
ATOM   702  C  CZ2 D TRP   B 2 41  ? -17.168 4.573   -1.309  0.25 27.95  ? 50  TRP   B CZ2 1 
ATOM   703  C  CZ3 A TRP   B 2 41  ? -13.039 5.438   -3.525  0.25 29.08  ? 50  TRP   B CZ3 1 
ATOM   704  C  CZ3 B TRP   B 2 41  ? -18.978 3.258   -2.213  0.25 27.94  ? 50  TRP   B CZ3 1 
ATOM   705  C  CZ3 C TRP   B 2 41  ? -13.039 5.438   -3.525  0.25 29.08  ? 50  TRP   B CZ3 1 
ATOM   706  C  CZ3 D TRP   B 2 41  ? -18.978 3.258   -2.213  0.25 27.94  ? 50  TRP   B CZ3 1 
ATOM   707  C  CH2 A TRP   B 2 41  ? -13.561 5.887   -2.309  0.25 29.22  ? 50  TRP   B CH2 1 
ATOM   708  C  CH2 B TRP   B 2 41  ? -18.428 4.049   -1.202  0.25 28.05  ? 50  TRP   B CH2 1 
ATOM   709  C  CH2 C TRP   B 2 41  ? -13.561 5.887   -2.309  0.25 29.22  ? 50  TRP   B CH2 1 
ATOM   710  C  CH2 D TRP   B 2 41  ? -18.428 4.049   -1.202  0.25 28.05  ? 50  TRP   B CH2 1 
ATOM   711  N  N   . HIS   B 2 42  ? -14.402 4.486   -7.974  1.00 27.00  ? 51  HIS   B N   1 
ATOM   712  C  CA  . HIS   B 2 42  ? -13.404 5.541   -8.189  1.00 27.91  ? 51  HIS   B CA  1 
ATOM   713  C  C   . HIS   B 2 42  ? -13.936 6.757   -8.987  1.00 29.01  ? 51  HIS   B C   1 
ATOM   714  O  O   . HIS   B 2 42  ? -13.375 7.839   -8.870  1.00 30.06  ? 51  HIS   B O   1 
ATOM   715  C  CB  . HIS   B 2 42  ? -12.112 4.983   -8.805  1.00 27.92  ? 51  HIS   B CB  1 
ATOM   716  C  CG  . HIS   B 2 42  ? -12.205 4.701   -10.265 1.00 29.02  ? 51  HIS   B CG  1 
ATOM   717  N  ND1 . HIS   B 2 42  ? -12.414 3.423   -10.738 1.00 30.83  ? 51  HIS   B ND1 1 
ATOM   718  C  CD2 . HIS   B 2 42  ? -12.059 5.537   -11.321 1.00 29.63  ? 51  HIS   B CD2 1 
ATOM   719  C  CE1 . HIS   B 2 42  ? -12.417 3.531   -12.057 1.00 30.67  ? 51  HIS   B CE1 1 
ATOM   720  N  NE2 . HIS   B 2 42  ? -12.224 4.786   -12.444 1.00 30.04  ? 51  HIS   B NE2 1 
ATOM   721  N  N   . VAL   B 2 43  ? -15.042 6.593   -9.732  1.00 28.68  ? 52  VAL   B N   1 
ATOM   722  C  CA  . VAL   B 2 43  ? -15.679 7.656   -10.504 1.00 28.82  ? 52  VAL   B CA  1 
ATOM   723  C  C   . VAL   B 2 43  ? -16.395 8.658   -9.593  1.00 29.78  ? 52  VAL   B C   1 
ATOM   724  O  O   . VAL   B 2 43  ? -16.108 9.848   -9.669  1.00 30.12  ? 52  VAL   B O   1 
ATOM   725  C  CB  . VAL   B 2 43  ? -16.628 7.041   -11.569 1.00 29.11  ? 52  VAL   B CB  1 
ATOM   726  C  CG1 . VAL   B 2 43  ? -17.570 8.084   -12.171 1.00 29.85  ? 52  VAL   B CG1 1 
ATOM   727  C  CG2 . VAL   B 2 43  ? -15.832 6.332   -12.666 1.00 28.97  ? 52  VAL   B CG2 1 
ATOM   728  N  N   . THR   B 2 44  ? -17.275 8.171   -8.687  1.00 30.16  ? 53  THR   B N   1 
ATOM   729  C  CA  . THR   B 2 44  ? -18.113 9.015   -7.820  1.00 30.40  ? 53  THR   B CA  1 
ATOM   730  C  C   . THR   B 2 44  ? -17.666 9.151   -6.352  1.00 31.35  ? 53  THR   B C   1 
ATOM   731  O  O   . THR   B 2 44  ? -18.106 10.078  -5.678  1.00 31.71  ? 53  THR   B O   1 
ATOM   732  C  CB  . THR   B 2 44  ? -19.578 8.522   -7.863  1.00 30.68  ? 53  THR   B CB  1 
ATOM   733  O  OG1 . THR   B 2 44  ? -19.716 7.326   -7.098  1.00 31.71  ? 53  THR   B OG1 1 
ATOM   734  C  CG2 . THR   B 2 44  ? -20.086 8.262   -9.287  1.00 30.59  ? 53  THR   B CG2 1 
ATOM   735  N  N   . LYS   B 2 45  ? -16.815 8.249   -5.866  1.00 31.61  ? 54  LYS   B N   1 
ATOM   736  C  CA  . LYS   B 2 45  ? -16.352 8.140   -4.471  1.00 33.23  ? 54  LYS   B CA  1 
ATOM   737  C  C   . LYS   B 2 45  ? -17.523 7.934   -3.487  1.00 33.79  ? 54  LYS   B C   1 
ATOM   738  O  O   . LYS   B 2 45  ? -17.434 8.358   -2.338  1.00 33.35  ? 54  LYS   B O   1 
ATOM   739  C  CB  . LYS   B 2 45  ? -15.468 9.321   -4.026  1.00 35.38  ? 54  LYS   B CB  1 
ATOM   740  C  CG  . LYS   B 2 45  ? -14.399 9.723   -5.022  1.00 40.46  ? 54  LYS   B CG  1 
ATOM   741  C  CD  . LYS   B 2 45  ? -13.243 8.743   -5.067  1.00 46.01  ? 54  LYS   B CD  1 
ATOM   742  C  CE  . LYS   B 2 45  ? -12.176 9.251   -6.015  1.00 51.14  ? 54  LYS   B CE  1 
ATOM   743  N  NZ  . LYS   B 2 45  ? -11.556 8.169   -6.839  1.00 54.25  ? 54  LYS   B NZ  1 
ATOM   744  N  N   . GLY   B 2 46  ? -18.596 7.291   -3.964  1.00 34.36  ? 55  GLY   B N   1 
ATOM   745  C  CA  . GLY   B 2 46  ? -19.804 7.013   -3.196  1.00 34.96  ? 55  GLY   B CA  1 
ATOM   746  C  C   . GLY   B 2 46  ? -20.768 8.182   -3.081  1.00 36.01  ? 55  GLY   B C   1 
ATOM   747  O  O   . GLY   B 2 46  ? -21.782 8.076   -2.394  1.00 36.18  ? 55  GLY   B O   1 
ATOM   748  N  N   . ALA   B 2 47  ? -20.476 9.310   -3.747  1.00 36.65  ? 56  ALA   B N   1 
ATOM   749  C  CA  . ALA   B 2 47  ? -21.315 10.506  -3.654  1.00 37.36  ? 56  ALA   B CA  1 
ATOM   750  C  C   . ALA   B 2 47  ? -22.629 10.391  -4.404  1.00 37.89  ? 56  ALA   B C   1 
ATOM   751  O  O   . ALA   B 2 47  ? -22.709 9.688   -5.413  1.00 37.80  ? 56  ALA   B O   1 
ATOM   752  C  CB  . ALA   B 2 47  ? -20.551 11.722  -4.154  1.00 37.36  ? 56  ALA   B CB  1 
ATOM   753  N  N   . ALA   B 2 48  ? -23.649 11.117  -3.915  1.00 38.17  ? 57  ALA   B N   1 
ATOM   754  C  CA  . ALA   B 2 48  ? -24.981 11.194  -4.508  1.00 38.87  ? 57  ALA   B CA  1 
ATOM   755  C  C   . ALA   B 2 48  ? -24.910 11.823  -5.896  1.00 39.78  ? 57  ALA   B C   1 
ATOM   756  O  O   . ALA   B 2 48  ? -24.038 12.650  -6.167  1.00 40.02  ? 57  ALA   B O   1 
ATOM   757  C  CB  . ALA   B 2 48  ? -25.903 12.008  -3.617  1.00 38.86  ? 57  ALA   B CB  1 
ATOM   758  N  N   . LEU   B 2 49  ? -25.807 11.398  -6.782  1.00 40.15  ? 58  LEU   B N   1 
ATOM   759  C  CA  . LEU   B 2 49  ? -25.848 11.873  -8.159  1.00 41.52  ? 58  LEU   B CA  1 
ATOM   760  C  C   . LEU   B 2 49  ? -27.162 12.617  -8.448  1.00 43.68  ? 58  LEU   B C   1 
ATOM   761  O  O   . LEU   B 2 49  ? -28.126 12.502  -7.693  1.00 44.28  ? 58  LEU   B O   1 
ATOM   762  C  CB  . LEU   B 2 49  ? -25.693 10.684  -9.122  1.00 41.03  ? 58  LEU   B CB  1 
ATOM   763  C  CG  . LEU   B 2 49  ? -24.465 9.806   -8.939  1.00 41.60  ? 58  LEU   B CG  1 
ATOM   764  C  CD1 . LEU   B 2 49  ? -24.613 8.543   -9.706  1.00 41.87  ? 58  LEU   B CD1 1 
ATOM   765  C  CD2 . LEU   B 2 49  ? -23.223 10.498  -9.423  1.00 42.21  ? 58  LEU   B CD2 1 
ATOM   766  N  N   . ARG   B 2 50  ? -27.192 13.394  -9.521  1.00 44.75  ? 59  ARG   B N   1 
ATOM   767  C  CA  . ARG   B 2 50  ? -28.384 14.128  -9.915  1.00 46.42  ? 59  ARG   B CA  1 
ATOM   768  C  C   . ARG   B 2 50  ? -28.822 13.644  -11.307 1.00 47.45  ? 59  ARG   B C   1 
ATOM   769  O  O   . ARG   B 2 50  ? -27.986 13.469  -12.171 1.00 46.93  ? 59  ARG   B O   1 
ATOM   770  C  CB  . ARG   B 2 50  ? -28.077 15.632  -9.887  1.00 48.64  ? 59  ARG   B CB  1 
ATOM   771  C  CG  . ARG   B 2 50  ? -29.074 16.510  -10.628 1.00 54.06  ? 59  ARG   B CG  1 
ATOM   772  C  CD  . ARG   B 2 50  ? -28.916 17.992  -10.304 1.00 58.85  ? 59  ARG   B CD  1 
ATOM   773  N  NE  . ARG   B 2 50  ? -27.554 18.491  -10.520 1.00 62.83  ? 59  ARG   B NE  1 
ATOM   774  C  CZ  . ARG   B 2 50  ? -27.079 18.908  -11.689 1.00 65.93  ? 59  ARG   B CZ  1 
ATOM   775  N  NH1 . ARG   B 2 50  ? -27.846 18.875  -12.775 1.00 65.75  ? 59  ARG   B NH1 1 
ATOM   776  N  NH2 . ARG   B 2 50  ? -25.834 19.360  -11.783 1.00 66.34  ? 59  ARG   B NH2 1 
ATOM   777  N  N   . SER   B 2 51  ? -30.111 13.381  -11.511 1.00 48.91  ? 60  SER   B N   1 
ATOM   778  C  CA  . SER   B 2 51  ? -30.622 12.922  -12.807 1.00 50.83  ? 60  SER   B CA  1 
ATOM   779  C  C   . SER   B 2 51  ? -31.738 13.884  -13.224 1.00 52.97  ? 60  SER   B C   1 
ATOM   780  O  O   . SER   B 2 51  ? -32.916 13.608  -12.987 1.00 53.65  ? 60  SER   B O   1 
ATOM   781  C  CB  . SER   B 2 51  ? -31.170 11.505  -12.680 1.00 52.12  ? 60  SER   B CB  1 
ATOM   782  O  OG  . SER   B 2 51  ? -31.576 10.985  -13.933 1.00 54.65  ? 60  SER   B OG  1 
ATOM   783  N  N   . GLY   B 2 52  ? -31.362 15.027  -13.784 1.00 53.66  ? 61  GLY   B N   1 
ATOM   784  C  CA  . GLY   B 2 52  ? -32.332 16.057  -14.125 1.00 54.93  ? 61  GLY   B CA  1 
ATOM   785  C  C   . GLY   B 2 52  ? -32.732 16.756  -12.846 1.00 56.14  ? 61  GLY   B C   1 
ATOM   786  O  O   . GLY   B 2 52  ? -31.908 17.446  -12.239 1.00 56.86  ? 61  GLY   B O   1 
ATOM   787  N  N   . GLU   B 2 53  ? -33.969 16.531  -12.377 1.00 56.08  ? 62  GLU   B N   1 
ATOM   788  C  CA  . GLU   B 2 53  ? -34.398 17.079  -11.087 1.00 56.20  ? 62  GLU   B CA  1 
ATOM   789  C  C   . GLU   B 2 53  ? -34.300 16.037  -9.940  1.00 55.22  ? 62  GLU   B C   1 
ATOM   790  O  O   . GLU   B 2 53  ? -34.238 16.410  -8.762  1.00 55.51  ? 62  GLU   B O   1 
ATOM   791  C  CB  . GLU   B 2 53  ? -35.811 17.667  -11.161 1.00 59.75  ? 62  GLU   B CB  1 
ATOM   792  C  CG  . GLU   B 2 53  ? -36.035 18.771  -10.140 1.00 66.43  ? 62  GLU   B CG  1 
ATOM   793  C  CD  . GLU   B 2 53  ? -37.471 19.227  -9.963  1.00 75.72  ? 62  GLU   B CD  1 
ATOM   794  O  OE1 . GLU   B 2 53  ? -38.255 19.124  -10.935 1.00 78.09  ? 62  GLU   B OE1 1 
ATOM   795  O  OE2 . GLU   B 2 53  ? -37.811 19.693  -8.850  1.00 78.40  ? 62  GLU   B OE2 1 
ATOM   796  N  N   . GLY   B 2 54  ? -34.286 14.750  -10.291 1.00 53.84  ? 63  GLY   B N   1 
ATOM   797  C  CA  . GLY   B 2 54  ? -34.202 13.668  -9.319  1.00 52.87  ? 63  GLY   B CA  1 
ATOM   798  C  C   . GLY   B 2 54  ? -32.856 13.522  -8.633  1.00 51.03  ? 63  GLY   B C   1 
ATOM   799  O  O   . GLY   B 2 54  ? -31.884 14.192  -8.995  1.00 51.46  ? 63  GLY   B O   1 
ATOM   800  N  N   . ARG   B 2 55  ? -32.790 12.643  -7.628  1.00 48.66  ? 64  ARG   B N   1 
ATOM   801  C  CA  . ARG   B 2 55  ? -31.550 12.408  -6.899  1.00 46.66  ? 64  ARG   B CA  1 
ATOM   802  C  C   . ARG   B 2 55  ? -31.275 10.918  -6.752  1.00 43.63  ? 64  ARG   B C   1 
ATOM   803  O  O   . ARG   B 2 55  ? -32.138 10.178  -6.306  1.00 43.51  ? 64  ARG   B O   1 
ATOM   804  C  CB  . ARG   B 2 55  ? -31.609 13.075  -5.521  1.00 48.17  ? 64  ARG   B CB  1 
ATOM   805  C  CG  . ARG   B 2 55  ? -30.339 12.914  -4.707  1.00 51.86  ? 64  ARG   B CG  1 
ATOM   806  C  CD  . ARG   B 2 55  ? -30.509 13.496  -3.308  1.00 55.60  ? 64  ARG   B CD  1 
ATOM   807  N  NE  . ARG   B 2 55  ? -29.344 13.226  -2.466  1.00 58.53  ? 64  ARG   B NE  1 
ATOM   808  C  CZ  . ARG   B 2 55  ? -28.802 14.100  -1.624  1.00 60.49  ? 64  ARG   B CZ  1 
ATOM   809  N  NH1 . ARG   B 2 55  ? -29.313 15.321  -1.501  1.00 60.33  ? 64  ARG   B NH1 1 
ATOM   810  N  NH2 . ARG   B 2 55  ? -27.739 13.764  -0.902  1.00 59.64  ? 64  ARG   B NH2 1 
ATOM   811  N  N   . LEU   B 2 56  ? -30.083 10.479  -7.134  1.00 41.28  ? 65  LEU   B N   1 
ATOM   812  C  CA  . LEU   B 2 56  ? -29.689 9.088   -6.985  1.00 39.64  ? 65  LEU   B CA  1 
ATOM   813  C  C   . LEU   B 2 56  ? -28.812 8.962   -5.732  1.00 37.69  ? 65  LEU   B C   1 
ATOM   814  O  O   . LEU   B 2 56  ? -27.717 9.535   -5.678  1.00 37.45  ? 65  LEU   B O   1 
ATOM   815  C  CB  . LEU   B 2 56  ? -28.909 8.571   -8.214  1.00 39.69  ? 65  LEU   B CB  1 
ATOM   816  C  CG  . LEU   B 2 56  ? -29.509 8.720   -9.624  1.00 41.33  ? 65  LEU   B CG  1 
ATOM   817  C  CD1 . LEU   B 2 56  ? -28.843 7.770   -10.566 1.00 41.54  ? 65  LEU   B CD1 1 
ATOM   818  C  CD2 . LEU   B 2 56  ? -30.993 8.407   -9.663  1.00 42.32  ? 65  LEU   B CD2 1 
ATOM   819  N  N   . ASP   B 2 57  ? -29.287 8.229   -4.726  1.00 36.09  ? 66  ASP   B N   1 
ATOM   820  C  CA  . ASP   B 2 57  ? -28.503 8.017   -3.509  1.00 35.39  ? 66  ASP   B CA  1 
ATOM   821  C  C   . ASP   B 2 57  ? -27.851 6.633   -3.564  1.00 33.04  ? 66  ASP   B C   1 
ATOM   822  O  O   . ASP   B 2 57  ? -28.463 5.696   -4.064  1.00 32.98  ? 66  ASP   B O   1 
ATOM   823  C  CB  . ASP   B 2 57  ? -29.383 8.191   -2.266  1.00 39.23  ? 66  ASP   B CB  1 
ATOM   824  C  CG  . ASP   B 2 57  ? -29.840 9.626   -2.090  1.00 47.33  ? 66  ASP   B CG  1 
ATOM   825  O  OD1 . ASP   B 2 57  ? -28.970 10.510  -1.967  1.00 49.46  ? 66  ASP   B OD1 1 
ATOM   826  O  OD2 . ASP   B 2 57  ? -31.071 9.866   -2.089  1.00 50.24  ? 66  ASP   B OD2 1 
ATOM   827  N  N   . PRO   B 2 58  ? -26.596 6.482   -3.118  1.00 31.32  ? 67  PRO   B N   1 
ATOM   828  C  CA  . PRO   B 2 58  ? -25.968 5.149   -3.140  1.00 29.95  ? 67  PRO   B CA  1 
ATOM   829  C  C   . PRO   B 2 58  ? -26.732 4.114   -2.290  1.00 29.31  ? 67  PRO   B C   1 
ATOM   830  O  O   . PRO   B 2 58  ? -27.444 4.474   -1.352  1.00 29.89  ? 67  PRO   B O   1 
ATOM   831  C  CB  . PRO   B 2 58  ? -24.566 5.415   -2.593  1.00 30.52  ? 67  PRO   B CB  1 
ATOM   832  C  CG  . PRO   B 2 58  ? -24.719 6.614   -1.733  1.00 31.56  ? 67  PRO   B CG  1 
ATOM   833  C  CD  . PRO   B 2 58  ? -25.743 7.475   -2.434  1.00 30.67  ? 67  PRO   B CD  1 
ATOM   834  N  N   . TYR   B 2 59  ? -26.619 2.836   -2.639  1.00 27.54  ? 68  TYR   B N   1 
ATOM   835  C  CA  . TYR   B 2 59  ? -27.296 1.756   -1.927  1.00 26.02  ? 68  TYR   B CA  1 
ATOM   836  C  C   . TYR   B 2 59  ? -26.282 0.687   -1.513  1.00 25.25  ? 68  TYR   B C   1 
ATOM   837  O  O   . TYR   B 2 59  ? -26.426 0.097   -0.459  1.00 25.40  ? 68  TYR   B O   1 
ATOM   838  C  CB  . TYR   B 2 59  ? -28.388 1.146   -2.833  1.00 25.31  ? 68  TYR   B CB  1 
ATOM   839  C  CG  . TYR   B 2 59  ? -29.198 0.019   -2.222  1.00 24.42  ? 68  TYR   B CG  1 
ATOM   840  C  CD1 . TYR   B 2 59  ? -28.698 -1.278  -2.178  1.00 24.98  ? 68  TYR   B CD1 1 
ATOM   841  C  CD2 . TYR   B 2 59  ? -30.515 0.219   -1.825  1.00 23.77  ? 68  TYR   B CD2 1 
ATOM   842  C  CE1 . TYR   B 2 59  ? -29.438 -2.321  -1.638  1.00 25.30  ? 68  TYR   B CE1 1 
ATOM   843  C  CE2 . TYR   B 2 59  ? -31.286 -0.829  -1.341  1.00 24.27  ? 68  TYR   B CE2 1 
ATOM   844  C  CZ  . TYR   B 2 59  ? -30.739 -2.099  -1.243  1.00 25.77  ? 68  TYR   B CZ  1 
ATOM   845  O  OH  . TYR   B 2 59  ? -31.461 -3.150  -0.723  1.00 27.71  ? 68  TYR   B OH  1 
ATOM   846  N  N   . TRP   B 2 60  ? -25.292 0.400   -2.369  1.00 24.82  ? 69  TRP   B N   1 
ATOM   847  C  CA  . TRP   B 2 60  ? -24.267 -0.606  -2.121  1.00 24.09  ? 69  TRP   B CA  1 
ATOM   848  C  C   . TRP   B 2 60  ? -22.940 -0.139  -2.734  1.00 24.84  ? 69  TRP   B C   1 
ATOM   849  O  O   . TRP   B 2 60  ? -22.932 0.444   -3.815  1.00 23.88  ? 69  TRP   B O   1 
ATOM   850  C  CB  . TRP   B 2 60  ? -24.685 -1.945  -2.747  1.00 23.15  ? 69  TRP   B CB  1 
ATOM   851  C  CG  . TRP   B 2 60  ? -23.602 -2.972  -2.674  1.00 22.99  ? 69  TRP   B CG  1 
ATOM   852  C  CD1 . TRP   B 2 60  ? -23.232 -3.691  -1.575  1.00 24.04  ? 69  TRP   B CD1 1 
ATOM   853  C  CD2 . TRP   B 2 60  ? -22.637 -3.266  -3.692  1.00 22.86  ? 69  TRP   B CD2 1 
ATOM   854  N  NE1 . TRP   B 2 60  ? -22.120 -4.450  -1.860  1.00 24.35  ? 69  TRP   B NE1 1 
ATOM   855  C  CE2 . TRP   B 2 60  ? -21.737 -4.211  -3.157  1.00 23.61  ? 69  TRP   B CE2 1 
ATOM   856  C  CE3 . TRP   B 2 60  ? -22.453 -2.827  -5.024  1.00 23.01  ? 69  TRP   B CE3 1 
ATOM   857  C  CZ2 . TRP   B 2 60  ? -20.675 -4.732  -3.899  1.00 23.98  ? 69  TRP   B CZ2 1 
ATOM   858  C  CZ3 . TRP   B 2 60  ? -21.384 -3.318  -5.742  1.00 23.33  ? 69  TRP   B CZ3 1 
ATOM   859  C  CH2 . TRP   B 2 60  ? -20.526 -4.282  -5.196  1.00 23.88  ? 69  TRP   B CH2 1 
ATOM   860  N  N   . GLY   B 2 61  ? -21.831 -0.433  -2.066  1.00 25.76  ? 70  GLY   B N   1 
ATOM   861  C  CA  . GLY   B 2 61  ? -20.523 -0.069  -2.593  1.00 26.80  ? 70  GLY   B CA  1 
ATOM   862  C  C   . GLY   B 2 61  ? -19.407 -0.851  -1.960  1.00 27.45  ? 70  GLY   B C   1 
ATOM   863  O  O   . GLY   B 2 61  ? -19.545 -1.339  -0.832  1.00 27.19  ? 70  GLY   B O   1 
ATOM   864  N  N   . ASP   B 2 62  ? -18.281 -0.943  -2.669  1.00 27.72  ? 71  ASP   B N   1 
ATOM   865  C  CA  . ASP   B 2 62  ? -17.131 -1.689  -2.162  1.00 28.55  ? 71  ASP   B CA  1 
ATOM   866  C  C   . ASP   B 2 62  ? -15.862 -1.232  -2.906  1.00 28.71  ? 71  ASP   B C   1 
ATOM   867  O  O   . ASP   B 2 62  ? -15.748 -1.451  -4.097  1.00 29.14  ? 71  ASP   B O   1 
ATOM   868  C  CB  . ASP   B 2 62  ? -17.385 -3.192  -2.361  1.00 30.98  ? 71  ASP   B CB  1 
ATOM   869  C  CG  . ASP   B 2 62  ? -16.398 -4.088  -1.671  1.00 39.29  ? 71  ASP   B CG  1 
ATOM   870  O  OD1 . ASP   B 2 62  ? -15.223 -4.077  -2.054  1.00 41.09  ? 71  ASP   B OD1 1 
ATOM   871  O  OD2 . ASP   B 2 62  ? -16.810 -4.834  -0.770  1.00 43.76  ? 71  ASP   B OD2 1 
ATOM   872  N  N   . VAL   B 2 63  ? -14.919 -0.617  -2.205  1.00 28.39  ? 72  VAL   B N   1 
ATOM   873  C  CA  . VAL   B 2 63  ? -13.663 -0.108  -2.759  1.00 28.24  ? 72  VAL   B CA  1 
ATOM   874  C  C   . VAL   B 2 63  ? -12.768 -1.236  -3.311  1.00 28.44  ? 72  VAL   B C   1 
ATOM   875  O  O   . VAL   B 2 63  ? -12.103 -1.030  -4.316  1.00 29.15  ? 72  VAL   B O   1 
ATOM   876  C  CB  . VAL   B 2 63  ? -12.960 0.744   -1.656  1.00 29.04  ? 72  VAL   B CB  1 
ATOM   877  C  CG1 . VAL   B 2 63  ? -11.471 0.923   -1.900  1.00 29.37  ? 72  VAL   B CG1 1 
ATOM   878  C  CG2 . VAL   B 2 63  ? -13.648 2.089   -1.478  1.00 29.63  ? 72  VAL   B CG2 1 
ATOM   879  N  N   . LYS   B 2 64  ? -12.764 -2.423  -2.696  1.00 28.33  ? 73  LYS   B N   1 
ATOM   880  C  CA  . LYS   B 2 64  ? -11.940 -3.547  -3.172  1.00 28.57  ? 73  LYS   B CA  1 
ATOM   881  C  C   . LYS   B 2 64  ? -12.418 -3.987  -4.576  1.00 28.64  ? 73  LYS   B C   1 
ATOM   882  O  O   . LYS   B 2 64  ? -11.626 -4.066  -5.529  1.00 28.71  ? 73  LYS   B O   1 
ATOM   883  C  CB  . LYS   B 2 64  ? -12.010 -4.707  -2.163  1.00 30.32  ? 73  LYS   B CB  1 
ATOM   884  C  CG  . LYS   B 2 64  ? -11.239 -5.948  -2.557  1.00 34.04  ? 73  LYS   B CG  1 
ATOM   885  C  CD  . LYS   B 2 64  ? -9.808  -5.902  -2.085  1.00 37.41  ? 73  LYS   B CD  1 
ATOM   886  C  CE  . LYS   B 2 64  ? -9.166  -7.244  -2.236  1.00 40.74  ? 73  LYS   B CE  1 
ATOM   887  N  NZ  . LYS   B 2 64  ? -9.787  -8.218  -1.317  1.00 44.09  ? 73  LYS   B NZ  1 
ATOM   888  N  N   . GLN   B 2 65  ? -13.739 -4.192  -4.721  1.00 27.58  ? 74  GLN   B N   1 
ATOM   889  C  CA  . GLN   B 2 65  ? -14.306 -4.535  -6.017  1.00 25.88  ? 74  GLN   B CA  1 
ATOM   890  C  C   . GLN   B 2 65  ? -14.350 -3.342  -6.984  1.00 24.50  ? 74  GLN   B C   1 
ATOM   891  O  O   . GLN   B 2 65  ? -14.503 -3.543  -8.201  1.00 24.43  ? 74  GLN   B O   1 
ATOM   892  C  CB  . GLN   B 2 65  ? -15.707 -5.105  -5.839  1.00 27.67  ? 74  GLN   B CB  1 
ATOM   893  C  CG  . GLN   B 2 65  ? -15.784 -6.294  -4.872  1.00 31.96  ? 74  GLN   B CG  1 
ATOM   894  C  CD  . GLN   B 2 65  ? -17.206 -6.834  -4.789  1.00 37.92  ? 74  GLN   B CD  1 
ATOM   895  O  OE1 . GLN   B 2 65  ? -17.888 -7.049  -5.803  1.00 39.64  ? 74  GLN   B OE1 1 
ATOM   896  N  NE2 . GLN   B 2 65  ? -17.695 -7.065  -3.578  1.00 39.49  ? 74  GLN   B NE2 1 
ATOM   897  N  N   . ASP   B 2 66  ? -14.223 -2.116  -6.453  1.00 23.12  ? 75  ASP   B N   1 
ATOM   898  C  CA  . ASP   B 2 66  ? -14.289 -0.852  -7.171  1.00 22.84  ? 75  ASP   B CA  1 
ATOM   899  C  C   . ASP   B 2 66  ? -15.654 -0.708  -7.843  1.00 22.11  ? 75  ASP   B C   1 
ATOM   900  O  O   . ASP   B 2 66  ? -15.725 -0.199  -8.957  1.00 21.46  ? 75  ASP   B O   1 
ATOM   901  C  CB  . ASP   B 2 66  ? -13.124 -0.663  -8.182  1.00 23.64  ? 75  ASP   B CB  1 
ATOM   902  C  CG  . ASP   B 2 66  ? -12.996 0.763   -8.695  1.00 27.87  ? 75  ASP   B CG  1 
ATOM   903  O  OD1 . ASP   B 2 66  ? -13.499 1.693   -8.011  1.00 27.59  ? 75  ASP   B OD1 1 
ATOM   904  O  OD2 . ASP   B 2 66  ? -12.420 0.953   -9.796  1.00 30.49  ? 75  ASP   B OD2 1 
ATOM   905  N  N   . LEU   B 2 67  ? -16.753 -1.027  -7.126  1.00 21.45  ? 76  LEU   B N   1 
ATOM   906  C  CA  . LEU   B 2 67  ? -18.098 -0.905  -7.716  1.00 20.97  ? 76  LEU   B CA  1 
ATOM   907  C  C   . LEU   B 2 67  ? -19.071 -0.204  -6.795  1.00 21.06  ? 76  LEU   B C   1 
ATOM   908  O  O   . LEU   B 2 67  ? -18.860 -0.230  -5.598  1.00 20.93  ? 76  LEU   B O   1 
ATOM   909  C  CB  . LEU   B 2 67  ? -18.651 -2.287  -8.055  1.00 20.66  ? 76  LEU   B CB  1 
ATOM   910  C  CG  . LEU   B 2 67  ? -17.935 -3.038  -9.153  1.00 21.02  ? 76  LEU   B CG  1 
ATOM   911  C  CD1 . LEU   B 2 67  ? -18.444 -4.434  -9.228  1.00 21.19  ? 76  LEU   B CD1 1 
ATOM   912  C  CD2 . LEU   B 2 67  ? -18.056 -2.309  -10.521 1.00 21.52  ? 76  LEU   B CD2 1 
ATOM   913  N  N   . VAL   B 2 68  ? -20.160 0.382   -7.334  1.00 21.31  ? 77  VAL   B N   1 
ATOM   914  C  CA  . VAL   B 2 68  ? -21.178 1.101   -6.537  1.00 22.14  ? 77  VAL   B CA  1 
ATOM   915  C  C   . VAL   B 2 68  ? -22.542 1.156   -7.267  1.00 23.23  ? 77  VAL   B C   1 
ATOM   916  O  O   . VAL   B 2 68  ? -22.587 1.429   -8.468  1.00 24.95  ? 77  VAL   B O   1 
ATOM   917  C  CB  . VAL   B 2 68  ? -20.679 2.518   -6.126  1.00 22.64  ? 77  VAL   B CB  1 
ATOM   918  C  CG1 . VAL   B 2 68  ? -20.311 3.352   -7.346  1.00 23.51  ? 77  VAL   B CG1 1 
ATOM   919  C  CG2 . VAL   B 2 68  ? -21.677 3.250   -5.245  1.00 22.73  ? 77  VAL   B CG2 1 
ATOM   920  N  N   . SER   B 2 69  ? -23.643 0.862   -6.564  1.00 22.49  ? 78  SER   B N   1 
ATOM   921  C  CA  . SER   B 2 69  ? -24.976 0.903   -7.161  1.00 22.23  ? 78  SER   B CA  1 
ATOM   922  C  C   . SER   B 2 69  ? -25.848 1.943   -6.455  1.00 21.69  ? 78  SER   B C   1 
ATOM   923  O  O   . SER   B 2 69  ? -25.701 2.172   -5.257  1.00 20.86  ? 78  SER   B O   1 
ATOM   924  C  CB  . SER   B 2 69  ? -25.633 -0.473  -7.149  1.00 23.64  ? 78  SER   B CB  1 
ATOM   925  O  OG  . SER   B 2 69  ? -26.043 -0.823  -5.836  1.00 26.64  ? 78  SER   B OG  1 
ATOM   926  N  N   . TYR   B 2 70  ? -26.732 2.601   -7.211  1.00 21.82  ? 79  TYR   B N   1 
ATOM   927  C  CA  . TYR   B 2 70  ? -27.605 3.675   -6.714  1.00 22.20  ? 79  TYR   B CA  1 
ATOM   928  C  C   . TYR   B 2 70  ? -29.064 3.272   -6.866  1.00 22.75  ? 79  TYR   B C   1 
ATOM   929  O  O   . TYR   B 2 70  ? -29.416 2.734   -7.904  1.00 22.37  ? 79  TYR   B O   1 
ATOM   930  C  CB  . TYR   B 2 70  ? -27.359 4.968   -7.525  1.00 21.81  ? 79  TYR   B CB  1 
ATOM   931  C  CG  . TYR   B 2 70  ? -25.990 5.566   -7.299  1.00 22.22  ? 79  TYR   B CG  1 
ATOM   932  C  CD1 . TYR   B 2 70  ? -24.861 5.015   -7.891  1.00 22.55  ? 79  TYR   B CD1 1 
ATOM   933  C  CD2 . TYR   B 2 70  ? -25.819 6.656   -6.461  1.00 23.50  ? 79  TYR   B CD2 1 
ATOM   934  C  CE1 . TYR   B 2 70  ? -23.596 5.527   -7.642  1.00 23.67  ? 79  TYR   B CE1 1 
ATOM   935  C  CE2 . TYR   B 2 70  ? -24.556 7.160   -6.182  1.00 24.54  ? 79  TYR   B CE2 1 
ATOM   936  C  CZ  . TYR   B 2 70  ? -23.446 6.599   -6.783  1.00 25.72  ? 79  TYR   B CZ  1 
ATOM   937  O  OH  . TYR   B 2 70  ? -22.199 7.118   -6.521  1.00 28.40  ? 79  TYR   B OH  1 
ATOM   938  N  N   . CYS   B 2 71  ? -29.922 3.547   -5.857  1.00 23.15  ? 80  CYS   B N   1 
ATOM   939  C  CA  . CYS   B 2 71  ? -31.368 3.262   -5.922  1.00 24.83  ? 80  CYS   B CA  1 
ATOM   940  C  C   . CYS   B 2 71  ? -31.727 1.836   -5.581  1.00 24.46  ? 80  CYS   B C   1 
ATOM   941  O  O   . CYS   B 2 71  ? -32.871 1.590   -5.206  1.00 25.20  ? 80  CYS   B O   1 
ATOM   942  C  CB  . CYS   B 2 71  ? -31.993 3.672   -7.255  1.00 28.53  ? 80  CYS   B CB  1 
ATOM   943  S  SG  . CYS   B 2 71  ? -31.770 5.419   -7.690  1.00 39.01  ? 80  CYS   B SG  1 
ATOM   944  N  N   . GLY   B 2 72  ? -30.784 0.907   -5.703  1.00 23.24  ? 81  GLY   B N   1 
ATOM   945  C  CA  . GLY   B 2 72  ? -31.050 -0.475  -5.342  1.00 22.63  ? 81  GLY   B CA  1 
ATOM   946  C  C   . GLY   B 2 72  ? -29.822 -1.335  -5.403  1.00 22.65  ? 81  GLY   B C   1 
ATOM   947  O  O   . GLY   B 2 72  ? -28.722 -0.865  -5.695  1.00 22.21  ? 81  GLY   B O   1 
ATOM   948  N  N   . PRO   B 2 73  ? -29.988 -2.619  -5.093  1.00 23.22  ? 82  PRO   B N   1 
ATOM   949  C  CA  . PRO   B 2 73  ? -28.840 -3.536  -5.159  1.00 23.57  ? 82  PRO   B CA  1 
ATOM   950  C  C   . PRO   B 2 73  ? -28.339 -3.762  -6.585  1.00 24.50  ? 82  PRO   B C   1 
ATOM   951  O  O   . PRO   B 2 73  ? -29.090 -3.543  -7.546  1.00 24.99  ? 82  PRO   B O   1 
ATOM   952  C  CB  . PRO   B 2 73  ? -29.411 -4.838  -4.593  1.00 24.27  ? 82  PRO   B CB  1 
ATOM   953  C  CG  . PRO   B 2 73  ? -30.880 -4.750  -4.872  1.00 24.59  ? 82  PRO   B CG  1 
ATOM   954  C  CD  . PRO   B 2 73  ? -31.228 -3.309  -4.682  1.00 22.68  ? 82  PRO   B CD  1 
ATOM   955  N  N   . TRP   B 2 74  ? -27.089 -4.276  -6.728  1.00 24.24  ? 83  TRP   B N   1 
ATOM   956  C  CA  . TRP   B 2 74  ? -26.476 -4.620  -8.007  1.00 24.65  ? 83  TRP   B CA  1 
ATOM   957  C  C   . TRP   B 2 74  ? -27.379 -5.600  -8.758  1.00 26.28  ? 83  TRP   B C   1 
ATOM   958  O  O   . TRP   B 2 74  ? -27.898 -6.527  -8.147  1.00 26.35  ? 83  TRP   B O   1 
ATOM   959  C  CB  . TRP   B 2 74  ? -25.085 -5.227  -7.781  1.00 24.08  ? 83  TRP   B CB  1 
ATOM   960  C  CG  . TRP   B 2 74  ? -24.268 -5.337  -9.029  1.00 23.47  ? 83  TRP   B CG  1 
ATOM   961  C  CD1 . TRP   B 2 74  ? -24.209 -6.401  -9.876  1.00 23.83  ? 83  TRP   B CD1 1 
ATOM   962  C  CD2 . TRP   B 2 74  ? -23.383 -4.344  -9.569  1.00 23.46  ? 83  TRP   B CD2 1 
ATOM   963  N  NE1 . TRP   B 2 74  ? -23.324 -6.150  -10.892 1.00 24.10  ? 83  TRP   B NE1 1 
ATOM   964  C  CE2 . TRP   B 2 74  ? -22.838 -4.874  -10.757 1.00 24.19  ? 83  TRP   B CE2 1 
ATOM   965  C  CE3 . TRP   B 2 74  ? -23.007 -3.054  -9.171  1.00 23.58  ? 83  TRP   B CE3 1 
ATOM   966  C  CZ2 . TRP   B 2 74  ? -21.944 -4.151  -11.557 1.00 24.96  ? 83  TRP   B CZ2 1 
ATOM   967  C  CZ3 . TRP   B 2 74  ? -22.142 -2.334  -9.972  1.00 24.37  ? 83  TRP   B CZ3 1 
ATOM   968  C  CH2 . TRP   B 2 74  ? -21.622 -2.879  -11.152 1.00 24.91  ? 83  TRP   B CH2 1 
ATOM   969  N  N   . LYS   B 2 75  ? -27.636 -5.331  -10.059 1.00 27.59  ? 84  LYS   B N   1 
ATOM   970  C  CA  . LYS   B 2 75  ? -28.545 -6.096  -10.915 1.00 28.55  ? 84  LYS   B CA  1 
ATOM   971  C  C   . LYS   B 2 75  ? -27.844 -6.903  -12.005 1.00 30.26  ? 84  LYS   B C   1 
ATOM   972  O  O   . LYS   B 2 75  ? -28.419 -7.849  -12.528 1.00 30.51  ? 84  LYS   B O   1 
ATOM   973  C  CB  . LYS   B 2 75  ? -29.521 -5.133  -11.611 1.00 28.79  ? 84  LYS   B CB  1 
ATOM   974  C  CG  . LYS   B 2 75  ? -30.396 -4.344  -10.665 1.00 29.76  ? 84  LYS   B CG  1 
ATOM   975  C  CD  . LYS   B 2 75  ? -31.409 -5.228  -9.999  1.00 31.93  ? 84  LYS   B CD  1 
ATOM   976  C  CE  . LYS   B 2 75  ? -32.416 -4.403  -9.250  1.00 34.77  ? 84  LYS   B CE  1 
ATOM   977  N  NZ  . LYS   B 2 75  ? -33.243 -5.247  -8.359  1.00 37.63  ? 84  LYS   B NZ  1 
ATOM   978  N  N   . LEU   B 2 76  ? -26.656 -6.477  -12.415 1.00 31.38  ? 85  LEU   B N   1 
ATOM   979  C  CA  . LEU   B 2 76  ? -25.930 -7.096  -13.529 1.00 32.30  ? 85  LEU   B CA  1 
ATOM   980  C  C   . LEU   B 2 76  ? -25.260 -8.403  -13.092 1.00 34.35  ? 85  LEU   B C   1 
ATOM   981  O  O   . LEU   B 2 76  ? -24.338 -8.380  -12.279 1.00 34.54  ? 85  LEU   B O   1 
ATOM   982  C  CB  . LEU   B 2 76  ? -24.885 -6.128  -14.091 1.00 31.78  ? 85  LEU   B CB  1 
ATOM   983  C  CG  . LEU   B 2 76  ? -25.261 -4.663  -14.197 1.00 32.92  ? 85  LEU   B CG  1 
ATOM   984  C  CD1 . LEU   B 2 76  ? -24.091 -3.855  -14.661 1.00 33.71  ? 85  LEU   B CD1 1 
ATOM   985  C  CD2 . LEU   B 2 76  ? -26.429 -4.457  -15.142 1.00 33.32  ? 85  LEU   B CD2 1 
ATOM   986  N  N   . ASP   B 2 77  ? -25.719 -9.536  -13.626 1.00 35.65  ? 86  ASP   B N   1 
ATOM   987  C  CA  . ASP   B 2 77  ? -25.195 -10.832 -13.213 1.00 37.74  ? 86  ASP   B CA  1 
ATOM   988  C  C   . ASP   B 2 77  ? -24.639 -11.708 -14.361 1.00 39.18  ? 86  ASP   B C   1 
ATOM   989  O  O   . ASP   B 2 77  ? -24.278 -12.864 -14.108 1.00 39.99  ? 86  ASP   B O   1 
ATOM   990  C  CB  . ASP   B 2 77  ? -26.257 -11.598 -12.402 1.00 39.83  ? 86  ASP   B CB  1 
ATOM   991  C  CG  . ASP   B 2 77  ? -27.524 -11.937 -13.181 1.00 45.41  ? 86  ASP   B CG  1 
ATOM   992  O  OD1 . ASP   B 2 77  ? -27.710 -11.386 -14.292 1.00 45.92  ? 86  ASP   B OD1 1 
ATOM   993  O  OD2 . ASP   B 2 77  ? -28.330 -12.749 -12.678 1.00 48.24  ? 86  ASP   B OD2 1 
ATOM   994  N  N   . ALA   B 2 78  ? -24.547 -11.175 -15.590 1.00 39.18  ? 87  ALA   B N   1 
ATOM   995  C  CA  . ALA   B 2 78  ? -24.002 -11.950 -16.705 1.00 40.03  ? 87  ALA   B CA  1 
ATOM   996  C  C   . ALA   B 2 78  ? -22.483 -12.080 -16.586 1.00 41.10  ? 87  ALA   B C   1 
ATOM   997  O  O   . ALA   B 2 78  ? -21.832 -11.248 -15.940 1.00 41.31  ? 87  ALA   B O   1 
ATOM   998  C  CB  . ALA   B 2 78  ? -24.384 -11.329 -18.039 1.00 39.88  ? 87  ALA   B CB  1 
ATOM   999  N  N   . ALA   B 2 79  ? -21.921 -13.141 -17.178 1.00 41.40  ? 88  ALA   B N   1 
ATOM   1000 C  CA  . ALA   B 2 79  ? -20.487 -13.396 -17.090 1.00 41.98  ? 88  ALA   B CA  1 
ATOM   1001 C  C   . ALA   B 2 79  ? -19.878 -13.767 -18.429 1.00 42.93  ? 88  ALA   B C   1 
ATOM   1002 O  O   . ALA   B 2 79  ? -20.547 -14.378 -19.263 1.00 42.60  ? 88  ALA   B O   1 
ATOM   1003 C  CB  . ALA   B 2 79  ? -20.236 -14.515 -16.110 1.00 41.91  ? 88  ALA   B CB  1 
ATOM   1004 N  N   . TRP   B 2 80  ? -18.584 -13.429 -18.621 1.00 43.88  ? 89  TRP   B N   1 
ATOM   1005 C  CA  . TRP   B 2 80  ? -17.833 -13.787 -19.825 1.00 45.24  ? 89  TRP   B CA  1 
ATOM   1006 C  C   . TRP   B 2 80  ? -17.708 -15.307 -19.839 1.00 46.19  ? 89  TRP   B C   1 
ATOM   1007 O  O   . TRP   B 2 80  ? -17.441 -15.901 -18.787 1.00 45.83  ? 89  TRP   B O   1 
ATOM   1008 C  CB  . TRP   B 2 80  ? -16.425 -13.144 -19.831 1.00 45.32  ? 89  TRP   B CB  1 
ATOM   1009 C  CG  . TRP   B 2 80  ? -15.621 -13.444 -21.073 1.00 46.11  ? 89  TRP   B CG  1 
ATOM   1010 C  CD1 . TRP   B 2 80  ? -16.051 -13.360 -22.364 1.00 47.13  ? 89  TRP   B CD1 1 
ATOM   1011 C  CD2 . TRP   B 2 80  ? -14.227 -13.789 -21.136 1.00 46.33  ? 89  TRP   B CD2 1 
ATOM   1012 N  NE1 . TRP   B 2 80  ? -15.029 -13.692 -23.225 1.00 47.74  ? 89  TRP   B NE1 1 
ATOM   1013 C  CE2 . TRP   B 2 80  ? -13.896 -13.954 -22.496 1.00 47.29  ? 89  TRP   B CE2 1 
ATOM   1014 C  CE3 . TRP   B 2 80  ? -13.238 -14.031 -20.174 1.00 46.92  ? 89  TRP   B CE3 1 
ATOM   1015 C  CZ2 . TRP   B 2 80  ? -12.618 -14.333 -22.913 1.00 47.53  ? 89  TRP   B CZ2 1 
ATOM   1016 C  CZ3 . TRP   B 2 80  ? -11.976 -14.403 -20.592 1.00 47.41  ? 89  TRP   B CZ3 1 
ATOM   1017 C  CH2 . TRP   B 2 80  ? -11.674 -14.535 -21.946 1.00 47.32  ? 89  TRP   B CH2 1 
ATOM   1018 N  N   . ASP   B 2 81  ? -17.973 -15.943 -20.992 1.00 47.07  ? 90  ASP   B N   1 
ATOM   1019 C  CA  . ASP   B 2 81  ? -17.878 -17.402 -21.060 1.00 48.51  ? 90  ASP   B CA  1 
ATOM   1020 C  C   . ASP   B 2 81  ? -16.432 -17.934 -21.105 1.00 49.74  ? 90  ASP   B C   1 
ATOM   1021 O  O   . ASP   B 2 81  ? -16.237 -19.141 -20.983 1.00 50.28  ? 90  ASP   B O   1 
ATOM   1022 C  CB  . ASP   B 2 81  ? -18.722 -17.995 -22.201 1.00 49.86  ? 90  ASP   B CB  1 
ATOM   1023 C  CG  . ASP   B 2 81  ? -18.412 -17.498 -23.592 1.00 54.28  ? 90  ASP   B CG  1 
ATOM   1024 O  OD1 . ASP   B 2 81  ? -17.428 -16.743 -23.752 1.00 55.20  ? 90  ASP   B OD1 1 
ATOM   1025 O  OD2 . ASP   B 2 81  ? -19.158 -17.854 -24.526 1.00 56.26  ? 90  ASP   B OD2 1 
ATOM   1026 N  N   . GLY   B 2 82  ? -15.450 -17.045 -21.254 1.00 49.98  ? 91  GLY   B N   1 
ATOM   1027 C  CA  . GLY   B 2 82  ? -14.046 -17.423 -21.345 1.00 50.81  ? 91  GLY   B CA  1 
ATOM   1028 C  C   . GLY   B 2 82  ? -13.612 -17.833 -22.742 1.00 51.59  ? 91  GLY   B C   1 
ATOM   1029 O  O   . GLY   B 2 82  ? -12.447 -18.172 -22.953 1.00 52.00  ? 91  GLY   B O   1 
ATOM   1030 N  N   . LEU   B 2 83  ? -14.530 -17.804 -23.717 1.00 51.71  ? 92  LEU   B N   1 
ATOM   1031 C  CA  . LEU   B 2 83  ? -14.229 -18.187 -25.085 1.00 52.21  ? 92  LEU   B CA  1 
ATOM   1032 C  C   . LEU   B 2 83  ? -14.562 -17.114 -26.117 1.00 52.81  ? 92  LEU   B C   1 
ATOM   1033 O  O   . LEU   B 2 83  ? -13.800 -16.917 -27.056 1.00 54.05  ? 92  LEU   B O   1 
ATOM   1034 C  CB  . LEU   B 2 83  ? -15.055 -19.423 -25.462 1.00 52.58  ? 92  LEU   B CB  1 
ATOM   1035 C  CG  . LEU   B 2 83  ? -14.744 -20.760 -24.871 1.00 54.28  ? 92  LEU   B CG  1 
ATOM   1036 C  CD1 . LEU   B 2 83  ? -15.521 -21.829 -25.627 1.00 54.74  ? 92  LEU   B CD1 1 
ATOM   1037 C  CD2 . LEU   B 2 83  ? -13.268 -21.069 -24.969 1.00 55.14  ? 92  LEU   B CD2 1 
ATOM   1038 N  N   . SER   B 2 84  ? -15.750 -16.512 -26.030 1.00 52.18  ? 93  SER   B N   1 
ATOM   1039 C  CA  . SER   B 2 84  ? -16.234 -15.597 -27.057 1.00 51.72  ? 93  SER   B CA  1 
ATOM   1040 C  C   . SER   B 2 84  ? -15.681 -14.186 -27.014 1.00 50.22  ? 93  SER   B C   1 
ATOM   1041 O  O   . SER   B 2 84  ? -15.299 -13.683 -25.949 1.00 49.99  ? 93  SER   B O   1 
ATOM   1042 C  CB  . SER   B 2 84  ? -17.763 -15.527 -27.028 1.00 53.99  ? 93  SER   B CB  1 
ATOM   1043 O  OG  . SER   B 2 84  ? -18.398 -16.768 -26.766 1.00 56.95  ? 93  SER   B OG  1 
ATOM   1044 N  N   . GLU   B 2 85  ? -15.705 -13.525 -28.185 1.00 49.02  ? 94  GLU   B N   1 
ATOM   1045 C  CA  . GLU   B 2 85  ? -15.366 -12.113 -28.303 1.00 48.32  ? 94  GLU   B CA  1 
ATOM   1046 C  C   . GLU   B 2 85  ? -16.490 -11.304 -27.617 1.00 46.62  ? 94  GLU   B C   1 
ATOM   1047 O  O   . GLU   B 2 85  ? -17.635 -11.756 -27.473 1.00 46.93  ? 94  GLU   B O   1 
ATOM   1048 C  CB  . GLU   B 2 85  ? -15.217 -11.671 -29.775 1.00 51.10  ? 94  GLU   B CB  1 
ATOM   1049 C  CG  . GLU   B 2 85  ? -13.973 -12.197 -30.491 1.00 55.18  ? 94  GLU   B CG  1 
ATOM   1050 C  CD  . GLU   B 2 85  ? -13.465 -11.348 -31.645 1.00 58.83  ? 94  GLU   B CD  1 
ATOM   1051 O  OE1 . GLU   B 2 85  ? -14.262 -10.562 -32.208 1.00 57.80  ? 94  GLU   B OE1 1 
ATOM   1052 O  OE2 . GLU   B 2 85  ? -12.261 -11.455 -31.973 1.00 60.82  ? 94  GLU   B OE2 1 
ATOM   1053 N  N   . VAL   B 2 86  ? -16.129 -10.145 -27.119 1.00 44.42  ? 95  VAL   B N   1 
ATOM   1054 C  CA  . VAL   B 2 86  ? -17.056 -9.263  -26.421 1.00 42.07  ? 95  VAL   B CA  1 
ATOM   1055 C  C   . VAL   B 2 86  ? -17.004 -7.872  -27.091 1.00 40.49  ? 95  VAL   B C   1 
ATOM   1056 O  O   . VAL   B 2 86  ? -16.166 -7.627  -27.974 1.00 40.57  ? 95  VAL   B O   1 
ATOM   1057 C  CB  . VAL   B 2 86  ? -16.695 -9.182  -24.905 1.00 41.25  ? 95  VAL   B CB  1 
ATOM   1058 C  CG1 . VAL   B 2 86  ? -16.651 -10.560 -24.254 1.00 41.00  ? 95  VAL   B CG1 1 
ATOM   1059 C  CG2 . VAL   B 2 86  ? -15.388 -8.432  -24.703 1.00 41.37  ? 95  VAL   B CG2 1 
ATOM   1060 N  N   . GLN   B 2 87  ? -17.910 -6.971  -26.693 1.00 38.93  ? 96  GLN   B N   1 
ATOM   1061 C  CA  . GLN   B 2 87  ? -17.889 -5.611  -27.182 1.00 37.66  ? 96  GLN   B CA  1 
ATOM   1062 C  C   . GLN   B 2 87  ? -17.817 -4.635  -25.997 1.00 35.79  ? 96  GLN   B C   1 
ATOM   1063 O  O   . GLN   B 2 87  ? -18.612 -4.739  -25.067 1.00 35.68  ? 96  GLN   B O   1 
ATOM   1064 C  CB  . GLN   B 2 87  ? -19.099 -5.318  -28.092 1.00 38.80  ? 96  GLN   B CB  1 
ATOM   1065 C  CG  . GLN   B 2 87  ? -18.861 -5.732  -29.534 1.00 42.93  ? 96  GLN   B CG  1 
ATOM   1066 C  CD  . GLN   B 2 87  ? -20.033 -5.476  -30.474 1.00 46.64  ? 96  GLN   B CD  1 
ATOM   1067 O  OE1 . GLN   B 2 87  ? -21.008 -4.766  -30.154 1.00 47.91  ? 96  GLN   B OE1 1 
ATOM   1068 N  NE2 . GLN   B 2 87  ? -19.966 -6.068  -31.663 1.00 45.38  ? 96  GLN   B NE2 1 
ATOM   1069 N  N   . LEU   B 2 88  ? -16.854 -3.701  -26.032 1.00 34.24  ? 97  LEU   B N   1 
ATOM   1070 C  CA  . LEU   B 2 88  ? -16.764 -2.593  -25.093 1.00 33.82  ? 97  LEU   B CA  1 
ATOM   1071 C  C   . LEU   B 2 88  ? -17.669 -1.441  -25.633 1.00 33.91  ? 97  LEU   B C   1 
ATOM   1072 O  O   . LEU   B 2 88  ? -17.340 -0.860  -26.690 1.00 34.53  ? 97  LEU   B O   1 
ATOM   1073 C  CB  . LEU   B 2 88  ? -15.313 -2.075  -25.019 1.00 33.52  ? 97  LEU   B CB  1 
ATOM   1074 C  CG  . LEU   B 2 88  ? -15.114 -0.821  -24.149 1.00 34.51  ? 97  LEU   B CG  1 
ATOM   1075 C  CD1 . LEU   B 2 88  ? -15.511 -1.089  -22.720 1.00 35.33  ? 97  LEU   B CD1 1 
ATOM   1076 C  CD2 . LEU   B 2 88  ? -13.684 -0.328  -24.185 1.00 34.65  ? 97  LEU   B CD2 1 
ATOM   1077 N  N   . LEU   B 2 89  ? -18.811 -1.140  -24.971 1.00 32.90  ? 98  LEU   B N   1 
ATOM   1078 C  CA  . LEU   B 2 89  ? -19.610 -0.005  -25.424 1.00 32.30  ? 98  LEU   B CA  1 
ATOM   1079 C  C   . LEU   B 2 89  ? -18.919 1.199   -24.805 1.00 32.77  ? 98  LEU   B C   1 
ATOM   1080 O  O   . LEU   B 2 89  ? -19.216 1.572   -23.667 1.00 32.76  ? 98  LEU   B O   1 
ATOM   1081 C  CB  . LEU   B 2 89  ? -21.094 -0.096  -25.035 1.00 32.11  ? 98  LEU   B CB  1 
ATOM   1082 C  CG  . LEU   B 2 89  ? -22.009 1.122   -25.420 1.00 33.46  ? 98  LEU   B CG  1 
ATOM   1083 C  CD1 . LEU   B 2 89  ? -21.790 1.600   -26.856 1.00 34.19  ? 98  LEU   B CD1 1 
ATOM   1084 C  CD2 . LEU   B 2 89  ? -23.468 0.791   -25.230 1.00 33.65  ? 98  LEU   B CD2 1 
ATOM   1085 N  N   . ALA   B 2 90  ? -17.923 1.750   -25.519 1.00 32.85  ? 99  ALA   B N   1 
ATOM   1086 C  CA  . ALA   B 2 90  ? -17.148 2.882   -25.013 1.00 33.24  ? 99  ALA   B CA  1 
ATOM   1087 C  C   . ALA   B 2 90  ? -17.924 4.178   -25.135 1.00 33.47  ? 99  ALA   B C   1 
ATOM   1088 O  O   . ALA   B 2 90  ? -18.532 4.431   -26.165 1.00 33.72  ? 99  ALA   B O   1 
ATOM   1089 C  CB  . ALA   B 2 90  ? -15.834 3.008   -25.763 1.00 33.21  ? 99  ALA   B CB  1 
ATOM   1090 N  N   . VAL   B 2 91  ? -17.934 4.990   -24.063 1.00 33.03  ? 100 VAL   B N   1 
ATOM   1091 C  CA  . VAL   B 2 91  ? -18.598 6.285   -24.059 1.00 32.58  ? 100 VAL   B CA  1 
ATOM   1092 C  C   . VAL   B 2 91  ? -17.530 7.311   -23.680 1.00 33.28  ? 100 VAL   B C   1 
ATOM   1093 O  O   . VAL   B 2 91  ? -17.359 7.646   -22.501 1.00 33.86  ? 100 VAL   B O   1 
ATOM   1094 C  CB  . VAL   B 2 91  ? -19.784 6.285   -23.089 1.00 32.60  ? 100 VAL   B CB  1 
ATOM   1095 C  CG1 . VAL   B 2 91  ? -20.503 7.636   -23.099 1.00 32.95  ? 100 VAL   B CG1 1 
ATOM   1096 C  CG2 . VAL   B 2 91  ? -20.740 5.140   -23.405 1.00 32.60  ? 100 VAL   B CG2 1 
ATOM   1097 N  N   . PRO   B 2 92  ? -16.739 7.765   -24.666 1.00 33.27  ? 101 PRO   B N   1 
ATOM   1098 C  CA  . PRO   B 2 92  ? -15.625 8.664   -24.344 1.00 34.24  ? 101 PRO   B CA  1 
ATOM   1099 C  C   . PRO   B 2 92  ? -16.001 10.126  -24.088 1.00 36.43  ? 101 PRO   B C   1 
ATOM   1100 O  O   . PRO   B 2 92  ? -17.006 10.641  -24.610 1.00 36.17  ? 101 PRO   B O   1 
ATOM   1101 C  CB  . PRO   B 2 92  ? -14.671 8.505   -25.546 1.00 34.33  ? 101 PRO   B CB  1 
ATOM   1102 C  CG  . PRO   B 2 92  ? -15.399 7.686   -26.563 1.00 34.39  ? 101 PRO   B CG  1 
ATOM   1103 C  CD  . PRO   B 2 92  ? -16.792 7.446   -26.105 1.00 32.74  ? 101 PRO   B CD  1 
ATOM   1104 N  N   . PRO   B 2 93  ? -15.167 10.835  -23.307 1.00 38.16  ? 102 PRO   B N   1 
ATOM   1105 C  CA  . PRO   B 2 93  ? -15.474 12.249  -23.017 1.00 39.84  ? 102 PRO   B CA  1 
ATOM   1106 C  C   . PRO   B 2 93  ? -15.643 13.123  -24.259 1.00 41.63  ? 102 PRO   B C   1 
ATOM   1107 O  O   . PRO   B 2 93  ? -14.719 13.275  -25.063 1.00 41.99  ? 102 PRO   B O   1 
ATOM   1108 C  CB  . PRO   B 2 93  ? -14.292 12.702  -22.148 1.00 40.51  ? 102 PRO   B CB  1 
ATOM   1109 C  CG  . PRO   B 2 93  ? -13.743 11.429  -21.553 1.00 40.31  ? 102 PRO   B CG  1 
ATOM   1110 C  CD  . PRO   B 2 93  ? -13.949 10.380  -22.604 1.00 37.95  ? 102 PRO   B CD  1 
ATOM   1111 N  N   . GLY   B 2 94  ? -16.845 13.664  -24.422 1.00 42.26  ? 103 GLY   B N   1 
ATOM   1112 C  CA  . GLY   B 2 94  ? -17.188 14.540  -25.539 1.00 42.82  ? 103 GLY   B CA  1 
ATOM   1113 C  C   . GLY   B 2 94  ? -17.347 13.850  -26.879 1.00 43.75  ? 103 GLY   B C   1 
ATOM   1114 O  O   . GLY   B 2 94  ? -17.326 14.507  -27.924 1.00 44.46  ? 103 GLY   B O   1 
ATOM   1115 N  N   . GLU   B 2 95  ? -17.484 12.525  -26.881 1.00 43.95  ? 104 GLU   B N   1 
ATOM   1116 C  CA  . GLU   B 2 95  ? -17.612 11.757  -28.119 1.00 44.77  ? 104 GLU   B CA  1 
ATOM   1117 C  C   . GLU   B 2 95  ? -18.779 10.772  -28.018 1.00 45.49  ? 104 GLU   B C   1 
ATOM   1118 O  O   . GLU   B 2 95  ? -19.118 10.332  -26.921 1.00 45.61  ? 104 GLU   B O   1 
ATOM   1119 C  CB  . GLU   B 2 95  ? -16.299 11.023  -28.428 1.00 46.63  ? 104 GLU   B CB  1 
ATOM   1120 C  CG  . GLU   B 2 95  ? -15.104 11.952  -28.567 1.00 50.76  ? 104 GLU   B CG  1 
ATOM   1121 C  CD  . GLU   B 2 95  ? -13.746 11.280  -28.662 1.00 55.90  ? 104 GLU   B CD  1 
ATOM   1122 O  OE1 . GLU   B 2 95  ? -13.658 10.072  -28.352 1.00 57.02  ? 104 GLU   B OE1 1 
ATOM   1123 O  OE2 . GLU   B 2 95  ? -12.766 11.964  -29.041 1.00 57.47  ? 104 GLU   B OE2 1 
ATOM   1124 N  N   . ARG   B 2 96  ? -19.386 10.420  -29.159 1.00 45.53  ? 105 ARG   B N   1 
ATOM   1125 C  CA  . ARG   B 2 96  ? -20.543 9.527   -29.228 1.00 46.57  ? 105 ARG   B CA  1 
ATOM   1126 C  C   . ARG   B 2 96  ? -20.239 8.098   -28.745 1.00 46.76  ? 105 ARG   B C   1 
ATOM   1127 O  O   . ARG   B 2 96  ? -19.105 7.632   -28.904 1.00 47.29  ? 105 ARG   B O   1 
ATOM   1128 C  CB  . ARG   B 2 96  ? -21.058 9.491   -30.681 1.00 49.34  ? 105 ARG   B CB  1 
ATOM   1129 C  CG  . ARG   B 2 96  ? -22.456 8.912   -30.850 1.00 54.84  ? 105 ARG   B CG  1 
ATOM   1130 C  CD  . ARG   B 2 96  ? -23.165 9.461   -32.085 1.00 61.01  ? 105 ARG   B CD  1 
ATOM   1131 N  NE  . ARG   B 2 96  ? -22.595 8.957   -33.332 1.00 66.29  ? 105 ARG   B NE  1 
ATOM   1132 C  CZ  . ARG   B 2 96  ? -21.863 9.688   -34.170 1.00 71.71  ? 105 ARG   B CZ  1 
ATOM   1133 N  NH1 . ARG   B 2 96  ? -21.615 10.967  -33.904 1.00 72.73  ? 105 ARG   B NH1 1 
ATOM   1134 N  NH2 . ARG   B 2 96  ? -21.390 9.152   -35.290 1.00 72.25  ? 105 ARG   B NH2 1 
ATOM   1135 N  N   . ALA   B 2 97  ? -21.259 7.381   -28.187 1.00 45.93  ? 106 ALA   B N   1 
ATOM   1136 C  CA  . ALA   B 2 97  ? -21.129 5.976   -27.777 1.00 45.72  ? 106 ALA   B CA  1 
ATOM   1137 C  C   . ALA   B 2 97  ? -20.681 5.144   -28.991 1.00 46.48  ? 106 ALA   B C   1 
ATOM   1138 O  O   . ALA   B 2 97  ? -21.184 5.359   -30.089 1.00 46.16  ? 106 ALA   B O   1 
ATOM   1139 C  CB  . ALA   B 2 97  ? -22.456 5.455   -27.271 1.00 45.40  ? 106 ALA   B CB  1 
ATOM   1140 N  N   . LYS   B 2 98  ? -19.718 4.239   -28.802 1.00 47.08  ? 107 LYS   B N   1 
ATOM   1141 C  CA  . LYS   B 2 98  ? -19.123 3.485   -29.896 1.00 47.90  ? 107 LYS   B CA  1 
ATOM   1142 C  C   . LYS   B 2 98  ? -18.801 2.036   -29.482 1.00 47.43  ? 107 LYS   B C   1 
ATOM   1143 O  O   . LYS   B 2 98  ? -18.069 1.848   -28.518 1.00 47.84  ? 107 LYS   B O   1 
ATOM   1144 C  CB  . LYS   B 2 98  ? -17.832 4.240   -30.244 1.00 51.92  ? 107 LYS   B CB  1 
ATOM   1145 C  CG  . LYS   B 2 98  ? -16.955 3.648   -31.319 1.00 59.59  ? 107 LYS   B CG  1 
ATOM   1146 C  CD  . LYS   B 2 98  ? -15.645 4.449   -31.448 1.00 66.28  ? 107 LYS   B CD  1 
ATOM   1147 C  CE  . LYS   B 2 98  ? -14.842 4.536   -30.161 1.00 70.47  ? 107 LYS   B CE  1 
ATOM   1148 N  NZ  . LYS   B 2 98  ? -13.396 4.773   -30.443 1.00 73.32  ? 107 LYS   B NZ  1 
ATOM   1149 N  N   . ASN   B 2 99  ? -19.350 1.014   -30.189 1.00 46.36  ? 108 ASN   B N   1 
ATOM   1150 C  CA  . ASN   B 2 99  ? -19.090 -0.399  -29.862 1.00 45.47  ? 108 ASN   B CA  1 
ATOM   1151 C  C   . ASN   B 2 99  ? -17.743 -0.824  -30.429 1.00 45.70  ? 108 ASN   B C   1 
ATOM   1152 O  O   . ASN   B 2 99  ? -17.456 -0.570  -31.584 1.00 46.56  ? 108 ASN   B O   1 
ATOM   1153 C  CB  . ASN   B 2 99  ? -20.200 -1.342  -30.378 1.00 45.02  ? 108 ASN   B CB  1 
ATOM   1154 C  CG  . ASN   B 2 99  ? -21.552 -1.238  -29.687 1.00 47.12  ? 108 ASN   B CG  1 
ATOM   1155 O  OD1 . ASN   B 2 99  ? -22.221 -0.200  -29.688 1.00 48.67  ? 108 ASN   B OD1 1 
ATOM   1156 N  ND2 . ASN   B 2 99  ? -22.031 -2.332  -29.143 1.00 46.79  ? 108 ASN   B ND2 1 
ATOM   1157 N  N   . ILE   B 2 100 ? -16.907 -1.452  -29.625 1.00 45.55  ? 109 ILE   B N   1 
ATOM   1158 C  CA  . ILE   B 2 100 ? -15.584 -1.904  -30.057 1.00 45.71  ? 109 ILE   B CA  1 
ATOM   1159 C  C   . ILE   B 2 100 ? -15.463 -3.359  -29.715 1.00 45.37  ? 109 ILE   B C   1 
ATOM   1160 O  O   . ILE   B 2 100 ? -15.463 -3.693  -28.546 1.00 45.39  ? 109 ILE   B O   1 
ATOM   1161 C  CB  . ILE   B 2 100 ? -14.482 -1.123  -29.317 1.00 46.55  ? 109 ILE   B CB  1 
ATOM   1162 C  CG1 . ILE   B 2 100 ? -14.708 0.403   -29.402 1.00 47.73  ? 109 ILE   B CG1 1 
ATOM   1163 C  CG2 . ILE   B 2 100 ? -13.109 -1.536  -29.840 1.00 46.77  ? 109 ILE   B CG2 1 
ATOM   1164 C  CD1 . ILE   B 2 100 ? -14.537 0.949   -30.885 1.00 48.90  ? 109 ILE   B CD1 1 
ATOM   1165 N  N   . GLN   B 2 101 ? -15.358 -4.221  -30.698 1.00 45.35  ? 110 GLN   B N   1 
ATOM   1166 C  CA  . GLN   B 2 101 ? -15.263 -5.654  -30.471 1.00 46.44  ? 110 GLN   B CA  1 
ATOM   1167 C  C   . GLN   B 2 101 ? -13.820 -6.102  -30.222 1.00 47.49  ? 110 GLN   B C   1 
ATOM   1168 O  O   . GLN   B 2 101 ? -12.913 -5.698  -30.952 1.00 48.58  ? 110 GLN   B O   1 
ATOM   1169 C  CB  . GLN   B 2 101 ? -15.858 -6.406  -31.662 1.00 48.07  ? 110 GLN   B CB  1 
ATOM   1170 C  CG  . GLN   B 2 101 ? -16.075 -7.878  -31.402 1.00 51.04  ? 110 GLN   B CG  1 
ATOM   1171 C  CD  . GLN   B 2 101 ? -16.996 -8.449  -32.435 1.00 54.05  ? 110 GLN   B CD  1 
ATOM   1172 O  OE1 . GLN   B 2 101 ? -18.019 -7.852  -32.775 1.00 54.23  ? 110 GLN   B OE1 1 
ATOM   1173 N  NE2 . GLN   B 2 101 ? -16.650 -9.617  -32.949 1.00 54.47  ? 110 GLN   B NE2 1 
ATOM   1174 N  N   . THR   B 2 102 ? -13.612 -6.967  -29.221 1.00 46.63  ? 111 THR   B N   1 
ATOM   1175 C  CA  . THR   B 2 102 ? -12.292 -7.497  -28.901 1.00 46.76  ? 111 THR   B CA  1 
ATOM   1176 C  C   . THR   B 2 102 ? -12.398 -8.897  -28.259 1.00 46.86  ? 111 THR   B C   1 
ATOM   1177 O  O   . THR   B 2 102 ? -13.480 -9.290  -27.819 1.00 47.60  ? 111 THR   B O   1 
ATOM   1178 C  CB  . THR   B 2 102 ? -11.569 -6.529  -27.931 1.00 48.21  ? 111 THR   B CB  1 
ATOM   1179 O  OG1 . THR   B 2 102 ? -10.188 -6.896  -27.843 1.00 49.79  ? 111 THR   B OG1 1 
ATOM   1180 C  CG2 . THR   B 2 102 ? -12.199 -6.499  -26.536 1.00 47.68  ? 111 THR   B CG2 1 
ATOM   1181 N  N   . LEU   B 2 103 ? -11.279 -9.648  -28.192 1.00 45.87  ? 112 LEU   B N   1 
ATOM   1182 C  CA  . LEU   B 2 103 ? -11.270 -10.925 -27.491 1.00 45.34  ? 112 LEU   B CA  1 
ATOM   1183 C  C   . LEU   B 2 103 ? -10.516 -10.663 -26.207 1.00 45.13  ? 112 LEU   B C   1 
ATOM   1184 O  O   . LEU   B 2 103 ? -9.349  -10.276 -26.246 1.00 45.22  ? 112 LEU   B O   1 
ATOM   1185 C  CB  . LEU   B 2 103 ? -10.586 -12.067 -28.253 1.00 45.24  ? 112 LEU   B CB  1 
ATOM   1186 C  CG  . LEU   B 2 103 ? -10.592 -13.374 -27.440 1.00 46.83  ? 112 LEU   B CG  1 
ATOM   1187 C  CD1 . LEU   B 2 103 ? -11.950 -14.020 -27.460 1.00 47.59  ? 112 LEU   B CD1 1 
ATOM   1188 C  CD2 . LEU   B 2 103 ? -9.513  -14.318 -27.869 1.00 47.38  ? 112 LEU   B CD2 1 
ATOM   1189 N  N   . PRO   B 2 104 ? -11.158 -10.881 -25.056 1.00 44.52  ? 113 PRO   B N   1 
ATOM   1190 C  CA  . PRO   B 2 104 ? -10.486 -10.592 -23.787 1.00 44.27  ? 113 PRO   B CA  1 
ATOM   1191 C  C   . PRO   B 2 104 ? -9.317  -11.502 -23.465 1.00 44.99  ? 113 PRO   B C   1 
ATOM   1192 O  O   . PRO   B 2 104 ? -9.290  -12.672 -23.846 1.00 45.45  ? 113 PRO   B O   1 
ATOM   1193 C  CB  . PRO   B 2 104 ? -11.592 -10.768 -22.744 1.00 44.19  ? 113 PRO   B CB  1 
ATOM   1194 C  CG  . PRO   B 2 104 ? -12.852 -10.709 -23.485 1.00 44.70  ? 113 PRO   B CG  1 
ATOM   1195 C  CD  . PRO   B 2 104 ? -12.550 -11.302 -24.839 1.00 43.76  ? 113 PRO   B CD  1 
ATOM   1196 N  N   . GLY   B 2 105 ? -8.343  -10.922 -22.783 1.00 44.74  ? 114 GLY   B N   1 
ATOM   1197 C  CA  . GLY   B 2 105 ? -7.210  -11.613 -22.207 1.00 44.89  ? 114 GLY   B CA  1 
ATOM   1198 C  C   . GLY   B 2 105 ? -7.568  -12.056 -20.792 1.00 45.16  ? 114 GLY   B C   1 
ATOM   1199 O  O   . GLY   B 2 105 ? -8.752  -12.135 -20.441 1.00 44.69  ? 114 GLY   B O   1 
ATOM   1200 N  N   . ILE   B 2 106 ? -6.549  -12.347 -19.953 1.00 45.33  ? 115 ILE   B N   1 
ATOM   1201 C  CA  . ILE   B 2 106 ? -6.757  -12.861 -18.607 1.00 45.63  ? 115 ILE   B CA  1 
ATOM   1202 C  C   . ILE   B 2 106 ? -5.870  -12.210 -17.543 1.00 46.17  ? 115 ILE   B C   1 
ATOM   1203 O  O   . ILE   B 2 106 ? -4.652  -12.148 -17.685 1.00 46.62  ? 115 ILE   B O   1 
ATOM   1204 C  CB  . ILE   B 2 106 ? -6.520  -14.407 -18.640 1.00 46.70  ? 115 ILE   B CB  1 
ATOM   1205 C  CG1 . ILE   B 2 106 ? -7.636  -15.153 -19.369 1.00 47.93  ? 115 ILE   B CG1 1 
ATOM   1206 C  CG2 . ILE   B 2 106 ? -6.266  -15.028 -17.249 1.00 47.64  ? 115 ILE   B CG2 1 
ATOM   1207 C  CD1 . ILE   B 2 106 ? -8.910  -14.991 -18.747 1.00 49.24  ? 115 ILE   B CD1 1 
ATOM   1208 N  N   . PHE   B 2 107 ? -6.471  -11.830 -16.423 1.00 45.94  ? 116 PHE   B N   1 
ATOM   1209 C  CA  . PHE   B 2 107 ? -5.744  -11.358 -15.264 1.00 45.65  ? 116 PHE   B CA  1 
ATOM   1210 C  C   . PHE   B 2 107 ? -5.706  -12.577 -14.363 1.00 46.05  ? 116 PHE   B C   1 
ATOM   1211 O  O   . PHE   B 2 107 ? -6.746  -12.980 -13.866 1.00 46.06  ? 116 PHE   B O   1 
ATOM   1212 C  CB  . PHE   B 2 107 ? -6.540  -10.260 -14.547 1.00 45.07  ? 116 PHE   B CB  1 
ATOM   1213 C  CG  . PHE   B 2 107 ? -6.248  -8.827  -14.920 1.00 44.93  ? 116 PHE   B CG  1 
ATOM   1214 C  CD1 . PHE   B 2 107 ? -5.457  -8.525  -16.015 1.00 45.00  ? 116 PHE   B CD1 1 
ATOM   1215 C  CD2 . PHE   B 2 107 ? -6.776  -7.782  -14.180 1.00 45.48  ? 116 PHE   B CD2 1 
ATOM   1216 C  CE1 . PHE   B 2 107 ? -5.178  -7.207  -16.344 1.00 45.64  ? 116 PHE   B CE1 1 
ATOM   1217 C  CE2 . PHE   B 2 107 ? -6.500  -6.463  -14.515 1.00 46.11  ? 116 PHE   B CE2 1 
ATOM   1218 C  CZ  . PHE   B 2 107 ? -5.707  -6.184  -15.598 1.00 45.75  ? 116 PHE   B CZ  1 
ATOM   1219 N  N   . LYS   B 2 108 ? -4.544  -13.192 -14.183 1.00 46.53  ? 117 LYS   B N   1 
ATOM   1220 C  CA  . LYS   B 2 108 ? -4.400  -14.342 -13.300 1.00 47.71  ? 117 LYS   B CA  1 
ATOM   1221 C  C   . LYS   B 2 108 ? -4.122  -13.826 -11.893 1.00 47.72  ? 117 LYS   B C   1 
ATOM   1222 O  O   . LYS   B 2 108 ? -3.105  -13.170 -11.680 1.00 47.54  ? 117 LYS   B O   1 
ATOM   1223 C  CB  . LYS   B 2 108 ? -3.203  -15.189 -13.744 1.00 51.47  ? 117 LYS   B CB  1 
ATOM   1224 C  CG  . LYS   B 2 108 ? -3.420  -16.697 -13.656 1.00 57.82  ? 117 LYS   B CG  1 
ATOM   1225 C  CD  . LYS   B 2 108 ? -3.370  -17.322 -15.052 1.00 63.62  ? 117 LYS   B CD  1 
ATOM   1226 C  CE  . LYS   B 2 108 ? -3.727  -18.788 -15.065 1.00 68.42  ? 117 LYS   B CE  1 
ATOM   1227 N  NZ  . LYS   B 2 108 ? -3.665  -19.345 -16.453 1.00 71.93  ? 117 LYS   B NZ  1 
ATOM   1228 N  N   . THR   B 2 109 ? -5.026  -14.085 -10.938 1.00 47.67  ? 118 THR   B N   1 
ATOM   1229 C  CA  . THR   B 2 109 ? -4.839  -13.650 -9.543  1.00 47.91  ? 118 THR   B CA  1 
ATOM   1230 C  C   . THR   B 2 109 ? -4.826  -14.856 -8.600  1.00 48.48  ? 118 THR   B C   1 
ATOM   1231 O  O   . THR   B 2 109 ? -5.322  -15.922 -8.958  1.00 48.51  ? 118 THR   B O   1 
ATOM   1232 C  CB  . THR   B 2 109 ? -5.859  -12.539 -9.104  1.00 47.99  ? 118 THR   B CB  1 
ATOM   1233 O  OG1 . THR   B 2 109 ? -7.039  -13.093 -8.516  1.00 48.40  ? 118 THR   B OG1 1 
ATOM   1234 C  CG2 . THR   B 2 109 ? -6.226  -11.578 -10.215 1.00 47.87  ? 118 THR   B CG2 1 
ATOM   1235 N  N   . LYS   B 2 110 ? -4.317  -14.682 -7.383  1.00 49.18  ? 119 LYS   B N   1 
ATOM   1236 C  CA  . LYS   B 2 110 ? -4.309  -15.762 -6.388  1.00 50.31  ? 119 LYS   B CA  1 
ATOM   1237 C  C   . LYS   B 2 110 ? -5.738  -16.237 -6.028  1.00 51.46  ? 119 LYS   B C   1 
ATOM   1238 O  O   . LYS   B 2 110 ? -5.897  -17.344 -5.501  1.00 52.23  ? 119 LYS   B O   1 
ATOM   1239 C  CB  . LYS   B 2 110 ? -3.538  -15.348 -5.118  1.00 51.37  ? 119 LYS   B CB  1 
ATOM   1240 C  CG  . LYS   B 2 110 ? -4.206  -14.225 -4.326  1.00 55.54  ? 119 LYS   B CG  1 
ATOM   1241 C  CD  . LYS   B 2 110 ? -3.466  -13.945 -3.008  1.00 60.37  ? 119 LYS   B CD  1 
ATOM   1242 C  CE  . LYS   B 2 110 ? -4.248  -13.119 -2.008  1.00 63.99  ? 119 LYS   B CE  1 
ATOM   1243 N  NZ  . LYS   B 2 110 ? -4.126  -11.661 -2.259  1.00 66.52  ? 119 LYS   B NZ  1 
ATOM   1244 N  N   . ASP   B 2 111 ? -6.766  -15.406 -6.308  1.00 51.05  ? 120 ASP   B N   1 
ATOM   1245 C  CA  . ASP   B 2 111 ? -8.158  -15.727 -6.028  1.00 51.42  ? 120 ASP   B CA  1 
ATOM   1246 C  C   . ASP   B 2 111 ? -8.959  -16.120 -7.266  1.00 51.99  ? 120 ASP   B C   1 
ATOM   1247 O  O   . ASP   B 2 111 ? -10.187 -16.104 -7.204  1.00 52.57  ? 120 ASP   B O   1 
ATOM   1248 C  CB  . ASP   B 2 111 ? -8.853  -14.538 -5.360  1.00 52.98  ? 120 ASP   B CB  1 
ATOM   1249 C  CG  . ASP   B 2 111 ? -8.329  -14.190 -3.988  1.00 58.15  ? 120 ASP   B CG  1 
ATOM   1250 O  OD1 . ASP   B 2 111 ? -7.662  -15.055 -3.366  1.00 58.82  ? 120 ASP   B OD1 1 
ATOM   1251 O  OD2 . ASP   B 2 111 ? -8.592  -13.058 -3.527  1.00 60.81  ? 120 ASP   B OD2 1 
ATOM   1252 N  N   . GLY   B 2 112 ? -8.292  -16.446 -8.373  1.00 51.51  ? 121 GLY   B N   1 
ATOM   1253 C  CA  . GLY   B 2 112 ? -8.975  -16.831 -9.599  1.00 51.37  ? 121 GLY   B CA  1 
ATOM   1254 C  C   . GLY   B 2 112 ? -8.714  -15.932 -10.792 1.00 50.81  ? 121 GLY   B C   1 
ATOM   1255 O  O   . GLY   B 2 112 ? -8.240  -14.806 -10.635 1.00 50.82  ? 121 GLY   B O   1 
ATOM   1256 N  N   . ASP   B 2 113 ? -9.034  -16.427 -11.999 1.00 50.09  ? 122 ASP   B N   1 
ATOM   1257 C  CA  . ASP   B 2 113 ? -8.859  -15.668 -13.236 1.00 49.90  ? 122 ASP   B CA  1 
ATOM   1258 C  C   . ASP   B 2 113 ? -10.034 -14.709 -13.515 1.00 48.89  ? 122 ASP   B C   1 
ATOM   1259 O  O   . ASP   B 2 113 ? -11.187 -14.990 -13.175 1.00 48.96  ? 122 ASP   B O   1 
ATOM   1260 C  CB  . ASP   B 2 113 ? -8.660  -16.602 -14.440 1.00 51.90  ? 122 ASP   B CB  1 
ATOM   1261 C  CG  . ASP   B 2 113 ? -7.503  -17.577 -14.326 1.00 58.22  ? 122 ASP   B CG  1 
ATOM   1262 O  OD1 . ASP   B 2 113 ? -6.773  -17.521 -13.313 1.00 58.59  ? 122 ASP   B OD1 1 
ATOM   1263 O  OD2 . ASP   B 2 113 ? -7.332  -18.403 -15.251 1.00 62.07  ? 122 ASP   B OD2 1 
ATOM   1264 N  N   . ILE   B 2 114 ? -9.720  -13.566 -14.122 1.00 47.49  ? 123 ILE   B N   1 
ATOM   1265 C  CA  . ILE   B 2 114 ? -10.699 -12.546 -14.490 1.00 46.88  ? 123 ILE   B CA  1 
ATOM   1266 C  C   . ILE   B 2 114 ? -10.418 -12.181 -15.943 1.00 45.71  ? 123 ILE   B C   1 
ATOM   1267 O  O   . ILE   B 2 114 ? -9.256  -12.061 -16.323 1.00 45.15  ? 123 ILE   B O   1 
ATOM   1268 C  CB  . ILE   B 2 114 ? -10.573 -11.257 -13.616 1.00 47.52  ? 123 ILE   B CB  1 
ATOM   1269 C  CG1 . ILE   B 2 114 ? -10.326 -11.548 -12.147 1.00 49.24  ? 123 ILE   B CG1 1 
ATOM   1270 C  CG2 . ILE   B 2 114 ? -11.773 -10.344 -13.785 1.00 47.79  ? 123 ILE   B CG2 1 
ATOM   1271 C  CD1 . ILE   B 2 114 ? -9.878  -10.331 -11.358 1.00 51.21  ? 123 ILE   B CD1 1 
ATOM   1272 N  N   . GLY   B 2 115 ? -11.461 -11.950 -16.731 1.00 45.10  ? 124 GLY   B N   1 
ATOM   1273 C  CA  . GLY   B 2 115 ? -11.281 -11.493 -18.108 1.00 44.71  ? 124 GLY   B CA  1 
ATOM   1274 C  C   . GLY   B 2 115 ? -10.718 -10.082 -18.111 1.00 44.33  ? 124 GLY   B C   1 
ATOM   1275 O  O   . GLY   B 2 115 ? -10.905 -9.343  -17.140 1.00 45.24  ? 124 GLY   B O   1 
ATOM   1276 N  N   . ALA   B 2 116 ? -9.991  -9.704  -19.154 1.00 43.32  ? 125 ALA   B N   1 
ATOM   1277 C  CA  . ALA   B 2 116 ? -9.408  -8.366  -19.243 1.00 43.07  ? 125 ALA   B CA  1 
ATOM   1278 C  C   . ALA   B 2 116 ? -9.504  -7.834  -20.680 1.00 43.17  ? 125 ALA   B C   1 
ATOM   1279 O  O   . ALA   B 2 116 ? -9.312  -8.585  -21.613 1.00 43.32  ? 125 ALA   B O   1 
ATOM   1280 C  CB  . ALA   B 2 116 ? -7.960  -8.397  -18.785 1.00 42.70  ? 125 ALA   B CB  1 
ATOM   1281 N  N   A VAL   B 2 117 ? -9.817  -6.542  -20.851 0.25 43.19  ? 126 VAL   B N   1 
ATOM   1282 N  N   B VAL   B 2 117 ? -9.788  -6.546  -20.838 0.25 43.21  ? 126 VAL   B N   1 
ATOM   1283 N  N   C VAL   B 2 117 ? -9.817  -6.542  -20.851 0.25 43.19  ? 126 VAL   B N   1 
ATOM   1284 N  N   D VAL   B 2 117 ? -9.788  -6.546  -20.838 0.25 43.21  ? 126 VAL   B N   1 
ATOM   1285 C  CA  A VAL   B 2 117 ? -9.916  -5.947  -22.183 0.25 43.84  ? 126 VAL   B CA  1 
ATOM   1286 C  CA  B VAL   B 2 117 ? -9.917  -5.923  -22.147 0.25 43.91  ? 126 VAL   B CA  1 
ATOM   1287 C  CA  C VAL   B 2 117 ? -9.916  -5.947  -22.183 0.25 43.84  ? 126 VAL   B CA  1 
ATOM   1288 C  CA  D VAL   B 2 117 ? -9.917  -5.923  -22.147 0.25 43.91  ? 126 VAL   B CA  1 
ATOM   1289 C  C   A VAL   B 2 117 ? -8.747  -4.997  -22.466 0.25 44.52  ? 126 VAL   B C   1 
ATOM   1290 C  C   B VAL   B 2 117 ? -8.727  -5.000  -22.444 0.25 44.55  ? 126 VAL   B C   1 
ATOM   1291 C  C   C VAL   B 2 117 ? -8.747  -4.997  -22.466 0.25 44.52  ? 126 VAL   B C   1 
ATOM   1292 C  C   D VAL   B 2 117 ? -8.727  -5.000  -22.444 0.25 44.55  ? 126 VAL   B C   1 
ATOM   1293 O  O   A VAL   B 2 117 ? -8.519  -4.041  -21.727 0.25 44.74  ? 126 VAL   B O   1 
ATOM   1294 O  O   B VAL   B 2 117 ? -8.473  -4.058  -21.694 0.25 44.77  ? 126 VAL   B O   1 
ATOM   1295 O  O   C VAL   B 2 117 ? -8.519  -4.041  -21.727 0.25 44.74  ? 126 VAL   B O   1 
ATOM   1296 O  O   D VAL   B 2 117 ? -8.473  -4.058  -21.694 0.25 44.77  ? 126 VAL   B O   1 
ATOM   1297 C  CB  A VAL   B 2 117 ? -11.292 -5.300  -22.469 0.25 44.41  ? 126 VAL   B CB  1 
ATOM   1298 C  CB  B VAL   B 2 117 ? -11.282 -5.203  -22.255 0.25 44.56  ? 126 VAL   B CB  1 
ATOM   1299 C  CB  C VAL   B 2 117 ? -11.292 -5.300  -22.469 0.25 44.41  ? 126 VAL   B CB  1 
ATOM   1300 C  CB  D VAL   B 2 117 ? -11.282 -5.203  -22.255 0.25 44.56  ? 126 VAL   B CB  1 
ATOM   1301 C  CG1 A VAL   B 2 117 ? -12.331 -6.365  -22.800 0.25 44.87  ? 126 VAL   B CG1 1 
ATOM   1302 C  CG1 B VAL   B 2 117 ? -11.335 -4.277  -23.459 0.25 45.17  ? 126 VAL   B CG1 1 
ATOM   1303 C  CG1 C VAL   B 2 117 ? -12.331 -6.365  -22.800 0.25 44.87  ? 126 VAL   B CG1 1 
ATOM   1304 C  CG1 D VAL   B 2 117 ? -11.335 -4.277  -23.459 0.25 45.17  ? 126 VAL   B CG1 1 
ATOM   1305 C  CG2 A VAL   B 2 117 ? -11.754 -4.430  -21.306 0.25 44.89  ? 126 VAL   B CG2 1 
ATOM   1306 C  CG2 B VAL   B 2 117 ? -12.419 -6.216  -22.302 0.25 44.99  ? 126 VAL   B CG2 1 
ATOM   1307 C  CG2 C VAL   B 2 117 ? -11.754 -4.430  -21.306 0.25 44.89  ? 126 VAL   B CG2 1 
ATOM   1308 C  CG2 D VAL   B 2 117 ? -12.419 -6.216  -22.302 0.25 44.99  ? 126 VAL   B CG2 1 
ATOM   1309 N  N   . ALA   B 2 118 ? -7.984  -5.285  -23.521 1.00 44.64  ? 127 ALA   B N   1 
ATOM   1310 C  CA  . ALA   B 2 118 ? -6.829  -4.469  -23.887 1.00 45.89  ? 127 ALA   B CA  1 
ATOM   1311 C  C   . ALA   B 2 118 ? -7.244  -3.365  -24.841 1.00 47.35  ? 127 ALA   B C   1 
ATOM   1312 O  O   . ALA   B 2 118 ? -7.154  -3.516  -26.055 1.00 47.78  ? 127 ALA   B O   1 
ATOM   1313 C  CB  . ALA   B 2 118 ? -5.747  -5.332  -24.510 1.00 45.67  ? 127 ALA   B CB  1 
ATOM   1314 N  N   . LEU   B 2 119 ? -7.783  -2.281  -24.286 1.00 47.88  ? 128 LEU   B N   1 
ATOM   1315 C  CA  . LEU   B 2 119 ? -8.241  -1.120  -25.047 1.00 48.42  ? 128 LEU   B CA  1 
ATOM   1316 C  C   . LEU   B 2 119 ? -7.886  0.136   -24.248 1.00 49.20  ? 128 LEU   B C   1 
ATOM   1317 O  O   . LEU   B 2 119 ? -8.092  0.168   -23.030 1.00 49.33  ? 128 LEU   B O   1 
ATOM   1318 C  CB  . LEU   B 2 119 ? -9.757  -1.200  -25.319 1.00 48.29  ? 128 LEU   B CB  1 
ATOM   1319 C  CG  . LEU   B 2 119 ? -10.163 -2.157  -26.445 1.00 49.54  ? 128 LEU   B CG  1 
ATOM   1320 C  CD1 . LEU   B 2 119 ? -11.661 -2.346  -26.500 1.00 49.66  ? 128 LEU   B CD1 1 
ATOM   1321 C  CD2 . LEU   B 2 119 ? -9.605  -1.697  -27.804 1.00 50.10  ? 128 LEU   B CD2 1 
ATOM   1322 N  N   . ASP   B 2 120 ? -7.302  1.143   -24.913 1.00 49.43  ? 129 ASP   B N   1 
ATOM   1323 C  CA  . ASP   B 2 120 ? -6.879  2.360   -24.229 1.00 49.96  ? 129 ASP   B CA  1 
ATOM   1324 C  C   . ASP   B 2 120 ? -7.756  3.578   -24.579 1.00 49.88  ? 129 ASP   B C   1 
ATOM   1325 O  O   . ASP   B 2 120 ? -7.637  4.129   -25.668 1.00 50.51  ? 129 ASP   B O   1 
ATOM   1326 C  CB  . ASP   B 2 120 ? -5.388  2.640   -24.505 1.00 51.86  ? 129 ASP   B CB  1 
ATOM   1327 C  CG  . ASP   B 2 120 ? -4.673  3.414   -23.402 1.00 57.48  ? 129 ASP   B CG  1 
ATOM   1328 O  OD1 . ASP   B 2 120 ? -5.360  3.916   -22.481 1.00 57.89  ? 129 ASP   B OD1 1 
ATOM   1329 O  OD2 . ASP   B 2 120 ? -3.427  3.519   -23.461 1.00 60.41  ? 129 ASP   B OD2 1 
ATOM   1330 N  N   . TYR   B 2 121 ? -8.609  4.004   -23.637 1.00 49.00  ? 130 TYR   B N   1 
ATOM   1331 C  CA  . TYR   B 2 121 ? -9.531  5.136   -23.769 1.00 48.88  ? 130 TYR   B CA  1 
ATOM   1332 C  C   . TYR   B 2 121 ? -9.345  6.112   -22.603 1.00 47.62  ? 130 TYR   B C   1 
ATOM   1333 O  O   . TYR   B 2 121 ? -8.989  5.676   -21.506 1.00 47.78  ? 130 TYR   B O   1 
ATOM   1334 C  CB  . TYR   B 2 121 ? -10.983 4.625   -23.786 1.00 49.88  ? 130 TYR   B CB  1 
ATOM   1335 C  CG  . TYR   B 2 121 ? -11.354 4.012   -25.115 1.00 51.99  ? 130 TYR   B CG  1 
ATOM   1336 C  CD1 . TYR   B 2 121 ? -11.917 4.782   -26.123 1.00 53.41  ? 130 TYR   B CD1 1 
ATOM   1337 C  CD2 . TYR   B 2 121 ? -11.043 2.690   -25.403 1.00 53.47  ? 130 TYR   B CD2 1 
ATOM   1338 C  CE1 . TYR   B 2 121 ? -12.200 4.241   -27.370 1.00 54.61  ? 130 TYR   B CE1 1 
ATOM   1339 C  CE2 . TYR   B 2 121 ? -11.309 2.142   -26.652 1.00 54.62  ? 130 TYR   B CE2 1 
ATOM   1340 C  CZ  . TYR   B 2 121 ? -11.898 2.918   -27.628 1.00 55.99  ? 130 TYR   B CZ  1 
ATOM   1341 O  OH  . TYR   B 2 121 ? -12.165 2.386   -28.864 1.00 58.95  ? 130 TYR   B OH  1 
ATOM   1342 N  N   . PRO   B 2 122 ? -9.652  7.424   -22.762 1.00 45.88  ? 131 PRO   B N   1 
ATOM   1343 C  CA  . PRO   B 2 122 ? -9.468  8.364   -21.639 1.00 44.45  ? 131 PRO   B CA  1 
ATOM   1344 C  C   . PRO   B 2 122 ? -9.986  7.870   -20.285 1.00 42.80  ? 131 PRO   B C   1 
ATOM   1345 O  O   . PRO   B 2 122 ? -10.890 7.039   -20.262 1.00 43.20  ? 131 PRO   B O   1 
ATOM   1346 C  CB  . PRO   B 2 122 ? -10.203 9.617   -22.111 1.00 45.26  ? 131 PRO   B CB  1 
ATOM   1347 C  CG  . PRO   B 2 122 ? -10.076 9.584   -23.581 1.00 46.29  ? 131 PRO   B CG  1 
ATOM   1348 C  CD  . PRO   B 2 122 ? -10.119 8.125   -23.976 1.00 45.26  ? 131 PRO   B CD  1 
ATOM   1349 N  N   . ALA   B 2 123 ? -9.391  8.328   -19.167 1.00 40.62  ? 132 ALA   B N   1 
ATOM   1350 C  CA  . ALA   B 2 123 ? -9.818  7.894   -17.833 1.00 39.00  ? 132 ALA   B CA  1 
ATOM   1351 C  C   . ALA   B 2 123 ? -11.308 8.111   -17.579 1.00 37.52  ? 132 ALA   B C   1 
ATOM   1352 O  O   . ALA   B 2 123 ? -11.937 7.298   -16.904 1.00 37.20  ? 132 ALA   B O   1 
ATOM   1353 C  CB  . ALA   B 2 123 ? -9.001  8.589   -16.760 1.00 38.65  ? 132 ALA   B CB  1 
ATOM   1354 N  N   . GLY   B 2 124 ? -11.869 9.154   -18.190 1.00 36.44  ? 133 GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 2 124 ? -13.282 9.500   -18.065 1.00 35.58  ? 133 GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 2 124 ? -14.242 8.534   -18.735 1.00 34.19  ? 133 GLY   B C   1 
ATOM   1357 O  O   . GLY   B 2 124 ? -15.453 8.732   -18.670 1.00 33.91  ? 133 GLY   B O   1 
ATOM   1358 N  N   . THR   B 2 125 ? -13.713 7.490   -19.391 1.00 33.34  ? 134 THR   B N   1 
ATOM   1359 C  CA  . THR   B 2 125 ? -14.492 6.428   -20.033 1.00 33.19  ? 134 THR   B CA  1 
ATOM   1360 C  C   . THR   B 2 125 ? -14.870 5.322   -18.999 1.00 33.05  ? 134 THR   B C   1 
ATOM   1361 O  O   . THR   B 2 125 ? -15.787 4.548   -19.271 1.00 33.43  ? 134 THR   B O   1 
ATOM   1362 C  CB  . THR   B 2 125 ? -13.735 5.892   -21.283 1.00 34.53  ? 134 THR   B CB  1 
ATOM   1363 O  OG1 . THR   B 2 125 ? -13.379 6.990   -22.128 1.00 36.09  ? 134 THR   B OG1 1 
ATOM   1364 C  CG2 . THR   B 2 125 ? -14.557 4.931   -22.120 1.00 34.87  ? 134 THR   B CG2 1 
ATOM   1365 N  N   . SER   B 2 126 ? -14.190 5.268   -17.812 1.00 32.13  ? 135 SER   B N   1 
ATOM   1366 C  CA  . SER   B 2 126 ? -14.451 4.272   -16.760 1.00 32.30  ? 135 SER   B CA  1 
ATOM   1367 C  C   . SER   B 2 126 ? -15.930 4.136   -16.409 1.00 31.89  ? 135 SER   B C   1 
ATOM   1368 O  O   . SER   B 2 126 ? -16.577 5.121   -16.091 1.00 32.05  ? 135 SER   B O   1 
ATOM   1369 C  CB  . SER   B 2 126 ? -13.695 4.616   -15.484 1.00 33.61  ? 135 SER   B CB  1 
ATOM   1370 O  OG  . SER   B 2 126 ? -12.293 4.575   -15.672 1.00 35.94  ? 135 SER   B OG  1 
ATOM   1371 N  N   . GLY   B 2 127 ? -16.418 2.905   -16.383 1.00 30.74  ? 136 GLY   B N   1 
ATOM   1372 C  CA  . GLY   B 2 127 ? -17.813 2.601   -16.108 1.00 29.95  ? 136 GLY   B CA  1 
ATOM   1373 C  C   . GLY   B 2 127 ? -18.550 2.123   -17.345 1.00 29.74  ? 136 GLY   B C   1 
ATOM   1374 O  O   . GLY   B 2 127 ? -19.692 1.674   -17.241 1.00 29.83  ? 136 GLY   B O   1 
ATOM   1375 N  N   . SER   B 2 128 ? -17.911 2.229   -18.549 1.00 28.69  ? 137 SER   B N   1 
ATOM   1376 C  CA  . SER   B 2 128 ? -18.480 1.783   -19.813 1.00 28.50  ? 137 SER   B CA  1 
ATOM   1377 C  C   . SER   B 2 128 ? -18.703 0.288   -19.731 1.00 28.20  ? 137 SER   B C   1 
ATOM   1378 O  O   . SER   B 2 128 ? -17.836 -0.426  -19.252 1.00 28.32  ? 137 SER   B O   1 
ATOM   1379 C  CB  . SER   B 2 128 ? -17.521 2.101   -20.960 1.00 30.04  ? 137 SER   B CB  1 
ATOM   1380 O  OG  . SER   B 2 128 ? -17.377 3.502   -21.126 1.00 31.59  ? 137 SER   B OG  1 
ATOM   1381 N  N   . PRO   B 2 129 ? -19.886 -0.195  -20.115 1.00 28.32  ? 138 PRO   B N   1 
ATOM   1382 C  CA  . PRO   B 2 129 ? -20.158 -1.630  -19.994 1.00 29.02  ? 138 PRO   B CA  1 
ATOM   1383 C  C   . PRO   B 2 129 ? -19.482 -2.481  -21.063 1.00 30.57  ? 138 PRO   B C   1 
ATOM   1384 O  O   . PRO   B 2 129 ? -19.208 -2.009  -22.156 1.00 31.41  ? 138 PRO   B O   1 
ATOM   1385 C  CB  . PRO   B 2 129 ? -21.684 -1.701  -20.130 1.00 29.05  ? 138 PRO   B CB  1 
ATOM   1386 C  CG  . PRO   B 2 129 ? -22.039 -0.556  -20.996 1.00 28.94  ? 138 PRO   B CG  1 
ATOM   1387 C  CD  . PRO   B 2 129 ? -21.036 0.534   -20.692 1.00 27.51  ? 138 PRO   B CD  1 
ATOM   1388 N  N   . ILE   B 2 130 ? -19.230 -3.739  -20.734 1.00 31.00  ? 139 ILE   B N   1 
ATOM   1389 C  CA  . ILE   B 2 130 ? -18.716 -4.743  -21.643 1.00 32.07  ? 139 ILE   B CA  1 
ATOM   1390 C  C   . ILE   B 2 130 ? -19.882 -5.733  -21.863 1.00 33.31  ? 139 ILE   B C   1 
ATOM   1391 O  O   . ILE   B 2 130 ? -20.607 -6.054  -20.917 1.00 32.72  ? 139 ILE   B O   1 
ATOM   1392 C  CB  . ILE   B 2 130 ? -17.450 -5.391  -21.069 1.00 32.52  ? 139 ILE   B CB  1 
ATOM   1393 C  CG1 . ILE   B 2 130 ? -16.347 -4.341  -20.951 1.00 33.26  ? 139 ILE   B CG1 1 
ATOM   1394 C  CG2 . ILE   B 2 130 ? -17.004 -6.554  -21.950 1.00 33.06  ? 139 ILE   B CG2 1 
ATOM   1395 C  CD1 . ILE   B 2 130 ? -15.439 -4.584  -19.802 1.00 34.57  ? 139 ILE   B CD1 1 
ATOM   1396 N  N   . LEU   B 2 131 ? -20.123 -6.138  -23.116 1.00 34.63  ? 140 LEU   B N   1 
ATOM   1397 C  CA  . LEU   B 2 131 ? -21.293 -6.949  -23.472 1.00 36.66  ? 140 LEU   B CA  1 
ATOM   1398 C  C   . LEU   B 2 131 ? -21.024 -8.286  -24.144 1.00 38.51  ? 140 LEU   B C   1 
ATOM   1399 O  O   . LEU   B 2 131 ? -20.148 -8.376  -24.994 1.00 38.97  ? 140 LEU   B O   1 
ATOM   1400 C  CB  . LEU   B 2 131 ? -22.159 -6.176  -24.487 1.00 36.75  ? 140 LEU   B CB  1 
ATOM   1401 C  CG  . LEU   B 2 131 ? -22.387 -4.699  -24.269 1.00 37.76  ? 140 LEU   B CG  1 
ATOM   1402 C  CD1 . LEU   B 2 131 ? -23.227 -4.149  -25.373 1.00 37.84  ? 140 LEU   B CD1 1 
ATOM   1403 C  CD2 . LEU   B 2 131 ? -23.016 -4.433  -22.895 1.00 38.19  ? 140 LEU   B CD2 1 
ATOM   1404 N  N   . ASP   B 2 132 ? -21.901 -9.268  -23.893 1.00 39.18  ? 141 ASP   B N   1 
ATOM   1405 C  CA  . ASP   B 2 132 ? -21.849 -10.527 -24.605 1.00 40.83  ? 141 ASP   B CA  1 
ATOM   1406 C  C   . ASP   B 2 132 ? -22.715 -10.425 -25.904 1.00 43.30  ? 141 ASP   B C   1 
ATOM   1407 O  O   . ASP   B 2 132 ? -23.352 -9.393  -26.135 1.00 43.05  ? 141 ASP   B O   1 
ATOM   1408 C  CB  . ASP   B 2 132 ? -22.226 -11.705 -23.695 1.00 41.63  ? 141 ASP   B CB  1 
ATOM   1409 C  CG  . ASP   B 2 132 ? -23.666 -11.812 -23.264 1.00 45.63  ? 141 ASP   B CG  1 
ATOM   1410 O  OD1 . ASP   B 2 132 ? -24.478 -10.952 -23.675 1.00 46.47  ? 141 ASP   B OD1 1 
ATOM   1411 O  OD2 . ASP   B 2 132 ? -23.988 -12.764 -22.515 1.00 47.60  ? 141 ASP   B OD2 1 
ATOM   1412 N  N   . LYS   B 2 133 ? -22.742 -11.480 -26.741 1.00 45.30  ? 142 LYS   B N   1 
ATOM   1413 C  CA  . LYS   B 2 133 ? -23.472 -11.480 -28.013 1.00 47.19  ? 142 LYS   B CA  1 
ATOM   1414 C  C   . LYS   B 2 133 ? -24.994 -11.254 -27.851 1.00 48.21  ? 142 LYS   B C   1 
ATOM   1415 O  O   . LYS   B 2 133 ? -25.625 -10.712 -28.760 1.00 48.80  ? 142 LYS   B O   1 
ATOM   1416 C  CB  . LYS   B 2 133 ? -23.146 -12.743 -28.820 1.00 50.36  ? 142 LYS   B CB  1 
ATOM   1417 C  CG  . LYS   B 2 133 ? -21.634 -12.873 -29.049 1.00 56.55  ? 142 LYS   B CG  1 
ATOM   1418 C  CD  . LYS   B 2 133 ? -21.211 -14.038 -29.966 1.00 62.68  ? 142 LYS   B CD  1 
ATOM   1419 C  CE  . LYS   B 2 133 ? -19.703 -14.201 -29.932 1.00 68.02  ? 142 LYS   B CE  1 
ATOM   1420 N  NZ  . LYS   B 2 133 ? -19.246 -15.526 -30.445 1.00 71.17  ? 142 LYS   B NZ  1 
ATOM   1421 N  N   . CYS   B 2 134 ? -25.559 -11.577 -26.677 1.00 48.43  ? 143 CYS   B N   1 
ATOM   1422 C  CA  . CYS   B 2 134 ? -26.973 -11.299 -26.360 1.00 48.80  ? 143 CYS   B CA  1 
ATOM   1423 C  C   . CYS   B 2 134 ? -27.231 -9.834  -26.006 1.00 47.08  ? 143 CYS   B C   1 
ATOM   1424 O  O   . CYS   B 2 134 ? -28.382 -9.479  -25.788 1.00 47.33  ? 143 CYS   B O   1 
ATOM   1425 C  CB  . CYS   B 2 134 ? -27.439 -12.178 -25.207 1.00 51.67  ? 143 CYS   B CB  1 
ATOM   1426 S  SG  . CYS   B 2 134 ? -27.599 -13.924 -25.619 1.00 60.18  ? 143 CYS   B SG  1 
ATOM   1427 N  N   . GLY   B 2 135 ? -26.177 -9.045  -25.817 1.00 45.37  ? 144 GLY   B N   1 
ATOM   1428 C  CA  . GLY   B 2 135 ? -26.260 -7.662  -25.381 1.00 44.19  ? 144 GLY   B CA  1 
ATOM   1429 C  C   . GLY   B 2 135 ? -26.276 -7.516  -23.869 1.00 42.78  ? 144 GLY   B C   1 
ATOM   1430 O  O   . GLY   B 2 135 ? -26.477 -6.408  -23.373 1.00 43.78  ? 144 GLY   B O   1 
ATOM   1431 N  N   . ARG   B 2 136 ? -26.110 -8.612  -23.114 1.00 40.54  ? 145 ARG   B N   1 
ATOM   1432 C  CA  . ARG   B 2 136 ? -26.123 -8.561  -21.651 1.00 39.49  ? 145 ARG   B CA  1 
ATOM   1433 C  C   . ARG   B 2 136 ? -24.819 -8.017  -21.085 1.00 37.17  ? 145 ARG   B C   1 
ATOM   1434 O  O   . ARG   B 2 136 ? -23.738 -8.416  -21.538 1.00 36.68  ? 145 ARG   B O   1 
ATOM   1435 C  CB  . ARG   B 2 136 ? -26.391 -9.952  -21.064 1.00 42.12  ? 145 ARG   B CB  1 
ATOM   1436 C  CG  . ARG   B 2 136 ? -27.813 -10.432 -21.298 1.00 47.82  ? 145 ARG   B CG  1 
ATOM   1437 C  CD  . ARG   B 2 136 ? -28.031 -11.804 -20.695 1.00 52.46  ? 145 ARG   B CD  1 
ATOM   1438 N  NE  . ARG   B 2 136 ? -27.237 -12.811 -21.391 1.00 57.09  ? 145 ARG   B NE  1 
ATOM   1439 C  CZ  . ARG   B 2 136 ? -26.615 -13.823 -20.792 1.00 61.85  ? 145 ARG   B CZ  1 
ATOM   1440 N  NH1 . ARG   B 2 136 ? -26.680 -13.966 -19.469 1.00 61.70  ? 145 ARG   B NH1 1 
ATOM   1441 N  NH2 . ARG   B 2 136 ? -25.905 -14.690 -21.507 1.00 62.59  ? 145 ARG   B NH2 1 
ATOM   1442 N  N   . VAL   B 2 137 ? -24.912 -7.138  -20.057 1.00 35.20  ? 146 VAL   B N   1 
ATOM   1443 C  CA  . VAL   B 2 137 ? -23.723 -6.551  -19.449 1.00 33.71  ? 146 VAL   B CA  1 
ATOM   1444 C  C   . VAL   B 2 137 ? -22.986 -7.577  -18.614 1.00 33.46  ? 146 VAL   B C   1 
ATOM   1445 O  O   . VAL   B 2 137 ? -23.523 -8.068  -17.626 1.00 33.90  ? 146 VAL   B O   1 
ATOM   1446 C  CB  . VAL   B 2 137 ? -24.031 -5.272  -18.639 1.00 33.58  ? 146 VAL   B CB  1 
ATOM   1447 C  CG1 . VAL   B 2 137 ? -22.754 -4.658  -18.090 1.00 33.47  ? 146 VAL   B CG1 1 
ATOM   1448 C  CG2 . VAL   B 2 137 ? -24.789 -4.258  -19.490 1.00 33.95  ? 146 VAL   B CG2 1 
ATOM   1449 N  N   . ILE   B 2 138 ? -21.770 -7.923  -19.021 1.00 32.36  ? 147 ILE   B N   1 
ATOM   1450 C  CA  . ILE   B 2 138 ? -20.945 -8.881  -18.298 1.00 31.54  ? 147 ILE   B CA  1 
ATOM   1451 C  C   . ILE   B 2 138 ? -19.922 -8.223  -17.366 1.00 30.94  ? 147 ILE   B C   1 
ATOM   1452 O  O   . ILE   B 2 138 ? -19.226 -8.941  -16.635 1.00 31.51  ? 147 ILE   B O   1 
ATOM   1453 C  CB  . ILE   B 2 138 ? -20.254 -9.841  -19.288 1.00 32.12  ? 147 ILE   B CB  1 
ATOM   1454 C  CG1 . ILE   B 2 138 ? -19.347 -9.053  -20.253 1.00 33.00  ? 147 ILE   B CG1 1 
ATOM   1455 C  CG2 . ILE   B 2 138 ? -21.290 -10.659 -20.049 1.00 32.66  ? 147 ILE   B CG2 1 
ATOM   1456 C  CD1 . ILE   B 2 138 ? -18.473 -9.905  -21.112 1.00 34.69  ? 147 ILE   B CD1 1 
ATOM   1457 N  N   . GLY   B 2 139 ? -19.825 -6.895  -17.375 1.00 29.67  ? 148 GLY   B N   1 
ATOM   1458 C  CA  . GLY   B 2 139 ? -18.892 -6.204  -16.494 1.00 29.78  ? 148 GLY   B CA  1 
ATOM   1459 C  C   . GLY   B 2 139 ? -18.642 -4.764  -16.880 1.00 29.64  ? 148 GLY   B C   1 
ATOM   1460 O  O   . GLY   B 2 139 ? -19.216 -4.280  -17.859 1.00 30.25  ? 148 GLY   B O   1 
ATOM   1461 N  N   . LEU   B 2 140 ? -17.797 -4.060  -16.114 1.00 28.43  ? 149 LEU   B N   1 
ATOM   1462 C  CA  . LEU   B 2 140 ? -17.488 -2.664  -16.389 1.00 28.27  ? 149 LEU   B CA  1 
ATOM   1463 C  C   . LEU   B 2 140 ? -16.000 -2.468  -16.585 1.00 28.99  ? 149 LEU   B C   1 
ATOM   1464 O  O   . LEU   B 2 140 ? -15.192 -3.092  -15.904 1.00 29.10  ? 149 LEU   B O   1 
ATOM   1465 C  CB  . LEU   B 2 140 ? -17.974 -1.729  -15.277 1.00 27.79  ? 149 LEU   B CB  1 
ATOM   1466 C  CG  . LEU   B 2 140 ? -19.450 -1.780  -14.894 1.00 28.57  ? 149 LEU   B CG  1 
ATOM   1467 C  CD1 . LEU   B 2 140 ? -19.743 -0.841  -13.723 1.00 28.60  ? 149 LEU   B CD1 1 
ATOM   1468 C  CD2 . LEU   B 2 140 ? -20.348 -1.449  -16.078 1.00 28.79  ? 149 LEU   B CD2 1 
ATOM   1469 N  N   . TYR   B 2 141 ? -15.658 -1.557  -17.501 1.00 29.48  ? 150 TYR   B N   1 
ATOM   1470 C  CA  . TYR   B 2 141 ? -14.311 -1.175  -17.906 1.00 30.42  ? 150 TYR   B CA  1 
ATOM   1471 C  C   . TYR   B 2 141 ? -13.802 -0.023  -17.064 1.00 30.40  ? 150 TYR   B C   1 
ATOM   1472 O  O   . TYR   B 2 141 ? -14.556 0.918   -16.836 1.00 30.60  ? 150 TYR   B O   1 
ATOM   1473 C  CB  . TYR   B 2 141 ? -14.387 -0.715  -19.384 1.00 31.03  ? 150 TYR   B CB  1 
ATOM   1474 C  CG  . TYR   B 2 141 ? -13.157 -0.017  -19.940 1.00 32.86  ? 150 TYR   B CG  1 
ATOM   1475 C  CD1 . TYR   B 2 141 ? -13.052 1.372   -19.926 1.00 34.23  ? 150 TYR   B CD1 1 
ATOM   1476 C  CD2 . TYR   B 2 141 ? -12.145 -0.738  -20.565 1.00 33.95  ? 150 TYR   B CD2 1 
ATOM   1477 C  CE1 . TYR   B 2 141 ? -11.925 2.016   -20.432 1.00 35.46  ? 150 TYR   B CE1 1 
ATOM   1478 C  CE2 . TYR   B 2 141 ? -11.022 -0.104  -21.088 1.00 35.08  ? 150 TYR   B CE2 1 
ATOM   1479 C  CZ  . TYR   B 2 141 ? -10.918 1.276   -21.031 1.00 36.31  ? 150 TYR   B CZ  1 
ATOM   1480 O  OH  . TYR   B 2 141 ? -9.810  1.906   -21.565 1.00 37.60  ? 150 TYR   B OH  1 
ATOM   1481 N  N   . GLY   B 2 142 ? -12.518 -0.025  -16.732 1.00 30.15  ? 151 GLY   B N   1 
ATOM   1482 C  CA  . GLY   B 2 142 ? -11.934 1.108   -16.032 1.00 31.20  ? 151 GLY   B CA  1 
ATOM   1483 C  C   . GLY   B 2 142 ? -11.092 0.829   -14.810 1.00 32.29  ? 151 GLY   B C   1 
ATOM   1484 O  O   . GLY   B 2 142 ? -10.661 1.779   -14.154 1.00 33.20  ? 151 GLY   B O   1 
ATOM   1485 N  N   . ASN   B 2 143 ? -10.880 -0.444  -14.452 1.00 31.66  ? 152 ASN   B N   1 
ATOM   1486 C  CA  . ASN   B 2 143 ? -10.004 -0.748  -13.330 1.00 31.62  ? 152 ASN   B CA  1 
ATOM   1487 C  C   . ASN   B 2 143 ? -9.067  -1.817  -13.767 1.00 32.32  ? 152 ASN   B C   1 
ATOM   1488 O  O   . ASN   B 2 143 ? -9.496  -2.939  -13.982 1.00 32.53  ? 152 ASN   B O   1 
ATOM   1489 C  CB  . ASN   B 2 143 ? -10.761 -1.169  -12.085 1.00 32.35  ? 152 ASN   B CB  1 
ATOM   1490 C  CG  . ASN   B 2 143 ? -9.898  -1.037  -10.840 1.00 33.96  ? 152 ASN   B CG  1 
ATOM   1491 O  OD1 . ASN   B 2 143 ? -9.039  -0.145  -10.756 1.00 35.19  ? 152 ASN   B OD1 1 
ATOM   1492 N  ND2 . ASN   B 2 143 ? -10.105 -1.909  -9.848  1.00 32.76  ? 152 ASN   B ND2 1 
ATOM   1493 N  N   . GLY   B 2 144 ? -7.802  -1.474  -13.914 1.00 32.83  ? 153 GLY   B N   1 
ATOM   1494 C  CA  . GLY   B 2 144 ? -6.815  -2.443  -14.340 1.00 34.68  ? 153 GLY   B CA  1 
ATOM   1495 C  C   . GLY   B 2 144 ? -5.391  -2.033  -14.086 1.00 37.04  ? 153 GLY   B C   1 
ATOM   1496 O  O   . GLY   B 2 144 ? -5.080  -1.436  -13.054 1.00 36.15  ? 153 GLY   B O   1 
ATOM   1497 N  N   . VAL   B 2 145 ? -4.523  -2.332  -15.065 1.00 39.75  ? 154 VAL   B N   1 
ATOM   1498 C  CA  . VAL   B 2 145 ? -3.095  -2.109  -14.961 1.00 42.90  ? 154 VAL   B CA  1 
ATOM   1499 C  C   . VAL   B 2 145 ? -2.456  -1.553  -16.254 1.00 46.25  ? 154 VAL   B C   1 
ATOM   1500 O  O   . VAL   B 2 145 ? -3.021  -1.667  -17.338 1.00 46.46  ? 154 VAL   B O   1 
ATOM   1501 C  CB  . VAL   B 2 145 ? -2.467  -3.452  -14.516 1.00 43.99  ? 154 VAL   B CB  1 
ATOM   1502 C  CG1 . VAL   B 2 145 ? -2.108  -4.342  -15.707 1.00 44.44  ? 154 VAL   B CG1 1 
ATOM   1503 C  CG2 . VAL   B 2 145 ? -1.273  -3.238  -13.598 1.00 44.98  ? 154 VAL   B CG2 1 
ATOM   1504 N  N   . VAL   B 2 146 ? -1.266  -0.961  -16.125 1.00 48.58  ? 155 VAL   B N   1 
ATOM   1505 C  CA  . VAL   B 2 146 ? -0.503  -0.415  -17.235 1.00 51.15  ? 155 VAL   B CA  1 
ATOM   1506 C  C   . VAL   B 2 146 ? 0.627   -1.415  -17.526 1.00 54.59  ? 155 VAL   B C   1 
ATOM   1507 O  O   . VAL   B 2 146 ? 1.319   -1.833  -16.597 1.00 54.77  ? 155 VAL   B O   1 
ATOM   1508 C  CB  . VAL   B 2 146 ? 0.020   0.988   -16.870 1.00 51.47  ? 155 VAL   B CB  1 
ATOM   1509 C  CG1 . VAL   B 2 146 ? 1.004   1.492   -17.906 1.00 52.29  ? 155 VAL   B CG1 1 
ATOM   1510 C  CG2 . VAL   B 2 146 ? -1.134  1.963   -16.710 1.00 51.75  ? 155 VAL   B CG2 1 
ATOM   1511 N  N   . ILE   B 2 147 ? 0.774   -1.854  -18.795 1.00 56.97  ? 156 ILE   B N   1 
ATOM   1512 C  CA  . ILE   B 2 147 ? 1.762   -2.881  -19.122 1.00 59.76  ? 156 ILE   B CA  1 
ATOM   1513 C  C   . ILE   B 2 147 ? 3.113   -2.245  -19.653 1.00 62.21  ? 156 ILE   B C   1 
ATOM   1514 O  O   . ILE   B 2 147 ? 3.199   -1.017  -19.766 1.00 62.21  ? 156 ILE   B O   1 
ATOM   1515 C  CB  . ILE   B 2 147 ? 1.131   -3.994  -20.035 1.00 60.66  ? 156 ILE   B CB  1 
ATOM   1516 C  CG1 . ILE   B 2 147 ? 1.020   -3.567  -21.487 1.00 62.36  ? 156 ILE   B CG1 1 
ATOM   1517 C  CG2 . ILE   B 2 147 ? -0.207  -4.480  -19.498 1.00 61.00  ? 156 ILE   B CG2 1 
ATOM   1518 C  CD1 . ILE   B 2 147 ? 0.646   -4.732  -22.477 1.00 63.81  ? 156 ILE   B CD1 1 
ATOM   1519 N  N   A LYS   B 2 148 ? 4.129   -3.092  -19.930 0.25 62.64  ? 157 LYS   B N   1 
ATOM   1520 N  N   B LYS   B 2 148 ? 4.129   -3.092  -19.930 0.25 62.64  ? 157 LYS   B N   1 
ATOM   1521 N  N   C LYS   B 2 148 ? 4.132   -3.086  -19.925 0.25 62.64  ? 157 LYS   B N   1 
ATOM   1522 N  N   D LYS   B 2 148 ? 4.132   -3.086  -19.925 0.25 62.64  ? 157 LYS   B N   1 
ATOM   1523 C  CA  A LYS   B 2 148 ? 5.467   -2.726  -20.406 0.25 63.49  ? 157 LYS   B CA  1 
ATOM   1524 C  CA  B LYS   B 2 148 ? 5.467   -2.726  -20.406 0.25 63.49  ? 157 LYS   B CA  1 
ATOM   1525 C  CA  C LYS   B 2 148 ? 5.468   -2.694  -20.382 0.25 63.48  ? 157 LYS   B CA  1 
ATOM   1526 C  CA  D LYS   B 2 148 ? 5.468   -2.694  -20.382 0.25 63.48  ? 157 LYS   B CA  1 
ATOM   1527 C  C   A LYS   B 2 148 ? 5.503   -1.653  -21.492 0.25 63.91  ? 157 LYS   B C   1 
ATOM   1528 C  C   B LYS   B 2 148 ? 5.503   -1.653  -21.492 0.25 63.91  ? 157 LYS   B C   1 
ATOM   1529 C  C   C LYS   B 2 148 ? 5.505   -1.642  -21.490 0.25 63.91  ? 157 LYS   B C   1 
ATOM   1530 C  C   D LYS   B 2 148 ? 5.505   -1.642  -21.490 0.25 63.91  ? 157 LYS   B C   1 
ATOM   1531 O  O   A LYS   B 2 148 ? 6.333   -0.748  -21.429 0.25 64.04  ? 157 LYS   B O   1 
ATOM   1532 O  O   B LYS   B 2 148 ? 6.333   -0.748  -21.429 0.25 64.04  ? 157 LYS   B O   1 
ATOM   1533 O  O   C LYS   B 2 148 ? 6.333   -0.734  -21.434 0.25 64.04  ? 157 LYS   B O   1 
ATOM   1534 O  O   D LYS   B 2 148 ? 6.333   -0.734  -21.434 0.25 64.04  ? 157 LYS   B O   1 
ATOM   1535 C  CB  A LYS   B 2 148 ? 6.214   -3.973  -20.905 0.25 65.59  ? 157 LYS   B CB  1 
ATOM   1536 C  CB  B LYS   B 2 148 ? 6.214   -3.973  -20.905 0.25 65.59  ? 157 LYS   B CB  1 
ATOM   1537 C  CB  C LYS   B 2 148 ? 6.275   -3.927  -20.813 0.25 65.58  ? 157 LYS   B CB  1 
ATOM   1538 C  CB  D LYS   B 2 148 ? 6.275   -3.927  -20.813 0.25 65.58  ? 157 LYS   B CB  1 
ATOM   1539 C  CG  A LYS   B 2 148 ? 6.637   -4.931  -19.800 0.25 69.92  ? 157 LYS   B CG  1 
ATOM   1540 C  CG  B LYS   B 2 148 ? 6.637   -4.931  -19.800 0.25 69.92  ? 157 LYS   B CG  1 
ATOM   1541 C  CG  C LYS   B 2 148 ? 6.584   -4.877  -19.664 0.25 69.84  ? 157 LYS   B CG  1 
ATOM   1542 C  CG  D LYS   B 2 148 ? 6.584   -4.877  -19.664 0.25 69.84  ? 157 LYS   B CG  1 
ATOM   1543 C  CD  A LYS   B 2 148 ? 7.251   -6.213  -20.371 0.25 74.37  ? 157 LYS   B CD  1 
ATOM   1544 C  CD  B LYS   B 2 148 ? 7.251   -6.213  -20.371 0.25 74.37  ? 157 LYS   B CD  1 
ATOM   1545 C  CD  C LYS   B 2 148 ? 7.531   -5.996  -20.091 0.25 74.25  ? 157 LYS   B CD  1 
ATOM   1546 C  CD  D LYS   B 2 148 ? 7.531   -5.996  -20.091 0.25 74.25  ? 157 LYS   B CD  1 
ATOM   1547 C  CE  A LYS   B 2 148 ? 8.491   -5.966  -21.202 0.25 78.06  ? 157 LYS   B CE  1 
ATOM   1548 C  CE  B LYS   B 2 148 ? 8.491   -5.966  -21.202 0.25 78.06  ? 157 LYS   B CE  1 
ATOM   1549 C  CE  C LYS   B 2 148 ? 8.906   -5.482  -20.448 0.25 77.91  ? 157 LYS   B CE  1 
ATOM   1550 C  CE  D LYS   B 2 148 ? 8.906   -5.482  -20.448 0.25 77.91  ? 157 LYS   B CE  1 
ATOM   1551 N  NZ  A LYS   B 2 148 ? 9.586   -5.359  -20.399 0.25 80.29  ? 157 LYS   B NZ  1 
ATOM   1552 N  NZ  B LYS   B 2 148 ? 9.586   -5.359  -20.399 0.25 80.29  ? 157 LYS   B NZ  1 
ATOM   1553 N  NZ  C LYS   B 2 148 ? 9.832   -6.587  -20.813 0.25 80.08  ? 157 LYS   B NZ  1 
ATOM   1554 N  NZ  D LYS   B 2 148 ? 9.832   -6.587  -20.813 0.25 80.08  ? 157 LYS   B NZ  1 
ATOM   1555 N  N   . ASN   B 2 149 ? 4.623   -1.753  -22.491 1.00 63.98  ? 158 ASN   B N   1 
ATOM   1556 C  CA  . ASN   B 2 149 ? 4.608   -0.791  -23.597 1.00 64.43  ? 158 ASN   B CA  1 
ATOM   1557 C  C   . ASN   B 2 149 ? 3.816   0.518   -23.316 1.00 63.20  ? 158 ASN   B C   1 
ATOM   1558 O  O   . ASN   B 2 149 ? 3.579   1.305   -24.236 1.00 63.70  ? 158 ASN   B O   1 
ATOM   1559 C  CB  . ASN   B 2 149 ? 4.146   -1.469  -24.898 1.00 67.04  ? 158 ASN   B CB  1 
ATOM   1560 C  CG  . ASN   B 2 149 ? 2.867   -2.271  -24.785 1.00 71.79  ? 158 ASN   B CG  1 
ATOM   1561 O  OD1 . ASN   B 2 149 ? 2.009   -1.999  -23.937 1.00 73.24  ? 158 ASN   B OD1 1 
ATOM   1562 N  ND2 . ASN   B 2 149 ? 2.694   -3.257  -25.669 1.00 72.93  ? 158 ASN   B ND2 1 
ATOM   1563 N  N   . GLY   B 2 150 ? 3.423   0.738   -22.065 1.00 61.43  ? 159 GLY   B N   1 
ATOM   1564 C  CA  . GLY   B 2 150 ? 2.691   1.935   -21.662 1.00 60.05  ? 159 GLY   B CA  1 
ATOM   1565 C  C   . GLY   B 2 150 ? 1.186   1.886   -21.851 1.00 57.79  ? 159 GLY   B C   1 
ATOM   1566 O  O   . GLY   B 2 150 ? 0.470   2.753   -21.330 1.00 57.86  ? 159 GLY   B O   1 
ATOM   1567 N  N   A SER   B 2 151 ? 0.693   0.882   -22.597 0.25 57.15  ? 160 SER   B N   1 
ATOM   1568 N  N   B SER   B 2 151 ? 0.694   0.885   -22.597 0.25 57.09  ? 160 SER   B N   1 
ATOM   1569 N  N   C SER   B 2 151 ? 0.693   0.882   -22.597 0.25 57.15  ? 160 SER   B N   1 
ATOM   1570 N  N   D SER   B 2 151 ? 0.694   0.885   -22.597 0.25 57.09  ? 160 SER   B N   1 
ATOM   1571 C  CA  A SER   B 2 151 ? -0.737  0.720   -22.859 0.25 56.83  ? 160 SER   B CA  1 
ATOM   1572 C  CA  B SER   B 2 151 ? -0.734  0.723   -22.862 0.25 56.77  ? 160 SER   B CA  1 
ATOM   1573 C  CA  C SER   B 2 151 ? -0.737  0.720   -22.859 0.25 56.83  ? 160 SER   B CA  1 
ATOM   1574 C  CA  D SER   B 2 151 ? -0.734  0.723   -22.862 0.25 56.77  ? 160 SER   B CA  1 
ATOM   1575 C  C   A SER   B 2 151 ? -1.517  0.286   -21.612 0.25 56.11  ? 160 SER   B C   1 
ATOM   1576 C  C   B SER   B 2 151 ? -1.518  0.278   -21.620 0.25 56.06  ? 160 SER   B C   1 
ATOM   1577 C  C   C SER   B 2 151 ? -1.517  0.286   -21.612 0.25 56.11  ? 160 SER   B C   1 
ATOM   1578 C  C   D SER   B 2 151 ? -1.518  0.278   -21.620 0.25 56.06  ? 160 SER   B C   1 
ATOM   1579 O  O   A SER   B 2 151 ? -0.949  -0.291  -20.685 0.25 56.09  ? 160 SER   B O   1 
ATOM   1580 O  O   B SER   B 2 151 ? -0.951  -0.312  -20.700 0.25 56.04  ? 160 SER   B O   1 
ATOM   1581 O  O   C SER   B 2 151 ? -0.949  -0.291  -20.685 0.25 56.09  ? 160 SER   B O   1 
ATOM   1582 O  O   D SER   B 2 151 ? -0.951  -0.312  -20.700 0.25 56.04  ? 160 SER   B O   1 
ATOM   1583 C  CB  A SER   B 2 151 ? -0.965  -0.274  -23.994 0.25 58.16  ? 160 SER   B CB  1 
ATOM   1584 C  CB  B SER   B 2 151 ? -0.952  -0.261  -24.006 0.25 57.96  ? 160 SER   B CB  1 
ATOM   1585 C  CB  C SER   B 2 151 ? -0.965  -0.274  -23.994 0.25 58.16  ? 160 SER   B CB  1 
ATOM   1586 C  CB  D SER   B 2 151 ? -0.952  -0.261  -24.006 0.25 57.96  ? 160 SER   B CB  1 
ATOM   1587 O  OG  A SER   B 2 151 ? -2.350  -0.452  -24.248 0.25 60.30  ? 160 SER   B OG  1 
ATOM   1588 O  OG  B SER   B 2 151 ? -0.401  -1.529  -23.695 0.25 59.95  ? 160 SER   B OG  1 
ATOM   1589 O  OG  C SER   B 2 151 ? -2.350  -0.452  -24.248 0.25 60.30  ? 160 SER   B OG  1 
ATOM   1590 O  OG  D SER   B 2 151 ? -0.401  -1.529  -23.695 0.25 59.95  ? 160 SER   B OG  1 
ATOM   1591 N  N   . TYR   B 2 152 ? -2.824  0.561   -21.601 1.00 55.28  ? 161 TYR   B N   1 
ATOM   1592 C  CA  . TYR   B 2 152 ? -3.682  0.210   -20.488 1.00 52.92  ? 161 TYR   B CA  1 
ATOM   1593 C  C   . TYR   B 2 152 ? -4.510  -1.052  -20.742 1.00 49.48  ? 161 TYR   B C   1 
ATOM   1594 O  O   . TYR   B 2 152 ? -5.100  -1.208  -21.801 1.00 49.10  ? 161 TYR   B O   1 
ATOM   1595 C  CB  . TYR   B 2 152 ? -4.619  1.390   -20.221 1.00 53.19  ? 161 TYR   B CB  1 
ATOM   1596 C  CG  . TYR   B 2 152 ? -5.425  1.250   -18.955 1.00 53.88  ? 161 TYR   B CG  1 
ATOM   1597 C  CD1 . TYR   B 2 152 ? -4.864  1.525   -17.718 1.00 54.78  ? 161 TYR   B CD1 1 
ATOM   1598 C  CD2 . TYR   B 2 152 ? -6.765  0.893   -18.998 1.00 54.77  ? 161 TYR   B CD2 1 
ATOM   1599 C  CE1 . TYR   B 2 152 ? -5.606  1.415   -16.550 1.00 55.56  ? 161 TYR   B CE1 1 
ATOM   1600 C  CE2 . TYR   B 2 152 ? -7.515  0.772   -17.837 1.00 55.81  ? 161 TYR   B CE2 1 
ATOM   1601 C  CZ  . TYR   B 2 152 ? -6.931  1.034   -16.615 1.00 56.61  ? 161 TYR   B CZ  1 
ATOM   1602 O  OH  . TYR   B 2 152 ? -7.677  0.956   -15.470 1.00 58.84  ? 161 TYR   B OH  1 
ATOM   1603 N  N   . VAL   B 2 153 ? -4.595  -1.925  -19.741 1.00 46.83  ? 162 VAL   B N   1 
ATOM   1604 C  CA  . VAL   B 2 153 ? -5.387  -3.152  -19.791 1.00 44.52  ? 162 VAL   B CA  1 
ATOM   1605 C  C   . VAL   B 2 153 ? -6.328  -3.170  -18.574 1.00 41.84  ? 162 VAL   B C   1 
ATOM   1606 O  O   . VAL   B 2 153 ? -5.874  -3.301  -17.448 1.00 41.38  ? 162 VAL   B O   1 
ATOM   1607 C  CB  . VAL   B 2 153 ? -4.487  -4.414  -19.872 1.00 44.84  ? 162 VAL   B CB  1 
ATOM   1608 C  CG1 . VAL   B 2 153 ? -5.316  -5.696  -19.828 1.00 44.80  ? 162 VAL   B CG1 1 
ATOM   1609 C  CG2 . VAL   B 2 153 ? -3.633  -4.374  -21.135 1.00 45.60  ? 162 VAL   B CG2 1 
ATOM   1610 N  N   . SER   B 2 154 ? -7.621  -2.984  -18.806 1.00 39.83  ? 163 SER   B N   1 
ATOM   1611 C  CA  . SER   B 2 154 ? -8.634  -2.970  -17.756 1.00 38.61  ? 163 SER   B CA  1 
ATOM   1612 C  C   . SER   B 2 154 ? -9.168  -4.365  -17.506 1.00 36.64  ? 163 SER   B C   1 
ATOM   1613 O  O   . SER   B 2 154 ? -9.230  -5.154  -18.429 1.00 36.19  ? 163 SER   B O   1 
ATOM   1614 C  CB  . SER   B 2 154 ? -9.805  -2.077  -18.177 1.00 39.97  ? 163 SER   B CB  1 
ATOM   1615 O  OG  . SER   B 2 154 ? -11.020 -2.382  -17.499 1.00 41.26  ? 163 SER   B OG  1 
ATOM   1616 N  N   . ALA   B 2 155 ? -9.667  -4.629  -16.300 1.00 35.03  ? 164 ALA   B N   1 
ATOM   1617 C  CA  . ALA   B 2 155 ? -10.308 -5.906  -16.006 1.00 34.26  ? 164 ALA   B CA  1 
ATOM   1618 C  C   . ALA   B 2 155 ? -11.795 -5.829  -16.403 1.00 33.54  ? 164 ALA   B C   1 
ATOM   1619 O  O   . ALA   B 2 155 ? -12.354 -4.730  -16.534 1.00 33.54  ? 164 ALA   B O   1 
ATOM   1620 C  CB  . ALA   B 2 155 ? -10.197 -6.208  -14.521 1.00 34.41  ? 164 ALA   B CB  1 
ATOM   1621 N  N   . ILE   B 2 156 ? -12.437 -6.991  -16.610 1.00 32.46  ? 165 ILE   B N   1 
ATOM   1622 C  CA  . ILE   B 2 156 ? -13.874 -7.018  -16.817 1.00 31.86  ? 165 ILE   B CA  1 
ATOM   1623 C  C   . ILE   B 2 156 ? -14.389 -7.124  -15.363 1.00 31.23  ? 165 ILE   B C   1 
ATOM   1624 O  O   . ILE   B 2 156 ? -14.326 -8.204  -14.772 1.00 30.59  ? 165 ILE   B O   1 
ATOM   1625 C  CB  . ILE   B 2 156 ? -14.338 -8.207  -17.676 1.00 32.36  ? 165 ILE   B CB  1 
ATOM   1626 C  CG1 . ILE   B 2 156 ? -13.607 -8.239  -19.034 1.00 34.30  ? 165 ILE   B CG1 1 
ATOM   1627 C  CG2 . ILE   B 2 156 ? -15.848 -8.144  -17.870 1.00 32.52  ? 165 ILE   B CG2 1 
ATOM   1628 C  CD1 . ILE   B 2 156 ? -13.898 -9.482  -19.890 1.00 35.58  ? 165 ILE   B CD1 1 
ATOM   1629 N  N   . THR   B 2 157 ? -14.792 -5.983  -14.757 1.00 30.92  ? 166 THR   B N   1 
ATOM   1630 C  CA  . THR   B 2 157 ? -15.226 -5.968  -13.356 1.00 30.58  ? 166 THR   B CA  1 
ATOM   1631 C  C   . THR   B 2 157 ? -16.712 -6.204  -13.226 1.00 30.18  ? 166 THR   B C   1 
ATOM   1632 O  O   . THR   B 2 157 ? -17.481 -5.355  -13.656 1.00 30.28  ? 166 THR   B O   1 
ATOM   1633 C  CB  . THR   B 2 157 ? -14.881 -4.636  -12.681 1.00 31.54  ? 166 THR   B CB  1 
ATOM   1634 O  OG1 . THR   B 2 157 ? -13.470 -4.388  -12.732 1.00 32.73  ? 166 THR   B OG1 1 
ATOM   1635 C  CG2 . THR   B 2 157 ? -15.329 -4.608  -11.250 1.00 31.21  ? 166 THR   B CG2 1 
ATOM   1636 N  N   . GLN   B 2 158 ? -17.127 -7.306  -12.591 1.00 29.48  ? 167 GLN   B N   1 
ATOM   1637 C  CA  . GLN   B 2 158 ? -18.548 -7.582  -12.412 1.00 30.00  ? 167 GLN   B CA  1 
ATOM   1638 C  C   . GLN   B 2 158 ? -18.927 -7.731  -10.916 1.00 32.61  ? 167 GLN   B C   1 
ATOM   1639 O  O   . GLN   B 2 158 ? -18.123 -8.184  -10.127 1.00 32.29  ? 167 GLN   B O   1 
ATOM   1640 C  CB  . GLN   B 2 158 ? -18.945 -8.815  -13.236 1.00 28.91  ? 167 GLN   B CB  1 
ATOM   1641 C  CG  . GLN   B 2 158 ? -20.407 -9.232  -13.147 1.00 29.26  ? 167 GLN   B CG  1 
ATOM   1642 C  CD  . GLN   B 2 158 ? -21.368 -8.220  -13.736 1.00 31.79  ? 167 GLN   B CD  1 
ATOM   1643 O  OE1 . GLN   B 2 158 ? -21.436 -7.068  -13.287 1.00 32.44  ? 167 GLN   B OE1 1 
ATOM   1644 N  NE2 . GLN   B 2 158 ? -22.165 -8.639  -14.718 1.00 30.83  ? 167 GLN   B NE2 1 
ATOM   1645 N  N   . GLY   B 2 159 ? -20.134 -7.324  -10.549 1.00 35.20  ? 168 GLY   B N   1 
ATOM   1646 C  CA  . GLY   B 2 159 ? -20.652 -7.462  -9.198  1.00 38.28  ? 168 GLY   B CA  1 
ATOM   1647 C  C   . GLY   B 2 159 ? -21.417 -8.758  -9.006  1.00 42.21  ? 168 GLY   B C   1 
ATOM   1648 O  O   . GLY   B 2 159 ? -21.498 -9.583  -9.915  1.00 42.48  ? 168 GLY   B O   1 
ATOM   1649 N  N   . LYS   B 2 160 ? -21.977 -8.963  -7.816  1.00 45.24  ? 169 LYS   B N   1 
ATOM   1650 C  CA  . LYS   B 2 160 ? -22.732 -10.181 -7.516  1.00 48.29  ? 169 LYS   B CA  1 
ATOM   1651 C  C   . LYS   B 2 160 ? -24.208 -9.865  -7.238  1.00 51.00  ? 169 LYS   B C   1 
ATOM   1652 O  O   . LYS   B 2 160 ? -24.510 -9.248  -6.214  1.00 51.73  ? 169 LYS   B O   1 
ATOM   1653 C  CB  . LYS   B 2 160 ? -22.110 -10.926 -6.310  1.00 49.95  ? 169 LYS   B CB  1 
ATOM   1654 C  CG  . LYS   B 2 160 ? -22.873 -12.181 -5.898  1.00 54.47  ? 169 LYS   B CG  1 
ATOM   1655 C  CD  . LYS   B 2 160 ? -22.585 -12.560 -4.452  1.00 59.39  ? 169 LYS   B CD  1 
ATOM   1656 C  CE  . LYS   B 2 160 ? -23.601 -13.523 -3.876  1.00 63.07  ? 169 LYS   B CE  1 
ATOM   1657 N  NZ  . LYS   B 2 160 ? -23.568 -13.528 -2.381  1.00 64.94  ? 169 LYS   B NZ  1 
ATOM   1658 N  N   . ARG   B 2 161 ? -25.124 -10.320 -8.113  1.00 52.10  ? 170 ARG   B N   1 
ATOM   1659 C  CA  . ARG   B 2 161 ? -26.558 -10.116 -7.899  1.00 53.93  ? 170 ARG   B CA  1 
ATOM   1660 C  C   . ARG   B 2 161 ? -27.066 -11.106 -6.817  1.00 56.14  ? 170 ARG   B C   1 
ATOM   1661 O  O   . ARG   B 2 161 ? -26.702 -12.286 -6.843  1.00 56.67  ? 170 ARG   B O   1 
ATOM   1662 C  CB  . ARG   B 2 161 ? -27.320 -10.289 -9.222  1.00 54.55  ? 170 ARG   B CB  1 
ATOM   1663 C  CG  . ARG   B 2 161 ? -28.821 -10.135 -9.118  1.00 57.05  ? 170 ARG   B CG  1 
ATOM   1664 C  CD  . ARG   B 2 161 ? -29.495 -10.322 -10.467 1.00 60.66  ? 170 ARG   B CD  1 
ATOM   1665 N  NE  . ARG   B 2 161 ? -30.953 -10.262 -10.354 1.00 64.09  ? 170 ARG   B NE  1 
ATOM   1666 C  CZ  . ARG   B 2 161 ? -31.724 -9.361  -10.959 1.00 65.97  ? 170 ARG   B CZ  1 
ATOM   1667 N  NH1 . ARG   B 2 161 ? -31.188 -8.443  -11.751 1.00 64.82  ? 170 ARG   B NH1 1 
ATOM   1668 N  NH2 . ARG   B 2 161 ? -33.038 -9.378  -10.781 1.00 66.37  ? 170 ARG   B NH2 1 
ATOM   1669 N  N   . GLU   B 2 162 ? -27.858 -10.619 -5.843  1.00 56.97  ? 171 GLU   B N   1 
ATOM   1670 C  CA  . GLU   B 2 162 ? -28.373 -11.466 -4.766  1.00 58.25  ? 171 GLU   B CA  1 
ATOM   1671 C  C   . GLU   B 2 162 ? -29.528 -12.351 -5.249  1.00 59.05  ? 171 GLU   B C   1 
ATOM   1672 O  O   . GLU   B 2 162 ? -30.337 -12.808 -4.440  1.00 59.47  ? 171 GLU   B O   1 
ATOM   1673 C  CB  . GLU   B 2 162 ? -28.832 -10.612 -3.576  1.00 61.18  ? 171 GLU   B CB  1 
ATOM   1674 C  CG  . GLU   B 2 162 ? -27.791 -9.619  -3.087  1.00 67.47  ? 171 GLU   B CG  1 
ATOM   1675 C  CD  . GLU   B 2 162 ? -26.560 -10.229 -2.442  1.00 75.39  ? 171 GLU   B CD  1 
ATOM   1676 O  OE1 . GLU   B 2 162 ? -26.711 -10.949 -1.427  1.00 76.77  ? 171 GLU   B OE1 1 
ATOM   1677 O  OE2 . GLU   B 2 162 ? -25.441 -9.971  -2.944  1.00 77.88  ? 171 GLU   B OE2 1 
HETATM 1678 S  S   . DMS   C 3 .   ? -18.513 11.477  -0.175  1.00 66.43  ? 201 DMS   B S   1 
HETATM 1679 O  O   . DMS   C 3 .   ? -19.197 10.140  -0.315  1.00 66.27  ? 201 DMS   B O   1 
HETATM 1680 C  C1  . DMS   C 3 .   ? -19.592 12.768  -0.842  1.00 66.52  ? 201 DMS   B C1  1 
HETATM 1681 C  C2  . DMS   C 3 .   ? -17.274 11.672  -1.486  1.00 66.18  ? 201 DMS   B C2  1 
HETATM 1682 S  S   A DMS   D 3 .   ? -6.855  2.292   -13.097 0.15 76.85  ? 202 DMS   B S   1 
HETATM 1683 S  S   B DMS   D 3 .   ? -6.855  2.292   -13.097 0.15 76.85  ? 202 DMS   B S   1 
HETATM 1684 O  O   A DMS   D 3 .   ? -6.999  0.925   -12.507 0.15 76.87  ? 202 DMS   B O   1 
HETATM 1685 O  O   B DMS   D 3 .   ? -6.999  0.925   -12.507 0.15 76.87  ? 202 DMS   B O   1 
HETATM 1686 C  C1  A DMS   D 3 .   ? -7.293  3.486   -11.801 0.15 76.83  ? 202 DMS   B C1  1 
HETATM 1687 C  C1  B DMS   D 3 .   ? -7.293  3.486   -11.801 0.15 76.83  ? 202 DMS   B C1  1 
HETATM 1688 C  C2  A DMS   D 3 .   ? -5.086  2.692   -13.125 0.15 76.83  ? 202 DMS   B C2  1 
HETATM 1689 C  C2  B DMS   D 3 .   ? -5.086  2.692   -13.125 0.15 76.83  ? 202 DMS   B C2  1 
HETATM 1690 N  N1  . A1BXF E 4 .   ? -4.989  5.125   -16.805 0.86 73.07  ? 203 A1BXF B N1  1 
HETATM 1691 C  C4  . A1BXF E 4 .   ? -5.968  4.869   -19.425 0.86 74.15  ? 203 A1BXF B C4  1 
HETATM 1692 C  C5  . A1BXF E 4 .   ? -6.862  4.734   -18.320 0.86 72.25  ? 203 A1BXF B C5  1 
HETATM 1693 C  C6  . A1BXF E 4 .   ? -8.234  4.446   -18.462 0.86 69.67  ? 203 A1BXF B C6  1 
HETATM 1694 C  C7  . A1BXF E 4 .   ? -9.038  4.317   -17.365 0.86 68.77  ? 203 A1BXF B C7  1 
HETATM 1695 C  C8  . A1BXF E 4 .   ? -8.513  4.473   -16.093 0.86 70.11  ? 203 A1BXF B C8  1 
HETATM 1696 C  C10 . A1BXF E 4 .   ? -6.320  4.877   -17.021 0.86 72.41  ? 203 A1BXF B C10 1 
HETATM 1697 C  C1  . A1BXF E 4 .   ? -2.739  5.533   -17.568 0.86 77.24  ? 203 A1BXF B C1  1 
HETATM 1698 C  C2  . A1BXF E 4 .   ? -4.183  5.244   -17.848 0.86 74.78  ? 203 A1BXF B C2  1 
HETATM 1699 C  C3  . A1BXF E 4 .   ? -4.638  5.120   -19.175 0.86 75.32  ? 203 A1BXF B C3  1 
HETATM 1700 C  C9  . A1BXF E 4 .   ? -7.177  4.739   -15.899 0.86 71.94  ? 203 A1BXF B C9  1 
HETATM 1701 CL CL1 . A1BXF E 4 .   ? -6.556  4.907   -14.286 0.86 72.88  ? 203 A1BXF B CL1 1 
HETATM 1702 CL CL2 . A1BXF E 4 .   ? -9.568  4.323   -14.724 0.86 74.70  ? 203 A1BXF B CL2 1 
HETATM 1703 N  N2  . A1BXF E 4 .   ? -6.441  4.754   -20.712 0.86 74.78  ? 203 A1BXF B N2  1 
HETATM 1704 S  S   C SO4   F 5 .   ? -13.990 20.401  -20.504 0.50 134.26 ? 204 SO4   B S   1 
HETATM 1705 S  S   D SO4   F 5 .   ? -13.990 20.401  -20.504 0.50 134.26 ? 204 SO4   B S   1 
HETATM 1706 O  O1  C SO4   F 5 .   ? -13.881 21.810  -20.106 0.50 134.27 ? 204 SO4   B O1  1 
HETATM 1707 O  O1  D SO4   F 5 .   ? -13.881 21.810  -20.106 0.50 134.27 ? 204 SO4   B O1  1 
HETATM 1708 O  O2  C SO4   F 5 .   ? -14.201 19.560  -19.319 0.50 134.28 ? 204 SO4   B O2  1 
HETATM 1709 O  O2  D SO4   F 5 .   ? -14.201 19.560  -19.319 0.50 134.28 ? 204 SO4   B O2  1 
HETATM 1710 O  O3  C SO4   F 5 .   ? -15.139 20.243  -21.416 0.50 134.26 ? 204 SO4   B O3  1 
HETATM 1711 O  O3  D SO4   F 5 .   ? -15.139 20.243  -21.416 0.50 134.26 ? 204 SO4   B O3  1 
HETATM 1712 O  O4  C SO4   F 5 .   ? -12.757 19.967  -21.189 0.50 134.25 ? 204 SO4   B O4  1 
HETATM 1713 O  O4  D SO4   F 5 .   ? -12.757 19.967  -21.189 0.50 134.25 ? 204 SO4   B O4  1 
HETATM 1714 S  S   C SO4   G 5 .   ? -8.412  -15.953 -24.038 0.50 102.96 ? 205 SO4   B S   1 
HETATM 1715 S  S   D SO4   G 5 .   ? -8.412  -15.953 -24.038 0.50 102.96 ? 205 SO4   B S   1 
HETATM 1716 O  O1  C SO4   G 5 .   ? -8.174  -14.568 -24.455 0.50 102.95 ? 205 SO4   B O1  1 
HETATM 1717 O  O1  D SO4   G 5 .   ? -8.174  -14.568 -24.455 0.50 102.95 ? 205 SO4   B O1  1 
HETATM 1718 O  O2  C SO4   G 5 .   ? -8.079  -16.106 -22.617 0.50 103.09 ? 205 SO4   B O2  1 
HETATM 1719 O  O2  D SO4   G 5 .   ? -8.079  -16.106 -22.617 0.50 103.09 ? 205 SO4   B O2  1 
HETATM 1720 O  O3  C SO4   G 5 .   ? -9.834  -16.298 -24.245 0.50 102.87 ? 205 SO4   B O3  1 
HETATM 1721 O  O3  D SO4   G 5 .   ? -9.834  -16.298 -24.245 0.50 102.87 ? 205 SO4   B O3  1 
HETATM 1722 O  O4  C SO4   G 5 .   ? -7.564  -16.846 -24.857 0.50 103.01 ? 205 SO4   B O4  1 
HETATM 1723 O  O4  D SO4   G 5 .   ? -7.564  -16.846 -24.857 0.50 103.01 ? 205 SO4   B O4  1 
HETATM 1724 S  S   C DMS   H 3 .   ? -22.181 -15.457 -25.732 0.50 93.69  ? 206 DMS   B S   1 
HETATM 1725 S  S   D DMS   H 3 .   ? -22.181 -15.457 -25.732 0.50 93.69  ? 206 DMS   B S   1 
HETATM 1726 O  O   C DMS   H 3 .   ? -21.305 -14.252 -25.931 0.50 93.62  ? 206 DMS   B O   1 
HETATM 1727 O  O   D DMS   H 3 .   ? -21.305 -14.252 -25.931 0.50 93.62  ? 206 DMS   B O   1 
HETATM 1728 C  C1  C DMS   H 3 .   ? -22.154 -16.435 -27.262 0.50 93.78  ? 206 DMS   B C1  1 
HETATM 1729 C  C1  D DMS   H 3 .   ? -22.154 -16.435 -27.262 0.50 93.78  ? 206 DMS   B C1  1 
HETATM 1730 C  C2  C DMS   H 3 .   ? -23.908 -14.933 -25.892 0.50 93.75  ? 206 DMS   B C2  1 
HETATM 1731 C  C2  D DMS   H 3 .   ? -23.908 -14.933 -25.892 0.50 93.75  ? 206 DMS   B C2  1 
HETATM 1732 O  O   A HOH   I 6 .   ? -28.723 14.968  -15.385 0.50 39.86  ? 101 HOH   A O   1 
HETATM 1733 O  O   B HOH   I 6 .   ? -28.723 14.968  -15.385 0.50 39.86  ? 102 HOH   A O   1 
HETATM 1734 O  O   . HOH   I 6 .   ? -0.653  -15.044 -9.757  1.00 39.93  ? 103 HOH   A O   1 
HETATM 1735 O  O   . HOH   I 6 .   ? -24.761 20.745  -3.658  1.00 54.16  ? 104 HOH   A O   1 
HETATM 1736 O  O   . HOH   I 6 .   ? -1.385  -3.822  -5.837  1.00 31.45  ? 105 HOH   A O   1 
HETATM 1737 O  O   . HOH   I 6 .   ? -8.088  1.582   1.390   1.00 43.48  ? 106 HOH   A O   1 
HETATM 1738 O  O   . HOH   I 6 .   ? -15.206 2.648   -34.230 1.00 55.93  ? 107 HOH   A O   1 
HETATM 1739 O  O   . HOH   I 6 .   ? -8.952  -7.345  -25.329 1.00 42.79  ? 108 HOH   A O   1 
HETATM 1740 O  O   . HOH   I 6 .   ? -4.005  -15.009 -25.321 1.00 25.17  ? 109 HOH   A O   1 
HETATM 1741 O  O   . HOH   I 6 .   ? -25.981 0.565   -29.380 1.00 38.40  ? 110 HOH   A O   1 
HETATM 1742 O  O   . HOH   I 6 .   ? -2.622  -12.118 -6.842  1.00 24.74  ? 111 HOH   A O   1 
HETATM 1743 O  O   . HOH   I 6 .   ? -27.952 -7.002  -28.348 1.00 52.07  ? 112 HOH   A O   1 
HETATM 1744 O  O   C HOH   I 6 .   ? -22.074 -1.120  -37.772 0.25 24.93  ? 113 HOH   A O   1 
HETATM 1745 O  O   D HOH   I 6 .   ? -22.074 -1.120  -37.772 0.25 24.93  ? 114 HOH   A O   1 
HETATM 1746 O  O   . HOH   I 6 .   ? -28.743 0.750   -30.233 1.00 53.96  ? 115 HOH   A O   1 
HETATM 1747 O  O   . HOH   I 6 .   ? -6.791  -9.778  -2.941  1.00 36.30  ? 116 HOH   A O   1 
HETATM 1748 O  O   . HOH   I 6 .   ? -24.520 1.120   -35.471 1.00 40.37  ? 117 HOH   A O   1 
HETATM 1749 O  O   . HOH   I 6 .   ? 2.538   -10.046 -15.105 1.00 76.93  ? 118 HOH   A O   1 
HETATM 1750 O  O   . HOH   I 6 .   ? -21.400 -9.066  -34.982 1.00 30.50  ? 119 HOH   A O   1 
HETATM 1751 O  O   . HOH   I 6 .   ? -4.440  -10.806 -5.439  1.00 30.61  ? 120 HOH   A O   1 
HETATM 1752 O  O   . HOH   I 6 .   ? -4.247  -1.418  -0.011  1.00 40.43  ? 121 HOH   A O   1 
HETATM 1753 O  O   . HOH   I 6 .   ? -9.155  2.720   -6.908  1.00 43.82  ? 122 HOH   A O   1 
HETATM 1754 O  O   . HOH   I 6 .   ? -2.235  -8.738  -2.936  1.00 41.17  ? 123 HOH   A O   1 
HETATM 1755 O  O   . HOH   I 6 .   ? -6.610  -7.165  0.796   1.00 45.36  ? 124 HOH   A O   1 
HETATM 1756 O  O   . HOH   J 6 .   ? -25.696 -8.445  -16.661 1.00 25.03  ? 301 HOH   B O   1 
HETATM 1757 O  O   . HOH   J 6 .   ? -22.694 -11.616 -10.848 1.00 43.41  ? 302 HOH   B O   1 
HETATM 1758 O  O   . HOH   J 6 .   ? -17.781 -11.072 -16.392 1.00 33.90  ? 303 HOH   B O   1 
HETATM 1759 O  O   . HOH   J 6 .   ? -12.506 -2.819  -14.758 1.00 29.24  ? 304 HOH   B O   1 
HETATM 1760 O  O   . HOH   J 6 .   ? -20.048 -8.464  -5.317  1.00 41.47  ? 305 HOH   B O   1 
HETATM 1761 O  O   . HOH   J 6 .   ? -6.217  -0.871  -10.702 1.00 29.33  ? 306 HOH   B O   1 
HETATM 1762 O  O   . HOH   J 6 .   ? -12.242 -3.668  -10.065 1.00 34.37  ? 307 HOH   B O   1 
HETATM 1763 O  O   . HOH   J 6 .   ? -12.107 13.199  -18.118 1.00 45.86  ? 308 HOH   B O   1 
HETATM 1764 O  O   . HOH   J 6 .   ? -18.310 14.706  -22.242 1.00 22.19  ? 309 HOH   B O   1 
HETATM 1765 O  O   . HOH   J 6 .   ? -27.548 19.564  -15.543 1.00 51.41  ? 310 HOH   B O   1 
HETATM 1766 O  O   . HOH   J 6 .   ? -19.278 -6.336  -0.810  1.00 40.85  ? 311 HOH   B O   1 
HETATM 1767 O  O   . HOH   J 6 .   ? -31.704 6.645   -4.716  1.00 47.87  ? 312 HOH   B O   1 
HETATM 1768 O  O   . HOH   J 6 .   ? -15.832 -15.470 -16.422 1.00 42.65  ? 313 HOH   B O   1 
HETATM 1769 O  O   . HOH   J 6 .   ? -17.995 24.858  -14.045 1.00 57.40  ? 314 HOH   B O   1 
HETATM 1770 O  O   . HOH   J 6 .   ? -15.119 -9.283  -11.854 1.00 36.92  ? 315 HOH   B O   1 
HETATM 1771 O  O   . HOH   J 6 .   ? -21.698 -14.672 -21.950 1.00 35.78  ? 316 HOH   B O   1 
HETATM 1772 O  O   . HOH   J 6 .   ? -29.315 -2.248  -19.243 1.00 32.53  ? 317 HOH   B O   1 
HETATM 1773 O  O   . HOH   J 6 .   ? -19.313 -14.214 -22.970 1.00 30.89  ? 318 HOH   B O   1 
HETATM 1774 O  O   . HOH   J 6 .   ? -14.725 -5.818  1.071   1.00 34.06  ? 319 HOH   B O   1 
HETATM 1775 O  O   . HOH   J 6 .   ? -21.244 6.420   -0.002  0.50 30.22  ? 320 HOH   B O   1 
HETATM 1776 O  O   . HOH   J 6 .   ? -30.468 -5.861  -1.384  1.00 26.59  ? 321 HOH   B O   1 
HETATM 1777 O  O   . HOH   J 6 .   ? -2.199  -3.468  -25.054 1.00 47.71  ? 322 HOH   B O   1 
HETATM 1778 O  O   . HOH   J 6 .   ? -11.808 9.914   -10.317 1.00 43.05  ? 323 HOH   B O   1 
HETATM 1779 O  O   C HOH   J 6 .   ? -18.641 -11.122 -9.942  0.50 40.14  ? 324 HOH   B O   1 
HETATM 1780 O  O   D HOH   J 6 .   ? -18.641 -11.122 -9.942  0.50 40.14  ? 325 HOH   B O   1 
HETATM 1781 O  O   . HOH   J 6 .   ? -8.726  1.980   -8.654  1.00 41.53  ? 326 HOH   B O   1 
HETATM 1782 O  O   . HOH   J 6 .   ? -21.446 -12.310 -13.132 1.00 39.10  ? 327 HOH   B O   1 
HETATM 1783 O  O   . HOH   J 6 .   ? -7.888  -19.308 -6.678  1.00 39.28  ? 328 HOH   B O   1 
HETATM 1784 O  O   . HOH   J 6 .   ? -15.629 -15.174 -30.736 1.00 37.11  ? 329 HOH   B O   1 
HETATM 1785 O  O   . HOH   J 6 .   ? -17.212 14.053  -30.934 1.00 44.06  ? 330 HOH   B O   1 
HETATM 1786 O  O   . HOH   J 6 .   ? -14.923 -7.145  -1.413  1.00 31.07  ? 331 HOH   B O   1 
HETATM 1787 O  O   A HOH   J 6 .   ? -16.421 25.737  -11.954 0.50 52.27  ? 332 HOH   B O   1 
HETATM 1788 O  O   B HOH   J 6 .   ? -16.421 25.737  -11.954 0.50 52.27  ? 333 HOH   B O   1 
HETATM 1789 O  O   . HOH   J 6 .   ? -11.308 -5.286  -8.339  1.00 47.81  ? 334 HOH   B O   1 
HETATM 1790 O  O   . HOH   J 6 .   ? -10.288 11.636  -19.192 1.00 30.73  ? 335 HOH   B O   1 
HETATM 1791 O  O   . HOH   J 6 .   ? -25.576 -5.679  -4.286  1.00 25.23  ? 336 HOH   B O   1 
HETATM 1792 O  O   . HOH   J 6 .   ? -6.416  -10.478 -0.277  1.00 34.28  ? 337 HOH   B O   1 
HETATM 1793 O  O   . HOH   J 6 .   ? 0.362   -0.262  -13.375 1.00 45.10  ? 338 HOH   B O   1 
HETATM 1794 O  O   . HOH   J 6 .   ? -7.179  -10.976 -5.634  1.00 51.83  ? 339 HOH   B O   1 
HETATM 1795 O  O   . HOH   J 6 .   ? -9.042  1.533   -29.413 1.00 47.27  ? 340 HOH   B O   1 
HETATM 1796 O  O   . HOH   J 6 .   ? -14.644 15.884  -20.613 1.00 54.55  ? 341 HOH   B O   1 
HETATM 1797 O  O   . HOH   J 6 .   ? -14.603 -13.050 -16.549 1.00 33.36  ? 342 HOH   B O   1 
HETATM 1798 O  O   . HOH   J 6 .   ? -17.139 16.870  -21.732 1.00 26.29  ? 343 HOH   B O   1 
HETATM 1799 O  O   . HOH   J 6 .   ? -6.306  6.959   -23.681 1.00 39.34  ? 344 HOH   B O   1 
HETATM 1800 O  O   . HOH   J 6 .   ? -9.832  -11.265 -7.839  1.00 43.15  ? 345 HOH   B O   1 
HETATM 1801 O  O   . HOH   J 6 .   ? -9.277  -6.537  1.609   1.00 62.62  ? 346 HOH   B O   1 
HETATM 1802 O  O   . HOH   J 6 .   ? -10.775 7.722   -13.593 1.00 28.39  ? 347 HOH   B O   1 
HETATM 1803 O  O   . HOH   J 6 .   ? -30.875 -11.389 -27.281 0.50 64.02  ? 348 HOH   B O   1 
HETATM 1804 O  O   C HOH   J 6 .   ? -35.414 1.670   -7.659  0.50 39.89  ? 349 HOH   B O   1 
HETATM 1805 O  O   D HOH   J 6 .   ? -35.414 1.670   -7.659  0.50 39.89  ? 350 HOH   B O   1 
HETATM 1806 O  O   . HOH   J 6 .   ? -11.197 -8.371  2.019   1.00 40.07  ? 351 HOH   B O   1 
HETATM 1807 O  O   . HOH   J 6 .   ? -31.251 -7.901  -6.824  1.00 48.38  ? 352 HOH   B O   1 
HETATM 1808 O  O   . HOH   J 6 .   ? -19.514 6.470   -33.172 1.00 49.46  ? 353 HOH   B O   1 
HETATM 1809 O  O   . HOH   J 6 .   ? -5.876  -1.211  -28.737 1.00 45.63  ? 354 HOH   B O   1 
HETATM 1810 O  O   . HOH   J 6 .   ? -35.277 -12.441 -9.996  1.00 44.49  ? 355 HOH   B O   1 
HETATM 1811 O  O   A HOH   J 6 .   ? -21.047 15.881  -23.421 0.50 45.05  ? 356 HOH   B O   1 
HETATM 1812 O  O   B HOH   J 6 .   ? -21.047 15.881  -23.421 0.50 45.05  ? 357 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 1.0477 0.2375 0.5894 0.3052 0.0433  -0.1527 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 1.0225 0.2928 0.5654 0.3306 0.0533  -0.1369 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.9849 0.2814 0.5441 0.3195 0.0585  -0.0911 50  ASP   A C   
4    O  O   . ASP   A 7   ? 1.0093 0.2518 0.5701 0.3212 0.0588  -0.0664 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.0722 0.3347 0.6044 0.3823 0.0583  -0.1513 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.1522 0.4771 0.6727 0.4028 0.0647  -0.1819 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.1914 0.4869 0.6957 0.4353 0.0657  -0.2139 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.1550 0.5567 0.6810 0.3881 0.0701  -0.1728 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.9262 0.3029 0.4941 0.3097 0.0628  -0.0800 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.8943 0.3034 0.4746 0.3016 0.0668  -0.0428 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.8635 0.3030 0.4460 0.3392 0.0704  -0.0311 51  MET   A C   
12   O  O   . MET   A 8   ? 0.8479 0.3173 0.4303 0.3652 0.0733  -0.0516 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.8763 0.3526 0.4667 0.2740 0.0682  -0.0384 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.9106 0.3685 0.5081 0.2349 0.0634  -0.0395 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.9510 0.4885 0.5582 0.2121 0.0628  -0.0392 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.9605 0.4711 0.5814 0.1717 0.0537  -0.0480 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.8470 0.2855 0.4324 0.3424 0.0702  0.0015  52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.8280 0.3010 0.4185 0.3766 0.0690  0.0134  52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.8053 0.3252 0.4019 0.3656 0.0682  0.0403  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.8145 0.3229 0.4066 0.3365 0.0704  0.0563  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.8527 0.2627 0.4314 0.4116 0.0645  0.0200  52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.8988 0.2398 0.4613 0.4004 0.0635  0.0506  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.9452 0.2074 0.4994 0.3797 0.0654  0.0461  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.9131 0.2650 0.4672 0.4127 0.0607  0.0837  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.9915 0.1878 0.5332 0.3677 0.0682  0.0780  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.9543 0.2419 0.4879 0.4050 0.0633  0.1160  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 1.0016 0.2102 0.5306 0.3817 0.0687  0.1151  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.0591 0.2038 0.5708 0.3701 0.0750  0.1508  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.7741 0.3497 0.3833 0.3890 0.0648  0.0428  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.7564 0.3759 0.3698 0.3818 0.0610  0.0624  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.7709 0.3785 0.3731 0.4132 0.0511  0.0828  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.7753 0.3720 0.3801 0.4482 0.0457  0.0771  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.7190 0.4172 0.3581 0.3745 0.0627  0.0494  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.7025 0.4386 0.3633 0.4045 0.0624  0.0324  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.7210 0.4280 0.3622 0.3422 0.0712  0.0384  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.6764 0.4904 0.3679 0.3969 0.0642  0.0260  53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.7742 0.3845 0.3612 0.4034 0.0484  0.1063  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.7921 0.3950 0.3590 0.4322 0.0376  0.1290  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.7704 0.4357 0.3396 0.4248 0.0308  0.1334  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.7645 0.4367 0.3299 0.3941 0.0392  0.1371  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.8620 0.3866 0.3939 0.4276 0.0440  0.1582  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.9608 0.4118 0.4827 0.4502 0.0439  0.1605  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.1026 0.4712 0.5913 0.4445 0.0515  0.1943  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.1292 0.5043 0.6001 0.4252 0.0583  0.2187  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.1640 0.4599 0.6446 0.4595 0.0521  0.1968  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.7541 0.4652 0.3309 0.4534 0.0144  0.1307  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.7352 0.5030 0.3147 0.4466 0.0048  0.1291  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.7623 0.5033 0.2981 0.4405 0.0071  0.1547  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.7935 0.4844 0.2941 0.4587 0.0075  0.1798  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.7154 0.5393 0.3150 0.4785 -0.0168 0.1185  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.6996 0.5938 0.3305 0.4602 -0.0241 0.0985  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.6805 0.6380 0.3438 0.4864 -0.0463 0.0837  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.6643 0.6808 0.3551 0.4662 -0.0557 0.0654  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.6744 0.7053 0.3412 0.4685 -0.0720 0.0668  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.7157 0.7101 0.3270 0.4906 -0.0786 0.0892  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.6174 0.6957 0.3124 0.4486 -0.0809 0.0460  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.7465 0.5192 0.2833 0.4162 0.0103  0.1495  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.7618 0.5191 0.2576 0.4108 0.0156  0.1712  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.7426 0.5519 0.2280 0.4202 -0.0003 0.1627  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.7574 0.5588 0.2035 0.4208 0.0042  0.1790  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.7686 0.5055 0.2675 0.3741 0.0375  0.1751  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.7114 0.5733 0.2315 0.4274 -0.0182 0.1368  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.6984 0.6083 0.2125 0.4356 -0.0377 0.1231  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.6645 0.6277 0.2305 0.4186 -0.0467 0.0908  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.6547 0.6215 0.2611 0.4008 -0.0358 0.0809  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.6508 0.6543 0.2146 0.4242 -0.0670 0.0740  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.6258 0.6763 0.2397 0.4052 -0.0771 0.0431  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.6369 0.6743 0.2480 0.3757 -0.0617 0.0373  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.6592 0.6688 0.2247 0.3766 -0.0513 0.0516  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.6263 0.7223 0.2378 0.4237 -0.1094 0.0237  58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.6695 0.8005 0.3022 0.4526 -0.1320 0.0200  58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.6866 0.8003 0.3294 0.4635 -0.1214 0.0351  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.6744 0.8511 0.3132 0.4666 -0.1623 0.0002  58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.6167 0.6772 0.2764 0.3514 -0.0607 0.0166  59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.6296 0.6774 0.2886 0.3274 -0.0491 0.0098  59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.6383 0.7120 0.2989 0.3279 -0.0708 -0.0163 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.6168 0.7178 0.3253 0.3132 -0.0815 -0.0380 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.6143 0.6585 0.3157 0.3018 -0.0318 0.0086  59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.6339 0.6474 0.3221 0.3035 -0.0125 0.0308  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.6190 0.6522 0.3237 0.2807 -0.0240 0.0004  59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.6291 0.6446 0.3514 0.2868 0.0010  0.0294  59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.6604 0.7257 0.2680 0.3447 -0.0771 -0.0146 60  THR   A N   
83   N  N   B THR   A 17  ? 0.6605 0.7256 0.2681 0.3445 -0.0770 -0.0147 60  THR   A N   
84   N  N   C THR   A 17  ? 0.6604 0.7257 0.2680 0.3447 -0.0771 -0.0146 60  THR   A N   
85   N  N   D THR   A 17  ? 0.6605 0.7256 0.2681 0.3445 -0.0770 -0.0147 60  THR   A N   
86   C  CA  A THR   A 17  ? 0.6667 0.7526 0.2639 0.3495 -0.0994 -0.0429 60  THR   A CA  
87   C  CA  B THR   A 17  ? 0.6649 0.7516 0.2623 0.3500 -0.1000 -0.0430 60  THR   A CA  
88   C  CA  C THR   A 17  ? 0.6667 0.7526 0.2639 0.3495 -0.0994 -0.0429 60  THR   A CA  
89   C  CA  D THR   A 17  ? 0.6649 0.7516 0.2623 0.3500 -0.1000 -0.0430 60  THR   A CA  
90   C  C   A THR   A 17  ? 0.6940 0.7555 0.2450 0.3504 -0.0859 -0.0413 60  THR   A C   
91   C  C   B THR   A 17  ? 0.6942 0.7568 0.2437 0.3517 -0.0871 -0.0415 60  THR   A C   
92   C  C   C THR   A 17  ? 0.6940 0.7555 0.2450 0.3504 -0.0859 -0.0413 60  THR   A C   
93   C  C   D THR   A 17  ? 0.6942 0.7568 0.2437 0.3517 -0.0871 -0.0415 60  THR   A C   
94   O  O   A THR   A 17  ? 0.7122 0.7492 0.2267 0.3563 -0.0643 -0.0139 60  THR   A O   
95   O  O   B THR   A 17  ? 0.7131 0.7515 0.2244 0.3586 -0.0661 -0.0140 60  THR   A O   
96   O  O   C THR   A 17  ? 0.7122 0.7492 0.2267 0.3563 -0.0643 -0.0139 60  THR   A O   
97   O  O   D THR   A 17  ? 0.7131 0.7515 0.2244 0.3586 -0.0661 -0.0140 60  THR   A O   
98   C  CB  A THR   A 17  ? 0.6860 0.8002 0.2563 0.3803 -0.1282 -0.0484 60  THR   A CB  
99   C  CB  B THR   A 17  ? 0.6803 0.7966 0.2556 0.3804 -0.1288 -0.0476 60  THR   A CB  
100  C  CB  C THR   A 17  ? 0.6860 0.8002 0.2563 0.3803 -0.1282 -0.0484 60  THR   A CB  
101  C  CB  D THR   A 17  ? 0.6803 0.7966 0.2556 0.3804 -0.1288 -0.0476 60  THR   A CB  
102  O  OG1 A THR   A 17  ? 0.7293 0.8190 0.2358 0.4043 -0.1176 -0.0178 60  THR   A OG1 
103  O  OG1 B THR   A 17  ? 0.6672 0.8091 0.2913 0.3816 -0.1372 -0.0469 60  THR   A OG1 
104  O  OG1 C THR   A 17  ? 0.7293 0.8190 0.2358 0.4043 -0.1176 -0.0178 60  THR   A OG1 
105  O  OG1 D THR   A 17  ? 0.6672 0.8091 0.2913 0.3816 -0.1372 -0.0469 60  THR   A OG1 
106  C  CG2 A THR   A 17  ? 0.6625 0.8121 0.2844 0.3840 -0.1447 -0.0539 60  THR   A CG2 
107  C  CG2 B THR   A 17  ? 0.6778 0.8229 0.2449 0.3872 -0.1592 -0.0833 60  THR   A CG2 
108  C  CG2 C THR   A 17  ? 0.6625 0.8121 0.2844 0.3840 -0.1447 -0.0539 60  THR   A CG2 
109  C  CG2 D THR   A 17  ? 0.6778 0.8229 0.2449 0.3872 -0.1592 -0.0833 60  THR   A CG2 
110  N  N   . TRP   A 18  ? 0.6963 0.7653 0.2511 0.3449 -0.0986 -0.0719 61  TRP   A N   
111  C  CA  . TRP   A 18  ? 0.7599 0.8112 0.2710 0.3509 -0.0869 -0.0755 61  TRP   A CA  
112  C  C   . TRP   A 18  ? 0.8309 0.8970 0.2773 0.3835 -0.1026 -0.0771 61  TRP   A C   
113  O  O   . TRP   A 18  ? 0.8256 0.9193 0.2739 0.3949 -0.1344 -0.1005 61  TRP   A O   
114  C  CB  . TRP   A 18  ? 0.7493 0.7973 0.2877 0.3360 -0.0966 -0.1112 61  TRP   A CB  
115  C  CG  . TRP   A 18  ? 0.7733 0.8094 0.2649 0.3497 -0.0908 -0.1247 61  TRP   A CG  
116  C  CD1 . TRP   A 18  ? 0.7930 0.8424 0.2380 0.3727 -0.1107 -0.1502 61  TRP   A CD1 
117  C  CD2 . TRP   A 18  ? 0.7817 0.7938 0.2723 0.3428 -0.0651 -0.1183 61  TRP   A CD2 
118  N  NE1 . TRP   A 18  ? 0.8123 0.8464 0.2240 0.3818 -0.0954 -0.1589 61  TRP   A NE1 
119  C  CE2 . TRP   A 18  ? 0.8070 0.8195 0.2499 0.3637 -0.0679 -0.1398 61  TRP   A CE2 
120  C  CE3 . TRP   A 18  ? 0.7801 0.7738 0.3039 0.3236 -0.0411 -0.0973 61  TRP   A CE3 
121  C  CZ2 . TRP   A 18  ? 0.8244 0.8214 0.2571 0.3667 -0.0458 -0.1403 61  TRP   A CZ2 
122  C  CZ3 . TRP   A 18  ? 0.7959 0.7752 0.3102 0.3260 -0.0223 -0.0973 61  TRP   A CZ3 
123  C  CH2 . TRP   A 18  ? 0.8149 0.7965 0.2871 0.3474 -0.0240 -0.1185 61  TRP   A CH2 
124  N  N   . GLU   A 19  ? 0.8891 0.9405 0.2796 0.3984 -0.0808 -0.0511 62  GLU   A N   
125  C  CA  . GLU   A 19  ? 0.9473 1.0101 0.2677 0.4311 -0.0911 -0.0457 62  GLU   A CA  
126  C  C   . GLU   A 19  ? 0.9970 1.0629 0.2684 0.4446 -0.0876 -0.0652 62  GLU   A C   
127  O  O   . GLU   A 19  ? 1.0091 1.0599 0.2700 0.4385 -0.0570 -0.0519 62  GLU   A O   
128  C  CB  . GLU   A 19  ? 1.0086 1.0532 0.2948 0.4419 -0.0697 0.0020  62  GLU   A CB  
129  C  CG  . GLU   A 19  ? 1.0829 1.1281 0.4026 0.4422 -0.0824 0.0152  62  GLU   A CG  
130  C  CD  . GLU   A 19  ? 1.1629 1.2416 0.4767 0.4655 -0.1221 -0.0054 62  GLU   A CD  
131  O  OE1 . GLU   A 19  ? 1.2114 1.2953 0.4609 0.4975 -0.1324 0.0070  62  GLU   A OE1 
132  O  OE2 . GLU   A 19  ? 1.1512 1.2539 0.5255 0.4519 -0.1428 -0.0334 62  GLU   A OE2 
133  N  N   . LYS   A 20  ? 1.0217 1.1105 0.2638 0.4646 -0.1197 -0.0992 63  LYS   A N   
134  C  CA  . LYS   A 20  ? 1.0696 1.1620 0.2579 0.4823 -0.1186 -0.1235 63  LYS   A CA  
135  C  C   . LYS   A 20  ? 1.1262 1.2166 0.2363 0.5078 -0.0920 -0.0864 63  LYS   A C   
136  O  O   . LYS   A 20  ? 1.1495 1.2401 0.2330 0.5207 -0.0916 -0.0520 63  LYS   A O   
137  C  CB  . LYS   A 20  ? 1.0933 1.2112 0.2667 0.4979 -0.1632 -0.1727 63  LYS   A CB  
138  C  CG  . LYS   A 20  ? 1.1253 1.2435 0.3792 0.4684 -0.1866 -0.2126 63  LYS   A CG  
139  C  CD  . LYS   A 20  ? 1.1792 1.3229 0.4226 0.4804 -0.2327 -0.2659 63  LYS   A CD  
140  C  CE  . LYS   A 20  ? 1.2561 1.3868 0.4564 0.4928 -0.2334 -0.3041 63  LYS   A CE  
141  N  NZ  . LYS   A 20  ? 1.2836 1.3787 0.5375 0.4645 -0.2132 -0.3155 63  LYS   A NZ  
142  N  N   . ASP   A 21  ? 1.1471 1.2346 0.2229 0.5152 -0.0674 -0.0912 64  ASP   A N   
143  C  CA  . ASP   A 21  ? 1.1902 1.2798 0.1947 0.5365 -0.0357 -0.0543 64  ASP   A CA  
144  C  C   . ASP   A 21  ? 1.1867 1.2565 0.2148 0.5176 -0.0020 0.0004  64  ASP   A C   
145  O  O   . ASP   A 21  ? 1.2131 1.2774 0.1973 0.5314 0.0072  0.0396  64  ASP   A O   
146  C  CB  . ASP   A 21  ? 1.2593 1.3680 0.1799 0.5749 -0.0576 -0.0543 64  ASP   A CB  
147  C  CG  . ASP   A 21  ? 1.3828 1.5119 0.2562 0.5992 -0.0793 -0.1059 64  ASP   A CG  
148  O  OD1 . ASP   A 21  ? 1.4130 1.5405 0.2810 0.5989 -0.0565 -0.1224 64  ASP   A OD1 
149  O  OD2 . ASP   A 21  ? 1.4304 1.5784 0.2724 0.6204 -0.1203 -0.1317 64  ASP   A OD2 
150  N  N   . ALA   A 22  ? 1.1546 1.2109 0.2513 0.4863 0.0143  0.0020  65  ALA   A N   
151  C  CA  . ALA   A 22  ? 1.1375 1.1752 0.2644 0.4643 0.0446  0.0458  65  ALA   A CA  
152  C  C   . ALA   A 22  ? 1.1221 1.1675 0.2313 0.4632 0.0862  0.0636  65  ALA   A C   
153  O  O   . ALA   A 22  ? 1.1165 1.1806 0.1987 0.4794 0.0895  0.0373  65  ALA   A O   
154  C  CB  . ALA   A 22  ? 1.1167 1.1415 0.3255 0.4332 0.0366  0.0346  65  ALA   A CB  
155  N  N   A GLU   A 23  ? 1.1184 1.1516 0.2438 0.4452 0.1170  0.1055  66  GLU   A N   
156  N  N   B GLU   A 23  ? 1.1184 1.1516 0.2438 0.4452 0.1170  0.1055  66  GLU   A N   
157  N  N   C GLU   A 23  ? 1.1167 1.1498 0.2437 0.4446 0.1169  0.1052  66  GLU   A N   
158  N  N   D GLU   A 23  ? 1.1167 1.1498 0.2437 0.4446 0.1169  0.1052  66  GLU   A N   
159  C  CA  A GLU   A 23  ? 1.1182 1.1672 0.2384 0.4407 0.1572  0.1236  66  GLU   A CA  
160  C  CA  B GLU   A 23  ? 1.1182 1.1672 0.2384 0.4407 0.1572  0.1236  66  GLU   A CA  
161  C  CA  C GLU   A 23  ? 1.1148 1.1625 0.2391 0.4388 0.1574  0.1245  66  GLU   A CA  
162  C  CA  D GLU   A 23  ? 1.1148 1.1625 0.2391 0.4388 0.1574  0.1245  66  GLU   A CA  
163  C  C   A GLU   A 23  ? 1.0885 1.1481 0.2700 0.4239 0.1612  0.0966  66  GLU   A C   
164  C  C   B GLU   A 23  ? 1.0885 1.1481 0.2700 0.4239 0.1612  0.0966  66  GLU   A C   
165  C  C   C GLU   A 23  ? 1.0870 1.1462 0.2704 0.4234 0.1602  0.0956  66  GLU   A C   
166  C  C   D GLU   A 23  ? 1.0870 1.1462 0.2704 0.4234 0.1602  0.0956  66  GLU   A C   
167  O  O   A GLU   A 23  ? 1.0724 1.1178 0.3147 0.3976 0.1574  0.0993  66  GLU   A O   
168  O  O   B GLU   A 23  ? 1.0724 1.1178 0.3147 0.3976 0.1574  0.0993  66  GLU   A O   
169  O  O   C GLU   A 23  ? 1.0710 1.1160 0.3153 0.3977 0.1549  0.0961  66  GLU   A O   
170  O  O   D GLU   A 23  ? 1.0710 1.1160 0.3153 0.3977 0.1549  0.0961  66  GLU   A O   
171  C  CB  A GLU   A 23  ? 1.1548 1.1872 0.2816 0.4222 0.1873  0.1751  66  GLU   A CB  
172  C  CB  B GLU   A 23  ? 1.1548 1.1872 0.2816 0.4222 0.1873  0.1751  66  GLU   A CB  
173  C  CB  C GLU   A 23  ? 1.1448 1.1733 0.2854 0.4167 0.1844  0.1738  66  GLU   A CB  
174  C  CB  D GLU   A 23  ? 1.1448 1.1733 0.2854 0.4167 0.1844  0.1738  66  GLU   A CB  
175  C  CG  A GLU   A 23  ? 1.2106 1.2679 0.3399 0.4146 0.2305  0.1951  66  GLU   A CG  
176  C  CG  B GLU   A 23  ? 1.2106 1.2679 0.3399 0.4146 0.2305  0.1951  66  GLU   A CG  
177  C  CG  C GLU   A 23  ? 1.1896 1.2392 0.3444 0.4034 0.2270  0.1952  66  GLU   A CG  
178  C  CG  D GLU   A 23  ? 1.1896 1.2392 0.3444 0.4034 0.2270  0.1952  66  GLU   A CG  
179  C  CD  A GLU   A 23  ? 1.2929 1.3333 0.4364 0.3906 0.2611  0.2448  66  GLU   A CD  
180  C  CD  B GLU   A 23  ? 1.2929 1.3333 0.4364 0.3906 0.2611  0.2448  66  GLU   A CD  
181  C  CD  C GLU   A 23  ? 1.2489 1.2777 0.4431 0.3716 0.2489  0.2345  66  GLU   A CD  
182  C  CD  D GLU   A 23  ? 1.2489 1.2777 0.4431 0.3716 0.2489  0.2345  66  GLU   A CD  
183  O  OE1 A GLU   A 23  ? 1.3327 1.3409 0.4417 0.3954 0.2570  0.2740  66  GLU   A OE1 
184  O  OE1 B GLU   A 23  ? 1.3327 1.3409 0.4417 0.3954 0.2570  0.2740  66  GLU   A OE1 
185  O  OE1 C GLU   A 23  ? 1.2722 1.2637 0.4602 0.3670 0.2368  0.2542  66  GLU   A OE1 
186  O  OE1 D GLU   A 23  ? 1.2722 1.2637 0.4602 0.3670 0.2368  0.2542  66  GLU   A OE1 
187  O  OE2 A GLU   A 23  ? 1.2950 1.3540 0.4862 0.3672 0.2881  0.2539  66  GLU   A OE2 
188  O  OE2 B GLU   A 23  ? 1.2950 1.3540 0.4862 0.3672 0.2881  0.2539  66  GLU   A OE2 
189  O  OE2 C GLU   A 23  ? 1.2500 1.3007 0.4834 0.3519 0.2771  0.2437  66  GLU   A OE2 
190  O  OE2 D GLU   A 23  ? 1.2500 1.3007 0.4834 0.3519 0.2771  0.2437  66  GLU   A OE2 
191  N  N   . VAL   A 24  ? 1.0800 1.1634 0.2421 0.4423 0.1678  0.0699  67  VAL   A N   
192  C  CA  . VAL   A 24  ? 1.0395 1.1306 0.2540 0.4334 0.1701  0.0433  67  VAL   A CA  
193  C  C   . VAL   A 24  ? 0.9990 1.1150 0.2395 0.4229 0.2099  0.0681  67  VAL   A C   
194  O  O   . VAL   A 24  ? 1.0051 1.1501 0.2078 0.4418 0.2363  0.0737  67  VAL   A O   
195  C  CB  . VAL   A 24  ? 1.0505 1.1470 0.2421 0.4587 0.1512  -0.0059 67  VAL   A CB  
196  C  CG1 . VAL   A 24  ? 1.0412 1.1254 0.2965 0.4450 0.1406  -0.0322 67  VAL   A CG1 
197  C  CG2 . VAL   A 24  ? 1.0676 1.1520 0.2184 0.4737 0.1146  -0.0287 67  VAL   A CG2 
198  N  N   . THR   A 25  ? 0.9576 1.0669 0.2622 0.3932 0.2145  0.0827  68  THR   A N   
199  C  CA  . THR   A 25  ? 0.9287 1.0667 0.2696 0.3787 0.2483  0.1054  68  THR   A CA  
200  C  C   . THR   A 25  ? 0.9027 1.0403 0.3166 0.3583 0.2398  0.0941  68  THR   A C   
201  O  O   . THR   A 25  ? 0.9038 1.0134 0.3365 0.3529 0.2109  0.0751  68  THR   A O   
202  C  CB  . THR   A 25  ? 0.9444 1.0761 0.2763 0.3602 0.2697  0.1512  68  THR   A CB  
203  O  OG1 . THR   A 25  ? 0.9322 1.1014 0.2935 0.3482 0.3064  0.1722  68  THR   A OG1 
204  C  CG2 . THR   A 25  ? 0.9451 1.0398 0.3135 0.3331 0.2509  0.1623  68  THR   A CG2 
205  N  N   . GLY   A 26  ? 0.8732 1.0454 0.3273 0.3482 0.2650  0.1065  69  GLY   A N   
206  C  CA  . GLY   A 26  ? 0.8502 1.0279 0.3692 0.3323 0.2566  0.0983  69  GLY   A CA  
207  C  C   . GLY   A 26  ? 0.8361 1.0296 0.3696 0.3552 0.2513  0.0669  69  GLY   A C   
208  O  O   . GLY   A 26  ? 0.8558 1.0314 0.3543 0.3787 0.2368  0.0399  69  GLY   A O   
209  N  N   . ASN   A 27  ? 0.7963 1.0220 0.3840 0.3490 0.2608  0.0691  70  ASN   A N   
210  C  CA  . ASN   A 27  ? 0.7775 1.0177 0.3868 0.3725 0.2562  0.0428  70  ASN   A CA  
211  C  C   . ASN   A 27  ? 0.7587 0.9592 0.3964 0.3652 0.2242  0.0291  70  ASN   A C   
212  O  O   . ASN   A 27  ? 0.7686 0.9369 0.4074 0.3423 0.2082  0.0389  70  ASN   A O   
213  C  CB  . ASN   A 27  ? 0.7648 1.0694 0.4182 0.3744 0.2842  0.0537  70  ASN   A CB  
214  C  CG  . ASN   A 27  ? 0.7918 1.1130 0.5047 0.3423 0.2815  0.0735  70  ASN   A CG  
215  O  OD1 . ASN   A 27  ? 0.8127 1.1180 0.5264 0.3125 0.2814  0.0952  70  ASN   A OD1 
216  N  ND2 . ASN   A 27  ? 0.7738 1.1268 0.5369 0.3500 0.2777  0.0648  70  ASN   A ND2 
217  N  N   . SER   A 28  ? 0.7315 0.9315 0.3883 0.3869 0.2162  0.0075  71  SER   A N   
218  C  CA  . SER   A 28  ? 0.7219 0.8820 0.4010 0.3825 0.1894  -0.0015 71  SER   A CA  
219  C  C   . SER   A 28  ? 0.6804 0.8702 0.4091 0.3902 0.1907  0.0014  71  SER   A C   
220  O  O   . SER   A 28  ? 0.6851 0.8651 0.4196 0.4171 0.1847  -0.0171 71  SER   A O   
221  C  CB  . SER   A 28  ? 0.7643 0.8780 0.4143 0.4029 0.1723  -0.0314 71  SER   A CB  
222  O  OG  . SER   A 28  ? 0.8275 0.9317 0.4285 0.4096 0.1736  -0.0429 71  SER   A OG  
223  N  N   . PRO   A 29  ? 0.6427 0.8671 0.4085 0.3681 0.1958  0.0231  72  PRO   A N   
224  C  CA  . PRO   A 29  ? 0.6056 0.8684 0.4201 0.3777 0.1943  0.0247  72  PRO   A CA  
225  C  C   . PRO   A 29  ? 0.6052 0.8314 0.4327 0.3816 0.1679  0.0216  72  PRO   A C   
226  O  O   . PRO   A 29  ? 0.6120 0.7930 0.4241 0.3625 0.1520  0.0266  72  PRO   A O   
227  C  CB  . PRO   A 29  ? 0.5911 0.9009 0.4394 0.3479 0.2056  0.0466  72  PRO   A CB  
228  C  CG  . PRO   A 29  ? 0.6234 0.8894 0.4422 0.3188 0.1989  0.0575  72  PRO   A CG  
229  C  CD  . PRO   A 29  ? 0.6339 0.8652 0.4003 0.3348 0.2022  0.0454  72  PRO   A CD  
230  N  N   . ARG   A 30  ? 0.5927 0.8412 0.4489 0.4083 0.1645  0.0153  73  ARG   A N   
231  C  CA  . ARG   A 30  ? 0.6077 0.8244 0.4752 0.4151 0.1407  0.0179  73  ARG   A CA  
232  C  C   . ARG   A 30  ? 0.5580 0.8303 0.4701 0.4061 0.1357  0.0324  73  ARG   A C   
233  O  O   . ARG   A 30  ? 0.5234 0.8565 0.4719 0.4244 0.1445  0.0298  73  ARG   A O   
234  C  CB  . ARG   A 30  ? 0.6551 0.8420 0.5170 0.4547 0.1352  0.0008  73  ARG   A CB  
235  C  CG  . ARG   A 30  ? 0.7614 0.8816 0.5800 0.4567 0.1322  -0.0162 73  ARG   A CG  
236  C  CD  . ARG   A 30  ? 0.8470 0.9213 0.6593 0.4916 0.1238  -0.0349 73  ARG   A CD  
237  N  NE  . ARG   A 30  ? 0.9320 0.9638 0.7073 0.4968 0.1255  -0.0599 73  ARG   A NE  
238  C  CZ  . ARG   A 30  ? 0.9976 0.9560 0.7554 0.4957 0.1097  -0.0720 73  ARG   A CZ  
239  N  NH1 . ARG   A 30  ? 1.0160 0.9319 0.7870 0.4905 0.0946  -0.0572 73  ARG   A NH1 
240  N  NH2 . ARG   A 30  ? 1.0035 0.9314 0.7304 0.4995 0.1088  -0.0989 73  ARG   A NH2 
241  N  N   . LEU   A 31  ? 0.5509 0.8077 0.4613 0.3769 0.1219  0.0454  74  LEU   A N   
242  C  CA  . LEU   A 31  ? 0.5173 0.8225 0.4650 0.3620 0.1129  0.0558  74  LEU   A CA  
243  C  C   . LEU   A 31  ? 0.5218 0.8017 0.4656 0.3670 0.0871  0.0627  74  LEU   A C   
244  O  O   . LEU   A 31  ? 0.5534 0.7764 0.4634 0.3548 0.0786  0.0673  74  LEU   A O   
245  C  CB  . LEU   A 31  ? 0.5163 0.8258 0.4610 0.3220 0.1195  0.0638  74  LEU   A CB  
246  C  CG  . LEU   A 31  ? 0.5254 0.8590 0.4699 0.3125 0.1464  0.0641  74  LEU   A CG  
247  C  CD1 . LEU   A 31  ? 0.5419 0.8562 0.4730 0.2759 0.1500  0.0742  74  LEU   A CD1 
248  C  CD2 . LEU   A 31  ? 0.4874 0.9013 0.4824 0.3212 0.1616  0.0638  74  LEU   A CD2 
249  N  N   . ASP   A 32  ? 0.4844 0.8127 0.4636 0.3836 0.0749  0.0647  75  ASP   A N   
250  C  CA  . ASP   A 32  ? 0.4961 0.8087 0.4683 0.3907 0.0494  0.0739  75  ASP   A CA  
251  C  C   . ASP   A 32  ? 0.4774 0.8063 0.4525 0.3544 0.0401  0.0782  75  ASP   A C   
252  O  O   . ASP   A 32  ? 0.4507 0.8425 0.4664 0.3390 0.0422  0.0741  75  ASP   A O   
253  C  CB  . ASP   A 32  ? 0.5013 0.8689 0.5121 0.4247 0.0373  0.0733  75  ASP   A CB  
254  C  CG  . ASP   A 32  ? 0.6149 0.9372 0.6075 0.4665 0.0309  0.0755  75  ASP   A CG  
255  O  OD1 . ASP   A 32  ? 0.6711 0.9375 0.6300 0.4709 0.0156  0.0881  75  ASP   A OD1 
256  O  OD2 . ASP   A 32  ? 0.6372 0.9790 0.6491 0.4958 0.0422  0.0650  75  ASP   A OD2 
257  N  N   . VAL   A 33  ? 0.4865 0.7602 0.4213 0.3396 0.0315  0.0851  76  VAL   A N   
258  C  CA  . VAL   A 33  ? 0.4749 0.7585 0.4077 0.3082 0.0229  0.0852  76  VAL   A CA  
259  C  C   . VAL   A 33  ? 0.4839 0.7468 0.3886 0.3141 0.0001  0.0933  76  VAL   A C   
260  O  O   . VAL   A 33  ? 0.5030 0.7304 0.3833 0.3385 -0.0055 0.1036  76  VAL   A O   
261  C  CB  . VAL   A 33  ? 0.4933 0.7418 0.4054 0.2781 0.0393  0.0832  76  VAL   A CB  
262  C  CG1 . VAL   A 33  ? 0.4846 0.7510 0.4138 0.2754 0.0625  0.0788  76  VAL   A CG1 
263  C  CG2 . VAL   A 33  ? 0.5320 0.7123 0.3984 0.2794 0.0399  0.0888  76  VAL   A CG2 
264  N  N   . ALA   A 34  ? 0.4691 0.7530 0.3758 0.2919 -0.0125 0.0884  77  ALA   A N   
265  C  CA  . ALA   A 34  ? 0.4854 0.7552 0.3593 0.2953 -0.0328 0.0934  77  ALA   A CA  
266  C  C   . ALA   A 34  ? 0.5031 0.7436 0.3517 0.2649 -0.0284 0.0876  77  ALA   A C   
267  O  O   . ALA   A 34  ? 0.4957 0.7529 0.3680 0.2394 -0.0218 0.0762  77  ALA   A O   
268  C  CB  . ALA   A 34  ? 0.4530 0.7874 0.3553 0.3037 -0.0584 0.0867  77  ALA   A CB  
269  N  N   . LEU   A 35  ? 0.5254 0.7215 0.3269 0.2685 -0.0303 0.0964  78  LEU   A N   
270  C  CA  . LEU   A 35  ? 0.5401 0.7090 0.3152 0.2457 -0.0259 0.0901  78  LEU   A CA  
271  C  C   . LEU   A 35  ? 0.5442 0.7294 0.2949 0.2487 -0.0481 0.0852  78  LEU   A C   
272  O  O   . LEU   A 35  ? 0.5564 0.7356 0.2773 0.2714 -0.0578 0.0990  78  LEU   A O   
273  C  CB  . LEU   A 35  ? 0.5703 0.6832 0.3127 0.2474 -0.0084 0.1023  78  LEU   A CB  
274  C  CG  . LEU   A 35  ? 0.6067 0.6928 0.3250 0.2282 -0.0005 0.0962  78  LEU   A CG  
275  C  CD1 . LEU   A 35  ? 0.6041 0.6967 0.3469 0.2060 0.0066  0.0820  78  LEU   A CD1 
276  C  CD2 . LEU   A 35  ? 0.6357 0.6781 0.3313 0.2311 0.0155  0.1088  78  LEU   A CD2 
277  N  N   . ASP   A 36  ? 0.5325 0.7375 0.2948 0.2268 -0.0571 0.0654  79  ASP   A N   
278  C  CA  . ASP   A 36  ? 0.5394 0.7621 0.2768 0.2293 -0.0811 0.0541  79  ASP   A CA  
279  C  C   . ASP   A 36  ? 0.5714 0.7496 0.2546 0.2257 -0.0731 0.0535  79  ASP   A C   
280  O  O   . ASP   A 36  ? 0.5817 0.7206 0.2565 0.2183 -0.0501 0.0605  79  ASP   A O   
281  C  CB  . ASP   A 36  ? 0.5285 0.7988 0.3096 0.2085 -0.0995 0.0290  79  ASP   A CB  
282  C  CG  . ASP   A 36  ? 0.6029 0.8517 0.3963 0.1757 -0.0900 0.0114  79  ASP   A CG  
283  O  OD1 . ASP   A 36  ? 0.6415 0.8404 0.4059 0.1715 -0.0704 0.0170  79  ASP   A OD1 
284  O  OD2 . ASP   A 36  ? 0.6150 0.8969 0.4496 0.1543 -0.1027 -0.0078 79  ASP   A OD2 
285  N  N   . GLU   A 37  ? 0.5838 0.7728 0.2303 0.2336 -0.0923 0.0444  80  GLU   A N   
286  C  CA  . GLU   A 37  ? 0.6266 0.7823 0.2196 0.2344 -0.0842 0.0422  80  GLU   A CA  
287  C  C   . GLU   A 37  ? 0.6387 0.7691 0.2418 0.2094 -0.0720 0.0223  80  GLU   A C   
288  O  O   . GLU   A 37  ? 0.6605 0.7589 0.2303 0.2108 -0.0560 0.0246  80  GLU   A O   
289  C  CB  . GLU   A 37  ? 0.6674 0.8472 0.2171 0.2495 -0.1103 0.0316  80  GLU   A CB  
290  C  CG  . GLU   A 37  ? 0.7797 0.9312 0.2619 0.2651 -0.0977 0.0446  80  GLU   A CG  
291  C  CD  . GLU   A 37  ? 0.8858 1.0606 0.3148 0.2819 -0.1225 0.0319  80  GLU   A CD  
292  O  OE1 . GLU   A 37  ? 0.8976 1.0845 0.3261 0.2693 -0.1397 -0.0035 80  GLU   A OE1 
293  O  OE2 . GLU   A 37  ? 0.9290 1.1071 0.3140 0.3082 -0.1252 0.0573  80  GLU   A OE2 
294  N  N   . SER   A 38  ? 0.6205 0.7650 0.2710 0.1873 -0.0779 0.0048  81  SER   A N   
295  C  CA  . SER   A 38  ? 0.6301 0.7440 0.2904 0.1649 -0.0669 -0.0111 81  SER   A CA  
296  C  C   . SER   A 38  ? 0.6319 0.7193 0.3140 0.1576 -0.0406 0.0050  81  SER   A C   
297  O  O   . SER   A 38  ? 0.6455 0.7071 0.3378 0.1411 -0.0317 -0.0044 81  SER   A O   
298  C  CB  . SER   A 38  ? 0.6340 0.7690 0.3315 0.1415 -0.0858 -0.0375 81  SER   A CB  
299  O  OG  . SER   A 38  ? 0.6832 0.8337 0.3524 0.1463 -0.1120 -0.0611 81  SER   A OG  
300  N  N   . GLY   A 39  ? 0.6212 0.7120 0.3081 0.1710 -0.0297 0.0279  82  GLY   A N   
301  C  CA  . GLY   A 39  ? 0.6196 0.6885 0.3229 0.1668 -0.0078 0.0405  82  GLY   A CA  
302  C  C   . GLY   A 39  ? 0.5912 0.6799 0.3404 0.1536 -0.0046 0.0398  82  GLY   A C   
303  O  O   . GLY   A 39  ? 0.5946 0.6645 0.3533 0.1476 0.0125  0.0464  82  GLY   A O   
304  N  N   . ASP   A 40  ? 0.5565 0.6877 0.3349 0.1497 -0.0205 0.0323  83  ASP   A N   
305  C  CA  . ASP   A 40  ? 0.5222 0.6819 0.3495 0.1362 -0.0145 0.0328  83  ASP   A CA  
306  C  C   . ASP   A 40  ? 0.4919 0.6825 0.3375 0.1564 -0.0116 0.0461  83  ASP   A C   
307  O  O   . ASP   A 40  ? 0.4797 0.6974 0.3235 0.1743 -0.0283 0.0470  83  ASP   A O   
308  C  CB  . ASP   A 40  ? 0.5253 0.7192 0.3867 0.1150 -0.0323 0.0138  83  ASP   A CB  
309  C  CG  . ASP   A 40  ? 0.6267 0.7847 0.4758 0.0934 -0.0353 -0.0030 83  ASP   A CG  
310  O  OD1 . ASP   A 40  ? 0.6657 0.7774 0.4959 0.0897 -0.0173 0.0034  83  ASP   A OD1 
311  O  OD2 . ASP   A 40  ? 0.6612 0.8373 0.5200 0.0816 -0.0574 -0.0244 83  ASP   A OD2 
312  N  N   . PHE   A 41  ? 0.4750 0.6610 0.3357 0.1561 0.0089  0.0557  84  PHE   A N   
313  C  CA  . PHE   A 41  ? 0.4497 0.6629 0.3294 0.1764 0.0141  0.0644  84  PHE   A CA  
314  C  C   . PHE   A 41  ? 0.4349 0.7090 0.3687 0.1668 0.0114  0.0585  84  PHE   A C   
315  O  O   . PHE   A 41  ? 0.4217 0.7048 0.3801 0.1398 0.0179  0.0534  84  PHE   A O   
316  C  CB  . PHE   A 41  ? 0.4349 0.6197 0.3042 0.1814 0.0370  0.0731  84  PHE   A CB  
317  C  CG  . PHE   A 41  ? 0.4465 0.5808 0.2742 0.1927 0.0404  0.0789  84  PHE   A CG  
318  C  CD1 . PHE   A 41  ? 0.4448 0.5697 0.2596 0.2159 0.0354  0.0855  84  PHE   A CD1 
319  C  CD2 . PHE   A 41  ? 0.4643 0.5610 0.2702 0.1802 0.0494  0.0786  84  PHE   A CD2 
320  C  CE1 . PHE   A 41  ? 0.4704 0.5505 0.2550 0.2214 0.0405  0.0913  84  PHE   A CE1 
321  C  CE2 . PHE   A 41  ? 0.4817 0.5411 0.2586 0.1886 0.0528  0.0828  84  PHE   A CE2 
322  C  CZ  . PHE   A 41  ? 0.4790 0.5310 0.2475 0.2068 0.0490  0.0891  84  PHE   A CZ  
323  N  N   . SER   A 42  ? 0.4382 0.7542 0.3936 0.1892 0.0028  0.0603  85  SER   A N   
324  C  CA  . SER   A 42  ? 0.4248 0.8110 0.4401 0.1841 0.0012  0.0548  85  SER   A CA  
325  C  C   . SER   A 42  ? 0.4398 0.8507 0.4705 0.2147 0.0122  0.0623  85  SER   A C   
326  O  O   . SER   A 42  ? 0.4628 0.8396 0.4592 0.2425 0.0094  0.0691  85  SER   A O   
327  C  CB  . SER   A 42  ? 0.4164 0.8470 0.4519 0.1835 -0.0300 0.0429  85  SER   A CB  
328  O  OG  . SER   A 42  ? 0.4608 0.8770 0.4593 0.2157 -0.0474 0.0488  85  SER   A OG  
329  N  N   . LEU   A 43  ? 0.4266 0.8949 0.5093 0.2099 0.0261  0.0607  86  LEU   A N   
330  C  CA  . LEU   A 43  ? 0.4381 0.9340 0.5367 0.2426 0.0379  0.0643  86  LEU   A CA  
331  C  C   . LEU   A 43  ? 0.4370 0.9851 0.5647 0.2699 0.0133  0.0603  86  LEU   A C   
332  O  O   . LEU   A 43  ? 0.3998 1.0029 0.5680 0.2555 -0.0049 0.0522  86  LEU   A O   
333  C  CB  . LEU   A 43  ? 0.4136 0.9564 0.5548 0.2299 0.0668  0.0655  86  LEU   A CB  
334  C  CG  . LEU   A 43  ? 0.4668 0.9622 0.5715 0.2248 0.0958  0.0728  86  LEU   A CG  
335  C  CD1 . LEU   A 43  ? 0.4437 0.9913 0.5889 0.2098 0.1251  0.0774  86  LEU   A CD1 
336  C  CD2 . LEU   A 43  ? 0.5025 0.9606 0.5686 0.2624 0.0998  0.0725  86  LEU   A CD2 
337  N  N   . VAL   A 44  ? 0.4769 1.0075 0.5854 0.3100 0.0111  0.0652  87  VAL   A N   
338  C  CA  . VAL   A 44  ? 0.4866 1.0635 0.6203 0.3450 -0.0112 0.0645  87  VAL   A CA  
339  C  C   . VAL   A 44  ? 0.5021 1.1214 0.6733 0.3707 0.0099  0.0617  87  VAL   A C   
340  O  O   . VAL   A 44  ? 0.5379 1.1119 0.6789 0.4013 0.0187  0.0649  87  VAL   A O   
341  C  CB  . VAL   A 44  ? 0.5311 1.0431 0.6083 0.3741 -0.0287 0.0753  87  VAL   A CB  
342  C  CG1 . VAL   A 44  ? 0.5172 1.0728 0.6156 0.4145 -0.0534 0.0780  87  VAL   A CG1 
343  C  CG2 . VAL   A 44  ? 0.5632 1.0284 0.5950 0.3487 -0.0414 0.0785  87  VAL   A CG2 
344  N  N   . GLU   A 45  ? 0.4722 1.1740 0.7077 0.3556 0.0218  0.0548  88  GLU   A N   
345  C  CA  . GLU   A 45  ? 0.4695 1.2180 0.7400 0.3804 0.0472  0.0516  88  GLU   A CA  
346  C  C   . GLU   A 45  ? 0.4392 1.2630 0.7612 0.4210 0.0303  0.0465  88  GLU   A C   
347  O  O   . GLU   A 45  ? 0.4154 1.2877 0.7720 0.4474 0.0504  0.0417  88  GLU   A O   
348  C  CB  . GLU   A 45  ? 0.4787 1.2724 0.7867 0.3444 0.0795  0.0511  88  GLU   A CB  
349  C  CG  . GLU   A 45  ? 0.5961 1.3165 0.8486 0.3239 0.1049  0.0575  88  GLU   A CG  
350  C  CD  . GLU   A 45  ? 0.6816 1.4439 0.9602 0.3079 0.1436  0.0611  88  GLU   A CD  
351  O  OE1 . GLU   A 45  ? 0.6672 1.5056 0.9951 0.3290 0.1588  0.0572  88  GLU   A OE1 
352  O  OE2 . GLU   A 45  ? 0.7327 1.4527 0.9809 0.2766 0.1601  0.0693  88  GLU   A OE2 
353  N  N   . GLY   B 7   ? 0.7312 0.6821 0.5689 0.3060 0.0892  -0.0586 16  GLY   B N   
354  C  CA  . GLY   B 7   ? 0.7432 0.6812 0.5762 0.3276 0.0782  -0.0547 16  GLY   B CA  
355  C  C   . GLY   B 7   ? 0.7451 0.6916 0.5777 0.3303 0.0643  -0.0485 16  GLY   B C   
356  O  O   . GLY   B 7   ? 0.7377 0.7106 0.5924 0.3349 0.0555  -0.0549 16  GLY   B O   
357  N  N   . GLU   B 8   ? 0.7467 0.6714 0.5547 0.3280 0.0619  -0.0363 17  GLU   B N   
358  C  CA  . GLU   B 8   ? 0.7378 0.6678 0.5408 0.3326 0.0487  -0.0313 17  GLU   B CA  
359  C  C   . GLU   B 8   ? 0.7157 0.6622 0.5249 0.3127 0.0480  -0.0318 17  GLU   B C   
360  O  O   . GLU   B 8   ? 0.7323 0.6691 0.5282 0.2979 0.0558  -0.0258 17  GLU   B O   
361  C  CB  . GLU   B 8   ? 0.7824 0.6847 0.5559 0.3422 0.0469  -0.0180 17  GLU   B CB  
362  C  CG  . GLU   B 8   ? 0.8340 0.7408 0.6002 0.3554 0.0315  -0.0152 17  GLU   B CG  
363  C  CD  . GLU   B 8   ? 0.9348 0.8169 0.6707 0.3689 0.0302  -0.0018 17  GLU   B CD  
364  O  OE1 . GLU   B 8   ? 0.9586 0.8207 0.6796 0.3622 0.0424  0.0079  17  GLU   B OE1 
365  O  OE2 . GLU   B 8   ? 0.9728 0.8557 0.6998 0.3860 0.0170  -0.0008 17  GLU   B OE2 
366  N  N   A THR   B 9   ? 0.6942 0.6650 0.5244 0.3122 0.0378  -0.0388 18  THR   B N   
367  N  N   B THR   B 9   ? 0.6940 0.6648 0.5242 0.3122 0.0378  -0.0388 18  THR   B N   
368  N  N   C THR   B 9   ? 0.6942 0.6650 0.5244 0.3122 0.0378  -0.0388 18  THR   B N   
369  N  N   D THR   B 9   ? 0.6940 0.6648 0.5242 0.3122 0.0378  -0.0388 18  THR   B N   
370  C  CA  A THR   B 9   ? 0.6872 0.6708 0.5236 0.2935 0.0354  -0.0389 18  THR   B CA  
371  C  CA  B THR   B 9   ? 0.6864 0.6705 0.5234 0.2938 0.0352  -0.0391 18  THR   B CA  
372  C  CA  C THR   B 9   ? 0.6872 0.6708 0.5236 0.2935 0.0354  -0.0389 18  THR   B CA  
373  C  CA  D THR   B 9   ? 0.6864 0.6705 0.5234 0.2938 0.0352  -0.0391 18  THR   B CA  
374  C  C   A THR   B 9   ? 0.6821 0.6674 0.5151 0.3005 0.0174  -0.0380 18  THR   B C   
375  C  C   B THR   B 9   ? 0.6820 0.6672 0.5149 0.3006 0.0174  -0.0379 18  THR   B C   
376  C  C   C THR   B 9   ? 0.6821 0.6674 0.5151 0.3005 0.0174  -0.0380 18  THR   B C   
377  C  C   D THR   B 9   ? 0.6820 0.6672 0.5149 0.3006 0.0174  -0.0379 18  THR   B C   
378  O  O   A THR   B 9   ? 0.6774 0.6756 0.5223 0.2881 0.0108  -0.0407 18  THR   B O   
379  O  O   B THR   B 9   ? 0.6775 0.6755 0.5222 0.2880 0.0110  -0.0406 18  THR   B O   
380  O  O   C THR   B 9   ? 0.6774 0.6756 0.5223 0.2881 0.0108  -0.0407 18  THR   B O   
381  O  O   D THR   B 9   ? 0.6775 0.6755 0.5222 0.2880 0.0110  -0.0406 18  THR   B O   
382  C  CB  A THR   B 9   ? 0.6866 0.6971 0.5516 0.2792 0.0418  -0.0475 18  THR   B CB  
383  C  CB  B THR   B 9   ? 0.6842 0.6963 0.5514 0.2821 0.0398  -0.0483 18  THR   B CB  
384  C  CB  C THR   B 9   ? 0.6866 0.6971 0.5516 0.2792 0.0418  -0.0475 18  THR   B CB  
385  C  CB  D THR   B 9   ? 0.6842 0.6963 0.5514 0.2821 0.0398  -0.0483 18  THR   B CB  
386  O  OG1 A THR   B 9   ? 0.6959 0.7093 0.5685 0.2839 0.0541  -0.0529 18  THR   B OG1 
387  O  OG1 B THR   B 9   ? 0.6826 0.7133 0.5730 0.2964 0.0293  -0.0561 18  THR   B OG1 
388  O  OG1 C THR   B 9   ? 0.6959 0.7093 0.5685 0.2839 0.0541  -0.0529 18  THR   B OG1 
389  O  OG1 D THR   B 9   ? 0.6826 0.7133 0.5730 0.2964 0.0293  -0.0561 18  THR   B OG1 
390  C  CG2 A THR   B 9   ? 0.6925 0.7052 0.5537 0.2556 0.0484  -0.0440 18  THR   B CG2 
391  C  CG2 B THR   B 9   ? 0.6897 0.7011 0.5577 0.2749 0.0578  -0.0509 18  THR   B CG2 
392  C  CG2 C THR   B 9   ? 0.6925 0.7052 0.5537 0.2556 0.0484  -0.0440 18  THR   B CG2 
393  C  CG2 D THR   B 9   ? 0.6897 0.7011 0.5577 0.2749 0.0578  -0.0509 18  THR   B CG2 
394  N  N   . THR   B 10  ? 0.6824 0.6527 0.4972 0.3205 0.0090  -0.0339 19  THR   B N   
395  C  CA  . THR   B 10  ? 0.6486 0.6181 0.4556 0.3303 -0.0088 -0.0343 19  THR   B CA  
396  C  C   . THR   B 10  ? 0.6173 0.5754 0.4037 0.3208 -0.0080 -0.0273 19  THR   B C   
397  O  O   . THR   B 10  ? 0.6256 0.5699 0.3944 0.3163 0.0047  -0.0187 19  THR   B O   
398  C  CB  . THR   B 10  ? 0.6788 0.6343 0.4672 0.3563 -0.0164 -0.0310 19  THR   B CB  
399  O  OG1 . THR   B 10  ? 0.6912 0.6537 0.4960 0.3669 -0.0155 -0.0364 19  THR   B OG1 
400  C  CG2 . THR   B 10  ? 0.6848 0.6413 0.4652 0.3697 -0.0371 -0.0342 19  THR   B CG2 
401  N  N   . ASP   B 11  ? 0.5826 0.5460 0.3715 0.3185 -0.0228 -0.0313 20  ASP   B N   
402  C  CA  . ASP   B 11  ? 0.5759 0.5279 0.3442 0.3136 -0.0248 -0.0260 20  ASP   B CA  
403  C  C   . ASP   B 11  ? 0.5717 0.5064 0.3083 0.3320 -0.0228 -0.0172 20  ASP   B C   
404  O  O   . ASP   B 11  ? 0.5732 0.5037 0.3027 0.3506 -0.0267 -0.0168 20  ASP   B O   
405  C  CB  . ASP   B 11  ? 0.5975 0.5538 0.3718 0.3136 -0.0448 -0.0335 20  ASP   B CB  
406  C  CG  . ASP   B 11  ? 0.6613 0.6287 0.4584 0.2904 -0.0457 -0.0373 20  ASP   B CG  
407  O  OD1 . ASP   B 11  ? 0.6604 0.6405 0.4772 0.2767 -0.0330 -0.0377 20  ASP   B OD1 
408  O  OD2 . ASP   B 11  ? 0.7020 0.6643 0.4959 0.2865 -0.0592 -0.0399 20  ASP   B OD2 
409  N  N   . GLY   B 12  ? 0.5590 0.4851 0.2773 0.3270 -0.0166 -0.0098 21  GLY   B N   
410  C  CA  . GLY   B 12  ? 0.5597 0.4734 0.2496 0.3423 -0.0123 -0.0001 21  GLY   B CA  
411  C  C   . GLY   B 12  ? 0.5536 0.4627 0.2353 0.3301 0.0047  0.0101  21  GLY   B C   
412  O  O   . GLY   B 12  ? 0.5336 0.4478 0.2281 0.3105 0.0108  0.0087  21  GLY   B O   
413  N  N   . VAL   B 13  ? 0.5561 0.4564 0.2157 0.3417 0.0120  0.0209  22  VAL   B N   
414  C  CA  . VAL   B 13  ? 0.5538 0.4514 0.2068 0.3313 0.0277  0.0318  22  VAL   B CA  
415  C  C   . VAL   B 13  ? 0.5585 0.4464 0.2134 0.3289 0.0407  0.0387  22  VAL   B C   
416  O  O   . VAL   B 13  ? 0.5709 0.4511 0.2208 0.3436 0.0377  0.0394  22  VAL   B O   
417  C  CB  . VAL   B 13  ? 0.5711 0.4682 0.2003 0.3443 0.0278  0.0397  22  VAL   B CB  
418  C  CG1 . VAL   B 13  ? 0.5878 0.4762 0.1960 0.3664 0.0280  0.0470  22  VAL   B CG1 
419  C  CG2 . VAL   B 13  ? 0.5683 0.4692 0.1968 0.3310 0.0417  0.0491  22  VAL   B CG2 
420  N  N   . TYR   B 14  ? 0.5448 0.4317 0.2080 0.3104 0.0531  0.0423  23  TYR   B N   
421  C  CA  . TYR   B 14  ? 0.5434 0.4181 0.2098 0.3057 0.0643  0.0471  23  TYR   B CA  
422  C  C   . TYR   B 14  ? 0.5568 0.4270 0.2179 0.2940 0.0772  0.0587  23  TYR   B C   
423  O  O   . TYR   B 14  ? 0.5633 0.4439 0.2267 0.2832 0.0784  0.0591  23  TYR   B O   
424  C  CB  . TYR   B 14  ? 0.5256 0.4034 0.2127 0.2921 0.0654  0.0359  23  TYR   B CB  
425  C  CG  . TYR   B 14  ? 0.5184 0.4019 0.2168 0.3024 0.0556  0.0251  23  TYR   B CG  
426  C  CD1 . TYR   B 14  ? 0.5171 0.4142 0.2215 0.3058 0.0426  0.0175  23  TYR   B CD1 
427  C  CD2 . TYR   B 14  ? 0.5323 0.4084 0.2381 0.3075 0.0586  0.0217  23  TYR   B CD2 
428  C  CE1 . TYR   B 14  ? 0.5247 0.4301 0.2432 0.3141 0.0327  0.0077  23  TYR   B CE1 
429  C  CE2 . TYR   B 14  ? 0.5404 0.4258 0.2598 0.3180 0.0492  0.0117  23  TYR   B CE2 
430  C  CZ  . TYR   B 14  ? 0.5456 0.4474 0.2729 0.3203 0.0364  0.0048  23  TYR   B CZ  
431  O  OH  . TYR   B 14  ? 0.5638 0.4780 0.3086 0.3291 0.0264  -0.0053 23  TYR   B OH  
432  N  N   . ARG   B 15  ? 0.5601 0.4144 0.2165 0.2945 0.0862  0.0675  24  ARG   B N   
433  C  CA  . ARG   B 15  ? 0.5650 0.4141 0.2208 0.2804 0.0982  0.0783  24  ARG   B CA  
434  C  C   . ARG   B 15  ? 0.5701 0.4137 0.2412 0.2621 0.1020  0.0701  24  ARG   B C   
435  O  O   . ARG   B 15  ? 0.5750 0.4108 0.2522 0.2654 0.0994  0.0611  24  ARG   B O   
436  C  CB  . ARG   B 15  ? 0.5818 0.4121 0.2242 0.2890 0.1057  0.0928  24  ARG   B CB  
437  C  CG  . ARG   B 15  ? 0.6026 0.4347 0.2245 0.3101 0.1032  0.1021  24  ARG   B CG  
438  C  CD  . ARG   B 15  ? 0.6460 0.4584 0.2547 0.3137 0.1134  0.1195  24  ARG   B CD  
439  N  NE  . ARG   B 15  ? 0.6908 0.4998 0.2757 0.3372 0.1105  0.1280  24  ARG   B NE  
440  C  CZ  . ARG   B 15  ? 0.7081 0.5265 0.2768 0.3442 0.1167  0.1409  24  ARG   B CZ  
441  N  NH1 . ARG   B 15  ? 0.6991 0.5330 0.2762 0.3292 0.1264  0.1472  24  ARG   B NH1 
442  N  NH2 . ARG   B 15  ? 0.7034 0.5175 0.2473 0.3674 0.1132  0.1473  24  ARG   B NH2 
443  N  N   . VAL   B 16  ? 0.5648 0.4129 0.2418 0.2439 0.1079  0.0729  25  VAL   B N   
444  C  CA  . VAL   B 16  ? 0.5702 0.4117 0.2580 0.2258 0.1116  0.0659  25  VAL   B CA  
445  C  C   . VAL   B 16  ? 0.5852 0.4085 0.2707 0.2187 0.1205  0.0775  25  VAL   B C   
446  O  O   . VAL   B 16  ? 0.5829 0.4129 0.2668 0.2139 0.1252  0.0895  25  VAL   B O   
447  C  CB  . VAL   B 16  ? 0.5708 0.4302 0.2656 0.2109 0.1095  0.0609  25  VAL   B CB  
448  C  CG1 . VAL   B 16  ? 0.5807 0.4332 0.2831 0.1935 0.1122  0.0523  25  VAL   B CG1 
449  C  CG2 . VAL   B 16  ? 0.5693 0.4443 0.2646 0.2179 0.1004  0.0529  25  VAL   B CG2 
450  N  N   . MET   B 17  ? 0.6020 0.4022 0.2877 0.2191 0.1225  0.0744  26  MET   B N   
451  C  CA  . MET   B 17  ? 0.6350 0.4115 0.3179 0.2128 0.1294  0.0854  26  MET   B CA  
452  C  C   . MET   B 17  ? 0.6739 0.4357 0.3651 0.1949 0.1309  0.0767  26  MET   B C   
453  O  O   . MET   B 17  ? 0.6634 0.4290 0.3593 0.1926 0.1274  0.0611  26  MET   B O   
454  C  CB  . MET   B 17  ? 0.6473 0.4008 0.3195 0.2311 0.1288  0.0897  26  MET   B CB  
455  C  CG  . MET   B 17  ? 0.6646 0.4289 0.3256 0.2523 0.1247  0.0952  26  MET   B CG  
456  S  SD  . MET   B 17  ? 0.6677 0.4403 0.3164 0.2545 0.1319  0.1171  26  MET   B SD  
457  C  CE  . MET   B 17  ? 0.6052 0.3421 0.2459 0.2514 0.1403  0.1334  26  MET   B CE  
458  N  N   . THR   B 18  ? 0.7129 0.4558 0.4049 0.1829 0.1361  0.0870  27  THR   B N   
459  C  CA  . THR   B 18  ? 0.7526 0.4759 0.4504 0.1668 0.1359  0.0783  27  THR   B CA  
460  C  C   . THR   B 18  ? 0.7998 0.4867 0.4933 0.1647 0.1392  0.0880  27  THR   B C   
461  O  O   . THR   B 18  ? 0.7957 0.4770 0.4844 0.1682 0.1441  0.1063  27  THR   B O   
462  C  CB  . THR   B 18  ? 0.7587 0.4995 0.4671 0.1457 0.1354  0.0760  27  THR   B CB  
463  O  OG1 . THR   B 18  ? 0.7891 0.5085 0.5001 0.1326 0.1331  0.0645  27  THR   B OG1 
464  C  CG2 . THR   B 18  ? 0.7460 0.4965 0.4604 0.1358 0.1405  0.0944  27  THR   B CG2 
465  N  N   . ARG   B 19  ? 0.8436 0.5043 0.5376 0.1588 0.1366  0.0759  28  ARG   B N   
466  C  CA  . ARG   B 19  ? 0.8978 0.5180 0.5875 0.1554 0.1379  0.0839  28  ARG   B CA  
467  C  C   . ARG   B 19  ? 0.9159 0.5217 0.6148 0.1297 0.1369  0.0823  28  ARG   B C   
468  O  O   . ARG   B 19  ? 0.9283 0.4993 0.6257 0.1226 0.1375  0.0904  28  ARG   B O   
469  C  CB  . ARG   B 19  ? 0.9463 0.5389 0.6265 0.1739 0.1344  0.0727  28  ARG   B CB  
470  C  CG  . ARG   B 19  ? 1.0178 0.6189 0.6895 0.1986 0.1343  0.0789  28  ARG   B CG  
471  C  CD  . ARG   B 19  ? 1.1049 0.6687 0.7660 0.2157 0.1317  0.0792  28  ARG   B CD  
472  N  NE  . ARG   B 19  ? 1.1676 0.7405 0.8203 0.2399 0.1298  0.0849  28  ARG   B NE  
473  C  CZ  . ARG   B 19  ? 1.2029 0.7883 0.8577 0.2584 0.1246  0.0699  28  ARG   B CZ  
474  N  NH1 . ARG   B 19  ? 1.1957 0.7868 0.8597 0.2560 0.1228  0.0492  28  ARG   B NH1 
475  N  NH2 . ARG   B 19  ? 1.1995 0.7929 0.8472 0.2796 0.1211  0.0756  28  ARG   B NH2 
476  N  N   . ARG   B 20  ? 0.9130 0.5457 0.6215 0.1156 0.1346  0.0732  29  ARG   B N   
477  C  CA  . ARG   B 20  ? 0.9285 0.5567 0.6472 0.0914 0.1312  0.0688  29  ARG   B CA  
478  C  C   . ARG   B 20  ? 0.9271 0.5525 0.6572 0.0747 0.1355  0.0900  29  ARG   B C   
479  O  O   . ARG   B 20  ? 0.9343 0.5386 0.6724 0.0555 0.1322  0.0896  29  ARG   B O   
480  C  CB  . ARG   B 20  ? 0.9432 0.6087 0.6675 0.0853 0.1279  0.0581  29  ARG   B CB  
481  C  CG  . ARG   B 20  ? 1.0045 0.6667 0.7359 0.0638 0.1214  0.0473  29  ARG   B CG  
482  C  CD  . ARG   B 20  ? 1.0475 0.7479 0.7831 0.0591 0.1183  0.0414  29  ARG   B CD  
483  N  NE  . ARG   B 20  ? 1.0805 0.8106 0.8287 0.0544 0.1217  0.0586  29  ARG   B NE  
484  C  CZ  . ARG   B 20  ? 1.1003 0.8458 0.8635 0.0359 0.1187  0.0628  29  ARG   B CZ  
485  N  NH1 . ARG   B 20  ? 1.1082 0.8408 0.8748 0.0195 0.1106  0.0508  29  ARG   B NH1 
486  N  NH2 . ARG   B 20  ? 1.0755 0.8509 0.8506 0.0347 0.1231  0.0782  29  ARG   B NH2 
487  N  N   . LEU   B 21  ? 0.9093 0.5577 0.6406 0.0819 0.1428  0.1080  30  LEU   B N   
488  C  CA  . LEU   B 21  ? 0.8998 0.5540 0.6422 0.0686 0.1499  0.1304  30  LEU   B CA  
489  C  C   . LEU   B 21  ? 0.9092 0.5260 0.6396 0.0767 0.1555  0.1472  30  LEU   B C   
490  O  O   . LEU   B 21  ? 0.9258 0.5096 0.6426 0.0891 0.1513  0.1379  30  LEU   B O   
491  C  CB  . LEU   B 21  ? 0.8864 0.5884 0.6333 0.0749 0.1550  0.1389  30  LEU   B CB  
492  C  CG  . LEU   B 21  ? 0.8901 0.6276 0.6501 0.0647 0.1497  0.1278  30  LEU   B CG  
493  C  CD1 . LEU   B 21  ? 0.8927 0.6261 0.6713 0.0381 0.1458  0.1262  30  LEU   B CD1 
494  C  CD2 . LEU   B 21  ? 0.9026 0.6442 0.6523 0.0760 0.1420  0.1062  30  LEU   B CD2 
495  N  N   A LEU   B 22  ? 0.9034 0.5261 0.6386 0.0702 0.1651  0.1715  31  LEU   B N   
496  N  N   B LEU   B 22  ? 0.9034 0.5261 0.6386 0.0702 0.1651  0.1715  31  LEU   B N   
497  N  N   C LEU   B 22  ? 0.9034 0.5262 0.6386 0.0702 0.1651  0.1715  31  LEU   B N   
498  N  N   D LEU   B 22  ? 0.9034 0.5262 0.6386 0.0702 0.1651  0.1715  31  LEU   B N   
499  C  CA  A LEU   B 22  ? 0.9231 0.5114 0.6449 0.0771 0.1710  0.1902  31  LEU   B CA  
500  C  CA  B LEU   B 22  ? 0.9231 0.5114 0.6449 0.0771 0.1710  0.1902  31  LEU   B CA  
501  C  CA  C LEU   B 22  ? 0.9233 0.5115 0.6451 0.0771 0.1710  0.1902  31  LEU   B CA  
502  C  CA  D LEU   B 22  ? 0.9233 0.5115 0.6451 0.0771 0.1710  0.1902  31  LEU   B CA  
503  C  C   A LEU   B 22  ? 0.9310 0.5246 0.6309 0.1074 0.1731  0.1926  31  LEU   B C   
504  C  C   B LEU   B 22  ? 0.9310 0.5246 0.6309 0.1074 0.1731  0.1926  31  LEU   B C   
505  C  C   C LEU   B 22  ? 0.9310 0.5246 0.6309 0.1074 0.1730  0.1925  31  LEU   B C   
506  C  C   D LEU   B 22  ? 0.9310 0.5246 0.6309 0.1074 0.1730  0.1925  31  LEU   B C   
507  O  O   A LEU   B 22  ? 0.9220 0.5536 0.6206 0.1172 0.1773  0.1967  31  LEU   B O   
508  O  O   B LEU   B 22  ? 0.9220 0.5536 0.6206 0.1172 0.1773  0.1967  31  LEU   B O   
509  O  O   C LEU   B 22  ? 0.9220 0.5536 0.6206 0.1172 0.1773  0.1967  31  LEU   B O   
510  O  O   D LEU   B 22  ? 0.9220 0.5536 0.6206 0.1172 0.1773  0.1967  31  LEU   B O   
511  C  CB  A LEU   B 22  ? 0.9183 0.5168 0.6524 0.0596 0.1824  0.2169  31  LEU   B CB  
512  C  CB  B LEU   B 22  ? 0.9183 0.5168 0.6524 0.0596 0.1824  0.2169  31  LEU   B CB  
513  C  CB  C LEU   B 22  ? 0.9184 0.5169 0.6526 0.0596 0.1824  0.2169  31  LEU   B CB  
514  C  CB  D LEU   B 22  ? 0.9184 0.5169 0.6526 0.0596 0.1824  0.2169  31  LEU   B CB  
515  C  CG  A LEU   B 22  ? 0.9539 0.5179 0.6728 0.0649 0.1903  0.2405  31  LEU   B CG  
516  C  CG  B LEU   B 22  ? 0.9539 0.5179 0.6728 0.0649 0.1903  0.2405  31  LEU   B CG  
517  C  CG  C LEU   B 22  ? 0.9543 0.5182 0.6732 0.0649 0.1903  0.2405  31  LEU   B CG  
518  C  CG  D LEU   B 22  ? 0.9543 0.5182 0.6732 0.0649 0.1903  0.2405  31  LEU   B CG  
519  C  CD1 A LEU   B 22  ? 0.9744 0.4902 0.7003 0.0437 0.1864  0.2439  31  LEU   B CD1 
520  C  CD1 B LEU   B 22  ? 0.9744 0.4902 0.7003 0.0437 0.1864  0.2439  31  LEU   B CD1 
521  C  CD1 C LEU   B 22  ? 0.9747 0.4905 0.7005 0.0437 0.1864  0.2440  31  LEU   B CD1 
522  C  CD1 D LEU   B 22  ? 0.9747 0.4905 0.7005 0.0437 0.1864  0.2440  31  LEU   B CD1 
523  C  CD2 A LEU   B 22  ? 0.9518 0.5471 0.6731 0.0634 0.2053  0.2670  31  LEU   B CD2 
524  C  CD2 B LEU   B 22  ? 0.9518 0.5471 0.6731 0.0634 0.2053  0.2670  31  LEU   B CD2 
525  C  CD2 C LEU   B 22  ? 0.9522 0.5474 0.6734 0.0634 0.2053  0.2670  31  LEU   B CD2 
526  C  CD2 D LEU   B 22  ? 0.9522 0.5474 0.6734 0.0634 0.2053  0.2670  31  LEU   B CD2 
527  N  N   . GLY   B 23  ? 0.9452 0.5004 0.6282 0.1228 0.1687  0.1889  32  GLY   B N   
528  C  CA  . GLY   B 23  ? 0.9357 0.4926 0.5985 0.1523 0.1681  0.1897  32  GLY   B CA  
529  C  C   . GLY   B 23  ? 0.9000 0.4887 0.5644 0.1658 0.1614  0.1680  32  GLY   B C   
530  O  O   . GLY   B 23  ? 0.8969 0.4905 0.5723 0.1567 0.1555  0.1483  32  GLY   B O   
531  N  N   . SER   B 24  ? 0.8726 0.4832 0.5255 0.1865 0.1623  0.1719  33  SER   B N   
532  C  CA  . SER   B 24  ? 0.8462 0.4882 0.5020 0.1977 0.1559  0.1537  33  SER   B CA  
533  C  C   . SER   B 24  ? 0.8056 0.4881 0.4674 0.1924 0.1607  0.1610  33  SER   B C   
534  O  O   . SER   B 24  ? 0.8009 0.4938 0.4507 0.2047 0.1655  0.1757  33  SER   B O   
535  C  CB  . SER   B 24  ? 0.8729 0.5098 0.5126 0.2258 0.1506  0.1507  33  SER   B CB  
536  O  OG  . SER   B 24  ? 0.9201 0.5207 0.5546 0.2335 0.1459  0.1443  33  SER   B OG  
537  N  N   . THR   B 25  ? 0.7731 0.4770 0.4517 0.1750 0.1592  0.1512  34  THR   B N   
538  C  CA  . THR   B 25  ? 0.7477 0.4896 0.4333 0.1705 0.1628  0.1570  34  THR   B CA  
539  C  C   . THR   B 25  ? 0.7163 0.4850 0.4005 0.1828 0.1553  0.1418  34  THR   B C   
540  O  O   . THR   B 25  ? 0.7150 0.4827 0.4047 0.1793 0.1482  0.1239  34  THR   B O   
541  C  CB  . THR   B 25  ? 0.7573 0.5079 0.4631 0.1437 0.1654  0.1585  34  THR   B CB  
542  O  OG1 . THR   B 25  ? 0.7769 0.5022 0.4857 0.1309 0.1722  0.1745  34  THR   B OG1 
543  C  CG2 . THR   B 25  ? 0.7467 0.5384 0.4619 0.1404 0.1687  0.1640  34  THR   B CG2 
544  N  N   . GLN   B 26  ? 0.6884 0.4797 0.3639 0.1973 0.1567  0.1488  35  GLN   B N   
545  C  CA  . GLN   B 26  ? 0.6651 0.4797 0.3396 0.2077 0.1484  0.1351  35  GLN   B CA  
546  C  C   . GLN   B 26  ? 0.6367 0.4768 0.3262 0.1918 0.1476  0.1306  35  GLN   B C   
547  O  O   . GLN   B 26  ? 0.6370 0.4935 0.3318 0.1858 0.1544  0.1429  35  GLN   B O   
548  C  CB  . GLN   B 26  ? 0.6682 0.4946 0.3259 0.2303 0.1480  0.1424  35  GLN   B CB  
549  C  CG  . GLN   B 26  ? 0.6761 0.5262 0.3336 0.2391 0.1387  0.1297  35  GLN   B CG  
550  C  CD  . GLN   B 26  ? 0.7272 0.5826 0.3658 0.2632 0.1355  0.1335  35  GLN   B CD  
551  O  OE1 . GLN   B 26  ? 0.7663 0.6039 0.3915 0.2768 0.1353  0.1384  35  GLN   B OE1 
552  N  NE2 . GLN   B 26  ? 0.7184 0.5967 0.3541 0.2703 0.1317  0.1308  35  GLN   B NE2 
553  N  N   . VAL   B 27  ? 0.6094 0.4546 0.3055 0.1862 0.1395  0.1136  36  VAL   B N   
554  C  CA  . VAL   B 27  ? 0.5851 0.4521 0.2929 0.1725 0.1367  0.1085  36  VAL   B CA  
555  C  C   . VAL   B 27  ? 0.5613 0.4512 0.2647 0.1842 0.1298  0.1029  36  VAL   B C   
556  O  O   . VAL   B 27  ? 0.5572 0.4674 0.2677 0.1776 0.1279  0.1025  36  VAL   B O   
557  C  CB  . VAL   B 27  ? 0.6009 0.4571 0.3170 0.1559 0.1325  0.0948  36  VAL   B CB  
558  C  CG1 . VAL   B 27  ? 0.6171 0.4531 0.3401 0.1406 0.1377  0.1004  36  VAL   B CG1 
559  C  CG2 . VAL   B 27  ? 0.6094 0.4538 0.3190 0.1649 0.1272  0.0808  36  VAL   B CG2 
560  N  N   . GLY   B 28  ? 0.5435 0.4288 0.2360 0.2014 0.1248  0.0978  37  GLY   B N   
561  C  CA  . GLY   B 28  ? 0.5256 0.4268 0.2132 0.2124 0.1162  0.0912  37  GLY   B CA  
562  C  C   . GLY   B 28  ? 0.5166 0.4101 0.1937 0.2310 0.1101  0.0863  37  GLY   B C   
563  O  O   . GLY   B 28  ? 0.5243 0.4017 0.1958 0.2385 0.1132  0.0901  37  GLY   B O   
564  N  N   . VAL   B 29  ? 0.4949 0.3988 0.1697 0.2383 0.1001  0.0778  38  VAL   B N   
565  C  CA  . VAL   B 29  ? 0.4757 0.3771 0.1431 0.2551 0.0906  0.0711  38  VAL   B CA  
566  C  C   . VAL   B 29  ? 0.4618 0.3689 0.1380 0.2477 0.0809  0.0577  38  VAL   B C   
567  O  O   . VAL   B 29  ? 0.4547 0.3690 0.1368 0.2341 0.0807  0.0556  38  VAL   B O   
568  C  CB  . VAL   B 29  ? 0.4704 0.3805 0.1226 0.2735 0.0878  0.0774  38  VAL   B CB  
569  C  CG1 . VAL   B 29  ? 0.4749 0.3823 0.1185 0.2913 0.0752  0.0693  38  VAL   B CG1 
570  C  CG2 . VAL   B 29  ? 0.4769 0.3837 0.1195 0.2796 0.0995  0.0929  38  VAL   B CG2 
571  N  N   . GLY   B 30  ? 0.4554 0.3598 0.1327 0.2566 0.0725  0.0495  39  GLY   B N   
572  C  CA  . GLY   B 30  ? 0.4511 0.3614 0.1375 0.2494 0.0636  0.0386  39  GLY   B CA  
573  C  C   . GLY   B 30  ? 0.4530 0.3643 0.1395 0.2633 0.0516  0.0316  39  GLY   B C   
574  O  O   . GLY   B 30  ? 0.4516 0.3577 0.1307 0.2794 0.0499  0.0338  39  GLY   B O   
575  N  N   . VAL   B 31  ? 0.4517 0.3687 0.1471 0.2563 0.0426  0.0232  40  VAL   B N   
576  C  CA  . VAL   B 31  ? 0.4596 0.3788 0.1592 0.2662 0.0290  0.0155  40  VAL   B CA  
577  C  C   . VAL   B 31  ? 0.4534 0.3788 0.1731 0.2562 0.0283  0.0072  40  VAL   B C   
578  O  O   . VAL   B 31  ? 0.4621 0.3919 0.1902 0.2391 0.0308  0.0050  40  VAL   B O   
579  C  CB  . VAL   B 31  ? 0.4788 0.3988 0.1715 0.2683 0.0163  0.0132  40  VAL   B CB  
580  C  CG1 . VAL   B 31  ? 0.4912 0.4122 0.1908 0.2754 0.0001  0.0041  40  VAL   B CG1 
581  C  CG2 . VAL   B 31  ? 0.4879 0.4053 0.1606 0.2825 0.0169  0.0203  40  VAL   B CG2 
582  N  N   . MET   B 32  ? 0.4380 0.3651 0.1653 0.2674 0.0246  0.0027  41  MET   B N   
583  C  CA  . MET   B 32  ? 0.4342 0.3723 0.1839 0.2602 0.0234  -0.0058 41  MET   B CA  
584  C  C   . MET   B 32  ? 0.4416 0.3864 0.1996 0.2616 0.0066  -0.0121 41  MET   B C   
585  O  O   . MET   B 32  ? 0.4555 0.3957 0.2037 0.2779 -0.0054 -0.0130 41  MET   B O   
586  C  CB  . MET   B 32  ? 0.4383 0.3768 0.1949 0.2730 0.0262  -0.0084 41  MET   B CB  
587  C  CG  . MET   B 32  ? 0.4504 0.4044 0.2328 0.2652 0.0290  -0.0173 41  MET   B CG  
588  S  SD  . MET   B 32  ? 0.5110 0.4667 0.2985 0.2457 0.0479  -0.0177 41  MET   B SD  
589  C  CE  . MET   B 32  ? 0.4795 0.4132 0.2471 0.2554 0.0574  -0.0102 41  MET   B CE  
590  N  N   . GLN   B 33  ? 0.4338 0.3877 0.2075 0.2442 0.0052  -0.0158 42  GLN   B N   
591  C  CA  . GLN   B 33  ? 0.4346 0.3928 0.2187 0.2424 -0.0115 -0.0214 42  GLN   B CA  
592  C  C   . GLN   B 33  ? 0.4303 0.4038 0.2394 0.2229 -0.0078 -0.0249 42  GLN   B C   
593  O  O   . GLN   B 33  ? 0.4297 0.4038 0.2372 0.2074 0.0046  -0.0210 42  GLN   B O   
594  C  CB  . GLN   B 33  ? 0.4638 0.4090 0.2299 0.2421 -0.0213 -0.0185 42  GLN   B CB  
595  C  CG  . GLN   B 33  ? 0.5180 0.4624 0.2921 0.2448 -0.0421 -0.0256 42  GLN   B CG  
596  C  CD  . GLN   B 33  ? 0.5739 0.5026 0.3298 0.2471 -0.0544 -0.0249 42  GLN   B CD  
597  O  OE1 . GLN   B 33  ? 0.5849 0.5098 0.3484 0.2332 -0.0629 -0.0263 42  GLN   B OE1 
598  N  NE2 . GLN   B 33  ? 0.5941 0.5132 0.3256 0.2656 -0.0561 -0.0226 42  GLN   B NE2 
599  N  N   . GLU   B 34  ? 0.4209 0.4082 0.2535 0.2239 -0.0177 -0.0320 43  GLU   B N   
600  C  CA  . GLU   B 34  ? 0.4136 0.4201 0.2735 0.2053 -0.0128 -0.0345 43  GLU   B CA  
601  C  C   . GLU   B 34  ? 0.4037 0.4209 0.2689 0.1983 0.0088  -0.0334 43  GLU   B C   
602  O  O   . GLU   B 34  ? 0.4035 0.4295 0.2766 0.1797 0.0185  -0.0314 43  GLU   B O   
603  C  CB  . GLU   B 34  ? 0.4536 0.4540 0.3130 0.1866 -0.0192 -0.0310 43  GLU   B CB  
604  C  CG  . GLU   B 34  ? 0.5207 0.5120 0.3809 0.1923 -0.0424 -0.0350 43  GLU   B CG  
605  C  CD  . GLU   B 34  ? 0.6345 0.6090 0.4839 0.1789 -0.0507 -0.0306 43  GLU   B CD  
606  O  OE1 . GLU   B 34  ? 0.6688 0.6506 0.5352 0.1578 -0.0489 -0.0282 43  GLU   B OE1 
607  O  OE2 . GLU   B 34  ? 0.6736 0.6278 0.4973 0.1899 -0.0589 -0.0292 43  GLU   B OE2 
608  N  N   . GLY   B 35  ? 0.3951 0.4093 0.2535 0.2138 0.0155  -0.0346 44  GLY   B N   
609  C  CA  . GLY   B 35  ? 0.3884 0.4081 0.2491 0.2110 0.0338  -0.0354 44  GLY   B CA  
610  C  C   . GLY   B 35  ? 0.4010 0.4060 0.2394 0.2004 0.0458  -0.0291 44  GLY   B C   
611  O  O   . GLY   B 35  ? 0.4045 0.4133 0.2437 0.1950 0.0602  -0.0307 44  GLY   B O   
612  N  N   . VAL   B 36  ? 0.4076 0.3965 0.2262 0.1982 0.0391  -0.0227 45  VAL   B N   
613  C  CA  . VAL   B 36  ? 0.4136 0.3903 0.2125 0.1881 0.0478  -0.0166 45  VAL   B CA  
614  C  C   . VAL   B 36  ? 0.4234 0.3833 0.2017 0.2004 0.0470  -0.0113 45  VAL   B C   
615  O  O   . VAL   B 36  ? 0.4232 0.3774 0.1947 0.2129 0.0356  -0.0096 45  VAL   B O   
616  C  CB  . VAL   B 36  ? 0.4133 0.3889 0.2088 0.1717 0.0429  -0.0129 45  VAL   B CB  
617  C  CG1 . VAL   B 36  ? 0.4211 0.3842 0.1953 0.1642 0.0486  -0.0069 45  VAL   B CG1 
618  C  CG2 . VAL   B 36  ? 0.4067 0.3993 0.2209 0.1564 0.0484  -0.0157 45  VAL   B CG2 
619  N  N   . PHE   B 37  ? 0.4199 0.3723 0.1884 0.1971 0.0592  -0.0088 46  PHE   B N   
620  C  CA  . PHE   B 37  ? 0.4274 0.3662 0.1793 0.2056 0.0600  -0.0021 46  PHE   B CA  
621  C  C   . PHE   B 37  ? 0.4167 0.3516 0.1564 0.1955 0.0586  0.0034  46  PHE   B C   
622  O  O   . PHE   B 37  ? 0.4165 0.3526 0.1552 0.1808 0.0646  0.0029  46  PHE   B O   
623  C  CB  . PHE   B 37  ? 0.4302 0.3606 0.1791 0.2074 0.0718  -0.0018 46  PHE   B CB  
624  C  CG  . PHE   B 37  ? 0.4493 0.3670 0.1846 0.2182 0.0719  0.0065  46  PHE   B CG  
625  C  CD1 . PHE   B 37  ? 0.4547 0.3710 0.1857 0.2351 0.0636  0.0092  46  PHE   B CD1 
626  C  CD2 . PHE   B 37  ? 0.4692 0.3771 0.1959 0.2109 0.0803  0.0119  46  PHE   B CD2 
627  C  CE1 . PHE   B 37  ? 0.4736 0.3795 0.1907 0.2453 0.0659  0.0182  46  PHE   B CE1 
628  C  CE2 . PHE   B 37  ? 0.4791 0.3776 0.1955 0.2193 0.0820  0.0212  46  PHE   B CE2 
629  C  CZ  . PHE   B 37  ? 0.4796 0.3773 0.1905 0.2367 0.0758  0.0249  46  PHE   B CZ  
630  N  N   . HIS   B 38  ? 0.4063 0.3369 0.1355 0.2046 0.0508  0.0084  47  HIS   B N   
631  C  CA  . HIS   B 38  ? 0.4073 0.3357 0.1259 0.1980 0.0484  0.0134  47  HIS   B CA  
632  C  C   . HIS   B 38  ? 0.4205 0.3449 0.1293 0.2041 0.0545  0.0206  47  HIS   B C   
633  O  O   . HIS   B 38  ? 0.4222 0.3440 0.1266 0.2191 0.0536  0.0233  47  HIS   B O   
634  C  CB  . HIS   B 38  ? 0.4004 0.3283 0.1151 0.2051 0.0339  0.0127  47  HIS   B CB  
635  C  CG  . HIS   B 38  ? 0.4041 0.3356 0.1310 0.1996 0.0260  0.0065  47  HIS   B CG  
636  N  ND1 . HIS   B 38  ? 0.4148 0.3513 0.1538 0.2075 0.0232  0.0012  47  HIS   B ND1 
637  C  CD2 . HIS   B 38  ? 0.4164 0.3476 0.1460 0.1866 0.0202  0.0057  47  HIS   B CD2 
638  C  CE1 . HIS   B 38  ? 0.4118 0.3533 0.1632 0.1980 0.0161  -0.0029 47  HIS   B CE1 
639  N  NE2 . HIS   B 38  ? 0.4193 0.3563 0.1646 0.1848 0.0145  0.0003  47  HIS   B NE2 
640  N  N   . THR   B 39  ? 0.4234 0.3476 0.1288 0.1924 0.0606  0.0241  48  THR   B N   
641  C  CA  . THR   B 39  ? 0.4292 0.3526 0.1290 0.1960 0.0664  0.0320  48  THR   B CA  
642  C  C   . THR   B 39  ? 0.4329 0.3617 0.1298 0.1854 0.0652  0.0350  48  THR   B C   
643  O  O   . THR   B 39  ? 0.4278 0.3581 0.1236 0.1781 0.0587  0.0315  48  THR   B O   
644  C  CB  . THR   B 39  ? 0.4424 0.3579 0.1455 0.1949 0.0771  0.0334  48  THR   B CB  
645  O  OG1 . THR   B 39  ? 0.4452 0.3595 0.1436 0.2006 0.0821  0.0430  48  THR   B OG1 
646  C  CG2 . THR   B 39  ? 0.4515 0.3636 0.1585 0.1780 0.0833  0.0292  48  THR   B CG2 
647  N  N   . MET   B 40  ? 0.4351 0.3675 0.1314 0.1848 0.0708  0.0421  49  MET   B N   
648  C  CA  . MET   B 40  ? 0.4371 0.3773 0.1337 0.1751 0.0694  0.0445  49  MET   B CA  
649  C  C   . MET   B 40  ? 0.4469 0.3825 0.1483 0.1579 0.0758  0.0420  49  MET   B C   
650  O  O   . MET   B 40  ? 0.4550 0.3822 0.1596 0.1566 0.0835  0.0422  49  MET   B O   
651  C  CB  . MET   B 40  ? 0.4345 0.3858 0.1305 0.1847 0.0710  0.0532  49  MET   B CB  
652  C  CG  . MET   B 40  ? 0.4670 0.4204 0.1546 0.2040 0.0644  0.0535  49  MET   B CG  
653  S  SD  . MET   B 40  ? 0.5362 0.5064 0.2201 0.2150 0.0604  0.0588  49  MET   B SD  
654  C  CE  . MET   B 40  ? 0.4593 0.4280 0.1421 0.2059 0.0483  0.0524  49  MET   B CE  
655  N  N   A TRP   B 41  ? 0.4472 0.3860 0.1469 0.1460 0.0716  0.0393  50  TRP   B N   
656  N  N   B TRP   B 41  ? 0.4455 0.3842 0.1452 0.1459 0.0716  0.0392  50  TRP   B N   
657  N  N   C TRP   B 41  ? 0.4472 0.3860 0.1469 0.1460 0.0716  0.0393  50  TRP   B N   
658  N  N   D TRP   B 41  ? 0.4455 0.3842 0.1452 0.1459 0.0716  0.0392  50  TRP   B N   
659  C  CA  A TRP   B 41  ? 0.4583 0.3922 0.1591 0.1304 0.0754  0.0352  50  TRP   B CA  
660  C  CA  B TRP   B 41  ? 0.4551 0.3890 0.1558 0.1302 0.0753  0.0351  50  TRP   B CA  
661  C  CA  C TRP   B 41  ? 0.4583 0.3922 0.1591 0.1304 0.0754  0.0352  50  TRP   B CA  
662  C  CA  D TRP   B 41  ? 0.4551 0.3890 0.1558 0.1302 0.0753  0.0351  50  TRP   B CA  
663  C  C   A TRP   B 41  ? 0.4621 0.3969 0.1706 0.1255 0.0813  0.0400  50  TRP   B C   
664  C  C   B TRP   B 41  ? 0.4605 0.3955 0.1690 0.1250 0.0810  0.0399  50  TRP   B C   
665  C  C   C TRP   B 41  ? 0.4621 0.3969 0.1706 0.1255 0.0813  0.0400  50  TRP   B C   
666  C  C   D TRP   B 41  ? 0.4605 0.3955 0.1690 0.1250 0.0810  0.0399  50  TRP   B C   
667  O  O   A TRP   B 41  ? 0.4698 0.3935 0.1798 0.1173 0.0865  0.0361  50  TRP   B O   
668  O  O   B TRP   B 41  ? 0.4681 0.3923 0.1780 0.1162 0.0860  0.0358  50  TRP   B O   
669  O  O   C TRP   B 41  ? 0.4698 0.3935 0.1798 0.1173 0.0865  0.0361  50  TRP   B O   
670  O  O   D TRP   B 41  ? 0.4681 0.3923 0.1780 0.1162 0.0860  0.0358  50  TRP   B O   
671  C  CB  A TRP   B 41  ? 0.4589 0.3967 0.1534 0.1204 0.0679  0.0324  50  TRP   B CB  
672  C  CB  B TRP   B 41  ? 0.4533 0.3906 0.1473 0.1204 0.0678  0.0320  50  TRP   B CB  
673  C  CB  C TRP   B 41  ? 0.4589 0.3967 0.1534 0.1204 0.0679  0.0324  50  TRP   B CB  
674  C  CB  D TRP   B 41  ? 0.4533 0.3906 0.1473 0.1204 0.0678  0.0320  50  TRP   B CB  
675  C  CG  A TRP   B 41  ? 0.4722 0.4030 0.1628 0.1059 0.0706  0.0259  50  TRP   B CG  
676  C  CG  B TRP   B 41  ? 0.4628 0.3943 0.1536 0.1055 0.0703  0.0262  50  TRP   B CG  
677  C  CG  C TRP   B 41  ? 0.4722 0.4030 0.1628 0.1059 0.0706  0.0259  50  TRP   B CG  
678  C  CG  D TRP   B 41  ? 0.4628 0.3943 0.1536 0.1055 0.0703  0.0262  50  TRP   B CG  
679  C  CD1 A TRP   B 41  ? 0.4885 0.4118 0.1716 0.1005 0.0731  0.0188  50  TRP   B CD1 
680  C  CD1 B TRP   B 41  ? 0.4722 0.4060 0.1669 0.0963 0.0700  0.0267  50  TRP   B CD1 
681  C  CD1 C TRP   B 41  ? 0.4885 0.4118 0.1716 0.1005 0.0731  0.0188  50  TRP   B CD1 
682  C  CD1 D TRP   B 41  ? 0.4722 0.4060 0.1669 0.0963 0.0700  0.0267  50  TRP   B CD1 
683  C  CD2 A TRP   B 41  ? 0.4737 0.4053 0.1677 0.0953 0.0710  0.0254  50  TRP   B CD2 
684  C  CD2 B TRP   B 41  ? 0.4682 0.3914 0.1504 0.0985 0.0727  0.0184  50  TRP   B CD2 
685  C  CD2 C TRP   B 41  ? 0.4737 0.4053 0.1677 0.0953 0.0710  0.0254  50  TRP   B CD2 
686  C  CD2 D TRP   B 41  ? 0.4682 0.3914 0.1504 0.0985 0.0727  0.0184  50  TRP   B CD2 
687  N  NE1 A TRP   B 41  ? 0.4969 0.4147 0.1751 0.0889 0.0751  0.0131  50  TRP   B NE1 
688  N  NE1 B TRP   B 41  ? 0.4809 0.4055 0.1680 0.0849 0.0711  0.0185  50  TRP   B NE1 
689  N  NE1 C TRP   B 41  ? 0.4969 0.4147 0.1751 0.0889 0.0751  0.0131  50  TRP   B NE1 
690  N  NE1 D TRP   B 41  ? 0.4809 0.4055 0.1680 0.0849 0.0711  0.0185  50  TRP   B NE1 
691  C  CE2 A TRP   B 41  ? 0.4904 0.4119 0.1753 0.0850 0.0727  0.0166  50  TRP   B CE2 
692  C  CE2 B TRP   B 41  ? 0.4814 0.4001 0.1597 0.0867 0.0737  0.0135  50  TRP   B CE2 
693  C  CE2 C TRP   B 41  ? 0.4904 0.4119 0.1753 0.0850 0.0727  0.0166  50  TRP   B CE2 
694  C  CE2 D TRP   B 41  ? 0.4814 0.4001 0.1597 0.0867 0.0737  0.0135  50  TRP   B CE2 
695  C  CE3 A TRP   B 41  ? 0.4737 0.4150 0.1782 0.0933 0.0699  0.0314  50  TRP   B CE3 
696  C  CE3 B TRP   B 41  ? 0.4765 0.3972 0.1551 0.1009 0.0745  0.0150  50  TRP   B CE3 
697  C  CE3 C TRP   B 41  ? 0.4737 0.4150 0.1782 0.0933 0.0699  0.0314  50  TRP   B CE3 
698  C  CE3 D TRP   B 41  ? 0.4765 0.3972 0.1551 0.1009 0.0745  0.0150  50  TRP   B CE3 
699  C  CZ2 A TRP   B 41  ? 0.5006 0.4184 0.1851 0.0733 0.0714  0.0123  50  TRP   B CZ2 
700  C  CZ2 B TRP   B 41  ? 0.4945 0.4055 0.1619 0.0792 0.0771  0.0049  50  TRP   B CZ2 
701  C  CZ2 C TRP   B 41  ? 0.5006 0.4184 0.1851 0.0733 0.0714  0.0123  50  TRP   B CZ2 
702  C  CZ2 D TRP   B 41  ? 0.4945 0.4055 0.1619 0.0792 0.0771  0.0049  50  TRP   B CZ2 
703  C  CZ3 A TRP   B 41  ? 0.4859 0.4252 0.1938 0.0799 0.0689  0.0281  50  TRP   B CZ3 
704  C  CZ3 B TRP   B 41  ? 0.4916 0.4077 0.1624 0.0923 0.0792  0.0078  50  TRP   B CZ3 
705  C  CZ3 C TRP   B 41  ? 0.4859 0.4252 0.1938 0.0799 0.0689  0.0281  50  TRP   B CZ3 
706  C  CZ3 D TRP   B 41  ? 0.4916 0.4077 0.1624 0.0923 0.0792  0.0078  50  TRP   B CZ3 
707  C  CH2 A TRP   B 41  ? 0.4957 0.4220 0.1926 0.0702 0.0687  0.0181  50  TRP   B CH2 
708  C  CH2 B TRP   B 41  ? 0.4971 0.4081 0.1607 0.0825 0.0808  0.0026  50  TRP   B CH2 
709  C  CH2 C TRP   B 41  ? 0.4957 0.4220 0.1926 0.0702 0.0687  0.0181  50  TRP   B CH2 
710  C  CH2 D TRP   B 41  ? 0.4971 0.4081 0.1607 0.0825 0.0808  0.0026  50  TRP   B CH2 
711  N  N   . HIS   B 42  ? 0.4547 0.4027 0.1687 0.1301 0.0805  0.0483  51  HIS   B N   
712  C  CA  . HIS   B 42  ? 0.4614 0.4132 0.1861 0.1233 0.0866  0.0548  51  HIS   B CA  
713  C  C   . HIS   B 42  ? 0.4792 0.4172 0.2057 0.1269 0.0960  0.0587  51  HIS   B C   
714  O  O   . HIS   B 42  ? 0.4917 0.4244 0.2261 0.1168 0.1009  0.0622  51  HIS   B O   
715  C  CB  . HIS   B 42  ? 0.4515 0.4255 0.1838 0.1283 0.0851  0.0635  51  HIS   B CB  
716  C  CG  . HIS   B 42  ? 0.4645 0.4443 0.1939 0.1463 0.0892  0.0710  51  HIS   B CG  
717  N  ND1 . HIS   B 42  ? 0.4885 0.4740 0.2090 0.1610 0.0823  0.0693  51  HIS   B ND1 
718  C  CD2 . HIS   B 42  ? 0.4711 0.4508 0.2038 0.1516 0.0990  0.0805  51  HIS   B CD2 
719  C  CE1 . HIS   B 42  ? 0.4862 0.4754 0.2036 0.1758 0.0878  0.0763  51  HIS   B CE1 
720  N  NE2 . HIS   B 42  ? 0.4770 0.4633 0.2009 0.1708 0.0984  0.0839  51  HIS   B NE2 
721  N  N   . VAL   B 43  ? 0.4801 0.4103 0.1992 0.1407 0.0971  0.0578  52  VAL   B N   
722  C  CA  . VAL   B 43  ? 0.4872 0.4024 0.2053 0.1470 0.1043  0.0612  52  VAL   B CA  
723  C  C   . VAL   B 43  ? 0.5058 0.4018 0.2239 0.1375 0.1066  0.0524  52  VAL   B C   
724  O  O   . VAL   B 43  ? 0.5132 0.3961 0.2350 0.1317 0.1120  0.0561  52  VAL   B O   
725  C  CB  . VAL   B 43  ? 0.4937 0.4088 0.2037 0.1662 0.1020  0.0615  52  VAL   B CB  
726  C  CG1 . VAL   B 43  ? 0.5098 0.4073 0.2170 0.1740 0.1071  0.0623  52  VAL   B CG1 
727  C  CG2 . VAL   B 43  ? 0.4877 0.4184 0.1948 0.1782 0.1013  0.0706  52  VAL   B CG2 
728  N  N   . THR   B 44  ? 0.5126 0.4068 0.2266 0.1354 0.1026  0.0410  53  THR   B N   
729  C  CA  . THR   B 44  ? 0.5215 0.4000 0.2337 0.1300 0.1055  0.0309  53  THR   B CA  
730  C  C   . THR   B 44  ? 0.5348 0.4115 0.2448 0.1137 0.1035  0.0227  53  THR   B C   
731  O  O   . THR   B 44  ? 0.5453 0.4070 0.2527 0.1093 0.1064  0.0144  53  THR   B O   
732  C  CB  . THR   B 44  ? 0.5256 0.4048 0.2353 0.1403 0.1046  0.0236  53  THR   B CB  
733  O  OG1 . THR   B 44  ? 0.5355 0.4271 0.2424 0.1353 0.0996  0.0189  53  THR   B OG1 
734  C  CG2 . THR   B 44  ? 0.5236 0.4051 0.2338 0.1575 0.1037  0.0298  53  THR   B CG2 
735  N  N   . LYS   B 45  ? 0.5335 0.4245 0.2431 0.1065 0.0977  0.0243  54  LYS   B N   
736  C  CA  . LYS   B 45  ? 0.5556 0.4471 0.2601 0.0925 0.0934  0.0170  54  LYS   B CA  
737  C  C   . LYS   B 45  ? 0.5679 0.4542 0.2616 0.0917 0.0946  0.0059  54  LYS   B C   
738  O  O   . LYS   B 45  ? 0.5671 0.4465 0.2533 0.0820 0.0941  -0.0025 54  LYS   B O   
739  C  CB  . LYS   B 45  ? 0.5846 0.4660 0.2938 0.0802 0.0938  0.0157  54  LYS   B CB  
740  C  CG  . LYS   B 45  ? 0.6425 0.5295 0.3652 0.0793 0.0954  0.0279  54  LYS   B CG  
741  C  CD  . LYS   B 45  ? 0.7029 0.6134 0.4317 0.0772 0.0895  0.0345  54  LYS   B CD  
742  C  CE  . LYS   B 45  ? 0.7598 0.6791 0.5041 0.0757 0.0935  0.0470  54  LYS   B CE  
743  N  NZ  . LYS   B 45  ? 0.7894 0.7334 0.5385 0.0852 0.0920  0.0560  54  LYS   B NZ  
744  N  N   . GLY   B 46  ? 0.5737 0.4646 0.2673 0.1020 0.0962  0.0059  55  GLY   B N   
745  C  CA  . GLY   B 46  ? 0.5833 0.4743 0.2708 0.1019 0.0991  -0.0028 55  GLY   B CA  
746  C  C   . GLY   B 46  ? 0.6002 0.4793 0.2889 0.1063 0.1068  -0.0111 55  GLY   B C   
747  O  O   . GLY   B 46  ? 0.6026 0.4844 0.2877 0.1067 0.1111  -0.0191 55  GLY   B O   
748  N  N   . ALA   B 47  ? 0.6110 0.4768 0.3048 0.1100 0.1091  -0.0091 56  ALA   B N   
749  C  CA  . ALA   B 47  ? 0.6251 0.4754 0.3189 0.1157 0.1151  -0.0173 56  ALA   B CA  
750  C  C   . ALA   B 47  ? 0.6280 0.4832 0.3286 0.1307 0.1181  -0.0183 56  ALA   B C   
751  O  O   . ALA   B 47  ? 0.6216 0.4865 0.3281 0.1382 0.1149  -0.0101 56  ALA   B O   
752  C  CB  . ALA   B 47  ? 0.6307 0.4616 0.3270 0.1141 0.1154  -0.0133 56  ALA   B CB  
753  N  N   . ALA   B 48  ? 0.6337 0.4826 0.3338 0.1361 0.1236  -0.0292 57  ALA   B N   
754  C  CA  . ALA   B 48  ? 0.6375 0.4926 0.3468 0.1510 0.1263  -0.0323 57  ALA   B CA  
755  C  C   . ALA   B 48  ? 0.6516 0.4942 0.3656 0.1634 0.1242  -0.0243 57  ALA   B C   
756  O  O   . ALA   B 48  ? 0.6625 0.4860 0.3721 0.1603 0.1239  -0.0193 57  ALA   B O   
757  C  CB  . ALA   B 48  ? 0.6393 0.4904 0.3468 0.1548 0.1332  -0.0464 57  ALA   B CB  
758  N  N   . LEU   B 49  ? 0.6498 0.5033 0.3725 0.1766 0.1222  -0.0224 58  LEU   B N   
759  C  CA  . LEU   B 49  ? 0.6701 0.5132 0.3943 0.1906 0.1194  -0.0143 58  LEU   B CA  
760  C  C   . LEU   B 49  ? 0.6966 0.5355 0.4274 0.2070 0.1209  -0.0219 58  LEU   B C   
761  O  O   . LEU   B 49  ? 0.6976 0.5490 0.4356 0.2083 0.1241  -0.0332 58  LEU   B O   
762  C  CB  . LEU   B 49  ? 0.6579 0.5165 0.3845 0.1949 0.1129  -0.0053 58  LEU   B CB  
763  C  CG  . LEU   B 49  ? 0.6645 0.5302 0.3858 0.1823 0.1103  0.0019  58  LEU   B CG  
764  C  CD1 . LEU   B 49  ? 0.6619 0.5432 0.3856 0.1885 0.1030  0.0063  58  LEU   B CD1 
765  C  CD2 . LEU   B 49  ? 0.6790 0.5306 0.3941 0.1789 0.1120  0.0120  58  LEU   B CD2 
766  N  N   . ARG   B 50  ? 0.7167 0.5386 0.4448 0.2201 0.1189  -0.0154 59  ARG   B N   
767  C  CA  . ARG   B 50  ? 0.7379 0.5542 0.4715 0.2383 0.1184  -0.0217 59  ARG   B CA  
768  C  C   . ARG   B 50  ? 0.7473 0.5717 0.4838 0.2538 0.1108  -0.0140 59  ARG   B C   
769  O  O   . ARG   B 50  ? 0.7459 0.5640 0.4733 0.2537 0.1082  -0.0014 59  ARG   B O   
770  C  CB  . ARG   B 50  ? 0.7805 0.5628 0.5048 0.2414 0.1213  -0.0213 59  ARG   B CB  
771  C  CG  . ARG   B 50  ? 0.8531 0.6218 0.5790 0.2634 0.1187  -0.0234 59  ARG   B CG  
772  C  CD  . ARG   B 50  ? 0.9288 0.6615 0.6458 0.2657 0.1214  -0.0266 59  ARG   B CD  
773  N  NE  . ARG   B 50  ? 0.9915 0.6990 0.6966 0.2522 0.1224  -0.0137 59  ARG   B NE  
774  C  CZ  . ARG   B 50  ? 1.0397 0.7287 0.7367 0.2577 0.1204  0.0023  59  ARG   B CZ  
775  N  NH1 . ARG   B 50  ? 1.0370 0.7280 0.7333 0.2778 0.1160  0.0070  59  ARG   B NH1 
776  N  NH2 . ARG   B 50  ? 1.0537 0.7236 0.7434 0.2430 0.1227  0.0141  59  ARG   B NH2 
777  N  N   . SER   B 51  ? 0.7560 0.5969 0.5056 0.2670 0.1072  -0.0220 60  SER   B N   
778  C  CA  . SER   B 51  ? 0.7767 0.6256 0.5290 0.2828 0.0977  -0.0170 60  SER   B CA  
779  C  C   . SER   B 51  ? 0.8044 0.6458 0.5624 0.3034 0.0953  -0.0230 60  SER   B C   
780  O  O   . SER   B 51  ? 0.7995 0.6631 0.5759 0.3106 0.0929  -0.0339 60  SER   B O   
781  C  CB  . SER   B 51  ? 0.7778 0.6581 0.5445 0.2782 0.0924  -0.0218 60  SER   B CB  
782  O  OG  . SER   B 51  ? 0.8069 0.6941 0.5754 0.2931 0.0811  -0.0185 60  SER   B OG  
783  N  N   . GLY   B 52  ? 0.8284 0.6388 0.5718 0.3123 0.0961  -0.0158 61  GLY   B N   
784  C  CA  . GLY   B 52  ? 0.8479 0.6454 0.5939 0.3328 0.0933  -0.0210 61  GLY   B CA  
785  C  C   . GLY   B 52  ? 0.8618 0.6560 0.6152 0.3289 0.1012  -0.0349 61  GLY   B C   
786  O  O   . GLY   B 52  ? 0.8832 0.6526 0.6247 0.3181 0.1075  -0.0333 61  GLY   B O   
787  N  N   . GLU   B 53  ? 0.8453 0.6665 0.6190 0.3366 0.1011  -0.0490 62  GLU   B N   
788  C  CA  . GLU   B 53  ? 0.8439 0.6674 0.6241 0.3339 0.1101  -0.0636 62  GLU   B CA  
789  C  C   . GLU   B 53  ? 0.8185 0.6718 0.6079 0.3135 0.1174  -0.0697 62  GLU   B C   
790  O  O   . GLU   B 53  ? 0.8240 0.6747 0.6104 0.3057 0.1263  -0.0791 62  GLU   B O   
791  C  CB  . GLU   B 53  ? 0.8800 0.7138 0.6764 0.3572 0.1079  -0.0760 62  GLU   B CB  
792  C  CG  . GLU   B 53  ? 0.9717 0.7882 0.7641 0.3618 0.1159  -0.0889 62  GLU   B CG  
793  C  CD  . GLU   B 53  ? 1.0761 0.9125 0.8886 0.3837 0.1163  -0.1042 62  GLU   B CD  
794  O  OE1 . GLU   B 53  ? 1.0976 0.9466 0.9230 0.4016 0.1069  -0.1027 62  GLU   B OE1 
795  O  OE2 . GLU   B 53  ? 1.1078 0.9483 0.9228 0.3840 0.1257  -0.1184 62  GLU   B OE2 
796  N  N   . GLY   B 54  ? 0.7896 0.6684 0.5877 0.3056 0.1130  -0.0642 63  GLY   B N   
797  C  CA  . GLY   B 54  ? 0.7660 0.6710 0.5716 0.2863 0.1184  -0.0673 63  GLY   B CA  
798  C  C   . GLY   B 54  ? 0.7543 0.6435 0.5411 0.2661 0.1231  -0.0615 63  GLY   B C   
799  O  O   . GLY   B 54  ? 0.7751 0.6350 0.5452 0.2650 0.1218  -0.0537 63  GLY   B O   
800  N  N   . ARG   B 55  ? 0.7165 0.6258 0.5066 0.2495 0.1284  -0.0646 64  ARG   B N   
801  C  CA  . ARG   B 55  ? 0.7007 0.5983 0.4738 0.2306 0.1315  -0.0600 64  ARG   B CA  
802  C  C   . ARG   B 55  ? 0.6543 0.5727 0.4306 0.2162 0.1285  -0.0540 64  ARG   B C   
803  O  O   . ARG   B 55  ? 0.6396 0.5837 0.4297 0.2129 0.1308  -0.0586 64  ARG   B O   
804  C  CB  . ARG   B 55  ? 0.7240 0.6166 0.4897 0.2248 0.1415  -0.0715 64  ARG   B CB  
805  C  CG  . ARG   B 55  ? 0.7807 0.6612 0.5286 0.2059 0.1431  -0.0684 64  ARG   B CG  
806  C  CD  . ARG   B 55  ? 0.8323 0.7093 0.5709 0.2018 0.1520  -0.0816 64  ARG   B CD  
807  N  NE  . ARG   B 55  ? 0.8780 0.7464 0.5995 0.1836 0.1518  -0.0794 64  ARG   B NE  
808  C  CZ  . ARG   B 55  ? 0.9152 0.7622 0.6208 0.1790 0.1540  -0.0873 64  ARG   B CZ  
809  N  NH1 . ARG   B 55  ? 0.9199 0.7492 0.6233 0.1917 0.1569  -0.0983 64  ARG   B NH1 
810  N  NH2 . ARG   B 55  ? 0.9108 0.7528 0.6025 0.1626 0.1518  -0.0851 64  ARG   B NH2 
811  N  N   . LEU   B 56  ? 0.6323 0.5396 0.3967 0.2078 0.1234  -0.0433 65  LEU   B N   
812  C  CA  . LEU   B 56  ? 0.6066 0.5285 0.3711 0.1952 0.1193  -0.0376 65  LEU   B CA  
813  C  C   . LEU   B 56  ? 0.5880 0.5053 0.3389 0.1779 0.1245  -0.0383 65  LEU   B C   
814  O  O   . LEU   B 56  ? 0.5954 0.4938 0.3337 0.1735 0.1245  -0.0349 65  LEU   B O   
815  C  CB  . LEU   B 56  ? 0.6113 0.5264 0.3705 0.1991 0.1097  -0.0261 65  LEU   B CB  
816  C  CG  . LEU   B 56  ? 0.6301 0.5446 0.3958 0.2176 0.1023  -0.0235 65  LEU   B CG  
817  C  CD1 . LEU   B 56  ? 0.6345 0.5497 0.3940 0.2190 0.0931  -0.0142 65  LEU   B CD1 
818  C  CD2 . LEU   B 56  ? 0.6289 0.5643 0.4145 0.2253 0.1001  -0.0319 65  LEU   B CD2 
819  N  N   . ASP   B 57  ? 0.5609 0.4956 0.3146 0.1677 0.1286  -0.0423 66  ASP   B N   
820  C  CA  . ASP   B 57  ? 0.5585 0.4895 0.2966 0.1520 0.1324  -0.0428 66  ASP   B CA  
821  C  C   . ASP   B 57  ? 0.5278 0.4654 0.2624 0.1414 0.1249  -0.0333 66  ASP   B C   
822  O  O   . ASP   B 57  ? 0.5185 0.4697 0.2648 0.1429 0.1204  -0.0302 66  ASP   B O   
823  C  CB  . ASP   B 57  ? 0.6030 0.5465 0.3412 0.1485 0.1433  -0.0530 66  ASP   B CB  
824  C  CG  . ASP   B 57  ? 0.7093 0.6422 0.4468 0.1598 0.1500  -0.0640 66  ASP   B CG  
825  O  OD1 . ASP   B 57  ? 0.7487 0.6576 0.4729 0.1593 0.1486  -0.0652 66  ASP   B OD1 
826  O  OD2 . ASP   B 57  ? 0.7363 0.6847 0.4878 0.1695 0.1561  -0.0715 66  ASP   B OD2 
827  N  N   . PRO   B 58  ? 0.5146 0.4416 0.2338 0.1314 0.1220  -0.0289 67  PRO   B N   
828  C  CA  . PRO   B 58  ? 0.4971 0.4291 0.2120 0.1232 0.1141  -0.0205 67  PRO   B CA  
829  C  C   . PRO   B 58  ? 0.4838 0.4303 0.1997 0.1138 0.1164  -0.0209 67  PRO   B C   
830  O  O   . PRO   B 58  ? 0.4892 0.4426 0.2040 0.1102 0.1263  -0.0277 67  PRO   B O   
831  C  CB  . PRO   B 58  ? 0.5134 0.4334 0.2130 0.1147 0.1119  -0.0181 67  PRO   B CB  
832  C  CG  . PRO   B 58  ? 0.5315 0.4432 0.2245 0.1129 0.1202  -0.0275 67  PRO   B CG  
833  C  CD  . PRO   B 58  ? 0.5162 0.4271 0.2220 0.1264 0.1250  -0.0326 67  PRO   B CD  
834  N  N   . TYR   B 59  ? 0.4593 0.4099 0.1771 0.1102 0.1078  -0.0136 68  TYR   B N   
835  C  CA  . TYR   B 59  ? 0.4358 0.3976 0.1551 0.0996 0.1088  -0.0114 68  TYR   B CA  
836  C  C   . TYR   B 59  ? 0.4341 0.3876 0.1375 0.0898 0.1003  -0.0032 68  TYR   B C   
837  O  O   . TYR   B 59  ? 0.4386 0.3945 0.1321 0.0780 0.1035  -0.0009 68  TYR   B O   
838  C  CB  . TYR   B 59  ? 0.4157 0.3893 0.1565 0.1051 0.1042  -0.0108 68  TYR   B CB  
839  C  CG  . TYR   B 59  ? 0.3982 0.3840 0.1457 0.0927 0.1049  -0.0074 68  TYR   B CG  
840  C  CD1 . TYR   B 59  ? 0.4106 0.3884 0.1501 0.0841 0.0945  0.0011  68  TYR   B CD1 
841  C  CD2 . TYR   B 59  ? 0.3777 0.3833 0.1421 0.0905 0.1152  -0.0121 68  TYR   B CD2 
842  C  CE1 . TYR   B 59  ? 0.4099 0.3958 0.1555 0.0711 0.0948  0.0059  68  TYR   B CE1 
843  C  CE2 . TYR   B 59  ? 0.3766 0.3952 0.1504 0.0775 0.1165  -0.0073 68  TYR   B CE2 
844  C  CZ  . TYR   B 59  ? 0.4028 0.4098 0.1666 0.0669 0.1061  0.0023  68  TYR   B CZ  
845  O  OH  . TYR   B 59  ? 0.4215 0.4380 0.1935 0.0521 0.1073  0.0087  68  TYR   B OH  
846  N  N   . TRP   B 60  ? 0.4328 0.3771 0.1333 0.0959 0.0895  0.0015  69  TRP   B N   
847  C  CA  . TRP   B 60  ? 0.4306 0.3673 0.1176 0.0903 0.0796  0.0086  69  TRP   B CA  
848  C  C   . TRP   B 60  ? 0.4438 0.3737 0.1263 0.0978 0.0746  0.0103  69  TRP   B C   
849  O  O   . TRP   B 60  ? 0.4285 0.3586 0.1203 0.1091 0.0746  0.0094  69  TRP   B O   
850  C  CB  . TRP   B 60  ? 0.4165 0.3529 0.1100 0.0912 0.0690  0.0136  69  TRP   B CB  
851  C  CG  . TRP   B 60  ? 0.4226 0.3487 0.1024 0.0895 0.0571  0.0202  69  TRP   B CG  
852  C  CD1 . TRP   B 60  ? 0.4430 0.3632 0.1072 0.0780 0.0547  0.0250  69  TRP   B CD1 
853  C  CD2 . TRP   B 60  ? 0.4231 0.3439 0.1015 0.1014 0.0466  0.0226  69  TRP   B CD2 
854  N  NE1 . TRP   B 60  ? 0.4531 0.3641 0.1078 0.0825 0.0421  0.0298  69  TRP   B NE1 
855  C  CE2 . TRP   B 60  ? 0.4402 0.3528 0.1041 0.0970 0.0375  0.0280  69  TRP   B CE2 
856  C  CE3 . TRP   B 60  ? 0.4216 0.3442 0.1083 0.1164 0.0444  0.0209  69  TRP   B CE3 
857  C  CZ2 . TRP   B 60  ? 0.4476 0.3559 0.1074 0.1078 0.0266  0.0307  69  TRP   B CZ2 
858  C  CZ3 . TRP   B 60  ? 0.4288 0.3477 0.1098 0.1262 0.0350  0.0243  69  TRP   B CZ3 
859  C  CH2 . TRP   B 60  ? 0.4418 0.3546 0.1107 0.1223 0.0262  0.0286  69  TRP   B CH2 
860  N  N   . GLY   B 61  ? 0.4616 0.3868 0.1303 0.0916 0.0701  0.0136  70  GLY   B N   
861  C  CA  . GLY   B 61  ? 0.4758 0.3991 0.1435 0.0971 0.0656  0.0160  70  GLY   B CA  
862  C  C   . GLY   B 61  ? 0.4889 0.4100 0.1439 0.0917 0.0566  0.0204  70  GLY   B C   
863  O  O   . GLY   B 61  ? 0.4909 0.4089 0.1333 0.0817 0.0559  0.0208  70  GLY   B O   
864  N  N   . ASP   B 62  ? 0.4905 0.4143 0.1485 0.0992 0.0501  0.0242  71  ASP   B N   
865  C  CA  . ASP   B 62  ? 0.5040 0.4282 0.1526 0.0968 0.0402  0.0281  71  ASP   B CA  
866  C  C   . ASP   B 62  ? 0.5000 0.4333 0.1574 0.1041 0.0382  0.0305  71  ASP   B C   
867  O  O   . ASP   B 62  ? 0.5016 0.4389 0.1666 0.1164 0.0367  0.0333  71  ASP   B O   
868  C  CB  . ASP   B 62  ? 0.5388 0.4571 0.1813 0.1008 0.0296  0.0324  71  ASP   B CB  
869  C  CG  . ASP   B 62  ? 0.6494 0.5645 0.2788 0.0982 0.0185  0.0363  71  ASP   B CG  
870  O  OD1 . ASP   B 62  ? 0.6686 0.5912 0.3014 0.1054 0.0129  0.0379  71  ASP   B OD1 
871  O  OD2 . ASP   B 62  ? 0.7137 0.6194 0.3297 0.0897 0.0152  0.0385  71  ASP   B OD2 
872  N  N   . VAL   B 63  ? 0.4948 0.4323 0.1514 0.0965 0.0380  0.0295  72  VAL   B N   
873  C  CA  . VAL   B 63  ? 0.4850 0.4346 0.1534 0.1000 0.0372  0.0324  72  VAL   B CA  
874  C  C   . VAL   B 63  ? 0.4840 0.4431 0.1534 0.1108 0.0269  0.0377  72  VAL   B C   
875  O  O   . VAL   B 63  ? 0.4851 0.4562 0.1664 0.1201 0.0288  0.0415  72  VAL   B O   
876  C  CB  . VAL   B 63  ? 0.4950 0.4459 0.1624 0.0865 0.0371  0.0285  72  VAL   B CB  
877  C  CG1 . VAL   B 63  ? 0.4895 0.4567 0.1698 0.0870 0.0321  0.0322  72  VAL   B CG1 
878  C  CG2 . VAL   B 63  ? 0.5046 0.4466 0.1746 0.0799 0.0479  0.0229  72  VAL   B CG2 
879  N  N   . LYS   B 64  ? 0.4891 0.4421 0.1454 0.1109 0.0163  0.0384  73  LYS   B N   
880  C  CA  . LYS   B 64  ? 0.4902 0.4494 0.1458 0.1232 0.0051  0.0423  73  LYS   B CA  
881  C  C   . LYS   B 64  ? 0.4902 0.4482 0.1498 0.1387 0.0062  0.0437  73  LYS   B C   
882  O  O   . LYS   B 64  ? 0.4838 0.4552 0.1517 0.1517 0.0055  0.0461  73  LYS   B O   
883  C  CB  . LYS   B 64  ? 0.5227 0.4691 0.1601 0.1196 -0.0069 0.0432  73  LYS   B CB  
884  C  CG  . LYS   B 64  ? 0.5705 0.5183 0.2045 0.1337 -0.0204 0.0463  73  LYS   B CG  
885  C  CD  . LYS   B 64  ? 0.6066 0.5702 0.2446 0.1346 -0.0279 0.0472  73  LYS   B CD  
886  C  CE  . LYS   B 64  ? 0.6522 0.6131 0.2826 0.1487 -0.0431 0.0496  73  LYS   B CE  
887  N  NZ  . LYS   B 64  ? 0.7107 0.6462 0.3185 0.1429 -0.0526 0.0515  73  LYS   B NZ  
888  N  N   . GLN   B 65  ? 0.4831 0.4270 0.1378 0.1374 0.0086  0.0417  74  GLN   B N   
889  C  CA  . GLN   B 65  ? 0.4614 0.4028 0.1190 0.1514 0.0082  0.0414  74  GLN   B CA  
890  C  C   . GLN   B 65  ? 0.4369 0.3879 0.1062 0.1568 0.0200  0.0418  74  GLN   B C   
891  O  O   . GLN   B 65  ? 0.4351 0.3876 0.1056 0.1715 0.0195  0.0424  74  GLN   B O   
892  C  CB  . GLN   B 65  ? 0.4913 0.4169 0.1433 0.1469 0.0057  0.0391  74  GLN   B CB  
893  C  CG  . GLN   B 65  ? 0.5544 0.4669 0.1932 0.1397 -0.0052 0.0408  74  GLN   B CG  
894  C  CD  . GLN   B 65  ? 0.6347 0.5340 0.2721 0.1336 -0.0063 0.0397  74  GLN   B CD  
895  O  OE1 . GLN   B 65  ? 0.6552 0.5521 0.2989 0.1423 -0.0082 0.0373  74  GLN   B OE1 
896  N  NE2 . GLN   B 65  ? 0.6599 0.5515 0.2890 0.1183 -0.0053 0.0416  74  GLN   B NE2 
897  N  N   . ASP   B 66  ? 0.4159 0.3711 0.0917 0.1454 0.0299  0.0415  75  ASP   B N   
898  C  CA  . ASP   B 66  ? 0.4075 0.3672 0.0931 0.1473 0.0414  0.0429  75  ASP   B CA  
899  C  C   . ASP   B 66  ? 0.4018 0.3517 0.0866 0.1533 0.0448  0.0402  75  ASP   B C   
900  O  O   . ASP   B 66  ? 0.3914 0.3438 0.0800 0.1640 0.0498  0.0428  75  ASP   B O   
901  C  CB  . ASP   B 66  ? 0.4097 0.3855 0.1031 0.1582 0.0436  0.0491  75  ASP   B CB  
902  C  CG  . ASP   B 66  ? 0.4589 0.4379 0.1621 0.1556 0.0561  0.0529  75  ASP   B CG  
903  O  OD1 . ASP   B 66  ? 0.4580 0.4272 0.1630 0.1431 0.0615  0.0496  75  ASP   B OD1 
904  O  OD2 . ASP   B 66  ? 0.4869 0.4769 0.1947 0.1666 0.0607  0.0592  75  ASP   B OD2 
905  N  N   . LEU   B 67  ? 0.3980 0.3381 0.0787 0.1458 0.0432  0.0354  76  LEU   B N   
906  C  CA  . LEU   B 67  ? 0.3929 0.3271 0.0767 0.1511 0.0456  0.0321  76  LEU   B CA  
907  C  C   . LEU   B 67  ? 0.3947 0.3247 0.0810 0.1392 0.0533  0.0271  76  LEU   B C   
908  O  O   . LEU   B 67  ? 0.3952 0.3239 0.0761 0.1266 0.0541  0.0257  76  LEU   B O   
909  C  CB  . LEU   B 67  ? 0.3921 0.3213 0.0715 0.1572 0.0341  0.0310  76  LEU   B CB  
910  C  CG  . LEU   B 67  ? 0.3974 0.3288 0.0725 0.1734 0.0255  0.0336  76  LEU   B CG  
911  C  CD1 . LEU   B 67  ? 0.4047 0.3264 0.0742 0.1766 0.0121  0.0312  76  LEU   B CD1 
912  C  CD2 . LEU   B 67  ? 0.4013 0.3367 0.0796 0.1883 0.0307  0.0347  76  LEU   B CD2 
913  N  N   . VAL   B 68  ? 0.3961 0.3243 0.0892 0.1444 0.0585  0.0239  77  VAL   B N   
914  C  CA  . VAL   B 68  ? 0.4059 0.3324 0.1029 0.1362 0.0667  0.0179  77  VAL   B CA  
915  C  C   . VAL   B 68  ? 0.4160 0.3439 0.1226 0.1450 0.0672  0.0143  77  VAL   B C   
916  O  O   . VAL   B 68  ? 0.4370 0.3642 0.1466 0.1585 0.0654  0.0160  77  VAL   B O   
917  C  CB  . VAL   B 68  ? 0.4135 0.3363 0.1105 0.1314 0.0760  0.0166  77  VAL   B CB  
918  C  CG1 . VAL   B 68  ? 0.4237 0.3442 0.1253 0.1427 0.0788  0.0208  77  VAL   B CG1 
919  C  CG2 . VAL   B 68  ? 0.4150 0.3352 0.1134 0.1249 0.0843  0.0088  77  VAL   B CG2 
920  N  N   . SER   B 69  ? 0.4037 0.3355 0.1154 0.1378 0.0692  0.0096  78  SER   B N   
921  C  CA  . SER   B 69  ? 0.3941 0.3314 0.1191 0.1452 0.0690  0.0053  78  SER   B CA  
922  C  C   . SER   B 69  ? 0.3835 0.3251 0.1155 0.1417 0.0808  -0.0013 78  SER   B C   
923  O  O   . SER   B 69  ? 0.3751 0.3166 0.1007 0.1303 0.0879  -0.0033 78  SER   B O   
924  C  CB  . SER   B 69  ? 0.4089 0.3503 0.1390 0.1413 0.0598  0.0057  78  SER   B CB  
925  O  OG  . SER   B 69  ? 0.4457 0.3914 0.1753 0.1256 0.0650  0.0050  78  SER   B OG  
926  N  N   . TYR   B 70  ? 0.3802 0.3250 0.1238 0.1534 0.0824  -0.0052 79  TYR   B N   
927  C  CA  . TYR   B 70  ? 0.3813 0.3299 0.1325 0.1547 0.0928  -0.0126 79  TYR   B CA  
928  C  C   . TYR   B 70  ? 0.3763 0.3414 0.1466 0.1577 0.0917  -0.0176 79  TYR   B C   
929  O  O   . TYR   B 70  ? 0.3679 0.3359 0.1461 0.1663 0.0817  -0.0162 79  TYR   B O   
930  C  CB  . TYR   B 70  ? 0.3809 0.3177 0.1302 0.1679 0.0953  -0.0127 79  TYR   B CB  
931  C  CG  . TYR   B 70  ? 0.3957 0.3181 0.1306 0.1629 0.0980  -0.0081 79  TYR   B CG  
932  C  CD1 . TYR   B 70  ? 0.4036 0.3225 0.1309 0.1633 0.0916  0.0004  79  TYR   B CD1 
933  C  CD2 . TYR   B 70  ? 0.4165 0.3299 0.1466 0.1578 0.1065  -0.0128 79  TYR   B CD2 
934  C  CE1 . TYR   B 70  ? 0.4236 0.3339 0.1420 0.1571 0.0940  0.0048  79  TYR   B CE1 
935  C  CE2 . TYR   B 70  ? 0.4371 0.3385 0.1569 0.1508 0.1075  -0.0091 79  TYR   B CE2 
936  C  CZ  . TYR   B 70  ? 0.4533 0.3549 0.1689 0.1499 0.1015  0.0002  79  TYR   B CZ  
937  O  OH  . TYR   B 70  ? 0.4919 0.3855 0.2015 0.1422 0.1025  0.0041  79  TYR   B OH  
938  N  N   . CYS   B 71  ? 0.3747 0.3519 0.1529 0.1512 0.1019  -0.0238 80  CYS   B N   
939  C  CA  . CYS   B 71  ? 0.3813 0.3796 0.1824 0.1532 0.1028  -0.0288 80  CYS   B CA  
940  C  C   . CYS   B 71  ? 0.3703 0.3802 0.1788 0.1395 0.0979  -0.0247 80  CYS   B C   
941  O  O   . CYS   B 71  ? 0.3663 0.3971 0.1942 0.1350 0.1025  -0.0281 80  CYS   B O   
942  C  CB  . CYS   B 71  ? 0.4230 0.4234 0.2378 0.1714 0.0951  -0.0316 80  CYS   B CB  
943  S  SG  . CYS   B 71  ? 0.5637 0.5478 0.3707 0.1883 0.1007  -0.0353 80  CYS   B SG  
944  N  N   . GLY   B 72  ? 0.3638 0.3609 0.1584 0.1331 0.0888  -0.0173 81  GLY   B N   
945  C  CA  . GLY   B 72  ? 0.3529 0.3552 0.1518 0.1195 0.0829  -0.0124 81  GLY   B CA  
946  C  C   . GLY   B 72  ? 0.3659 0.3500 0.1449 0.1151 0.0731  -0.0050 81  GLY   B C   
947  O  O   . GLY   B 72  ? 0.3698 0.3407 0.1333 0.1219 0.0718  -0.0035 81  GLY   B O   
948  N  N   . PRO   B 73  ? 0.3729 0.3563 0.1532 0.1032 0.0661  0.0001  82  PRO   B N   
949  C  CA  . PRO   B 73  ? 0.3897 0.3547 0.1510 0.1007 0.0550  0.0067  82  PRO   B CA  
950  C  C   . PRO   B 73  ? 0.4054 0.3603 0.1650 0.1169 0.0408  0.0059  82  PRO   B C   
951  O  O   . PRO   B 73  ? 0.4045 0.3660 0.1789 0.1275 0.0362  0.0010  82  PRO   B O   
952  C  CB  . PRO   B 73  ? 0.3970 0.3623 0.1629 0.0847 0.0502  0.0121  82  PRO   B CB  
953  C  CG  . PRO   B 73  ? 0.3850 0.3701 0.1791 0.0833 0.0527  0.0075  82  PRO   B CG  
954  C  CD  . PRO   B 73  ? 0.3541 0.3533 0.1542 0.0912 0.0675  0.0005  82  PRO   B CD  
955  N  N   . TRP   B 74  ? 0.4133 0.3533 0.1543 0.1197 0.0330  0.0105  83  TRP   B N   
956  C  CA  . TRP   B 74  ? 0.4234 0.3542 0.1588 0.1358 0.0202  0.0101  83  TRP   B CA  
957  C  C   . TRP   B 74  ? 0.4407 0.3699 0.1880 0.1383 0.0059  0.0072  83  TRP   B C   
958  O  O   . TRP   B 74  ? 0.4406 0.3677 0.1931 0.1243 0.0015  0.0095  83  TRP   B O   
959  C  CB  . TRP   B 74  ? 0.4269 0.3452 0.1427 0.1359 0.0143  0.0155  83  TRP   B CB  
960  C  CG  . TRP   B 74  ? 0.4238 0.3364 0.1317 0.1544 0.0055  0.0151  83  TRP   B CG  
961  C  CD1 . TRP   B 74  ? 0.4329 0.3358 0.1367 0.1640 -0.0103 0.0138  83  TRP   B CD1 
962  C  CD2 . TRP   B 74  ? 0.4244 0.3407 0.1264 0.1658 0.0125  0.0163  83  TRP   B CD2 
963  N  NE1 . TRP   B 74  ? 0.4398 0.3420 0.1339 0.1821 -0.0126 0.0137  83  TRP   B NE1 
964  C  CE2 . TRP   B 74  ? 0.4378 0.3492 0.1320 0.1827 0.0019  0.0162  83  TRP   B CE2 
965  C  CE3 . TRP   B 74  ? 0.4236 0.3461 0.1262 0.1630 0.0265  0.0174  83  TRP   B CE3 
966  C  CZ2 . TRP   B 74  ? 0.4484 0.3638 0.1361 0.1964 0.0068  0.0187  83  TRP   B CZ2 
967  C  CZ3 . TRP   B 74  ? 0.4348 0.3588 0.1326 0.1749 0.0299  0.0200  83  TRP   B CZ3 
968  C  CH2 . TRP   B 74  ? 0.4446 0.3665 0.1354 0.1911 0.0212  0.0214  83  TRP   B CH2 
969  N  N   . LYS   B 75  ? 0.4553 0.3857 0.2072 0.1555 -0.0011 0.0024  84  LYS   B N   
970  C  CA  . LYS   B 75  ? 0.4637 0.3933 0.2278 0.1603 -0.0164 -0.0026 84  LYS   B CA  
971  C  C   . LYS   B 75  ? 0.4958 0.4094 0.2445 0.1757 -0.0333 -0.0041 84  LYS   B C   
972  O  O   . LYS   B 75  ? 0.4993 0.4062 0.2539 0.1768 -0.0494 -0.0082 84  LYS   B O   
973  C  CB  . LYS   B 75  ? 0.4564 0.4005 0.2370 0.1706 -0.0132 -0.0088 84  LYS   B CB  
974  C  CG  . LYS   B 75  ? 0.4569 0.4187 0.2551 0.1588 0.0024  -0.0097 84  LYS   B CG  
975  C  CD  . LYS   B 75  ? 0.4748 0.4459 0.2927 0.1410 -0.0006 -0.0098 84  LYS   B CD  
976  C  CE  . LYS   B 75  ? 0.4964 0.4902 0.3343 0.1331 0.0152  -0.0122 84  LYS   B CE  
977  N  NZ  . LYS   B 75  ? 0.5229 0.5281 0.3788 0.1126 0.0163  -0.0096 84  LYS   B NZ  
978  N  N   . LEU   B 76  ? 0.5178 0.4265 0.2479 0.1885 -0.0297 -0.0014 85  LEU   B N   
979  C  CA  . LEU   B 76  ? 0.5388 0.4358 0.2525 0.2068 -0.0432 -0.0032 85  LEU   B CA  
980  C  C   . LEU   B 76  ? 0.5736 0.4551 0.2762 0.2012 -0.0543 -0.0011 85  LEU   B C   
981  O  O   . LEU   B 76  ? 0.5793 0.4596 0.2733 0.1942 -0.0470 0.0048  85  LEU   B O   
982  C  CB  . LEU   B 76  ? 0.5355 0.4367 0.2354 0.2217 -0.0330 0.0003  85  LEU   B CB  
983  C  CG  . LEU   B 76  ? 0.5436 0.4563 0.2511 0.2239 -0.0184 0.0014  85  LEU   B CG  
984  C  CD1 . LEU   B 76  ? 0.5577 0.4718 0.2513 0.2348 -0.0087 0.0073  85  LEU   B CD1 
985  C  CD2 . LEU   B 76  ? 0.5445 0.4603 0.2611 0.2349 -0.0257 -0.0050 85  LEU   B CD2 
986  N  N   . ASP   B 77  ? 0.5947 0.4628 0.2972 0.2048 -0.0732 -0.0064 86  ASP   B N   
987  C  CA  . ASP   B 77  ? 0.6311 0.4799 0.3229 0.1997 -0.0857 -0.0047 86  ASP   B CA  
988  C  C   . ASP   B 77  ? 0.6608 0.4927 0.3351 0.2213 -0.1043 -0.0111 86  ASP   B C   
989  O  O   . ASP   B 77  ? 0.6808 0.4927 0.3459 0.2191 -0.1179 -0.0111 86  ASP   B O   
990  C  CB  . ASP   B 77  ? 0.6543 0.4970 0.3621 0.1772 -0.0917 -0.0034 86  ASP   B CB  
991  C  CG  . ASP   B 77  ? 0.7195 0.5618 0.4442 0.1784 -0.1055 -0.0116 86  ASP   B CG  
992  O  OD1 . ASP   B 77  ? 0.7236 0.5731 0.4481 0.1965 -0.1082 -0.0184 86  ASP   B OD1 
993  O  OD2 . ASP   B 77  ? 0.7533 0.5883 0.4914 0.1608 -0.1139 -0.0106 86  ASP   B OD2 
994  N  N   . ALA   B 78  ? 0.6610 0.4993 0.3285 0.2429 -0.1051 -0.0163 87  ALA   B N   
995  C  CA  . ALA   B 78  ? 0.6832 0.5069 0.3308 0.2660 -0.1214 -0.0233 87  ALA   B CA  
996  C  C   . ALA   B 78  ? 0.7030 0.5265 0.3320 0.2765 -0.1160 -0.0186 87  ALA   B C   
997  O  O   . ALA   B 78  ? 0.6997 0.5385 0.3314 0.2697 -0.0980 -0.0103 87  ALA   B O   
998  C  CB  . ALA   B 78  ? 0.6803 0.5114 0.3236 0.2863 -0.1235 -0.0297 87  ALA   B CB  
999  N  N   . ALA   B 79  ? 0.7185 0.5247 0.3296 0.2933 -0.1324 -0.0245 88  ALA   B N   
1000 C  CA  . ALA   B 79  ? 0.7307 0.5384 0.3260 0.3053 -0.1291 -0.0211 88  ALA   B CA  
1001 C  C   . ALA   B 79  ? 0.7510 0.5551 0.3250 0.3361 -0.1382 -0.0291 88  ALA   B C   
1002 O  O   . ALA   B 79  ? 0.7546 0.5426 0.3215 0.3470 -0.1555 -0.0394 88  ALA   B O   
1003 C  CB  . ALA   B 79  ? 0.7371 0.5251 0.3304 0.2929 -0.1399 -0.0190 88  ALA   B CB  
1004 N  N   . TRP   B 80  ? 0.7612 0.5811 0.3250 0.3505 -0.1268 -0.0247 89  TRP   B N   
1005 C  CA  . TRP   B 80  ? 0.7854 0.6061 0.3274 0.3815 -0.1324 -0.0313 89  TRP   B CA  
1006 C  C   . TRP   B 80  ? 0.8115 0.6033 0.3402 0.3906 -0.1563 -0.0408 89  TRP   B C   
1007 O  O   . TRP   B 80  ? 0.8089 0.5897 0.3428 0.3764 -0.1609 -0.0371 89  TRP   B O   
1008 C  CB  . TRP   B 80  ? 0.7784 0.6262 0.3176 0.3912 -0.1136 -0.0228 89  TRP   B CB  
1009 C  CG  . TRP   B 80  ? 0.7936 0.6477 0.3107 0.4240 -0.1157 -0.0284 89  TRP   B CG  
1010 C  CD1 . TRP   B 80  ? 0.8129 0.6645 0.3135 0.4447 -0.1198 -0.0354 89  TRP   B CD1 
1011 C  CD2 . TRP   B 80  ? 0.7946 0.6622 0.3036 0.4407 -0.1120 -0.0271 89  TRP   B CD2 
1012 N  NE1 . TRP   B 80  ? 0.8242 0.6851 0.3045 0.4737 -0.1189 -0.0389 89  TRP   B NE1 
1013 C  CE2 . TRP   B 80  ? 0.8125 0.6850 0.2993 0.4718 -0.1136 -0.0339 89  TRP   B CE2 
1014 C  CE3 . TRP   B 80  ? 0.7962 0.6725 0.3141 0.4335 -0.1088 -0.0216 89  TRP   B CE3 
1015 C  CZ2 . TRP   B 80  ? 0.8142 0.7024 0.2893 0.4958 -0.1102 -0.0351 89  TRP   B CZ2 
1016 C  CZ3 . TRP   B 80  ? 0.8004 0.6924 0.3087 0.4571 -0.1070 -0.0230 89  TRP   B CZ3 
1017 C  CH2 . TRP   B 80  ? 0.8036 0.7027 0.2916 0.4877 -0.1066 -0.0296 89  TRP   B CH2 
1018 N  N   . ASP   B 81  ? 0.8340 0.6104 0.3442 0.4136 -0.1728 -0.0533 90  ASP   B N   
1019 C  CA  . ASP   B 81  ? 0.8677 0.6119 0.3636 0.4236 -0.1977 -0.0640 90  ASP   B CA  
1020 C  C   . ASP   B 81  ? 0.8874 0.6352 0.3672 0.4450 -0.1974 -0.0647 90  ASP   B C   
1021 O  O   . ASP   B 81  ? 0.9076 0.6270 0.3759 0.4525 -0.2176 -0.0723 90  ASP   B O   
1022 C  CB  . ASP   B 81  ? 0.8969 0.6189 0.3785 0.4397 -0.2192 -0.0793 90  ASP   B CB  
1023 C  CG  . ASP   B 81  ? 0.9547 0.6920 0.4155 0.4703 -0.2139 -0.0852 90  ASP   B CG  
1024 O  OD1 . ASP   B 81  ? 0.9579 0.7244 0.4152 0.4803 -0.1923 -0.0766 90  ASP   B OD1 
1025 O  OD2 . ASP   B 81  ? 0.9897 0.7104 0.4377 0.4838 -0.2315 -0.0981 90  ASP   B OD2 
1026 N  N   . GLY   B 82  ? 0.8787 0.6609 0.3594 0.4541 -0.1753 -0.0567 91  GLY   B N   
1027 C  CA  . GLY   B 82  ? 0.8889 0.6830 0.3587 0.4752 -0.1725 -0.0568 91  GLY   B CA  
1028 C  C   . GLY   B 82  ? 0.9074 0.7019 0.3507 0.5126 -0.1787 -0.0686 91  GLY   B C   
1029 O  O   . GLY   B 82  ? 0.9115 0.7193 0.3452 0.5342 -0.1758 -0.0701 91  GLY   B O   
1030 N  N   . LEU   B 83  ? 0.9174 0.6991 0.3482 0.5217 -0.1875 -0.0776 92  LEU   B N   
1031 C  CA  . LEU   B 83  ? 0.9343 0.7139 0.3357 0.5581 -0.1947 -0.0902 92  LEU   B CA  
1032 C  C   . LEU   B 83  ? 0.9373 0.7384 0.3310 0.5677 -0.1798 -0.0872 92  LEU   B C   
1033 O  O   . LEU   B 83  ? 0.9530 0.7737 0.3270 0.5956 -0.1698 -0.0884 92  LEU   B O   
1034 C  CB  . LEU   B 83  ? 0.9593 0.6940 0.3445 0.5661 -0.2271 -0.1080 92  LEU   B CB  
1035 C  CG  . LEU   B 83  ? 0.9933 0.6957 0.3734 0.5680 -0.2488 -0.1156 92  LEU   B CG  
1036 C  CD1 . LEU   B 83  ? 1.0203 0.6801 0.3794 0.5823 -0.2801 -0.1350 92  LEU   B CD1 
1037 C  CD2 . LEU   B 83  ? 1.0026 0.7221 0.3704 0.5941 -0.2417 -0.1160 92  LEU   B CD2 
1038 N  N   . SER   B 84  ? 0.9269 0.7224 0.3334 0.5474 -0.1803 -0.0846 93  SER   B N   
1039 C  CA  . SER   B 84  ? 0.9202 0.7288 0.3162 0.5580 -0.1712 -0.0833 93  SER   B CA  
1040 C  C   . SER   B 84  ? 0.8853 0.7307 0.2922 0.5513 -0.1400 -0.0654 93  SER   B C   
1041 O  O   . SER   B 84  ? 0.8693 0.7291 0.3011 0.5277 -0.1256 -0.0531 93  SER   B O   
1042 C  CB  . SER   B 84  ? 0.9523 0.7406 0.3583 0.5415 -0.1863 -0.0889 93  SER   B CB  
1043 O  OG  . SER   B 84  ? 1.0012 0.7547 0.4080 0.5361 -0.2145 -0.1023 93  SER   B OG  
1044 N  N   . GLU   B 85  ? 0.8725 0.7307 0.2594 0.5717 -0.1307 -0.0639 94  GLU   B N   
1045 C  CA  . GLU   B 85  ? 0.8509 0.7390 0.2459 0.5652 -0.1026 -0.0464 94  GLU   B CA  
1046 C  C   . GLU   B 85  ? 0.8230 0.7054 0.2428 0.5354 -0.1007 -0.0403 94  GLU   B C   
1047 O  O   . GLU   B 85  ? 0.8333 0.6926 0.2573 0.5277 -0.1204 -0.0505 94  GLU   B O   
1048 C  CB  . GLU   B 85  ? 0.8933 0.7917 0.2565 0.5952 -0.0951 -0.0460 94  GLU   B CB  
1049 C  CG  . GLU   B 85  ? 0.9477 0.8617 0.2870 0.6259 -0.0891 -0.0486 94  GLU   B CG  
1050 C  CD  . GLU   B 85  ? 0.9941 0.9317 0.3093 0.6481 -0.0687 -0.0389 94  GLU   B CD  
1051 O  OE1 . GLU   B 85  ? 0.9861 0.9179 0.2920 0.6480 -0.0671 -0.0351 94  GLU   B OE1 
1052 O  OE2 . GLU   B 85  ? 1.0139 0.9769 0.3201 0.6657 -0.0536 -0.0341 94  GLU   B OE2 
1053 N  N   . VAL   B 86  ? 0.7817 0.6857 0.2202 0.5179 -0.0774 -0.0241 95  VAL   B N   
1054 C  CA  . VAL   B 86  ? 0.7449 0.6466 0.2070 0.4913 -0.0724 -0.0177 95  VAL   B CA  
1055 C  C   . VAL   B 86  ? 0.7214 0.6393 0.1778 0.4959 -0.0519 -0.0046 95  VAL   B C   
1056 O  O   . VAL   B 86  ? 0.7242 0.6568 0.1605 0.5166 -0.0401 0.0012  95  VAL   B O   
1057 C  CB  . VAL   B 86  ? 0.7230 0.6302 0.2142 0.4620 -0.0651 -0.0109 95  VAL   B CB  
1058 C  CG1 . VAL   B 86  ? 0.7249 0.6146 0.2182 0.4587 -0.0845 -0.0215 95  VAL   B CG1 
1059 C  CG2 . VAL   B 86  ? 0.7132 0.6480 0.2106 0.4599 -0.0414 0.0033  95  VAL   B CG2 
1060 N  N   . GLN   B 87  ? 0.6972 0.6118 0.1703 0.4774 -0.0476 0.0004  96  GLN   B N   
1061 C  CA  . GLN   B 87  ? 0.6786 0.6041 0.1482 0.4789 -0.0289 0.0139  96  GLN   B CA  
1062 C  C   . GLN   B 87  ? 0.6425 0.5759 0.1416 0.4494 -0.0130 0.0252  96  GLN   B C   
1063 O  O   . GLN   B 87  ? 0.6374 0.5615 0.1569 0.4297 -0.0206 0.0199  96  GLN   B O   
1064 C  CB  . GLN   B 87  ? 0.7024 0.6142 0.1578 0.4916 -0.0401 0.0083  96  GLN   B CB  
1065 C  CG  . GLN   B 87  ? 0.7677 0.6774 0.1859 0.5250 -0.0465 0.0035  96  GLN   B CG  
1066 C  CD  . GLN   B 87  ? 0.8248 0.7207 0.2265 0.5395 -0.0600 -0.0028 96  GLN   B CD  
1067 O  OE1 . GLN   B 87  ? 0.8370 0.7277 0.2558 0.5258 -0.0615 -0.0012 96  GLN   B OE1 
1068 N  NE2 . GLN   B 87  ? 0.8222 0.7124 0.1895 0.5692 -0.0711 -0.0111 96  GLN   B NE2 
1069 N  N   . LEU   B 88  ? 0.6164 0.5673 0.1174 0.4465 0.0091  0.0405  97  LEU   B N   
1070 C  CA  . LEU   B 88  ? 0.6012 0.5575 0.1261 0.4211 0.0243  0.0514  97  LEU   B CA  
1071 C  C   . LEU   B 88  ? 0.6072 0.5540 0.1273 0.4228 0.0291  0.0571  97  LEU   B C   
1072 O  O   . LEU   B 88  ? 0.6203 0.5711 0.1203 0.4393 0.0387  0.0666  97  LEU   B O   
1073 C  CB  . LEU   B 88  ? 0.5885 0.5673 0.1179 0.4178 0.0447  0.0656  97  LEU   B CB  
1074 C  CG  . LEU   B 88  ? 0.5920 0.5750 0.1441 0.3924 0.0606  0.0774  97  LEU   B CG  
1075 C  CD1 . LEU   B 88  ? 0.5972 0.5732 0.1721 0.3690 0.0529  0.0696  97  LEU   B CD1 
1076 C  CD2 . LEU   B 88  ? 0.5839 0.5905 0.1421 0.3893 0.0793  0.0916  97  LEU   B CD2 
1077 N  N   . LEU   B 89  ? 0.5930 0.5275 0.1296 0.4079 0.0224  0.0515  98  LEU   B N   
1078 C  CA  . LEU   B 89  ? 0.5893 0.5152 0.1229 0.4103 0.0269  0.0570  98  LEU   B CA  
1079 C  C   . LEU   B 89  ? 0.5887 0.5204 0.1359 0.3924 0.0476  0.0716  98  LEU   B C   
1080 O  O   . LEU   B 89  ? 0.5821 0.5110 0.1517 0.3710 0.0498  0.0697  98  LEU   B O   
1081 C  CB  . LEU   B 89  ? 0.5865 0.5002 0.1333 0.4040 0.0121  0.0450  98  LEU   B CB  
1082 C  CG  . LEU   B 89  ? 0.6068 0.5116 0.1532 0.4075 0.0153  0.0494  98  LEU   B CG  
1083 C  CD1 . LEU   B 89  ? 0.6272 0.5286 0.1434 0.4320 0.0190  0.0584  98  LEU   B CD1 
1084 C  CD2 . LEU   B 89  ? 0.6070 0.5053 0.1663 0.4065 -0.0022 0.0354  98  LEU   B CD2 
1085 N  N   . ALA   B 90  ? 0.5911 0.5319 0.1250 0.4006 0.0629  0.0859  99  ALA   B N   
1086 C  CA  . ALA   B 90  ? 0.5897 0.5361 0.1371 0.3831 0.0821  0.1008  99  ALA   B CA  
1087 C  C   . ALA   B 90  ? 0.5982 0.5275 0.1458 0.3792 0.0873  0.1076  99  ALA   B C   
1088 O  O   . ALA   B 90  ? 0.6117 0.5311 0.1386 0.3978 0.0840  0.1098  99  ALA   B O   
1089 C  CB  . ALA   B 90  ? 0.5875 0.5516 0.1227 0.3924 0.0971  0.1150  99  ALA   B CB  
1090 N  N   . VAL   B 91  ? 0.5870 0.5113 0.1566 0.3563 0.0941  0.1098  100 VAL   B N   
1091 C  CA  . VAL   B 91  ? 0.5870 0.4930 0.1581 0.3519 0.0993  0.1158  100 VAL   B CA  
1092 C  C   . VAL   B 91  ? 0.5919 0.4998 0.1729 0.3346 0.1170  0.1312  100 VAL   B C   
1093 O  O   . VAL   B 91  ? 0.5925 0.4994 0.1947 0.3130 0.1196  0.1281  100 VAL   B O   
1094 C  CB  . VAL   B 91  ? 0.5849 0.4806 0.1731 0.3418 0.0887  0.1013  100 VAL   B CB  
1095 C  CG1 . VAL   B 91  ? 0.5957 0.4716 0.1848 0.3405 0.0931  0.1061  100 VAL   B CG1 
1096 C  CG2 . VAL   B 91  ? 0.5860 0.4835 0.1693 0.3556 0.0705  0.0863  100 VAL   B CG2 
1097 N  N   . PRO   B 92  ? 0.5955 0.5077 0.1611 0.3434 0.1295  0.1482  101 PRO   B N   
1098 C  CA  . PRO   B 92  ? 0.6019 0.5189 0.1800 0.3251 0.1463  0.1639  101 PRO   B CA  
1099 C  C   . PRO   B 92  ? 0.6366 0.5278 0.2196 0.3131 0.1526  0.1722  101 PRO   B C   
1100 O  O   . PRO   B 92  ? 0.6454 0.5149 0.2139 0.3255 0.1479  0.1722  101 PRO   B O   
1101 C  CB  . PRO   B 92  ? 0.6036 0.5376 0.1634 0.3400 0.1580  0.1794  101 PRO   B CB  
1102 C  CG  . PRO   B 92  ? 0.6137 0.5464 0.1466 0.3682 0.1464  0.1712  101 PRO   B CG  
1103 C  CD  . PRO   B 92  ? 0.5979 0.5121 0.1339 0.3699 0.1288  0.1539  101 PRO   B CD  
1104 N  N   . PRO   B 93  ? 0.6515 0.5439 0.2546 0.2894 0.1624  0.1794  102 PRO   B N   
1105 C  CA  . PRO   B 93  ? 0.6807 0.5448 0.2883 0.2772 0.1673  0.1865  102 PRO   B CA  
1106 C  C   . PRO   B 93  ? 0.7173 0.5628 0.3017 0.2909 0.1751  0.2046  102 PRO   B C   
1107 O  O   . PRO   B 93  ? 0.7209 0.5779 0.2968 0.2932 0.1880  0.2227  102 PRO   B O   
1108 C  CB  . PRO   B 93  ? 0.6779 0.5515 0.3097 0.2506 0.1764  0.1928  102 PRO   B CB  
1109 C  CG  . PRO   B 93  ? 0.6612 0.5651 0.3054 0.2474 0.1710  0.1811  102 PRO   B CG  
1110 C  CD  . PRO   B 93  ? 0.6333 0.5516 0.2569 0.2730 0.1673  0.1797  102 PRO   B CD  
1111 N  N   . GLY   B 94  ? 0.7380 0.5561 0.3116 0.3012 0.1672  0.1998  103 GLY   B N   
1112 C  CA  . GLY   B 94  ? 0.7610 0.5558 0.3100 0.3159 0.1718  0.2159  103 GLY   B CA  
1113 C  C   . GLY   B 94  ? 0.7790 0.5844 0.2990 0.3431 0.1701  0.2208  103 GLY   B C   
1114 O  O   . GLY   B 94  ? 0.8008 0.5917 0.2967 0.3552 0.1772  0.2385  103 GLY   B O   
1115 N  N   . GLU   B 95  ? 0.7737 0.6028 0.2935 0.3534 0.1605  0.2056  104 GLU   B N   
1116 C  CA  . GLU   B 95  ? 0.7903 0.6296 0.2813 0.3803 0.1566  0.2070  104 GLU   B CA  
1117 C  C   . GLU   B 95  ? 0.7992 0.6401 0.2891 0.3946 0.1357  0.1839  104 GLU   B C   
1118 O  O   . GLU   B 95  ? 0.7909 0.6368 0.3052 0.3811 0.1275  0.1677  104 GLU   B O   
1119 C  CB  . GLU   B 95  ? 0.8039 0.6743 0.2937 0.3800 0.1677  0.2144  104 GLU   B CB  
1120 C  CG  . GLU   B 95  ? 0.8532 0.7276 0.3479 0.3646 0.1892  0.2383  104 GLU   B CG  
1121 C  CD  . GLU   B 95  ? 0.9035 0.8143 0.4062 0.3608 0.2011  0.2445  104 GLU   B CD  
1122 O  OE1 . GLU   B 95  ? 0.9088 0.8402 0.4176 0.3664 0.1916  0.2279  104 GLU   B OE1 
1123 O  OE2 . GLU   B 95  ? 0.9202 0.8392 0.4240 0.3521 0.2198  0.2662  104 GLU   B OE2 
1124 N  N   . ARG   B 96  ? 0.8106 0.6475 0.2720 0.4213 0.1268  0.1827  105 ARG   B N   
1125 C  CA  . ARG   B 96  ? 0.8241 0.6617 0.2838 0.4359 0.1054  0.1616  105 ARG   B CA  
1126 C  C   . ARG   B 96  ? 0.8145 0.6753 0.2866 0.4324 0.0974  0.1458  105 ARG   B C   
1127 O  O   . ARG   B 96  ? 0.8167 0.6952 0.2850 0.4310 0.1071  0.1523  105 ARG   B O   
1128 C  CB  . ARG   B 96  ? 0.8744 0.7031 0.2971 0.4662 0.0979  0.1657  105 ARG   B CB  
1129 C  CG  . ARG   B 96  ? 0.9461 0.7696 0.3680 0.4815 0.0742  0.1457  105 ARG   B CG  
1130 C  CD  . ARG   B 96  ? 1.0411 0.8467 0.4302 0.5078 0.0671  0.1524  105 ARG   B CD  
1131 N  NE  . ARG   B 96  ? 1.1182 0.9305 0.4700 0.5301 0.0689  0.1598  105 ARG   B NE  
1132 C  CZ  . ARG   B 96  ? 1.1986 1.0041 0.5219 0.5382 0.0855  0.1826  105 ARG   B CZ  
1133 N  NH1 . ARG   B 96  ? 1.2152 1.0043 0.5440 0.5246 0.1005  0.2007  105 ARG   B NH1 
1134 N  NH2 . ARG   B 96  ? 1.2144 1.0284 0.5023 0.5602 0.0871  0.1875  105 ARG   B NH2 
1135 N  N   . ALA   B 97  ? 0.7991 0.6602 0.2860 0.4317 0.0794  0.1255  106 ALA   B N   
1136 C  CA  . ALA   B 97  ? 0.7878 0.6653 0.2841 0.4296 0.0687  0.1102  106 ALA   B CA  
1137 C  C   . ALA   B 97  ? 0.8047 0.6904 0.2710 0.4537 0.0646  0.1108  106 ALA   B C   
1138 O  O   . ALA   B 97  ? 0.8126 0.6887 0.2528 0.4757 0.0589  0.1132  106 ALA   B O   
1139 C  CB  . ALA   B 97  ? 0.7798 0.6532 0.2920 0.4283 0.0497  0.0911  106 ALA   B CB  
1140 N  N   . LYS   B 98  ? 0.8059 0.7087 0.2742 0.4511 0.0676  0.1087  107 LYS   B N   
1141 C  CA  . LYS   B 98  ? 0.8228 0.7350 0.2621 0.4747 0.0662  0.1095  107 LYS   B CA  
1142 C  C   . LYS   B 98  ? 0.8105 0.7345 0.2570 0.4748 0.0547  0.0941  107 LYS   B C   
1143 O  O   . LYS   B 98  ? 0.8045 0.7401 0.2732 0.4561 0.0620  0.0951  107 LYS   B O   
1144 C  CB  . LYS   B 98  ? 0.8728 0.7964 0.3035 0.4731 0.0907  0.1314  107 LYS   B CB  
1145 C  CG  . LYS   B 98  ? 0.9740 0.9135 0.3766 0.4956 0.0963  0.1359  107 LYS   B CG  
1146 C  CD  . LYS   B 98  ? 1.0526 1.0088 0.4568 0.4874 0.1230  0.1587  107 LYS   B CD  
1147 C  CE  . LYS   B 98  ? 1.0884 1.0587 0.5306 0.4583 0.1320  0.1607  107 LYS   B CE  
1148 N  NZ  . LYS   B 98  ? 1.1148 1.1128 0.5584 0.4571 0.1528  0.1763  107 LYS   B NZ  
1149 N  N   . ASN   B 99  ? 0.8051 0.7240 0.2324 0.4959 0.0354  0.0795  108 ASN   B N   
1150 C  CA  . ASN   B 99  ? 0.7907 0.7153 0.2217 0.4980 0.0220  0.0643  108 ASN   B CA  
1151 C  C   . ASN   B 99  ? 0.7940 0.7357 0.2067 0.5123 0.0333  0.0707  108 ASN   B C   
1152 O  O   . ASN   B 99  ? 0.8140 0.7585 0.1965 0.5346 0.0397  0.0780  108 ASN   B O   
1153 C  CB  . ASN   B 99  ? 0.7938 0.7042 0.2125 0.5142 -0.0048 0.0453  108 ASN   B CB  
1154 C  CG  . ASN   B 99  ? 0.8159 0.7148 0.2595 0.4988 -0.0190 0.0353  108 ASN   B CG  
1155 O  OD1 . ASN   B 99  ? 0.8354 0.7288 0.2851 0.4944 -0.0146 0.0413  108 ASN   B OD1 
1156 N  ND2 . ASN   B 99  ? 0.8085 0.7032 0.2662 0.4918 -0.0369 0.0196  108 ASN   B ND2 
1157 N  N   . ILE   B 100 ? 0.7819 0.7365 0.2122 0.5007 0.0362  0.0682  109 ILE   B N   
1158 C  CA  . ILE   B 100 ? 0.7811 0.7564 0.1992 0.5142 0.0470  0.0732  109 ILE   B CA  
1159 C  C   . ILE   B 100 ? 0.7771 0.7505 0.1963 0.5201 0.0289  0.0555  109 ILE   B C   
1160 O  O   . ILE   B 100 ? 0.7687 0.7412 0.2145 0.4990 0.0243  0.0508  109 ILE   B O   
1161 C  CB  . ILE   B 100 ? 0.7767 0.7727 0.2192 0.4928 0.0701  0.0898  109 ILE   B CB  
1162 C  CG1 . ILE   B 100 ? 0.7917 0.7831 0.2386 0.4805 0.0864  0.1072  109 ILE   B CG1 
1163 C  CG2 . ILE   B 100 ? 0.7739 0.7967 0.2063 0.5079 0.0828  0.0958  109 ILE   B CG2 
1164 C  CD1 . ILE   B 100 ? 0.8174 0.8110 0.2297 0.5047 0.0975  0.1200  109 ILE   B CD1 
1165 N  N   . GLN   B 101 ? 0.7877 0.7584 0.1771 0.5487 0.0181  0.0456  110 GLN   B N   
1166 C  CA  . GLN   B 101 ? 0.8045 0.7684 0.1914 0.5570 -0.0013 0.0278  110 GLN   B CA  
1167 C  C   . GLN   B 101 ? 0.8083 0.7962 0.1999 0.5611 0.0105  0.0318  110 GLN   B C   
1168 O  O   . GLN   B 101 ? 0.8193 0.8296 0.1971 0.5757 0.0293  0.0432  110 GLN   B O   
1169 C  CB  . GLN   B 101 ? 0.8426 0.7901 0.1938 0.5875 -0.0209 0.0129  110 GLN   B CB  
1170 C  CG  . GLN   B 101 ? 0.8864 0.8172 0.2357 0.5938 -0.0463 -0.0076 110 GLN   B CG  
1171 C  CD  . GLN   B 101 ? 0.9417 0.8502 0.2619 0.6169 -0.0698 -0.0237 110 GLN   B CD  
1172 O  OE1 . GLN   B 101 ? 0.9481 0.8465 0.2659 0.6148 -0.0751 -0.0233 110 GLN   B OE1 
1173 N  NE2 . GLN   B 101 ? 0.9574 0.8571 0.2551 0.6401 -0.0855 -0.0391 110 GLN   B NE2 
1174 N  N   . THR   B 102 ? 0.7922 0.7765 0.2029 0.5492 -0.0006 0.0228  111 THR   B N   
1175 C  CA  . THR   B 102 ? 0.7844 0.7906 0.2018 0.5538 0.0070  0.0245  111 THR   B CA  
1176 C  C   . THR   B 102 ? 0.7905 0.7787 0.2114 0.5544 -0.0166 0.0074  111 THR   B C   
1177 O  O   . THR   B 102 ? 0.8069 0.7682 0.2333 0.5424 -0.0353 -0.0023 111 THR   B O   
1178 C  CB  . THR   B 102 ? 0.7843 0.8131 0.2343 0.5262 0.0281  0.0413  111 THR   B CB  
1179 O  OG1 . THR   B 102 ? 0.7928 0.8501 0.2488 0.5343 0.0381  0.0450  111 THR   B OG1 
1180 C  CG2 . THR   B 102 ? 0.7735 0.7865 0.2516 0.4950 0.0189  0.0383  111 THR   B CG2 
1181 N  N   . LEU   B 103 ? 0.7736 0.7769 0.1925 0.5680 -0.0159 0.0043  112 LEU   B N   
1182 C  CA  . LEU   B 103 ? 0.7717 0.7564 0.1947 0.5674 -0.0375 -0.0097 112 LEU   B CA  
1183 C  C   . LEU   B 103 ? 0.7524 0.7547 0.2075 0.5428 -0.0273 0.0001  112 LEU   B C   
1184 O  O   . LEU   B 103 ? 0.7397 0.7751 0.2033 0.5468 -0.0090 0.0102  112 LEU   B O   
1185 C  CB  . LEU   B 103 ? 0.7789 0.7639 0.1759 0.6021 -0.0477 -0.0225 112 LEU   B CB  
1186 C  CG  . LEU   B 103 ? 0.8057 0.7663 0.2073 0.5998 -0.0714 -0.0360 112 LEU   B CG  
1187 C  CD1 . LEU   B 103 ? 0.8325 0.7510 0.2247 0.5953 -0.0976 -0.0498 112 LEU   B CD1 
1188 C  CD2 . LEU   B 103 ? 0.8147 0.7852 0.2002 0.6305 -0.0754 -0.0446 112 LEU   B CD2 
1189 N  N   . PRO   B 104 ? 0.7454 0.7273 0.2188 0.5170 -0.0390 -0.0025 113 PRO   B N   
1190 C  CA  . PRO   B 104 ? 0.7279 0.7249 0.2293 0.4933 -0.0305 0.0065  113 PRO   B CA  
1191 C  C   . PRO   B 104 ? 0.7326 0.7413 0.2354 0.5058 -0.0356 0.0026  113 PRO   B C   
1192 O  O   . PRO   B 104 ? 0.7505 0.7418 0.2345 0.5270 -0.0536 -0.0105 113 PRO   B O   
1193 C  CB  . PRO   B 104 ? 0.7322 0.7008 0.2460 0.4667 -0.0439 0.0028  113 PRO   B CB  
1194 C  CG  . PRO   B 104 ? 0.7507 0.6973 0.2503 0.4720 -0.0533 -0.0041 113 PRO   B CG  
1195 C  CD  . PRO   B 104 ? 0.7484 0.6951 0.2191 0.5068 -0.0592 -0.0125 113 PRO   B CD  
1196 N  N   . GLY   B 105 ? 0.7121 0.7502 0.2377 0.4930 -0.0204 0.0137  114 GLY   B N   
1197 C  CA  . GLY   B 105 ? 0.7058 0.7593 0.2406 0.4992 -0.0243 0.0121  114 GLY   B CA  
1198 C  C   . GLY   B 105 ? 0.7124 0.7434 0.2601 0.4751 -0.0388 0.0099  114 GLY   B C   
1199 O  O   . GLY   B 105 ? 0.7178 0.7178 0.2622 0.4597 -0.0490 0.0065  114 GLY   B O   
1200 N  N   . ILE   B 106 ? 0.7040 0.7516 0.2666 0.4719 -0.0398 0.0123  115 ILE   B N   
1201 C  CA  . ILE   B 106 ? 0.7122 0.7386 0.2827 0.4520 -0.0542 0.0108  115 ILE   B CA  
1202 C  C   . ILE   B 106 ? 0.7011 0.7552 0.2978 0.4325 -0.0439 0.0208  115 ILE   B C   
1203 O  O   . ILE   B 106 ? 0.6915 0.7803 0.2995 0.4441 -0.0359 0.0241  115 ILE   B O   
1204 C  CB  . ILE   B 106 ? 0.7393 0.7431 0.2921 0.4741 -0.0772 -0.0013 115 ILE   B CB  
1205 C  CG1 . ILE   B 106 ? 0.7760 0.7411 0.3042 0.4856 -0.0935 -0.0127 115 ILE   B CG1 
1206 C  CG2 . ILE   B 106 ? 0.7533 0.7431 0.3139 0.4592 -0.0909 -0.0005 115 ILE   B CG2 
1207 C  CD1 . ILE   B 106 ? 0.8013 0.7372 0.3322 0.4591 -0.0996 -0.0116 115 ILE   B CD1 
1208 N  N   . PHE   B 107 ? 0.7003 0.7388 0.3063 0.4037 -0.0460 0.0245  116 PHE   B N   
1209 C  CA  . PHE   B 107 ? 0.6836 0.7406 0.3105 0.3842 -0.0415 0.0315  116 PHE   B CA  
1210 C  C   . PHE   B 107 ? 0.6998 0.7322 0.3176 0.3849 -0.0629 0.0258  116 PHE   B C   
1211 O  O   . PHE   B 107 ? 0.7153 0.7127 0.3221 0.3727 -0.0737 0.0230  116 PHE   B O   
1212 C  CB  . PHE   B 107 ? 0.6752 0.7247 0.3124 0.3536 -0.0320 0.0376  116 PHE   B CB  
1213 C  CG  . PHE   B 107 ? 0.6584 0.7360 0.3126 0.3443 -0.0103 0.0467  116 PHE   B CG  
1214 C  CD1 . PHE   B 107 ? 0.6482 0.7556 0.3061 0.3625 0.0021  0.0506  116 PHE   B CD1 
1215 C  CD2 . PHE   B 107 ? 0.6633 0.7362 0.3285 0.3176 -0.0021 0.0517  116 PHE   B CD2 
1216 C  CE1 . PHE   B 107 ? 0.6432 0.7742 0.3168 0.3521 0.0222  0.0608  116 PHE   B CE1 
1217 C  CE2 . PHE   B 107 ? 0.6593 0.7535 0.3394 0.3085 0.0165  0.0603  116 PHE   B CE2 
1218 C  CZ  . PHE   B 107 ? 0.6438 0.7662 0.3284 0.3250 0.0285  0.0656  116 PHE   B CZ  
1219 N  N   . LYS   B 108 ? 0.6986 0.7487 0.3207 0.4000 -0.0694 0.0243  117 LYS   B N   
1220 C  CA  . LYS   B 108 ? 0.7249 0.7509 0.3372 0.4021 -0.0906 0.0201  117 LYS   B CA  
1221 C  C   . LYS   B 108 ? 0.7177 0.7507 0.3446 0.3761 -0.0896 0.0271  117 LYS   B C   
1222 O  O   . LYS   B 108 ? 0.6959 0.7665 0.3438 0.3736 -0.0800 0.0318  117 LYS   B O   
1223 C  CB  . LYS   B 108 ? 0.7672 0.8109 0.3776 0.4331 -0.0987 0.0147  117 LYS   B CB  
1224 C  CG  . LYS   B 108 ? 0.8693 0.8724 0.4552 0.4501 -0.1234 0.0055  117 LYS   B CG  
1225 C  CD  . LYS   B 108 ? 0.9468 0.9522 0.5182 0.4853 -0.1263 -0.0043 117 LYS   B CD  
1226 C  CE  . LYS   B 108 ? 1.0330 0.9894 0.5774 0.5004 -0.1515 -0.0148 117 LYS   B CE  
1227 N  NZ  . LYS   B 108 ? 1.0831 1.0393 0.6105 0.5344 -0.1541 -0.0261 117 LYS   B NZ  
1228 N  N   . THR   B 109 ? 0.7322 0.7305 0.3486 0.3561 -0.0989 0.0280  118 THR   B N   
1229 C  CA  . THR   B 109 ? 0.7318 0.7324 0.3563 0.3320 -0.0993 0.0338  118 THR   B CA  
1230 C  C   . THR   B 109 ? 0.7552 0.7248 0.3622 0.3330 -0.1208 0.0327  118 THR   B C   
1231 O  O   . THR   B 109 ? 0.7723 0.7103 0.3606 0.3454 -0.1345 0.0280  118 THR   B O   
1232 C  CB  . THR   B 109 ? 0.7335 0.7272 0.3628 0.3038 -0.0859 0.0380  118 THR   B CB  
1233 O  OG1 . THR   B 109 ? 0.7575 0.7119 0.3696 0.2914 -0.0951 0.0373  118 THR   B OG1 
1234 C  CG2 . THR   B 109 ? 0.7236 0.7333 0.3622 0.3057 -0.0681 0.0387  118 THR   B CG2 
1235 N  N   . LYS   B 110 ? 0.7608 0.7360 0.3720 0.3191 -0.1248 0.0371  119 LYS   B N   
1236 C  CA  . LYS   B 110 ? 0.7918 0.7360 0.3839 0.3184 -0.1448 0.0382  119 LYS   B CA  
1237 C  C   . LYS   B 110 ? 0.8282 0.7272 0.3999 0.3026 -0.1499 0.0400  119 LYS   B C   
1238 O  O   . LYS   B 110 ? 0.8555 0.7212 0.4077 0.3047 -0.1674 0.0413  119 LYS   B O   
1239 C  CB  . LYS   B 110 ? 0.7972 0.7581 0.3966 0.3054 -0.1473 0.0428  119 LYS   B CB  
1240 C  CG  . LYS   B 110 ? 0.8482 0.8102 0.4519 0.2754 -0.1342 0.0471  119 LYS   B CG  
1241 C  CD  . LYS   B 110 ? 0.9054 0.8777 0.5105 0.2637 -0.1406 0.0503  119 LYS   B CD  
1242 C  CE  . LYS   B 110 ? 0.9564 0.9187 0.5561 0.2355 -0.1318 0.0535  119 LYS   B CE  
1243 N  NZ  . LYS   B 110 ? 0.9710 0.9625 0.5941 0.2240 -0.1128 0.0523  119 LYS   B NZ  
1244 N  N   . ASP   B 111 ? 0.8213 0.7197 0.3986 0.2866 -0.1349 0.0406  120 ASP   B N   
1245 C  CA  . ASP   B 111 ? 0.8423 0.7054 0.4062 0.2706 -0.1372 0.0423  120 ASP   B CA  
1246 C  C   . ASP   B 111 ? 0.8555 0.7037 0.4161 0.2820 -0.1387 0.0364  120 ASP   B C   
1247 O  O   . ASP   B 111 ? 0.8708 0.6987 0.4279 0.2671 -0.1368 0.0372  120 ASP   B O   
1248 C  CB  . ASP   B 111 ? 0.8564 0.7281 0.4286 0.2440 -0.1208 0.0465  120 ASP   B CB  
1249 C  CG  . ASP   B 111 ? 0.9192 0.7998 0.4904 0.2301 -0.1208 0.0514  120 ASP   B CG  
1250 O  OD1 . ASP   B 111 ? 0.9357 0.8047 0.4943 0.2364 -0.1364 0.0536  120 ASP   B OD1 
1251 O  OD2 . ASP   B 111 ? 0.9439 0.8412 0.5255 0.2137 -0.1063 0.0525  120 ASP   B OD2 
1252 N  N   . GLY   B 112 ? 0.8452 0.7050 0.4072 0.3083 -0.1420 0.0300  121 GLY   B N   
1253 C  CA  . GLY   B 112 ? 0.8500 0.6958 0.4060 0.3221 -0.1452 0.0229  121 GLY   B CA  
1254 C  C   . GLY   B 112 ? 0.8281 0.7064 0.3960 0.3356 -0.1296 0.0195  121 GLY   B C   
1255 O  O   . GLY   B 112 ? 0.8118 0.7229 0.3960 0.3282 -0.1132 0.0242  121 GLY   B O   
1256 N  N   . ASP   B 113 ? 0.8258 0.6933 0.3841 0.3553 -0.1353 0.0116  122 ASP   B N   
1257 C  CA  . ASP   B 113 ? 0.8123 0.7071 0.3765 0.3703 -0.1211 0.0089  122 ASP   B CA  
1258 C  C   . ASP   B 113 ? 0.7975 0.6918 0.3682 0.3536 -0.1084 0.0109  122 ASP   B C   
1259 O  O   . ASP   B 113 ? 0.8089 0.6759 0.3756 0.3388 -0.1155 0.0098  122 ASP   B O   
1260 C  CB  . ASP   B 113 ? 0.8469 0.7309 0.3942 0.4021 -0.1334 -0.0016 122 ASP   B CB  
1261 C  CG  . ASP   B 113 ? 0.9289 0.8141 0.4690 0.4242 -0.1463 -0.0054 122 ASP   B CG  
1262 O  OD1 . ASP   B 113 ? 0.9270 0.8231 0.4762 0.4150 -0.1464 0.0008  122 ASP   B OD1 
1263 O  OD2 . ASP   B 113 ? 0.9865 0.8611 0.5108 0.4520 -0.1573 -0.0153 122 ASP   B OD2 
1264 N  N   . ILE   B 114 ? 0.7656 0.6912 0.3475 0.3559 -0.0894 0.0145  123 ILE   B N   
1265 C  CA  . ILE   B 114 ? 0.7552 0.6829 0.3432 0.3439 -0.0767 0.0166  123 ILE   B CA  
1266 C  C   . ILE   B 114 ? 0.7361 0.6815 0.3192 0.3669 -0.0681 0.0146  123 ILE   B C   
1267 O  O   . ILE   B 114 ? 0.7191 0.6911 0.3053 0.3816 -0.0608 0.0170  123 ILE   B O   
1268 C  CB  . ILE   B 114 ? 0.7508 0.6976 0.3572 0.3193 -0.0597 0.0256  123 ILE   B CB  
1269 C  CG1 . ILE   B 114 ? 0.7739 0.7133 0.3837 0.3010 -0.0658 0.0287  123 ILE   B CG1 
1270 C  CG2 . ILE   B 114 ? 0.7547 0.6954 0.3657 0.3055 -0.0503 0.0267  123 ILE   B CG2 
1271 C  CD1 . ILE   B 114 ? 0.7860 0.7475 0.4122 0.2820 -0.0509 0.0357  123 ILE   B CD1 
1272 N  N   . GLY   B 115 ? 0.7346 0.6680 0.3109 0.3696 -0.0679 0.0110  124 GLY   B N   
1273 C  CA  . GLY   B 115 ? 0.7272 0.6762 0.2955 0.3907 -0.0586 0.0104  124 GLY   B CA  
1274 C  C   . GLY   B 115 ? 0.7067 0.6870 0.2907 0.3816 -0.0354 0.0219  124 GLY   B C   
1275 O  O   . GLY   B 115 ? 0.7121 0.6949 0.3119 0.3568 -0.0278 0.0281  124 GLY   B O   
1276 N  N   . ALA   B 116 ? 0.6877 0.6914 0.2670 0.4009 -0.0238 0.0252  125 ALA   B N   
1277 C  CA  . ALA   B 116 ? 0.6697 0.7025 0.2642 0.3920 -0.0014 0.0376  125 ALA   B CA  
1278 C  C   . ALA   B 116 ? 0.6724 0.7146 0.2533 0.4110 0.0096  0.0407  125 ALA   B C   
1279 O  O   . ALA   B 116 ? 0.6807 0.7228 0.2425 0.4373 0.0035  0.0342  125 ALA   B O   
1280 C  CB  . ALA   B 116 ? 0.6501 0.7128 0.2595 0.3928 0.0047  0.0427  125 ALA   B CB  
1281 N  N   A VAL   B 117 ? 0.6682 0.7162 0.2565 0.3984 0.0254  0.0505  126 VAL   B N   
1282 N  N   B VAL   B 117 ? 0.6682 0.7168 0.2569 0.3984 0.0255  0.0506  126 VAL   B N   
1283 N  N   C VAL   B 117 ? 0.6682 0.7162 0.2565 0.3984 0.0254  0.0505  126 VAL   B N   
1284 N  N   D VAL   B 117 ? 0.6682 0.7168 0.2569 0.3984 0.0255  0.0506  126 VAL   B N   
1285 C  CA  A VAL   B 117 ? 0.6790 0.7344 0.2523 0.4153 0.0368  0.0559  126 VAL   B CA  
1286 C  CA  B VAL   B 117 ? 0.6797 0.7351 0.2537 0.4145 0.0370  0.0560  126 VAL   B CA  
1287 C  CA  C VAL   B 117 ? 0.6790 0.7344 0.2523 0.4153 0.0368  0.0559  126 VAL   B CA  
1288 C  CA  D VAL   B 117 ? 0.6797 0.7351 0.2537 0.4145 0.0370  0.0560  126 VAL   B CA  
1289 C  C   A VAL   B 117 ? 0.6720 0.7618 0.2578 0.4136 0.0595  0.0709  126 VAL   B C   
1290 C  C   B VAL   B 117 ? 0.6722 0.7622 0.2584 0.4134 0.0596  0.0710  126 VAL   B C   
1291 C  C   C VAL   B 117 ? 0.6720 0.7618 0.2578 0.4136 0.0595  0.0709  126 VAL   B C   
1292 C  C   D VAL   B 117 ? 0.6722 0.7622 0.2584 0.4134 0.0596  0.0710  126 VAL   B C   
1293 O  O   A VAL   B 117 ? 0.6649 0.7627 0.2725 0.3898 0.0702  0.0801  126 VAL   B O   
1294 O  O   B VAL   B 117 ? 0.6647 0.7633 0.2730 0.3896 0.0702  0.0801  126 VAL   B O   
1295 O  O   C VAL   B 117 ? 0.6649 0.7627 0.2725 0.3898 0.0702  0.0801  126 VAL   B O   
1296 O  O   D VAL   B 117 ? 0.6647 0.7633 0.2730 0.3896 0.0702  0.0801  126 VAL   B O   
1297 C  CB  A VAL   B 117 ? 0.6964 0.7283 0.2626 0.4088 0.0353  0.0552  126 VAL   B CB  
1298 C  CB  B VAL   B 117 ? 0.6968 0.7290 0.2672 0.4040 0.0361  0.0560  126 VAL   B CB  
1299 C  CB  C VAL   B 117 ? 0.6964 0.7283 0.2626 0.4088 0.0353  0.0552  126 VAL   B CB  
1300 C  CB  D VAL   B 117 ? 0.6968 0.7290 0.2672 0.4040 0.0361  0.0560  126 VAL   B CB  
1301 C  CG1 A VAL   B 117 ? 0.7175 0.7220 0.2656 0.4215 0.0135  0.0402  126 VAL   B CG1 
1302 C  CG1 B VAL   B 117 ? 0.7065 0.7461 0.2635 0.4167 0.0504  0.0653  126 VAL   B CG1 
1303 C  CG1 C VAL   B 117 ? 0.7175 0.7220 0.2656 0.4215 0.0135  0.0402  126 VAL   B CG1 
1304 C  CG1 D VAL   B 117 ? 0.7065 0.7461 0.2635 0.4167 0.0504  0.0653  126 VAL   B CG1 
1305 C  CG2 A VAL   B 117 ? 0.6975 0.7225 0.2858 0.3781 0.0398  0.0597  126 VAL   B CG2 
1306 C  CG2 B VAL   B 117 ? 0.7164 0.7192 0.2739 0.4100 0.0139  0.0413  126 VAL   B CG2 
1307 C  CG2 C VAL   B 117 ? 0.6975 0.7225 0.2858 0.3781 0.0398  0.0597  126 VAL   B CG2 
1308 C  CG2 D VAL   B 117 ? 0.7164 0.7192 0.2739 0.4100 0.0139  0.0413  126 VAL   B CG2 
1309 N  N   . ALA   B 118 ? 0.6711 0.7816 0.2434 0.4388 0.0668  0.0732  127 ALA   B N   
1310 C  CA  . ALA   B 118 ? 0.6705 0.8175 0.2555 0.4383 0.0895  0.0887  127 ALA   B CA  
1311 C  C   . ALA   B 118 ? 0.6936 0.8386 0.2668 0.4399 0.1052  0.1008  127 ALA   B C   
1312 O  O   . ALA   B 118 ? 0.7047 0.8569 0.2540 0.4648 0.1111  0.1028  127 ALA   B O   
1313 C  CB  . ALA   B 118 ? 0.6608 0.8359 0.2387 0.4650 0.0916  0.0859  127 ALA   B CB  
1314 N  N   . LEU   B 119 ? 0.7003 0.8318 0.2869 0.4148 0.1104  0.1081  128 LEU   B N   
1315 C  CA  . LEU   B 119 ? 0.7128 0.8372 0.2896 0.4133 0.1241  0.1206  128 LEU   B CA  
1316 C  C   . LEU   B 119 ? 0.7111 0.8420 0.3163 0.3831 0.1377  0.1339  128 LEU   B C   
1317 O  O   . LEU   B 119 ? 0.7094 0.8308 0.3341 0.3615 0.1295  0.1280  128 LEU   B O   
1318 C  CB  . LEU   B 119 ? 0.7299 0.8182 0.2865 0.4186 0.1097  0.1111  128 LEU   B CB  
1319 C  CG  . LEU   B 119 ? 0.7593 0.8396 0.2832 0.4505 0.0984  0.1006  128 LEU   B CG  
1320 C  CD1 . LEU   B 119 ? 0.7763 0.8230 0.2875 0.4521 0.0805  0.0887  128 LEU   B CD1 
1321 C  CD2 . LEU   B 119 ? 0.7677 0.8658 0.2699 0.4716 0.1157  0.1133  128 LEU   B CD2 
1322 N  N   . ASP   B 120 ? 0.7079 0.8550 0.3150 0.3813 0.1583  0.1520  129 ASP   B N   
1323 C  CA  . ASP   B 120 ? 0.7038 0.8561 0.3383 0.3524 0.1708  0.1651  129 ASP   B CA  
1324 C  C   . ASP   B 120 ? 0.7153 0.8398 0.3400 0.3444 0.1772  0.1746  129 ASP   B C   
1325 O  O   . ASP   B 120 ? 0.7277 0.8555 0.3361 0.3556 0.1908  0.1885  129 ASP   B O   
1326 C  CB  . ASP   B 120 ? 0.7078 0.9020 0.3608 0.3502 0.1895  0.1801  129 ASP   B CB  
1327 C  CG  . ASP   B 120 ? 0.7623 0.9688 0.4528 0.3185 0.1950  0.1868  129 ASP   B CG  
1328 O  OD1 . ASP   B 120 ? 0.7738 0.9531 0.4725 0.2982 0.1863  0.1813  129 ASP   B OD1 
1329 O  OD2 . ASP   B 120 ? 0.7797 1.0240 0.4915 0.3144 0.2077  0.1972  129 ASP   B OD2 
1330 N  N   . TYR   B 121 ? 0.7100 0.8076 0.3442 0.3256 0.1677  0.1674  130 TYR   B N   
1331 C  CA  . TYR   B 121 ? 0.7205 0.7888 0.3480 0.3177 0.1708  0.1734  130 TYR   B CA  
1332 C  C   . TYR   B 121 ? 0.6979 0.7588 0.3527 0.2869 0.1741  0.1767  130 TYR   B C   
1333 O  O   . TYR   B 121 ? 0.6904 0.7602 0.3648 0.2732 0.1668  0.1675  130 TYR   B O   
1334 C  CB  . TYR   B 121 ? 0.7486 0.7887 0.3579 0.3291 0.1531  0.1575  130 TYR   B CB  
1335 C  CG  . TYR   B 121 ? 0.7860 0.8252 0.3641 0.3593 0.1499  0.1562  130 TYR   B CG  
1336 C  CD1 . TYR   B 121 ? 0.8163 0.8402 0.3728 0.3707 0.1560  0.1661  130 TYR   B CD1 
1337 C  CD2 . TYR   B 121 ? 0.8034 0.8567 0.3717 0.3776 0.1408  0.1455  130 TYR   B CD2 
1338 C  CE1 . TYR   B 121 ? 0.8421 0.8656 0.3670 0.3995 0.1527  0.1648  130 TYR   B CE1 
1339 C  CE2 . TYR   B 121 ? 0.8285 0.8808 0.3660 0.4065 0.1375  0.1434  130 TYR   B CE2 
1340 C  CZ  . TYR   B 121 ? 0.8581 0.8959 0.3735 0.4173 0.1433  0.1527  130 TYR   B CZ  
1341 O  OH  . TYR   B 121 ? 0.9073 0.9433 0.3892 0.4469 0.1389  0.1499  130 TYR   B OH  
1342 N  N   . PRO   B 122 ? 0.6825 0.7235 0.3373 0.2760 0.1831  0.1884  131 PRO   B N   
1343 C  CA  . PRO   B 122 ? 0.6595 0.6906 0.3390 0.2473 0.1847  0.1897  131 PRO   B CA  
1344 C  C   . PRO   B 122 ? 0.6380 0.6596 0.3287 0.2360 0.1689  0.1704  131 PRO   B C   
1345 O  O   . PRO   B 122 ? 0.6508 0.6628 0.3278 0.2491 0.1565  0.1569  131 PRO   B O   
1346 C  CB  . PRO   B 122 ? 0.6839 0.6838 0.3520 0.2453 0.1907  0.1997  131 PRO   B CB  
1347 C  CG  . PRO   B 122 ? 0.7025 0.7092 0.3469 0.2672 0.2006  0.2134  131 PRO   B CG  
1348 C  CD  . PRO   B 122 ? 0.6878 0.7131 0.3186 0.2899 0.1916  0.2012  131 PRO   B CD  
1349 N  N   . ALA   B 123 ? 0.6010 0.6265 0.3158 0.2118 0.1691  0.1692  132 ALA   B N   
1350 C  CA  . ALA   B 123 ? 0.5805 0.5977 0.3035 0.2006 0.1553  0.1521  132 ALA   B CA  
1351 C  C   . ALA   B 123 ? 0.5768 0.5622 0.2866 0.2038 0.1474  0.1414  132 ALA   B C   
1352 O  O   . ALA   B 123 ? 0.5748 0.5565 0.2820 0.2053 0.1356  0.1269  132 ALA   B O   
1353 C  CB  . ALA   B 123 ? 0.5663 0.5884 0.3139 0.1745 0.1571  0.1534  132 ALA   B CB  
1354 N  N   . GLY   B 124 ? 0.5731 0.5370 0.2742 0.2062 0.1540  0.1494  133 GLY   B N   
1355 C  CA  . GLY   B 124 ? 0.5753 0.5110 0.2656 0.2113 0.1476  0.1404  133 GLY   B CA  
1356 C  C   . GLY   B 124 ? 0.5639 0.4989 0.2364 0.2338 0.1387  0.1323  133 GLY   B C   
1357 O  O   . GLY   B 124 ? 0.5687 0.4848 0.2350 0.2391 0.1325  0.1241  133 GLY   B O   
1358 N  N   . THR   B 125 ? 0.5484 0.5045 0.2138 0.2477 0.1372  0.1337  134 THR   B N   
1359 C  CA  . THR   B 125 ? 0.5521 0.5082 0.2007 0.2689 0.1264  0.1247  134 THR   B CA  
1360 C  C   . THR   B 125 ? 0.5468 0.5059 0.2030 0.2633 0.1126  0.1083  134 THR   B C   
1361 O  O   . THR   B 125 ? 0.5568 0.5100 0.2033 0.2759 0.1013  0.0985  134 THR   B O   
1362 C  CB  . THR   B 125 ? 0.5680 0.5421 0.2017 0.2885 0.1313  0.1336  134 THR   B CB  
1363 O  OG1 . THR   B 125 ? 0.5905 0.5623 0.2184 0.2898 0.1461  0.1512  134 THR   B OG1 
1364 C  CG2 . THR   B 125 ? 0.5813 0.5501 0.1935 0.3127 0.1197  0.1251  134 THR   B CG2 
1365 N  N   . SER   B 126 ? 0.5268 0.4940 0.1999 0.2441 0.1129  0.1057  135 SER   B N   
1366 C  CA  . SER   B 126 ? 0.5267 0.4956 0.2051 0.2372 0.1011  0.0926  135 SER   B CA  
1367 C  C   . SER   B 126 ? 0.5284 0.4796 0.2037 0.2377 0.0927  0.0814  135 SER   B C   
1368 O  O   . SER   B 126 ? 0.5337 0.4711 0.2130 0.2301 0.0969  0.0807  135 SER   B O   
1369 C  CB  . SER   B 126 ? 0.5358 0.5104 0.2307 0.2151 0.1035  0.0922  135 SER   B CB  
1370 O  OG  . SER   B 126 ? 0.5554 0.5519 0.2582 0.2135 0.1091  0.1009  135 SER   B OG  
1371 N  N   . GLY   B 127 ? 0.5153 0.4675 0.1852 0.2453 0.0806  0.0723  136 GLY   B N   
1372 C  CA  . GLY   B 127 ? 0.5093 0.4495 0.1791 0.2458 0.0719  0.0619  136 GLY   B CA  
1373 C  C   . GLY   B 127 ? 0.5122 0.4483 0.1695 0.2667 0.0642  0.0594  136 GLY   B C   
1374 O  O   . GLY   B 127 ? 0.5149 0.4444 0.1742 0.2684 0.0547  0.0503  136 GLY   B O   
1375 N  N   . SER   B 128 ? 0.5015 0.4428 0.1459 0.2831 0.0681  0.0676  137 SER   B N   
1376 C  CA  . SER   B 128 ? 0.5057 0.4433 0.1337 0.3055 0.0602  0.0653  137 SER   B CA  
1377 C  C   . SER   B 128 ? 0.5027 0.4413 0.1276 0.3109 0.0444  0.0544  137 SER   B C   
1378 O  O   . SER   B 128 ? 0.5007 0.4476 0.1278 0.3064 0.0430  0.0541  137 SER   B O   
1379 C  CB  . SER   B 128 ? 0.5275 0.4733 0.1405 0.3205 0.0696  0.0772  137 SER   B CB  
1380 O  OG  . SER   B 128 ? 0.5481 0.4892 0.1629 0.3153 0.0837  0.0889  137 SER   B OG  
1381 N  N   . PRO   B 129 ? 0.5083 0.4377 0.1299 0.3194 0.0312  0.0450  138 PRO   B N   
1382 C  CA  . PRO   B 129 ? 0.5187 0.4452 0.1386 0.3221 0.0146  0.0345  138 PRO   B CA  
1383 C  C   . PRO   B 129 ? 0.5445 0.4730 0.1440 0.3440 0.0074  0.0334  138 PRO   B C   
1384 O  O   . PRO   B 129 ? 0.5594 0.4907 0.1432 0.3614 0.0127  0.0388  138 PRO   B O   
1385 C  CB  . PRO   B 129 ? 0.5200 0.4375 0.1462 0.3231 0.0034  0.0254  138 PRO   B CB  
1386 C  CG  . PRO   B 129 ? 0.5216 0.4372 0.1407 0.3348 0.0104  0.0307  138 PRO   B CG  
1387 C  CD  . PRO   B 129 ? 0.5014 0.4222 0.1217 0.3269 0.0295  0.0434  138 PRO   B CD  
1388 N  N   . ILE   B 130 ? 0.5512 0.4772 0.1494 0.3439 -0.0047 0.0263  139 ILE   B N   
1389 C  CA  . ILE   B 130 ? 0.5718 0.4965 0.1504 0.3657 -0.0151 0.0216  139 ILE   B CA  
1390 C  C   . ILE   B 130 ? 0.5937 0.5017 0.1701 0.3700 -0.0369 0.0081  139 ILE   B C   
1391 O  O   . ILE   B 130 ? 0.5829 0.4840 0.1762 0.3514 -0.0434 0.0038  139 ILE   B O   
1392 C  CB  . ILE   B 130 ? 0.5742 0.5076 0.1538 0.3629 -0.0131 0.0238  139 ILE   B CB  
1393 C  CG1 . ILE   B 130 ? 0.5753 0.5281 0.1603 0.3582 0.0078  0.0371  139 ILE   B CG1 
1394 C  CG2 . ILE   B 130 ? 0.5892 0.5188 0.1481 0.3871 -0.0261 0.0163  139 ILE   B CG2 
1395 C  CD1 . ILE   B 130 ? 0.5845 0.5465 0.1826 0.3434 0.0110  0.0398  139 ILE   B CD1 
1396 N  N   . LEU   B 131 ? 0.6194 0.5211 0.1755 0.3937 -0.0478 0.0018  140 LEU   B N   
1397 C  CA  . LEU   B 131 ? 0.6508 0.5367 0.2056 0.3985 -0.0698 -0.0114 140 LEU   B CA  
1398 C  C   . LEU   B 131 ? 0.6850 0.5584 0.2199 0.4174 -0.0889 -0.0225 140 LEU   B C   
1399 O  O   . LEU   B 131 ? 0.6967 0.5751 0.2090 0.4392 -0.0853 -0.0212 140 LEU   B O   
1400 C  CB  . LEU   B 131 ? 0.6546 0.5400 0.2016 0.4120 -0.0710 -0.0123 140 LEU   B CB  
1401 C  CG  . LEU   B 131 ? 0.6607 0.5556 0.2184 0.4029 -0.0523 -0.0012 140 LEU   B CG  
1402 C  CD1 . LEU   B 131 ? 0.6670 0.5581 0.2125 0.4205 -0.0575 -0.0030 140 LEU   B CD1 
1403 C  CD2 . LEU   B 131 ? 0.6556 0.5522 0.2433 0.3751 -0.0485 -0.0010 140 LEU   B CD2 
1404 N  N   . ASP   B 132 ? 0.6965 0.5531 0.2390 0.4108 -0.1099 -0.0340 141 ASP   B N   
1405 C  CA  . ASP   B 132 ? 0.7298 0.5689 0.2527 0.4292 -0.1319 -0.0468 141 ASP   B CA  
1406 C  C   . ASP   B 132 ? 0.7683 0.6009 0.2761 0.4495 -0.1456 -0.0562 141 ASP   B C   
1407 O  O   . ASP   B 132 ? 0.7595 0.6017 0.2746 0.4472 -0.1375 -0.0516 141 ASP   B O   
1408 C  CB  . ASP   B 132 ? 0.7412 0.5623 0.2783 0.4115 -0.1488 -0.0535 141 ASP   B CB  
1409 C  CG  . ASP   B 132 ? 0.7862 0.6003 0.3471 0.3919 -0.1601 -0.0584 141 ASP   B CG  
1410 O  OD1 . ASP   B 132 ? 0.7909 0.6152 0.3594 0.3926 -0.1559 -0.0579 141 ASP   B OD1 
1411 O  OD2 . ASP   B 132 ? 0.8124 0.6114 0.3850 0.3758 -0.1731 -0.0622 141 ASP   B OD2 
1412 N  N   . LYS   B 133 ? 0.8067 0.6219 0.2926 0.4701 -0.1673 -0.0699 142 LYS   B N   
1413 C  CA  . LYS   B 133 ? 0.8394 0.6470 0.3067 0.4919 -0.1830 -0.0805 142 LYS   B CA  
1414 C  C   . LYS   B 133 ? 0.8448 0.6497 0.3372 0.4762 -0.1953 -0.0858 142 LYS   B C   
1415 O  O   . LYS   B 133 ? 0.8545 0.6621 0.3377 0.4905 -0.2003 -0.0891 142 LYS   B O   
1416 C  CB  . LYS   B 133 ? 0.8959 0.6828 0.3346 0.5161 -0.2056 -0.0961 142 LYS   B CB  
1417 C  CG  . LYS   B 133 ? 0.9795 0.7745 0.3946 0.5344 -0.1916 -0.0909 142 LYS   B CG  
1418 C  CD  . LYS   B 133 ? 1.0747 0.8505 0.4563 0.5641 -0.2120 -0.1071 142 LYS   B CD  
1419 C  CE  . LYS   B 133 ? 1.1433 0.9325 0.5088 0.5794 -0.1956 -0.1008 142 LYS   B CE  
1420 N  NZ  . LYS   B 133 ? 1.1987 0.9662 0.5391 0.6027 -0.2165 -0.1173 142 LYS   B NZ  
1421 N  N   . CYS   B 134 ? 0.8377 0.6401 0.3622 0.4472 -0.1984 -0.0852 143 CYS   B N   
1422 C  CA  . CYS   B 134 ? 0.8309 0.6373 0.3859 0.4290 -0.2060 -0.0884 143 CYS   B CA  
1423 C  C   . CYS   B 134 ? 0.7966 0.6252 0.3672 0.4201 -0.1830 -0.0761 143 CYS   B C   
1424 O  O   . CYS   B 134 ? 0.7891 0.6249 0.3844 0.4087 -0.1874 -0.0787 143 CYS   B O   
1425 C  CB  . CYS   B 134 ? 0.8610 0.6587 0.4435 0.4006 -0.2142 -0.0899 143 CYS   B CB  
1426 S  SG  . CYS   B 134 ? 0.9823 0.7483 0.5560 0.4058 -0.2494 -0.1073 143 CYS   B SG  
1427 N  N   . GLY   B 135 ? 0.7749 0.6142 0.3350 0.4228 -0.1589 -0.0631 144 GLY   B N   
1428 C  CA  . GLY   B 135 ? 0.7498 0.6060 0.3232 0.4132 -0.1364 -0.0509 144 GLY   B CA  
1429 C  C   . GLY   B 135 ? 0.7201 0.5836 0.3218 0.3833 -0.1233 -0.0439 144 GLY   B C   
1430 O  O   . GLY   B 135 ? 0.7242 0.5997 0.3394 0.3733 -0.1061 -0.0356 144 GLY   B O   
1431 N  N   . ARG   B 136 ? 0.6921 0.5466 0.3016 0.3694 -0.1319 -0.0474 145 ARG   B N   
1432 C  CA  . ARG   B 136 ? 0.6693 0.5292 0.3019 0.3415 -0.1205 -0.0408 145 ARG   B CA  
1433 C  C   . ARG   B 136 ? 0.6401 0.5075 0.2645 0.3385 -0.0998 -0.0292 145 ARG   B C   
1434 O  O   . ARG   B 136 ? 0.6422 0.5058 0.2455 0.3531 -0.1003 -0.0281 145 ARG   B O   
1435 C  CB  . ARG   B 136 ? 0.7048 0.5497 0.3457 0.3279 -0.1377 -0.0470 145 ARG   B CB  
1436 C  CG  . ARG   B 136 ? 0.7719 0.6131 0.4318 0.3217 -0.1565 -0.0570 145 ARG   B CG  
1437 C  CD  . ARG   B 136 ? 0.8338 0.6574 0.5019 0.3062 -0.1731 -0.0613 145 ARG   B CD  
1438 N  NE  . ARG   B 136 ? 0.9089 0.7106 0.5497 0.3246 -0.1893 -0.0679 145 ARG   B NE  
1439 C  CZ  . ARG   B 136 ? 0.9773 0.7612 0.6113 0.3175 -0.1956 -0.0667 145 ARG   B CZ  
1440 N  NH1 . ARG   B 136 ? 0.9692 0.7546 0.6205 0.2914 -0.1868 -0.0579 145 ARG   B NH1 
1441 N  NH2 . ARG   B 136 ? 1.0021 0.7661 0.6100 0.3380 -0.2108 -0.0742 145 ARG   B NH2 
1442 N  N   . VAL   B 137 ? 0.6054 0.4844 0.2475 0.3193 -0.0822 -0.0212 146 VAL   B N   
1443 C  CA  . VAL   B 137 ? 0.5855 0.4722 0.2232 0.3137 -0.0636 -0.0108 146 VAL   B CA  
1444 C  C   . VAL   B 137 ? 0.5851 0.4649 0.2211 0.3037 -0.0682 -0.0101 146 VAL   B C   
1445 O  O   . VAL   B 137 ? 0.5876 0.4629 0.2377 0.2844 -0.0721 -0.0113 146 VAL   B O   
1446 C  CB  . VAL   B 137 ? 0.5745 0.4725 0.2290 0.2979 -0.0453 -0.0042 146 VAL   B CB  
1447 C  CG1 . VAL   B 137 ? 0.5723 0.4774 0.2221 0.2926 -0.0283 0.0057  146 VAL   B CG1 
1448 C  CG2 . VAL   B 137 ? 0.5774 0.4795 0.2330 0.3096 -0.0426 -0.0050 146 VAL   B CG2 
1449 N  N   . ILE   B 138 ? 0.5774 0.4568 0.1955 0.3177 -0.0678 -0.0080 147 ILE   B N   
1450 C  CA  . ILE   B 138 ? 0.5704 0.4432 0.1848 0.3119 -0.0730 -0.0072 147 ILE   B CA  
1451 C  C   . ILE   B 138 ? 0.5565 0.4428 0.1761 0.3001 -0.0556 0.0028  147 ILE   B C   
1452 O  O   . ILE   B 138 ? 0.5658 0.4479 0.1834 0.2940 -0.0595 0.0042  147 ILE   B O   
1453 C  CB  . ILE   B 138 ? 0.5880 0.4517 0.1805 0.3363 -0.0866 -0.0134 147 ILE   B CB  
1454 C  CG1 . ILE   B 138 ? 0.5985 0.4783 0.1769 0.3568 -0.0735 -0.0085 147 ILE   B CG1 
1455 C  CG2 . ILE   B 138 ? 0.6023 0.4484 0.1902 0.3451 -0.1079 -0.0252 147 ILE   B CG2 
1456 C  CD1 . ILE   B 138 ? 0.6286 0.5047 0.1847 0.3820 -0.0827 -0.0136 147 ILE   B CD1 
1457 N  N   . GLY   B 139 ? 0.5337 0.4342 0.1594 0.2968 -0.0382 0.0094  148 GLY   B N   
1458 C  CA  . GLY   B 139 ? 0.5289 0.4415 0.1611 0.2844 -0.0231 0.0179  148 GLY   B CA  
1459 C  C   . GLY   B 139 ? 0.5220 0.4471 0.1571 0.2862 -0.0059 0.0251  148 GLY   B C   
1460 O  O   . GLY   B 139 ? 0.5317 0.4557 0.1620 0.2984 -0.0051 0.0242  148 GLY   B O   
1461 N  N   . LEU   B 140 ? 0.5007 0.4363 0.1432 0.2739 0.0070  0.0322  149 LEU   B N   
1462 C  CA  . LEU   B 140 ? 0.4943 0.4389 0.1408 0.2728 0.0231  0.0400  149 LEU   B CA  
1463 C  C   . LEU   B 140 ? 0.4988 0.4591 0.1436 0.2772 0.0316  0.0481  149 LEU   B C   
1464 O  O   . LEU   B 140 ? 0.4973 0.4637 0.1447 0.2722 0.0280  0.0479  149 LEU   B O   
1465 C  CB  . LEU   B 140 ? 0.4844 0.4267 0.1448 0.2517 0.0317  0.0408  149 LEU   B CB  
1466 C  CG  . LEU   B 140 ? 0.4956 0.4277 0.1624 0.2447 0.0264  0.0335  149 LEU   B CG  
1467 C  CD1 . LEU   B 140 ? 0.4922 0.4241 0.1705 0.2256 0.0366  0.0338  149 LEU   B CD1 
1468 C  CD2 . LEU   B 140 ? 0.5011 0.4290 0.1638 0.2604 0.0239  0.0313  149 LEU   B CD2 
1469 N  N   . TYR   B 141 ? 0.5036 0.4714 0.1449 0.2863 0.0432  0.0559  150 TYR   B N   
1470 C  CA  . TYR   B 141 ? 0.5091 0.4956 0.1510 0.2911 0.0545  0.0657  150 TYR   B CA  
1471 C  C   . TYR   B 141 ? 0.5014 0.4939 0.1598 0.2703 0.0671  0.0731  150 TYR   B C   
1472 O  O   . TYR   B 141 ? 0.5064 0.4872 0.1690 0.2609 0.0721  0.0738  150 TYR   B O   
1473 C  CB  . TYR   B 141 ? 0.5211 0.5095 0.1485 0.3109 0.0611  0.0717  150 TYR   B CB  
1474 C  CG  . TYR   B 141 ? 0.5371 0.5456 0.1660 0.3144 0.0772  0.0851  150 TYR   B CG  
1475 C  CD1 . TYR   B 141 ? 0.5516 0.5599 0.1890 0.3024 0.0917  0.0961  150 TYR   B CD1 
1476 C  CD2 . TYR   B 141 ? 0.5471 0.5743 0.1685 0.3311 0.0780  0.0871  150 TYR   B CD2 
1477 C  CE1 . TYR   B 141 ? 0.5595 0.5869 0.2008 0.3031 0.1071  0.1100  150 TYR   B CE1 
1478 C  CE2 . TYR   B 141 ? 0.5525 0.6025 0.1780 0.3336 0.0944  0.1004  150 TYR   B CE2 
1479 C  CZ  . TYR   B 141 ? 0.5645 0.6147 0.2005 0.3186 0.1092  0.1126  150 TYR   B CZ  
1480 O  OH  . TYR   B 141 ? 0.5711 0.6445 0.2130 0.3192 0.1260  0.1274  150 TYR   B OH  
1481 N  N   . GLY   B 142 ? 0.4888 0.5001 0.1566 0.2650 0.0723  0.0786  151 GLY   B N   
1482 C  CA  . GLY   B 142 ? 0.4947 0.5120 0.1789 0.2453 0.0832  0.0855  151 GLY   B CA  
1483 C  C   . GLY   B 142 ? 0.5002 0.5285 0.1980 0.2300 0.0795  0.0836  151 GLY   B C   
1484 O  O   . GLY   B 142 ? 0.5060 0.5378 0.2177 0.2126 0.0866  0.0877  151 GLY   B O   
1485 N  N   . ASN   B 143 ? 0.4927 0.5241 0.1860 0.2361 0.0672  0.0768  152 ASN   B N   
1486 C  CA  . ASN   B 143 ? 0.4849 0.5274 0.1893 0.2239 0.0624  0.0755  152 ASN   B CA  
1487 C  C   . ASN   B 143 ? 0.4886 0.5490 0.1906 0.2407 0.0563  0.0754  152 ASN   B C   
1488 O  O   . ASN   B 143 ? 0.4995 0.5490 0.1876 0.2539 0.0447  0.0686  152 ASN   B O   
1489 C  CB  . ASN   B 143 ? 0.5015 0.5254 0.2022 0.2104 0.0521  0.0670  152 ASN   B CB  
1490 C  CG  . ASN   B 143 ? 0.5151 0.5484 0.2268 0.1942 0.0495  0.0669  152 ASN   B CG  
1491 O  OD1 . ASN   B 143 ? 0.5205 0.5695 0.2471 0.1855 0.0576  0.0726  152 ASN   B OD1 
1492 N  ND2 . ASN   B 143 ? 0.5057 0.5292 0.2101 0.1892 0.0375  0.0608  152 ASN   B ND2 
1493 N  N   . GLY   B 144 ? 0.4809 0.5687 0.1976 0.2406 0.0638  0.0825  153 GLY   B N   
1494 C  CA  . GLY   B 144 ? 0.4972 0.6067 0.2139 0.2586 0.0593  0.0823  153 GLY   B CA  
1495 C  C   . GLY   B 144 ? 0.5080 0.6514 0.2480 0.2522 0.0662  0.0892  153 GLY   B C   
1496 O  O   . GLY   B 144 ? 0.4908 0.6367 0.2461 0.2310 0.0657  0.0899  153 GLY   B O   
1497 N  N   . VAL   B 145 ? 0.5321 0.7031 0.2752 0.2710 0.0727  0.0941  154 VAL   B N   
1498 C  CA  . VAL   B 145 ? 0.5506 0.7608 0.3189 0.2683 0.0792  0.1008  154 VAL   B CA  
1499 C  C   . VAL   B 145 ? 0.5810 0.8203 0.3561 0.2797 0.0983  0.1127  154 VAL   B C   
1500 O  O   . VAL   B 145 ? 0.5937 0.8235 0.3480 0.2972 0.1036  0.1139  154 VAL   B O   
1501 C  CB  . VAL   B 145 ? 0.5612 0.7815 0.3285 0.2820 0.0633  0.0923  154 VAL   B CB  
1502 C  CG1 . VAL   B 145 ? 0.5663 0.8010 0.3210 0.3136 0.0641  0.0907  154 VAL   B CG1 
1503 C  CG2 . VAL   B 145 ? 0.5543 0.8045 0.3502 0.2685 0.0613  0.0946  154 VAL   B CG2 
1504 N  N   . VAL   B 146 ? 0.5887 0.8643 0.3928 0.2695 0.1082  0.1217  155 VAL   B N   
1505 C  CA  . VAL   B 146 ? 0.6065 0.9155 0.4214 0.2773 0.1281  0.1353  155 VAL   B CA  
1506 C  C   . VAL   B 146 ? 0.6337 0.9825 0.4578 0.2991 0.1263  0.1330  155 VAL   B C   
1507 O  O   . VAL   B 146 ? 0.6244 0.9891 0.4674 0.2933 0.1151  0.1275  155 VAL   B O   
1508 C  CB  . VAL   B 146 ? 0.5962 0.9189 0.4407 0.2485 0.1408  0.1478  155 VAL   B CB  
1509 C  CG1 . VAL   B 146 ? 0.5880 0.9505 0.4483 0.2539 0.1623  0.1640  155 VAL   B CG1 
1510 C  CG2 . VAL   B 146 ? 0.6178 0.8987 0.4500 0.2311 0.1423  0.1490  155 VAL   B CG2 
1511 N  N   . ILE   B 147 ? 0.6642 1.0276 0.4726 0.3264 0.1358  0.1357  156 ILE   B N   
1512 C  CA  . ILE   B 147 ? 0.6861 1.0851 0.4995 0.3516 0.1334  0.1314  156 ILE   B CA  
1513 C  C   . ILE   B 147 ? 0.6868 1.1440 0.5329 0.3502 0.1552  0.1465  156 ILE   B C   
1514 O  O   . ILE   B 147 ? 0.6792 1.1430 0.5416 0.3280 0.1710  0.1608  156 ILE   B O   
1515 C  CB  . ILE   B 147 ? 0.7173 1.0958 0.4919 0.3855 0.1260  0.1210  156 ILE   B CB  
1516 C  CG1 . ILE   B 147 ? 0.7420 1.1284 0.4990 0.4010 0.1455  0.1307  156 ILE   B CG1 
1517 C  CG2 . ILE   B 147 ? 0.7481 1.0726 0.4973 0.3816 0.1058  0.1082  156 ILE   B CG2 
1518 C  CD1 . ILE   B 147 ? 0.7767 1.1513 0.4967 0.4386 0.1381  0.1193  156 ILE   B CD1 
1519 N  N   A LYS   B 148 ? 0.6755 1.1728 0.5316 0.3733 0.1551  0.1431  157 LYS   B N   
1520 N  N   B LYS   B 148 ? 0.6755 1.1728 0.5316 0.3733 0.1551  0.1431  157 LYS   B N   
1521 N  N   C LYS   B 148 ? 0.6754 1.1728 0.5317 0.3731 0.1551  0.1431  157 LYS   B N   
1522 N  N   D LYS   B 148 ? 0.6754 1.1728 0.5317 0.3731 0.1551  0.1431  157 LYS   B N   
1523 C  CA  A LYS   B 148 ? 0.6546 1.2137 0.5439 0.3759 0.1744  0.1555  157 LYS   B CA  
1524 C  CA  B LYS   B 148 ? 0.6546 1.2137 0.5439 0.3759 0.1744  0.1555  157 LYS   B CA  
1525 C  CA  C LYS   B 148 ? 0.6543 1.2133 0.5444 0.3748 0.1744  0.1557  157 LYS   B CA  
1526 C  CA  D LYS   B 148 ? 0.6543 1.2133 0.5444 0.3748 0.1744  0.1557  157 LYS   B CA  
1527 C  C   A LYS   B 148 ? 0.6549 1.2288 0.5447 0.3706 0.2019  0.1746  157 LYS   B C   
1528 C  C   B LYS   B 148 ? 0.6549 1.2288 0.5447 0.3706 0.2019  0.1746  157 LYS   B C   
1529 C  C   C LYS   B 148 ? 0.6547 1.2287 0.5447 0.3703 0.2020  0.1747  157 LYS   B C   
1530 C  C   D LYS   B 148 ? 0.6547 1.2287 0.5447 0.3703 0.2020  0.1747  157 LYS   B C   
1531 O  O   A LYS   B 148 ? 0.6322 1.2427 0.5584 0.3500 0.2175  0.1894  157 LYS   B O   
1532 O  O   B LYS   B 148 ? 0.6322 1.2427 0.5584 0.3500 0.2175  0.1894  157 LYS   B O   
1533 O  O   C LYS   B 148 ? 0.6321 1.2427 0.5584 0.3498 0.2177  0.1896  157 LYS   B O   
1534 O  O   D LYS   B 148 ? 0.6321 1.2427 0.5584 0.3498 0.2177  0.1896  157 LYS   B O   
1535 C  CB  A LYS   B 148 ? 0.6722 1.2633 0.5566 0.4129 0.1710  0.1465  157 LYS   B CB  
1536 C  CB  B LYS   B 148 ? 0.6722 1.2633 0.5566 0.4129 0.1710  0.1465  157 LYS   B CB  
1537 C  CB  C LYS   B 148 ? 0.6702 1.2632 0.5582 0.4104 0.1707  0.1468  157 LYS   B CB  
1538 C  CB  D LYS   B 148 ? 0.6702 1.2632 0.5582 0.4104 0.1707  0.1468  157 LYS   B CB  
1539 C  CG  A LYS   B 148 ? 0.7219 1.3158 0.6189 0.4168 0.1470  0.1320  157 LYS   B CG  
1540 C  CG  B LYS   B 148 ? 0.7219 1.3158 0.6189 0.4168 0.1470  0.1320  157 LYS   B CG  
1541 C  CG  C LYS   B 148 ? 0.7225 1.3115 0.6195 0.4134 0.1451  0.1315  157 LYS   B CG  
1542 C  CG  D LYS   B 148 ? 0.7225 1.3115 0.6195 0.4134 0.1451  0.1315  157 LYS   B CG  
1543 C  CD  A LYS   B 148 ? 0.7739 1.3916 0.6602 0.4573 0.1421  0.1215  157 LYS   B CD  
1544 C  CD  B LYS   B 148 ? 0.7739 1.3916 0.6602 0.4573 0.1421  0.1215  157 LYS   B CD  
1545 C  CD  C LYS   B 148 ? 0.7642 1.3924 0.6647 0.4489 0.1426  0.1238  157 LYS   B CD  
1546 C  CD  D LYS   B 148 ? 0.7642 1.3924 0.6647 0.4489 0.1426  0.1238  157 LYS   B CD  
1547 C  CE  A LYS   B 148 ? 0.7889 1.4748 0.7022 0.4710 0.1659  0.1325  157 LYS   B CE  
1548 C  CE  B LYS   B 148 ? 0.7889 1.4748 0.7022 0.4710 0.1659  0.1325  157 LYS   B CE  
1549 C  CE  C LYS   B 148 ? 0.7723 1.4722 0.7159 0.4480 0.1637  0.1367  157 LYS   B CE  
1550 C  CE  D LYS   B 148 ? 0.7723 1.4722 0.7159 0.4480 0.1637  0.1367  157 LYS   B CE  
1551 N  NZ  A LYS   B 148 ? 0.7831 1.5174 0.7502 0.4471 0.1698  0.1408  157 LYS   B NZ  
1552 N  NZ  B LYS   B 148 ? 0.7831 1.5174 0.7502 0.4471 0.1698  0.1408  157 LYS   B NZ  
1553 N  NZ  C LYS   B 148 ? 0.7846 1.5250 0.7331 0.4845 0.1608  0.1278  157 LYS   B NZ  
1554 N  NZ  D LYS   B 148 ? 0.7846 1.5250 0.7331 0.4845 0.1608  0.1278  157 LYS   B NZ  
1555 N  N   . ASN   B 149 ? 0.6786 1.2242 0.5283 0.3887 0.2073  0.1749  158 ASN   B N   
1556 C  CA  . ASN   B 149 ? 0.6828 1.2389 0.5262 0.3870 0.2330  0.1938  158 ASN   B CA  
1557 C  C   . ASN   B 149 ? 0.6792 1.1989 0.5234 0.3546 0.2374  0.2046  158 ASN   B C   
1558 O  O   . ASN   B 149 ? 0.6912 1.2071 0.5222 0.3541 0.2559  0.2199  158 ASN   B O   
1559 C  CB  . ASN   B 149 ? 0.7337 1.2807 0.5326 0.4241 0.2376  0.1899  158 ASN   B CB  
1560 C  CG  . ASN   B 149 ? 0.8259 1.3166 0.5853 0.4373 0.2141  0.1713  158 ASN   B CG  
1561 O  OD1 . ASN   B 149 ? 0.8578 1.3084 0.6167 0.4156 0.1998  0.1659  158 ASN   B OD1 
1562 N  ND2 . ASN   B 149 ? 0.8528 1.3399 0.5782 0.4734 0.2102  0.1611  158 ASN   B ND2 
1563 N  N   . GLY   B 150 ? 0.6614 1.1539 0.5186 0.3297 0.2205  0.1966  159 GLY   B N   
1564 C  CA  . GLY   B 150 ? 0.6552 1.1122 0.5143 0.3000 0.2221  0.2038  159 GLY   B CA  
1565 C  C   . GLY   B 150 ? 0.6586 1.0594 0.4778 0.3063 0.2122  0.1957  159 GLY   B C   
1566 O  O   . GLY   B 150 ? 0.6704 1.0376 0.4903 0.2834 0.2092  0.1973  159 GLY   B O   
1567 N  N   A SER   B 151 ? 0.6652 1.0557 0.4504 0.3378 0.2064  0.1862  160 SER   B N   
1568 N  N   B SER   B 151 ? 0.6645 1.0550 0.4497 0.3377 0.2065  0.1863  160 SER   B N   
1569 N  N   C SER   B 151 ? 0.6652 1.0557 0.4504 0.3378 0.2064  0.1862  160 SER   B N   
1570 N  N   D SER   B 151 ? 0.6645 1.0550 0.4497 0.3377 0.2065  0.1863  160 SER   B N   
1571 C  CA  A SER   B 151 ? 0.6899 1.0310 0.4386 0.3463 0.1956  0.1774  160 SER   B CA  
1572 C  CA  B SER   B 151 ? 0.6890 1.0302 0.4378 0.3462 0.1958  0.1776  160 SER   B CA  
1573 C  CA  C SER   B 151 ? 0.6899 1.0310 0.4386 0.3463 0.1956  0.1774  160 SER   B CA  
1574 C  CA  D SER   B 151 ? 0.6890 1.0302 0.4378 0.3462 0.1958  0.1776  160 SER   B CA  
1575 C  C   A SER   B 151 ? 0.6922 0.9989 0.4408 0.3336 0.1724  0.1609  160 SER   B C   
1576 C  C   B SER   B 151 ? 0.6917 0.9984 0.4400 0.3339 0.1724  0.1609  160 SER   B C   
1577 C  C   C SER   B 151 ? 0.6922 0.9989 0.4408 0.3336 0.1724  0.1609  160 SER   B C   
1578 C  C   D SER   B 151 ? 0.6917 0.9984 0.4400 0.3339 0.1724  0.1609  160 SER   B C   
1579 O  O   A SER   B 151 ? 0.6815 1.0012 0.4484 0.3283 0.1612  0.1527  160 SER   B O   
1580 O  O   B SER   B 151 ? 0.6811 1.0009 0.4475 0.3290 0.1611  0.1526  160 SER   B O   
1581 O  O   C SER   B 151 ? 0.6815 1.0012 0.4484 0.3283 0.1612  0.1527  160 SER   B O   
1582 O  O   D SER   B 151 ? 0.6811 1.0009 0.4475 0.3290 0.1611  0.1526  160 SER   B O   
1583 C  CB  A SER   B 151 ? 0.7179 1.0596 0.4321 0.3833 0.1940  0.1706  160 SER   B CB  
1584 C  CB  B SER   B 151 ? 0.7154 1.0573 0.4296 0.3831 0.1946  0.1711  160 SER   B CB  
1585 C  CB  C SER   B 151 ? 0.7179 1.0596 0.4321 0.3833 0.1940  0.1706  160 SER   B CB  
1586 C  CB  D SER   B 151 ? 0.7154 1.0573 0.4296 0.3831 0.1946  0.1711  160 SER   B CB  
1587 O  OG  A SER   B 151 ? 0.7713 1.0670 0.4529 0.3909 0.1817  0.1614  160 SER   B OG  
1588 O  OG  B SER   B 151 ? 0.7346 1.0926 0.4508 0.4008 0.1814  0.1570  160 SER   B OG  
1589 O  OG  C SER   B 151 ? 0.7713 1.0670 0.4529 0.3909 0.1817  0.1614  160 SER   B OG  
1590 O  OG  D SER   B 151 ? 0.7346 1.0926 0.4508 0.4008 0.1814  0.1570  160 SER   B OG  
1591 N  N   . TYR   B 152 ? 0.7032 0.9669 0.4305 0.3295 0.1654  0.1564  161 TYR   B N   
1592 C  CA  . TYR   B 152 ? 0.6848 0.9158 0.4100 0.3174 0.1460  0.1422  161 TYR   B CA  
1593 C  C   . TYR   B 152 ? 0.6585 0.8664 0.3551 0.3402 0.1287  0.1267  161 TYR   B C   
1594 O  O   . TYR   B 152 ? 0.6657 0.8629 0.3369 0.3599 0.1306  0.1265  161 TYR   B O   
1595 C  CB  . TYR   B 152 ? 0.6991 0.8990 0.4231 0.2967 0.1495  0.1469  161 TYR   B CB  
1596 C  CG  . TYR   B 152 ? 0.7166 0.8877 0.4430 0.2801 0.1333  0.1343  161 TYR   B CG  
1597 C  CD1 . TYR   B 152 ? 0.7172 0.8960 0.4682 0.2574 0.1295  0.1328  161 TYR   B CD1 
1598 C  CD2 . TYR   B 152 ? 0.7465 0.8836 0.4508 0.2866 0.1222  0.1243  161 TYR   B CD2 
1599 C  CE1 . TYR   B 152 ? 0.7360 0.8890 0.4861 0.2429 0.1161  0.1219  161 TYR   B CE1 
1600 C  CE2 . TYR   B 152 ? 0.7667 0.8804 0.4736 0.2712 0.1095  0.1139  161 TYR   B CE2 
1601 C  CZ  . TYR   B 152 ? 0.7671 0.8884 0.4953 0.2498 0.1071  0.1129  161 TYR   B CZ  
1602 O  OH  . TYR   B 152 ? 0.8031 0.9017 0.5308 0.2353 0.0962  0.1033  161 TYR   B OH  
1603 N  N   . VAL   B 153 ? 0.6271 0.8251 0.3273 0.3362 0.1109  0.1140  162 VAL   B N   
1604 C  CA  . VAL   B 153 ? 0.6141 0.7866 0.2908 0.3530 0.0922  0.0992  162 VAL   B CA  
1605 C  C   . VAL   B 153 ? 0.5897 0.7309 0.2690 0.3316 0.0788  0.0914  162 VAL   B C   
1606 O  O   . VAL   B 153 ? 0.5770 0.7230 0.2722 0.3166 0.0727  0.0892  162 VAL   B O   
1607 C  CB  . VAL   B 153 ? 0.6124 0.8041 0.2874 0.3740 0.0832  0.0918  162 VAL   B CB  
1608 C  CG1 . VAL   B 153 ? 0.6304 0.7900 0.2817 0.3883 0.0615  0.0765  162 VAL   B CG1 
1609 C  CG2 . VAL   B 153 ? 0.6125 0.8371 0.2830 0.3973 0.0983  0.0991  162 VAL   B CG2 
1610 N  N   . SER   B 154 ? 0.5793 0.6907 0.2433 0.3304 0.0752  0.0878  163 SER   B N   
1611 C  CA  . SER   B 154 ? 0.5726 0.6563 0.2381 0.3118 0.0647  0.0808  163 SER   B CA  
1612 C  C   . SER   B 154 ? 0.5585 0.6234 0.2102 0.3218 0.0449  0.0680  163 SER   B C   
1613 O  O   . SER   B 154 ? 0.5588 0.6223 0.1939 0.3450 0.0388  0.0632  163 SER   B O   
1614 C  CB  . SER   B 154 ? 0.5992 0.6625 0.2572 0.3073 0.0700  0.0828  163 SER   B CB  
1615 O  OG  . SER   B 154 ? 0.6257 0.6622 0.2797 0.2980 0.0579  0.0733  163 SER   B OG  
1616 N  N   . ALA   B 155 ? 0.5425 0.5899 0.1987 0.3042 0.0349  0.0626  164 ALA   B N   
1617 C  CA  . ALA   B 155 ? 0.5443 0.5695 0.1878 0.3099 0.0163  0.0521  164 ALA   B CA  
1618 C  C   . ALA   B 155 ? 0.5469 0.5472 0.1804 0.3091 0.0119  0.0472  164 ALA   B C   
1619 O  O   . ALA   B 155 ? 0.5455 0.5445 0.1843 0.2997 0.0225  0.0514  164 ALA   B O   
1620 C  CB  . ALA   B 155 ? 0.5455 0.5647 0.1974 0.2909 0.0085  0.0504  164 ALA   B CB  
1621 N  N   . ILE   B 156 ? 0.5442 0.5248 0.1643 0.3194 -0.0048 0.0380  165 ILE   B N   
1622 C  CA  . ILE   B 156 ? 0.5455 0.5044 0.1607 0.3160 -0.0114 0.0325  165 ILE   B CA  
1623 C  C   . ILE   B 156 ? 0.5378 0.4853 0.1635 0.2911 -0.0153 0.0316  165 ILE   B C   
1624 O  O   . ILE   B 156 ? 0.5352 0.4705 0.1566 0.2890 -0.0287 0.0277  165 ILE   B O   
1625 C  CB  . ILE   B 156 ? 0.5631 0.5055 0.1609 0.3363 -0.0285 0.0227  165 ILE   B CB  
1626 C  CG1 . ILE   B 156 ? 0.5879 0.5439 0.1714 0.3636 -0.0244 0.0232  165 ILE   B CG1 
1627 C  CG2 . ILE   B 156 ? 0.5715 0.4952 0.1690 0.3308 -0.0356 0.0171  165 ILE   B CG2 
1628 C  CD1 . ILE   B 156 ? 0.6167 0.5556 0.1797 0.3867 -0.0430 0.0116  165 ILE   B CD1 
1629 N  N   . THR   B 157 ? 0.5285 0.4799 0.1663 0.2729 -0.0030 0.0361  166 THR   B N   
1630 C  CA  . THR   B 157 ? 0.5243 0.4677 0.1699 0.2502 -0.0041 0.0355  166 THR   B CA  
1631 C  C   . THR   B 157 ? 0.5245 0.4512 0.1708 0.2432 -0.0102 0.0301  166 THR   B C   
1632 O  O   . THR   B 157 ? 0.5239 0.4515 0.1750 0.2429 -0.0029 0.0298  166 THR   B O   
1633 C  CB  . THR   B 157 ? 0.5285 0.4838 0.1861 0.2346 0.0112  0.0413  166 THR   B CB  
1634 O  OG1 . THR   B 157 ? 0.5361 0.5101 0.1975 0.2384 0.0167  0.0468  166 THR   B OG1 
1635 C  CG2 . THR   B 157 ? 0.5256 0.4729 0.1874 0.2133 0.0105  0.0398  166 THR   B CG2 
1636 N  N   . GLN   B 158 ? 0.5218 0.4337 0.1646 0.2367 -0.0230 0.0266  167 GLN   B N   
1637 C  CA  . GLN   B 158 ? 0.5311 0.4302 0.1784 0.2277 -0.0285 0.0222  167 GLN   B CA  
1638 C  C   . GLN   B 158 ? 0.5644 0.4582 0.2166 0.2047 -0.0268 0.0244  167 GLN   B C   
1639 O  O   . GLN   B 158 ? 0.5629 0.4549 0.2092 0.1992 -0.0295 0.0277  167 GLN   B O   
1640 C  CB  . GLN   B 158 ? 0.5254 0.4090 0.1641 0.2413 -0.0464 0.0160  167 GLN   B CB  
1641 C  CG  . GLN   B 158 ? 0.5311 0.4029 0.1777 0.2319 -0.0545 0.0112  167 GLN   B CG  
1642 C  CD  . GLN   B 158 ? 0.5565 0.4377 0.2138 0.2336 -0.0465 0.0089  167 GLN   B CD  
1643 O  OE1 . GLN   B 158 ? 0.5580 0.4511 0.2236 0.2250 -0.0310 0.0126  167 GLN   B OE1 
1644 N  NE2 . GLN   B 158 ? 0.5466 0.4210 0.2036 0.2447 -0.0584 0.0020  167 GLN   B NE2 
1645 N  N   . GLY   B 159 ? 0.5940 0.4870 0.2562 0.1926 -0.0221 0.0226  168 GLY   B N   
1646 C  CA  . GLY   B 159 ? 0.6330 0.5227 0.2987 0.1717 -0.0189 0.0247  168 GLY   B CA  
1647 C  C   . GLY   B 159 ? 0.6883 0.5623 0.3531 0.1653 -0.0325 0.0238  168 GLY   B C   
1648 O  O   . GLY   B 159 ? 0.6965 0.5601 0.3576 0.1776 -0.0465 0.0203  168 GLY   B O   
1649 N  N   . LYS   B 160 ? 0.7268 0.5982 0.3940 0.1460 -0.0288 0.0271  169 LYS   B N   
1650 C  CA  . LYS   B 160 ? 0.7704 0.6263 0.4381 0.1359 -0.0404 0.0285  169 LYS   B CA  
1651 C  C   . LYS   B 160 ? 0.7956 0.6607 0.4816 0.1222 -0.0329 0.0272  169 LYS   B C   
1652 O  O   . LYS   B 160 ? 0.8008 0.6753 0.4893 0.1079 -0.0192 0.0304  169 LYS   B O   
1653 C  CB  . LYS   B 160 ? 0.8007 0.6441 0.4533 0.1242 -0.0436 0.0360  169 LYS   B CB  
1654 C  CG  . LYS   B 160 ? 0.8647 0.6889 0.5162 0.1115 -0.0550 0.0400  169 LYS   B CG  
1655 C  CD  . LYS   B 160 ? 0.9339 0.7505 0.5721 0.0947 -0.0512 0.0494  169 LYS   B CD  
1656 C  CE  . LYS   B 160 ? 0.9845 0.7866 0.6254 0.0766 -0.0564 0.0557  169 LYS   B CE  
1657 N  NZ  . LYS   B 160 ? 1.0129 0.8134 0.6410 0.0585 -0.0469 0.0655  169 LYS   B NZ  
1658 N  N   . ARG   B 161 ? 0.8059 0.6690 0.5046 0.1268 -0.0424 0.0220  170 ARG   B N   
1659 C  CA  . ARG   B 161 ? 0.8179 0.6930 0.5384 0.1144 -0.0370 0.0203  170 ARG   B CA  
1660 C  C   . ARG   B 161 ? 0.8483 0.7143 0.5704 0.0925 -0.0395 0.0276  170 ARG   B C   
1661 O  O   . ARG   B 161 ? 0.8659 0.7096 0.5778 0.0911 -0.0551 0.0306  170 ARG   B O   
1662 C  CB  . ARG   B 161 ? 0.8208 0.6970 0.5548 0.1267 -0.0492 0.0121  170 ARG   B CB  
1663 C  CG  . ARG   B 161 ? 0.8384 0.7301 0.5993 0.1151 -0.0461 0.0094  170 ARG   B CG  
1664 C  CD  . ARG   B 161 ? 0.8800 0.7716 0.6532 0.1282 -0.0616 0.0004  170 ARG   B CD  
1665 N  NE  . ARG   B 161 ? 0.9075 0.8169 0.7106 0.1163 -0.0602 -0.0023 170 ARG   B NE  
1666 C  CZ  . ARG   B 161 ? 0.9190 0.8483 0.7394 0.1256 -0.0563 -0.0091 170 ARG   B CZ  
1667 N  NH1 . ARG   B 161 ? 0.9079 0.8386 0.7164 0.1464 -0.0533 -0.0129 170 ARG   B NH1 
1668 N  NH2 . ARG   B 161 ? 0.9076 0.8562 0.7580 0.1142 -0.0553 -0.0115 170 ARG   B NH2 
1669 N  N   . GLU   B 162 ? 0.8499 0.7319 0.5828 0.0759 -0.0237 0.0310  171 GLU   B N   
1670 C  CA  . GLU   B 162 ? 0.8679 0.7440 0.6015 0.0539 -0.0226 0.0399  171 GLU   B CA  
1671 C  C   . GLU   B 162 ? 0.8713 0.7452 0.6272 0.0455 -0.0346 0.0390  171 GLU   B C   
1672 O  O   . GLU   B 162 ? 0.8720 0.7494 0.6380 0.0249 -0.0299 0.0463  171 GLU   B O   
1673 C  CB  . GLU   B 162 ? 0.8968 0.7938 0.6340 0.0406 -0.0003 0.0432  171 GLU   B CB  
1674 C  CG  . GLU   B 162 ? 0.9823 0.8817 0.6996 0.0475 0.0106  0.0426  171 GLU   B CG  
1675 C  CD  . GLU   B 162 ? 1.0990 0.9770 0.7886 0.0459 0.0033  0.0499  171 GLU   B CD  
1676 O  OE1 . GLU   B 162 ? 1.1226 0.9921 0.8021 0.0298 0.0046  0.0591  171 GLU   B OE1 
1677 O  OE2 . GLU   B 162 ? 1.1367 1.0076 0.8150 0.0610 -0.0035 0.0468  171 GLU   B OE2 
1678 S  S   . DMS   C .   ? 1.0088 0.8398 0.6754 0.0723 0.1030  -0.0346 201 DMS   B S   
1679 O  O   . DMS   C .   ? 1.0005 0.8511 0.6665 0.0787 0.1047  -0.0303 201 DMS   B O   
1680 C  C1  . DMS   C .   ? 1.0155 0.8255 0.6864 0.0845 0.1108  -0.0398 201 DMS   B C1  
1681 C  C2  . DMS   C .   ? 0.9990 0.8318 0.6835 0.0699 0.0995  -0.0191 201 DMS   B C2  
1682 S  S   A DMS   D .   ? 1.0189 1.1195 0.7817 0.1878 0.0952  0.1025  202 DMS   B S   
1683 S  S   B DMS   D .   ? 1.0189 1.1195 0.7817 0.1878 0.0952  0.1025  202 DMS   B S   
1684 O  O   A DMS   D .   ? 1.0239 1.1208 0.7760 0.1959 0.0797  0.0921  202 DMS   B O   
1685 O  O   B DMS   D .   ? 1.0239 1.1208 0.7760 0.1959 0.0797  0.0921  202 DMS   B O   
1686 C  C1  A DMS   D .   ? 1.0233 1.1020 0.7940 0.1600 0.0947  0.0985  202 DMS   B C1  
1687 C  C1  B DMS   D .   ? 1.0233 1.1020 0.7940 0.1600 0.0947  0.0985  202 DMS   B C1  
1688 C  C2  A DMS   D .   ? 0.9954 1.1364 0.7873 0.1799 0.1024  0.1125  202 DMS   B C2  
1689 C  C2  B DMS   D .   ? 0.9954 1.1364 0.7873 0.1799 0.1024  0.1125  202 DMS   B C2  
1690 N  N1  . A1BXF E .   ? 0.9458 1.0979 0.7326 0.1965 0.1523  0.1542  203 A1BXF B N1  
1691 C  C4  . A1BXF E .   ? 0.9786 1.1201 0.7186 0.2403 0.1662  0.1654  203 A1BXF B C4  
1692 C  C5  . A1BXF E .   ? 0.9639 1.0784 0.7028 0.2292 0.1514  0.1510  203 A1BXF B C5  
1693 C  C6  . A1BXF E .   ? 0.9486 1.0331 0.6654 0.2393 0.1422  0.1412  203 A1BXF B C6  
1694 C  C7  . A1BXF E .   ? 0.9438 1.0073 0.6618 0.2277 0.1302  0.1285  203 A1BXF B C7  
1695 C  C8  . A1BXF E .   ? 0.9527 1.0212 0.6899 0.2069 0.1263  0.1246  203 A1BXF B C8  
1696 C  C10 . A1BXF E .   ? 0.9563 1.0771 0.7178 0.2075 0.1457  0.1462  203 A1BXF B C10 
1697 C  C1  . A1BXF E .   ? 0.9645 1.1818 0.7884 0.1925 0.1736  0.1766  203 A1BXF B C1  
1698 C  C2  . A1BXF E .   ? 0.9570 1.1361 0.7482 0.2062 0.1664  0.1678  203 A1BXF B C2  
1699 C  C3  . A1BXF E .   ? 0.9734 1.1480 0.7403 0.2284 0.1745  0.1741  203 A1BXF B C3  
1700 C  C9  . A1BXF E .   ? 0.9599 1.0555 0.7180 0.1970 0.1327  0.1326  203 A1BXF B C9  
1701 CL CL1 . A1BXF E .   ? 0.9627 1.0635 0.7429 0.1720 0.1246  0.1259  203 A1BXF B CL1 
1702 CL CL2 . A1BXF E .   ? 1.0205 1.0628 0.7549 0.1937 0.1132  0.1093  203 A1BXF B CL2 
1703 N  N2  . A1BXF E .   ? 0.9969 1.1328 0.7116 0.2628 0.1718  0.1703  203 A1BXF B N2  
1704 S  S   C SO4   F .   ? 1.9151 1.6085 1.5775 0.1633 0.1982  0.2375  204 SO4   B S   
1705 S  S   D SO4   F .   ? 1.9151 1.6085 1.5775 0.1633 0.1982  0.2375  204 SO4   B S   
1706 O  O1  C SO4   F .   ? 1.9271 1.5794 1.5952 0.1460 0.1981  0.2422  204 SO4   B O1  
1707 O  O1  D SO4   F .   ? 1.9271 1.5794 1.5952 0.1460 0.1981  0.2422  204 SO4   B O1  
1708 O  O2  C SO4   F .   ? 1.9038 1.6182 1.5801 0.1596 0.1882  0.2131  204 SO4   B O2  
1709 O  O2  D SO4   F .   ? 1.9038 1.6182 1.5801 0.1596 0.1882  0.2131  204 SO4   B O2  
1710 O  O3  C SO4   F .   ? 1.9282 1.6095 1.5636 0.1922 0.1950  0.2382  204 SO4   B O3  
1711 O  O3  D SO4   F .   ? 1.9282 1.6095 1.5636 0.1922 0.1950  0.2382  204 SO4   B O3  
1712 O  O4  C SO4   F .   ? 1.9020 1.6278 1.5709 0.1563 0.2111  0.2567  204 SO4   B O4  
1713 O  O4  D SO4   F .   ? 1.9020 1.6278 1.5709 0.1563 0.2111  0.2567  204 SO4   B O4  
1714 S  S   C SO4   G .   ? 1.5054 1.4548 0.9520 0.5791 -0.1019 -0.0432 205 SO4   B S   
1715 S  S   D SO4   G .   ? 1.5054 1.4548 0.9520 0.5791 -0.1019 -0.0432 205 SO4   B S   
1716 O  O1  C SO4   G .   ? 1.4905 1.4750 0.9462 0.5736 -0.0750 -0.0296 205 SO4   B O1  
1717 O  O1  D SO4   G .   ? 1.4905 1.4750 0.9462 0.5736 -0.0750 -0.0296 205 SO4   B O1  
1718 O  O2  C SO4   G .   ? 1.4986 1.4495 0.9690 0.5555 -0.1035 -0.0364 205 SO4   B O2  
1719 O  O2  D SO4   G .   ? 1.4986 1.4495 0.9690 0.5555 -0.1035 -0.0364 205 SO4   B O2  
1720 O  O3  C SO4   G .   ? 1.5222 1.4297 0.9568 0.5716 -0.1212 -0.0525 205 SO4   B O3  
1721 O  O3  D SO4   G .   ? 1.5222 1.4297 0.9568 0.5716 -0.1212 -0.0525 205 SO4   B O3  
1722 O  O4  C SO4   G .   ? 1.5114 1.4664 0.9362 0.6173 -0.1086 -0.0544 205 SO4   B O4  
1723 O  O4  D SO4   G .   ? 1.5114 1.4664 0.9362 0.6173 -0.1086 -0.0544 205 SO4   B O4  
1724 S  S   C DMS   H .   ? 1.4446 1.1924 0.9229 0.4644 -0.2241 -0.0974 206 DMS   B S   
1725 S  S   D DMS   H .   ? 1.4446 1.1924 0.9229 0.4644 -0.2241 -0.0974 206 DMS   B S   
1726 O  O   C DMS   H .   ? 1.4359 1.2136 0.9078 0.4732 -0.1956 -0.0843 206 DMS   B O   
1727 O  O   D DMS   H .   ? 1.4359 1.2136 0.9078 0.4732 -0.1956 -0.0843 206 DMS   B O   
1728 C  C1  C DMS   H .   ? 1.4662 1.1904 0.9064 0.5021 -0.2510 -0.1177 206 DMS   B C1  
1729 C  C1  D DMS   H .   ? 1.4662 1.1904 0.9064 0.5021 -0.2510 -0.1177 206 DMS   B C1  
1730 C  C2  C DMS   H .   ? 1.4371 1.1868 0.9382 0.4495 -0.2329 -0.1013 206 DMS   B C2  
1731 C  C2  D DMS   H .   ? 1.4371 1.1868 0.9382 0.4495 -0.2329 -0.1013 206 DMS   B C2  
# 
