data_7I22
# 
_entry.id   7I22 
# 
_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   7I22         pdb_00007i22 10.2210/pdb7i22/pdb 
WWPDB D_1001408217 ?            ?                   
# 
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                        7I22 
_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    1  ? ?    ? ? 
4 non-polymer syn 'N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]-3-(piperidin-4-yl)propanamide' 327.421   1  ? ?    ? ? 
5 water       nat water                                                                       18.015    68 ? ?    ? ? 
# 
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 'N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]-3-(piperidin-4-yl)propanamide' A1BXV 
5 water                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BXV non-polymer         . 'N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]-3-(piperidin-4-yl)propanamide' ? 'C19 H25 N3 O2'  327.421 
ALA   'L-peptide linking' y ALANINE                                                                     ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                  ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                             ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                    ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                        ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                   ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                             ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                     ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                       ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                  ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                     ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                      ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                  ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                               ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                     ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                      ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                   ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                  ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                    ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                      ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BXV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXV 
_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 4 A1BXV 1  202 203 A1BXV LIG B . 
E 5 HOH   1  101 34  HOH   HOH A . 
E 5 HOH   2  102 118 HOH   HOH A . 
E 5 HOH   3  103 98  HOH   HOH A . 
E 5 HOH   4  104 121 HOH   HOH A . 
E 5 HOH   5  105 123 HOH   HOH A . 
E 5 HOH   6  106 16  HOH   HOH A . 
E 5 HOH   7  107 105 HOH   HOH A . 
E 5 HOH   8  108 20  HOH   HOH A . 
E 5 HOH   9  109 49  HOH   HOH A . 
E 5 HOH   10 110 65  HOH   HOH A . 
E 5 HOH   11 111 120 HOH   HOH A . 
E 5 HOH   12 112 110 HOH   HOH A . 
E 5 HOH   13 113 50  HOH   HOH A . 
E 5 HOH   14 114 29  HOH   HOH A . 
E 5 HOH   15 115 124 HOH   HOH A . 
E 5 HOH   16 116 40  HOH   HOH A . 
E 5 HOH   17 117 119 HOH   HOH A . 
F 5 HOH   1  301 14  HOH   HOH B . 
F 5 HOH   2  302 92  HOH   HOH B . 
F 5 HOH   3  303 48  HOH   HOH B . 
F 5 HOH   4  304 51  HOH   HOH B . 
F 5 HOH   5  305 5   HOH   HOH B . 
F 5 HOH   6  306 46  HOH   HOH B . 
F 5 HOH   7  307 4   HOH   HOH B . 
F 5 HOH   8  308 68  HOH   HOH B . 
F 5 HOH   9  309 58  HOH   HOH B . 
F 5 HOH   10 310 1   HOH   HOH B . 
F 5 HOH   11 311 117 HOH   HOH B . 
F 5 HOH   12 312 100 HOH   HOH B . 
F 5 HOH   13 313 66  HOH   HOH B . 
F 5 HOH   14 314 35  HOH   HOH B . 
F 5 HOH   15 315 32  HOH   HOH B . 
F 5 HOH   16 316 56  HOH   HOH B . 
F 5 HOH   17 317 89  HOH   HOH B . 
F 5 HOH   18 318 2   HOH   HOH B . 
F 5 HOH   19 319 9   HOH   HOH B . 
F 5 HOH   20 320 79  HOH   HOH B . 
F 5 HOH   21 321 54  HOH   HOH B . 
F 5 HOH   22 322 10  HOH   HOH B . 
F 5 HOH   23 323 30  HOH   HOH B . 
F 5 HOH   24 324 24  HOH   HOH B . 
F 5 HOH   25 325 18  HOH   HOH B . 
F 5 HOH   26 326 57  HOH   HOH B . 
F 5 HOH   27 327 62  HOH   HOH B . 
F 5 HOH   28 328 36  HOH   HOH B . 
F 5 HOH   29 329 23  HOH   HOH B . 
F 5 HOH   30 330 3   HOH   HOH B . 
F 5 HOH   31 331 102 HOH   HOH B . 
F 5 HOH   32 332 39  HOH   HOH B . 
F 5 HOH   33 333 69  HOH   HOH B . 
F 5 HOH   34 334 106 HOH   HOH B . 
F 5 HOH   35 335 115 HOH   HOH B . 
F 5 HOH   36 336 64  HOH   HOH B . 
F 5 HOH   37 337 116 HOH   HOH B . 
F 5 HOH   38 338 73  HOH   HOH B . 
F 5 HOH   39 339 12  HOH   HOH B . 
F 5 HOH   40 340 21  HOH   HOH B . 
F 5 HOH   41 341 60  HOH   HOH B . 
F 5 HOH   42 342 61  HOH   HOH B . 
F 5 HOH   43 343 26  HOH   HOH B . 
F 5 HOH   44 344 122 HOH   HOH B . 
F 5 HOH   45 345 107 HOH   HOH B . 
F 5 HOH   46 346 27  HOH   HOH B . 
F 5 HOH   47 347 87  HOH   HOH B . 
F 5 HOH   48 348 72  HOH   HOH B . 
F 5 HOH   49 349 75  HOH   HOH B . 
F 5 HOH   50 350 109 HOH   HOH B . 
F 5 HOH   51 351 44  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       BUSTER  '2.10.4 (20-OCT-2021)' ? 1 ? ? ? ? 
'data scaling'   Aimless .                      ? 2 ? ? ? ? 
phasing          PHASER  .                      ? 3 ? ? ? ? 
'data reduction' XDS     .                      ? 4 ? ? ? ? 
# 
_cell.entry_id           7I22 
_cell.length_a           42.396 
_cell.length_b           42.396 
_cell.length_c           217.025 
_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                         7I22 
_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          7I22 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.10 
_exptl_crystal.density_percent_sol   41.51 
_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   2023-10-11 
_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                     7I22 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.78 
_reflns.d_resolution_high            1.91 
_reflns.number_obs                   16494 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            0.184 
_reflns.pdbx_netI_over_sigmaI        8.5 
_reflns.pdbx_redundancy              25.2 
_reflns.pdbx_Rrim_I_all              0.188 
_reflns.pdbx_Rpim_I_all              0.037 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     415382 
_reflns.pdbx_chi_squared             0.29 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.91 
_reflns_shell.d_res_low                   1.95 
_reflns_shell.number_measured_all         27721 
_reflns_shell.number_unique_obs           1027 
_reflns_shell.Rmerge_I_obs                9.305 
_reflns_shell.pdbx_chi_squared            0.13 
_reflns_shell.pdbx_redundancy             27.0 
_reflns_shell.percent_possible_obs        95.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             9.485 
_reflns_shell.pdbx_Rpim_I_all             1.818 
_reflns_shell.pdbx_CC_half                0.414 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I22 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     15549 
_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                             23.08 
_refine.ls_d_res_high                            1.912 
_refine.ls_percent_reflns_obs                    95.1 
_refine.ls_R_factor_obs                          0.2500 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2481 
_refine.ls_R_factor_R_free                       0.2862 
_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                  746 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.B_iso_mean                               62.77 
_refine.aniso_B[1][1]                            -0.23450 
_refine.aniso_B[2][2]                            -0.23450 
_refine.aniso_B[3][3]                            0.46910 
_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             0.213 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.184 
_refine.pdbx_overall_SU_R_Blow_DPI               0.229 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.190 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I22 
_refine_analyze.Luzzati_coordinate_error_obs    0.39 
_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         28 
_refine_hist.number_atoms_solvent             68 
_refine_hist.number_atoms_total               1572 
_refine_hist.d_res_high                       1.912 
_refine_hist.d_res_low                        23.08 
# 
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  1680 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  2306 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  578  '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  293  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1680 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.20  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           19.20 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  208  '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  1252 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   38 
_refine_ls_shell.d_res_high                       1.91 
_refine_ls_shell.d_res_low                        1.96 
_refine_ls_shell.number_reflns_R_work             400 
_refine_ls_shell.R_factor_R_work                  0.5221 
_refine_ls_shell.percent_reflns_obs               35.38 
_refine_ls_shell.R_factor_R_free                  0.6035 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.99 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                421 
_refine_ls_shell.R_factor_all                     0.5267 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7I22 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with Amine4-Ac06' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I22 
_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 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I22 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I22 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 7I22 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I22 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I22 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I22 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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N 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 ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7I22 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 64  ? ? 73.48  38.47  
2 1 CYS B 80  ? ? 74.42  -14.68 
3 1 LYS B 157 ? C -49.64 -18.85 
4 1 LYS B 157 ? D -49.64 -18.85 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 332 ? F HOH . 
2 1 B HOH 351 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.9485 -1.5288 -19.5108 -0.0254 0.0811 -0.3714 0.1870 0.1410 0.1061 3.0816 5.0635 5.1019 -1.9311 
0.7809 1.3455 0.4844 0.4973 0.0799 -0.5034 -0.3396 -0.2419 -0.4204 0.6856 -0.1448 
'X-RAY DIFFRACTION' 2 ? refined -18.1096 1.0754  -15.7015 0.1923  0.1043 -0.2311 0.1628 0.0423 0.0403 1.1115 1.8816 2.6457 -1.0126 
0.4161 0.3354 0.3192 0.1544 0.1162 -0.1656 -0.2710 -0.0068 -0.0550 0.2308 -0.0482 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BXV N1   N N N 1   
A1BXV N3   N Y N 2   
A1BXV C4   C Y N 3   
A1BXV C5   C N N 4   
A1BXV C6   C Y N 5   
A1BXV C7   C Y N 6   
A1BXV C8   C Y N 7   
A1BXV C10  C Y N 8   
A1BXV C13  C N N 9   
A1BXV C15  C N N 10  
A1BXV C17  C N N 11  
A1BXV C1   C N N 12  
A1BXV C2   C Y N 13  
A1BXV C3   C Y N 14  
A1BXV O1   O N N 15  
A1BXV C9   C Y N 16  
A1BXV C11  C N N 17  
A1BXV O2   O N N 18  
A1BXV C12  C N N 19  
A1BXV C14  C N N 20  
A1BXV C16  C N N 21  
A1BXV N2   N N N 22  
A1BXV C18  C N N 23  
A1BXV C19  C Y N 24  
A1BXV H11  H N N 25  
A1BXV H6   H N N 26  
A1BXV H5   H N N 27  
A1BXV H8   H N N 28  
A1BXV H9   H N N 29  
A1BXV H15  H N N 30  
A1BXV H14  H N N 31  
A1BXV H18  H N N 32  
A1BXV H17  H N N 33  
A1BXV H23  H N N 34  
A1BXV H22  H N N 35  
A1BXV H3   H N N 36  
A1BXV H1   H N N 37  
A1BXV H2   H N N 38  
A1BXV H4   H N N 39  
A1BXV H7   H N N 40  
A1BXV H10  H N N 41  
A1BXV H13  H N N 42  
A1BXV H12  H N N 43  
A1BXV H16  H N N 44  
A1BXV H20  H N N 45  
A1BXV H19  H N N 46  
A1BXV H26  H N N 47  
A1BXV H25  H N N 48  
A1BXV H24  H N N 49  
ALA   N    N N N 50  
ALA   CA   C N S 51  
ALA   C    C N N 52  
ALA   O    O N N 53  
ALA   CB   C N N 54  
ALA   OXT  O N N 55  
ALA   H    H N N 56  
ALA   H2   H N N 57  
ALA   HA   H N N 58  
ALA   HB1  H N N 59  
ALA   HB2  H N N 60  
ALA   HB3  H N N 61  
ALA   HXT  H N N 62  
ARG   N    N N N 63  
ARG   CA   C N S 64  
ARG   C    C N N 65  
ARG   O    O N N 66  
ARG   CB   C N N 67  
ARG   CG   C N N 68  
ARG   CD   C N N 69  
ARG   NE   N N N 70  
ARG   CZ   C N N 71  
ARG   NH1  N N N 72  
ARG   NH2  N N N 73  
ARG   OXT  O N N 74  
ARG   H    H N N 75  
ARG   H2   H N N 76  
ARG   HA   H N N 77  
ARG   HB2  H N N 78  
ARG   HB3  H N N 79  
ARG   HG2  H N N 80  
ARG   HG3  H N N 81  
ARG   HD2  H N N 82  
ARG   HD3  H N N 83  
ARG   HE   H N N 84  
ARG   HH11 H N N 85  
ARG   HH12 H N N 86  
ARG   HH21 H N N 87  
ARG   HH22 H N N 88  
ARG   HXT  H N N 89  
ASN   N    N N N 90  
ASN   CA   C N S 91  
ASN   C    C N N 92  
ASN   O    O N N 93  
ASN   CB   C N N 94  
ASN   CG   C N N 95  
ASN   OD1  O N N 96  
ASN   ND2  N N N 97  
ASN   OXT  O N N 98  
ASN   H    H N N 99  
ASN   H2   H N N 100 
ASN   HA   H N N 101 
ASN   HB2  H N N 102 
ASN   HB3  H N N 103 
ASN   HD21 H N N 104 
ASN   HD22 H N N 105 
ASN   HXT  H N N 106 
ASP   N    N N N 107 
ASP   CA   C N S 108 
ASP   C    C N N 109 
ASP   O    O N N 110 
ASP   CB   C N N 111 
ASP   CG   C N N 112 
ASP   OD1  O N N 113 
ASP   OD2  O N N 114 
ASP   OXT  O N N 115 
ASP   H    H N N 116 
ASP   H2   H N N 117 
ASP   HA   H N N 118 
ASP   HB2  H N N 119 
ASP   HB3  H N N 120 
ASP   HD2  H N N 121 
ASP   HXT  H N N 122 
CYS   N    N N N 123 
CYS   CA   C N R 124 
CYS   C    C N N 125 
CYS   O    O N N 126 
CYS   CB   C N N 127 
CYS   SG   S N N 128 
CYS   OXT  O N N 129 
CYS   H    H N N 130 
CYS   H2   H N N 131 
CYS   HA   H N N 132 
CYS   HB2  H N N 133 
CYS   HB3  H N N 134 
CYS   HG   H N N 135 
CYS   HXT  H N N 136 
DMS   S    S N N 137 
DMS   O    O N N 138 
DMS   C1   C N N 139 
DMS   C2   C N N 140 
DMS   H11  H N N 141 
DMS   H12  H N N 142 
DMS   H13  H N N 143 
DMS   H21  H N N 144 
DMS   H22  H N N 145 
DMS   H23  H N N 146 
GLN   N    N N N 147 
GLN   CA   C N S 148 
GLN   C    C N N 149 
GLN   O    O N N 150 
GLN   CB   C N N 151 
GLN   CG   C N N 152 
GLN   CD   C N N 153 
GLN   OE1  O N N 154 
GLN   NE2  N N N 155 
GLN   OXT  O N N 156 
GLN   H    H N N 157 
GLN   H2   H N N 158 
GLN   HA   H N N 159 
GLN   HB2  H N N 160 
GLN   HB3  H N N 161 
GLN   HG2  H N N 162 
GLN   HG3  H N N 163 
GLN   HE21 H N N 164 
GLN   HE22 H N N 165 
GLN   HXT  H N N 166 
GLU   N    N N N 167 
GLU   CA   C N S 168 
GLU   C    C N N 169 
GLU   O    O N N 170 
GLU   CB   C N N 171 
GLU   CG   C N N 172 
GLU   CD   C N N 173 
GLU   OE1  O N N 174 
GLU   OE2  O N N 175 
GLU   OXT  O N N 176 
GLU   H    H N N 177 
GLU   H2   H N N 178 
GLU   HA   H N N 179 
GLU   HB2  H N N 180 
GLU   HB3  H N N 181 
GLU   HG2  H N N 182 
GLU   HG3  H N N 183 
GLU   HE2  H N N 184 
GLU   HXT  H N N 185 
GLY   N    N N N 186 
GLY   CA   C N N 187 
GLY   C    C N N 188 
GLY   O    O N N 189 
GLY   OXT  O N N 190 
GLY   H    H N N 191 
GLY   H2   H N N 192 
GLY   HA2  H N N 193 
GLY   HA3  H N N 194 
GLY   HXT  H N N 195 
HIS   N    N N N 196 
HIS   CA   C N S 197 
HIS   C    C N N 198 
HIS   O    O N N 199 
HIS   CB   C N N 200 
HIS   CG   C Y N 201 
HIS   ND1  N Y N 202 
HIS   CD2  C Y N 203 
HIS   CE1  C Y N 204 
HIS   NE2  N Y N 205 
HIS   OXT  O N N 206 
HIS   H    H N N 207 
HIS   H2   H N N 208 
HIS   HA   H N N 209 
HIS   HB2  H N N 210 
HIS   HB3  H N N 211 
HIS   HD1  H N N 212 
HIS   HD2  H N N 213 
HIS   HE1  H N N 214 
HIS   HE2  H N N 215 
HIS   HXT  H N N 216 
HOH   O    O N N 217 
HOH   H1   H N N 218 
HOH   H2   H N N 219 
ILE   N    N N N 220 
ILE   CA   C N S 221 
ILE   C    C N N 222 
ILE   O    O N N 223 
ILE   CB   C N S 224 
ILE   CG1  C N N 225 
ILE   CG2  C N N 226 
ILE   CD1  C N N 227 
ILE   OXT  O N N 228 
ILE   H    H N N 229 
ILE   H2   H N N 230 
ILE   HA   H N N 231 
ILE   HB   H N N 232 
ILE   HG12 H N N 233 
ILE   HG13 H N N 234 
ILE   HG21 H N N 235 
ILE   HG22 H N N 236 
ILE   HG23 H N N 237 
ILE   HD11 H N N 238 
ILE   HD12 H N N 239 
ILE   HD13 H N N 240 
ILE   HXT  H N N 241 
LEU   N    N N N 242 
LEU   CA   C N S 243 
LEU   C    C N N 244 
LEU   O    O N N 245 
LEU   CB   C N N 246 
LEU   CG   C N N 247 
LEU   CD1  C N N 248 
LEU   CD2  C N N 249 
LEU   OXT  O N N 250 
LEU   H    H N N 251 
LEU   H2   H N N 252 
LEU   HA   H N N 253 
LEU   HB2  H N N 254 
LEU   HB3  H N N 255 
LEU   HG   H N N 256 
LEU   HD11 H N N 257 
LEU   HD12 H N N 258 
LEU   HD13 H N N 259 
LEU   HD21 H N N 260 
LEU   HD22 H N N 261 
LEU   HD23 H N N 262 
LEU   HXT  H N N 263 
LYS   N    N N N 264 
LYS   CA   C N S 265 
LYS   C    C N N 266 
LYS   O    O N N 267 
LYS   CB   C N N 268 
LYS   CG   C N N 269 
LYS   CD   C N N 270 
LYS   CE   C N N 271 
LYS   NZ   N N N 272 
LYS   OXT  O N N 273 
LYS   H    H N N 274 
LYS   H2   H N N 275 
LYS   HA   H N N 276 
LYS   HB2  H N N 277 
LYS   HB3  H N N 278 
LYS   HG2  H N N 279 
LYS   HG3  H N N 280 
LYS   HD2  H N N 281 
LYS   HD3  H N N 282 
LYS   HE2  H N N 283 
LYS   HE3  H N N 284 
LYS   HZ1  H N N 285 
LYS   HZ2  H N N 286 
LYS   HZ3  H N N 287 
LYS   HXT  H N N 288 
MET   N    N N N 289 
MET   CA   C N S 290 
MET   C    C N N 291 
MET   O    O N N 292 
MET   CB   C N N 293 
MET   CG   C N N 294 
MET   SD   S N N 295 
MET   CE   C N N 296 
MET   OXT  O N N 297 
MET   H    H N N 298 
MET   H2   H N N 299 
MET   HA   H N N 300 
MET   HB2  H N N 301 
MET   HB3  H N N 302 
MET   HG2  H N N 303 
MET   HG3  H N N 304 
MET   HE1  H N N 305 
MET   HE2  H N N 306 
MET   HE3  H N N 307 
MET   HXT  H N N 308 
PHE   N    N N N 309 
PHE   CA   C N S 310 
PHE   C    C N N 311 
PHE   O    O N N 312 
PHE   CB   C N N 313 
PHE   CG   C Y N 314 
PHE   CD1  C Y N 315 
PHE   CD2  C Y N 316 
PHE   CE1  C Y N 317 
PHE   CE2  C Y N 318 
PHE   CZ   C Y N 319 
PHE   OXT  O N N 320 
PHE   H    H N N 321 
PHE   H2   H N N 322 
PHE   HA   H N N 323 
PHE   HB2  H N N 324 
PHE   HB3  H N N 325 
PHE   HD1  H N N 326 
PHE   HD2  H N N 327 
PHE   HE1  H N N 328 
PHE   HE2  H N N 329 
PHE   HZ   H N N 330 
PHE   HXT  H N N 331 
PRO   N    N N N 332 
PRO   CA   C N S 333 
PRO   C    C N N 334 
PRO   O    O N N 335 
PRO   CB   C N N 336 
PRO   CG   C N N 337 
PRO   CD   C N N 338 
PRO   OXT  O N N 339 
PRO   H    H N N 340 
PRO   HA   H N N 341 
PRO   HB2  H N N 342 
PRO   HB3  H N N 343 
PRO   HG2  H N N 344 
PRO   HG3  H N N 345 
PRO   HD2  H N N 346 
PRO   HD3  H N N 347 
PRO   HXT  H N N 348 
SER   N    N N N 349 
SER   CA   C N S 350 
SER   C    C N N 351 
SER   O    O N N 352 
SER   CB   C N N 353 
SER   OG   O N N 354 
SER   OXT  O N N 355 
SER   H    H N N 356 
SER   H2   H N N 357 
SER   HA   H N N 358 
SER   HB2  H N N 359 
SER   HB3  H N N 360 
SER   HG   H N N 361 
SER   HXT  H N N 362 
THR   N    N N N 363 
THR   CA   C N S 364 
THR   C    C N N 365 
THR   O    O N N 366 
THR   CB   C N R 367 
THR   OG1  O N N 368 
THR   CG2  C N N 369 
THR   OXT  O N N 370 
THR   H    H N N 371 
THR   H2   H N N 372 
THR   HA   H N N 373 
THR   HB   H N N 374 
THR   HG1  H N N 375 
THR   HG21 H N N 376 
THR   HG22 H N N 377 
THR   HG23 H N N 378 
THR   HXT  H N N 379 
TRP   N    N N N 380 
TRP   CA   C N S 381 
TRP   C    C N N 382 
TRP   O    O N N 383 
TRP   CB   C N N 384 
TRP   CG   C Y N 385 
TRP   CD1  C Y N 386 
TRP   CD2  C Y N 387 
TRP   NE1  N Y N 388 
TRP   CE2  C Y N 389 
TRP   CE3  C Y N 390 
TRP   CZ2  C Y N 391 
TRP   CZ3  C Y N 392 
TRP   CH2  C Y N 393 
TRP   OXT  O N N 394 
TRP   H    H N N 395 
TRP   H2   H N N 396 
TRP   HA   H N N 397 
TRP   HB2  H N N 398 
TRP   HB3  H N N 399 
TRP   HD1  H N N 400 
TRP   HE1  H N N 401 
TRP   HE3  H N N 402 
TRP   HZ2  H N N 403 
TRP   HZ3  H N N 404 
TRP   HH2  H N N 405 
TRP   HXT  H N N 406 
TYR   N    N N N 407 
TYR   CA   C N S 408 
TYR   C    C N N 409 
TYR   O    O N N 410 
TYR   CB   C N N 411 
TYR   CG   C Y N 412 
TYR   CD1  C Y N 413 
TYR   CD2  C Y N 414 
TYR   CE1  C Y N 415 
TYR   CE2  C Y N 416 
TYR   CZ   C Y N 417 
TYR   OH   O N N 418 
TYR   OXT  O N N 419 
TYR   H    H N N 420 
TYR   H2   H N N 421 
TYR   HA   H N N 422 
TYR   HB2  H N N 423 
TYR   HB3  H N N 424 
TYR   HD1  H N N 425 
TYR   HD2  H N N 426 
TYR   HE1  H N N 427 
TYR   HE2  H N N 428 
TYR   HH   H N N 429 
TYR   HXT  H N N 430 
VAL   N    N N N 431 
VAL   CA   C N S 432 
VAL   C    C N N 433 
VAL   O    O N N 434 
VAL   CB   C N N 435 
VAL   CG1  C N N 436 
VAL   CG2  C N N 437 
VAL   OXT  O N N 438 
VAL   H    H N N 439 
VAL   H2   H N N 440 
VAL   HA   H N N 441 
VAL   HB   H N N 442 
VAL   HG11 H N N 443 
VAL   HG12 H N N 444 
VAL   HG13 H N N 445 
VAL   HG21 H N N 446 
VAL   HG22 H N N 447 
VAL   HG23 H N N 448 
VAL   HXT  H N N 449 
# 
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 
A1BXV C1  C2   sing N N 1   
A1BXV C2  C3   doub Y N 2   
A1BXV C3  C4   sing Y N 3   
A1BXV C4  C5   sing N N 4   
A1BXV C5  O1   sing N N 5   
A1BXV C4  C6   doub Y N 6   
A1BXV C6  C7   sing Y N 7   
A1BXV C7  C8   doub Y N 8   
A1BXV C8  C9   sing Y N 9   
A1BXV C9  C10  doub Y N 10  
A1BXV C10 N1   sing N N 11  
A1BXV N1  C11  sing N N 12  
A1BXV C11 O2   doub N N 13  
A1BXV C11 C12  sing N N 14  
A1BXV C12 C13  sing N N 15  
A1BXV C13 C14  sing N N 16  
A1BXV C14 C15  sing N N 17  
A1BXV C15 C16  sing N N 18  
A1BXV C16 N2   sing N N 19  
A1BXV N2  C17  sing N N 20  
A1BXV C17 C18  sing N N 21  
A1BXV C10 C19  sing Y N 22  
A1BXV C19 N3   doub Y N 23  
A1BXV C2  N3   sing Y N 24  
A1BXV C6  C19  sing Y N 25  
A1BXV C14 C18  sing N N 26  
A1BXV N1  H11  sing N N 27  
A1BXV C5  H6   sing N N 28  
A1BXV C5  H5   sing N N 29  
A1BXV C7  H8   sing N N 30  
A1BXV C8  H9   sing N N 31  
A1BXV C13 H15  sing N N 32  
A1BXV C13 H14  sing N N 33  
A1BXV C15 H18  sing N N 34  
A1BXV C15 H17  sing N N 35  
A1BXV C17 H23  sing N N 36  
A1BXV C17 H22  sing N N 37  
A1BXV C1  H3   sing N N 38  
A1BXV C1  H1   sing N N 39  
A1BXV C1  H2   sing N N 40  
A1BXV C3  H4   sing N N 41  
A1BXV O1  H7   sing N N 42  
A1BXV C9  H10  sing N N 43  
A1BXV C12 H13  sing N N 44  
A1BXV C12 H12  sing N N 45  
A1BXV C14 H16  sing N N 46  
A1BXV C16 H20  sing N N 47  
A1BXV C16 H19  sing N N 48  
A1BXV N2  H26  sing N N 49  
A1BXV C18 H25  sing N N 50  
A1BXV C18 H24  sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
DMS   S   O    doub N N 134 
DMS   S   C1   sing N N 135 
DMS   S   C2   sing N N 136 
DMS   C1  H11  sing N N 137 
DMS   C1  H12  sing N N 138 
DMS   C1  H13  sing N N 139 
DMS   C2  H21  sing N N 140 
DMS   C2  H22  sing N N 141 
DMS   C2  H23  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
HOH   O   H1   sing N N 210 
HOH   O   H2   sing N N 211 
ILE   N   CA   sing N N 212 
ILE   N   H    sing N N 213 
ILE   N   H2   sing N N 214 
ILE   CA  C    sing N N 215 
ILE   CA  CB   sing N N 216 
ILE   CA  HA   sing N N 217 
ILE   C   O    doub N N 218 
ILE   C   OXT  sing N N 219 
ILE   CB  CG1  sing N N 220 
ILE   CB  CG2  sing N N 221 
ILE   CB  HB   sing N N 222 
ILE   CG1 CD1  sing N N 223 
ILE   CG1 HG12 sing N N 224 
ILE   CG1 HG13 sing N N 225 
ILE   CG2 HG21 sing N N 226 
ILE   CG2 HG22 sing N N 227 
ILE   CG2 HG23 sing N N 228 
ILE   CD1 HD11 sing N N 229 
ILE   CD1 HD12 sing N N 230 
ILE   CD1 HD13 sing N N 231 
ILE   OXT HXT  sing N N 232 
LEU   N   CA   sing N N 233 
LEU   N   H    sing N N 234 
LEU   N   H2   sing N N 235 
LEU   CA  C    sing N N 236 
LEU   CA  CB   sing N N 237 
LEU   CA  HA   sing N N 238 
LEU   C   O    doub N N 239 
LEU   C   OXT  sing N N 240 
LEU   CB  CG   sing N N 241 
LEU   CB  HB2  sing N N 242 
LEU   CB  HB3  sing N N 243 
LEU   CG  CD1  sing N N 244 
LEU   CG  CD2  sing N N 245 
LEU   CG  HG   sing N N 246 
LEU   CD1 HD11 sing N N 247 
LEU   CD1 HD12 sing N N 248 
LEU   CD1 HD13 sing N N 249 
LEU   CD2 HD21 sing N N 250 
LEU   CD2 HD22 sing N N 251 
LEU   CD2 HD23 sing N N 252 
LEU   OXT HXT  sing N N 253 
LYS   N   CA   sing N N 254 
LYS   N   H    sing N N 255 
LYS   N   H2   sing N N 256 
LYS   CA  C    sing N N 257 
LYS   CA  CB   sing N N 258 
LYS   CA  HA   sing N N 259 
LYS   C   O    doub N N 260 
LYS   C   OXT  sing N N 261 
LYS   CB  CG   sing N N 262 
LYS   CB  HB2  sing N N 263 
LYS   CB  HB3  sing N N 264 
LYS   CG  CD   sing N N 265 
LYS   CG  HG2  sing N N 266 
LYS   CG  HG3  sing N N 267 
LYS   CD  CE   sing N N 268 
LYS   CD  HD2  sing N N 269 
LYS   CD  HD3  sing N N 270 
LYS   CE  NZ   sing N N 271 
LYS   CE  HE2  sing N N 272 
LYS   CE  HE3  sing N N 273 
LYS   NZ  HZ1  sing N N 274 
LYS   NZ  HZ2  sing N N 275 
LYS   NZ  HZ3  sing N N 276 
LYS   OXT HXT  sing N N 277 
MET   N   CA   sing N N 278 
MET   N   H    sing N N 279 
MET   N   H2   sing N N 280 
MET   CA  C    sing N N 281 
MET   CA  CB   sing N N 282 
MET   CA  HA   sing N N 283 
MET   C   O    doub N N 284 
MET   C   OXT  sing N N 285 
MET   CB  CG   sing N N 286 
MET   CB  HB2  sing N N 287 
MET   CB  HB3  sing N N 288 
MET   CG  SD   sing N N 289 
MET   CG  HG2  sing N N 290 
MET   CG  HG3  sing N N 291 
MET   SD  CE   sing N N 292 
MET   CE  HE1  sing N N 293 
MET   CE  HE2  sing N N 294 
MET   CE  HE3  sing N N 295 
MET   OXT HXT  sing N N 296 
PHE   N   CA   sing N N 297 
PHE   N   H    sing N N 298 
PHE   N   H2   sing N N 299 
PHE   CA  C    sing N N 300 
PHE   CA  CB   sing N N 301 
PHE   CA  HA   sing N N 302 
PHE   C   O    doub N N 303 
PHE   C   OXT  sing N N 304 
PHE   CB  CG   sing N N 305 
PHE   CB  HB2  sing N N 306 
PHE   CB  HB3  sing N N 307 
PHE   CG  CD1  doub Y N 308 
PHE   CG  CD2  sing Y N 309 
PHE   CD1 CE1  sing Y N 310 
PHE   CD1 HD1  sing N N 311 
PHE   CD2 CE2  doub Y N 312 
PHE   CD2 HD2  sing N N 313 
PHE   CE1 CZ   doub Y N 314 
PHE   CE1 HE1  sing N N 315 
PHE   CE2 CZ   sing Y N 316 
PHE   CE2 HE2  sing N N 317 
PHE   CZ  HZ   sing N N 318 
PHE   OXT HXT  sing N N 319 
PRO   N   CA   sing N N 320 
PRO   N   CD   sing N N 321 
PRO   N   H    sing N N 322 
PRO   CA  C    sing N N 323 
PRO   CA  CB   sing N N 324 
PRO   CA  HA   sing N N 325 
PRO   C   O    doub N N 326 
PRO   C   OXT  sing N N 327 
PRO   CB  CG   sing N N 328 
PRO   CB  HB2  sing N N 329 
PRO   CB  HB3  sing N N 330 
PRO   CG  CD   sing N N 331 
PRO   CG  HG2  sing N N 332 
PRO   CG  HG3  sing N N 333 
PRO   CD  HD2  sing N N 334 
PRO   CD  HD3  sing N N 335 
PRO   OXT HXT  sing N N 336 
SER   N   CA   sing N N 337 
SER   N   H    sing N N 338 
SER   N   H2   sing N N 339 
SER   CA  C    sing N N 340 
SER   CA  CB   sing N N 341 
SER   CA  HA   sing N N 342 
SER   C   O    doub N N 343 
SER   C   OXT  sing N N 344 
SER   CB  OG   sing N N 345 
SER   CB  HB2  sing N N 346 
SER   CB  HB3  sing N N 347 
SER   OG  HG   sing N N 348 
SER   OXT HXT  sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TRP   N   CA   sing N N 366 
TRP   N   H    sing N N 367 
TRP   N   H2   sing N N 368 
TRP   CA  C    sing N N 369 
TRP   CA  CB   sing N N 370 
TRP   CA  HA   sing N N 371 
TRP   C   O    doub N N 372 
TRP   C   OXT  sing N N 373 
TRP   CB  CG   sing N N 374 
TRP   CB  HB2  sing N N 375 
TRP   CB  HB3  sing N N 376 
TRP   CG  CD1  doub Y N 377 
TRP   CG  CD2  sing Y N 378 
TRP   CD1 NE1  sing Y N 379 
TRP   CD1 HD1  sing N N 380 
TRP   CD2 CE2  doub Y N 381 
TRP   CD2 CE3  sing Y N 382 
TRP   NE1 CE2  sing Y N 383 
TRP   NE1 HE1  sing N N 384 
TRP   CE2 CZ2  sing Y N 385 
TRP   CE3 CZ3  doub Y N 386 
TRP   CE3 HE3  sing N N 387 
TRP   CZ2 CH2  doub Y N 388 
TRP   CZ2 HZ2  sing N N 389 
TRP   CZ3 CH2  sing Y N 390 
TRP   CZ3 HZ3  sing N N 391 
TRP   CH2 HH2  sing N N 392 
TRP   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_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                    7I22 
_atom_sites.fract_transf_matrix[1][1]   0.023587 
_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]   0.023587 
_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]   0.004608 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -21.058 19.565  -7.322  1.00 73.52  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.243 18.722  -7.418  1.00 73.64  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.408 18.094  -8.827  1.00 71.77  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.427 18.802  -9.843  1.00 72.12  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.487 19.493  -6.950  1.00 77.26  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.751 18.662  -6.930  1.00 84.94  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.963 17.910  -5.929  1.00 85.54  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.534 18.756  -7.908  1.00 88.53  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.505 16.750  -8.860  1.00 69.18  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.604 15.926  -10.064 1.00 67.12  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -24.013 15.655  -10.559 1.00 65.42  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.940 15.569  -9.752  1.00 65.29  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.917 14.584  -9.833  1.00 66.74  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.466 14.700  -9.571  1.00 68.05  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.771 13.063  -9.304  1.00 71.73  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.072 13.505  -9.058  1.00 71.71  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.155 15.458  -11.893 1.00 63.84  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.426 15.167  -12.554 1.00 63.44  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.285 14.159  -13.710 1.00 62.65  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.188 13.955  -14.227 1.00 62.52  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.145 16.458  -13.006 1.00 63.97  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.426 17.224  -14.095 1.00 65.69  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.515 18.225  -13.783 1.00 66.80  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.691 16.979  -15.439 1.00 66.90  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.838 18.917  -14.779 1.00 67.92  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -25.023 17.669  -16.445 1.00 67.84  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -24.101 18.642  -16.111 1.00 69.11  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.423 19.320  -17.097 1.00 71.20  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.393 13.503  -14.096 1.00 61.91  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.367 12.532  -15.189 1.00 61.55  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.168 13.002  -16.435 1.00 61.76  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.165 13.720  -16.314 1.00 62.11  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.779 11.104  -14.741 1.00 61.40  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.198 11.063  -14.169 1.00 61.92  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.766 10.501  -13.771 1.00 61.88  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.745 9.653   -14.003 1.00 62.56  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.700 12.604  -17.630 1.00 61.68  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.320 12.909  -18.932 1.00 62.03  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.322 11.634  -19.769 1.00 61.67  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.269 11.004  -19.892 1.00 61.34  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.503 13.956  -19.713 1.00 64.54  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.482 15.350  -19.123 1.00 71.51  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.751 16.358  -19.991 1.00 82.17  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.886 15.941  -20.796 1.00 83.71  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -26.039 17.572  -19.862 1.00 87.08  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.460 11.270  -20.387 1.00 61.31  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.497 10.048  -21.208 1.00 61.51  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.537 10.126  -22.394 1.00 61.51  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.405 11.189  -22.993 1.00 61.93  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.922 9.760   -21.702 1.00 62.86  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.149 8.279   -21.924 1.00 64.94  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.599 7.888   -22.079 1.00 67.23  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.698 6.446   -22.293 1.00 70.34  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.690 5.873   -23.494 1.00 72.56  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.644 6.617   -24.592 1.00 73.53  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.711 4.548   -23.605 1.00 70.63  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.866 9.013   -22.726 1.00 61.13  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.949 8.937   -23.870 1.00 61.51  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.320 7.851   -24.896 1.00 61.61  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.655 7.756   -25.929 1.00 62.31  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.514 8.738   -23.404 1.00 61.89  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.342 7.035   -24.620 1.00 60.45  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.741 5.990   -25.564 1.00 58.89  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.252 4.697   -24.958 1.00 56.73  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.318 4.553   -23.736 1.00 55.56  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.653 3.751   -25.834 1.00 55.59  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.158 2.431   -25.442 1.00 54.68  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.054 1.451   -25.256 1.00 55.91  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.054 1.558   -25.944 1.00 56.92  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.053 1.851   -26.561 1.00 53.89  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.376 2.547   -26.723 1.00 56.28  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.621 3.497   -26.000 1.00 56.71  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.162 2.138   -27.612 1.00 58.37  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.287 0.407   -24.461 1.00 55.94  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.308 -0.669  -24.334 1.00 56.97  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.787 -1.760  -25.277 1.00 59.14  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.716 -2.511  -24.973 1.00 59.34  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.160 -1.090  -22.888 1.00 56.58  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.650 0.120   -22.096 1.00 57.20  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.199 -2.286  -22.791 1.00 56.94  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.765 0.016   -20.674 1.00 58.40  ? 59  ILE   A CD1 1 
ATOM   82   N N   B THR   A 1 17  ? -27.191 -1.789  -26.466 0.50 60.05  ? 60  THR   A N   1 
ATOM   83   N N   D THR   A 1 17  ? -27.191 -1.789  -26.466 0.50 60.05  ? 60  THR   A N   1 
ATOM   84   C CA  B THR   A 1 17  ? -27.544 -2.712  -27.537 0.50 61.63  ? 60  THR   A CA  1 
ATOM   85   C CA  D THR   A 1 17  ? -27.544 -2.712  -27.537 0.50 61.63  ? 60  THR   A CA  1 
ATOM   86   C C   B THR   A 1 17  ? -26.272 -3.202  -28.241 0.50 62.65  ? 60  THR   A C   1 
ATOM   87   C C   D THR   A 1 17  ? -26.272 -3.202  -28.241 0.50 62.65  ? 60  THR   A C   1 
ATOM   88   O O   B THR   A 1 17  ? -25.339 -2.426  -28.425 0.50 62.50  ? 60  THR   A O   1 
ATOM   89   O O   D THR   A 1 17  ? -25.339 -2.426  -28.425 0.50 62.50  ? 60  THR   A O   1 
ATOM   90   C CB  B THR   A 1 17  ? -28.524 -1.997  -28.497 0.50 63.61  ? 60  THR   A CB  1 
ATOM   91   C CB  D THR   A 1 17  ? -28.524 -1.997  -28.497 0.50 63.61  ? 60  THR   A CB  1 
ATOM   92   O OG1 B THR   A 1 17  ? -29.794 -1.859  -27.858 0.50 64.67  ? 60  THR   A OG1 1 
ATOM   93   O OG1 D THR   A 1 17  ? -29.794 -1.859  -27.858 0.50 64.67  ? 60  THR   A OG1 1 
ATOM   94   C CG2 B THR   A 1 17  ? -28.717 -2.720  -29.799 0.50 64.45  ? 60  THR   A CG2 1 
ATOM   95   C CG2 D THR   A 1 17  ? -28.717 -2.720  -29.799 0.50 64.45  ? 60  THR   A CG2 1 
ATOM   96   N N   . TRP   A 1 18  ? -26.216 -4.491  -28.596 1.00 63.71  ? 61  TRP   A N   1 
ATOM   97   C CA  . TRP   A 1 18  ? -25.081 -5.037  -29.342 1.00 67.18  ? 61  TRP   A CA  1 
ATOM   98   C C   . TRP   A 1 18  ? -25.258 -4.532  -30.793 1.00 71.32  ? 61  TRP   A C   1 
ATOM   99   O O   . TRP   A 1 18  ? -26.363 -4.618  -31.332 1.00 72.17  ? 61  TRP   A O   1 
ATOM   100  C CB  . TRP   A 1 18  ? -25.120 -6.575  -29.329 1.00 66.96  ? 61  TRP   A CB  1 
ATOM   101  C CG  . TRP   A 1 18  ? -24.080 -7.249  -30.187 1.00 67.44  ? 61  TRP   A CG  1 
ATOM   102  C CD1 . TRP   A 1 18  ? -24.210 -7.618  -31.496 1.00 68.51  ? 61  TRP   A CD1 1 
ATOM   103  C CD2 . TRP   A 1 18  ? -22.799 -7.735  -29.762 1.00 67.23  ? 61  TRP   A CD2 1 
ATOM   104  N NE1 . TRP   A 1 18  ? -23.062 -8.235  -31.929 1.00 68.63  ? 61  TRP   A NE1 1 
ATOM   105  C CE2 . TRP   A 1 18  ? -22.192 -8.348  -30.876 1.00 68.13  ? 61  TRP   A CE2 1 
ATOM   106  C CE3 . TRP   A 1 18  ? -22.093 -7.685  -28.552 1.00 67.29  ? 61  TRP   A CE3 1 
ATOM   107  C CZ2 . TRP   A 1 18  ? -20.925 -8.931  -30.808 1.00 68.53  ? 61  TRP   A CZ2 1 
ATOM   108  C CZ3 . TRP   A 1 18  ? -20.856 -8.288  -28.479 1.00 67.94  ? 61  TRP   A CZ3 1 
ATOM   109  C CH2 . TRP   A 1 18  ? -20.269 -8.872  -29.601 1.00 68.32  ? 61  TRP   A CH2 1 
ATOM   110  N N   . GLU   A 1 19  ? -24.206 -3.972  -31.409 1.00 73.95  ? 62  GLU   A N   1 
ATOM   111  C CA  . GLU   A 1 19  ? -24.331 -3.440  -32.759 1.00 77.37  ? 62  GLU   A CA  1 
ATOM   112  C C   . GLU   A 1 19  ? -23.581 -4.278  -33.791 1.00 80.90  ? 62  GLU   A C   1 
ATOM   113  O O   . GLU   A 1 19  ? -22.366 -4.473  -33.678 1.00 81.00  ? 62  GLU   A O   1 
ATOM   114  C CB  . GLU   A 1 19  ? -23.944 -1.959  -32.807 1.00 80.45  ? 62  GLU   A CB  1 
ATOM   115  C CG  . GLU   A 1 19  ? -24.637 -1.110  -31.741 1.00 86.79  ? 62  GLU   A CG  1 
ATOM   116  C CD  . GLU   A 1 19  ? -26.116 -0.768  -31.851 1.00 96.23  ? 62  GLU   A CD  1 
ATOM   117  O OE1 . GLU   A 1 19  ? -26.744 -1.094  -32.887 1.00 98.53  ? 62  GLU   A OE1 1 
ATOM   118  O OE2 . GLU   A 1 19  ? -26.642 -0.143  -30.898 1.00 98.84  ? 62  GLU   A OE2 1 
ATOM   119  N N   . LYS   A 1 20  ? -24.325 -4.836  -34.760 1.00 83.37  ? 63  LYS   A N   1 
ATOM   120  C CA  . LYS   A 1 20  ? -23.732 -5.677  -35.796 1.00 86.79  ? 63  LYS   A CA  1 
ATOM   121  C C   . LYS   A 1 20  ? -22.863 -4.824  -36.692 1.00 88.57  ? 63  LYS   A C   1 
ATOM   122  O O   . LYS   A 1 20  ? -23.295 -3.750  -37.131 1.00 88.95  ? 63  LYS   A O   1 
ATOM   123  C CB  . LYS   A 1 20  ? -24.822 -6.351  -36.656 1.00 90.53  ? 63  LYS   A CB  1 
ATOM   124  C CG  . LYS   A 1 20  ? -25.604 -7.445  -35.937 1.00 96.58  ? 63  LYS   A CG  1 
ATOM   125  C CD  . LYS   A 1 20  ? -26.799 -7.896  -36.772 1.00 101.36 ? 63  LYS   A CD  1 
ATOM   126  C CE  . LYS   A 1 20  ? -27.672 -8.887  -36.043 1.00 105.76 ? 63  LYS   A CE  1 
ATOM   127  N NZ  . LYS   A 1 20  ? -28.762 -9.395  -36.916 1.00 108.53 ? 63  LYS   A NZ  1 
ATOM   128  N N   . ASP   A 1 21  ? -21.648 -5.305  -36.965 1.00 89.34  ? 64  ASP   A N   1 
ATOM   129  C CA  . ASP   A 1 21  ? -20.669 -4.632  -37.825 1.00 90.96  ? 64  ASP   A CA  1 
ATOM   130  C C   . ASP   A 1 21  ? -20.038 -3.416  -37.157 1.00 90.96  ? 64  ASP   A C   1 
ATOM   131  O O   . ASP   A 1 21  ? -19.779 -2.399  -37.813 1.00 91.41  ? 64  ASP   A O   1 
ATOM   132  C CB  . ASP   A 1 21  ? -21.220 -4.287  -39.227 1.00 93.76  ? 64  ASP   A CB  1 
ATOM   133  C CG  . ASP   A 1 21  ? -21.597 -5.499  -40.050 1.00 100.91 ? 64  ASP   A CG  1 
ATOM   134  O OD1 . ASP   A 1 21  ? -20.873 -6.519  -39.971 1.00 102.95 ? 64  ASP   A OD1 1 
ATOM   135  O OD2 . ASP   A 1 21  ? -22.612 -5.427  -40.780 1.00 103.36 ? 64  ASP   A OD2 1 
ATOM   136  N N   . ALA   A 1 22  ? -19.771 -3.536  -35.852 1.00 90.20  ? 65  ALA   A N   1 
ATOM   137  C CA  . ALA   A 1 22  ? -19.056 -2.517  -35.103 1.00 89.79  ? 65  ALA   A CA  1 
ATOM   138  C C   . ALA   A 1 22  ? -17.547 -2.686  -35.422 1.00 89.57  ? 65  ALA   A C   1 
ATOM   139  O O   . ALA   A 1 22  ? -17.119 -3.734  -35.918 1.00 89.13  ? 65  ALA   A O   1 
ATOM   140  C CB  . ALA   A 1 22  ? -19.305 -2.704  -33.612 1.00 89.80  ? 65  ALA   A CB  1 
ATOM   141  N N   . GLU   A 1 23  ? -16.748 -1.654  -35.151 1.00 89.64  ? 66  GLU   A N   1 
ATOM   142  C CA  . GLU   A 1 23  ? -15.303 -1.682  -35.397 1.00 89.85  ? 66  GLU   A CA  1 
ATOM   143  C C   . GLU   A 1 23  ? -14.627 -2.700  -34.458 1.00 88.10  ? 66  GLU   A C   1 
ATOM   144  O O   . GLU   A 1 23  ? -14.766 -2.603  -33.248 1.00 87.50  ? 66  GLU   A O   1 
ATOM   145  C CB  . GLU   A 1 23  ? -14.742 -0.260  -35.200 1.00 94.17  ? 66  GLU   A CB  1 
ATOM   146  C CG  . GLU   A 1 23  ? -13.232 -0.106  -35.268 1.00 101.04 ? 66  GLU   A CG  1 
ATOM   147  C CD  . GLU   A 1 23  ? -12.702 0.919   -34.277 1.00 108.77 ? 66  GLU   A CD  1 
ATOM   148  O OE1 . GLU   A 1 23  ? -13.467 1.835   -33.890 1.00 108.88 ? 66  GLU   A OE1 1 
ATOM   149  O OE2 . GLU   A 1 23  ? -11.516 0.809   -33.889 1.00 111.79 ? 66  GLU   A OE2 1 
ATOM   150  N N   . VAL   A 1 24  ? -13.943 -3.702  -35.035 1.00 87.00  ? 67  VAL   A N   1 
ATOM   151  C CA  . VAL   A 1 24  ? -13.279 -4.781  -34.299 1.00 86.06  ? 67  VAL   A CA  1 
ATOM   152  C C   . VAL   A 1 24  ? -11.792 -4.481  -34.095 1.00 85.60  ? 67  VAL   A C   1 
ATOM   153  O O   . VAL   A 1 24  ? -11.024 -4.521  -35.044 1.00 85.85  ? 67  VAL   A O   1 
ATOM   154  C CB  . VAL   A 1 24  ? -13.475 -6.160  -34.983 1.00 86.08  ? 67  VAL   A CB  1 
ATOM   155  C CG1 . VAL   A 1 24  ? -13.058 -7.277  -34.057 1.00 86.41  ? 67  VAL   A CG1 1 
ATOM   156  C CG2 . VAL   A 1 24  ? -14.914 -6.370  -35.440 1.00 86.42  ? 67  VAL   A CG2 1 
ATOM   157  N N   . THR   A 1 25  ? -11.384 -4.172  -32.863 1.00 85.07  ? 68  THR   A N   1 
ATOM   158  C CA  . THR   A 1 25  ? -9.988  -3.844  -32.561 1.00 84.77  ? 68  THR   A CA  1 
ATOM   159  C C   . THR   A 1 25  ? -9.605  -4.328  -31.147 1.00 84.38  ? 68  THR   A C   1 
ATOM   160  O O   . THR   A 1 25  ? -10.454 -4.835  -30.440 1.00 84.30  ? 68  THR   A O   1 
ATOM   161  C CB  . THR   A 1 25  ? -9.768  -2.334  -32.758 1.00 85.78  ? 68  THR   A CB  1 
ATOM   162  O OG1 . THR   A 1 25  ? -8.367  -2.078  -32.840 1.00 86.76  ? 68  THR   A OG1 1 
ATOM   163  C CG2 . THR   A 1 25  ? -10.388 -1.517  -31.650 1.00 85.76  ? 68  THR   A CG2 1 
ATOM   164  N N   . GLY   A 1 26  ? -8.332  -4.227  -30.767 1.00 84.15  ? 69  GLY   A N   1 
ATOM   165  C CA  . GLY   A 1 26  ? -7.885  -4.624  -29.439 1.00 84.17  ? 69  GLY   A CA  1 
ATOM   166  C C   . GLY   A 1 26  ? -7.389  -6.048  -29.315 1.00 83.84  ? 69  GLY   A C   1 
ATOM   167  O O   . GLY   A 1 26  ? -8.066  -6.987  -29.737 1.00 84.02  ? 69  GLY   A O   1 
ATOM   168  N N   . ASN   A 1 27  ? -6.217  -6.222  -28.690 1.00 83.06  ? 70  ASN   A N   1 
ATOM   169  C CA  . ASN   A 1 27  ? -5.654  -7.552  -28.476 1.00 82.80  ? 70  ASN   A CA  1 
ATOM   170  C C   . ASN   A 1 27  ? -6.199  -8.215  -27.161 1.00 81.55  ? 70  ASN   A C   1 
ATOM   171  O O   . ASN   A 1 27  ? -7.035  -7.616  -26.486 1.00 81.79  ? 70  ASN   A O   1 
ATOM   172  C CB  . ASN   A 1 27  ? -4.109  -7.510  -28.555 1.00 84.89  ? 70  ASN   A CB  1 
ATOM   173  C CG  . ASN   A 1 27  ? -3.484  -6.882  -27.339 1.00 88.68  ? 70  ASN   A CG  1 
ATOM   174  O OD1 . ASN   A 1 27  ? -3.874  -5.786  -26.916 1.00 89.87  ? 70  ASN   A OD1 1 
ATOM   175  N ND2 . ASN   A 1 27  ? -2.518  -7.568  -26.737 1.00 88.72  ? 70  ASN   A ND2 1 
ATOM   176  N N   . SER   A 1 28  ? -5.787  -9.464  -26.833 1.00 80.34  ? 71  SER   A N   1 
ATOM   177  C CA  . SER   A 1 28  ? -6.270  -10.197 -25.646 1.00 79.12  ? 71  SER   A CA  1 
ATOM   178  C C   . SER   A 1 28  ? -5.100  -10.687 -24.776 1.00 77.56  ? 71  SER   A C   1 
ATOM   179  O O   . SER   A 1 28  ? -4.790  -11.878 -24.765 1.00 77.84  ? 71  SER   A O   1 
ATOM   180  C CB  . SER   A 1 28  ? -7.124  -11.395 -26.064 1.00 80.76  ? 71  SER   A CB  1 
ATOM   181  O OG  . SER   A 1 28  ? -7.898  -11.170 -27.229 1.00 84.44  ? 71  SER   A OG  1 
ATOM   182  N N   . PRO   A 1 29  ? -4.428  -9.797  -24.034 1.00 76.30  ? 72  PRO   A N   1 
ATOM   183  C CA  . PRO   A 1 29  ? -3.262  -10.236 -23.251 1.00 75.83  ? 72  PRO   A CA  1 
ATOM   184  C C   . PRO   A 1 29  ? -3.601  -10.940 -21.941 1.00 74.89  ? 72  PRO   A C   1 
ATOM   185  O O   . PRO   A 1 29  ? -4.630  -10.660 -21.338 1.00 74.38  ? 72  PRO   A O   1 
ATOM   186  C CB  . PRO   A 1 29  ? -2.493  -8.938  -23.023 1.00 76.77  ? 72  PRO   A CB  1 
ATOM   187  C CG  . PRO   A 1 29  ? -3.567  -7.897  -22.956 1.00 77.48  ? 72  PRO   A CG  1 
ATOM   188  C CD  . PRO   A 1 29  ? -4.652  -8.343  -23.906 1.00 75.95  ? 72  PRO   A CD  1 
ATOM   189  N N   . ARG   A 1 30  ? -2.742  -11.875 -21.519 1.00 74.56  ? 73  ARG   A N   1 
ATOM   190  C CA  . ARG   A 1 30  ? -2.896  -12.585 -20.249 1.00 75.04  ? 73  ARG   A CA  1 
ATOM   191  C C   . ARG   A 1 30  ? -1.847  -12.019 -19.308 1.00 73.87  ? 73  ARG   A C   1 
ATOM   192  O O   . ARG   A 1 30  ? -0.650  -12.184 -19.548 1.00 74.08  ? 73  ARG   A O   1 
ATOM   193  C CB  . ARG   A 1 30  ? -2.764  -14.107 -20.420 1.00 78.17  ? 73  ARG   A CB  1 
ATOM   194  C CG  . ARG   A 1 30  ? -3.927  -14.673 -21.227 1.00 84.86  ? 73  ARG   A CG  1 
ATOM   195  C CD  . ARG   A 1 30  ? -3.903  -16.185 -21.374 1.00 91.70  ? 73  ARG   A CD  1 
ATOM   196  N NE  . ARG   A 1 30  ? -4.935  -16.616 -22.320 1.00 97.44  ? 73  ARG   A NE  1 
ATOM   197  C CZ  . ARG   A 1 30  ? -5.475  -17.831 -22.350 1.00 101.02 ? 73  ARG   A CZ  1 
ATOM   198  N NH1 . ARG   A 1 30  ? -5.078  -18.765 -21.491 1.00 101.56 ? 73  ARG   A NH1 1 
ATOM   199  N NH2 . ARG   A 1 30  ? -6.419  -18.122 -23.239 1.00 100.48 ? 73  ARG   A NH2 1 
ATOM   200  N N   . LEU   A 1 31  ? -2.302  -11.283 -18.280 1.00 72.52  ? 74  LEU   A N   1 
ATOM   201  C CA  . LEU   A 1 31  ? -1.427  -10.585 -17.344 1.00 71.60  ? 74  LEU   A CA  1 
ATOM   202  C C   . LEU   A 1 31  ? -1.532  -11.112 -15.920 1.00 70.63  ? 74  LEU   A C   1 
ATOM   203  O O   . LEU   A 1 31  ? -2.631  -11.392 -15.461 1.00 70.44  ? 74  LEU   A O   1 
ATOM   204  C CB  . LEU   A 1 31  ? -1.805  -9.093  -17.335 1.00 71.56  ? 74  LEU   A CB  1 
ATOM   205  C CG  . LEU   A 1 31  ? -1.849  -8.405  -18.691 1.00 72.79  ? 74  LEU   A CG  1 
ATOM   206  C CD1 . LEU   A 1 31  ? -2.559  -7.078  -18.602 1.00 73.15  ? 74  LEU   A CD1 1 
ATOM   207  C CD2 . LEU   A 1 31  ? -0.456  -8.258  -19.267 1.00 73.05  ? 74  LEU   A CD2 1 
ATOM   208  N N   . ASP   A 1 32  ? -0.398  -11.193 -15.195 1.00 69.85  ? 75  ASP   A N   1 
ATOM   209  C CA  . ASP   A 1 32  ? -0.430  -11.583 -13.787 1.00 69.44  ? 75  ASP   A CA  1 
ATOM   210  C C   . ASP   A 1 32  ? -0.623  -10.295 -13.009 1.00 67.66  ? 75  ASP   A C   1 
ATOM   211  O O   . ASP   A 1 32  ? 0.248   -9.427  -13.069 1.00 68.44  ? 75  ASP   A O   1 
ATOM   212  C CB  . ASP   A 1 32  ? 0.891   -12.230 -13.362 1.00 72.50  ? 75  ASP   A CB  1 
ATOM   213  C CG  . ASP   A 1 32  ? 1.189   -13.540 -14.056 1.00 80.73  ? 75  ASP   A CG  1 
ATOM   214  O OD1 . ASP   A 1 32  ? 0.235   -14.171 -14.579 1.00 81.93  ? 75  ASP   A OD1 1 
ATOM   215  O OD2 . ASP   A 1 32  ? 2.376   -13.938 -14.080 1.00 84.82  ? 75  ASP   A OD2 1 
ATOM   216  N N   . VAL   A 1 33  ? -1.772  -10.127 -12.335 1.00 65.23  ? 76  VAL   A N   1 
ATOM   217  C CA  . VAL   A 1 33  ? -2.041  -8.882  -11.618 1.00 63.32  ? 76  VAL   A CA  1 
ATOM   218  C C   . VAL   A 1 33  ? -2.377  -9.105  -10.127 1.00 62.15  ? 76  VAL   A C   1 
ATOM   219  O O   . VAL   A 1 33  ? -2.760  -10.204 -9.711  1.00 61.90  ? 76  VAL   A O   1 
ATOM   220  C CB  . VAL   A 1 33  ? -3.121  -8.002  -12.325 1.00 62.65  ? 76  VAL   A CB  1 
ATOM   221  C CG1 . VAL   A 1 33  ? -2.856  -7.868  -13.820 1.00 63.03  ? 76  VAL   A CG1 1 
ATOM   222  C CG2 . VAL   A 1 33  ? -4.513  -8.545  -12.081 1.00 62.52  ? 76  VAL   A CG2 1 
ATOM   223  N N   . ALA   A 1 34  ? -2.211  -8.040  -9.330  1.00 60.99  ? 77  ALA   A N   1 
ATOM   224  C CA  . ALA   A 1 34  ? -2.546  -8.015  -7.916  1.00 60.25  ? 77  ALA   A CA  1 
ATOM   225  C C   . ALA   A 1 34  ? -3.576  -6.905  -7.689  1.00 59.61  ? 77  ALA   A C   1 
ATOM   226  O O   . ALA   A 1 34  ? -3.557  -5.883  -8.382  1.00 60.33  ? 77  ALA   A O   1 
ATOM   227  C CB  . ALA   A 1 34  ? -1.312  -7.762  -7.072  1.00 60.11  ? 77  ALA   A CB  1 
ATOM   228  N N   . LEU   A 1 35  ? -4.503  -7.121  -6.758  1.00 57.84  ? 78  LEU   A N   1 
ATOM   229  C CA  . LEU   A 1 35  ? -5.519  -6.126  -6.446  1.00 56.74  ? 78  LEU   A CA  1 
ATOM   230  C C   . LEU   A 1 35  ? -5.366  -5.776  -4.964  1.00 56.49  ? 78  LEU   A C   1 
ATOM   231  O O   . LEU   A 1 35  ? -5.447  -6.665  -4.101  1.00 56.84  ? 78  LEU   A O   1 
ATOM   232  C CB  . LEU   A 1 35  ? -6.926  -6.659  -6.755  1.00 55.93  ? 78  LEU   A CB  1 
ATOM   233  C CG  . LEU   A 1 35  ? -8.080  -5.739  -6.348  1.00 56.63  ? 78  LEU   A CG  1 
ATOM   234  C CD1 . LEU   A 1 35  ? -8.176  -4.529  -7.252  1.00 56.67  ? 78  LEU   A CD1 1 
ATOM   235  C CD2 . LEU   A 1 35  ? -9.391  -6.484  -6.352  1.00 57.22  ? 78  LEU   A CD2 1 
ATOM   236  N N   . ASP   A 1 36  ? -5.069  -4.506  -4.670  1.00 55.72  ? 79  ASP   A N   1 
ATOM   237  C CA  . ASP   A 1 36  ? -4.877  -4.089  -3.291  1.00 55.77  ? 79  ASP   A CA  1 
ATOM   238  C C   . ASP   A 1 36  ? -6.204  -3.635  -2.620  1.00 56.61  ? 79  ASP   A C   1 
ATOM   239  O O   . ASP   A 1 36  ? -7.241  -3.531  -3.289  1.00 57.17  ? 79  ASP   A O   1 
ATOM   240  C CB  . ASP   A 1 36  ? -3.743  -3.051  -3.184  1.00 56.53  ? 79  ASP   A CB  1 
ATOM   241  C CG  . ASP   A 1 36  ? -4.027  -1.644  -3.662  1.00 60.02  ? 79  ASP   A CG  1 
ATOM   242  O OD1 . ASP   A 1 36  ? -5.187  -1.351  -3.998  1.00 59.37  ? 79  ASP   A OD1 1 
ATOM   243  O OD2 . ASP   A 1 36  ? -3.084  -0.829  -3.686  1.00 63.13  ? 79  ASP   A OD2 1 
ATOM   244  N N   . GLU   A 1 37  ? -6.158  -3.365  -1.307  1.00 56.76  ? 80  GLU   A N   1 
ATOM   245  C CA  . GLU   A 1 37  ? -7.284  -2.924  -0.487  1.00 57.01  ? 80  GLU   A CA  1 
ATOM   246  C C   . GLU   A 1 37  ? -7.898  -1.614  -1.008  1.00 56.44  ? 80  GLU   A C   1 
ATOM   247  O O   . GLU   A 1 37  ? -9.103  -1.424  -0.892  1.00 56.41  ? 80  GLU   A O   1 
ATOM   248  C CB  . GLU   A 1 37  ? -6.839  -2.794  0.983   1.00 59.60  ? 80  GLU   A CB  1 
ATOM   249  C CG  . GLU   A 1 37  ? -7.928  -3.093  1.999   1.00 66.11  ? 80  GLU   A CG  1 
ATOM   250  C CD  . GLU   A 1 37  ? -7.532  -2.844  3.446   1.00 74.01  ? 80  GLU   A CD  1 
ATOM   251  O OE1 . GLU   A 1 37  ? -7.470  -1.662  3.854   1.00 74.59  ? 80  GLU   A OE1 1 
ATOM   252  O OE2 . GLU   A 1 37  ? -7.279  -3.831  4.173   1.00 77.04  ? 80  GLU   A OE2 1 
ATOM   253  N N   . SER   A 1 38  ? -7.098  -0.741  -1.631  1.00 55.90  ? 81  SER   A N   1 
ATOM   254  C CA  . SER   A 1 38  ? -7.614  0.498   -2.215  1.00 56.15  ? 81  SER   A CA  1 
ATOM   255  C C   . SER   A 1 38  ? -8.250  0.314   -3.618  1.00 56.08  ? 81  SER   A C   1 
ATOM   256  O O   . SER   A 1 38  ? -8.598  1.319   -4.252  1.00 56.34  ? 81  SER   A O   1 
ATOM   257  C CB  . SER   A 1 38  ? -6.513  1.542   -2.312  1.00 58.24  ? 81  SER   A CB  1 
ATOM   258  O OG  . SER   A 1 38  ? -6.028  1.868   -1.026  1.00 63.00  ? 81  SER   A OG  1 
ATOM   259  N N   . GLY   A 1 39  ? -8.369  -0.928  -4.107  1.00 55.20  ? 82  GLY   A N   1 
ATOM   260  C CA  . GLY   A 1 39  ? -8.972  -1.180  -5.414  1.00 55.37  ? 82  GLY   A CA  1 
ATOM   261  C C   . GLY   A 1 39  ? -8.078  -0.889  -6.610  1.00 55.66  ? 82  GLY   A C   1 
ATOM   262  O O   . GLY   A 1 39  ? -8.560  -0.812  -7.741  1.00 55.00  ? 82  GLY   A O   1 
ATOM   263  N N   . ASP   A 1 40  ? -6.762  -0.742  -6.377  1.00 56.23  ? 83  ASP   A N   1 
ATOM   264  C CA  . ASP   A 1 40  ? -5.791  -0.461  -7.432  1.00 57.15  ? 83  ASP   A CA  1 
ATOM   265  C C   . ASP   A 1 40  ? -5.127  -1.745  -7.909  1.00 58.15  ? 83  ASP   A C   1 
ATOM   266  O O   . ASP   A 1 40  ? -4.533  -2.481  -7.109  1.00 58.31  ? 83  ASP   A O   1 
ATOM   267  C CB  . ASP   A 1 40  ? -4.700  0.509   -6.931  1.00 58.79  ? 83  ASP   A CB  1 
ATOM   268  C CG  . ASP   A 1 40  ? -5.229  1.854   -6.481  1.00 63.54  ? 83  ASP   A CG  1 
ATOM   269  O OD1 . ASP   A 1 40  ? -5.965  2.475   -7.244  1.00 64.18  ? 83  ASP   A OD1 1 
ATOM   270  O OD2 . ASP   A 1 40  ? -4.902  2.277   -5.355  1.00 66.87  ? 83  ASP   A OD2 1 
ATOM   271  N N   . PHE   A 1 41  ? -5.190  -1.990  -9.222  1.00 58.61  ? 84  PHE   A N   1 
ATOM   272  C CA  . PHE   A 1 41  ? -4.554  -3.134  -9.864  1.00 59.48  ? 84  PHE   A CA  1 
ATOM   273  C C   . PHE   A 1 41  ? -3.085  -2.831  -10.149 1.00 62.98  ? 84  PHE   A C   1 
ATOM   274  O O   . PHE   A 1 41  ? -2.743  -1.707  -10.517 1.00 63.77  ? 84  PHE   A O   1 
ATOM   275  C CB  . PHE   A 1 41  ? -5.258  -3.467  -11.183 1.00 57.34  ? 84  PHE   A CB  1 
ATOM   276  C CG  . PHE   A 1 41  ? -6.550  -4.231  -11.054 1.00 56.21  ? 84  PHE   A CG  1 
ATOM   277  C CD1 . PHE   A 1 41  ? -6.554  -5.563  -10.694 1.00 56.46  ? 84  PHE   A CD1 1 
ATOM   278  C CD2 . PHE   A 1 41  ? -7.760  -3.631  -11.345 1.00 55.97  ? 84  PHE   A CD2 1 
ATOM   279  C CE1 . PHE   A 1 41  ? -7.747  -6.272  -10.606 1.00 56.59  ? 84  PHE   A CE1 1 
ATOM   280  C CE2 . PHE   A 1 41  ? -8.949  -4.343  -11.252 1.00 56.00  ? 84  PHE   A CE2 1 
ATOM   281  C CZ  . PHE   A 1 41  ? -8.935  -5.657  -10.887 1.00 55.68  ? 84  PHE   A CZ  1 
ATOM   282  N N   . SER   A 1 42  ? -2.221  -3.827  -10.010 1.00 65.11  ? 85  SER   A N   1 
ATOM   283  C CA  . SER   A 1 42  ? -0.801  -3.661  -10.324 1.00 67.99  ? 85  SER   A CA  1 
ATOM   284  C C   . SER   A 1 42  ? -0.244  -4.914  -10.993 1.00 70.84  ? 85  SER   A C   1 
ATOM   285  O O   . SER   A 1 42  ? -0.805  -5.998  -10.823 1.00 70.92  ? 85  SER   A O   1 
ATOM   286  C CB  . SER   A 1 42  ? 0.002   -3.316  -9.075  1.00 69.37  ? 85  SER   A CB  1 
ATOM   287  O OG  . SER   A 1 42  ? -0.063  -4.369  -8.129  1.00 72.41  ? 85  SER   A OG  1 
ATOM   288  N N   . LEU   A 1 43  ? 0.841   -4.772  -11.769 1.00 72.84  ? 86  LEU   A N   1 
ATOM   289  C CA  . LEU   A 1 43  ? 1.434   -5.932  -12.432 1.00 75.32  ? 86  LEU   A CA  1 
ATOM   290  C C   . LEU   A 1 43  ? 2.382   -6.692  -11.532 1.00 78.13  ? 86  LEU   A C   1 
ATOM   291  O O   . LEU   A 1 43  ? 3.271   -6.105  -10.910 1.00 77.84  ? 86  LEU   A O   1 
ATOM   292  C CB  . LEU   A 1 43  ? 2.135   -5.554  -13.737 1.00 75.43  ? 86  LEU   A CB  1 
ATOM   293  C CG  . LEU   A 1 43  ? 1.230   -5.062  -14.855 1.00 77.28  ? 86  LEU   A CG  1 
ATOM   294  C CD1 . LEU   A 1 43  ? 2.031   -4.749  -16.090 1.00 77.69  ? 86  LEU   A CD1 1 
ATOM   295  C CD2 . LEU   A 1 43  ? 0.155   -6.082  -15.192 1.00 78.32  ? 86  LEU   A CD2 1 
ATOM   296  N N   . VAL   A 1 44  ? 2.190   -8.009  -11.471 1.00 80.65  ? 87  VAL   A N   1 
ATOM   297  C CA  . VAL   A 1 44  ? 3.047   -8.923  -10.722 1.00 83.46  ? 87  VAL   A CA  1 
ATOM   298  C C   . VAL   A 1 44  ? 4.013   -9.536  -11.730 1.00 86.98  ? 87  VAL   A C   1 
ATOM   299  O O   . VAL   A 1 44  ? 3.577   -10.001 -12.790 1.00 87.74  ? 87  VAL   A O   1 
ATOM   300  C CB  . VAL   A 1 44  ? 2.211   -10.036 -10.051 1.00 83.87  ? 87  VAL   A CB  1 
ATOM   301  C CG1 . VAL   A 1 44  ? 3.113   -11.062 -9.370  1.00 84.57  ? 87  VAL   A CG1 1 
ATOM   302  C CG2 . VAL   A 1 44  ? 1.204   -9.451  -9.074  1.00 84.00  ? 87  VAL   A CG2 1 
ATOM   303  N N   . GLU   A 1 45  ? 5.315   -9.512  -11.438 1.00 89.00  ? 88  GLU   A N   1 
ATOM   304  C CA  . GLU   A 1 45  ? 6.302   -10.094 -12.347 1.00 91.57  ? 88  GLU   A CA  1 
ATOM   305  C C   . GLU   A 1 45  ? 7.304   -10.963 -11.588 1.00 92.95  ? 88  GLU   A C   1 
ATOM   306  O O   . GLU   A 1 45  ? 8.114   -11.658 -12.207 1.00 94.02  ? 88  GLU   A O   1 
ATOM   307  C CB  . GLU   A 1 45  ? 7.020   -9.002  -13.157 1.00 95.22  ? 88  GLU   A CB  1 
ATOM   308  C CG  . GLU   A 1 45  ? 6.111   -8.209  -14.084 1.00 101.44 ? 88  GLU   A CG  1 
ATOM   309  C CD  . GLU   A 1 45  ? 6.030   -8.721  -15.506 1.00 109.50 ? 88  GLU   A CD  1 
ATOM   310  O OE1 . GLU   A 1 45  ? 6.633   -9.781  -15.799 1.00 110.86 ? 88  GLU   A OE1 1 
ATOM   311  O OE2 . GLU   A 1 45  ? 5.371   -8.052  -16.334 1.00 112.43 ? 88  GLU   A OE2 1 
ATOM   312  N N   . GLY   B 2 7   ? -35.615 12.050  -11.489 1.00 74.74  ? 16  GLY   B N   1 
ATOM   313  C CA  . GLY   B 2 7   ? -35.608 12.495  -12.874 1.00 75.30  ? 16  GLY   B CA  1 
ATOM   314  C C   . GLY   B 2 7   ? -35.658 11.345  -13.866 1.00 75.61  ? 16  GLY   B C   1 
ATOM   315  O O   . GLY   B 2 7   ? -36.418 10.389  -13.654 1.00 76.65  ? 16  GLY   B O   1 
ATOM   316  N N   . GLU   B 2 8   ? -34.848 11.416  -14.958 1.00 74.15  ? 17  GLU   B N   1 
ATOM   317  C CA  . GLU   B 2 8   ? -34.829 10.354  -15.969 1.00 73.03  ? 17  GLU   B CA  1 
ATOM   318  C C   . GLU   B 2 8   ? -34.380 8.986   -15.441 1.00 70.96  ? 17  GLU   B C   1 
ATOM   319  O O   . GLU   B 2 8   ? -33.225 8.806   -15.058 1.00 71.27  ? 17  GLU   B O   1 
ATOM   320  C CB  . GLU   B 2 8   ? -34.016 10.730  -17.207 1.00 75.73  ? 17  GLU   B CB  1 
ATOM   321  C CG  . GLU   B 2 8   ? -34.293 9.776   -18.355 1.00 80.83  ? 17  GLU   B CG  1 
ATOM   322  C CD  . GLU   B 2 8   ? -33.604 10.135  -19.653 1.00 88.50  ? 17  GLU   B CD  1 
ATOM   323  O OE1 . GLU   B 2 8   ? -32.568 10.836  -19.592 1.00 89.96  ? 17  GLU   B OE1 1 
ATOM   324  O OE2 . GLU   B 2 8   ? -34.111 9.745   -20.732 1.00 91.06  ? 17  GLU   B OE2 1 
ATOM   325  N N   A THR   B 2 9   ? -35.299 8.020   -15.425 0.25 70.47  ? 18  THR   B N   1 
ATOM   326  N N   B THR   B 2 9   ? -35.306 8.028   -15.424 0.25 70.35  ? 18  THR   B N   1 
ATOM   327  N N   C THR   B 2 9   ? -35.299 8.020   -15.425 0.25 70.47  ? 18  THR   B N   1 
ATOM   328  N N   D THR   B 2 9   ? -35.306 8.028   -15.424 0.25 70.35  ? 18  THR   B N   1 
ATOM   329  C CA  A THR   B 2 9   ? -34.989 6.669   -14.941 0.25 70.46  ? 18  THR   B CA  1 
ATOM   330  C CA  B THR   B 2 9   ? -35.037 6.673   -14.950 0.25 70.24  ? 18  THR   B CA  1 
ATOM   331  C CA  C THR   B 2 9   ? -34.989 6.669   -14.941 0.25 70.46  ? 18  THR   B CA  1 
ATOM   332  C CA  D THR   B 2 9   ? -35.037 6.673   -14.950 0.25 70.24  ? 18  THR   B CA  1 
ATOM   333  C C   A THR   B 2 9   ? -35.026 5.613   -16.066 0.25 69.83  ? 18  THR   B C   1 
ATOM   334  C C   B THR   B 2 9   ? -35.065 5.620   -16.067 0.25 69.74  ? 18  THR   B C   1 
ATOM   335  C C   C THR   B 2 9   ? -35.026 5.613   -16.066 0.25 69.83  ? 18  THR   B C   1 
ATOM   336  C C   D THR   B 2 9   ? -35.065 5.620   -16.067 0.25 69.74  ? 18  THR   B C   1 
ATOM   337  O O   A THR   B 2 9   ? -35.084 4.419   -15.778 0.25 70.05  ? 18  THR   B O   1 
ATOM   338  O O   B THR   B 2 9   ? -35.153 4.430   -15.770 0.25 69.97  ? 18  THR   B O   1 
ATOM   339  O O   C THR   B 2 9   ? -35.084 4.419   -15.778 0.25 70.05  ? 18  THR   B O   1 
ATOM   340  O O   D THR   B 2 9   ? -35.153 4.430   -15.770 0.25 69.97  ? 18  THR   B O   1 
ATOM   341  C CB  A THR   B 2 9   ? -35.877 6.256   -13.733 0.25 72.02  ? 18  THR   B CB  1 
ATOM   342  C CB  B THR   B 2 9   ? -36.014 6.310   -13.827 0.25 71.53  ? 18  THR   B CB  1 
ATOM   343  C CB  C THR   B 2 9   ? -35.877 6.256   -13.733 0.25 72.02  ? 18  THR   B CB  1 
ATOM   344  C CB  D THR   B 2 9   ? -36.014 6.310   -13.827 0.25 71.53  ? 18  THR   B CB  1 
ATOM   345  O OG1 A THR   B 2 9   ? -36.483 7.391   -13.101 0.25 73.25  ? 18  THR   B OG1 1 
ATOM   346  O OG1 B THR   B 2 9   ? -37.352 6.550   -14.274 0.25 72.34  ? 18  THR   B OG1 1 
ATOM   347  O OG1 C THR   B 2 9   ? -36.483 7.391   -13.101 0.25 73.25  ? 18  THR   B OG1 1 
ATOM   348  O OG1 D THR   B 2 9   ? -37.352 6.550   -14.274 0.25 72.34  ? 18  THR   B OG1 1 
ATOM   349  C CG2 A THR   B 2 9   ? -35.107 5.447   -12.694 0.25 72.46  ? 18  THR   B CG2 1 
ATOM   350  C CG2 B THR   B 2 9   ? -35.741 7.090   -12.549 0.25 72.04  ? 18  THR   B CG2 1 
ATOM   351  C CG2 C THR   B 2 9   ? -35.107 5.447   -12.694 0.25 72.46  ? 18  THR   B CG2 1 
ATOM   352  C CG2 D THR   B 2 9   ? -35.741 7.090   -12.549 0.25 72.04  ? 18  THR   B CG2 1 
ATOM   353  N N   . THR   B 2 10  ? -34.991 6.044   -17.338 1.00 68.90  ? 19  THR   B N   1 
ATOM   354  C CA  . THR   B 2 10  ? -35.019 5.133   -18.475 1.00 65.65  ? 19  THR   B CA  1 
ATOM   355  C C   . THR   B 2 10  ? -33.727 4.344   -18.543 1.00 61.76  ? 19  THR   B C   1 
ATOM   356  O O   . THR   B 2 10  ? -32.651 4.919   -18.387 1.00 61.19  ? 19  THR   B O   1 
ATOM   357  C CB  . THR   B 2 10  ? -35.185 5.955   -19.789 1.00 66.97  ? 19  THR   B CB  1 
ATOM   358  O OG1 . THR   B 2 10  ? -36.290 6.855   -19.678 1.00 68.18  ? 19  THR   B OG1 1 
ATOM   359  C CG2 . THR   B 2 10  ? -35.356 5.079   -21.020 1.00 67.23  ? 19  THR   B CG2 1 
ATOM   360  N N   . ASP   B 2 11  ? -33.821 3.031   -18.804 1.00 59.18  ? 20  ASP   B N   1 
ATOM   361  C CA  . ASP   B 2 11  ? -32.651 2.175   -19.004 1.00 58.24  ? 20  ASP   B CA  1 
ATOM   362  C C   . ASP   B 2 11  ? -31.739 2.762   -20.115 1.00 57.11  ? 20  ASP   B C   1 
ATOM   363  O O   . ASP   B 2 11  ? -32.226 3.426   -21.034 1.00 56.99  ? 20  ASP   B O   1 
ATOM   364  C CB  . ASP   B 2 11  ? -33.082 0.757   -19.426 1.00 59.78  ? 20  ASP   B CB  1 
ATOM   365  C CG  . ASP   B 2 11  ? -33.530 -0.183  -18.322 1.00 64.94  ? 20  ASP   B CG  1 
ATOM   366  O OD1 . ASP   B 2 11  ? -33.849 0.306   -17.210 1.00 64.36  ? 20  ASP   B OD1 1 
ATOM   367  O OD2 . ASP   B 2 11  ? -33.567 -1.418  -18.573 1.00 68.60  ? 20  ASP   B OD2 1 
ATOM   368  N N   . GLY   B 2 12  ? -30.442 2.590   -19.964 1.00 55.64  ? 21  GLY   B N   1 
ATOM   369  C CA  . GLY   B 2 12  ? -29.482 3.108   -20.923 1.00 54.17  ? 21  GLY   B CA  1 
ATOM   370  C C   . GLY   B 2 12  ? -28.151 3.454   -20.298 1.00 52.64  ? 21  GLY   B C   1 
ATOM   371  O O   . GLY   B 2 12  ? -27.910 3.185   -19.118 1.00 52.91  ? 21  GLY   B O   1 
ATOM   372  N N   . VAL   B 2 13  ? -27.273 4.042   -21.089 1.00 50.69  ? 22  VAL   B N   1 
ATOM   373  C CA  . VAL   B 2 13  ? -25.956 4.475   -20.650 1.00 49.09  ? 22  VAL   B CA  1 
ATOM   374  C C   . VAL   B 2 13  ? -25.983 6.005   -20.478 1.00 49.19  ? 22  VAL   B C   1 
ATOM   375  O O   . VAL   B 2 13  ? -26.714 6.693   -21.186 1.00 49.81  ? 22  VAL   B O   1 
ATOM   376  C CB  . VAL   B 2 13  ? -24.858 3.969   -21.600 1.00 48.06  ? 22  VAL   B CB  1 
ATOM   377  C CG1 . VAL   B 2 13  ? -25.064 4.499   -23.040 1.00 48.11  ? 22  VAL   B CG1 1 
ATOM   378  C CG2 . VAL   B 2 13  ? -23.484 4.321   -21.075 1.00 47.09  ? 22  VAL   B CG2 1 
ATOM   379  N N   . TYR   B 2 14  ? -25.310 6.522   -19.450 1.00 49.13  ? 23  TYR   B N   1 
ATOM   380  C CA  . TYR   B 2 14  ? -25.380 7.941   -19.106 1.00 49.05  ? 23  TYR   B CA  1 
ATOM   381  C C   . TYR   B 2 14  ? -24.013 8.508   -18.815 1.00 49.70  ? 23  TYR   B C   1 
ATOM   382  O O   . TYR   B 2 14  ? -23.193 7.845   -18.193 1.00 49.57  ? 23  TYR   B O   1 
ATOM   383  C CB  . TYR   B 2 14  ? -26.191 8.098   -17.797 1.00 48.30  ? 23  TYR   B CB  1 
ATOM   384  C CG  . TYR   B 2 14  ? -27.682 7.905   -17.948 1.00 47.81  ? 23  TYR   B CG  1 
ATOM   385  C CD1 . TYR   B 2 14  ? -28.219 6.652   -18.201 1.00 48.11  ? 23  TYR   B CD1 1 
ATOM   386  C CD2 . TYR   B 2 14  ? -28.560 8.957   -17.748 1.00 48.00  ? 23  TYR   B CD2 1 
ATOM   387  C CE1 . TYR   B 2 14  ? -29.580 6.475   -18.378 1.00 49.02  ? 23  TYR   B CE1 1 
ATOM   388  C CE2 . TYR   B 2 14  ? -29.927 8.786   -17.892 1.00 49.12  ? 23  TYR   B CE2 1 
ATOM   389  C CZ  . TYR   B 2 14  ? -30.434 7.543   -18.208 1.00 50.47  ? 23  TYR   B CZ  1 
ATOM   390  O OH  . TYR   B 2 14  ? -31.786 7.355   -18.319 1.00 53.39  ? 23  TYR   B OH  1 
ATOM   391  N N   . ARG   B 2 15  ? -23.835 9.789   -19.104 1.00 49.78  ? 24  ARG   B N   1 
ATOM   392  C CA  . ARG   B 2 15  ? -22.615 10.505  -18.759 1.00 49.86  ? 24  ARG   B CA  1 
ATOM   393  C C   . ARG   B 2 15  ? -22.753 11.027  -17.323 1.00 49.53  ? 24  ARG   B C   1 
ATOM   394  O O   . ARG   B 2 15  ? -23.825 11.484  -16.934 1.00 49.72  ? 24  ARG   B O   1 
ATOM   395  C CB  . ARG   B 2 15  ? -22.404 11.708  -19.708 1.00 50.70  ? 24  ARG   B CB  1 
ATOM   396  C CG  . ARG   B 2 15  ? -22.395 11.368  -21.195 1.00 52.20  ? 24  ARG   B CG  1 
ATOM   397  C CD  . ARG   B 2 15  ? -22.379 12.618  -22.083 1.00 53.27  ? 24  ARG   B CD  1 
ATOM   398  N NE  . ARG   B 2 15  ? -22.509 12.264  -23.507 1.00 54.01  ? 24  ARG   B NE  1 
ATOM   399  C CZ  . ARG   B 2 15  ? -21.490 11.919  -24.291 1.00 54.27  ? 24  ARG   B CZ  1 
ATOM   400  N NH1 . ARG   B 2 15  ? -20.249 11.944  -23.825 1.00 52.35  ? 24  ARG   B NH1 1 
ATOM   401  N NH2 . ARG   B 2 15  ? -21.705 11.562  -25.552 1.00 54.71  ? 24  ARG   B NH2 1 
ATOM   402  N N   . VAL   B 2 16  ? -21.659 11.002  -16.557 1.00 49.23  ? 25  VAL   B N   1 
ATOM   403  C CA  . VAL   B 2 16  ? -21.570 11.545  -15.209 1.00 49.80  ? 25  VAL   B CA  1 
ATOM   404  C C   . VAL   B 2 16  ? -20.785 12.837  -15.362 1.00 51.20  ? 25  VAL   B C   1 
ATOM   405  O O   . VAL   B 2 16  ? -19.622 12.807  -15.737 1.00 50.86  ? 25  VAL   B O   1 
ATOM   406  C CB  . VAL   B 2 16  ? -20.874 10.597  -14.183 1.00 50.30  ? 25  VAL   B CB  1 
ATOM   407  C CG1 . VAL   B 2 16  ? -20.875 11.221  -12.788 1.00 50.02  ? 25  VAL   B CG1 1 
ATOM   408  C CG2 . VAL   B 2 16  ? -21.510 9.199   -14.166 1.00 50.39  ? 25  VAL   B CG2 1 
ATOM   409  N N   . MET   B 2 17  ? -21.430 13.975  -15.124 1.00 52.76  ? 26  MET   B N   1 
ATOM   410  C CA  . MET   B 2 17  ? -20.807 15.277  -15.303 1.00 54.35  ? 26  MET   B CA  1 
ATOM   411  C C   . MET   B 2 17  ? -20.627 16.024  -13.980 1.00 56.82  ? 26  MET   B C   1 
ATOM   412  O O   . MET   B 2 17  ? -21.344 15.762  -13.022 1.00 56.47  ? 26  MET   B O   1 
ATOM   413  C CB  . MET   B 2 17  ? -21.711 16.143  -16.204 1.00 54.32  ? 26  MET   B CB  1 
ATOM   414  C CG  . MET   B 2 17  ? -22.156 15.477  -17.502 1.00 53.80  ? 26  MET   B CG  1 
ATOM   415  S SD  . MET   B 2 17  ? -20.800 15.207  -18.671 1.00 54.88  ? 26  MET   B SD  1 
ATOM   416  C CE  . MET   B 2 17  ? -20.165 16.840  -18.849 1.00 51.93  ? 26  MET   B CE  1 
ATOM   417  N N   . THR   B 2 18  ? -19.734 17.025  -13.964 1.00 58.83  ? 27  THR   B N   1 
ATOM   418  C CA  . THR   B 2 18  ? -19.570 17.918  -12.827 1.00 61.20  ? 27  THR   B CA  1 
ATOM   419  C C   . THR   B 2 18  ? -19.360 19.366  -13.308 1.00 63.32  ? 27  THR   B C   1 
ATOM   420  O O   . THR   B 2 18  ? -18.685 19.593  -14.317 1.00 62.96  ? 27  THR   B O   1 
ATOM   421  C CB  . THR   B 2 18  ? -18.464 17.443  -11.858 1.00 62.84  ? 27  THR   B CB  1 
ATOM   422  O OG1 . THR   B 2 18  ? -18.319 18.425  -10.819 1.00 63.80  ? 27  THR   B OG1 1 
ATOM   423  C CG2 . THR   B 2 18  ? -17.126 17.217  -12.556 1.00 62.97  ? 27  THR   B CG2 1 
ATOM   424  N N   . ARG   B 2 19  ? -19.936 20.342  -12.583 1.00 65.27  ? 28  ARG   B N   1 
ATOM   425  C CA  . ARG   B 2 19  ? -19.742 21.772  -12.875 1.00 67.81  ? 28  ARG   B CA  1 
ATOM   426  C C   . ARG   B 2 19  ? -18.720 22.437  -11.901 1.00 69.47  ? 28  ARG   B C   1 
ATOM   427  O O   . ARG   B 2 19  ? -18.531 23.651  -11.951 1.00 69.40  ? 28  ARG   B O   1 
ATOM   428  C CB  . ARG   B 2 19  ? -21.081 22.531  -12.814 1.00 70.16  ? 28  ARG   B CB  1 
ATOM   429  C CG  . ARG   B 2 19  ? -22.150 21.989  -13.747 1.00 74.72  ? 28  ARG   B CG  1 
ATOM   430  C CD  . ARG   B 2 19  ? -22.429 22.946  -14.886 1.00 79.73  ? 28  ARG   B CD  1 
ATOM   431  N NE  . ARG   B 2 19  ? -23.454 22.449  -15.807 1.00 84.64  ? 28  ARG   B NE  1 
ATOM   432  C CZ  . ARG   B 2 19  ? -24.766 22.556  -15.605 1.00 88.14  ? 28  ARG   B CZ  1 
ATOM   433  N NH1 . ARG   B 2 19  ? -25.232 23.113  -14.490 1.00 87.93  ? 28  ARG   B NH1 1 
ATOM   434  N NH2 . ARG   B 2 19  ? -25.623 22.081  -16.502 1.00 88.48  ? 28  ARG   B NH2 1 
ATOM   435  N N   . ARG   B 2 20  ? -18.061 21.642  -11.041 1.00 71.17  ? 29  ARG   B N   1 
ATOM   436  C CA  . ARG   B 2 20  ? -17.116 22.088  -10.013 1.00 73.22  ? 29  ARG   B CA  1 
ATOM   437  C C   . ARG   B 2 20  ? -15.803 22.580  -10.611 1.00 74.01  ? 29  ARG   B C   1 
ATOM   438  O O   . ARG   B 2 20  ? -15.234 23.570  -10.137 1.00 74.75  ? 29  ARG   B O   1 
ATOM   439  C CB  . ARG   B 2 20  ? -16.875 20.945  -9.012  1.00 75.95  ? 29  ARG   B CB  1 
ATOM   440  C CG  . ARG   B 2 20  ? -16.069 21.331  -7.779  1.00 82.05  ? 29  ARG   B CG  1 
ATOM   441  C CD  . ARG   B 2 20  ? -15.799 20.131  -6.885  1.00 87.71  ? 29  ARG   B CD  1 
ATOM   442  N NE  . ARG   B 2 20  ? -15.206 19.000  -7.614  1.00 92.62  ? 29  ARG   B NE  1 
ATOM   443  C CZ  . ARG   B 2 20  ? -13.899 18.785  -7.734  1.00 95.79  ? 29  ARG   B CZ  1 
ATOM   444  N NH1 . ARG   B 2 20  ? -13.027 19.622  -7.185  1.00 96.18  ? 29  ARG   B NH1 1 
ATOM   445  N NH2 . ARG   B 2 20  ? -13.452 17.734  -8.413  1.00 95.49  ? 29  ARG   B NH2 1 
ATOM   446  N N   . LEU   B 2 21  ? -15.339 21.919  -11.675 1.00 73.37  ? 30  LEU   B N   1 
ATOM   447  C CA  . LEU   B 2 21  ? -14.101 22.310  -12.348 1.00 73.03  ? 30  LEU   B CA  1 
ATOM   448  C C   . LEU   B 2 21  ? -14.419 23.370  -13.460 1.00 71.86  ? 30  LEU   B C   1 
ATOM   449  O O   . LEU   B 2 21  ? -15.499 23.982  -13.435 1.00 71.56  ? 30  LEU   B O   1 
ATOM   450  C CB  . LEU   B 2 21  ? -13.452 21.025  -12.930 1.00 73.76  ? 30  LEU   B CB  1 
ATOM   451  C CG  . LEU   B 2 21  ? -12.462 20.184  -12.086 1.00 75.89  ? 30  LEU   B CG  1 
ATOM   452  C CD1 . LEU   B 2 21  ? -12.569 20.427  -10.577 1.00 76.56  ? 30  LEU   B CD1 1 
ATOM   453  C CD2 . LEU   B 2 21  ? -12.619 18.709  -12.389 1.00 76.79  ? 30  LEU   B CD2 1 
ATOM   454  N N   . LEU   B 2 22  ? -13.487 23.608  -14.410 1.00 70.78  ? 31  LEU   B N   1 
ATOM   455  C CA  . LEU   B 2 22  ? -13.738 24.554  -15.494 1.00 70.39  ? 31  LEU   B CA  1 
ATOM   456  C C   . LEU   B 2 22  ? -14.769 23.942  -16.452 1.00 70.54  ? 31  LEU   B C   1 
ATOM   457  O O   . LEU   B 2 22  ? -14.669 22.750  -16.761 1.00 71.40  ? 31  LEU   B O   1 
ATOM   458  C CB  . LEU   B 2 22  ? -12.443 24.862  -16.242 1.00 70.05  ? 31  LEU   B CB  1 
ATOM   459  C CG  . LEU   B 2 22  ? -12.586 25.877  -17.346 1.00 70.31  ? 31  LEU   B CG  1 
ATOM   460  C CD1 . LEU   B 2 22  ? -12.246 27.260  -16.853 1.00 69.92  ? 31  LEU   B CD1 1 
ATOM   461  C CD2 . LEU   B 2 22  ? -11.774 25.468  -18.563 1.00 71.06  ? 31  LEU   B CD2 1 
ATOM   462  N N   . GLY   B 2 23  ? -15.771 24.734  -16.856 1.00 69.32  ? 32  GLY   B N   1 
ATOM   463  C CA  . GLY   B 2 23  ? -16.855 24.287  -17.728 1.00 68.36  ? 32  GLY   B CA  1 
ATOM   464  C C   . GLY   B 2 23  ? -17.640 23.108  -17.179 1.00 66.99  ? 32  GLY   B C   1 
ATOM   465  O O   . GLY   B 2 23  ? -17.755 22.944  -15.963 1.00 66.89  ? 32  GLY   B O   1 
ATOM   466  N N   . SER   B 2 24  ? -18.178 22.265  -18.067 1.00 65.89  ? 33  SER   B N   1 
ATOM   467  C CA  . SER   B 2 24  ? -18.883 21.052  -17.642 1.00 65.26  ? 33  SER   B CA  1 
ATOM   468  C C   . SER   B 2 24  ? -17.952 19.928  -18.019 1.00 63.83  ? 33  SER   B C   1 
ATOM   469  O O   . SER   B 2 24  ? -17.706 19.718  -19.203 1.00 63.66  ? 33  SER   B O   1 
ATOM   470  C CB  . SER   B 2 24  ? -20.217 20.902  -18.366 1.00 67.20  ? 33  SER   B CB  1 
ATOM   471  O OG  . SER   B 2 24  ? -21.054 22.033  -18.162 1.00 69.58  ? 33  SER   B OG  1 
ATOM   472  N N   . THR   B 2 25  ? -17.364 19.263  -17.014 1.00 62.54  ? 34  THR   B N   1 
ATOM   473  C CA  . THR   B 2 25  ? -16.385 18.208  -17.233 1.00 61.51  ? 34  THR   B CA  1 
ATOM   474  C C   . THR   B 2 25  ? -16.989 16.818  -17.045 1.00 60.01  ? 34  THR   B C   1 
ATOM   475  O O   . THR   B 2 25  ? -17.675 16.588  -16.049 1.00 60.43  ? 34  THR   B O   1 
ATOM   476  C CB  . THR   B 2 25  ? -15.149 18.447  -16.331 1.00 62.56  ? 34  THR   B CB  1 
ATOM   477  O OG1 . THR   B 2 25  ? -14.499 19.676  -16.705 1.00 63.59  ? 34  THR   B OG1 1 
ATOM   478  C CG2 . THR   B 2 25  ? -14.156 17.299  -16.380 1.00 62.48  ? 34  THR   B CG2 1 
ATOM   479  N N   . GLN   B 2 26  ? -16.749 15.895  -18.005 1.00 57.93  ? 35  GLN   B N   1 
ATOM   480  C CA  . GLN   B 2 26  ? -17.244 14.531  -17.860 1.00 56.77  ? 35  GLN   B CA  1 
ATOM   481  C C   . GLN   B 2 26  ? -16.265 13.735  -17.000 1.00 56.66  ? 35  GLN   B C   1 
ATOM   482  O O   . GLN   B 2 26  ? -15.099 13.590  -17.385 1.00 57.34  ? 35  GLN   B O   1 
ATOM   483  C CB  . GLN   B 2 26  ? -17.464 13.836  -19.211 1.00 55.63  ? 35  GLN   B CB  1 
ATOM   484  C CG  . GLN   B 2 26  ? -18.008 12.420  -19.048 1.00 55.33  ? 35  GLN   B CG  1 
ATOM   485  C CD  . GLN   B 2 26  ? -18.308 11.758  -20.370 1.00 58.09  ? 35  GLN   B CD  1 
ATOM   486  O OE1 . GLN   B 2 26  ? -19.017 12.307  -21.212 1.00 59.44  ? 35  GLN   B OE1 1 
ATOM   487  N NE2 . GLN   B 2 26  ? -17.787 10.561  -20.586 1.00 57.76  ? 35  GLN   B NE2 1 
ATOM   488  N N   . VAL   B 2 27  ? -16.724 13.239  -15.838 1.00 55.39  ? 36  VAL   B N   1 
ATOM   489  C CA  . VAL   B 2 27  ? -15.856 12.469  -14.949 1.00 54.92  ? 36  VAL   B CA  1 
ATOM   490  C C   . VAL   B 2 27  ? -16.011 10.931  -15.111 1.00 53.75  ? 36  VAL   B C   1 
ATOM   491  O O   . VAL   B 2 27  ? -15.145 10.172  -14.674 1.00 54.21  ? 36  VAL   B O   1 
ATOM   492  C CB  . VAL   B 2 27  ? -15.983 12.903  -13.465 1.00 55.65  ? 36  VAL   B CB  1 
ATOM   493  C CG1 . VAL   B 2 27  ? -15.268 14.222  -13.236 1.00 56.72  ? 36  VAL   B CG1 1 
ATOM   494  C CG2 . VAL   B 2 27  ? -17.435 12.985  -13.010 1.00 55.45  ? 36  VAL   B CG2 1 
ATOM   495  N N   . GLY   B 2 28  ? -17.102 10.496  -15.718 1.00 51.91  ? 37  GLY   B N   1 
ATOM   496  C CA  . GLY   B 2 28  ? -17.362 9.082   -15.897 1.00 50.40  ? 37  GLY   B CA  1 
ATOM   497  C C   . GLY   B 2 28  ? -18.662 8.795   -16.603 1.00 48.83  ? 37  GLY   B C   1 
ATOM   498  O O   . GLY   B 2 28  ? -19.299 9.693   -17.152 1.00 48.02  ? 37  GLY   B O   1 
ATOM   499  N N   . VAL   B 2 29  ? -19.047 7.527   -16.599 1.00 48.38  ? 38  VAL   B N   1 
ATOM   500  C CA  . VAL   B 2 29  ? -20.209 6.973   -17.296 1.00 48.66  ? 38  VAL   B CA  1 
ATOM   501  C C   . VAL   B 2 29  ? -20.892 5.933   -16.357 1.00 48.50  ? 38  VAL   B C   1 
ATOM   502  O O   . VAL   B 2 29  ? -20.248 5.382   -15.473 1.00 49.50  ? 38  VAL   B O   1 
ATOM   503  C CB  . VAL   B 2 29  ? -19.731 6.287   -18.639 1.00 49.14  ? 38  VAL   B CB  1 
ATOM   504  C CG1 . VAL   B 2 29  ? -20.904 5.845   -19.501 1.00 49.80  ? 38  VAL   B CG1 1 
ATOM   505  C CG2 . VAL   B 2 29  ? -18.809 7.195   -19.467 1.00 49.47  ? 38  VAL   B CG2 1 
ATOM   506  N N   . GLY   B 2 30  ? -22.166 5.650   -16.586 1.00 47.43  ? 39  GLY   B N   1 
ATOM   507  C CA  . GLY   B 2 30  ? -22.889 4.655   -15.812 1.00 46.76  ? 39  GLY   B CA  1 
ATOM   508  C C   . GLY   B 2 30  ? -24.035 4.003   -16.555 1.00 46.31  ? 39  GLY   B C   1 
ATOM   509  O O   . GLY   B 2 30  ? -24.395 4.434   -17.653 1.00 46.86  ? 39  GLY   B O   1 
ATOM   510  N N   . VAL   B 2 31  ? -24.620 2.959   -15.955 1.00 45.30  ? 40  VAL   B N   1 
ATOM   511  C CA  . VAL   B 2 31  ? -25.716 2.182   -16.538 1.00 45.20  ? 40  VAL   B CA  1 
ATOM   512  C C   . VAL   B 2 31  ? -26.988 2.300   -15.711 1.00 45.43  ? 40  VAL   B C   1 
ATOM   513  O O   . VAL   B 2 31  ? -26.958 2.032   -14.505 1.00 45.19  ? 40  VAL   B O   1 
ATOM   514  C CB  . VAL   B 2 31  ? -25.301 0.679   -16.668 1.00 45.27  ? 40  VAL   B CB  1 
ATOM   515  C CG1 . VAL   B 2 31  ? -26.478 -0.197  -17.090 1.00 45.37  ? 40  VAL   B CG1 1 
ATOM   516  C CG2 . VAL   B 2 31  ? -24.125 0.506   -17.622 1.00 45.02  ? 40  VAL   B CG2 1 
ATOM   517  N N   . MET   B 2 32  ? -28.109 2.660   -16.337 1.00 45.78  ? 41  MET   B N   1 
ATOM   518  C CA  . MET   B 2 32  ? -29.382 2.714   -15.620 1.00 46.80  ? 41  MET   B CA  1 
ATOM   519  C C   . MET   B 2 32  ? -30.121 1.408   -15.945 1.00 48.82  ? 41  MET   B C   1 
ATOM   520  O O   . MET   B 2 32  ? -30.301 1.101   -17.122 1.00 49.41  ? 41  MET   B O   1 
ATOM   521  C CB  . MET   B 2 32  ? -30.200 3.944   -16.031 1.00 46.75  ? 41  MET   B CB  1 
ATOM   522  C CG  . MET   B 2 32  ? -31.397 4.198   -15.140 1.00 49.74  ? 41  MET   B CG  1 
ATOM   523  S SD  . MET   B 2 32  ? -30.996 4.767   -13.454 1.00 57.98  ? 41  MET   B SD  1 
ATOM   524  C CE  . MET   B 2 32  ? -30.766 6.498   -13.760 1.00 59.94  ? 41  MET   B CE  1 
ATOM   525  N N   . GLN   B 2 33  ? -30.457 0.596   -14.933 1.00 49.32  ? 42  GLN   B N   1 
ATOM   526  C CA  . GLN   B 2 33  ? -31.164 -0.652  -15.171 1.00 50.47  ? 42  GLN   B CA  1 
ATOM   527  C C   . GLN   B 2 33  ? -32.059 -0.990  -14.020 1.00 52.26  ? 42  GLN   B C   1 
ATOM   528  O O   . GLN   B 2 33  ? -31.588 -1.063  -12.879 1.00 53.08  ? 42  GLN   B O   1 
ATOM   529  C CB  . GLN   B 2 33  ? -30.217 -1.806  -15.458 1.00 51.65  ? 42  GLN   B CB  1 
ATOM   530  C CG  . GLN   B 2 33  ? -30.988 -3.044  -15.895 1.00 55.87  ? 42  GLN   B CG  1 
ATOM   531  C CD  . GLN   B 2 33  ? -30.102 -4.127  -16.467 1.00 61.41  ? 42  GLN   B CD  1 
ATOM   532  O OE1 . GLN   B 2 33  ? -30.154 -5.293  -16.041 1.00 62.66  ? 42  GLN   B OE1 1 
ATOM   533  N NE2 . GLN   B 2 33  ? -29.271 -3.765  -17.450 1.00 61.86  ? 42  GLN   B NE2 1 
ATOM   534  N N   . GLU   B 2 34  ? -33.352 -1.195  -14.305 1.00 52.71  ? 43  GLU   B N   1 
ATOM   535  C CA  . GLU   B 2 34  ? -34.354 -1.522  -13.298 1.00 53.57  ? 43  GLU   B CA  1 
ATOM   536  C C   . GLU   B 2 34  ? -34.417 -0.486  -12.167 1.00 53.66  ? 43  GLU   B C   1 
ATOM   537  O O   . GLU   B 2 34  ? -34.536 -0.853  -11.006 1.00 54.84  ? 43  GLU   B O   1 
ATOM   538  C CB  . GLU   B 2 34  ? -34.156 -2.946  -12.744 1.00 56.34  ? 43  GLU   B CB  1 
ATOM   539  C CG  . GLU   B 2 34  ? -34.142 -4.025  -13.815 1.00 60.89  ? 43  GLU   B CG  1 
ATOM   540  C CD  . GLU   B 2 34  ? -33.408 -5.300  -13.427 1.00 69.30  ? 43  GLU   B CD  1 
ATOM   541  O OE1 . GLU   B 2 34  ? -33.841 -5.978  -12.467 1.00 69.48  ? 43  GLU   B OE1 1 
ATOM   542  O OE2 . GLU   B 2 34  ? -32.399 -5.627  -14.093 1.00 73.86  ? 43  GLU   B OE2 1 
ATOM   543  N N   . GLY   B 2 35  ? -34.330 0.794   -12.524 1.00 52.57  ? 44  GLY   B N   1 
ATOM   544  C CA  . GLY   B 2 35  ? -34.400 1.915   -11.590 1.00 51.71  ? 44  GLY   B CA  1 
ATOM   545  C C   . GLY   B 2 35  ? -33.156 2.139   -10.751 1.00 50.64  ? 44  GLY   B C   1 
ATOM   546  O O   . GLY   B 2 35  ? -33.197 2.918   -9.790  1.00 51.41  ? 44  GLY   B O   1 
ATOM   547  N N   . VAL   B 2 36  ? -32.040 1.450   -11.096 1.00 48.61  ? 45  VAL   B N   1 
ATOM   548  C CA  . VAL   B 2 36  ? -30.775 1.499   -10.360 1.00 47.41  ? 45  VAL   B CA  1 
ATOM   549  C C   . VAL   B 2 36  ? -29.641 2.043   -11.240 1.00 46.19  ? 45  VAL   B C   1 
ATOM   550  O O   . VAL   B 2 36  ? -29.474 1.594   -12.380 1.00 46.34  ? 45  VAL   B O   1 
ATOM   551  C CB  . VAL   B 2 36  ? -30.438 0.112   -9.688  1.00 47.72  ? 45  VAL   B CB  1 
ATOM   552  C CG1 . VAL   B 2 36  ? -29.033 0.083   -9.081  1.00 48.34  ? 45  VAL   B CG1 1 
ATOM   553  C CG2 . VAL   B 2 36  ? -31.474 -0.250  -8.623  1.00 47.74  ? 45  VAL   B CG2 1 
ATOM   554  N N   . PHE   B 2 37  ? -28.902 3.052   -10.748 1.00 45.00  ? 46  PHE   B N   1 
ATOM   555  C CA  . PHE   B 2 37  ? -27.796 3.620   -11.518 1.00 45.09  ? 46  PHE   B CA  1 
ATOM   556  C C   . PHE   B 2 37  ? -26.509 2.935   -11.069 1.00 44.50  ? 46  PHE   B C   1 
ATOM   557  O O   . PHE   B 2 37  ? -26.243 2.878   -9.891  1.00 44.18  ? 46  PHE   B O   1 
ATOM   558  C CB  . PHE   B 2 37  ? -27.710 5.156   -11.340 1.00 44.86  ? 46  PHE   B CB  1 
ATOM   559  C CG  . PHE   B 2 37  ? -26.765 5.771   -12.343 1.00 44.71  ? 46  PHE   B CG  1 
ATOM   560  C CD1 . PHE   B 2 37  ? -27.041 5.716   -13.704 1.00 44.94  ? 46  PHE   B CD1 1 
ATOM   561  C CD2 . PHE   B 2 37  ? -25.561 6.324   -11.936 1.00 45.03  ? 46  PHE   B CD2 1 
ATOM   562  C CE1 . PHE   B 2 37  ? -26.168 6.261   -14.631 1.00 45.44  ? 46  PHE   B CE1 1 
ATOM   563  C CE2 . PHE   B 2 37  ? -24.675 6.840   -12.865 1.00 45.80  ? 46  PHE   B CE2 1 
ATOM   564  C CZ  . PHE   B 2 37  ? -24.991 6.818   -14.209 1.00 45.66  ? 46  PHE   B CZ  1 
ATOM   565  N N   . HIS   B 2 38  ? -25.751 2.364   -11.991 1.00 43.86  ? 47  HIS   B N   1 
ATOM   566  C CA  . HIS   B 2 38  ? -24.551 1.591   -11.682 1.00 43.60  ? 47  HIS   B CA  1 
ATOM   567  C C   . HIS   B 2 38  ? -23.351 2.313   -12.236 1.00 44.13  ? 47  HIS   B C   1 
ATOM   568  O O   . HIS   B 2 38  ? -23.352 2.644   -13.404 1.00 43.70  ? 47  HIS   B O   1 
ATOM   569  C CB  . HIS   B 2 38  ? -24.608 0.201   -12.361 1.00 43.37  ? 47  HIS   B CB  1 
ATOM   570  C CG  . HIS   B 2 38  ? -25.832 -0.591  -12.048 1.00 44.67  ? 47  HIS   B CG  1 
ATOM   571  N ND1 . HIS   B 2 38  ? -27.080 -0.213  -12.518 1.00 46.31  ? 47  HIS   B ND1 1 
ATOM   572  C CD2 . HIS   B 2 38  ? -25.959 -1.740  -11.346 1.00 45.69  ? 47  HIS   B CD2 1 
ATOM   573  C CE1 . HIS   B 2 38  ? -27.928 -1.117  -12.052 1.00 46.42  ? 47  HIS   B CE1 1 
ATOM   574  N NE2 . HIS   B 2 38  ? -27.300 -2.054  -11.342 1.00 46.67  ? 47  HIS   B NE2 1 
ATOM   575  N N   . THR   B 2 39  ? -22.310 2.542   -11.420 1.00 44.44  ? 48  THR   B N   1 
ATOM   576  C CA  . THR   B 2 39  ? -21.102 3.199   -11.923 1.00 44.63  ? 48  THR   B CA  1 
ATOM   577  C C   . THR   B 2 39  ? -19.879 2.719   -11.118 1.00 43.97  ? 48  THR   B C   1 
ATOM   578  O O   . THR   B 2 39  ? -20.007 1.832   -10.267 1.00 42.80  ? 48  THR   B O   1 
ATOM   579  C CB  . THR   B 2 39  ? -21.300 4.740   -12.008 1.00 46.08  ? 48  THR   B CB  1 
ATOM   580  O OG1 . THR   B 2 39  ? -20.172 5.303   -12.672 1.00 47.11  ? 48  THR   B OG1 1 
ATOM   581  C CG2 . THR   B 2 39  ? -21.528 5.385   -10.638 1.00 46.50  ? 48  THR   B CG2 1 
ATOM   582  N N   . MET   B 2 40  ? -18.679 3.228   -11.453 1.00 44.25  ? 49  MET   B N   1 
ATOM   583  C CA  . MET   B 2 40  ? -17.480 2.878   -10.701 1.00 44.65  ? 49  MET   B CA  1 
ATOM   584  C C   . MET   B 2 40  ? -17.357 3.847   -9.524  1.00 46.04  ? 49  MET   B C   1 
ATOM   585  O O   . MET   B 2 40  ? -17.778 5.013   -9.639  1.00 46.97  ? 49  MET   B O   1 
ATOM   586  C CB  . MET   B 2 40  ? -16.257 2.886   -11.597 1.00 44.59  ? 49  MET   B CB  1 
ATOM   587  C CG  . MET   B 2 40  ? -16.475 2.055   -12.859 1.00 46.77  ? 49  MET   B CG  1 
ATOM   588  S SD  . MET   B 2 40  ? -15.001 1.168   -13.353 1.00 55.54  ? 49  MET   B SD  1 
ATOM   589  C CE  . MET   B 2 40  ? -15.044 -0.196  -12.254 1.00 49.19  ? 49  MET   B CE  1 
ATOM   590  N N   A TRP   B 2 41  ? -16.796 3.378   -8.403  0.25 46.01  ? 50  TRP   B N   1 
ATOM   591  N N   B TRP   B 2 41  ? -16.798 3.377   -8.400  0.25 45.68  ? 50  TRP   B N   1 
ATOM   592  N N   C TRP   B 2 41  ? -16.796 3.378   -8.403  0.25 46.01  ? 50  TRP   B N   1 
ATOM   593  N N   D TRP   B 2 41  ? -16.803 3.378   -8.395  0.25 45.78  ? 50  TRP   B N   1 
ATOM   594  C CA  A TRP   B 2 41  ? -16.639 4.181   -7.195  0.25 46.73  ? 50  TRP   B CA  1 
ATOM   595  C CA  B TRP   B 2 41  ? -16.635 4.174   -7.186  0.25 46.07  ? 50  TRP   B CA  1 
ATOM   596  C CA  C TRP   B 2 41  ? -16.639 4.181   -7.195  0.25 46.73  ? 50  TRP   B CA  1 
ATOM   597  C CA  D TRP   B 2 41  ? -16.646 4.186   -7.185  0.25 46.27  ? 50  TRP   B CA  1 
ATOM   598  C C   A TRP   B 2 41  ? -15.730 5.377   -7.402  0.25 46.94  ? 50  TRP   B C   1 
ATOM   599  C C   B TRP   B 2 41  ? -15.720 5.373   -7.388  0.25 46.63  ? 50  TRP   B C   1 
ATOM   600  C C   C TRP   B 2 41  ? -15.730 5.377   -7.402  0.25 46.94  ? 50  TRP   B C   1 
ATOM   601  C C   D TRP   B 2 41  ? -15.724 5.378   -7.390  0.25 46.72  ? 50  TRP   B C   1 
ATOM   602  O O   A TRP   B 2 41  ? -16.030 6.446   -6.890  0.25 47.08  ? 50  TRP   B O   1 
ATOM   603  O O   B TRP   B 2 41  ? -16.010 6.438   -6.860  0.25 46.77  ? 50  TRP   B O   1 
ATOM   604  O O   C TRP   B 2 41  ? -16.030 6.446   -6.890  0.25 47.08  ? 50  TRP   B O   1 
ATOM   605  O O   D TRP   B 2 41  ? -16.020 6.449   -6.879  0.25 46.85  ? 50  TRP   B O   1 
ATOM   606  C CB  A TRP   B 2 41  ? -16.145 3.338   -6.005  0.25 46.93  ? 50  TRP   B CB  1 
ATOM   607  C CB  B TRP   B 2 41  ? -16.145 3.314   -6.001  0.25 45.80  ? 50  TRP   B CB  1 
ATOM   608  C CB  C TRP   B 2 41  ? -16.145 3.338   -6.005  0.25 46.93  ? 50  TRP   B CB  1 
ATOM   609  C CB  D TRP   B 2 41  ? -16.187 3.340   -5.976  0.25 46.14  ? 50  TRP   B CB  1 
ATOM   610  C CG  A TRP   B 2 41  ? -16.268 4.050   -4.688  0.25 47.87  ? 50  TRP   B CG  1 
ATOM   611  C CG  B TRP   B 2 41  ? -15.982 4.091   -4.725  0.25 46.08  ? 50  TRP   B CG  1 
ATOM   612  C CG  C TRP   B 2 41  ? -16.268 4.050   -4.688  0.25 47.87  ? 50  TRP   B CG  1 
ATOM   613  C CG  D TRP   B 2 41  ? -16.087 4.123   -4.694  0.25 46.59  ? 50  TRP   B CG  1 
ATOM   614  C CD1 A TRP   B 2 41  ? -17.347 4.047   -3.857  0.25 48.84  ? 50  TRP   B CD1 1 
ATOM   615  C CD1 B TRP   B 2 41  ? -14.873 4.772   -4.312  0.25 46.90  ? 50  TRP   B CD1 1 
ATOM   616  C CD1 C TRP   B 2 41  ? -17.347 4.047   -3.857  0.25 48.84  ? 50  TRP   B CD1 1 
ATOM   617  C CD1 D TRP   B 2 41  ? -15.040 4.897   -4.284  0.25 47.47  ? 50  TRP   B CD1 1 
ATOM   618  C CD2 A TRP   B 2 41  ? -15.297 4.918   -4.083  0.25 48.26  ? 50  TRP   B CD2 1 
ATOM   619  C CD2 B TRP   B 2 41  ? -16.986 4.322   -3.732  0.25 46.00  ? 50  TRP   B CD2 1 
ATOM   620  C CD2 C TRP   B 2 41  ? -15.297 4.918   -4.083  0.25 48.26  ? 50  TRP   B CD2 1 
ATOM   621  C CD2 D TRP   B 2 41  ? -17.082 4.218   -3.667  0.25 46.63  ? 50  TRP   B CD2 1 
ATOM   622  N NE1 A TRP   B 2 41  ? -17.099 4.835   -2.757  0.25 49.31  ? 50  TRP   B NE1 1 
ATOM   623  N NE1 B TRP   B 2 41  ? -15.126 5.407   -3.119  0.25 47.00  ? 50  TRP   B NE1 1 
ATOM   624  N NE1 C TRP   B 2 41  ? -17.099 4.835   -2.757  0.25 49.31  ? 50  TRP   B NE1 1 
ATOM   625  N NE1 D TRP   B 2 41  ? -15.331 5.485   -3.076  0.25 47.63  ? 50  TRP   B NE1 1 
ATOM   626  C CE2 A TRP   B 2 41  ? -15.850 5.387   -2.875  0.25 49.08  ? 50  TRP   B CE2 1 
ATOM   627  C CE2 B TRP   B 2 41  ? -16.412 5.133   -2.732  0.25 46.72  ? 50  TRP   B CE2 1 
ATOM   628  C CE2 C TRP   B 2 41  ? -15.850 5.387   -2.875  0.25 49.08  ? 50  TRP   B CE2 1 
ATOM   629  C CE2 D TRP   B 2 41  ? -16.572 5.070   -2.665  0.25 47.39  ? 50  TRP   B CE2 1 
ATOM   630  C CE3 A TRP   B 2 41  ? -14.002 5.323   -4.432  0.25 48.94  ? 50  TRP   B CE3 1 
ATOM   631  C CE3 B TRP   B 2 41  ? -18.311 3.906   -3.580  0.25 46.52  ? 50  TRP   B CE3 1 
ATOM   632  C CE3 C TRP   B 2 41  ? -14.002 5.323   -4.432  0.25 48.94  ? 50  TRP   B CE3 1 
ATOM   633  C CE3 D TRP   B 2 41  ? -18.351 3.658   -3.489  0.25 47.18  ? 50  TRP   B CE3 1 
ATOM   634  C CZ2 A TRP   B 2 41  ? -15.164 6.256   -2.030  0.25 49.86  ? 50  TRP   B CZ2 1 
ATOM   635  C CZ2 B TRP   B 2 41  ? -17.123 5.547   -1.606  0.25 47.21  ? 50  TRP   B CZ2 1 
ATOM   636  C CZ2 C TRP   B 2 41  ? -15.164 6.256   -2.030  0.25 49.86  ? 50  TRP   B CZ2 1 
ATOM   637  C CZ2 D TRP   B 2 41  ? -17.296 5.387   -1.515  0.25 47.92  ? 50  TRP   B CZ2 1 
ATOM   638  C CZ3 A TRP   B 2 41  ? -13.326 6.184   -3.591  0.25 49.85  ? 50  TRP   B CZ3 1 
ATOM   639  C CZ3 B TRP   B 2 41  ? -19.011 4.315   -2.461  0.25 47.35  ? 50  TRP   B CZ3 1 
ATOM   640  C CZ3 C TRP   B 2 41  ? -13.326 6.184   -3.591  0.25 49.85  ? 50  TRP   B CZ3 1 
ATOM   641  C CZ3 D TRP   B 2 41  ? -19.060 3.966   -2.342  0.25 48.09  ? 50  TRP   B CZ3 1 
ATOM   642  C CH2 A TRP   B 2 41  ? -13.902 6.633   -2.402  0.25 50.05  ? 50  TRP   B CH2 1 
ATOM   643  C CH2 B TRP   B 2 41  ? -18.414 5.111   -1.482  0.25 47.29  ? 50  TRP   B CH2 1 
ATOM   644  C CH2 C TRP   B 2 41  ? -13.902 6.633   -2.402  0.25 50.05  ? 50  TRP   B CH2 1 
ATOM   645  C CH2 D TRP   B 2 41  ? -18.532 4.820   -1.372  0.25 47.99  ? 50  TRP   B CH2 1 
ATOM   646  N N   . HIS   B 2 42  ? -14.618 5.211   -8.129  1.00 46.76  ? 51  HIS   B N   1 
ATOM   647  C CA  . HIS   B 2 42  ? -13.672 6.327   -8.345  1.00 47.70  ? 51  HIS   B CA  1 
ATOM   648  C C   . HIS   B 2 42  ? -14.240 7.526   -9.175  1.00 48.69  ? 51  HIS   B C   1 
ATOM   649  O O   . HIS   B 2 42  ? -13.676 8.608   -9.126  1.00 48.93  ? 51  HIS   B O   1 
ATOM   650  C CB  . HIS   B 2 42  ? -12.329 5.838   -8.922  1.00 47.84  ? 51  HIS   B CB  1 
ATOM   651  C CG  . HIS   B 2 42  ? -12.377 5.489   -10.373 1.00 48.53  ? 51  HIS   B CG  1 
ATOM   652  N ND1 . HIS   B 2 42  ? -12.556 4.183   -10.796 1.00 50.03  ? 51  HIS   B ND1 1 
ATOM   653  C CD2 . HIS   B 2 42  ? -12.288 6.291   -11.460 1.00 48.69  ? 51  HIS   B CD2 1 
ATOM   654  C CE1 . HIS   B 2 42  ? -12.542 4.237   -12.116 1.00 50.13  ? 51  HIS   B CE1 1 
ATOM   655  N NE2 . HIS   B 2 42  ? -12.392 5.487   -12.553 1.00 49.46  ? 51  HIS   B NE2 1 
ATOM   656  N N   . VAL   B 2 43  ? -15.396 7.356   -9.832  1.00 49.18  ? 52  VAL   B N   1 
ATOM   657  C CA  . VAL   B 2 43  ? -16.065 8.393   -10.605 1.00 49.71  ? 52  VAL   B CA  1 
ATOM   658  C C   . VAL   B 2 43  ? -16.809 9.375   -9.667  1.00 50.65  ? 52  VAL   B C   1 
ATOM   659  O O   . VAL   B 2 43  ? -16.650 10.587  -9.788  1.00 51.29  ? 52  VAL   B O   1 
ATOM   660  C CB  . VAL   B 2 43  ? -17.036 7.736   -11.628 1.00 50.14  ? 52  VAL   B CB  1 
ATOM   661  C CG1 . VAL   B 2 43  ? -17.922 8.777   -12.304 1.00 50.62  ? 52  VAL   B CG1 1 
ATOM   662  C CG2 . VAL   B 2 43  ? -16.283 6.900   -12.659 1.00 50.26  ? 52  VAL   B CG2 1 
ATOM   663  N N   . THR   B 2 44  ? -17.633 8.857   -8.749  1.00 50.52  ? 53  THR   B N   1 
ATOM   664  C CA  . THR   B 2 44  ? -18.419 9.710   -7.854  1.00 50.61  ? 53  THR   B CA  1 
ATOM   665  C C   . THR   B 2 44  ? -17.843 9.909   -6.473  1.00 50.70  ? 53  THR   B C   1 
ATOM   666  O O   . THR   B 2 44  ? -18.182 10.884  -5.809  1.00 50.80  ? 53  THR   B O   1 
ATOM   667  C CB  . THR   B 2 44  ? -19.834 9.140   -7.733  1.00 50.77  ? 53  THR   B CB  1 
ATOM   668  O OG1 . THR   B 2 44  ? -19.754 7.834   -7.155  1.00 50.86  ? 53  THR   B OG1 1 
ATOM   669  C CG2 . THR   B 2 44  ? -20.533 9.035   -9.103  1.00 51.31  ? 53  THR   B CG2 1 
ATOM   670  N N   . LYS   B 2 45  ? -16.982 8.989   -6.036  1.00 50.86  ? 54  LYS   B N   1 
ATOM   671  C CA  . LYS   B 2 45  ? -16.466 8.845   -4.666  1.00 51.61  ? 54  LYS   B CA  1 
ATOM   672  C C   . LYS   B 2 45  ? -17.654 8.644   -3.681  1.00 51.97  ? 54  LYS   B C   1 
ATOM   673  O O   . LYS   B 2 45  ? -17.578 9.061   -2.531  1.00 51.89  ? 54  LYS   B O   1 
ATOM   674  C CB  . LYS   B 2 45  ? -15.565 10.010  -4.212  1.00 53.50  ? 54  LYS   B CB  1 
ATOM   675  C CG  . LYS   B 2 45  ? -14.483 10.419  -5.188  1.00 59.31  ? 54  LYS   B CG  1 
ATOM   676  C CD  . LYS   B 2 45  ? -13.456 9.341   -5.453  1.00 65.99  ? 54  LYS   B CD  1 
ATOM   677  C CE  . LYS   B 2 45  ? -12.384 9.921   -6.361  1.00 71.87  ? 54  LYS   B CE  1 
ATOM   678  N NZ  . LYS   B 2 45  ? -11.697 8.889   -7.201  1.00 74.94  ? 54  LYS   B NZ  1 
ATOM   679  N N   . GLY   B 2 46  ? -18.748 8.044   -4.149  1.00 51.84  ? 55  GLY   B N   1 
ATOM   680  C CA  . GLY   B 2 46  ? -19.929 7.838   -3.326  1.00 51.82  ? 55  GLY   B CA  1 
ATOM   681  C C   . GLY   B 2 46  ? -20.807 9.062   -3.132  1.00 52.09  ? 55  GLY   B C   1 
ATOM   682  O O   . GLY   B 2 46  ? -21.754 9.006   -2.353  1.00 52.57  ? 55  GLY   B O   1 
ATOM   683  N N   . ALA   B 2 47  ? -20.530 10.175  -3.827  1.00 51.98  ? 56  ALA   B N   1 
ATOM   684  C CA  . ALA   B 2 47  ? -21.352 11.384  -3.685  1.00 52.02  ? 56  ALA   B CA  1 
ATOM   685  C C   . ALA   B 2 47  ? -22.737 11.219  -4.323  1.00 52.64  ? 56  ALA   B C   1 
ATOM   686  O O   . ALA   B 2 47  ? -22.888 10.417  -5.232  1.00 53.06  ? 56  ALA   B O   1 
ATOM   687  C CB  . ALA   B 2 47  ? -20.639 12.574  -4.300  1.00 51.99  ? 56  ALA   B CB  1 
ATOM   688  N N   . ALA   B 2 48  ? -23.732 12.008  -3.893  1.00 53.01  ? 57  ALA   B N   1 
ATOM   689  C CA  . ALA   B 2 48  ? -25.074 11.958  -4.480  1.00 54.23  ? 57  ALA   B CA  1 
ATOM   690  C C   . ALA   B 2 48  ? -25.055 12.491  -5.917  1.00 55.89  ? 57  ALA   B C   1 
ATOM   691  O O   . ALA   B 2 48  ? -24.152 13.235  -6.287  1.00 56.70  ? 57  ALA   B O   1 
ATOM   692  C CB  . ALA   B 2 48  ? -26.067 12.770  -3.639  1.00 53.81  ? 57  ALA   B CB  1 
ATOM   693  N N   . LEU   B 2 49  ? -26.037 12.101  -6.730  1.00 56.42  ? 58  LEU   B N   1 
ATOM   694  C CA  . LEU   B 2 49  ? -26.120 12.548  -8.114  1.00 57.99  ? 58  LEU   B CA  1 
ATOM   695  C C   . LEU   B 2 49  ? -27.435 13.261  -8.386  1.00 59.83  ? 58  LEU   B C   1 
ATOM   696  O O   . LEU   B 2 49  ? -28.434 13.013  -7.731  1.00 59.93  ? 58  LEU   B O   1 
ATOM   697  C CB  . LEU   B 2 49  ? -25.968 11.370  -9.086  1.00 57.94  ? 58  LEU   B CB  1 
ATOM   698  C CG  . LEU   B 2 49  ? -24.703 10.557  -8.952  1.00 58.92  ? 58  LEU   B CG  1 
ATOM   699  C CD1 . LEU   B 2 49  ? -24.772 9.329   -9.818  1.00 59.10  ? 58  LEU   B CD1 1 
ATOM   700  C CD2 . LEU   B 2 49  ? -23.496 11.383  -9.264  1.00 59.51  ? 58  LEU   B CD2 1 
ATOM   701  N N   . ARG   B 2 50  ? -27.432 14.136  -9.363  1.00 61.53  ? 59  ARG   B N   1 
ATOM   702  C CA  . ARG   B 2 50  ? -28.611 14.886  -9.753  1.00 64.08  ? 59  ARG   B CA  1 
ATOM   703  C C   . ARG   B 2 50  ? -29.100 14.385  -11.139 1.00 66.11  ? 59  ARG   B C   1 
ATOM   704  O O   . ARG   B 2 50  ? -28.293 13.948  -11.956 1.00 65.89  ? 59  ARG   B O   1 
ATOM   705  C CB  . ARG   B 2 50  ? -28.248 16.377  -9.747  1.00 66.17  ? 59  ARG   B CB  1 
ATOM   706  C CG  . ARG   B 2 50  ? -29.371 17.302  -10.139 1.00 71.49  ? 59  ARG   B CG  1 
ATOM   707  C CD  . ARG   B 2 50  ? -29.035 18.772  -9.933  1.00 76.47  ? 59  ARG   B CD  1 
ATOM   708  N NE  . ARG   B 2 50  ? -27.747 19.184  -10.505 1.00 80.35  ? 59  ARG   B NE  1 
ATOM   709  C CZ  . ARG   B 2 50  ? -27.572 19.571  -11.765 1.00 83.68  ? 59  ARG   B CZ  1 
ATOM   710  N NH1 . ARG   B 2 50  ? -28.588 19.553  -12.622 1.00 83.42  ? 59  ARG   B NH1 1 
ATOM   711  N NH2 . ARG   B 2 50  ? -26.372 19.952  -12.187 1.00 84.43  ? 59  ARG   B NH2 1 
ATOM   712  N N   . SER   B 2 51  ? -30.416 14.351  -11.360 1.00 67.88  ? 60  SER   B N   1 
ATOM   713  C CA  . SER   B 2 51  ? -30.979 13.932  -12.647 1.00 70.37  ? 60  SER   B CA  1 
ATOM   714  C C   . SER   B 2 51  ? -32.088 14.926  -12.963 1.00 72.78  ? 60  SER   B C   1 
ATOM   715  O O   . SER   B 2 51  ? -33.256 14.674  -12.662 1.00 73.43  ? 60  SER   B O   1 
ATOM   716  C CB  . SER   B 2 51  ? -31.541 12.519  -12.553 1.00 71.74  ? 60  SER   B CB  1 
ATOM   717  O OG  . SER   B 2 51  ? -31.936 12.043  -13.829 1.00 73.89  ? 60  SER   B OG  1 
ATOM   718  N N   . GLY   B 2 52  ? -31.707 16.093  -13.479 1.00 73.69  ? 61  GLY   B N   1 
ATOM   719  C CA  . GLY   B 2 52  ? -32.652 17.178  -13.693 1.00 74.52  ? 61  GLY   B CA  1 
ATOM   720  C C   . GLY   B 2 52  ? -32.938 17.761  -12.323 1.00 75.55  ? 61  GLY   B C   1 
ATOM   721  O O   . GLY   B 2 52  ? -32.006 18.196  -11.639 1.00 76.28  ? 61  GLY   B O   1 
ATOM   722  N N   . GLU   B 2 53  ? -34.193 17.674  -11.857 1.00 75.36  ? 62  GLU   B N   1 
ATOM   723  C CA  . GLU   B 2 53  ? -34.513 18.128  -10.504 1.00 75.51  ? 62  GLU   B CA  1 
ATOM   724  C C   . GLU   B 2 53  ? -34.500 16.970  -9.467  1.00 74.53  ? 62  GLU   B C   1 
ATOM   725  O O   . GLU   B 2 53  ? -34.416 17.236  -8.264  1.00 74.89  ? 62  GLU   B O   1 
ATOM   726  C CB  . GLU   B 2 53  ? -35.809 18.949  -10.453 1.00 79.08  ? 62  GLU   B CB  1 
ATOM   727  C CG  . GLU   B 2 53  ? -35.597 20.405  -10.853 1.00 87.20  ? 62  GLU   B CG  1 
ATOM   728  C CD  . GLU   B 2 53  ? -36.535 21.404  -10.194 1.00 99.07  ? 62  GLU   B CD  1 
ATOM   729  O OE1 . GLU   B 2 53  ? -37.541 20.962  -9.591  1.00 102.44 ? 62  GLU   B OE1 1 
ATOM   730  O OE2 . GLU   B 2 53  ? -36.264 22.627  -10.275 1.00 101.72 ? 62  GLU   B OE2 1 
ATOM   731  N N   . GLY   B 2 54  ? -34.523 15.716  -9.932  1.00 73.03  ? 63  GLY   B N   1 
ATOM   732  C CA  . GLY   B 2 54  ? -34.500 14.549  -9.056  1.00 71.91  ? 63  GLY   B CA  1 
ATOM   733  C C   . GLY   B 2 54  ? -33.137 14.253  -8.457  1.00 70.26  ? 63  GLY   B C   1 
ATOM   734  O O   . GLY   B 2 54  ? -32.112 14.683  -8.994  1.00 71.25  ? 63  GLY   B O   1 
ATOM   735  N N   . ARG   B 2 55  ? -33.109 13.511  -7.345  1.00 67.41  ? 64  ARG   B N   1 
ATOM   736  C CA  . ARG   B 2 55  ? -31.860 13.149  -6.674  1.00 65.40  ? 64  ARG   B CA  1 
ATOM   737  C C   . ARG   B 2 55  ? -31.636 11.621  -6.629  1.00 62.65  ? 64  ARG   B C   1 
ATOM   738  O O   . ARG   B 2 55  ? -32.576 10.852  -6.415  1.00 62.80  ? 64  ARG   B O   1 
ATOM   739  C CB  . ARG   B 2 55  ? -31.848 13.722  -5.240  1.00 66.63  ? 64  ARG   B CB  1 
ATOM   740  C CG  . ARG   B 2 55  ? -30.520 13.567  -4.494  1.00 69.13  ? 64  ARG   B CG  1 
ATOM   741  C CD  . ARG   B 2 55  ? -30.578 14.236  -3.123  1.00 72.41  ? 64  ARG   B CD  1 
ATOM   742  N NE  . ARG   B 2 55  ? -29.453 13.852  -2.271  1.00 74.73  ? 64  ARG   B NE  1 
ATOM   743  C CZ  . ARG   B 2 55  ? -28.802 14.679  -1.458  1.00 76.78  ? 64  ARG   B CZ  1 
ATOM   744  N NH1 . ARG   B 2 55  ? -29.152 15.959  -1.382  1.00 76.37  ? 64  ARG   B NH1 1 
ATOM   745  N NH2 . ARG   B 2 55  ? -27.792 14.235  -0.718  1.00 76.17  ? 64  ARG   B NH2 1 
ATOM   746  N N   . LEU   B 2 56  ? -30.386 11.189  -6.810  1.00 59.75  ? 65  LEU   B N   1 
ATOM   747  C CA  . LEU   B 2 56  ? -30.031 9.789   -6.721  1.00 57.57  ? 65  LEU   B CA  1 
ATOM   748  C C   . LEU   B 2 56  ? -29.100 9.664   -5.539  1.00 55.74  ? 65  LEU   B C   1 
ATOM   749  O O   . LEU   B 2 56  ? -28.056 10.306  -5.527  1.00 55.38  ? 65  LEU   B O   1 
ATOM   750  C CB  . LEU   B 2 56  ? -29.282 9.314   -7.986  1.00 57.47  ? 65  LEU   B CB  1 
ATOM   751  C CG  . LEU   B 2 56  ? -29.891 9.596   -9.339  1.00 58.43  ? 65  LEU   B CG  1 
ATOM   752  C CD1 . LEU   B 2 56  ? -29.037 8.981   -10.426 1.00 58.49  ? 65  LEU   B CD1 1 
ATOM   753  C CD2 . LEU   B 2 56  ? -31.290 9.046   -9.439  1.00 58.99  ? 65  LEU   B CD2 1 
ATOM   754  N N   . ASP   B 2 57  ? -29.456 8.849   -4.552  1.00 54.67  ? 66  ASP   B N   1 
ATOM   755  C CA  . ASP   B 2 57  ? -28.601 8.637   -3.387  1.00 54.41  ? 66  ASP   B CA  1 
ATOM   756  C C   . ASP   B 2 57  ? -27.931 7.271   -3.459  1.00 52.83  ? 66  ASP   B C   1 
ATOM   757  O O   . ASP   B 2 57  ? -28.539 6.307   -3.936  1.00 52.80  ? 66  ASP   B O   1 
ATOM   758  C CB  . ASP   B 2 57  ? -29.413 8.750   -2.089  1.00 57.58  ? 66  ASP   B CB  1 
ATOM   759  C CG  . ASP   B 2 57  ? -30.010 10.126  -1.917  1.00 64.43  ? 66  ASP   B CG  1 
ATOM   760  O OD1 . ASP   B 2 57  ? -29.278 11.114  -2.120  1.00 65.46  ? 66  ASP   B OD1 1 
ATOM   761  O OD2 . ASP   B 2 57  ? -31.217 10.213  -1.609  1.00 67.14  ? 66  ASP   B OD2 1 
ATOM   762  N N   . PRO   B 2 58  ? -26.671 7.157   -2.999  1.00 51.15  ? 67  PRO   B N   1 
ATOM   763  C CA  . PRO   B 2 58  ? -26.009 5.845   -3.021  1.00 49.78  ? 67  PRO   B CA  1 
ATOM   764  C C   . PRO   B 2 58  ? -26.699 4.798   -2.129  1.00 48.34  ? 67  PRO   B C   1 
ATOM   765  O O   . PRO   B 2 58  ? -27.337 5.126   -1.128  1.00 47.53  ? 67  PRO   B O   1 
ATOM   766  C CB  . PRO   B 2 58  ? -24.580 6.166   -2.578  1.00 50.73  ? 67  PRO   B CB  1 
ATOM   767  C CG  . PRO   B 2 58  ? -24.702 7.390   -1.760  1.00 51.56  ? 67  PRO   B CG  1 
ATOM   768  C CD  . PRO   B 2 58  ? -25.797 8.194   -2.419  1.00 50.48  ? 67  PRO   B CD  1 
ATOM   769  N N   . TYR   B 2 59  ? -26.611 3.532   -2.531  1.00 47.43  ? 68  TYR   B N   1 
ATOM   770  C CA  . TYR   B 2 59  ? -27.264 2.435   -1.835  1.00 46.38  ? 68  TYR   B CA  1 
ATOM   771  C C   . TYR   B 2 59  ? -26.251 1.373   -1.431  1.00 46.11  ? 68  TYR   B C   1 
ATOM   772  O O   . TYR   B 2 59  ? -26.335 0.828   -0.345  1.00 46.61  ? 68  TYR   B O   1 
ATOM   773  C CB  . TYR   B 2 59  ? -28.336 1.834   -2.759  1.00 45.67  ? 68  TYR   B CB  1 
ATOM   774  C CG  . TYR   B 2 59  ? -29.127 0.695   -2.155  1.00 45.22  ? 68  TYR   B CG  1 
ATOM   775  C CD1 . TYR   B 2 59  ? -28.611 -0.597  -2.119  1.00 45.35  ? 68  TYR   B CD1 1 
ATOM   776  C CD2 . TYR   B 2 59  ? -30.406 0.898   -1.666  1.00 45.66  ? 68  TYR   B CD2 1 
ATOM   777  C CE1 . TYR   B 2 59  ? -29.334 -1.648  -1.572  1.00 46.12  ? 68  TYR   B CE1 1 
ATOM   778  C CE2 . TYR   B 2 59  ? -31.154 -0.152  -1.149  1.00 46.63  ? 68  TYR   B CE2 1 
ATOM   779  C CZ  . TYR   B 2 59  ? -30.621 -1.429  -1.120  1.00 47.43  ? 68  TYR   B CZ  1 
ATOM   780  O OH  . TYR   B 2 59  ? -31.346 -2.460  -0.567  1.00 48.72  ? 68  TYR   B OH  1 
ATOM   781  N N   . TRP   B 2 60  ? -25.320 1.059   -2.304  1.00 45.79  ? 69  TRP   B N   1 
ATOM   782  C CA  . TRP   B 2 60  ? -24.276 0.068   -2.037  1.00 45.68  ? 69  TRP   B CA  1 
ATOM   783  C C   . TRP   B 2 60  ? -22.992 0.553   -2.700  1.00 46.53  ? 69  TRP   B C   1 
ATOM   784  O O   . TRP   B 2 60  ? -23.033 1.139   -3.769  1.00 47.32  ? 69  TRP   B O   1 
ATOM   785  C CB  . TRP   B 2 60  ? -24.667 -1.341  -2.551  1.00 44.62  ? 69  TRP   B CB  1 
ATOM   786  C CG  . TRP   B 2 60  ? -23.506 -2.308  -2.547  1.00 44.53  ? 69  TRP   B CG  1 
ATOM   787  C CD1 . TRP   B 2 60  ? -22.998 -2.975  -1.472  1.00 45.21  ? 69  TRP   B CD1 1 
ATOM   788  C CD2 . TRP   B 2 60  ? -22.629 -2.598  -3.653  1.00 44.38  ? 69  TRP   B CD2 1 
ATOM   789  N NE1 . TRP   B 2 60  ? -21.874 -3.681  -1.843  1.00 45.11  ? 69  TRP   B NE1 1 
ATOM   790  C CE2 . TRP   B 2 60  ? -21.615 -3.448  -3.171  1.00 44.89  ? 69  TRP   B CE2 1 
ATOM   791  C CE3 . TRP   B 2 60  ? -22.555 -2.148  -4.976  1.00 44.96  ? 69  TRP   B CE3 1 
ATOM   792  C CZ2 . TRP   B 2 60  ? -20.559 -3.877  -3.977  1.00 45.40  ? 69  TRP   B CZ2 1 
ATOM   793  C CZ3 . TRP   B 2 60  ? -21.541 -2.619  -5.792  1.00 45.83  ? 69  TRP   B CZ3 1 
ATOM   794  C CH2 . TRP   B 2 60  ? -20.563 -3.482  -5.296  1.00 45.81  ? 69  TRP   B CH2 1 
ATOM   795  N N   . GLY   B 2 61  ? -21.864 0.281   -2.075  1.00 46.88  ? 70  GLY   B N   1 
ATOM   796  C CA  . GLY   B 2 61  ? -20.570 0.653   -2.634  1.00 47.02  ? 70  GLY   B CA  1 
ATOM   797  C C   . GLY   B 2 61  ? -19.450 -0.122  -1.990  1.00 46.35  ? 70  GLY   B C   1 
ATOM   798  O O   . GLY   B 2 61  ? -19.592 -0.576  -0.856  1.00 47.05  ? 70  GLY   B O   1 
ATOM   799  N N   . ASP   B 2 62  ? -18.327 -0.241  -2.685  1.00 45.30  ? 71  ASP   B N   1 
ATOM   800  C CA  . ASP   B 2 62  ? -17.165 -0.977  -2.220  1.00 45.72  ? 71  ASP   B CA  1 
ATOM   801  C C   . ASP   B 2 62  ? -15.935 -0.465  -2.956  1.00 45.62  ? 71  ASP   B C   1 
ATOM   802  O O   . ASP   B 2 62  ? -15.819 -0.662  -4.150  1.00 44.97  ? 71  ASP   B O   1 
ATOM   803  C CB  . ASP   B 2 62  ? -17.360 -2.484  -2.485  1.00 48.66  ? 71  ASP   B CB  1 
ATOM   804  C CG  . ASP   B 2 62  ? -16.393 -3.392  -1.757  1.00 57.16  ? 71  ASP   B CG  1 
ATOM   805  O OD1 . ASP   B 2 62  ? -15.172 -3.221  -1.931  1.00 58.50  ? 71  ASP   B OD1 1 
ATOM   806  O OD2 . ASP   B 2 62  ? -16.859 -4.282  -1.024  1.00 61.90  ? 71  ASP   B OD2 1 
ATOM   807  N N   . VAL   B 2 63  ? -14.994 0.143   -2.234  1.00 46.51  ? 72  VAL   B N   1 
ATOM   808  C CA  . VAL   B 2 63  ? -13.776 0.696   -2.827  1.00 46.53  ? 72  VAL   B CA  1 
ATOM   809  C C   . VAL   B 2 63  ? -12.889 -0.381  -3.448  1.00 47.01  ? 72  VAL   B C   1 
ATOM   810  O O   . VAL   B 2 63  ? -12.220 -0.101  -4.428  1.00 48.23  ? 72  VAL   B O   1 
ATOM   811  C CB  . VAL   B 2 63  ? -13.031 1.556   -1.771  1.00 46.46  ? 72  VAL   B CB  1 
ATOM   812  C CG1 . VAL   B 2 63  ? -11.562 1.772   -2.122  1.00 47.02  ? 72  VAL   B CG1 1 
ATOM   813  C CG2 . VAL   B 2 63  ? -13.729 2.892   -1.577  1.00 46.64  ? 72  VAL   B CG2 1 
ATOM   814  N N   . LYS   B 2 64  ? -12.876 -1.605  -2.897  1.00 47.32  ? 73  LYS   B N   1 
ATOM   815  C CA  . LYS   B 2 64  ? -12.016 -2.658  -3.436  1.00 47.16  ? 73  LYS   B CA  1 
ATOM   816  C C   . LYS   B 2 64  ? -12.521 -3.161  -4.777  1.00 47.42  ? 73  LYS   B C   1 
ATOM   817  O O   . LYS   B 2 64  ? -11.746 -3.246  -5.723  1.00 47.77  ? 73  LYS   B O   1 
ATOM   818  C CB  . LYS   B 2 64  ? -11.769 -3.788  -2.443  1.00 47.74  ? 73  LYS   B CB  1 
ATOM   819  C CG  . LYS   B 2 64  ? -10.628 -4.691  -2.926  1.00 50.22  ? 73  LYS   B CG  1 
ATOM   820  C CD  . LYS   B 2 64  ? -10.148 -5.606  -1.831  1.00 54.42  ? 73  LYS   B CD  1 
ATOM   821  C CE  . LYS   B 2 64  ? -9.218  -6.616  -2.438  1.00 58.44  ? 73  LYS   B CE  1 
ATOM   822  N NZ  . LYS   B 2 64  ? -9.180  -7.853  -1.634  1.00 61.25  ? 73  LYS   B NZ  1 
ATOM   823  N N   . GLN   B 2 65  ? -13.821 -3.445  -4.876  1.00 47.29  ? 74  GLN   B N   1 
ATOM   824  C CA  . GLN   B 2 65  ? -14.440 -3.823  -6.146  1.00 47.71  ? 74  GLN   B CA  1 
ATOM   825  C C   . GLN   B 2 65  ? -14.480 -2.642  -7.122  1.00 47.52  ? 74  GLN   B C   1 
ATOM   826  O O   . GLN   B 2 65  ? -14.619 -2.859  -8.332  1.00 47.91  ? 74  GLN   B O   1 
ATOM   827  C CB  . GLN   B 2 65  ? -15.886 -4.288  -5.921  1.00 49.99  ? 74  GLN   B CB  1 
ATOM   828  C CG  . GLN   B 2 65  ? -15.996 -5.626  -5.198  1.00 54.83  ? 74  GLN   B CG  1 
ATOM   829  C CD  . GLN   B 2 65  ? -17.436 -6.096  -5.156  1.00 61.62  ? 74  GLN   B CD  1 
ATOM   830  O OE1 . GLN   B 2 65  ? -18.142 -6.130  -6.186  1.00 63.84  ? 74  GLN   B OE1 1 
ATOM   831  N NE2 . GLN   B 2 65  ? -17.902 -6.465  -3.962  1.00 61.89  ? 74  GLN   B NE2 1 
ATOM   832  N N   . ASP   B 2 66  ? -14.423 -1.393  -6.586  1.00 46.41  ? 75  ASP   B N   1 
ATOM   833  C CA  . ASP   B 2 66  ? -14.515 -0.128  -7.303  1.00 46.14  ? 75  ASP   B CA  1 
ATOM   834  C C   . ASP   B 2 66  ? -15.861 -0.024  -7.993  1.00 45.25  ? 75  ASP   B C   1 
ATOM   835  O O   . ASP   B 2 66  ? -15.939 0.469   -9.114  1.00 45.14  ? 75  ASP   B O   1 
ATOM   836  C CB  . ASP   B 2 66  ? -13.345 0.122   -8.283  1.00 47.39  ? 75  ASP   B CB  1 
ATOM   837  C CG  . ASP   B 2 66  ? -13.343 1.522   -8.879  1.00 51.00  ? 75  ASP   B CG  1 
ATOM   838  O OD1 . ASP   B 2 66  ? -13.714 2.472   -8.163  1.00 51.71  ? 75  ASP   B OD1 1 
ATOM   839  O OD2 . ASP   B 2 66  ? -12.994 1.663   -10.067 1.00 52.01  ? 75  ASP   B OD2 1 
ATOM   840  N N   . LEU   B 2 67  ? -16.944 -0.353  -7.279  1.00 44.12  ? 76  LEU   B N   1 
ATOM   841  C CA  . LEU   B 2 67  ? -18.298 -0.224  -7.813  1.00 43.17  ? 76  LEU   B CA  1 
ATOM   842  C C   . LEU   B 2 67  ? -19.190 0.478   -6.817  1.00 43.70  ? 76  LEU   B C   1 
ATOM   843  O O   . LEU   B 2 67  ? -18.917 0.472   -5.602  1.00 43.38  ? 76  LEU   B O   1 
ATOM   844  C CB  . LEU   B 2 67  ? -18.903 -1.593  -8.157  1.00 42.85  ? 76  LEU   B CB  1 
ATOM   845  C CG  . LEU   B 2 67  ? -18.186 -2.371  -9.255  1.00 43.58  ? 76  LEU   B CG  1 
ATOM   846  C CD1 . LEU   B 2 67  ? -18.615 -3.817  -9.264  1.00 43.32  ? 76  LEU   B CD1 1 
ATOM   847  C CD2 . LEU   B 2 67  ? -18.384 -1.680  -10.662 1.00 44.35  ? 76  LEU   B CD2 1 
ATOM   848  N N   . VAL   B 2 68  ? -20.286 1.069   -7.329  1.00 43.53  ? 77  VAL   B N   1 
ATOM   849  C CA  . VAL   B 2 68  ? -21.294 1.747   -6.514  1.00 43.43  ? 77  VAL   B CA  1 
ATOM   850  C C   . VAL   B 2 68  ? -22.647 1.710   -7.264  1.00 42.87  ? 77  VAL   B C   1 
ATOM   851  O O   . VAL   B 2 68  ? -22.671 1.776   -8.486  1.00 42.99  ? 77  VAL   B O   1 
ATOM   852  C CB  . VAL   B 2 68  ? -20.838 3.194   -6.162  1.00 43.62  ? 77  VAL   B CB  1 
ATOM   853  C CG1 . VAL   B 2 68  ? -20.508 3.996   -7.415  1.00 43.76  ? 77  VAL   B CG1 1 
ATOM   854  C CG2 . VAL   B 2 68  ? -21.844 3.918   -5.275  1.00 43.97  ? 77  VAL   B CG2 1 
ATOM   855  N N   . SER   B 2 69  ? -23.754 1.542   -6.533  1.00 42.99  ? 78  SER   B N   1 
ATOM   856  C CA  . SER   B 2 69  ? -25.128 1.528   -7.059  1.00 42.43  ? 78  SER   B CA  1 
ATOM   857  C C   . SER   B 2 69  ? -25.957 2.619   -6.369  1.00 42.96  ? 78  SER   B C   1 
ATOM   858  O O   . SER   B 2 69  ? -25.715 2.971   -5.218  1.00 43.60  ? 78  SER   B O   1 
ATOM   859  C CB  . SER   B 2 69  ? -25.790 0.158   -6.889  1.00 41.81  ? 78  SER   B CB  1 
ATOM   860  O OG  . SER   B 2 69  ? -26.133 -0.133  -5.542  1.00 41.87  ? 78  SER   B OG  1 
ATOM   861  N N   . TYR   B 2 70  ? -26.891 3.182   -7.100  1.00 43.05  ? 79  TYR   B N   1 
ATOM   862  C CA  . TYR   B 2 70  ? -27.727 4.270   -6.613  1.00 43.88  ? 79  TYR   B CA  1 
ATOM   863  C C   . TYR   B 2 70  ? -29.174 3.845   -6.746  1.00 44.16  ? 79  TYR   B C   1 
ATOM   864  O O   . TYR   B 2 70  ? -29.545 3.197   -7.750  1.00 43.23  ? 79  TYR   B O   1 
ATOM   865  C CB  . TYR   B 2 70  ? -27.482 5.541   -7.462  1.00 44.43  ? 79  TYR   B CB  1 
ATOM   866  C CG  . TYR   B 2 70  ? -26.157 6.216   -7.178  1.00 45.16  ? 79  TYR   B CG  1 
ATOM   867  C CD1 . TYR   B 2 70  ? -24.973 5.741   -7.740  1.00 45.37  ? 79  TYR   B CD1 1 
ATOM   868  C CD2 . TYR   B 2 70  ? -26.090 7.347   -6.378  1.00 46.12  ? 79  TYR   B CD2 1 
ATOM   869  C CE1 . TYR   B 2 70  ? -23.752 6.362   -7.484  1.00 46.30  ? 79  TYR   B CE1 1 
ATOM   870  C CE2 . TYR   B 2 70  ? -24.875 7.945   -6.075  1.00 47.33  ? 79  TYR   B CE2 1 
ATOM   871  C CZ  . TYR   B 2 70  ? -23.708 7.460   -6.640  1.00 48.23  ? 79  TYR   B CZ  1 
ATOM   872  O OH  . TYR   B 2 70  ? -22.523 8.077   -6.321  1.00 49.93  ? 79  TYR   B OH  1 
ATOM   873  N N   . CYS   B 2 71  ? -29.989 4.207   -5.721  1.00 44.75  ? 80  CYS   B N   1 
ATOM   874  C CA  . CYS   B 2 71  ? -31.434 3.945   -5.611  1.00 45.76  ? 80  CYS   B CA  1 
ATOM   875  C C   . CYS   B 2 71  ? -31.781 2.503   -5.281  1.00 45.75  ? 80  CYS   B C   1 
ATOM   876  O O   . CYS   B 2 71  ? -32.921 2.248   -4.893  1.00 47.38  ? 80  CYS   B O   1 
ATOM   877  C CB  . CYS   B 2 71  ? -32.205 4.422   -6.841  1.00 48.22  ? 80  CYS   B CB  1 
ATOM   878  S SG  . CYS   B 2 71  ? -31.858 6.138   -7.322  1.00 56.10  ? 80  CYS   B SG  1 
ATOM   879  N N   . GLY   B 2 72  ? -30.835 1.576   -5.415  1.00 43.85  ? 81  GLY   B N   1 
ATOM   880  C CA  . GLY   B 2 72  ? -31.115 0.190   -5.089  1.00 42.83  ? 81  GLY   B CA  1 
ATOM   881  C C   . GLY   B 2 72  ? -29.908 -0.696  -5.190  1.00 41.87  ? 81  GLY   B C   1 
ATOM   882  O O   . GLY   B 2 72  ? -28.808 -0.242  -5.498  1.00 40.81  ? 81  GLY   B O   1 
ATOM   883  N N   . PRO   B 2 73  ? -30.099 -1.975  -4.872  1.00 41.92  ? 82  PRO   B N   1 
ATOM   884  C CA  . PRO   B 2 73  ? -28.982 -2.921  -4.996  1.00 43.09  ? 82  PRO   B CA  1 
ATOM   885  C C   . PRO   B 2 73  ? -28.474 -3.142  -6.425  1.00 44.23  ? 82  PRO   B C   1 
ATOM   886  O O   . PRO   B 2 73  ? -29.212 -2.982  -7.405  1.00 44.85  ? 82  PRO   B O   1 
ATOM   887  C CB  . PRO   B 2 73  ? -29.537 -4.209  -4.377  1.00 43.25  ? 82  PRO   B CB  1 
ATOM   888  C CG  . PRO   B 2 73  ? -31.031 -4.092  -4.531  1.00 42.94  ? 82  PRO   B CG  1 
ATOM   889  C CD  . PRO   B 2 73  ? -31.354 -2.634  -4.463  1.00 41.05  ? 82  PRO   B CD  1 
ATOM   890  N N   . TRP   B 2 74  ? -27.205 -3.570  -6.548  1.00 44.62  ? 83  TRP   B N   1 
ATOM   891  C CA  . TRP   B 2 74  ? -26.575 -3.896  -7.813  1.00 45.65  ? 83  TRP   B CA  1 
ATOM   892  C C   . TRP   B 2 74  ? -27.442 -4.917  -8.608  1.00 47.24  ? 83  TRP   B C   1 
ATOM   893  O O   . TRP   B 2 74  ? -27.749 -5.985  -8.086  1.00 47.54  ? 83  TRP   B O   1 
ATOM   894  C CB  . TRP   B 2 74  ? -25.155 -4.435  -7.559  1.00 45.29  ? 83  TRP   B CB  1 
ATOM   895  C CG  . TRP   B 2 74  ? -24.360 -4.611  -8.817  1.00 45.00  ? 83  TRP   B CG  1 
ATOM   896  C CD1 . TRP   B 2 74  ? -24.346 -5.707  -9.628  1.00 45.23  ? 83  TRP   B CD1 1 
ATOM   897  C CD2 . TRP   B 2 74  ? -23.547 -3.618  -9.468  1.00 44.93  ? 83  TRP   B CD2 1 
ATOM   898  N NE1 . TRP   B 2 74  ? -23.524 -5.485  -10.703 1.00 45.50  ? 83  TRP   B NE1 1 
ATOM   899  C CE2 . TRP   B 2 74  ? -23.064 -4.193  -10.661 1.00 45.26  ? 83  TRP   B CE2 1 
ATOM   900  C CE3 . TRP   B 2 74  ? -23.184 -2.298  -9.159  1.00 45.20  ? 83  TRP   B CE3 1 
ATOM   901  C CZ2 . TRP   B 2 74  ? -22.219 -3.503  -11.536 1.00 45.70  ? 83  TRP   B CZ2 1 
ATOM   902  C CZ3 . TRP   B 2 74  ? -22.338 -1.623  -10.016 1.00 45.94  ? 83  TRP   B CZ3 1 
ATOM   903  C CH2 . TRP   B 2 74  ? -21.861 -2.226  -11.188 1.00 46.02  ? 83  TRP   B CH2 1 
ATOM   904  N N   . LYS   B 2 75  ? -27.901 -4.543  -9.824  1.00 47.85  ? 84  LYS   B N   1 
ATOM   905  C CA  . LYS   B 2 75  ? -28.794 -5.380  -10.637 1.00 49.00  ? 84  LYS   B CA  1 
ATOM   906  C C   . LYS   B 2 75  ? -28.078 -6.159  -11.754 1.00 51.03  ? 84  LYS   B C   1 
ATOM   907  O O   . LYS   B 2 75  ? -28.651 -7.102  -12.299 1.00 51.77  ? 84  LYS   B O   1 
ATOM   908  C CB  . LYS   B 2 75  ? -29.880 -4.507  -11.291 1.00 50.00  ? 84  LYS   B CB  1 
ATOM   909  C CG  . LYS   B 2 75  ? -30.778 -3.750  -10.326 1.00 50.28  ? 84  LYS   B CG  1 
ATOM   910  C CD  . LYS   B 2 75  ? -31.679 -4.721  -9.600  1.00 53.98  ? 84  LYS   B CD  1 
ATOM   911  C CE  . LYS   B 2 75  ? -32.470 -4.089  -8.487  1.00 57.76  ? 84  LYS   B CE  1 
ATOM   912  N NZ  . LYS   B 2 75  ? -33.767 -3.594  -8.993  1.00 60.64  ? 84  LYS   B NZ  1 
ATOM   913  N N   . LEU   B 2 76  ? -26.863 -5.745  -12.139 1.00 51.45  ? 85  LEU   B N   1 
ATOM   914  C CA  . LEU   B 2 76  ? -26.146 -6.345  -13.265 1.00 51.90  ? 85  LEU   B CA  1 
ATOM   915  C C   . LEU   B 2 76  ? -25.461 -7.651  -12.883 1.00 53.74  ? 85  LEU   B C   1 
ATOM   916  O O   . LEU   B 2 76  ? -24.503 -7.638  -12.116 1.00 53.14  ? 85  LEU   B O   1 
ATOM   917  C CB  . LEU   B 2 76  ? -25.134 -5.339  -13.837 1.00 51.37  ? 85  LEU   B CB  1 
ATOM   918  C CG  . LEU   B 2 76  ? -25.662 -3.917  -14.101 1.00 50.87  ? 85  LEU   B CG  1 
ATOM   919  C CD1 . LEU   B 2 76  ? -24.561 -3.011  -14.577 1.00 50.78  ? 85  LEU   B CD1 1 
ATOM   920  C CD2 . LEU   B 2 76  ? -26.753 -3.932  -15.124 1.00 50.98  ? 85  LEU   B CD2 1 
ATOM   921  N N   . ASP   B 2 77  ? -25.935 -8.783  -13.433 1.00 55.52  ? 86  ASP   B N   1 
ATOM   922  C CA  . ASP   B 2 77  ? -25.383 -10.083 -13.054 1.00 57.64  ? 86  ASP   B CA  1 
ATOM   923  C C   . ASP   B 2 77  ? -24.887 -10.971 -14.203 1.00 58.15  ? 86  ASP   B C   1 
ATOM   924  O O   . ASP   B 2 77  ? -24.457 -12.096 -13.936 1.00 58.55  ? 86  ASP   B O   1 
ATOM   925  C CB  . ASP   B 2 77  ? -26.375 -10.870 -12.184 1.00 61.12  ? 86  ASP   B CB  1 
ATOM   926  C CG  . ASP   B 2 77  ? -27.698 -11.192 -12.855 1.00 69.41  ? 86  ASP   B CG  1 
ATOM   927  O OD1 . ASP   B 2 77  ? -28.063 -10.489 -13.835 1.00 71.18  ? 86  ASP   B OD1 1 
ATOM   928  O OD2 . ASP   B 2 77  ? -28.381 -12.131 -12.394 1.00 72.79  ? 86  ASP   B OD2 1 
ATOM   929  N N   . ALA   B 2 78  ? -24.901 -10.485 -15.446 1.00 57.94  ? 87  ALA   B N   1 
ATOM   930  C CA  . ALA   B 2 78  ? -24.384 -11.270 -16.567 1.00 57.82  ? 87  ALA   B CA  1 
ATOM   931  C C   . ALA   B 2 78  ? -22.862 -11.362 -16.462 1.00 58.02  ? 87  ALA   B C   1 
ATOM   932  O O   . ALA   B 2 78  ? -22.217 -10.471 -15.894 1.00 57.53  ? 87  ALA   B O   1 
ATOM   933  C CB  . ALA   B 2 78  ? -24.783 -10.637 -17.896 1.00 57.53  ? 87  ALA   B CB  1 
ATOM   934  N N   . ALA   B 2 79  ? -22.285 -12.446 -17.001 1.00 58.13  ? 88  ALA   B N   1 
ATOM   935  C CA  . ALA   B 2 79  ? -20.840 -12.605 -16.974 1.00 58.76  ? 88  ALA   B CA  1 
ATOM   936  C C   . ALA   B 2 79  ? -20.284 -13.022 -18.327 1.00 59.29  ? 88  ALA   B C   1 
ATOM   937  O O   . ALA   B 2 79  ? -20.979 -13.656 -19.117 1.00 59.44  ? 88  ALA   B O   1 
ATOM   938  C CB  . ALA   B 2 79  ? -20.444 -13.616 -15.910 1.00 59.09  ? 88  ALA   B CB  1 
ATOM   939  N N   . TRP   B 2 80  ? -19.015 -12.682 -18.591 1.00 59.48  ? 89  TRP   B N   1 
ATOM   940  C CA  . TRP   B 2 80  ? -18.319 -13.073 -19.808 1.00 59.96  ? 89  TRP   B CA  1 
ATOM   941  C C   . TRP   B 2 80  ? -18.208 -14.600 -19.828 1.00 61.39  ? 89  TRP   B C   1 
ATOM   942  O O   . TRP   B 2 80  ? -17.897 -15.191 -18.794 1.00 60.89  ? 89  TRP   B O   1 
ATOM   943  C CB  . TRP   B 2 80  ? -16.913 -12.468 -19.827 1.00 59.47  ? 89  TRP   B CB  1 
ATOM   944  C CG  . TRP   B 2 80  ? -16.137 -12.823 -21.060 1.00 59.80  ? 89  TRP   B CG  1 
ATOM   945  C CD1 . TRP   B 2 80  ? -16.588 -12.811 -22.343 1.00 60.53  ? 89  TRP   B CD1 1 
ATOM   946  C CD2 . TRP   B 2 80  ? -14.759 -13.224 -21.121 1.00 59.84  ? 89  TRP   B CD2 1 
ATOM   947  N NE1 . TRP   B 2 80  ? -15.589 -13.213 -23.200 1.00 60.92  ? 89  TRP   B NE1 1 
ATOM   948  C CE2 . TRP   B 2 80  ? -14.443 -13.430 -22.481 1.00 60.57  ? 89  TRP   B CE2 1 
ATOM   949  C CE3 . TRP   B 2 80  ? -13.751 -13.375 -20.165 1.00 60.21  ? 89  TRP   B CE3 1 
ATOM   950  C CZ2 . TRP   B 2 80  ? -13.170 -13.802 -22.907 1.00 60.88  ? 89  TRP   B CZ2 1 
ATOM   951  C CZ3 . TRP   B 2 80  ? -12.492 -13.761 -20.590 1.00 61.43  ? 89  TRP   B CZ3 1 
ATOM   952  C CH2 . TRP   B 2 80  ? -12.211 -13.963 -21.949 1.00 61.25  ? 89  TRP   B CH2 1 
ATOM   953  N N   . ASP   B 2 81  ? -18.506 -15.242 -20.970 1.00 62.59  ? 90  ASP   B N   1 
ATOM   954  C CA  . ASP   B 2 81  ? -18.443 -16.701 -21.030 1.00 64.32  ? 90  ASP   B CA  1 
ATOM   955  C C   . ASP   B 2 81  ? -17.001 -17.278 -21.147 1.00 66.40  ? 90  ASP   B C   1 
ATOM   956  O O   . ASP   B 2 81  ? -16.848 -18.500 -21.227 1.00 67.37  ? 90  ASP   B O   1 
ATOM   957  C CB  . ASP   B 2 81  ? -19.354 -17.249 -22.135 1.00 64.98  ? 90  ASP   B CB  1 
ATOM   958  C CG  . ASP   B 2 81  ? -18.936 -16.921 -23.542 1.00 69.62  ? 90  ASP   B CG  1 
ATOM   959  O OD1 . ASP   B 2 81  ? -17.911 -16.223 -23.713 1.00 70.03  ? 90  ASP   B OD1 1 
ATOM   960  O OD2 . ASP   B 2 81  ? -19.647 -17.348 -24.490 1.00 72.81  ? 90  ASP   B OD2 1 
ATOM   961  N N   . GLY   B 2 82  ? -15.987 -16.405 -21.161 1.00 66.62  ? 91  GLY   B N   1 
ATOM   962  C CA  . GLY   B 2 82  ? -14.582 -16.785 -21.265 1.00 67.58  ? 91  GLY   B CA  1 
ATOM   963  C C   . GLY   B 2 82  ? -14.128 -17.182 -22.656 1.00 68.88  ? 91  GLY   B C   1 
ATOM   964  O O   . GLY   B 2 82  ? -12.962 -17.536 -22.853 1.00 69.63  ? 91  GLY   B O   1 
ATOM   965  N N   . LEU   B 2 83  ? -15.036 -17.109 -23.644 1.00 68.72  ? 92  LEU   B N   1 
ATOM   966  C CA  . LEU   B 2 83  ? -14.751 -17.544 -24.993 1.00 68.83  ? 92  LEU   B CA  1 
ATOM   967  C C   . LEU   B 2 83  ? -15.029 -16.525 -26.077 1.00 69.21  ? 92  LEU   B C   1 
ATOM   968  O O   . LEU   B 2 83  ? -14.258 -16.452 -27.035 1.00 70.61  ? 92  LEU   B O   1 
ATOM   969  C CB  . LEU   B 2 83  ? -15.637 -18.757 -25.286 1.00 69.01  ? 92  LEU   B CB  1 
ATOM   970  C CG  . LEU   B 2 83  ? -15.006 -20.111 -25.208 1.00 70.21  ? 92  LEU   B CG  1 
ATOM   971  C CD1 . LEU   B 2 83  ? -15.328 -20.758 -23.891 1.00 70.69  ? 92  LEU   B CD1 1 
ATOM   972  C CD2 . LEU   B 2 83  ? -15.547 -20.965 -26.289 1.00 70.52  ? 92  LEU   B CD2 1 
ATOM   973  N N   . SER   B 2 84  ? -16.187 -15.841 -26.029 1.00 67.64  ? 93  SER   B N   1 
ATOM   974  C CA  . SER   B 2 84  ? -16.607 -14.993 -27.141 1.00 66.55  ? 93  SER   B CA  1 
ATOM   975  C C   . SER   B 2 84  ? -16.187 -13.538 -27.041 1.00 65.77  ? 93  SER   B C   1 
ATOM   976  O O   . SER   B 2 84  ? -15.802 -13.063 -25.971 1.00 66.64  ? 93  SER   B O   1 
ATOM   977  C CB  . SER   B 2 84  ? -18.121 -15.088 -27.363 1.00 67.34  ? 93  SER   B CB  1 
ATOM   978  O OG  . SER   B 2 84  ? -18.816 -15.880 -26.413 1.00 69.01  ? 93  SER   B OG  1 
ATOM   979  N N   . GLU   B 2 85  ? -16.245 -12.841 -28.175 1.00 64.47  ? 94  GLU   B N   1 
ATOM   980  C CA  . GLU   B 2 85  ? -15.986 -11.410 -28.280 1.00 63.57  ? 94  GLU   B CA  1 
ATOM   981  C C   . GLU   B 2 85  ? -17.110 -10.640 -27.569 1.00 61.53  ? 94  GLU   B C   1 
ATOM   982  O O   . GLU   B 2 85  ? -18.208 -11.163 -27.355 1.00 61.64  ? 94  GLU   B O   1 
ATOM   983  C CB  . GLU   B 2 85  ? -15.864 -10.958 -29.756 1.00 64.99  ? 94  GLU   B CB  1 
ATOM   984  C CG  . GLU   B 2 85  ? -14.664 -11.567 -30.469 1.00 70.59  ? 94  GLU   B CG  1 
ATOM   985  C CD  . GLU   B 2 85  ? -14.276 -10.929 -31.789 1.00 76.29  ? 94  GLU   B CD  1 
ATOM   986  O OE1 . GLU   B 2 85  ? -15.161 -10.347 -32.455 1.00 77.02  ? 94  GLU   B OE1 1 
ATOM   987  O OE2 . GLU   B 2 85  ? -13.082 -11.004 -32.156 1.00 78.88  ? 94  GLU   B OE2 1 
ATOM   988  N N   . VAL   B 2 86  ? -16.809 -9.405  -27.174 1.00 59.52  ? 95  VAL   B N   1 
ATOM   989  C CA  . VAL   B 2 86  ? -17.713 -8.533  -26.418 1.00 57.65  ? 95  VAL   B CA  1 
ATOM   990  C C   . VAL   B 2 86  ? -17.717 -7.135  -27.043 1.00 57.48  ? 95  VAL   B C   1 
ATOM   991  O O   . VAL   B 2 86  ? -16.880 -6.852  -27.902 1.00 59.08  ? 95  VAL   B O   1 
ATOM   992  C CB  . VAL   B 2 86  ? -17.226 -8.445  -24.931 1.00 55.90  ? 95  VAL   B CB  1 
ATOM   993  C CG1 . VAL   B 2 86  ? -17.081 -9.824  -24.308 1.00 56.03  ? 95  VAL   B CG1 1 
ATOM   994  C CG2 . VAL   B 2 86  ? -15.918 -7.661  -24.840 1.00 55.24  ? 95  VAL   B CG2 1 
ATOM   995  N N   . GLN   B 2 87  ? -18.608 -6.237  -26.583 1.00 56.02  ? 96  GLN   B N   1 
ATOM   996  C CA  . GLN   B 2 87  ? -18.598 -4.866  -27.053 1.00 55.61  ? 96  GLN   B CA  1 
ATOM   997  C C   . GLN   B 2 87  ? -18.459 -3.866  -25.920 1.00 55.12  ? 96  GLN   B C   1 
ATOM   998  O O   . GLN   B 2 87  ? -19.204 -3.916  -24.936 1.00 55.13  ? 96  GLN   B O   1 
ATOM   999  C CB  . GLN   B 2 87  ? -19.808 -4.544  -27.965 1.00 56.32  ? 96  GLN   B CB  1 
ATOM   1000 C CG  . GLN   B 2 87  ? -19.600 -5.115  -29.348 1.00 59.00  ? 96  GLN   B CG  1 
ATOM   1001 C CD  . GLN   B 2 87  ? -20.672 -4.795  -30.356 1.00 60.16  ? 96  GLN   B CD  1 
ATOM   1002 O OE1 . GLN   B 2 87  ? -21.565 -3.960  -30.137 1.00 58.54  ? 96  GLN   B OE1 1 
ATOM   1003 N NE2 . GLN   B 2 87  ? -20.601 -5.478  -31.489 1.00 60.72  ? 96  GLN   B NE2 1 
ATOM   1004 N N   . LEU   B 2 88  ? -17.486 -2.969  -26.047 1.00 54.11  ? 97  LEU   B N   1 
ATOM   1005 C CA  . LEU   B 2 88  ? -17.334 -1.883  -25.106 1.00 54.02  ? 97  LEU   B CA  1 
ATOM   1006 C C   . LEU   B 2 88  ? -18.198 -0.779  -25.675 1.00 53.50  ? 97  LEU   B C   1 
ATOM   1007 O O   . LEU   B 2 88  ? -17.938 -0.307  -26.795 1.00 54.54  ? 97  LEU   B O   1 
ATOM   1008 C CB  . LEU   B 2 88  ? -15.878 -1.400  -25.009 1.00 54.30  ? 97  LEU   B CB  1 
ATOM   1009 C CG  . LEU   B 2 88  ? -15.653 -0.072  -24.270 1.00 55.00  ? 97  LEU   B CG  1 
ATOM   1010 C CD1 . LEU   B 2 88  ? -16.173 -0.128  -22.824 1.00 54.76  ? 97  LEU   B CD1 1 
ATOM   1011 C CD2 . LEU   B 2 88  ? -14.184 0.333   -24.316 1.00 55.78  ? 97  LEU   B CD2 1 
ATOM   1012 N N   . LEU   B 2 89  ? -19.254 -0.415  -24.959 1.00 51.34  ? 98  LEU   B N   1 
ATOM   1013 C CA  . LEU   B 2 89  ? -20.076 0.690   -25.387 1.00 50.62  ? 98  LEU   B CA  1 
ATOM   1014 C C   . LEU   B 2 89  ? -19.414 1.900   -24.733 1.00 51.20  ? 98  LEU   B C   1 
ATOM   1015 O O   . LEU   B 2 89  ? -19.774 2.329   -23.621 1.00 51.33  ? 98  LEU   B O   1 
ATOM   1016 C CB  . LEU   B 2 89  ? -21.552 0.487   -25.031 1.00 49.96  ? 98  LEU   B CB  1 
ATOM   1017 C CG  . LEU   B 2 89  ? -22.531 1.683   -25.225 1.00 50.57  ? 98  LEU   B CG  1 
ATOM   1018 C CD1 . LEU   B 2 89  ? -22.311 2.395   -26.502 1.00 51.91  ? 98  LEU   B CD1 1 
ATOM   1019 C CD2 . LEU   B 2 89  ? -23.952 1.225   -25.150 1.00 50.99  ? 98  LEU   B CD2 1 
ATOM   1020 N N   . ALA   B 2 90  ? -18.337 2.365   -25.403 1.00 51.15  ? 99  ALA   B N   1 
ATOM   1021 C CA  . ALA   B 2 90  ? -17.512 3.478   -24.956 1.00 51.04  ? 99  ALA   B CA  1 
ATOM   1022 C C   . ALA   B 2 90  ? -18.276 4.781   -25.084 1.00 51.13  ? 99  ALA   B C   1 
ATOM   1023 O O   . ALA   B 2 90  ? -18.727 5.085   -26.189 1.00 51.88  ? 99  ALA   B O   1 
ATOM   1024 C CB  . ALA   B 2 90  ? -16.266 3.571   -25.822 1.00 50.22  ? 99  ALA   B CB  1 
ATOM   1025 N N   . VAL   B 2 91  ? -18.368 5.577   -24.001 1.00 50.38  ? 100 VAL   B N   1 
ATOM   1026 C CA  . VAL   B 2 91  ? -18.992 6.905   -24.024 1.00 51.25  ? 100 VAL   B CA  1 
ATOM   1027 C C   . VAL   B 2 91  ? -17.901 7.946   -23.664 1.00 53.62  ? 100 VAL   B C   1 
ATOM   1028 O O   . VAL   B 2 91  ? -17.745 8.318   -22.505 1.00 53.53  ? 100 VAL   B O   1 
ATOM   1029 C CB  . VAL   B 2 91  ? -20.250 7.026   -23.124 1.00 51.04  ? 100 VAL   B CB  1 
ATOM   1030 C CG1 . VAL   B 2 91  ? -20.846 8.429   -23.212 1.00 51.41  ? 100 VAL   B CG1 1 
ATOM   1031 C CG2 . VAL   B 2 91  ? -21.295 5.981   -23.491 1.00 50.62  ? 100 VAL   B CG2 1 
ATOM   1032 N N   . PRO   B 2 92  ? -17.097 8.393   -24.656 1.00 55.86  ? 101 PRO   B N   1 
ATOM   1033 C CA  . PRO   B 2 92  ? -15.974 9.298   -24.345 1.00 56.64  ? 101 PRO   B CA  1 
ATOM   1034 C C   . PRO   B 2 92  ? -16.396 10.736  -24.110 1.00 57.74  ? 101 PRO   B C   1 
ATOM   1035 O O   . PRO   B 2 92  ? -17.396 11.178  -24.673 1.00 58.77  ? 101 PRO   B O   1 
ATOM   1036 C CB  . PRO   B 2 92  ? -15.065 9.179   -25.592 1.00 56.98  ? 101 PRO   B CB  1 
ATOM   1037 C CG  . PRO   B 2 92  ? -15.670 8.101   -26.453 1.00 57.31  ? 101 PRO   B CG  1 
ATOM   1038 C CD  . PRO   B 2 92  ? -17.113 8.035   -26.088 1.00 55.52  ? 101 PRO   B CD  1 
ATOM   1039 N N   . PRO   B 2 93  ? -15.619 11.514  -23.334 1.00 57.63  ? 102 PRO   B N   1 
ATOM   1040 C CA  . PRO   B 2 93  ? -15.998 12.920  -23.103 1.00 57.57  ? 102 PRO   B CA  1 
ATOM   1041 C C   . PRO   B 2 93  ? -16.139 13.719  -24.399 1.00 58.17  ? 102 PRO   B C   1 
ATOM   1042 O O   . PRO   B 2 93  ? -15.292 13.627  -25.286 1.00 58.39  ? 102 PRO   B O   1 
ATOM   1043 C CB  . PRO   B 2 93  ? -14.877 13.449  -22.197 1.00 57.94  ? 102 PRO   B CB  1 
ATOM   1044 C CG  . PRO   B 2 93  ? -14.347 12.201  -21.490 1.00 58.65  ? 102 PRO   B CG  1 
ATOM   1045 C CD  . PRO   B 2 93  ? -14.399 11.150  -22.584 1.00 57.36  ? 102 PRO   B CD  1 
ATOM   1046 N N   . GLY   B 2 94  ? -17.261 14.429  -24.516 1.00 58.14  ? 103 GLY   B N   1 
ATOM   1047 C CA  . GLY   B 2 94  ? -17.613 15.248  -25.667 1.00 58.26  ? 103 GLY   B CA  1 
ATOM   1048 C C   . GLY   B 2 94  ? -17.853 14.492  -26.960 1.00 58.71  ? 103 GLY   B C   1 
ATOM   1049 O O   . GLY   B 2 94  ? -18.037 15.107  -28.008 1.00 58.47  ? 103 GLY   B O   1 
ATOM   1050 N N   . GLU   B 2 95  ? -17.785 13.151  -26.928 1.00 59.00  ? 104 GLU   B N   1 
ATOM   1051 C CA  . GLU   B 2 95  ? -17.949 12.347  -28.140 1.00 59.26  ? 104 GLU   B CA  1 
ATOM   1052 C C   . GLU   B 2 95  ? -19.125 11.387  -28.005 1.00 58.76  ? 104 GLU   B C   1 
ATOM   1053 O O   . GLU   B 2 95  ? -19.514 11.042  -26.894 1.00 58.14  ? 104 GLU   B O   1 
ATOM   1054 C CB  . GLU   B 2 95  ? -16.648 11.588  -28.470 1.00 62.39  ? 104 GLU   B CB  1 
ATOM   1055 C CG  . GLU   B 2 95  ? -15.444 12.507  -28.606 1.00 67.93  ? 104 GLU   B CG  1 
ATOM   1056 C CD  . GLU   B 2 95  ? -14.108 11.812  -28.796 1.00 74.79  ? 104 GLU   B CD  1 
ATOM   1057 O OE1 . GLU   B 2 95  ? -14.061 10.570  -28.648 1.00 76.21  ? 104 GLU   B OE1 1 
ATOM   1058 O OE2 . GLU   B 2 95  ? -13.107 12.510  -29.087 1.00 76.71  ? 104 GLU   B OE2 1 
ATOM   1059 N N   . ARG   B 2 96  ? -19.699 10.986  -29.138 1.00 58.98  ? 105 ARG   B N   1 
ATOM   1060 C CA  . ARG   B 2 96  ? -20.859 10.102  -29.225 1.00 60.61  ? 105 ARG   B CA  1 
ATOM   1061 C C   . ARG   B 2 96  ? -20.562 8.713   -28.684 1.00 61.31  ? 105 ARG   B C   1 
ATOM   1062 O O   . ARG   B 2 96  ? -19.432 8.237   -28.836 1.00 61.78  ? 105 ARG   B O   1 
ATOM   1063 C CB  . ARG   B 2 96  ? -21.229 9.947   -30.709 1.00 63.31  ? 105 ARG   B CB  1 
ATOM   1064 C CG  . ARG   B 2 96  ? -22.688 10.136  -31.073 1.00 68.82  ? 105 ARG   B CG  1 
ATOM   1065 C CD  . ARG   B 2 96  ? -22.769 10.562  -32.541 1.00 75.42  ? 105 ARG   B CD  1 
ATOM   1066 N NE  . ARG   B 2 96  ? -22.388 11.970  -32.713 1.00 81.21  ? 105 ARG   B NE  1 
ATOM   1067 C CZ  . ARG   B 2 96  ? -21.805 12.469  -33.797 1.00 84.29  ? 105 ARG   B CZ  1 
ATOM   1068 N NH1 . ARG   B 2 96  ? -21.526 11.682  -34.830 1.00 85.71  ? 105 ARG   B NH1 1 
ATOM   1069 N NH2 . ARG   B 2 96  ? -21.497 13.761  -33.859 1.00 83.34  ? 105 ARG   B NH2 1 
ATOM   1070 N N   . ALA   B 2 97  ? -21.595 8.012   -28.148 1.00 61.02  ? 106 ALA   B N   1 
ATOM   1071 C CA  . ALA   B 2 97  ? -21.459 6.624   -27.703 1.00 61.77  ? 106 ALA   B CA  1 
ATOM   1072 C C   . ALA   B 2 97  ? -21.059 5.750   -28.915 1.00 62.41  ? 106 ALA   B C   1 
ATOM   1073 O O   . ALA   B 2 97  ? -21.586 5.941   -30.006 1.00 62.88  ? 106 ALA   B O   1 
ATOM   1074 C CB  . ALA   B 2 97  ? -22.765 6.133   -27.112 1.00 61.84  ? 106 ALA   B CB  1 
ATOM   1075 N N   . LYS   B 2 98  ? -20.098 4.846   -28.739 1.00 62.91  ? 107 LYS   B N   1 
ATOM   1076 C CA  . LYS   B 2 98  ? -19.577 4.039   -29.844 1.00 63.96  ? 107 LYS   B CA  1 
ATOM   1077 C C   . LYS   B 2 98  ? -19.300 2.603   -29.395 1.00 63.08  ? 107 LYS   B C   1 
ATOM   1078 O O   . LYS   B 2 98  ? -18.690 2.405   -28.348 1.00 63.47  ? 107 LYS   B O   1 
ATOM   1079 C CB  . LYS   B 2 98  ? -18.282 4.718   -30.318 1.00 67.99  ? 107 LYS   B CB  1 
ATOM   1080 C CG  . LYS   B 2 98  ? -17.539 4.059   -31.455 1.00 75.69  ? 107 LYS   B CG  1 
ATOM   1081 C CD  . LYS   B 2 98  ? -16.266 4.867   -31.826 1.00 82.75  ? 107 LYS   B CD  1 
ATOM   1082 C CE  . LYS   B 2 98  ? -15.387 5.209   -30.623 1.00 87.08  ? 107 LYS   B CE  1 
ATOM   1083 N NZ  . LYS   B 2 98  ? -13.937 5.010   -30.919 1.00 89.73  ? 107 LYS   B NZ  1 
ATOM   1084 N N   . ASN   B 2 99  ? -19.778 1.603   -30.147 1.00 61.78  ? 108 ASN   B N   1 
ATOM   1085 C CA  . ASN   B 2 99  ? -19.551 0.200   -29.782 1.00 61.56  ? 108 ASN   B CA  1 
ATOM   1086 C C   . ASN   B 2 99  ? -18.265 -0.294  -30.406 1.00 62.02  ? 108 ASN   B C   1 
ATOM   1087 O O   . ASN   B 2 99  ? -18.073 -0.119  -31.606 1.00 63.36  ? 108 ASN   B O   1 
ATOM   1088 C CB  . ASN   B 2 99  ? -20.705 -0.701  -30.233 1.00 61.62  ? 108 ASN   B CB  1 
ATOM   1089 C CG  . ASN   B 2 99  ? -22.013 -0.449  -29.525 1.00 64.35  ? 108 ASN   B CG  1 
ATOM   1090 O OD1 . ASN   B 2 99  ? -22.640 0.611   -29.686 1.00 66.78  ? 108 ASN   B OD1 1 
ATOM   1091 N ND2 . ASN   B 2 99  ? -22.487 -1.428  -28.764 1.00 62.64  ? 108 ASN   B ND2 1 
ATOM   1092 N N   . ILE   B 2 100 ? -17.378 -0.890  -29.612 1.00 60.91  ? 109 ILE   B N   1 
ATOM   1093 C CA  . ILE   B 2 100 ? -16.117 -1.427  -30.111 1.00 60.77  ? 109 ILE   B CA  1 
ATOM   1094 C C   . ILE   B 2 100 ? -16.056 -2.900  -29.739 1.00 59.82  ? 109 ILE   B C   1 
ATOM   1095 O O   . ILE   B 2 100 ? -16.179 -3.245  -28.565 1.00 59.83  ? 109 ILE   B O   1 
ATOM   1096 C CB  . ILE   B 2 100 ? -14.907 -0.694  -29.507 1.00 62.06  ? 109 ILE   B CB  1 
ATOM   1097 C CG1 . ILE   B 2 100 ? -15.065 0.842   -29.535 1.00 63.61  ? 109 ILE   B CG1 1 
ATOM   1098 C CG2 . ILE   B 2 100 ? -13.625 -1.165  -30.169 1.00 62.44  ? 109 ILE   B CG2 1 
ATOM   1099 C CD1 . ILE   B 2 100 ? -14.906 1.498   -30.891 1.00 65.50  ? 109 ILE   B CD1 1 
ATOM   1100 N N   . GLN   B 2 101 ? -15.830 -3.759  -30.703 1.00 59.03  ? 110 GLN   B N   1 
ATOM   1101 C CA  . GLN   B 2 101 ? -15.787 -5.196  -30.501 1.00 58.93  ? 110 GLN   B CA  1 
ATOM   1102 C C   . GLN   B 2 101 ? -14.364 -5.717  -30.299 1.00 59.46  ? 110 GLN   B C   1 
ATOM   1103 O O   . GLN   B 2 101 ? -13.469 -5.412  -31.090 1.00 59.98  ? 110 GLN   B O   1 
ATOM   1104 C CB  . GLN   B 2 101 ? -16.447 -5.887  -31.696 1.00 60.17  ? 110 GLN   B CB  1 
ATOM   1105 C CG  . GLN   B 2 101 ? -16.473 -7.405  -31.618 1.00 63.90  ? 110 GLN   B CG  1 
ATOM   1106 C CD  . GLN   B 2 101 ? -17.590 -7.964  -32.464 1.00 67.08  ? 110 GLN   B CD  1 
ATOM   1107 O OE1 . GLN   B 2 101 ? -18.649 -7.348  -32.636 1.00 67.39  ? 110 GLN   B OE1 1 
ATOM   1108 N NE2 . GLN   B 2 101 ? -17.377 -9.153  -33.002 1.00 66.89  ? 110 GLN   B NE2 1 
ATOM   1109 N N   . THR   B 2 102 ? -14.156 -6.512  -29.244 1.00 59.07  ? 111 THR   B N   1 
ATOM   1110 C CA  . THR   B 2 102 ? -12.836 -7.038  -28.946 1.00 59.94  ? 111 THR   B CA  1 
ATOM   1111 C C   . THR   B 2 102 ? -12.926 -8.421  -28.340 1.00 60.83  ? 111 THR   B C   1 
ATOM   1112 O O   . THR   B 2 102 ? -13.990 -8.803  -27.857 1.00 61.55  ? 111 THR   B O   1 
ATOM   1113 C CB  . THR   B 2 102 ? -12.061 -6.035  -28.036 1.00 61.35  ? 111 THR   B CB  1 
ATOM   1114 O OG1 . THR   B 2 102 ? -10.667 -6.395  -27.996 1.00 62.65  ? 111 THR   B OG1 1 
ATOM   1115 C CG2 . THR   B 2 102 ? -12.659 -5.910  -26.590 1.00 62.01  ? 111 THR   B CG2 1 
ATOM   1116 N N   . LEU   B 2 103 ? -11.825 -9.186  -28.360 1.00 60.96  ? 112 LEU   B N   1 
ATOM   1117 C CA  . LEU   B 2 103 ? -11.811 -10.456 -27.645 1.00 61.02  ? 112 LEU   B CA  1 
ATOM   1118 C C   . LEU   B 2 103 ? -11.053 -10.142 -26.375 1.00 61.34  ? 112 LEU   B C   1 
ATOM   1119 O O   . LEU   B 2 103 ? -9.899  -9.693  -26.425 1.00 61.39  ? 112 LEU   B O   1 
ATOM   1120 C CB  . LEU   B 2 103 ? -11.155 -11.634 -28.372 1.00 61.63  ? 112 LEU   B CB  1 
ATOM   1121 C CG  . LEU   B 2 103 ? -11.198 -12.919 -27.516 1.00 63.88  ? 112 LEU   B CG  1 
ATOM   1122 C CD1 . LEU   B 2 103 ? -12.480 -13.667 -27.722 1.00 64.43  ? 112 LEU   B CD1 1 
ATOM   1123 C CD2 . LEU   B 2 103 ? -10.020 -13.813 -27.774 1.00 65.39  ? 112 LEU   B CD2 1 
ATOM   1124 N N   . PRO   B 2 104 ? -11.693 -10.335 -25.216 1.00 61.01  ? 113 PRO   B N   1 
ATOM   1125 C CA  . PRO   B 2 104 ? -11.013 -10.010 -23.964 1.00 61.22  ? 113 PRO   B CA  1 
ATOM   1126 C C   . PRO   B 2 104 ? -9.814  -10.888 -23.647 1.00 62.01  ? 113 PRO   B C   1 
ATOM   1127 O O   . PRO   B 2 104 ? -9.751  -12.065 -24.002 1.00 62.52  ? 113 PRO   B O   1 
ATOM   1128 C CB  . PRO   B 2 104 ? -12.111 -10.169 -22.900 1.00 61.46  ? 113 PRO   B CB  1 
ATOM   1129 C CG  . PRO   B 2 104 ? -13.398 -10.152 -23.653 1.00 62.11  ? 113 PRO   B CG  1 
ATOM   1130 C CD  . PRO   B 2 104 ? -13.075 -10.787 -24.984 1.00 60.37  ? 113 PRO   B CD  1 
ATOM   1131 N N   . GLY   B 2 105 ? -8.866  -10.286 -22.953 1.00 61.96  ? 114 GLY   B N   1 
ATOM   1132 C CA  . GLY   B 2 105 ? -7.725  -10.972 -22.375 1.00 62.04  ? 114 GLY   B CA  1 
ATOM   1133 C C   . GLY   B 2 105 ? -8.078  -11.449 -20.973 1.00 62.06  ? 114 GLY   B C   1 
ATOM   1134 O O   . GLY   B 2 105 ? -9.257  -11.526 -20.615 1.00 61.48  ? 114 GLY   B O   1 
ATOM   1135 N N   . ILE   B 2 106 ? -7.070  -11.757 -20.151 1.00 62.58  ? 115 ILE   B N   1 
ATOM   1136 C CA  . ILE   B 2 106 ? -7.290  -12.275 -18.800 1.00 63.27  ? 115 ILE   B CA  1 
ATOM   1137 C C   . ILE   B 2 106 ? -6.380  -11.596 -17.780 1.00 64.01  ? 115 ILE   B C   1 
ATOM   1138 O O   . ILE   B 2 106 ? -5.195  -11.392 -18.023 1.00 64.88  ? 115 ILE   B O   1 
ATOM   1139 C CB  . ILE   B 2 106 ? -7.021  -13.816 -18.804 1.00 64.38  ? 115 ILE   B CB  1 
ATOM   1140 C CG1 . ILE   B 2 106 ? -8.011  -14.596 -19.673 1.00 66.27  ? 115 ILE   B CG1 1 
ATOM   1141 C CG2 . ILE   B 2 106 ? -6.944  -14.410 -17.417 1.00 65.10  ? 115 ILE   B CG2 1 
ATOM   1142 C CD1 . ILE   B 2 106 ? -9.384  -14.533 -19.201 1.00 67.98  ? 115 ILE   B CD1 1 
ATOM   1143 N N   . PHE   B 2 107 ? -6.919  -11.296 -16.617 1.00 63.92  ? 116 PHE   B N   1 
ATOM   1144 C CA  . PHE   B 2 107 ? -6.158  -10.820 -15.479 1.00 63.89  ? 116 PHE   B CA  1 
ATOM   1145 C C   . PHE   B 2 107 ? -6.105  -12.041 -14.586 1.00 64.62  ? 116 PHE   B C   1 
ATOM   1146 O O   . PHE   B 2 107 ? -7.144  -12.443 -14.065 1.00 64.75  ? 116 PHE   B O   1 
ATOM   1147 C CB  . PHE   B 2 107 ? -6.924  -9.722  -14.712 1.00 63.27  ? 116 PHE   B CB  1 
ATOM   1148 C CG  . PHE   B 2 107 ? -6.681  -8.295  -15.125 1.00 63.28  ? 116 PHE   B CG  1 
ATOM   1149 C CD1 . PHE   B 2 107 ? -6.019  -7.999  -16.307 1.00 63.82  ? 116 PHE   B CD1 1 
ATOM   1150 C CD2 . PHE   B 2 107 ? -7.150  -7.247  -14.354 1.00 63.64  ? 116 PHE   B CD2 1 
ATOM   1151 C CE1 . PHE   B 2 107 ? -5.835  -6.682  -16.708 1.00 64.26  ? 116 PHE   B CE1 1 
ATOM   1152 C CE2 . PHE   B 2 107 ? -6.963  -5.932  -14.755 1.00 64.34  ? 116 PHE   B CE2 1 
ATOM   1153 C CZ  . PHE   B 2 107 ? -6.316  -5.658  -15.935 1.00 64.22  ? 116 PHE   B CZ  1 
ATOM   1154 N N   . LYS   B 2 108 ? -4.938  -12.663 -14.438 1.00 65.10  ? 117 LYS   B N   1 
ATOM   1155 C CA  . LYS   B 2 108 ? -4.805  -13.802 -13.536 1.00 66.19  ? 117 LYS   B CA  1 
ATOM   1156 C C   . LYS   B 2 108 ? -4.453  -13.222 -12.171 1.00 66.59  ? 117 LYS   B C   1 
ATOM   1157 O O   . LYS   B 2 108 ? -3.442  -12.531 -12.062 1.00 66.40  ? 117 LYS   B O   1 
ATOM   1158 C CB  . LYS   B 2 108 ? -3.692  -14.774 -14.004 1.00 68.32  ? 117 LYS   B CB  1 
ATOM   1159 C CG  . LYS   B 2 108 ? -4.013  -15.544 -15.288 1.00 73.17  ? 117 LYS   B CG  1 
ATOM   1160 C CD  . LYS   B 2 108 ? -2.747  -15.837 -16.120 1.00 79.13  ? 117 LYS   B CD  1 
ATOM   1161 C CE  . LYS   B 2 108 ? -2.671  -17.270 -16.626 1.00 84.62  ? 117 LYS   B CE  1 
ATOM   1162 N NZ  . LYS   B 2 108 ? -2.298  -17.371 -18.087 1.00 88.25  ? 117 LYS   B NZ  1 
ATOM   1163 N N   . THR   B 2 109 ? -5.296  -13.449 -11.148 1.00 66.92  ? 118 THR   B N   1 
ATOM   1164 C CA  . THR   B 2 109 ? -5.003  -12.977 -9.789  1.00 68.35  ? 118 THR   B CA  1 
ATOM   1165 C C   . THR   B 2 109 ? -4.828  -14.196 -8.818  1.00 69.51  ? 118 THR   B C   1 
ATOM   1166 O O   . THR   B 2 109 ? -5.021  -15.346 -9.231  1.00 69.76  ? 118 THR   B O   1 
ATOM   1167 C CB  . THR   B 2 109 ? -6.042  -11.924 -9.293  1.00 69.78  ? 118 THR   B CB  1 
ATOM   1168 O OG1 . THR   B 2 109 ? -7.194  -12.569 -8.760  1.00 71.11  ? 118 THR   B OG1 1 
ATOM   1169 C CG2 . THR   B 2 109 ? -6.446  -10.923 -10.353 1.00 69.99  ? 118 THR   B CG2 1 
ATOM   1170 N N   . LYS   B 2 110 ? -4.460  -13.949 -7.538  1.00 69.79  ? 119 LYS   B N   1 
ATOM   1171 C CA  . LYS   B 2 110 ? -4.339  -15.034 -6.561  1.00 70.20  ? 119 LYS   B CA  1 
ATOM   1172 C C   . LYS   B 2 110 ? -5.725  -15.595 -6.153  1.00 70.96  ? 119 LYS   B C   1 
ATOM   1173 O O   . LYS   B 2 110 ? -5.796  -16.691 -5.594  1.00 71.43  ? 119 LYS   B O   1 
ATOM   1174 C CB  . LYS   B 2 110 ? -3.541  -14.576 -5.328  1.00 71.03  ? 119 LYS   B CB  1 
ATOM   1175 C CG  . LYS   B 2 110 ? -4.291  -13.600 -4.436  1.00 73.42  ? 119 LYS   B CG  1 
ATOM   1176 C CD  . LYS   B 2 110 ? -3.333  -12.738 -3.624  1.00 77.47  ? 119 LYS   B CD  1 
ATOM   1177 C CE  . LYS   B 2 110 ? -3.818  -12.478 -2.212  1.00 81.24  ? 119 LYS   B CE  1 
ATOM   1178 N NZ  . LYS   B 2 110 ? -5.044  -11.638 -2.178  1.00 83.68  ? 119 LYS   B NZ  1 
ATOM   1179 N N   . ASP   B 2 111 ? -6.817  -14.856 -6.449  1.00 70.64  ? 120 ASP   B N   1 
ATOM   1180 C CA  . ASP   B 2 111 ? -8.186  -15.254 -6.158  1.00 71.13  ? 120 ASP   B CA  1 
ATOM   1181 C C   . ASP   B 2 111 ? -8.997  -15.599 -7.415  1.00 71.24  ? 120 ASP   B C   1 
ATOM   1182 O O   . ASP   B 2 111 ? -10.226 -15.566 -7.355  1.00 72.05  ? 120 ASP   B O   1 
ATOM   1183 C CB  . ASP   B 2 111 ? -8.903  -14.132 -5.403  1.00 73.57  ? 120 ASP   B CB  1 
ATOM   1184 C CG  . ASP   B 2 111 ? -8.395  -13.926 -3.996  1.00 80.04  ? 120 ASP   B CG  1 
ATOM   1185 O OD1 . ASP   B 2 111 ? -8.198  -14.939 -3.279  1.00 81.35  ? 120 ASP   B OD1 1 
ATOM   1186 O OD2 . ASP   B 2 111 ? -8.206  -12.756 -3.603  1.00 82.89  ? 120 ASP   B OD2 1 
ATOM   1187 N N   . GLY   B 2 112 ? -8.338  -15.883 -8.535  1.00 70.03  ? 121 GLY   B N   1 
ATOM   1188 C CA  . GLY   B 2 112 ? -9.044  -16.246 -9.757  1.00 70.03  ? 121 GLY   B CA  1 
ATOM   1189 C C   . GLY   B 2 112 ? -8.814  -15.360 -10.966 1.00 69.64  ? 121 GLY   B C   1 
ATOM   1190 O O   . GLY   B 2 112 ? -8.156  -14.319 -10.875 1.00 69.75  ? 121 GLY   B O   1 
ATOM   1191 N N   . ASP   B 2 113 ? -9.356  -15.780 -12.120 1.00 68.84  ? 122 ASP   B N   1 
ATOM   1192 C CA  . ASP   B 2 113 ? -9.214  -15.035 -13.370 1.00 68.84  ? 122 ASP   B CA  1 
ATOM   1193 C C   . ASP   B 2 113 ? -10.392 -14.089 -13.622 1.00 67.64  ? 122 ASP   B C   1 
ATOM   1194 O O   . ASP   B 2 113 ? -11.541 -14.414 -13.318 1.00 67.92  ? 122 ASP   B O   1 
ATOM   1195 C CB  . ASP   B 2 113 ? -9.061  -15.985 -14.565 1.00 71.37  ? 122 ASP   B CB  1 
ATOM   1196 C CG  . ASP   B 2 113 ? -7.815  -16.847 -14.541 1.00 78.73  ? 122 ASP   B CG  1 
ATOM   1197 O OD1 . ASP   B 2 113 ? -6.925  -16.588 -13.696 1.00 79.93  ? 122 ASP   B OD1 1 
ATOM   1198 O OD2 . ASP   B 2 113 ? -7.725  -17.784 -15.373 1.00 82.20  ? 122 ASP   B OD2 1 
ATOM   1199 N N   . ILE   B 2 114 ? -10.085 -12.910 -14.167 1.00 65.89  ? 123 ILE   B N   1 
ATOM   1200 C CA  . ILE   B 2 114 ? -11.045 -11.864 -14.522 1.00 64.72  ? 123 ILE   B CA  1 
ATOM   1201 C C   . ILE   B 2 114 ? -10.829 -11.529 -16.009 1.00 62.84  ? 123 ILE   B C   1 
ATOM   1202 O O   . ILE   B 2 114 ? -9.688  -11.510 -16.473 1.00 62.00  ? 123 ILE   B O   1 
ATOM   1203 C CB  . ILE   B 2 114 ? -10.805 -10.594 -13.655 1.00 65.23  ? 123 ILE   B CB  1 
ATOM   1204 C CG1 . ILE   B 2 114 ? -10.779 -10.937 -12.170 1.00 67.10  ? 123 ILE   B CG1 1 
ATOM   1205 C CG2 . ILE   B 2 114 ? -11.839 -9.515  -13.925 1.00 65.57  ? 123 ILE   B CG2 1 
ATOM   1206 C CD1 . ILE   B 2 114 ? -9.928  -10.033 -11.346 1.00 68.95  ? 123 ILE   B CD1 1 
ATOM   1207 N N   . GLY   B 2 115 ? -11.906 -11.248 -16.738 1.00 61.51  ? 124 GLY   B N   1 
ATOM   1208 C CA  . GLY   B 2 115 ? -11.786 -10.809 -18.123 1.00 61.16  ? 124 GLY   B CA  1 
ATOM   1209 C C   . GLY   B 2 115 ? -11.159 -9.424  -18.161 1.00 60.79  ? 124 GLY   B C   1 
ATOM   1210 O O   . GLY   B 2 115 ? -11.224 -8.674  -17.178 1.00 61.00  ? 124 GLY   B O   1 
ATOM   1211 N N   . ALA   B 2 116 ? -10.495 -9.093  -19.251 1.00 60.24  ? 125 ALA   B N   1 
ATOM   1212 C CA  . ALA   B 2 116 ? -9.844  -7.795  -19.395 1.00 60.45  ? 125 ALA   B CA  1 
ATOM   1213 C C   . ALA   B 2 116 ? -10.008 -7.293  -20.835 1.00 60.71  ? 125 ALA   B C   1 
ATOM   1214 O O   . ALA   B 2 116 ? -9.996  -8.072  -21.754 1.00 61.63  ? 125 ALA   B O   1 
ATOM   1215 C CB  . ALA   B 2 116 ? -8.373  -7.913  -19.032 1.00 60.31  ? 125 ALA   B CB  1 
ATOM   1216 N N   A VAL   B 2 117 ? -10.189 -5.981  -21.018 0.25 60.75  ? 126 VAL   B N   1 
ATOM   1217 N N   B VAL   B 2 117 ? -10.148 -5.990  -21.006 0.25 60.65  ? 126 VAL   B N   1 
ATOM   1218 N N   C VAL   B 2 117 ? -10.189 -5.981  -21.018 0.25 60.75  ? 126 VAL   B N   1 
ATOM   1219 N N   D VAL   B 2 117 ? -10.148 -5.990  -21.006 0.25 60.65  ? 126 VAL   B N   1 
ATOM   1220 C CA  A VAL   B 2 117 ? -10.335 -5.389  -22.344 0.25 61.36  ? 126 VAL   B CA  1 
ATOM   1221 C CA  B VAL   B 2 117 ? -10.340 -5.374  -22.305 0.25 61.19  ? 126 VAL   B CA  1 
ATOM   1222 C CA  C VAL   B 2 117 ? -10.335 -5.389  -22.344 0.25 61.36  ? 126 VAL   B CA  1 
ATOM   1223 C CA  D VAL   B 2 117 ? -10.340 -5.374  -22.305 0.25 61.19  ? 126 VAL   B CA  1 
ATOM   1224 C C   A VAL   B 2 117 ? -9.197  -4.409  -22.635 0.25 61.83  ? 126 VAL   B C   1 
ATOM   1225 C C   B VAL   B 2 117 ? -9.183  -4.411  -22.614 0.25 61.72  ? 126 VAL   B C   1 
ATOM   1226 C C   C VAL   B 2 117 ? -9.197  -4.409  -22.635 0.25 61.83  ? 126 VAL   B C   1 
ATOM   1227 C C   D VAL   B 2 117 ? -9.183  -4.411  -22.614 0.25 61.72  ? 126 VAL   B C   1 
ATOM   1228 O O   A VAL   B 2 117 ? -8.976  -3.456  -21.886 0.25 61.79  ? 126 VAL   B O   1 
ATOM   1229 O O   B VAL   B 2 117 ? -8.936  -3.470  -21.856 0.25 61.67  ? 126 VAL   B O   1 
ATOM   1230 O O   C VAL   B 2 117 ? -8.976  -3.456  -21.886 0.25 61.79  ? 126 VAL   B O   1 
ATOM   1231 O O   D VAL   B 2 117 ? -8.936  -3.470  -21.856 0.25 61.67  ? 126 VAL   B O   1 
ATOM   1232 C CB  A VAL   B 2 117 ? -11.734 -4.782  -22.617 0.25 61.96  ? 126 VAL   B CB  1 
ATOM   1233 C CB  B VAL   B 2 117 ? -11.742 -4.714  -22.357 0.25 61.65  ? 126 VAL   B CB  1 
ATOM   1234 C CB  C VAL   B 2 117 ? -11.734 -4.782  -22.617 0.25 61.96  ? 126 VAL   B CB  1 
ATOM   1235 C CB  D VAL   B 2 117 ? -11.742 -4.714  -22.357 0.25 61.65  ? 126 VAL   B CB  1 
ATOM   1236 C CG1 A VAL   B 2 117 ? -12.765 -5.880  -22.852 0.25 62.40  ? 126 VAL   B CG1 1 
ATOM   1237 C CG1 B VAL   B 2 117 ? -11.833 -3.649  -23.434 0.25 61.99  ? 126 VAL   B CG1 1 
ATOM   1238 C CG1 C VAL   B 2 117 ? -12.765 -5.880  -22.852 0.25 62.40  ? 126 VAL   B CG1 1 
ATOM   1239 C CG1 D VAL   B 2 117 ? -11.833 -3.649  -23.434 0.25 61.99  ? 126 VAL   B CG1 1 
ATOM   1240 C CG2 A VAL   B 2 117 ? -12.172 -3.854  -21.489 0.25 62.39  ? 126 VAL   B CG2 1 
ATOM   1241 C CG2 B VAL   B 2 117 ? -12.829 -5.767  -22.546 0.25 62.04  ? 126 VAL   B CG2 1 
ATOM   1242 C CG2 C VAL   B 2 117 ? -12.172 -3.854  -21.489 0.25 62.39  ? 126 VAL   B CG2 1 
ATOM   1243 C CG2 D VAL   B 2 117 ? -12.829 -5.767  -22.546 0.25 62.04  ? 126 VAL   B CG2 1 
ATOM   1244 N N   . ALA   B 2 118 ? -8.452  -4.674  -23.709 1.00 61.89  ? 127 ALA   B N   1 
ATOM   1245 C CA  . ALA   B 2 118 ? -7.328  -3.841  -24.088 1.00 63.33  ? 127 ALA   B CA  1 
ATOM   1246 C C   . ALA   B 2 118 ? -7.744  -2.759  -25.078 1.00 64.98  ? 127 ALA   B C   1 
ATOM   1247 O O   . ALA   B 2 118 ? -7.437  -2.826  -26.271 1.00 65.44  ? 127 ALA   B O   1 
ATOM   1248 C CB  . ALA   B 2 118 ? -6.213  -4.693  -24.663 1.00 63.34  ? 127 ALA   B CB  1 
ATOM   1249 N N   . LEU   B 2 119 ? -8.494  -1.773  -24.580 1.00 65.26  ? 128 LEU   B N   1 
ATOM   1250 C CA  . LEU   B 2 119 ? -8.928  -0.633  -25.368 1.00 65.49  ? 128 LEU   B CA  1 
ATOM   1251 C C   . LEU   B 2 119 ? -8.566  0.588   -24.525 1.00 65.80  ? 128 LEU   B C   1 
ATOM   1252 O O   . LEU   B 2 119 ? -8.862  0.623   -23.334 1.00 66.10  ? 128 LEU   B O   1 
ATOM   1253 C CB  . LEU   B 2 119 ? -10.436 -0.698  -25.671 1.00 65.45  ? 128 LEU   B CB  1 
ATOM   1254 C CG  . LEU   B 2 119 ? -10.894 -1.880  -26.523 1.00 66.27  ? 128 LEU   B CG  1 
ATOM   1255 C CD1 . LEU   B 2 119 ? -12.405 -1.988  -26.539 1.00 66.53  ? 128 LEU   B CD1 1 
ATOM   1256 C CD2 . LEU   B 2 119 ? -10.348 -1.791  -27.950 1.00 66.99  ? 128 LEU   B CD2 1 
ATOM   1257 N N   C ASP   B 2 120 ? -7.887  1.567   -25.126 0.50 65.77  ? 129 ASP   B N   1 
ATOM   1258 N N   D ASP   B 2 120 ? -7.887  1.567   -25.126 0.50 65.77  ? 129 ASP   B N   1 
ATOM   1259 C CA  C ASP   B 2 120 ? -7.454  2.757   -24.406 0.50 66.05  ? 129 ASP   B CA  1 
ATOM   1260 C CA  D ASP   B 2 120 ? -7.454  2.757   -24.406 0.50 66.05  ? 129 ASP   B CA  1 
ATOM   1261 C C   C ASP   B 2 120 ? -8.386  3.927   -24.678 0.50 65.79  ? 129 ASP   B C   1 
ATOM   1262 C C   D ASP   B 2 120 ? -8.386  3.927   -24.678 0.50 65.79  ? 129 ASP   B C   1 
ATOM   1263 O O   C ASP   B 2 120 ? -8.557  4.323   -25.828 0.50 66.10  ? 129 ASP   B O   1 
ATOM   1264 O O   D ASP   B 2 120 ? -8.557  4.323   -25.828 0.50 66.10  ? 129 ASP   B O   1 
ATOM   1265 C CB  C ASP   B 2 120 ? -6.010  3.110   -24.791 0.50 68.15  ? 129 ASP   B CB  1 
ATOM   1266 C CB  D ASP   B 2 120 ? -6.010  3.110   -24.791 0.50 68.15  ? 129 ASP   B CB  1 
ATOM   1267 C CG  C ASP   B 2 120 ? -5.254  3.872   -23.720 0.50 73.62  ? 129 ASP   B CG  1 
ATOM   1268 C CG  D ASP   B 2 120 ? -5.254  3.872   -23.720 0.50 73.62  ? 129 ASP   B CG  1 
ATOM   1269 O OD1 C ASP   B 2 120 ? -5.844  4.798   -23.119 0.50 74.15  ? 129 ASP   B OD1 1 
ATOM   1270 O OD1 D ASP   B 2 120 ? -5.844  4.798   -23.119 0.50 74.15  ? 129 ASP   B OD1 1 
ATOM   1271 O OD2 C ASP   B 2 120 ? -4.065  3.552   -23.491 0.50 76.46  ? 129 ASP   B OD2 1 
ATOM   1272 O OD2 D ASP   B 2 120 ? -4.065  3.552   -23.491 0.50 76.46  ? 129 ASP   B OD2 1 
ATOM   1273 N N   . TYR   B 2 121 ? -8.975  4.489   -23.619 1.00 65.21  ? 130 TYR   B N   1 
ATOM   1274 C CA  . TYR   B 2 121 ? -9.898  5.620   -23.705 1.00 64.73  ? 130 TYR   B CA  1 
ATOM   1275 C C   . TYR   B 2 121 ? -9.621  6.635   -22.573 1.00 63.80  ? 130 TYR   B C   1 
ATOM   1276 O O   . TYR   B 2 121 ? -9.019  6.265   -21.563 1.00 63.86  ? 130 TYR   B O   1 
ATOM   1277 C CB  . TYR   B 2 121 ? -11.352 5.110   -23.626 1.00 64.99  ? 130 TYR   B CB  1 
ATOM   1278 C CG  . TYR   B 2 121 ? -11.856 4.648   -24.968 1.00 66.16  ? 130 TYR   B CG  1 
ATOM   1279 C CD1 . TYR   B 2 121 ? -12.293 5.559   -25.917 1.00 67.13  ? 130 TYR   B CD1 1 
ATOM   1280 C CD2 . TYR   B 2 121 ? -11.808 3.310   -25.326 1.00 67.35  ? 130 TYR   B CD2 1 
ATOM   1281 C CE1 . TYR   B 2 121 ? -12.688 5.149   -27.182 1.00 68.24  ? 130 TYR   B CE1 1 
ATOM   1282 C CE2 . TYR   B 2 121 ? -12.197 2.887   -26.589 1.00 68.28  ? 130 TYR   B CE2 1 
ATOM   1283 C CZ  . TYR   B 2 121 ? -12.632 3.811   -27.517 1.00 69.31  ? 130 TYR   B CZ  1 
ATOM   1284 O OH  . TYR   B 2 121 ? -13.026 3.406   -28.764 1.00 71.40  ? 130 TYR   B OH  1 
ATOM   1285 N N   . PRO   B 2 122 ? -10.063 7.908   -22.696 1.00 62.72  ? 131 PRO   B N   1 
ATOM   1286 C CA  . PRO   B 2 122 ? -9.791  8.882   -21.620 1.00 61.77  ? 131 PRO   B CA  1 
ATOM   1287 C C   . PRO   B 2 122 ? -10.344 8.474   -20.245 1.00 60.37  ? 131 PRO   B C   1 
ATOM   1288 O O   . PRO   B 2 122 ? -11.263 7.672   -20.180 1.00 60.31  ? 131 PRO   B O   1 
ATOM   1289 C CB  . PRO   B 2 122 ? -10.420 10.178  -22.144 1.00 62.57  ? 131 PRO   B CB  1 
ATOM   1290 C CG  . PRO   B 2 122 ? -10.531 9.995   -23.626 1.00 63.29  ? 131 PRO   B CG  1 
ATOM   1291 C CD  . PRO   B 2 122 ? -10.756 8.538   -23.842 1.00 62.18  ? 131 PRO   B CD  1 
ATOM   1292 N N   . ALA   B 2 123 ? -9.774  8.994   -19.150 1.00 59.08  ? 132 ALA   B N   1 
ATOM   1293 C CA  . ALA   B 2 123 ? -10.222 8.635   -17.797 1.00 58.67  ? 132 ALA   B CA  1 
ATOM   1294 C C   . ALA   B 2 123 ? -11.735 8.846   -17.570 1.00 57.37  ? 132 ALA   B C   1 
ATOM   1295 O O   . ALA   B 2 123 ? -12.368 8.023   -16.915 1.00 56.64  ? 132 ALA   B O   1 
ATOM   1296 C CB  . ALA   B 2 123 ? -9.416  9.391   -16.754 1.00 58.97  ? 132 ALA   B CB  1 
ATOM   1297 N N   . GLY   B 2 124 ? -12.308 9.867   -18.219 1.00 56.13  ? 133 GLY   B N   1 
ATOM   1298 C CA  . GLY   B 2 124 ? -13.733 10.174  -18.131 1.00 54.80  ? 133 GLY   B CA  1 
ATOM   1299 C C   . GLY   B 2 124 ? -14.659 9.186   -18.813 1.00 53.21  ? 133 GLY   B C   1 
ATOM   1300 O O   . GLY   B 2 124 ? -15.879 9.365   -18.784 1.00 52.81  ? 133 GLY   B O   1 
ATOM   1301 N N   . THR   B 2 125 ? -14.088 8.170   -19.486 1.00 52.42  ? 134 THR   B N   1 
ATOM   1302 C CA  . THR   B 2 125 ? -14.825 7.071   -20.116 1.00 52.36  ? 134 THR   B CA  1 
ATOM   1303 C C   . THR   B 2 125 ? -15.148 5.970   -19.043 1.00 51.17  ? 134 THR   B C   1 
ATOM   1304 O O   . THR   B 2 125 ? -15.989 5.116   -19.294 1.00 51.26  ? 134 THR   B O   1 
ATOM   1305 C CB  . THR   B 2 125 ? -14.048 6.547   -21.369 1.00 54.90  ? 134 THR   B CB  1 
ATOM   1306 O OG1 . THR   B 2 125 ? -13.713 7.643   -22.227 1.00 56.37  ? 134 THR   B OG1 1 
ATOM   1307 C CG2 . THR   B 2 125 ? -14.823 5.515   -22.191 1.00 55.14  ? 134 THR   B CG2 1 
ATOM   1308 N N   . SER   B 2 126 ? -14.494 6.001   -17.849 1.00 50.15  ? 135 SER   B N   1 
ATOM   1309 C CA  . SER   B 2 126 ? -14.698 5.058   -16.737 1.00 49.80  ? 135 SER   B CA  1 
ATOM   1310 C C   . SER   B 2 126 ? -16.167 4.850   -16.360 1.00 49.26  ? 135 SER   B C   1 
ATOM   1311 O O   . SER   B 2 126 ? -16.858 5.802   -16.053 1.00 49.57  ? 135 SER   B O   1 
ATOM   1312 C CB  . SER   B 2 126 ? -13.948 5.535   -15.505 1.00 50.46  ? 135 SER   B CB  1 
ATOM   1313 O OG  . SER   B 2 126 ? -12.568 5.244   -15.611 1.00 52.58  ? 135 SER   B OG  1 
ATOM   1314 N N   . GLY   B 2 127 ? -16.609 3.604   -16.357 1.00 48.14  ? 136 GLY   B N   1 
ATOM   1315 C CA  . GLY   B 2 127 ? -17.986 3.234   -16.073 1.00 48.03  ? 136 GLY   B CA  1 
ATOM   1316 C C   . GLY   B 2 127 ? -18.768 2.813   -17.305 1.00 48.46  ? 136 GLY   B C   1 
ATOM   1317 O O   . GLY   B 2 127 ? -19.928 2.416   -17.186 1.00 48.96  ? 136 GLY   B O   1 
ATOM   1318 N N   . SER   B 2 128 ? -18.166 2.933   -18.510 1.00 48.05  ? 137 SER   B N   1 
ATOM   1319 C CA  . SER   B 2 128 ? -18.802 2.530   -19.766 1.00 48.46  ? 137 SER   B CA  1 
ATOM   1320 C C   . SER   B 2 128 ? -19.024 1.005   -19.717 1.00 48.49  ? 137 SER   B C   1 
ATOM   1321 O O   . SER   B 2 128 ? -18.154 0.257   -19.281 1.00 48.80  ? 137 SER   B O   1 
ATOM   1322 C CB  . SER   B 2 128 ? -17.933 2.917   -20.968 1.00 49.51  ? 137 SER   B CB  1 
ATOM   1323 O OG  . SER   B 2 128 ? -17.938 4.315   -21.219 1.00 50.68  ? 137 SER   B OG  1 
ATOM   1324 N N   . PRO   B 2 129 ? -20.227 0.549   -20.076 1.00 47.89  ? 138 PRO   B N   1 
ATOM   1325 C CA  . PRO   B 2 129 ? -20.521 -0.891  -20.006 1.00 47.75  ? 138 PRO   B CA  1 
ATOM   1326 C C   . PRO   B 2 129 ? -19.916 -1.768  -21.103 1.00 48.20  ? 138 PRO   B C   1 
ATOM   1327 O O   . PRO   B 2 129 ? -19.787 -1.384  -22.290 1.00 48.06  ? 138 PRO   B O   1 
ATOM   1328 C CB  . PRO   B 2 129 ? -22.048 -0.931  -20.080 1.00 48.20  ? 138 PRO   B CB  1 
ATOM   1329 C CG  . PRO   B 2 129 ? -22.394 0.272   -20.938 1.00 48.61  ? 138 PRO   B CG  1 
ATOM   1330 C CD  . PRO   B 2 129 ? -21.392 1.329   -20.544 1.00 46.78  ? 138 PRO   B CD  1 
ATOM   1331 N N   . ILE   B 2 130 ? -19.621 -3.001  -20.712 1.00 48.12  ? 139 ILE   B N   1 
ATOM   1332 C CA  . ILE   B 2 130 ? -19.118 -4.036  -21.619 1.00 49.40  ? 139 ILE   B CA  1 
ATOM   1333 C C   . ILE   B 2 130 ? -20.259 -5.041  -21.768 1.00 51.06  ? 139 ILE   B C   1 
ATOM   1334 O O   . ILE   B 2 130 ? -20.862 -5.430  -20.764 1.00 50.49  ? 139 ILE   B O   1 
ATOM   1335 C CB  . ILE   B 2 130 ? -17.841 -4.667  -21.069 1.00 49.42  ? 139 ILE   B CB  1 
ATOM   1336 C CG1 . ILE   B 2 130 ? -16.754 -3.601  -20.927 1.00 50.30  ? 139 ILE   B CG1 1 
ATOM   1337 C CG2 . ILE   B 2 130 ? -17.383 -5.854  -21.935 1.00 49.37  ? 139 ILE   B CG2 1 
ATOM   1338 C CD1 . ILE   B 2 130 ? -15.904 -3.842  -19.739 1.00 51.96  ? 139 ILE   B CD1 1 
ATOM   1339 N N   . LEU   B 2 131 ? -20.620 -5.385  -23.018 1.00 52.39  ? 140 LEU   B N   1 
ATOM   1340 C CA  . LEU   B 2 131 ? -21.793 -6.211  -23.259 1.00 54.46  ? 140 LEU   B CA  1 
ATOM   1341 C C   . LEU   B 2 131 ? -21.552 -7.478  -24.020 1.00 55.51  ? 140 LEU   B C   1 
ATOM   1342 O O   . LEU   B 2 131 ? -20.613 -7.559  -24.790 1.00 56.37  ? 140 LEU   B O   1 
ATOM   1343 C CB  . LEU   B 2 131 ? -22.934 -5.422  -23.974 1.00 55.42  ? 140 LEU   B CB  1 
ATOM   1344 C CG  . LEU   B 2 131 ? -22.662 -4.019  -24.501 1.00 57.21  ? 140 LEU   B CG  1 
ATOM   1345 C CD1 . LEU   B 2 131 ? -23.553 -3.704  -25.667 1.00 56.62  ? 140 LEU   B CD1 1 
ATOM   1346 C CD2 . LEU   B 2 131 ? -22.826 -3.000  -23.386 1.00 58.17  ? 140 LEU   B CD2 1 
ATOM   1347 N N   . ASP   B 2 132 ? -22.451 -8.457  -23.842 1.00 55.90  ? 141 ASP   B N   1 
ATOM   1348 C CA  . ASP   B 2 132 ? -22.411 -9.708  -24.582 1.00 56.95  ? 141 ASP   B CA  1 
ATOM   1349 C C   . ASP   B 2 132 ? -23.311 -9.640  -25.854 1.00 59.02  ? 141 ASP   B C   1 
ATOM   1350 O O   . ASP   B 2 132 ? -24.006 -8.631  -26.070 1.00 59.41  ? 141 ASP   B O   1 
ATOM   1351 C CB  . ASP   B 2 132 ? -22.727 -10.909 -23.670 1.00 56.96  ? 141 ASP   B CB  1 
ATOM   1352 C CG  . ASP   B 2 132 ? -24.094 -10.951 -23.032 1.00 59.75  ? 141 ASP   B CG  1 
ATOM   1353 O OD1 . ASP   B 2 132 ? -25.038 -10.391 -23.605 1.00 59.42  ? 141 ASP   B OD1 1 
ATOM   1354 O OD2 . ASP   B 2 132 ? -24.217 -11.554 -21.960 1.00 63.46  ? 141 ASP   B OD2 1 
ATOM   1355 N N   . LYS   B 2 133 ? -23.333 -10.701 -26.670 1.00 60.21  ? 142 LYS   B N   1 
ATOM   1356 C CA  . LYS   B 2 133 ? -24.109 -10.707 -27.918 1.00 62.52  ? 142 LYS   B CA  1 
ATOM   1357 C C   . LYS   B 2 133 ? -25.619 -10.470 -27.708 1.00 63.19  ? 142 LYS   B C   1 
ATOM   1358 O O   . LYS   B 2 133 ? -26.300 -10.014 -28.635 1.00 62.59  ? 142 LYS   B O   1 
ATOM   1359 C CB  . LYS   B 2 133 ? -23.841 -11.983 -28.733 1.00 66.83  ? 142 LYS   B CB  1 
ATOM   1360 C CG  . LYS   B 2 133 ? -22.517 -11.955 -29.507 1.00 73.57  ? 142 LYS   B CG  1 
ATOM   1361 C CD  . LYS   B 2 133 ? -21.634 -13.201 -29.262 1.00 79.62  ? 142 LYS   B CD  1 
ATOM   1362 C CE  . LYS   B 2 133 ? -20.569 -13.349 -30.338 1.00 84.22  ? 142 LYS   B CE  1 
ATOM   1363 N NZ  . LYS   B 2 133 ? -19.816 -14.638 -30.237 1.00 86.99  ? 142 LYS   B NZ  1 
ATOM   1364 N N   . CYS   B 2 134 ? -26.124 -10.708 -26.476 1.00 63.55  ? 143 CYS   B N   1 
ATOM   1365 C CA  . CYS   B 2 134 ? -27.536 -10.460 -26.151 1.00 64.33  ? 143 CYS   B CA  1 
ATOM   1366 C C   . CYS   B 2 134 ? -27.838 -9.039  -25.669 1.00 63.13  ? 143 CYS   B C   1 
ATOM   1367 O O   . CYS   B 2 134 ? -28.996 -8.729  -25.389 1.00 63.55  ? 143 CYS   B O   1 
ATOM   1368 C CB  . CYS   B 2 134 ? -28.049 -11.486 -25.150 1.00 66.77  ? 143 CYS   B CB  1 
ATOM   1369 S SG  . CYS   B 2 134 ? -27.927 -13.195 -25.729 1.00 74.94  ? 143 CYS   B SG  1 
ATOM   1370 N N   . GLY   B 2 135 ? -26.820 -8.194  -25.581 1.00 61.69  ? 144 GLY   B N   1 
ATOM   1371 C CA  . GLY   B 2 135 ? -26.969 -6.838  -25.074 1.00 60.72  ? 144 GLY   B CA  1 
ATOM   1372 C C   . GLY   B 2 135 ? -26.905 -6.746  -23.559 1.00 59.19  ? 144 GLY   B C   1 
ATOM   1373 O O   . GLY   B 2 135 ? -27.147 -5.674  -23.007 1.00 59.68  ? 144 GLY   B O   1 
ATOM   1374 N N   . ARG   B 2 136 ? -26.600 -7.851  -22.863 1.00 57.62  ? 145 ARG   B N   1 
ATOM   1375 C CA  . ARG   B 2 136 ? -26.512 -7.850  -21.394 1.00 57.10  ? 145 ARG   B CA  1 
ATOM   1376 C C   . ARG   B 2 136 ? -25.191 -7.260  -20.903 1.00 55.30  ? 145 ARG   B C   1 
ATOM   1377 O O   . ARG   B 2 136 ? -24.155 -7.520  -21.503 1.00 55.58  ? 145 ARG   B O   1 
ATOM   1378 C CB  . ARG   B 2 136 ? -26.711 -9.268  -20.838 1.00 58.57  ? 145 ARG   B CB  1 
ATOM   1379 C CG  . ARG   B 2 136 ? -28.138 -9.756  -21.014 1.00 62.27  ? 145 ARG   B CG  1 
ATOM   1380 C CD  . ARG   B 2 136 ? -28.275 -11.174 -20.552 1.00 67.28  ? 145 ARG   B CD  1 
ATOM   1381 N NE  . ARG   B 2 136 ? -27.534 -12.076 -21.426 1.00 72.82  ? 145 ARG   B NE  1 
ATOM   1382 C CZ  . ARG   B 2 136 ? -26.997 -13.230 -21.043 1.00 76.98  ? 145 ARG   B CZ  1 
ATOM   1383 N NH1 . ARG   B 2 136 ? -27.090 -13.629 -19.776 1.00 76.68  ? 145 ARG   B NH1 1 
ATOM   1384 N NH2 . ARG   B 2 136 ? -26.344 -13.985 -21.918 1.00 78.22  ? 145 ARG   B NH2 1 
ATOM   1385 N N   . VAL   B 2 137 ? -25.225 -6.458  -19.833 1.00 53.63  ? 146 VAL   B N   1 
ATOM   1386 C CA  . VAL   B 2 137 ? -24.018 -5.843  -19.299 1.00 52.63  ? 146 VAL   B CA  1 
ATOM   1387 C C   . VAL   B 2 137 ? -23.281 -6.871  -18.458 1.00 52.25  ? 146 VAL   B C   1 
ATOM   1388 O O   . VAL   B 2 137 ? -23.789 -7.307  -17.436 1.00 52.80  ? 146 VAL   B O   1 
ATOM   1389 C CB  . VAL   B 2 137 ? -24.334 -4.569  -18.472 1.00 53.34  ? 146 VAL   B CB  1 
ATOM   1390 C CG1 . VAL   B 2 137 ? -23.051 -3.902  -17.982 1.00 53.94  ? 146 VAL   B CG1 1 
ATOM   1391 C CG2 . VAL   B 2 137 ? -25.203 -3.584  -19.255 1.00 53.32  ? 146 VAL   B CG2 1 
ATOM   1392 N N   . ILE   B 2 138 ? -22.114 -7.297  -18.921 1.00 51.41  ? 147 ILE   B N   1 
ATOM   1393 C CA  . ILE   B 2 138 ? -21.264 -8.258  -18.244 1.00 50.52  ? 147 ILE   B CA  1 
ATOM   1394 C C   . ILE   B 2 138 ? -20.199 -7.589  -17.348 1.00 49.47  ? 147 ILE   B C   1 
ATOM   1395 O O   . ILE   B 2 138 ? -19.449 -8.293  -16.664 1.00 49.82  ? 147 ILE   B O   1 
ATOM   1396 C CB  . ILE   B 2 138 ? -20.611 -9.226  -19.279 1.00 50.82  ? 147 ILE   B CB  1 
ATOM   1397 C CG1 . ILE   B 2 138 ? -19.737 -8.462  -20.274 1.00 51.80  ? 147 ILE   B CG1 1 
ATOM   1398 C CG2 . ILE   B 2 138 ? -21.662 -10.059 -19.991 1.00 50.99  ? 147 ILE   B CG2 1 
ATOM   1399 C CD1 . ILE   B 2 138 ? -18.865 -9.335  -21.117 1.00 53.54  ? 147 ILE   B CD1 1 
ATOM   1400 N N   . GLY   B 2 139 ? -20.151 -6.261  -17.325 1.00 47.71  ? 148 GLY   B N   1 
ATOM   1401 C CA  . GLY   B 2 139 ? -19.195 -5.544  -16.497 1.00 47.22  ? 148 GLY   B CA  1 
ATOM   1402 C C   . GLY   B 2 139 ? -19.009 -4.100  -16.915 1.00 46.97  ? 148 GLY   B C   1 
ATOM   1403 O O   . GLY   B 2 139 ? -19.559 -3.669  -17.927 1.00 46.39  ? 148 GLY   B O   1 
ATOM   1404 N N   . LEU   B 2 140 ? -18.254 -3.328  -16.119 1.00 47.04  ? 149 LEU   B N   1 
ATOM   1405 C CA  . LEU   B 2 140 ? -17.943 -1.929  -16.416 1.00 47.24  ? 149 LEU   B CA  1 
ATOM   1406 C C   . LEU   B 2 140 ? -16.422 -1.775  -16.617 1.00 48.17  ? 149 LEU   B C   1 
ATOM   1407 O O   . LEU   B 2 140 ? -15.611 -2.453  -15.956 1.00 47.90  ? 149 LEU   B O   1 
ATOM   1408 C CB  . LEU   B 2 140 ? -18.407 -0.975  -15.302 1.00 46.81  ? 149 LEU   B CB  1 
ATOM   1409 C CG  . LEU   B 2 140 ? -19.873 -1.015  -14.864 1.00 47.79  ? 149 LEU   B CG  1 
ATOM   1410 C CD1 . LEU   B 2 140 ? -20.143 0.038   -13.745 1.00 48.20  ? 149 LEU   B CD1 1 
ATOM   1411 C CD2 . LEU   B 2 140 ? -20.817 -0.826  -16.028 1.00 47.81  ? 149 LEU   B CD2 1 
ATOM   1412 N N   . TYR   B 2 141 ? -16.062 -0.852  -17.525 1.00 48.49  ? 150 TYR   B N   1 
ATOM   1413 C CA  . TYR   B 2 141 ? -14.719 -0.488  -17.973 1.00 48.94  ? 150 TYR   B CA  1 
ATOM   1414 C C   . TYR   B 2 141 ? -14.198 0.689   -17.174 1.00 49.96  ? 150 TYR   B C   1 
ATOM   1415 O O   . TYR   B 2 141 ? -14.953 1.626   -16.959 1.00 51.00  ? 150 TYR   B O   1 
ATOM   1416 C CB  . TYR   B 2 141 ? -14.829 -0.058  -19.458 1.00 48.96  ? 150 TYR   B CB  1 
ATOM   1417 C CG  . TYR   B 2 141 ? -13.574 0.569   -20.045 1.00 49.41  ? 150 TYR   B CG  1 
ATOM   1418 C CD1 . TYR   B 2 141 ? -13.393 1.948   -20.044 1.00 50.36  ? 150 TYR   B CD1 1 
ATOM   1419 C CD2 . TYR   B 2 141 ? -12.576 -0.218  -20.607 1.00 49.82  ? 150 TYR   B CD2 1 
ATOM   1420 C CE1 . TYR   B 2 141 ? -12.244 2.528   -20.578 1.00 51.81  ? 150 TYR   B CE1 1 
ATOM   1421 C CE2 . TYR   B 2 141 ? -11.445 0.352   -21.186 1.00 50.96  ? 150 TYR   B CE2 1 
ATOM   1422 C CZ  . TYR   B 2 141 ? -11.282 1.728   -21.174 1.00 52.22  ? 150 TYR   B CZ  1 
ATOM   1423 O OH  . TYR   B 2 141 ? -10.139 2.302   -21.698 1.00 52.79  ? 150 TYR   B OH  1 
ATOM   1424 N N   . GLY   B 2 142 ? -12.913 0.704   -16.843 1.00 49.89  ? 151 GLY   B N   1 
ATOM   1425 C CA  . GLY   B 2 142 ? -12.345 1.839   -16.130 1.00 50.86  ? 151 GLY   B CA  1 
ATOM   1426 C C   . GLY   B 2 142 ? -11.453 1.561   -14.940 1.00 51.79  ? 151 GLY   B C   1 
ATOM   1427 O O   . GLY   B 2 142 ? -10.944 2.517   -14.344 1.00 52.90  ? 151 GLY   B O   1 
ATOM   1428 N N   . ASN   B 2 143 ? -11.240 0.281   -14.564 1.00 50.90  ? 152 ASN   B N   1 
ATOM   1429 C CA  . ASN   B 2 143 ? -10.275 -0.030  -13.503 1.00 50.90  ? 152 ASN   B CA  1 
ATOM   1430 C C   . ASN   B 2 143 ? -9.298  -1.061  -14.028 1.00 52.06  ? 152 ASN   B C   1 
ATOM   1431 O O   . ASN   B 2 143 ? -9.692  -2.197  -14.292 1.00 51.71  ? 152 ASN   B O   1 
ATOM   1432 C CB  . ASN   B 2 143 ? -10.918 -0.506  -12.192 1.00 50.37  ? 152 ASN   B CB  1 
ATOM   1433 C CG  . ASN   B 2 143 ? -9.924  -0.592  -11.043 1.00 51.29  ? 152 ASN   B CG  1 
ATOM   1434 O OD1 . ASN   B 2 143 ? -8.837  0.014   -11.062 1.00 51.46  ? 152 ASN   B OD1 1 
ATOM   1435 N ND2 . ASN   B 2 143 ? -10.268 -1.355  -10.012 1.00 50.52  ? 152 ASN   B ND2 1 
ATOM   1436 N N   . GLY   B 2 144 ? -8.045  -0.659  -14.187 1.00 53.43  ? 153 GLY   B N   1 
ATOM   1437 C CA  . GLY   B 2 144 ? -7.048  -1.573  -14.712 1.00 56.40  ? 153 GLY   B CA  1 
ATOM   1438 C C   . GLY   B 2 144 ? -5.602  -1.232  -14.461 1.00 59.38  ? 153 GLY   B C   1 
ATOM   1439 O O   . GLY   B 2 144 ? -5.229  -0.740  -13.393 1.00 59.57  ? 153 GLY   B O   1 
ATOM   1440 N N   . VAL   B 2 145 ? -4.774  -1.505  -15.459 1.00 61.48  ? 154 VAL   B N   1 
ATOM   1441 C CA  . VAL   B 2 145 ? -3.336  -1.361  -15.315 1.00 63.83  ? 154 VAL   B CA  1 
ATOM   1442 C C   . VAL   B 2 145 ? -2.643  -0.825  -16.584 1.00 66.48  ? 154 VAL   B C   1 
ATOM   1443 O O   . VAL   B 2 145 ? -3.240  -0.771  -17.667 1.00 66.05  ? 154 VAL   B O   1 
ATOM   1444 C CB  . VAL   B 2 145 ? -2.787  -2.741  -14.859 1.00 64.34  ? 154 VAL   B CB  1 
ATOM   1445 C CG1 . VAL   B 2 145 ? -2.567  -3.680  -16.038 1.00 64.46  ? 154 VAL   B CG1 1 
ATOM   1446 C CG2 . VAL   B 2 145 ? -1.535  -2.599  -14.010 1.00 65.23  ? 154 VAL   B CG2 1 
ATOM   1447 N N   . VAL   B 2 146 ? -1.398  -0.372  -16.413 1.00 68.79  ? 155 VAL   B N   1 
ATOM   1448 C CA  . VAL   B 2 146 ? -0.550  0.130   -17.477 1.00 71.66  ? 155 VAL   B CA  1 
ATOM   1449 C C   . VAL   B 2 146 ? 0.433   -0.985  -17.761 1.00 74.36  ? 155 VAL   B C   1 
ATOM   1450 O O   . VAL   B 2 146 ? 1.182   -1.384  -16.869 1.00 74.37  ? 155 VAL   B O   1 
ATOM   1451 C CB  . VAL   B 2 146 ? 0.166   1.424   -17.064 1.00 72.67  ? 155 VAL   B CB  1 
ATOM   1452 C CG1 . VAL   B 2 146 ? 1.211   1.808   -18.103 1.00 73.64  ? 155 VAL   B CG1 1 
ATOM   1453 C CG2 . VAL   B 2 146 ? -0.844  2.549   -16.873 1.00 73.25  ? 155 VAL   B CG2 1 
ATOM   1454 N N   . ILE   B 2 147 ? 0.383   -1.541  -18.977 1.00 76.20  ? 156 ILE   B N   1 
ATOM   1455 C CA  . ILE   B 2 147 ? 1.224   -2.683  -19.311 1.00 78.41  ? 156 ILE   B CA  1 
ATOM   1456 C C   . ILE   B 2 147 ? 2.628   -2.246  -19.796 1.00 80.71  ? 156 ILE   B C   1 
ATOM   1457 O O   . ILE   B 2 147 ? 2.853   -1.053  -19.993 1.00 80.80  ? 156 ILE   B O   1 
ATOM   1458 C CB  . ILE   B 2 147 ? 0.470   -3.629  -20.286 1.00 79.06  ? 156 ILE   B CB  1 
ATOM   1459 C CG1 . ILE   B 2 147 ? 0.364   -3.042  -21.700 1.00 79.77  ? 156 ILE   B CG1 1 
ATOM   1460 C CG2 . ILE   B 2 147 ? -0.908  -4.003  -19.720 1.00 79.60  ? 156 ILE   B CG2 1 
ATOM   1461 C CD1 . ILE   B 2 147 ? -0.152  -4.040  -22.701 1.00 80.73  ? 156 ILE   B CD1 1 
ATOM   1462 N N   C LYS   B 2 148 ? 3.562   -3.209  -19.950 0.50 81.47  ? 157 LYS   B N   1 
ATOM   1463 N N   D LYS   B 2 148 ? 3.562   -3.209  -19.950 0.50 81.47  ? 157 LYS   B N   1 
ATOM   1464 C CA  C LYS   B 2 148 ? 4.952   -2.997  -20.382 0.50 82.79  ? 157 LYS   B CA  1 
ATOM   1465 C CA  D LYS   B 2 148 ? 4.952   -2.997  -20.382 0.50 82.79  ? 157 LYS   B CA  1 
ATOM   1466 C C   C LYS   B 2 148 ? 5.100   -2.140  -21.650 0.50 83.54  ? 157 LYS   B C   1 
ATOM   1467 C C   D LYS   B 2 148 ? 5.100   -2.140  -21.650 0.50 83.54  ? 157 LYS   B C   1 
ATOM   1468 O O   C LYS   B 2 148 ? 6.180   -1.611  -21.907 0.50 83.85  ? 157 LYS   B O   1 
ATOM   1469 O O   D LYS   B 2 148 ? 6.180   -1.611  -21.907 0.50 83.85  ? 157 LYS   B O   1 
ATOM   1470 C CB  C LYS   B 2 148 ? 5.718   -4.333  -20.550 0.50 85.26  ? 157 LYS   B CB  1 
ATOM   1471 C CB  D LYS   B 2 148 ? 5.718   -4.333  -20.550 0.50 85.26  ? 157 LYS   B CB  1 
ATOM   1472 C CG  C LYS   B 2 148 ? 5.020   -5.592  -20.012 0.50 90.18  ? 157 LYS   B CG  1 
ATOM   1473 C CG  D LYS   B 2 148 ? 5.020   -5.592  -20.012 0.50 90.18  ? 157 LYS   B CG  1 
ATOM   1474 C CD  C LYS   B 2 148 ? 4.167   -6.286  -21.083 0.50 94.94  ? 157 LYS   B CD  1 
ATOM   1475 C CD  D LYS   B 2 148 ? 4.167   -6.286  -21.083 0.50 94.94  ? 157 LYS   B CD  1 
ATOM   1476 C CE  C LYS   B 2 148 ? 5.004   -6.835  -22.214 0.50 98.75  ? 157 LYS   B CE  1 
ATOM   1477 C CE  D LYS   B 2 148 ? 5.004   -6.835  -22.214 0.50 98.75  ? 157 LYS   B CE  1 
ATOM   1478 N NZ  C LYS   B 2 148 ? 5.980   -7.847  -21.729 0.50 100.99 ? 157 LYS   B NZ  1 
ATOM   1479 N NZ  D LYS   B 2 148 ? 5.980   -7.847  -21.729 0.50 100.99 ? 157 LYS   B NZ  1 
ATOM   1480 N N   . ASN   B 2 149 ? 4.024   -2.004  -22.436 1.00 83.58  ? 158 ASN   B N   1 
ATOM   1481 C CA  . ASN   B 2 149 ? 4.012   -1.193  -23.656 1.00 83.85  ? 158 ASN   B CA  1 
ATOM   1482 C C   . ASN   B 2 149 ? 3.630   0.286   -23.408 1.00 82.63  ? 158 ASN   B C   1 
ATOM   1483 O O   . ASN   B 2 149 ? 3.814   1.124   -24.286 1.00 83.23  ? 158 ASN   B O   1 
ATOM   1484 C CB  . ASN   B 2 149 ? 2.966   -1.756  -24.630 1.00 86.79  ? 158 ASN   B CB  1 
ATOM   1485 C CG  . ASN   B 2 149 ? 3.160   -3.199  -25.009 1.00 93.00  ? 158 ASN   B CG  1 
ATOM   1486 O OD1 . ASN   B 2 149 ? 4.274   -3.744  -24.953 1.00 95.96  ? 158 ASN   B OD1 1 
ATOM   1487 N ND2 . ASN   B 2 149 ? 2.079   -3.845  -25.435 1.00 93.81  ? 158 ASN   B ND2 1 
ATOM   1488 N N   . GLY   B 2 150 ? 3.018   0.573   -22.272 1.00 80.99  ? 159 GLY   B N   1 
ATOM   1489 C CA  . GLY   B 2 150 ? 2.486   1.897   -21.968 1.00 79.56  ? 159 GLY   B CA  1 
ATOM   1490 C C   . GLY   B 2 150 ? 0.980   2.022   -22.186 1.00 77.40  ? 159 GLY   B C   1 
ATOM   1491 O O   . GLY   B 2 150 ? 0.361   2.979   -21.693 1.00 77.98  ? 159 GLY   B O   1 
ATOM   1492 N N   A SER   B 2 151 ? 0.379   1.069   -22.916 0.09 76.59  ? 160 SER   B N   1 
ATOM   1493 N N   B SER   B 2 151 ? 0.379   1.079   -22.927 0.07 76.62  ? 160 SER   B N   1 
ATOM   1494 N N   C SER   B 2 151 ? 0.377   1.063   -22.918 0.42 76.66  ? 160 SER   B N   1 
ATOM   1495 N N   D SER   B 2 151 ? 0.379   1.068   -22.920 0.42 76.78  ? 160 SER   B N   1 
ATOM   1496 C CA  A SER   B 2 151 ? -1.055  1.071   -23.197 0.09 76.30  ? 160 SER   B CA  1 
ATOM   1497 C CA  B SER   B 2 151 ? -1.056  1.101   -23.199 0.07 76.34  ? 160 SER   B CA  1 
ATOM   1498 C CA  C SER   B 2 151 ? -1.061  1.072   -23.190 0.42 76.42  ? 160 SER   B CA  1 
ATOM   1499 C CA  D SER   B 2 151 ? -1.056  1.088   -23.192 0.42 76.65  ? 160 SER   B CA  1 
ATOM   1500 C C   A SER   B 2 151 ? -1.887  0.663   -21.976 0.09 75.63  ? 160 SER   B C   1 
ATOM   1501 C C   B SER   B 2 151 ? -1.887  0.663   -21.987 0.07 75.65  ? 160 SER   B C   1 
ATOM   1502 C C   C SER   B 2 151 ? -1.884  0.676   -21.961 0.42 75.76  ? 160 SER   B C   1 
ATOM   1503 C C   D SER   B 2 151 ? -1.885  0.670   -21.971 0.42 75.82  ? 160 SER   B C   1 
ATOM   1504 O O   A SER   B 2 151 ? -1.384  -0.005  -21.072 0.09 75.74  ? 160 SER   B O   1 
ATOM   1505 O O   B SER   B 2 151 ? -1.381  -0.018  -21.095 0.07 75.76  ? 160 SER   B O   1 
ATOM   1506 O O   C SER   B 2 151 ? -1.376  0.032   -21.041 0.42 75.89  ? 160 SER   B O   1 
ATOM   1507 O O   D SER   B 2 151 ? -1.377  0.013   -21.059 0.42 75.95  ? 160 SER   B O   1 
ATOM   1508 C CB  A SER   B 2 151 ? -1.369  0.158   -24.380 0.09 77.60  ? 160 SER   B CB  1 
ATOM   1509 C CB  B SER   B 2 151 ? -1.384  0.248   -24.421 0.07 77.70  ? 160 SER   B CB  1 
ATOM   1510 C CB  C SER   B 2 151 ? -1.398  0.163   -24.372 0.42 77.73  ? 160 SER   B CB  1 
ATOM   1511 C CB  D SER   B 2 151 ? -1.388  0.211   -24.397 0.42 78.24  ? 160 SER   B CB  1 
ATOM   1512 O OG  A SER   B 2 151 ? -2.759  0.147   -24.665 0.09 79.74  ? 160 SER   B OG  1 
ATOM   1513 O OG  B SER   B 2 151 ? -0.856  -1.062  -24.291 0.07 79.94  ? 160 SER   B OG  1 
ATOM   1514 O OG  C SER   B 2 151 ? -2.795  0.141   -24.624 0.42 79.58  ? 160 SER   B OG  1 
ATOM   1515 O OG  D SER   B 2 151 ? -1.005  -1.135  -24.172 0.42 80.56  ? 160 SER   B OG  1 
ATOM   1516 N N   . TYR   B 2 152 ? -3.160  1.065   -21.953 1.00 74.80  ? 161 TYR   B N   1 
ATOM   1517 C CA  . TYR   B 2 152 ? -4.052  0.754   -20.854 1.00 71.58  ? 161 TYR   B CA  1 
ATOM   1518 C C   . TYR   B 2 152 ? -4.905  -0.513  -21.060 1.00 68.83  ? 161 TYR   B C   1 
ATOM   1519 O O   . TYR   B 2 152 ? -5.581  -0.643  -22.070 1.00 68.92  ? 161 TYR   B O   1 
ATOM   1520 C CB  . TYR   B 2 152 ? -4.947  1.976   -20.628 1.00 70.67  ? 161 TYR   B CB  1 
ATOM   1521 C CG  . TYR   B 2 152 ? -5.942  1.806   -19.512 1.00 70.24  ? 161 TYR   B CG  1 
ATOM   1522 C CD1 . TYR   B 2 152 ? -5.527  1.749   -18.190 1.00 70.39  ? 161 TYR   B CD1 1 
ATOM   1523 C CD2 . TYR   B 2 152 ? -7.303  1.738   -19.774 1.00 70.51  ? 161 TYR   B CD2 1 
ATOM   1524 C CE1 . TYR   B 2 152 ? -6.438  1.594   -17.159 1.00 70.91  ? 161 TYR   B CE1 1 
ATOM   1525 C CE2 . TYR   B 2 152 ? -8.223  1.594   -18.753 1.00 70.93  ? 161 TYR   B CE2 1 
ATOM   1526 C CZ  . TYR   B 2 152 ? -7.785  1.510   -17.446 1.00 71.71  ? 161 TYR   B CZ  1 
ATOM   1527 O OH  . TYR   B 2 152 ? -8.691  1.361   -16.436 1.00 72.96  ? 161 TYR   B OH  1 
ATOM   1528 N N   . VAL   B 2 153 ? -4.908  -1.420  -20.071 1.00 66.22  ? 162 VAL   B N   1 
ATOM   1529 C CA  . VAL   B 2 153 ? -5.742  -2.624  -20.084 1.00 63.73  ? 162 VAL   B CA  1 
ATOM   1530 C C   . VAL   B 2 153 ? -6.691  -2.584  -18.848 1.00 60.70  ? 162 VAL   B C   1 
ATOM   1531 O O   . VAL   B 2 153 ? -6.234  -2.549  -17.706 1.00 60.16  ? 162 VAL   B O   1 
ATOM   1532 C CB  . VAL   B 2 153 ? -4.900  -3.927  -20.183 1.00 64.34  ? 162 VAL   B CB  1 
ATOM   1533 C CG1 . VAL   B 2 153 ? -5.766  -5.172  -20.001 1.00 64.34  ? 162 VAL   B CG1 1 
ATOM   1534 C CG2 . VAL   B 2 153 ? -4.152  -3.986  -21.513 1.00 65.18  ? 162 VAL   B CG2 1 
ATOM   1535 N N   . SER   B 2 154 ? -8.005  -2.510  -19.087 1.00 58.44  ? 163 SER   B N   1 
ATOM   1536 C CA  . SER   B 2 154 ? -9.000  -2.442  -18.020 1.00 56.64  ? 163 SER   B CA  1 
ATOM   1537 C C   . SER   B 2 154 ? -9.580  -3.808  -17.715 1.00 54.94  ? 163 SER   B C   1 
ATOM   1538 O O   . SER   B 2 154 ? -9.828  -4.550  -18.631 1.00 54.52  ? 163 SER   B O   1 
ATOM   1539 C CB  . SER   B 2 154 ? -10.154 -1.534  -18.446 1.00 56.65  ? 163 SER   B CB  1 
ATOM   1540 O OG  . SER   B 2 154 ? -11.343 -1.696  -17.679 1.00 55.98  ? 163 SER   B OG  1 
ATOM   1541 N N   . ALA   B 2 155 ? -9.962  -4.066  -16.463 1.00 53.26  ? 164 ALA   B N   1 
ATOM   1542 C CA  . ALA   B 2 155 ? -10.664 -5.285  -16.100 1.00 52.17  ? 164 ALA   B CA  1 
ATOM   1543 C C   . ALA   B 2 155 ? -12.137 -5.205  -16.592 1.00 51.23  ? 164 ALA   B C   1 
ATOM   1544 O O   . ALA   B 2 155 ? -12.654 -4.124  -16.894 1.00 50.65  ? 164 ALA   B O   1 
ATOM   1545 C CB  . ALA   B 2 155 ? -10.644 -5.440  -14.578 1.00 52.29  ? 164 ALA   B CB  1 
ATOM   1546 N N   . ILE   B 2 156 ? -12.805 -6.353  -16.693 1.00 50.81  ? 165 ILE   B N   1 
ATOM   1547 C CA  . ILE   B 2 156 ? -14.241 -6.390  -16.937 1.00 50.56  ? 165 ILE   B CA  1 
ATOM   1548 C C   . ILE   B 2 156 ? -14.768 -6.543  -15.473 1.00 49.84  ? 165 ILE   B C   1 
ATOM   1549 O O   . ILE   B 2 156 ? -14.766 -7.652  -14.922 1.00 48.85  ? 165 ILE   B O   1 
ATOM   1550 C CB  . ILE   B 2 156 ? -14.678 -7.566  -17.850 1.00 50.83  ? 165 ILE   B CB  1 
ATOM   1551 C CG1 . ILE   B 2 156 ? -14.146 -7.376  -19.289 1.00 52.37  ? 165 ILE   B CG1 1 
ATOM   1552 C CG2 . ILE   B 2 156 ? -16.218 -7.683  -17.864 1.00 50.96  ? 165 ILE   B CG2 1 
ATOM   1553 C CD1 . ILE   B 2 156 ? -14.184 -8.662  -20.107 1.00 53.55  ? 165 ILE   B CD1 1 
ATOM   1554 N N   . THR   B 2 157 ? -15.054 -5.407  -14.817 1.00 49.70  ? 166 THR   B N   1 
ATOM   1555 C CA  . THR   B 2 157 ? -15.491 -5.359  -13.409 1.00 49.92  ? 166 THR   B CA  1 
ATOM   1556 C C   . THR   B 2 157 ? -16.993 -5.564  -13.261 1.00 49.90  ? 166 THR   B C   1 
ATOM   1557 O O   . THR   B 2 157 ? -17.765 -4.722  -13.692 1.00 49.81  ? 166 THR   B O   1 
ATOM   1558 C CB  . THR   B 2 157 ? -15.121 -4.019  -12.776 1.00 50.95  ? 166 THR   B CB  1 
ATOM   1559 O OG1 . THR   B 2 157 ? -13.732 -3.762  -12.964 1.00 52.52  ? 166 THR   B OG1 1 
ATOM   1560 C CG2 . THR   B 2 157 ? -15.463 -3.963  -11.314 1.00 50.51  ? 166 THR   B CG2 1 
ATOM   1561 N N   . GLN   B 2 158 ? -17.401 -6.672  -12.655 1.00 49.91  ? 167 GLN   B N   1 
ATOM   1562 C CA  . GLN   B 2 158 ? -18.814 -6.960  -12.446 1.00 50.69  ? 167 GLN   B CA  1 
ATOM   1563 C C   . GLN   B 2 158 ? -19.116 -7.074  -10.938 1.00 53.05  ? 167 GLN   B C   1 
ATOM   1564 O O   . GLN   B 2 158 ? -18.262 -7.496  -10.154 1.00 51.80  ? 167 GLN   B O   1 
ATOM   1565 C CB  . GLN   B 2 158 ? -19.213 -8.257  -13.191 1.00 49.84  ? 167 GLN   B CB  1 
ATOM   1566 C CG  . GLN   B 2 158 ? -20.702 -8.619  -13.142 1.00 49.79  ? 167 GLN   B CG  1 
ATOM   1567 C CD  . GLN   B 2 158 ? -21.622 -7.555  -13.722 1.00 50.25  ? 167 GLN   B CD  1 
ATOM   1568 O OE1 . GLN   B 2 158 ? -21.809 -6.465  -13.152 1.00 51.94  ? 167 GLN   B OE1 1 
ATOM   1569 N NE2 . GLN   B 2 158 ? -22.280 -7.864  -14.823 1.00 46.51  ? 167 GLN   B NE2 1 
ATOM   1570 N N   . GLY   B 2 159 ? -20.314 -6.676  -10.552 1.00 55.99  ? 168 GLY   B N   1 
ATOM   1571 C CA  . GLY   B 2 159 ? -20.752 -6.810  -9.179  1.00 60.07  ? 168 GLY   B CA  1 
ATOM   1572 C C   . GLY   B 2 159 ? -21.401 -8.163  -8.950  1.00 64.77  ? 168 GLY   B C   1 
ATOM   1573 O O   . GLY   B 2 159 ? -21.270 -9.098  -9.751  1.00 64.71  ? 168 GLY   B O   1 
ATOM   1574 N N   . LYS   B 2 160 ? -22.112 -8.268  -7.840  1.00 68.45  ? 169 LYS   B N   1 
ATOM   1575 C CA  . LYS   B 2 160 ? -22.842 -9.469  -7.469  1.00 72.23  ? 169 LYS   B CA  1 
ATOM   1576 C C   . LYS   B 2 160 ? -24.304 -9.043  -7.260  1.00 75.43  ? 169 LYS   B C   1 
ATOM   1577 O O   . LYS   B 2 160 ? -24.548 -8.050  -6.572  1.00 75.99  ? 169 LYS   B O   1 
ATOM   1578 C CB  . LYS   B 2 160 ? -22.250 -10.055 -6.174  1.00 75.05  ? 169 LYS   B CB  1 
ATOM   1579 C CG  . LYS   B 2 160 ? -22.962 -11.305 -5.695  1.00 80.67  ? 169 LYS   B CG  1 
ATOM   1580 C CD  . LYS   B 2 160 ? -22.597 -11.639 -4.255  1.00 85.94  ? 169 LYS   B CD  1 
ATOM   1581 C CE  . LYS   B 2 160 ? -23.174 -12.968 -3.829  1.00 90.33  ? 169 LYS   B CE  1 
ATOM   1582 N NZ  . LYS   B 2 160 ? -23.119 -13.148 -2.351  1.00 93.19  ? 169 LYS   B NZ  1 
ATOM   1583 N N   . ARG   B 2 161 ? -25.269 -9.734  -7.894  1.00 77.31  ? 170 ARG   B N   1 
ATOM   1584 C CA  . ARG   B 2 161 ? -26.683 -9.391  -7.718  1.00 79.59  ? 170 ARG   B CA  1 
ATOM   1585 C C   . ARG   B 2 161 ? -27.274 -10.225 -6.566  1.00 82.14  ? 170 ARG   B C   1 
ATOM   1586 O O   . ARG   B 2 161 ? -27.443 -11.436 -6.716  1.00 82.35  ? 170 ARG   B O   1 
ATOM   1587 C CB  . ARG   B 2 161 ? -27.475 -9.606  -9.025  1.00 80.48  ? 170 ARG   B CB  1 
ATOM   1588 C CG  . ARG   B 2 161 ? -28.927 -9.159  -8.942  1.00 82.24  ? 170 ARG   B CG  1 
ATOM   1589 C CD  . ARG   B 2 161 ? -29.756 -9.602  -10.132 1.00 84.68  ? 170 ARG   B CD  1 
ATOM   1590 N NE  . ARG   B 2 161 ? -31.155 -9.193  -9.984  1.00 87.44  ? 170 ARG   B NE  1 
ATOM   1591 C CZ  . ARG   B 2 161 ? -31.833 -8.475  -10.878 1.00 89.22  ? 170 ARG   B CZ  1 
ATOM   1592 N NH1 . ARG   B 2 161 ? -31.254 -8.092  -12.010 1.00 87.87  ? 170 ARG   B NH1 1 
ATOM   1593 N NH2 . ARG   B 2 161 ? -33.095 -8.139  -10.649 1.00 89.48  ? 170 ARG   B NH2 1 
ATOM   1594 N N   . GLU   B 2 162 ? -27.551 -9.586  -5.412  1.00 83.79  ? 171 GLU   B N   1 
ATOM   1595 C CA  . GLU   B 2 162 ? -28.116 -10.268 -4.241  1.00 86.04  ? 171 GLU   B CA  1 
ATOM   1596 C C   . GLU   B 2 162 ? -29.520 -10.831 -4.509  1.00 87.17  ? 171 GLU   B C   1 
ATOM   1597 O O   . GLU   B 2 162 ? -29.827 -11.958 -4.116  1.00 87.73  ? 171 GLU   B O   1 
ATOM   1598 C CB  . GLU   B 2 162 ? -28.166 -9.317  -3.038  1.00 89.84  ? 171 GLU   B CB  1 
ATOM   1599 C CG  . GLU   B 2 162 ? -26.841 -9.166  -2.311  1.00 97.02  ? 171 GLU   B CG  1 
ATOM   1600 C CD  . GLU   B 2 162 ? -26.501 -10.315 -1.381  1.00 105.53 ? 171 GLU   B CD  1 
ATOM   1601 O OE1 . GLU   B 2 162 ? -26.847 -10.226 -0.179  1.00 106.57 ? 171 GLU   B OE1 1 
ATOM   1602 O OE2 . GLU   B 2 162 ? -25.884 -11.302 -1.849  1.00 108.71 ? 171 GLU   B OE2 1 
HETATM 1603 S S   . DMS   C 3 .   ? -18.848 12.143  -0.206  1.00 91.12  ? 201 DMS   B S   1 
HETATM 1604 O O   . DMS   C 3 .   ? -19.618 10.938  -0.503  1.00 90.95  ? 201 DMS   B O   1 
HETATM 1605 C C1  . DMS   C 3 .   ? -19.689 13.474  -1.002  1.00 91.28  ? 201 DMS   B C1  1 
HETATM 1606 C C2  . DMS   C 3 .   ? -17.457 12.137  -1.300  1.00 91.05  ? 201 DMS   B C2  1 
HETATM 1607 N N1  . A1BXV D 4 .   ? -7.853  4.601   -14.206 1.00 72.85  ? 202 A1BXV B N1  1 
HETATM 1608 N N3  . A1BXV D 4 .   ? -5.783  5.306   -15.814 1.00 74.54  ? 202 A1BXV B N3  1 
HETATM 1609 C C4  . A1BXV D 4 .   ? -6.093  5.799   -18.560 1.00 74.62  ? 202 A1BXV B C4  1 
HETATM 1610 C C5  . A1BXV D 4 .   ? -6.266  6.106   -20.026 1.00 75.08  ? 202 A1BXV B C5  1 
HETATM 1611 C C6  . A1BXV D 4 .   ? -7.225  5.443   -17.769 1.00 74.09  ? 202 A1BXV B C6  1 
HETATM 1612 C C7  . A1BXV D 4 .   ? -8.522  5.286   -18.316 1.00 73.78  ? 202 A1BXV B C7  1 
HETATM 1613 C C8  . A1BXV D 4 .   ? -9.564  4.931   -17.517 1.00 73.81  ? 202 A1BXV B C8  1 
HETATM 1614 C C10 . A1BXV D 4 .   ? -8.135  4.831   -15.563 1.00 73.59  ? 202 A1BXV B C10 1 
HETATM 1615 C C13 . A1BXV D 4 .   ? -9.098  4.070   -11.449 1.00 71.77  ? 202 A1BXV B C13 1 
HETATM 1616 C C15 . A1BXV D 4 .   ? -8.117  4.754   -9.192  1.00 71.93  ? 202 A1BXV B C15 1 
HETATM 1617 C C17 . A1BXV D 4 .   ? -9.132  2.463   -7.917  1.00 71.36  ? 202 A1BXV B C17 1 
HETATM 1618 C C1  . A1BXV D 4 .   ? -3.416  5.767   -15.895 1.00 74.10  ? 202 A1BXV B C1  1 
HETATM 1619 C C2  . A1BXV D 4 .   ? -4.750  5.644   -16.568 1.00 74.41  ? 202 A1BXV B C2  1 
HETATM 1620 C C3  . A1BXV D 4 .   ? -4.877  5.911   -17.947 1.00 74.62  ? 202 A1BXV B C3  1 
HETATM 1621 O O1  . A1BXV D 4 .   ? -5.088  5.881   -20.797 1.00 75.66  ? 202 A1BXV B O1  1 
HETATM 1622 C C9  . A1BXV D 4 .   ? -9.375  4.701   -16.142 1.00 73.66  ? 202 A1BXV B C9  1 
HETATM 1623 C C11 . A1BXV D 4 .   ? -7.773  3.426   -13.540 1.00 72.22  ? 202 A1BXV B C11 1 
HETATM 1624 O O2  . A1BXV D 4 .   ? -7.725  2.333   -14.088 1.00 71.89  ? 202 A1BXV B O2  1 
HETATM 1625 C C12 . A1BXV D 4 .   ? -7.782  3.530   -12.033 1.00 72.07  ? 202 A1BXV B C12 1 
HETATM 1626 C C14 . A1BXV D 4 .   ? -9.240  4.029   -9.929  1.00 71.75  ? 202 A1BXV B C14 1 
HETATM 1627 C C16 . A1BXV D 4 .   ? -8.257  4.743   -7.685  1.00 71.99  ? 202 A1BXV B C16 1 
HETATM 1628 N N2  . A1BXV D 4 .   ? -9.242  3.752   -7.219  1.00 71.73  ? 202 A1BXV B N2  1 
HETATM 1629 C C18 . A1BXV D 4 .   ? -9.422  2.615   -9.382  1.00 71.51  ? 202 A1BXV B C18 1 
HETATM 1630 C C19 . A1BXV D 4 .   ? -7.018  5.195   -16.383 1.00 74.13  ? 202 A1BXV B C19 1 
HETATM 1631 O O   . HOH   E 5 .   ? -2.399  -3.468  -6.490  1.00 49.87  ? 101 HOH   A O   1 
HETATM 1632 O O   . HOH   E 5 .   ? -4.097  -14.144 -25.489 1.00 48.28  ? 102 HOH   A O   1 
HETATM 1633 O O   . HOH   E 5 .   ? -23.744 19.072  -19.651 1.00 55.89  ? 103 HOH   A O   1 
HETATM 1634 O O   . HOH   E 5 .   ? -32.367 -0.205  -28.768 1.00 75.89  ? 104 HOH   A O   1 
HETATM 1635 O O   . HOH   E 5 .   ? -26.253 2.000   -29.233 1.00 70.13  ? 105 HOH   A O   1 
HETATM 1636 O O   A HOH   E 5 .   ? -29.389 15.988  -15.255 0.50 66.53  ? 106 HOH   A O   1 
HETATM 1637 O O   B HOH   E 5 .   ? -29.389 15.988  -15.255 0.50 66.53  ? 106 HOH   A O   1 
HETATM 1638 O O   . HOH   E 5 .   ? -28.464 -6.130  -27.952 1.00 55.89  ? 107 HOH   A O   1 
HETATM 1639 O O   . HOH   E 5 .   ? -6.795  -9.053  -3.229  1.00 44.97  ? 108 HOH   A O   1 
HETATM 1640 O O   . HOH   E 5 .   ? -8.047  -1.499  6.672   1.00 63.61  ? 109 HOH   A O   1 
HETATM 1641 O O   . HOH   E 5 .   ? -24.081 9.465   -27.639 1.00 52.45  ? 110 HOH   A O   1 
HETATM 1642 O O   . HOH   E 5 .   ? -22.210 -9.204  -34.584 1.00 59.42  ? 111 HOH   A O   1 
HETATM 1643 O O   . HOH   E 5 .   ? -3.611  -3.995  0.171   1.00 71.89  ? 112 HOH   A O   1 
HETATM 1644 O O   . HOH   E 5 .   ? -31.015 0.465   -23.186 1.00 55.61  ? 113 HOH   A O   1 
HETATM 1645 O O   . HOH   E 5 .   ? -4.371  -9.974  -5.783  1.00 52.82  ? 114 HOH   A O   1 
HETATM 1646 O O   . HOH   E 5 .   ? -7.621  -19.534 -20.042 1.00 75.55  ? 115 HOH   A O   1 
HETATM 1647 O O   . HOH   E 5 .   ? -4.751  2.259   -10.161 1.00 65.02  ? 116 HOH   A O   1 
HETATM 1648 O O   . HOH   E 5 .   ? -3.684  -0.690  -0.120  1.00 57.32  ? 117 HOH   A O   1 
HETATM 1649 O O   . HOH   F 5 .   ? -6.400  -0.132  -11.104 1.00 45.95  ? 301 HOH   B O   1 
HETATM 1650 O O   . HOH   F 5 .   ? -15.434 -9.992  -15.226 1.00 56.95  ? 302 HOH   B O   1 
HETATM 1651 O O   . HOH   F 5 .   ? -34.400 0.885   -3.390  1.00 66.71  ? 303 HOH   B O   1 
HETATM 1652 O O   . HOH   F 5 .   ? -31.026 12.809  -19.302 1.00 56.24  ? 304 HOH   B O   1 
HETATM 1653 O O   . HOH   F 5 .   ? -26.255 -7.641  -16.695 1.00 39.68  ? 305 HOH   B O   1 
HETATM 1654 O O   . HOH   F 5 .   ? -16.605 21.150  -14.406 1.00 57.49  ? 306 HOH   B O   1 
HETATM 1655 O O   . HOH   F 5 .   ? -18.090 -10.535 -16.578 1.00 47.16  ? 307 HOH   B O   1 
HETATM 1656 O O   . HOH   F 5 .   ? -22.372 -13.681 -21.349 1.00 54.61  ? 308 HOH   B O   1 
HETATM 1657 O O   . HOH   F 5 .   ? -17.120 13.290  -5.648  1.00 58.53  ? 309 HOH   B O   1 
HETATM 1658 O O   . HOH   F 5 .   ? -13.067 -2.012  -14.855 1.00 41.25  ? 310 HOH   B O   1 
HETATM 1659 O O   . HOH   F 5 .   ? -9.459  -6.649  -25.616 1.00 52.16  ? 311 HOH   B O   1 
HETATM 1660 O O   . HOH   F 5 .   ? -35.385 3.567   -8.380  1.00 64.78  ? 312 HOH   B O   1 
HETATM 1661 O O   A HOH   F 5 .   ? -12.007 -17.521 -28.070 0.50 68.78  ? 313 HOH   B O   1 
HETATM 1662 O O   B HOH   F 5 .   ? -12.007 -17.521 -28.070 0.50 68.78  ? 313 HOH   B O   1 
HETATM 1663 O O   . HOH   F 5 .   ? -17.141 -15.121 -30.704 1.00 60.70  ? 314 HOH   B O   1 
HETATM 1664 O O   . HOH   F 5 .   ? -12.384 -3.151  -9.938  1.00 48.22  ? 315 HOH   B O   1 
HETATM 1665 O O   . HOH   F 5 .   ? -16.335 -14.512 -16.602 1.00 55.19  ? 316 HOH   B O   1 
HETATM 1666 O O   . HOH   F 5 .   ? -29.131 -4.003  -21.938 1.00 78.80  ? 317 HOH   B O   1 
HETATM 1667 O O   . HOH   F 5 .   ? -27.871 -6.073  -18.330 1.00 52.05  ? 318 HOH   B O   1 
HETATM 1668 O O   . HOH   F 5 .   ? -15.561 -4.854  1.440   1.00 51.80  ? 319 HOH   B O   1 
HETATM 1669 O O   A HOH   F 5 .   ? -23.710 -6.781  -4.149  0.50 76.54  ? 320 HOH   B O   1 
HETATM 1670 O O   B HOH   F 5 .   ? -23.710 -6.781  -4.149  0.50 76.54  ? 320 HOH   B O   1 
HETATM 1671 O O   . HOH   F 5 .   ? -35.522 -2.398  -16.654 1.00 73.01  ? 321 HOH   B O   1 
HETATM 1672 O O   . HOH   F 5 .   ? -19.001 15.405  -22.395 1.00 49.22  ? 322 HOH   B O   1 
HETATM 1673 O O   A HOH   F 5 .   ? -11.216 12.375  -19.250 0.50 67.38  ? 323 HOH   B O   1 
HETATM 1674 O O   B HOH   F 5 .   ? -11.216 12.375  -19.250 0.50 67.38  ? 323 HOH   B O   1 
HETATM 1675 O O   . HOH   F 5 .   ? -16.039 -6.863  -8.361  1.00 65.46  ? 324 HOH   B O   1 
HETATM 1676 O O   A HOH   F 5 .   ? -20.142 -13.675 -22.850 0.50 51.38  ? 325 HOH   B O   1 
HETATM 1677 O O   B HOH   F 5 .   ? -20.142 -13.675 -22.850 0.50 51.38  ? 325 HOH   B O   1 
HETATM 1678 O O   . HOH   F 5 .   ? -16.564 26.630  -12.677 1.00 75.60  ? 326 HOH   B O   1 
HETATM 1679 O O   A HOH   F 5 .   ? -15.518 -6.906  -1.409  0.50 56.29  ? 327 HOH   B O   1 
HETATM 1680 O O   B HOH   F 5 .   ? -15.518 -6.906  -1.409  0.50 56.29  ? 327 HOH   B O   1 
HETATM 1681 O O   A HOH   F 5 .   ? -31.162 12.845  -16.628 0.50 68.12  ? 328 HOH   B O   1 
HETATM 1682 O O   B HOH   F 5 .   ? -31.162 12.845  -16.628 0.50 68.12  ? 328 HOH   B O   1 
HETATM 1683 O O   . HOH   F 5 .   ? -32.051 7.296   -4.386  1.00 61.69  ? 329 HOH   B O   1 
HETATM 1684 O O   . HOH   F 5 .   ? -25.955 -4.397  -3.908  1.00 45.50  ? 330 HOH   B O   1 
HETATM 1685 O O   . HOH   F 5 .   ? -30.685 4.842   -2.239  1.00 58.30  ? 331 HOH   B O   1 
HETATM 1686 O O   A HOH   F 5 .   ? -21.198 7.012   0.000   0.25 65.30  ? 332 HOH   B O   1 
HETATM 1687 O O   B HOH   F 5 .   ? -21.198 7.041   0.000   0.25 59.99  ? 332 HOH   B O   1 
HETATM 1688 O O   A HOH   F 5 .   ? -6.786  -10.672 -5.466  0.50 64.97  ? 333 HOH   B O   1 
HETATM 1689 O O   B HOH   F 5 .   ? -6.786  -10.672 -5.466  0.50 64.97  ? 333 HOH   B O   1 
HETATM 1690 O O   . HOH   F 5 .   ? -18.502 18.585  -22.047 1.00 64.17  ? 334 HOH   B O   1 
HETATM 1691 O O   . HOH   F 5 .   ? -15.009 9.665   -0.727  1.00 65.07  ? 335 HOH   B O   1 
HETATM 1692 O O   . HOH   F 5 .   ? -19.777 -5.807  -0.677  1.00 50.87  ? 336 HOH   B O   1 
HETATM 1693 O O   . HOH   F 5 .   ? -14.980 -12.199 -16.476 1.00 60.18  ? 337 HOH   B O   1 
HETATM 1694 O O   . HOH   F 5 .   ? -10.950 8.062   -13.985 1.00 55.15  ? 338 HOH   B O   1 
HETATM 1695 O O   . HOH   F 5 .   ? -7.269  -6.382  0.554   1.00 73.54  ? 339 HOH   B O   1 
HETATM 1696 O O   . HOH   F 5 .   ? -14.587 16.882  -20.245 1.00 57.94  ? 340 HOH   B O   1 
HETATM 1697 O O   . HOH   F 5 .   ? -20.210 6.376   -33.108 1.00 75.20  ? 341 HOH   B O   1 
HETATM 1698 O O   A HOH   F 5 .   ? -29.187 -5.122  -0.748  0.50 56.84  ? 342 HOH   B O   1 
HETATM 1699 O O   B HOH   F 5 .   ? -29.187 -5.122  -0.748  0.50 56.84  ? 342 HOH   B O   1 
HETATM 1700 O O   . HOH   F 5 .   ? -16.568 16.603  -21.928 1.00 70.97  ? 343 HOH   B O   1 
HETATM 1701 O O   . HOH   F 5 .   ? -35.485 1.016   -7.369  1.00 59.67  ? 344 HOH   B O   1 
HETATM 1702 O O   . HOH   F 5 .   ? -10.207 -10.599 -7.608  1.00 76.63  ? 345 HOH   B O   1 
HETATM 1703 O O   . HOH   F 5 .   ? -2.322  -9.153  -3.359  1.00 60.32  ? 346 HOH   B O   1 
HETATM 1704 O O   . HOH   F 5 .   ? -1.264  -15.381 -10.271 1.00 61.38  ? 347 HOH   B O   1 
HETATM 1705 O O   . HOH   F 5 .   ? -17.525 13.189  -31.545 1.00 66.28  ? 348 HOH   B O   1 
HETATM 1706 O O   . HOH   F 5 .   ? -11.783 13.155  -14.727 1.00 70.23  ? 349 HOH   B O   1 
HETATM 1707 O O   A HOH   F 5 .   ? -11.893 -6.956  1.792   0.50 66.94  ? 350 HOH   B O   1 
HETATM 1708 O O   B HOH   F 5 .   ? -11.893 -6.956  1.792   0.50 66.94  ? 350 HOH   B O   1 
HETATM 1709 O O   A HOH   F 5 .   ? -21.198 4.261   -0.000  0.25 69.93  ? 351 HOH   B O   1 
HETATM 1710 O O   B HOH   F 5 .   ? -21.198 3.214   0.000   0.25 67.26  ? 351 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   ? 1.4817 0.6623 0.6495 0.1570  0.0740  0.0013  50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.4556 0.6994 0.6430 0.1957  0.0838  -0.0022 50  ASP   A CA  
3    C C   . ASP   A 7   ? 1.4126 0.6903 0.6240 0.1983  0.0936  0.0203  50  ASP   A C   
4    O O   . ASP   A 7   ? 1.4458 0.6669 0.6277 0.2022  0.0909  0.0336  50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.5272 0.7315 0.6767 0.2427  0.0771  -0.0235 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.5899 0.8679 0.7696 0.2806  0.0883  -0.0312 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.5706 0.9067 0.7726 0.2828  0.0978  -0.0423 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.6353 0.9126 0.8159 0.3081  0.0874  -0.0264 50  ASP   A OD2 
9    N N   . MET   A 8   ? 1.3344 0.6998 0.5943 0.1966  0.1041  0.0243  51  MET   A N   
10   C CA  . MET   A 8   ? 1.2849 0.6933 0.5722 0.1987  0.1115  0.0416  51  MET   A CA  
11   C C   . MET   A 8   ? 1.2518 0.6864 0.5475 0.2420  0.1109  0.0345  51  MET   A C   
12   O O   . MET   A 8   ? 1.2392 0.6976 0.5439 0.2664  0.1117  0.0158  51  MET   A O   
13   C CB  . MET   A 8   ? 1.2385 0.7230 0.5742 0.1735  0.1199  0.0478  51  MET   A CB  
14   C CG  . MET   A 8   ? 1.2573 0.7318 0.5966 0.1321  0.1188  0.0544  51  MET   A CG  
15   S SD  . MET   A 8   ? 1.2560 0.8202 0.6493 0.1127  0.1256  0.0598  51  MET   A SD  
16   C CE  . MET   A 8   ? 1.2595 0.8072 0.6579 0.0674  0.1205  0.0638  51  MET   A CE  
17   N N   . TYR   A 9   ? 1.2314 0.6674 0.5268 0.2515  0.1098  0.0485  52  TYR   A N   
18   C CA  . TYR   A 9   ? 1.2131 0.6768 0.5207 0.2925  0.1041  0.0406  52  TYR   A CA  
19   C C   . TYR   A 9   ? 1.1791 0.6881 0.5131 0.2899  0.1056  0.0539  52  TYR   A C   
20   O O   . TYR   A 9   ? 1.1820 0.6837 0.5100 0.2608  0.1121  0.0726  52  TYR   A O   
21   C CB  . TYR   A 9   ? 1.2624 0.6510 0.5169 0.3288  0.0906  0.0353  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 1.3279 0.6390 0.5288 0.3193  0.0875  0.0583  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 1.3815 0.6156 0.5410 0.2914  0.0894  0.0676  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 1.3474 0.6585 0.5361 0.3390  0.0827  0.0702  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 1.4361 0.5974 0.5473 0.2780  0.0917  0.0918  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 1.4029 0.6396 0.5349 0.3306  0.0844  0.0946  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.4568 0.6183 0.5509 0.2986  0.0911  0.1068  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.5267 0.6129 0.5657 0.2856  0.0977  0.1337  52  TYR   A OH  
29   N N   . ILE   A 10  ? 1.1420 0.7018 0.5086 0.3203  0.0995  0.0420  53  ILE   A N   
30   C CA  . ILE   A 10  ? 1.1162 0.7166 0.5059 0.3223  0.0965  0.0497  53  ILE   A CA  
31   C C   . ILE   A 10  ? 1.1384 0.7102 0.4981 0.3637  0.0790  0.0477  53  ILE   A C   
32   O O   . ILE   A 10  ? 1.1530 0.7060 0.5008 0.3987  0.0673  0.0321  53  ILE   A O   
33   C CB  . ILE   A 10  ? 1.0622 0.7498 0.5208 0.3155  0.1015  0.0390  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 1.0447 0.7697 0.5381 0.3443  0.0981  0.0153  53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 1.0552 0.7642 0.5318 0.2759  0.1165  0.0463  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 1.0030 0.8088 0.5653 0.3386  0.1025  0.0063  53  ILE   A CD1 
37   N N   . GLU   A 11  ? 1.1442 0.7117 0.4875 0.3625  0.0764  0.0627  54  GLU   A N   
38   C CA  . GLU   A 11  ? 1.1706 0.7095 0.4768 0.4025  0.0581  0.0629  54  GLU   A CA  
39   C C   . GLU   A 11  ? 1.1355 0.7329 0.4746 0.4052  0.0526  0.0614  54  GLU   A C   
40   O O   . GLU   A 11  ? 1.1241 0.7371 0.4697 0.3735  0.0670  0.0765  54  GLU   A O   
41   C CB  . GLU   A 11  ? 1.2601 0.7075 0.4847 0.3987  0.0630  0.0889  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 1.3903 0.7586 0.5681 0.3993  0.0640  0.0916  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.5853 0.8562 0.6808 0.3948  0.0695  0.1194  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.6084 0.8817 0.6904 0.3749  0.0829  0.1408  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.6920 0.8819 0.7346 0.4113  0.0619  0.1201  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 1.1141 0.7423 0.4731 0.4441  0.0298  0.0418  55  ARG   A N   
47   C CA  . ARG   A 12  ? 1.0897 0.7689 0.4787 0.4483  0.0201  0.0366  55  ARG   A CA  
48   C C   . ARG   A 12  ? 1.1260 0.7605 0.4507 0.4476  0.0239  0.0602  55  ARG   A C   
49   O O   . ARG   A 12  ? 1.1800 0.7414 0.4316 0.4651  0.0224  0.0747  55  ARG   A O   
50   C CB  . ARG   A 12  ? 1.0831 0.8000 0.5051 0.4918  -0.0096 0.0080  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 1.0623 0.8539 0.5514 0.4836  -0.0177 -0.0067 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 1.0533 0.8996 0.6017 0.5158  -0.0448 -0.0399 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 1.0511 0.9597 0.6618 0.5014  -0.0520 -0.0523 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 1.0843 0.9933 0.6791 0.5212  -0.0753 -0.0586 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 1.1412 0.9946 0.6582 0.5585  -0.0926 -0.0528 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 1.0246 0.9838 0.6752 0.5051  -0.0817 -0.0704 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 1.0998 0.7748 0.4482 0.4283  0.0305  0.0647  56  ALA   A N   
58   C CA  . ALA   A 13  ? 1.1333 0.7782 0.4255 0.4292  0.0376  0.0854  56  ALA   A CA  
59   C C   . ALA   A 13  ? 1.1186 0.8008 0.4213 0.4555  0.0166  0.0709  56  ALA   A C   
60   O O   . ALA   A 13  ? 1.1528 0.8114 0.4032 0.4634  0.0215  0.0856  56  ALA   A O   
61   C CB  . ALA   A 13  ? 1.1342 0.7850 0.4325 0.3822  0.0680  0.1064  56  ALA   A CB  
62   N N   . GLY   A 14  ? 1.0627 0.8022 0.4321 0.4678  -0.0055 0.0420  57  GLY   A N   
63   C CA  . GLY   A 14  ? 1.0269 0.7999 0.4110 0.4918  -0.0302 0.0238  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.9443 0.7905 0.4206 0.4757  -0.0393 0.0001  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.9022 0.7768 0.4319 0.4456  -0.0237 -0.0009 57  GLY   A O   
66   N N   . ASP   A 15  ? 0.9161 0.7884 0.4075 0.4971  -0.0658 -0.0197 58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.8555 0.7900 0.4321 0.4822  -0.0777 -0.0430 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.8644 0.8108 0.4492 0.4513  -0.0600 -0.0309 58  ASP   A C   
69   O O   . ASP   A 15  ? 0.9075 0.8237 0.4316 0.4554  -0.0497 -0.0131 58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.8364 0.7881 0.4231 0.5207  -0.1197 -0.0731 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.8589 0.8182 0.4615 0.5551  -0.1465 -0.0955 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.8690 0.8163 0.4694 0.5520  -0.1317 -0.0872 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.8751 0.8520 0.4908 0.5883  -0.1851 -0.1238 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.8254 0.8161 0.4840 0.4248  -0.0590 -0.0425 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.8319 0.8329 0.4996 0.4013  -0.0485 -0.0350 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.8474 0.8653 0.5345 0.4220  -0.0814 -0.0608 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.8157 0.8673 0.5717 0.4149  -0.0982 -0.0833 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.8015 0.8260 0.5224 0.3611  -0.0265 -0.0281 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.8277 0.8284 0.5172 0.3467  0.0011  -0.0054 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.8005 0.8331 0.5301 0.3422  -0.0211 -0.0230 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.8232 0.8416 0.5539 0.3166  0.0197  -0.0012 59  ILE   A CD1 
82   N N   B THR   A 17  ? 0.8882 0.8810 0.5124 0.4488  -0.0908 -0.0585 60  THR   A N   
83   N N   D THR   A 17  ? 0.8882 0.8810 0.5124 0.4488  -0.0908 -0.0585 60  THR   A N   
84   C CA  B THR   A 17  ? 0.9063 0.9052 0.5302 0.4763  -0.1254 -0.0844 60  THR   A CA  
85   C CA  D THR   A 17  ? 0.9063 0.9052 0.5302 0.4763  -0.1254 -0.0844 60  THR   A CA  
86   C C   B THR   A 17  ? 0.9440 0.9248 0.5118 0.4834  -0.1157 -0.0727 60  THR   A C   
87   C C   D THR   A 17  ? 0.9440 0.9248 0.5118 0.4834  -0.1157 -0.0727 60  THR   A C   
88   O O   B THR   A 17  ? 0.9705 0.9263 0.4778 0.4841  -0.0888 -0.0461 60  THR   A O   
89   O O   D THR   A 17  ? 0.9705 0.9263 0.4778 0.4841  -0.0888 -0.0461 60  THR   A O   
90   C CB  B THR   A 17  ? 0.9463 0.9312 0.5395 0.5205  -0.1563 -0.1017 60  THR   A CB  
91   C CB  D THR   A 17  ? 0.9463 0.9312 0.5395 0.5205  -0.1563 -0.1017 60  THR   A CB  
92   O OG1 B THR   A 17  ? 0.9247 0.9422 0.5901 0.5150  -0.1701 -0.1210 60  THR   A OG1 
93   O OG1 D THR   A 17  ? 0.9247 0.9422 0.5901 0.5150  -0.1701 -0.1210 60  THR   A OG1 
94   C CG2 B THR   A 17  ? 0.9673 0.9470 0.5345 0.5575  -0.1937 -0.1269 60  THR   A CG2 
95   C CG2 D THR   A 17  ? 0.9673 0.9470 0.5345 0.5575  -0.1937 -0.1269 60  THR   A CG2 
96   N N   . TRP   A 18  ? 0.9455 0.9394 0.5359 0.4872  -0.1359 -0.0926 61  TRP   A N   
97   C CA  . TRP   A 18  ? 1.0112 0.9921 0.5491 0.5011  -0.1298 -0.0868 61  TRP   A CA  
98   C C   . TRP   A 18  ? 1.0992 1.0519 0.5587 0.5503  -0.1486 -0.0939 61  TRP   A C   
99   O O   . TRP   A 18  ? 1.1064 1.0592 0.5764 0.5762  -0.1864 -0.1211 61  TRP   A O   
100  C CB  . TRP   A 18  ? 0.9886 0.9844 0.5711 0.4961  -0.1523 -0.1107 61  TRP   A CB  
101  C CG  . TRP   A 18  ? 1.0161 1.0004 0.5460 0.5189  -0.1525 -0.1124 61  TRP   A CG  
102  C CD1 . TRP   A 18  ? 1.0513 1.0197 0.5323 0.5624  -0.1813 -0.1341 61  TRP   A CD1 
103  C CD2 . TRP   A 18  ? 1.0127 1.0038 0.5379 0.5021  -0.1257 -0.0958 61  TRP   A CD2 
104  N NE1 . TRP   A 18  ? 1.0669 1.0317 0.5090 0.5744  -0.1697 -0.1303 61  TRP   A NE1 
105  C CE2 . TRP   A 18  ? 1.0448 1.0260 0.5177 0.5378  -0.1366 -0.1078 61  TRP   A CE2 
106  C CE3 . TRP   A 18  ? 0.9979 1.0034 0.5552 0.4639  -0.0948 -0.0733 61  TRP   A CE3 
107  C CZ2 . TRP   A 18  ? 1.0516 1.0419 0.5105 0.5361  -0.1168 -0.0989 61  TRP   A CZ2 
108  C CZ3 . TRP   A 18  ? 1.0077 1.0210 0.5525 0.4620  -0.0791 -0.0655 61  TRP   A CZ3 
109  C CH2 . TRP   A 18  ? 1.0300 1.0381 0.5277 0.4978  -0.0886 -0.0777 61  TRP   A CH2 
110  N N   . GLU   A 19  ? 1.1665 1.0956 0.5479 0.5636  -0.1221 -0.0696 62  GLU   A N   
111  C CA  . GLU   A 19  ? 1.2504 1.1450 0.5444 0.6111  -0.1350 -0.0715 62  GLU   A CA  
112  C C   . GLU   A 19  ? 1.3140 1.2036 0.5561 0.6402  -0.1397 -0.0801 62  GLU   A C   
113  O O   . GLU   A 19  ? 1.3175 1.2158 0.5444 0.6259  -0.1058 -0.0608 62  GLU   A O   
114  C CB  . GLU   A 19  ? 1.3211 1.1818 0.5537 0.6095  -0.1019 -0.0365 62  GLU   A CB  
115  C CG  . GLU   A 19  ? 1.3849 1.2477 0.6652 0.5832  -0.0970 -0.0295 62  GLU   A CG  
116  C CD  . GLU   A 19  ? 1.4990 1.3586 0.7989 0.6077  -0.1353 -0.0538 62  GLU   A CD  
117  O OE1 . GLU   A 19  ? 1.5408 1.3916 0.8112 0.6506  -0.1727 -0.0784 62  GLU   A OE1 
118  O OE2 . GLU   A 19  ? 1.5145 1.3821 0.8589 0.5862  -0.1285 -0.0497 62  GLU   A OE2 
119  N N   . LYS   A 20  ? 1.3557 1.2354 0.5765 0.6819  -0.1843 -0.1130 63  LYS   A N   
120  C CA  . LYS   A 20  ? 1.4197 1.2914 0.5866 0.7163  -0.1946 -0.1272 63  LYS   A CA  
121  C C   . LYS   A 20  ? 1.4889 1.3291 0.5474 0.7429  -0.1613 -0.0979 63  LYS   A C   
122  O O   . LYS   A 20  ? 1.5238 1.3302 0.5258 0.7627  -0.1613 -0.0853 63  LYS   A O   
123  C CB  . LYS   A 20  ? 1.4708 1.3341 0.6349 0.7577  -0.2552 -0.1722 63  LYS   A CB  
124  C CG  . LYS   A 20  ? 1.5009 1.3949 0.7736 0.7312  -0.2894 -0.2048 63  LYS   A CG  
125  C CD  . LYS   A 20  ? 1.5632 1.4503 0.8377 0.7707  -0.3517 -0.2507 63  LYS   A CD  
126  C CE  . LYS   A 20  ? 1.5705 1.4883 0.9596 0.7400  -0.3845 -0.2828 63  LYS   A CE  
127  N NZ  . LYS   A 20  ? 1.6049 1.5188 1.0000 0.7777  -0.4482 -0.3313 63  LYS   A NZ  
128  N N   . ASP   A 21  ? 1.5051 1.3554 0.5340 0.7442  -0.1322 -0.0871 64  ASP   A N   
129  C CA  . ASP   A 21  ? 1.5657 1.3940 0.4962 0.7656  -0.0922 -0.0579 64  ASP   A CA  
130  C C   . ASP   A 21  ? 1.5669 1.3918 0.4975 0.7256  -0.0408 -0.0137 64  ASP   A C   
131  O O   . ASP   A 21  ? 1.6128 1.3998 0.4606 0.7407  -0.0159 0.0131  64  ASP   A O   
132  C CB  . ASP   A 21  ? 1.6519 1.4332 0.4773 0.8263  -0.1175 -0.0682 64  ASP   A CB  
133  C CG  . ASP   A 21  ? 1.7471 1.5294 0.5576 0.8703  -0.1653 -0.1124 64  ASP   A CG  
134  O OD1 . ASP   A 21  ? 1.7554 1.5657 0.5908 0.8658  -0.1589 -0.1235 64  ASP   A OD1 
135  O OD2 . ASP   A 21  ? 1.8003 1.5539 0.5733 0.9114  -0.2119 -0.1379 64  ASP   A OD2 
136  N N   . ALA   A 22  ? 1.5159 1.3757 0.5357 0.6747  -0.0256 -0.0064 65  ALA   A N   
137  C CA  . ALA   A 22  ? 1.5059 1.3681 0.5376 0.6322  0.0208  0.0309  65  ALA   A CA  
138  C C   . ALA   A 22  ? 1.5035 1.3902 0.5096 0.6264  0.0660  0.0507  65  ALA   A C   
139  O O   . ALA   A 22  ? 1.4923 1.4019 0.4922 0.6500  0.0585  0.0322  65  ALA   A O   
140  C CB  . ALA   A 22  ? 1.4623 1.3548 0.5949 0.5855  0.0162  0.0268  65  ALA   A CB  
141  N N   . GLU   A 23  ? 1.5098 1.3925 0.5035 0.5956  0.1123  0.0866  66  GLU   A N   
142  C CA  . GLU   A 23  ? 1.5062 1.4208 0.4869 0.5846  0.1599  0.1068  66  GLU   A CA  
143  C C   . GLU   A 23  ? 1.4336 1.4105 0.5033 0.5592  0.1595  0.0923  66  GLU   A C   
144  O O   . GLU   A 23  ? 1.3975 1.3891 0.5381 0.5207  0.1546  0.0931  66  GLU   A O   
145  C CB  . GLU   A 23  ? 1.5756 1.4681 0.5345 0.5499  0.2059  0.1473  66  GLU   A CB  
146  C CG  . GLU   A 23  ? 1.6462 1.5804 0.6127 0.5254  0.2597  0.1704  66  GLU   A CG  
147  C CD  . GLU   A 23  ? 1.7271 1.6652 0.7404 0.4678  0.2904  0.1969  66  GLU   A CD  
148  O OE1 . GLU   A 23  ? 1.7486 1.6363 0.7522 0.4542  0.2797  0.2065  66  GLU   A OE1 
149  O OE2 . GLU   A 23  ? 1.7315 1.7240 0.7921 0.4381  0.3234  0.2057  66  GLU   A OE2 
150  N N   . VAL   A 24  ? 1.4122 1.4216 0.4717 0.5858  0.1620  0.0776  67  VAL   A N   
151  C CA  . VAL   A 24  ? 1.3585 1.4215 0.4901 0.5729  0.1574  0.0610  67  VAL   A CA  
152  C C   . VAL   A 24  ? 1.3289 1.4423 0.4812 0.5481  0.2079  0.0832  67  VAL   A C   
153  O O   . VAL   A 24  ? 1.3422 1.4726 0.4469 0.5722  0.2368  0.0895  67  VAL   A O   
154  C CB  . VAL   A 24  ? 1.3632 1.4301 0.4774 0.6197  0.1233  0.0259  67  VAL   A CB  
155  C CG1 . VAL   A 24  ? 1.3292 1.4349 0.5193 0.6056  0.1084  0.0074  67  VAL   A CG1 
156  C CG2 . VAL   A 24  ? 1.3930 1.4114 0.4791 0.6482  0.0744  0.0026  67  VAL   A CG2 
157  N N   . THR   A 25  ? 1.2893 1.4295 0.5134 0.5010  0.2188  0.0936  68  THR   A N   
158  C CA  . THR   A 25  ? 1.2563 1.4507 0.5140 0.4731  0.2626  0.1115  68  THR   A CA  
159  C C   . THR   A 25  ? 1.2079 1.4429 0.5552 0.4410  0.2498  0.1016  68  THR   A C   
160  O O   . THR   A 25  ? 1.2047 1.4188 0.5795 0.4389  0.2121  0.0855  68  THR   A O   
161  C CB  . THR   A 25  ? 1.2874 1.4577 0.5141 0.4441  0.3027  0.1468  68  THR   A CB  
162  O OG1 . THR   A 25  ? 1.2734 1.5004 0.5229 0.4244  0.3496  0.1625  68  THR   A OG1 
163  C CG2 . THR   A 25  ? 1.2851 1.4251 0.5482 0.4033  0.2910  0.1561  68  THR   A CG2 
164  N N   . GLY   A 26  ? 1.1706 1.4646 0.5619 0.4187  0.2804  0.1100  69  GLY   A N   
165  C CA  . GLY   A 26  ? 1.1324 1.4639 0.6017 0.3917  0.2675  0.1010  69  GLY   A CA  
166  C C   . GLY   A 26  ? 1.1054 1.4775 0.6028 0.4205  0.2473  0.0747  69  GLY   A C   
167  O O   . GLY   A 26  ? 1.1262 1.4712 0.5948 0.4570  0.2174  0.0547  69  GLY   A O   
168  N N   . ASN   A 27  ? 1.0550 1.4901 0.6107 0.4048  0.2601  0.0728  70  ASN   A N   
169  C CA  . ASN   A 27  ? 1.0296 1.5029 0.6135 0.4338  0.2396  0.0477  70  ASN   A CA  
170  C C   . ASN   A 27  ? 1.0101 1.4576 0.6309 0.4227  0.1975  0.0350  70  ASN   A C   
171  O O   . ASN   A 27  ? 1.0258 1.4315 0.6503 0.3932  0.1877  0.0454  70  ASN   A O   
172  C CB  . ASN   A 27  ? 1.0132 1.5733 0.6390 0.4318  0.2731  0.0484  70  ASN   A CB  
173  C CG  . ASN   A 27  ? 1.0260 1.6227 0.7207 0.3861  0.2790  0.0566  70  ASN   A CG  
174  O OD1 . ASN   A 27  ? 1.0495 1.6176 0.7474 0.3458  0.2886  0.0759  70  ASN   A OD1 
175  N ND2 . ASN   A 27  ? 0.9882 1.6458 0.7370 0.3944  0.2700  0.0398  70  ASN   A ND2 
176  N N   . SER   A 28  ? 0.9818 1.4479 0.6229 0.4491  0.1729  0.0129  71  SER   A N   
177  C CA  . SER   A 28  ? 0.9686 1.4030 0.6344 0.4418  0.1354  0.0031  71  SER   A CA  
178  C C   . SER   A 28  ? 0.9144 1.4024 0.6299 0.4423  0.1307  -0.0054 71  SER   A C   
179  O O   . SER   A 28  ? 0.9168 1.4080 0.6326 0.4763  0.1078  -0.0252 71  SER   A O   
180  C CB  . SER   A 28  ? 1.0176 1.4002 0.6506 0.4764  0.1004  -0.0168 71  SER   A CB  
181  O OG  . SER   A 28  ? 1.0914 1.4415 0.6754 0.4927  0.1029  -0.0174 71  SER   A OG  
182  N N   . PRO   A 29  ? 0.8711 1.3994 0.6284 0.4070  0.1488  0.0072  72  PRO   A N   
183  C CA  . PRO   A 29  ? 0.8293 1.4155 0.6364 0.4110  0.1413  -0.0041 72  PRO   A CA  
184  C C   . PRO   A 29  ? 0.8273 1.3749 0.6435 0.4086  0.1032  -0.0108 72  PRO   A C   
185  O O   . PRO   A 29  ? 0.8457 1.3343 0.6461 0.3850  0.0922  -0.0004 72  PRO   A O   
186  C CB  . PRO   A 29  ? 0.8094 1.4499 0.6574 0.3713  0.1740  0.0107  72  PRO   A CB  
187  C CG  . PRO   A 29  ? 0.8479 1.4284 0.6677 0.3372  0.1826  0.0313  72  PRO   A CG  
188  C CD  . PRO   A 29  ? 0.8673 1.3901 0.6284 0.3641  0.1748  0.0299  72  PRO   A CD  
189  N N   . ARG   A 30  ? 0.8049 1.3847 0.6432 0.4358  0.0837  -0.0282 73  ARG   A N   
190  C CA  . ARG   A 30  ? 0.8226 1.3653 0.6634 0.4375  0.0484  -0.0332 73  ARG   A CA  
191  C C   . ARG   A 30  ? 0.7708 1.3739 0.6619 0.4184  0.0506  -0.0336 73  ARG   A C   
192  O O   . ARG   A 30  ? 0.7355 1.4152 0.6641 0.4370  0.0568  -0.0471 73  ARG   A O   
193  C CB  . ARG   A 30  ? 0.8765 1.3970 0.6965 0.4861  0.0186  -0.0533 73  ARG   A CB  
194  C CG  . ARG   A 30  ? 1.0020 1.4486 0.7738 0.4986  0.0082  -0.0545 73  ARG   A CG  
195  C CD  . ARG   A 30  ? 1.1075 1.5217 0.8551 0.5454  -0.0225 -0.0756 73  ARG   A CD  
196  N NE  . ARG   A 30  ? 1.2122 1.5698 0.9201 0.5575  -0.0294 -0.0809 73  ARG   A NE  
197  C CZ  . ARG   A 30  ? 1.2892 1.5802 0.9688 0.5813  -0.0616 -0.0943 73  ARG   A CZ  
198  N NH1 . ARG   A 30  ? 1.3045 1.5703 0.9842 0.5973  -0.0883 -0.1009 73  ARG   A NH1 
199  N NH2 . ARG   A 30  ? 1.3076 1.5529 0.9572 0.5894  -0.0691 -0.1017 73  ARG   A NH2 
200  N N   . LEU   A 31  ? 0.7628 1.3358 0.6570 0.3810  0.0466  -0.0204 74  LEU   A N   
201  C CA  . LEU   A 31  ? 0.7193 1.3423 0.6588 0.3578  0.0460  -0.0217 74  LEU   A CA  
202  C C   . LEU   A 31  ? 0.7237 1.3078 0.6523 0.3617  0.0104  -0.0253 74  LEU   A C   
203  O O   . LEU   A 31  ? 0.7616 1.2674 0.6475 0.3566  -0.0014 -0.0153 74  LEU   A O   
204  C CB  . LEU   A 31  ? 0.7177 1.3362 0.6650 0.3096  0.0727  -0.0036 74  LEU   A CB  
205  C CG  . LEU   A 31  ? 0.7271 1.3668 0.6718 0.3008  0.1106  0.0062  74  LEU   A CG  
206  C CD1 . LEU   A 31  ? 0.7472 1.3514 0.6809 0.2578  0.1295  0.0258  74  LEU   A CD1 
207  C CD2 . LEU   A 31  ? 0.6814 1.4173 0.6770 0.3073  0.1321  -0.0033 74  LEU   A CD2 
208  N N   . ASP   A 32  ? 0.6821 1.3221 0.6497 0.3695  -0.0058 -0.0393 75  ASP   A N   
209  C CA  . ASP   A 32  ? 0.6955 1.2972 0.6457 0.3743  -0.0400 -0.0419 75  ASP   A CA  
210  C C   . ASP   A 32  ? 0.6701 1.2684 0.6321 0.3290  -0.0321 -0.0318 75  ASP   A C   
211  O O   . ASP   A 32  ? 0.6384 1.3079 0.6541 0.3090  -0.0207 -0.0387 75  ASP   A O   
212  C CB  . ASP   A 32  ? 0.7021 1.3660 0.6865 0.4087  -0.0664 -0.0649 75  ASP   A CB  
213  C CG  . ASP   A 32  ? 0.8103 1.4761 0.7809 0.4598  -0.0787 -0.0784 75  ASP   A CG  
214  O OD1 . ASP   A 32  ? 0.8651 1.4607 0.7869 0.4700  -0.0771 -0.0698 75  ASP   A OD1 
215  O OD2 . ASP   A 32  ? 0.8246 1.5630 0.8353 0.4906  -0.0916 -0.0999 75  ASP   A OD2 
216  N N   . VAL   A 33  ? 0.6820 1.1996 0.5970 0.3114  -0.0356 -0.0162 76  VAL   A N   
217  C CA  . VAL   A 33  ? 0.6598 1.1670 0.5790 0.2715  -0.0280 -0.0080 76  VAL   A CA  
218  C C   . VAL   A 33  ? 0.6762 1.1285 0.5567 0.2734  -0.0554 -0.0063 76  VAL   A C   
219  O O   . VAL   A 33  ? 0.7040 1.1053 0.5425 0.2998  -0.0742 -0.0040 76  VAL   A O   
220  C CB  . VAL   A 33  ? 0.6684 1.1406 0.5714 0.2418  0.0033  0.0099  76  VAL   A CB  
221  C CG1 . VAL   A 33  ? 0.6517 1.1665 0.5768 0.2453  0.0302  0.0105  76  VAL   A CG1 
222  C CG2 . VAL   A 33  ? 0.7128 1.1014 0.5612 0.2467  -0.0011 0.0224  76  VAL   A CG2 
223  N N   . ALA   A 34  ? 0.6554 1.1148 0.5470 0.2453  -0.0571 -0.0074 77  ALA   A N   
224  C CA  . ALA   A 34  ? 0.6773 1.0852 0.5269 0.2446  -0.0790 -0.0057 77  ALA   A CA  
225  C C   . ALA   A 34  ? 0.6911 1.0548 0.5192 0.2093  -0.0584 0.0083  77  ALA   A C   
226  O O   . ALA   A 34  ? 0.6807 1.0709 0.5405 0.1819  -0.0355 0.0105  77  ALA   A O   
227  C CB  . ALA   A 34  ? 0.6481 1.1070 0.5287 0.2497  -0.1074 -0.0263 77  ALA   A CB  
228  N N   . LEU   A 35  ? 0.7111 1.0045 0.4822 0.2115  -0.0644 0.0188  78  LEU   A N   
229  C CA  . LEU   A 35  ? 0.7189 0.9702 0.4666 0.1839  -0.0462 0.0298  78  LEU   A CA  
230  C C   . LEU   A 35  ? 0.7352 0.9610 0.4501 0.1834  -0.0673 0.0238  78  LEU   A C   
231  O O   . LEU   A 35  ? 0.7669 0.9559 0.4368 0.2070  -0.0856 0.0262  78  LEU   A O   
232  C CB  . LEU   A 35  ? 0.7400 0.9339 0.4513 0.1863  -0.0283 0.0475  78  LEU   A CB  
233  C CG  . LEU   A 35  ? 0.7716 0.9227 0.4573 0.1637  -0.0102 0.0576  78  LEU   A CG  
234  C CD1 . LEU   A 35  ? 0.7535 0.9286 0.4713 0.1398  0.0102  0.0576  78  LEU   A CD1 
235  C CD2 . LEU   A 35  ? 0.8075 0.9066 0.4602 0.1695  0.0018  0.0722  78  LEU   A CD2 
236  N N   . ASP   A 36  ? 0.7134 0.9562 0.4475 0.1584  -0.0668 0.0150  79  ASP   A N   
237  C CA  . ASP   A 36  ? 0.7325 0.9521 0.4343 0.1592  -0.0897 0.0051  79  ASP   A CA  
238  C C   . ASP   A 36  ? 0.7865 0.9356 0.4290 0.1509  -0.0741 0.0185  79  ASP   A C   
239  O O   . ASP   A 36  ? 0.8026 0.9290 0.4406 0.1412  -0.0459 0.0337  79  ASP   A O   
240  C CB  . ASP   A 36  ? 0.7062 0.9807 0.4609 0.1389  -0.1045 -0.0164 79  ASP   A CB  
241  C CG  . ASP   A 36  ? 0.7422 1.0165 0.5216 0.1013  -0.0820 -0.0147 79  ASP   A CG  
242  O OD1 . ASP   A 36  ? 0.7592 0.9877 0.5088 0.0931  -0.0563 0.0021  79  ASP   A OD1 
243  O OD2 . ASP   A 36  ? 0.7500 1.0690 0.5795 0.0799  -0.0912 -0.0311 79  ASP   A OD2 
244  N N   . GLU   A 37  ? 0.8136 0.9317 0.4114 0.1572  -0.0934 0.0108  80  GLU   A N   
245  C CA  . GLU   A 37  ? 0.8575 0.9136 0.3951 0.1541  -0.0804 0.0199  80  GLU   A CA  
246  C C   . GLU   A 37  ? 0.8449 0.8970 0.4025 0.1252  -0.0569 0.0206  80  GLU   A C   
247  O O   . GLU   A 37  ? 0.8694 0.8801 0.3938 0.1231  -0.0340 0.0331  80  GLU   A O   
248  C CB  . GLU   A 37  ? 0.9155 0.9471 0.4021 0.1697  -0.1105 0.0064  80  GLU   A CB  
249  C CG  . GLU   A 37  ? 1.0486 1.0109 0.4523 0.1838  -0.0984 0.0212  80  GLU   A CG  
250  C CD  . GLU   A 37  ? 1.1791 1.1118 0.5213 0.2018  -0.1273 0.0072  80  GLU   A CD  
251  O OE1 . GLU   A 37  ? 1.1880 1.1180 0.5282 0.1889  -0.1347 -0.0094 80  GLU   A OE1 
252  O OE2 . GLU   A 37  ? 1.2430 1.1501 0.5341 0.2305  -0.1445 0.0123  80  GLU   A OE2 
253  N N   . SER   A 38  ? 0.8053 0.9002 0.4186 0.1034  -0.0608 0.0080  81  SER   A N   
254  C CA  . SER   A 38  ? 0.8069 0.8907 0.4358 0.0768  -0.0394 0.0104  81  SER   A CA  
255  C C   . SER   A 38  ? 0.7947 0.8873 0.4486 0.0710  -0.0092 0.0277  81  SER   A C   
256  O O   . SER   A 38  ? 0.7969 0.8805 0.4633 0.0514  0.0077  0.0308  81  SER   A O   
257  C CB  . SER   A 38  ? 0.8064 0.9243 0.4820 0.0518  -0.0537 -0.0079 81  SER   A CB  
258  O OG  . SER   A 38  ? 0.8811 0.9828 0.5299 0.0556  -0.0833 -0.0272 81  SER   A OG  
259  N N   . GLY   A 39  ? 0.7779 0.8836 0.4358 0.0891  -0.0052 0.0376  82  GLY   A N   
260  C CA  . GLY   A 39  ? 0.7714 0.8839 0.4486 0.0877  0.0186  0.0507  82  GLY   A CA  
261  C C   . GLY   A 39  ? 0.7404 0.9039 0.4704 0.0757  0.0249  0.0481  82  GLY   A C   
262  O O   . GLY   A 39  ? 0.7284 0.8931 0.4683 0.0730  0.0452  0.0580  82  GLY   A O   
263  N N   . ASP   A 40  ? 0.7212 0.9297 0.4856 0.0698  0.0079  0.0340  83  ASP   A N   
264  C CA  . ASP   A 40  ? 0.6952 0.9610 0.5153 0.0563  0.0172  0.0310  83  ASP   A CA  
265  C C   . ASP   A 40  ? 0.6847 0.9969 0.5279 0.0814  0.0102  0.0279  83  ASP   A C   
266  O O   . ASP   A 40  ? 0.6825 1.0091 0.5239 0.1003  -0.0159 0.0166  83  ASP   A O   
267  C CB  . ASP   A 40  ? 0.6932 0.9901 0.5504 0.0313  0.0039  0.0147  83  ASP   A CB  
268  C CG  . ASP   A 40  ? 0.7771 1.0249 0.6123 0.0062  0.0080  0.0146  83  ASP   A CG  
269  O OD1 . ASP   A 40  ? 0.7993 1.0170 0.6223 -0.0053 0.0327  0.0287  83  ASP   A OD1 
270  O OD2 . ASP   A 40  ? 0.8260 1.0626 0.6523 0.0013  -0.0160 -0.0011 83  ASP   A OD2 
271  N N   . PHE   A 41  ? 0.6777 1.0110 0.5382 0.0844  0.0317  0.0366  84  PHE   A N   
272  C CA  . PHE   A 41  ? 0.6664 1.0446 0.5490 0.1100  0.0278  0.0321  84  PHE   A CA  
273  C C   . PHE   A 41  ? 0.6636 1.1207 0.6086 0.1002  0.0268  0.0185  84  PHE   A C   
274  O O   . PHE   A 41  ? 0.6577 1.1336 0.6317 0.0687  0.0440  0.0202  84  PHE   A O   
275  C CB  . PHE   A 41  ? 0.6469 1.0139 0.5180 0.1193  0.0511  0.0448  84  PHE   A CB  
276  C CG  . PHE   A 41  ? 0.6679 0.9751 0.4926 0.1365  0.0478  0.0535  84  PHE   A CG  
277  C CD1 . PHE   A 41  ? 0.6795 0.9766 0.4890 0.1643  0.0288  0.0495  84  PHE   A CD1 
278  C CD2 . PHE   A 41  ? 0.6885 0.9505 0.4877 0.1252  0.0639  0.0651  84  PHE   A CD2 
279  C CE1 . PHE   A 41  ? 0.7114 0.9540 0.4847 0.1748  0.0283  0.0580  84  PHE   A CE1 
280  C CE2 . PHE   A 41  ? 0.7144 0.9308 0.4824 0.1384  0.0618  0.0711  84  PHE   A CE2 
281  C CZ  . PHE   A 41  ? 0.7171 0.9242 0.4743 0.1605  0.0453  0.0680  84  PHE   A CZ  
282  N N   . SER   A 42  ? 0.6678 1.1710 0.6353 0.1269  0.0076  0.0050  85  SER   A N   
283  C CA  . SER   A 42  ? 0.6517 1.2433 0.6883 0.1215  0.0071  -0.0107 85  SER   A CA  
284  C C   . SER   A 42  ? 0.6671 1.3047 0.7198 0.1598  0.0033  -0.0184 85  SER   A C   
285  O O   . SER   A 42  ? 0.6971 1.2922 0.7054 0.1922  -0.0120 -0.0161 85  SER   A O   
286  C CB  . SER   A 42  ? 0.6527 1.2683 0.7148 0.1132  -0.0243 -0.0302 85  SER   A CB  
287  O OG  . SER   A 42  ? 0.7098 1.3039 0.7376 0.1500  -0.0589 -0.0389 85  SER   A OG  
288  N N   . LEU   A 43  ? 0.6433 1.3656 0.7586 0.1562  0.0187  -0.0275 86  LEU   A N   
289  C CA  . LEU   A 43  ? 0.6529 1.4243 0.7847 0.1964  0.0158  -0.0378 86  LEU   A CA  
290  C C   . LEU   A 43  ? 0.6657 1.4796 0.8234 0.2260  -0.0238 -0.0619 86  LEU   A C   
291  O O   . LEU   A 43  ? 0.6264 1.4947 0.8367 0.2088  -0.0374 -0.0777 86  LEU   A O   
292  C CB  . LEU   A 43  ? 0.6125 1.4586 0.7949 0.1864  0.0536  -0.0367 86  LEU   A CB  
293  C CG  . LEU   A 43  ? 0.6631 1.4654 0.8078 0.1718  0.0916  -0.0130 86  LEU   A CG  
294  C CD1 . LEU   A 43  ? 0.6289 1.5060 0.8171 0.1660  0.1300  -0.0114 86  LEU   A CD1 
295  C CD2 . LEU   A 43  ? 0.7218 1.4549 0.7993 0.2066  0.0829  -0.0059 86  LEU   A CD2 
296  N N   . VAL   A 44  ? 0.7195 1.5058 0.8392 0.2715  -0.0446 -0.0657 87  VAL   A N   
297  C CA  . VAL   A 44  ? 0.7406 1.5579 0.8727 0.3105  -0.0847 -0.0879 87  VAL   A CA  
298  C C   . VAL   A 44  ? 0.7396 1.6432 0.9221 0.3405  -0.0752 -0.1035 87  VAL   A C   
299  O O   . VAL   A 44  ? 0.7623 1.6498 0.9216 0.3554  -0.0531 -0.0945 87  VAL   A O   
300  C CB  . VAL   A 44  ? 0.8047 1.5261 0.8557 0.3434  -0.1124 -0.0802 87  VAL   A CB  
301  C CG1 . VAL   A 44  ? 0.8048 1.5497 0.8588 0.3904  -0.1551 -0.1020 87  VAL   A CG1 
302  C CG2 . VAL   A 44  ? 0.8513 1.4901 0.8501 0.3155  -0.1160 -0.0638 87  VAL   A CG2 
303  N N   . GLU   A 45  ? 0.7099 1.7086 0.9630 0.3502  -0.0915 -0.1287 88  GLU   A N   
304  C CA  . GLU   A 45  ? 0.6933 1.7854 1.0005 0.3821  -0.0816 -0.1466 88  GLU   A CA  
305  C C   . GLU   A 45  ? 0.6859 1.8262 1.0196 0.4289  -0.1285 -0.1764 88  GLU   A C   
306  O O   . GLU   A 45  ? 0.6667 1.8729 1.0326 0.4700  -0.1299 -0.1945 88  GLU   A O   
307  C CB  . GLU   A 45  ? 0.6793 1.8690 1.0695 0.3415  -0.0385 -0.1477 88  GLU   A CB  
308  C CG  . GLU   A 45  ? 0.7842 1.9269 1.1431 0.3028  0.0090  -0.1180 88  GLU   A CG  
309  C CD  . GLU   A 45  ? 0.8848 2.0451 1.2306 0.3266  0.0436  -0.1117 88  GLU   A CD  
310  O OE1 . GLU   A 45  ? 0.8848 2.0871 1.2402 0.3769  0.0302  -0.1305 88  GLU   A OE1 
311  O OE2 . GLU   A 45  ? 0.9399 2.0699 1.2619 0.2979  0.0826  -0.0889 88  GLU   A OE2 
312  N N   . GLY   B 7   ? 1.0985 1.0231 0.7182 0.2510  0.0546  -0.0553 16  GLY   B N   
313  C CA  . GLY   B 7   ? 1.1154 1.0241 0.7215 0.2674  0.0460  -0.0550 16  GLY   B CA  
314  C C   . GLY   B 7   ? 1.1081 1.0339 0.7309 0.2649  0.0381  -0.0547 16  GLY   B C   
315  O O   . GLY   B 7   ? 1.1002 1.0600 0.7519 0.2589  0.0362  -0.0606 16  GLY   B O   
316  N N   . GLU   B 8   ? 1.1039 1.0056 0.7079 0.2691  0.0336  -0.0478 17  GLU   B N   
317  C CA  . GLU   B 8   ? 1.0822 0.9958 0.6968 0.2694  0.0250  -0.0479 17  GLU   B CA  
318  C C   . GLU   B 8   ? 1.0438 0.9740 0.6784 0.2474  0.0267  -0.0449 17  GLU   B C   
319  O O   . GLU   B 8   ? 1.0560 0.9710 0.6810 0.2335  0.0327  -0.0358 17  GLU   B O   
320  C CB  . GLU   B 8   ? 1.1354 1.0193 0.7226 0.2798  0.0217  -0.0403 17  GLU   B CB  
321  C CG  . GLU   B 8   ? 1.1931 1.0898 0.7882 0.2879  0.0101  -0.0439 17  GLU   B CG  
322  C CD  . GLU   B 8   ? 1.3092 1.1783 0.8751 0.3015  0.0073  -0.0366 17  GLU   B CD  
323  O OE1 . GLU   B 8   ? 1.3444 1.1858 0.8877 0.2968  0.0166  -0.0255 17  GLU   B OE1 
324  O OE2 . GLU   B 8   ? 1.3400 1.2150 0.9049 0.3172  -0.0041 -0.0421 17  GLU   B OE2 
325  N N   A THR   B 9   ? 1.0181 0.9791 0.6805 0.2444  0.0210  -0.0529 18  THR   B N   
326  N N   B THR   B 9   ? 1.0165 0.9776 0.6790 0.2445  0.0210  -0.0529 18  THR   B N   
327  N N   C THR   B 9   ? 1.0181 0.9791 0.6805 0.2444  0.0210  -0.0529 18  THR   B N   
328  N N   D THR   B 9   ? 1.0165 0.9776 0.6790 0.2445  0.0210  -0.0529 18  THR   B N   
329  C CA  A THR   B 9   ? 1.0077 0.9817 0.6876 0.2241  0.0218  -0.0504 18  THR   B CA  
330  C CA  B THR   B 9   ? 1.0046 0.9793 0.6851 0.2245  0.0216  -0.0507 18  THR   B CA  
331  C CA  C THR   B 9   ? 1.0077 0.9817 0.6876 0.2241  0.0218  -0.0504 18  THR   B CA  
332  C CA  D THR   B 9   ? 1.0046 0.9793 0.6851 0.2245  0.0216  -0.0507 18  THR   B CA  
333  C C   A THR   B 9   ? 0.9959 0.9748 0.6827 0.2268  0.0091  -0.0528 18  THR   B C   
334  C C   B THR   B 9   ? 0.9943 0.9739 0.6816 0.2270  0.0090  -0.0531 18  THR   B C   
335  C C   C THR   B 9   ? 0.9959 0.9748 0.6827 0.2268  0.0091  -0.0528 18  THR   B C   
336  C C   D THR   B 9   ? 0.9943 0.9739 0.6816 0.2270  0.0090  -0.0531 18  THR   B C   
337  O O   A THR   B 9   ? 0.9886 0.9803 0.6928 0.2123  0.0068  -0.0536 18  THR   B O   
338  O O   B THR   B 9   ? 0.9869 0.9797 0.6921 0.2125  0.0067  -0.0540 18  THR   B O   
339  O O   C THR   B 9   ? 0.9886 0.9803 0.6928 0.2123  0.0068  -0.0536 18  THR   B O   
340  O O   D THR   B 9   ? 0.9869 0.9797 0.6921 0.2125  0.0067  -0.0540 18  THR   B O   
341  C CB  A THR   B 9   ? 1.0092 1.0118 0.7156 0.2119  0.0281  -0.0555 18  THR   B CB  
342  C CB  B THR   B 9   ? 1.0020 1.0064 0.7095 0.2140  0.0270  -0.0566 18  THR   B CB  
343  C CB  C THR   B 9   ? 1.0092 1.0118 0.7156 0.2119  0.0281  -0.0555 18  THR   B CB  
344  C CB  D THR   B 9   ? 1.0020 1.0064 0.7095 0.2140  0.0270  -0.0566 18  THR   B CB  
345  O OG1 A THR   B 9   ? 1.0245 1.0309 0.7278 0.2210  0.0349  -0.0594 18  THR   B OG1 
346  O OG1 B THR   B 9   ? 0.9979 1.0272 0.7236 0.2282  0.0203  -0.0680 18  THR   B OG1 
347  O OG1 C THR   B 9   ? 1.0245 1.0309 0.7278 0.2210  0.0349  -0.0594 18  THR   B OG1 
348  O OG1 D THR   B 9   ? 0.9979 1.0272 0.7236 0.2282  0.0203  -0.0680 18  THR   B OG1 
349  C CG2 A THR   B 9   ? 1.0153 1.0144 0.7232 0.1897  0.0360  -0.0478 18  THR   B CG2 
350  C CG2 B THR   B 9   ? 1.0142 1.0111 0.7119 0.2083  0.0401  -0.0530 18  THR   B CG2 
351  C CG2 C THR   B 9   ? 1.0153 1.0144 0.7232 0.1897  0.0360  -0.0478 18  THR   B CG2 
352  C CG2 D THR   B 9   ? 1.0142 1.0111 0.7119 0.2083  0.0401  -0.0530 18  THR   B CG2 
353  N N   . THR   B 10  ? 0.9937 0.9599 0.6642 0.2460  0.0006  -0.0541 19  THR   B N   
354  C CA  . THR   B 10  ? 0.9514 0.9193 0.6236 0.2523  -0.0127 -0.0574 19  THR   B CA  
355  C C   . THR   B 10  ? 0.9116 0.8632 0.5718 0.2409  -0.0106 -0.0478 19  THR   B C   
356  O O   . THR   B 10  ? 0.9182 0.8493 0.5575 0.2389  -0.0015 -0.0377 19  THR   B O   
357  C CB  . THR   B 10  ? 0.9803 0.9339 0.6306 0.2786  -0.0206 -0.0598 19  THR   B CB  
358  O OG1 . THR   B 10  ? 0.9889 0.9552 0.6465 0.2919  -0.0222 -0.0686 19  THR   B OG1 
359  C CG2 . THR   B 10  ? 0.9832 0.9385 0.6328 0.2890  -0.0361 -0.0652 19  THR   B CG2 
360  N N   . ASP   B 11  ? 0.8717 0.8321 0.5448 0.2339  -0.0198 -0.0513 20  ASP   B N   
361  C CA  . ASP   B 11  ? 0.8691 0.8145 0.5293 0.2270  -0.0204 -0.0438 20  ASP   B CA  
362  C C   . ASP   B 11  ? 0.8722 0.7955 0.5020 0.2442  -0.0206 -0.0371 20  ASP   B C   
363  O O   . ASP   B 11  ? 0.8753 0.7948 0.4951 0.2634  -0.0261 -0.0410 20  ASP   B O   
364  C CB  . ASP   B 11  ? 0.8810 0.8350 0.5555 0.2231  -0.0344 -0.0511 20  ASP   B CB  
365  C CG  . ASP   B 11  ? 0.9332 0.9016 0.6326 0.2007  -0.0323 -0.0532 20  ASP   B CG  
366  O OD1 . ASP   B 11  ? 0.9185 0.8976 0.6292 0.1901  -0.0207 -0.0515 20  ASP   B OD1 
367  O OD2 . ASP   B 11  ? 0.9780 0.9449 0.6834 0.1941  -0.0424 -0.0562 20  ASP   B OD2 
368  N N   . GLY   B 12  ? 0.8630 0.7729 0.4781 0.2375  -0.0133 -0.0268 21  GLY   B N   
369  C CA  . GLY   B 12  ? 0.8594 0.7511 0.4477 0.2510  -0.0104 -0.0187 21  GLY   B CA  
370  C C   . GLY   B 12  ? 0.8463 0.7288 0.4250 0.2392  0.0029  -0.0068 21  GLY   B C   
371  O O   . GLY   B 12  ? 0.8435 0.7323 0.4346 0.2216  0.0084  -0.0055 21  GLY   B O   
372  N N   . VAL   B 13  ? 0.8335 0.7018 0.3905 0.2490  0.0083  0.0018  22  VAL   B N   
373  C CA  . VAL   B 13  ? 0.8181 0.6797 0.3675 0.2385  0.0208  0.0131  22  VAL   B CA  
374  C C   . VAL   B 13  ? 0.8271 0.6750 0.3671 0.2388  0.0304  0.0178  22  VAL   B C   
375  O O   . VAL   B 13  ? 0.8416 0.6803 0.3708 0.2540  0.0277  0.0153  22  VAL   B O   
376  C CB  . VAL   B 13  ? 0.8115 0.6695 0.3453 0.2467  0.0215  0.0202  22  VAL   B CB  
377  C CG1 . VAL   B 13  ? 0.8237 0.6691 0.3352 0.2691  0.0196  0.0222  22  VAL   B CG1 
378  C CG2 . VAL   B 13  ? 0.7999 0.6574 0.3319 0.2339  0.0340  0.0309  22  VAL   B CG2 
379  N N   . TYR   B 14  ? 0.8257 0.6713 0.3700 0.2225  0.0400  0.0229  23  TYR   B N   
380  C CA  . TYR   B 14  ? 0.8327 0.6625 0.3687 0.2205  0.0477  0.0260  23  TYR   B CA  
381  C C   . TYR   B 14  ? 0.8459 0.6668 0.3758 0.2078  0.0584  0.0368  23  TYR   B C   
382  O O   . TYR   B 14  ? 0.8367 0.6695 0.3773 0.1948  0.0600  0.0387  23  TYR   B O   
383  C CB  . TYR   B 14  ? 0.8155 0.6527 0.3670 0.2107  0.0470  0.0180  23  TYR   B CB  
384  C CG  . TYR   B 14  ? 0.8029 0.6503 0.3633 0.2221  0.0386  0.0070  23  TYR   B CG  
385  C CD1 . TYR   B 14  ? 0.7960 0.6615 0.3705 0.2239  0.0293  0.0004  23  TYR   B CD1 
386  C CD2 . TYR   B 14  ? 0.8091 0.6493 0.3654 0.2299  0.0394  0.0023  23  TYR   B CD2 
387  C CE1 . TYR   B 14  ? 0.7993 0.6776 0.3858 0.2330  0.0210  -0.0102 23  TYR   B CE1 
388  C CE2 . TYR   B 14  ? 0.8148 0.6694 0.3822 0.2410  0.0314  -0.0085 23  TYR   B CE2 
389  C CZ  . TYR   B 14  ? 0.8192 0.6946 0.4037 0.2416  0.0223  -0.0148 23  TYR   B CZ  
390  O OH  . TYR   B 14  ? 0.8449 0.7385 0.4450 0.2505  0.0142  -0.0261 23  TYR   B OH  
391  N N   . ARG   B 15  ? 0.8593 0.6586 0.3733 0.2103  0.0653  0.0428  24  ARG   B N   
392  C CA  . ARG   B 15  ? 0.8648 0.6542 0.3754 0.1956  0.0755  0.0525  24  ARG   B CA  
393  C C   . ARG   B 15  ? 0.8585 0.6450 0.3786 0.1807  0.0763  0.0474  24  ARG   B C   
394  O O   . ARG   B 15  ? 0.8638 0.6434 0.3820 0.1866  0.0728  0.0400  24  ARG   B O   
395  C CB  . ARG   B 15  ? 0.8925 0.6546 0.3792 0.2036  0.0828  0.0618  24  ARG   B CB  
396  C CG  . ARG   B 15  ? 0.9175 0.6776 0.3882 0.2221  0.0827  0.0670  24  ARG   B CG  
397  C CD  . ARG   B 15  ? 0.9510 0.6795 0.3936 0.2317  0.0901  0.0763  24  ARG   B CD  
398  N NE  . ARG   B 15  ? 0.9675 0.6933 0.3913 0.2532  0.0887  0.0800  24  ARG   B NE  
399  C CZ  . ARG   B 15  ? 0.9713 0.7026 0.3883 0.2542  0.0966  0.0906  24  ARG   B CZ  
400  N NH1 . ARG   B 15  ? 0.9394 0.6808 0.3690 0.2344  0.1067  0.0989  24  ARG   B NH1 
401  N NH2 . ARG   B 15  ? 0.9844 0.7124 0.3817 0.2763  0.0941  0.0925  24  ARG   B NH2 
402  N N   . VAL   B 16  ? 0.8496 0.6418 0.3790 0.1629  0.0806  0.0512  25  VAL   B N   
403  C CA  . VAL   B 16  ? 0.8566 0.6437 0.3919 0.1487  0.0811  0.0470  25  VAL   B CA  
404  C C   . VAL   B 16  ? 0.8860 0.6494 0.4099 0.1404  0.0885  0.0551  25  VAL   B C   
405  O O   . VAL   B 16  ? 0.8790 0.6473 0.4062 0.1317  0.0940  0.0637  25  VAL   B O   
406  C CB  . VAL   B 16  ? 0.8500 0.6588 0.4025 0.1349  0.0789  0.0444  25  VAL   B CB  
407  C CG1 . VAL   B 16  ? 0.8483 0.6493 0.4031 0.1228  0.0786  0.0391  25  VAL   B CG1 
408  C CG2 . VAL   B 16  ? 0.8411 0.6703 0.4031 0.1417  0.0723  0.0385  25  VAL   B CG2 
409  N N   . MET   B 17  ? 0.9189 0.6565 0.4292 0.1435  0.0887  0.0524  26  MET   B N   
410  C CA  . MET   B 17  ? 0.9537 0.6617 0.4497 0.1357  0.0949  0.0601  26  MET   B CA  
411  C C   . MET   B 17  ? 0.9890 0.6834 0.4864 0.1214  0.0930  0.0545  26  MET   B C   
412  O O   . MET   B 17  ? 0.9803 0.6824 0.4829 0.1238  0.0874  0.0441  26  MET   B O   
413  C CB  . MET   B 17  ? 0.9711 0.6506 0.4424 0.1539  0.0955  0.0617  26  MET   B CB  
414  C CG  . MET   B 17  ? 0.9632 0.6525 0.4286 0.1727  0.0948  0.0645  26  MET   B CG  
415  S SD  . MET   B 17  ? 0.9761 0.6703 0.4389 0.1678  0.1047  0.0802  26  MET   B SD  
416  C CE  . MET   B 17  ? 0.9594 0.6122 0.4015 0.1572  0.1146  0.0914  26  MET   B CE  
417  N N   . THR   B 18  ? 1.0243 0.6958 0.5150 0.1075  0.0978  0.0613  27  THR   B N   
418  C CA  . THR   B 18  ? 1.0625 0.7133 0.5497 0.0952  0.0947  0.0557  27  THR   B CA  
419  C C   . THR   B 18  ? 1.1111 0.7186 0.5762 0.0913  0.0992  0.0629  27  THR   B C   
420  O O   . THR   B 18  ? 1.1099 0.7111 0.5714 0.0869  0.1072  0.0753  27  THR   B O   
421  C CB  . THR   B 18  ? 1.0685 0.7414 0.5776 0.0751  0.0925  0.0534  27  THR   B CB  
422  O OG1 . THR   B 18  ? 1.0913 0.7394 0.5935 0.0643  0.0882  0.0472  27  THR   B OG1 
423  C CG2 . THR   B 18  ? 1.0606 0.7486 0.5832 0.0617  0.0993  0.0648  27  THR   B CG2 
424  N N   . ARG   B 19  ? 1.1518 0.7280 0.6004 0.0933  0.0943  0.0555  28  ARG   B N   
425  C CA  . ARG   B 19  ? 1.2079 0.7362 0.6326 0.0884  0.0969  0.0611  28  ARG   B CA  
426  C C   . ARG   B 19  ? 1.2315 0.7452 0.6628 0.0632  0.0942  0.0594  28  ARG   B C   
427  O O   . ARG   B 19  ? 1.2516 0.7219 0.6632 0.0562  0.0946  0.0625  28  ARG   B O   
428  C CB  . ARG   B 19  ? 1.2575 0.7541 0.6542 0.1103  0.0920  0.0536  28  ARG   B CB  
429  C CG  . ARG   B 19  ? 1.3130 0.8228 0.7034 0.1358  0.0925  0.0534  28  ARG   B CG  
430  C CD  . ARG   B 19  ? 1.4005 0.8695 0.7594 0.1487  0.0963  0.0621  28  ARG   B CD  
431  N NE  . ARG   B 19  ? 1.4607 0.9425 0.8129 0.1748  0.0948  0.0606  28  ARG   B NE  
432  C CZ  . ARG   B 19  ? 1.5079 0.9895 0.8514 0.1971  0.0874  0.0490  28  ARG   B CZ  
433  N NH1 . ARG   B 19  ? 1.5109 0.9803 0.8497 0.1978  0.0820  0.0381  28  ARG   B NH1 
434  N NH2 . ARG   B 19  ? 1.5085 1.0044 0.8488 0.2194  0.0851  0.0473  28  ARG   B NH2 
435  N N   . ARG   B 20  ? 1.2329 0.7809 0.6903 0.0500  0.0906  0.0541  29  ARG   B N   
436  C CA  . ARG   B 20  ? 1.2576 0.7994 0.7250 0.0275  0.0853  0.0496  29  ARG   B CA  
437  C C   . ARG   B 20  ? 1.2663 0.8020 0.7437 0.0046  0.0922  0.0620  29  ARG   B C   
438  O O   . ARG   B 20  ? 1.2867 0.7935 0.7600 -0.0130 0.0889  0.0609  29  ARG   B O   
439  C CB  . ARG   B 20  ? 1.2706 0.8540 0.7614 0.0243  0.0792  0.0405  29  ARG   B CB  
440  C CG  . ARG   B 20  ? 1.3471 0.9249 0.8454 0.0057  0.0705  0.0321  29  ARG   B CG  
441  C CD  . ARG   B 20  ? 1.3986 1.0169 0.9170 0.0046  0.0649  0.0244  29  ARG   B CD  
442  N NE  . ARG   B 20  ? 1.4398 1.0986 0.9805 0.0031  0.0708  0.0325  29  ARG   B NE  
443  C CZ  . ARG   B 20  ? 1.4655 1.1457 1.0284 -0.0143 0.0720  0.0375  29  ARG   B CZ  
444  N NH1 . ARG   B 20  ? 1.4732 1.1393 1.0419 -0.0342 0.0674  0.0353  29  ARG   B NH1 
445  N NH2 . ARG   B 20  ? 1.4438 1.1604 1.0239 -0.0117 0.0772  0.0442  29  ARG   B NH2 
446  N N   . LEU   B 21  ? 1.2452 0.8074 0.7350 0.0049  0.1021  0.0738  30  LEU   B N   
447  C CA  . LEU   B 21  ? 1.2368 0.7999 0.7382 -0.0157 0.1116  0.0873  30  LEU   B CA  
448  C C   . LEU   B 21  ? 1.2470 0.7645 0.7188 -0.0110 0.1211  0.0999  30  LEU   B C   
449  O O   . LEU   B 21  ? 1.2652 0.7462 0.7077 0.0056  0.1168  0.0952  30  LEU   B O   
450  C CB  . LEU   B 21  ? 1.2201 0.8355 0.7469 -0.0142 0.1180  0.0934  30  LEU   B CB  
451  C CG  . LEU   B 21  ? 1.2212 0.8807 0.7815 -0.0288 0.1128  0.0876  30  LEU   B CG  
452  C CD1 . LEU   B 21  ? 1.2312 0.8836 0.7942 -0.0355 0.0987  0.0720  30  LEU   B CD1 
453  C CD2 . LEU   B 21  ? 1.2141 0.9168 0.7866 -0.0133 0.1136  0.0871  30  LEU   B CD2 
454  N N   . LEU   B 22  ? 1.2309 0.7498 0.7086 -0.0248 0.1340  0.1158  31  LEU   B N   
455  C CA  . LEU   B 22  ? 1.2510 0.7256 0.6977 -0.0198 0.1442  0.1294  31  LEU   B CA  
456  C C   . LEU   B 22  ? 1.2576 0.7376 0.6851 0.0117  0.1469  0.1315  31  LEU   B C   
457  O O   . LEU   B 22  ? 1.2472 0.7726 0.6930 0.0207  0.1481  0.1307  31  LEU   B O   
458  C CB  . LEU   B 22  ? 1.2406 0.7207 0.7004 -0.0428 0.1593  0.1469  31  LEU   B CB  
459  C CG  . LEU   B 22  ? 1.2720 0.7019 0.6977 -0.0409 0.1713  0.1629  31  LEU   B CG  
460  C CD1 . LEU   B 22  ? 1.2874 0.6669 0.7024 -0.0646 0.1692  0.1641  31  LEU   B CD1 
461  C CD2 . LEU   B 22  ? 1.2706 0.7253 0.7042 -0.0440 0.1898  0.1814  31  LEU   B CD2 
462  N N   . GLY   B 23  ? 1.2700 0.7034 0.6604 0.0292  0.1460  0.1325  32  GLY   B N   
463  C CA  . GLY   B 23  ? 1.2645 0.6985 0.6343 0.0606  0.1460  0.1326  32  GLY   B CA  
464  C C   . GLY   B 23  ? 1.2279 0.7026 0.6146 0.0771  0.1354  0.1174  32  GLY   B C   
465  O O   . GLY   B 23  ? 1.2180 0.7038 0.6196 0.0703  0.1258  0.1044  32  GLY   B O   
466  N N   . SER   B 24  ? 1.2078 0.7042 0.5916 0.0985  0.1368  0.1190  33  SER   B N   
467  C CA  . SER   B 24  ? 1.1805 0.7166 0.5824 0.1120  0.1275  0.1060  33  SER   B CA  
468  C C   . SER   B 24  ? 1.1395 0.7190 0.5666 0.1043  0.1331  0.1120  33  SER   B C   
469  O O   . SER   B 24  ? 1.1395 0.7216 0.5578 0.1121  0.1415  0.1232  33  SER   B O   
470  C CB  . SER   B 24  ? 1.2147 0.7432 0.5956 0.1423  0.1228  0.1016  33  SER   B CB  
471  O OG  . SER   B 24  ? 1.2678 0.7540 0.6218 0.1524  0.1184  0.0970  33  SER   B OG  
472  N N   . THR   B 25  ? 1.1030 0.7143 0.5591 0.0891  0.1287  0.1050  34  THR   B N   
473  C CA  . THR   B 25  ? 1.0678 0.7207 0.5485 0.0813  0.1328  0.1095  34  THR   B CA  
474  C C   . THR   B 25  ? 1.0333 0.7205 0.5265 0.0956  0.1245  0.0996  34  THR   B C   
475  O O   . THR   B 25  ? 1.0355 0.7264 0.5343 0.0971  0.1150  0.0872  34  THR   B O   
476  C CB  . THR   B 25  ? 1.0699 0.7335 0.5736 0.0536  0.1339  0.1100  34  THR   B CB  
477  O OG1 . THR   B 25  ? 1.0969 0.7291 0.5902 0.0385  0.1430  0.1212  34  THR   B OG1 
478  C CG2 . THR   B 25  ? 1.0442 0.7546 0.5751 0.0472  0.1364  0.1123  34  THR   B CG2 
479  N N   . GLN   B 26  ? 0.9981 0.7088 0.4943 0.1062  0.1281  0.1051  35  GLN   B N   
480  C CA  . GLN   B 26  ? 0.9696 0.7101 0.4772 0.1181  0.1196  0.0961  35  GLN   B CA  
481  C C   . GLN   B 26  ? 0.9488 0.7214 0.4826 0.1027  0.1176  0.0932  35  GLN   B C   
482  O O   . GLN   B 26  ? 0.9487 0.7378 0.4923 0.0943  0.1250  0.1018  35  GLN   B O   
483  C CB  . GLN   B 26  ? 0.9560 0.7050 0.4528 0.1381  0.1218  0.1012  35  GLN   B CB  
484  C CG  . GLN   B 26  ? 0.9396 0.7152 0.4475 0.1491  0.1115  0.0912  35  GLN   B CG  
485  C CD  . GLN   B 26  ? 0.9773 0.7577 0.4723 0.1702  0.1110  0.0942  35  GLN   B CD  
486  O OE1 . GLN   B 26  ? 1.0087 0.7673 0.4823 0.1853  0.1117  0.0963  35  GLN   B OE1 
487  N NE2 . GLN   B 26  ? 0.9608 0.7679 0.4661 0.1734  0.1089  0.0937  35  GLN   B NE2 
488  N N   . VAL   B 27  ? 0.9262 0.7081 0.4705 0.0998  0.1080  0.0814  36  VAL   B N   
489  C CA  . VAL   B 27  ? 0.9039 0.7133 0.4694 0.0876  0.1044  0.0776  36  VAL   B CA  
490  C C   . VAL   B 27  ? 0.8778 0.7141 0.4503 0.0992  0.0988  0.0737  36  VAL   B C   
491  O O   . VAL   B 27  ? 0.8708 0.7310 0.4579 0.0927  0.0967  0.0727  36  VAL   B O   
492  C CB  . VAL   B 27  ? 0.9141 0.7154 0.4848 0.0750  0.0981  0.0683  36  VAL   B CB  
493  C CG1 . VAL   B 27  ? 0.9346 0.7160 0.5044 0.0581  0.1025  0.0727  36  VAL   B CG1 
494  C CG2 . VAL   B 27  ? 0.9205 0.7067 0.4798 0.0863  0.0923  0.0592  36  VAL   B CG2 
495  N N   . GLY   B 28  ? 0.8597 0.6910 0.4216 0.1163  0.0954  0.0708  37  GLY   B N   
496  C CA  . GLY   B 28  ? 0.8325 0.6835 0.3990 0.1267  0.0889  0.0664  37  GLY   B CA  
497  C C   . GLY   B 28  ? 0.8189 0.6617 0.3745 0.1443  0.0842  0.0624  37  GLY   B C   
498  O O   . GLY   B 28  ? 0.8196 0.6428 0.3621 0.1517  0.0867  0.0641  37  GLY   B O   
499  N N   . VAL   B 29  ? 0.8068 0.6641 0.3675 0.1513  0.0765  0.0567  38  VAL   B N   
500  C CA  . VAL   B 29  ? 0.8130 0.6683 0.3678 0.1673  0.0696  0.0514  38  VAL   B CA  
501  C C   . VAL   B 29  ? 0.8033 0.6693 0.3701 0.1634  0.0611  0.0419  38  VAL   B C   
502  O O   . VAL   B 29  ? 0.8100 0.6856 0.3851 0.1526  0.0605  0.0413  38  VAL   B O   
503  C CB  . VAL   B 29  ? 0.8198 0.6815 0.3658 0.1815  0.0691  0.0564  38  VAL   B CB  
504  C CG1 . VAL   B 29  ? 0.8325 0.6895 0.3703 0.1993  0.0606  0.0504  38  VAL   B CG1 
505  C CG2 . VAL   B 29  ? 0.8299 0.6848 0.3652 0.1826  0.0804  0.0681  38  VAL   B CG2 
506  N N   . GLY   B 30  ? 0.7901 0.6547 0.3573 0.1723  0.0547  0.0349  39  GLY   B N   
507  C CA  . GLY   B 30  ? 0.7744 0.6488 0.3534 0.1678  0.0480  0.0271  39  GLY   B CA  
508  C C   . GLY   B 30  ? 0.7669 0.6447 0.3480 0.1798  0.0391  0.0204  39  GLY   B C   
509  O O   . GLY   B 30  ? 0.7791 0.6506 0.3509 0.1940  0.0374  0.0206  39  GLY   B O   
510  N N   . VAL   B 31  ? 0.7473 0.6339 0.3399 0.1740  0.0332  0.0144  40  VAL   B N   
511  C CA  . VAL   B 31  ? 0.7421 0.6340 0.3412 0.1818  0.0232  0.0068  40  VAL   B CA  
512  C C   . VAL   B 31  ? 0.7370 0.6373 0.3517 0.1753  0.0232  -0.0003 40  VAL   B C   
513  O O   . VAL   B 31  ? 0.7303 0.6345 0.3523 0.1615  0.0275  -0.0001 40  VAL   B O   
514  C CB  . VAL   B 31  ? 0.7423 0.6363 0.3416 0.1800  0.0153  0.0061  40  VAL   B CB  
515  C CG1 . VAL   B 31  ? 0.7388 0.6373 0.3478 0.1838  0.0038  -0.0028 40  VAL   B CG1 
516  C CG2 . VAL   B 31  ? 0.7459 0.6351 0.3296 0.1902  0.0150  0.0122  40  VAL   B CG2 
517  N N   . MET   B 32  ? 0.7383 0.6430 0.3580 0.1860  0.0184  -0.0068 41  MET   B N   
518  C CA  . MET   B 32  ? 0.7406 0.6590 0.3786 0.1810  0.0185  -0.0143 41  MET   B CA  
519  C C   . MET   B 32  ? 0.7574 0.6872 0.4105 0.1791  0.0078  -0.0211 41  MET   B C   
520  O O   . MET   B 32  ? 0.7667 0.6947 0.4160 0.1917  -0.0025 -0.0246 41  MET   B O   
521  C CB  . MET   B 32  ? 0.7405 0.6592 0.3766 0.1946  0.0193  -0.0185 41  MET   B CB  
522  C CG  . MET   B 32  ? 0.7666 0.7023 0.4211 0.1903  0.0221  -0.0257 41  MET   B CG  
523  S SD  . MET   B 32  ? 0.8725 0.8053 0.5253 0.1751  0.0359  -0.0213 41  MET   B SD  
524  C CE  . MET   B 32  ? 0.9106 0.8240 0.5429 0.1883  0.0403  -0.0193 41  MET   B CE  
525  N N   . GLN   B 33  ? 0.7559 0.6945 0.4234 0.1631  0.0097  -0.0223 42  GLN   B N   
526  C CA  . GLN   B 33  ? 0.7627 0.7095 0.4454 0.1579  -0.0003 -0.0283 42  GLN   B CA  
527  C C   . GLN   B 33  ? 0.7733 0.7354 0.4768 0.1420  0.0056  -0.0307 42  GLN   B C   
528  O O   . GLN   B 33  ? 0.7868 0.7445 0.4857 0.1299  0.0154  -0.0247 42  GLN   B O   
529  C CB  . GLN   B 33  ? 0.7867 0.7188 0.4571 0.1551  -0.0066 -0.0244 42  GLN   B CB  
530  C CG  . GLN   B 33  ? 0.8347 0.7701 0.5180 0.1515  -0.0196 -0.0317 42  GLN   B CG  
531  C CD  . GLN   B 33  ? 0.9165 0.8339 0.5830 0.1549  -0.0290 -0.0297 42  GLN   B CD  
532  O OE1 . GLN   B 33  ? 0.9337 0.8440 0.6029 0.1429  -0.0334 -0.0299 42  GLN   B OE1 
533  N NE2 . GLN   B 33  ? 0.9317 0.8400 0.5787 0.1719  -0.0319 -0.0273 42  GLN   B NE2 
534  N N   . GLU   B 34  ? 0.7650 0.7463 0.4914 0.1423  -0.0003 -0.0396 43  GLU   B N   
535  C CA  . GLU   B 34  ? 0.7613 0.7626 0.5116 0.1270  0.0063  -0.0421 43  GLU   B CA  
536  C C   . GLU   B 34  ? 0.7610 0.7686 0.5092 0.1250  0.0219  -0.0387 43  GLU   B C   
537  O O   . GLU   B 34  ? 0.7728 0.7846 0.5261 0.1101  0.0318  -0.0349 43  GLU   B O   
538  C CB  . GLU   B 34  ? 0.7980 0.7912 0.5513 0.1082  0.0053  -0.0382 43  GLU   B CB  
539  C CG  . GLU   B 34  ? 0.8584 0.8426 0.6126 0.1101  -0.0115 -0.0428 43  GLU   B CG  
540  C CD  . GLU   B 34  ? 0.9764 0.9386 0.7181 0.0972  -0.0138 -0.0368 43  GLU   B CD  
541  O OE1 . GLU   B 34  ? 0.9741 0.9391 0.7269 0.0786  -0.0076 -0.0342 43  GLU   B OE1 
542  O OE2 . GLU   B 34  ? 1.0484 0.9900 0.7679 0.1068  -0.0215 -0.0345 43  GLU   B OE2 
543  N N   . GLY   B 35  ? 0.7514 0.7568 0.4894 0.1407  0.0236  -0.0400 44  GLY   B N   
544  C CA  . GLY   B 35  ? 0.7414 0.7492 0.4741 0.1423  0.0361  -0.0384 44  GLY   B CA  
545  C C   . GLY   B 35  ? 0.7425 0.7288 0.4527 0.1353  0.0445  -0.0293 44  GLY   B C   
546  O O   . GLY   B 35  ? 0.7541 0.7405 0.4590 0.1343  0.0544  -0.0283 44  GLY   B O   
547  N N   . VAL   B 36  ? 0.7271 0.6958 0.4239 0.1315  0.0397  -0.0234 45  VAL   B N   
548  C CA  . VAL   B 36  ? 0.7241 0.6753 0.4021 0.1246  0.0454  -0.0156 45  VAL   B CA  
549  C C   . VAL   B 36  ? 0.7201 0.6547 0.3802 0.1343  0.0416  -0.0116 45  VAL   B C   
550  O O   . VAL   B 36  ? 0.7234 0.6554 0.3820 0.1418  0.0329  -0.0121 45  VAL   B O   
551  C CB  . VAL   B 36  ? 0.7290 0.6767 0.4074 0.1098  0.0452  -0.0116 45  VAL   B CB  
552  C CG1 . VAL   B 36  ? 0.7493 0.6798 0.4076 0.1056  0.0481  -0.0045 45  VAL   B CG1 
553  C CG2 . VAL   B 36  ? 0.7194 0.6818 0.4128 0.0983  0.0531  -0.0132 45  VAL   B CG2 
554  N N   . PHE   B 37  ? 0.7132 0.6369 0.3598 0.1346  0.0482  -0.0078 46  PHE   B N   
555  C CA  . PHE   B 37  ? 0.7241 0.6335 0.3557 0.1411  0.0468  -0.0028 46  PHE   B CA  
556  C C   . PHE   B 37  ? 0.7212 0.6244 0.3452 0.1319  0.0470  0.0032  46  PHE   B C   
557  O O   . PHE   B 37  ? 0.7181 0.6202 0.3403 0.1222  0.0517  0.0042  46  PHE   B O   
558  C CB  . PHE   B 37  ? 0.7278 0.6270 0.3497 0.1460  0.0526  -0.0023 46  PHE   B CB  
559  C CG  . PHE   B 37  ? 0.7351 0.6202 0.3435 0.1528  0.0519  0.0033  46  PHE   B CG  
560  C CD1 . PHE   B 37  ? 0.7391 0.6235 0.3448 0.1660  0.0465  0.0030  46  PHE   B CD1 
561  C CD2 . PHE   B 37  ? 0.7462 0.6199 0.3448 0.1455  0.0565  0.0092  46  PHE   B CD2 
562  C CE1 . PHE   B 37  ? 0.7547 0.6259 0.3460 0.1724  0.0478  0.0096  46  PHE   B CE1 
563  C CE2 . PHE   B 37  ? 0.7629 0.6261 0.3512 0.1498  0.0576  0.0156  46  PHE   B CE2 
564  C CZ  . PHE   B 37  ? 0.7632 0.6247 0.3469 0.1634  0.0542  0.0164  46  PHE   B CZ  
565  N N   . HIS   B 38  ? 0.7158 0.6159 0.3346 0.1365  0.0416  0.0065  47  HIS   B N   
566  C CA  . HIS   B 38  ? 0.7157 0.6128 0.3279 0.1307  0.0404  0.0111  47  HIS   B CA  
567  C C   . HIS   B 38  ? 0.7271 0.6194 0.3302 0.1347  0.0429  0.0168  47  HIS   B C   
568  O O   . HIS   B 38  ? 0.7236 0.6140 0.3229 0.1453  0.0416  0.0181  47  HIS   B O   
569  C CB  . HIS   B 38  ? 0.7122 0.6105 0.3250 0.1343  0.0314  0.0100  47  HIS   B CB  
570  C CG  . HIS   B 38  ? 0.7234 0.6263 0.3476 0.1293  0.0279  0.0047  47  HIS   B CG  
571  N ND1 . HIS   B 38  ? 0.7376 0.6485 0.3735 0.1341  0.0264  -0.0010 47  HIS   B ND1 
572  C CD2 . HIS   B 38  ? 0.7365 0.6373 0.3622 0.1198  0.0257  0.0046  47  HIS   B CD2 
573  C CE1 . HIS   B 38  ? 0.7332 0.6498 0.3808 0.1256  0.0241  -0.0045 47  HIS   B CE1 
574  N NE2 . HIS   B 38  ? 0.7412 0.6499 0.3821 0.1162  0.0240  -0.0007 47  HIS   B NE2 
575  N N   . THR   B 39  ? 0.7326 0.6236 0.3322 0.1264  0.0466  0.0201  48  THR   B N   
576  C CA  . THR   B 39  ? 0.7370 0.6270 0.3318 0.1275  0.0497  0.0258  48  THR   B CA  
577  C C   . THR   B 39  ? 0.7269 0.6223 0.3214 0.1196  0.0489  0.0278  48  THR   B C   
578  O O   . THR   B 39  ? 0.7120 0.6083 0.3061 0.1153  0.0455  0.0252  48  THR   B O   
579  C CB  . THR   B 39  ? 0.7593 0.6399 0.3517 0.1271  0.0559  0.0268  48  THR   B CB  
580  O OG1 . THR   B 39  ? 0.7739 0.6533 0.3626 0.1274  0.0596  0.0336  48  THR   B OG1 
581  C CG2 . THR   B 39  ? 0.7661 0.6415 0.3591 0.1172  0.0588  0.0233  48  THR   B CG2 
582  N N   . MET   B 40  ? 0.7291 0.6288 0.3236 0.1183  0.0519  0.0328  49  MET   B N   
583  C CA  . MET   B 40  ? 0.7305 0.6389 0.3270 0.1116  0.0503  0.0336  49  MET   B CA  
584  C C   . MET   B 40  ? 0.7495 0.6523 0.3476 0.1000  0.0529  0.0312  49  MET   B C   
585  O O   . MET   B 40  ? 0.7647 0.6575 0.3624 0.0976  0.0575  0.0314  49  MET   B O   
586  C CB  . MET   B 40  ? 0.7248 0.6456 0.3238 0.1156  0.0521  0.0393  49  MET   B CB  
587  C CG  . MET   B 40  ? 0.7534 0.6767 0.3469 0.1300  0.0494  0.0410  49  MET   B CG  
588  S SD  . MET   B 40  ? 0.8581 0.8005 0.4517 0.1376  0.0474  0.0446  49  MET   B SD  
589  C CE  . MET   B 40  ? 0.7798 0.7204 0.3689 0.1368  0.0373  0.0386  49  MET   B CE  
590  N N   A TRP   B 41  ? 0.7481 0.6547 0.3455 0.0941  0.0490  0.0284  50  TRP   B N   
591  N N   B TRP   B 41  ? 0.7439 0.6505 0.3412 0.0941  0.0490  0.0284  50  TRP   B N   
592  N N   C TRP   B 41  ? 0.7481 0.6547 0.3455 0.0941  0.0490  0.0284  50  TRP   B N   
593  N N   D TRP   B 41  ? 0.7452 0.6517 0.3425 0.0941  0.0490  0.0283  50  TRP   B N   
594  C CA  A TRP   B 41  ? 0.7597 0.6601 0.3559 0.0845  0.0494  0.0247  50  TRP   B CA  
595  C CA  B TRP   B 41  ? 0.7512 0.6516 0.3475 0.0844  0.0494  0.0247  50  TRP   B CA  
596  C CA  C TRP   B 41  ? 0.7597 0.6601 0.3559 0.0845  0.0494  0.0247  50  TRP   B CA  
597  C CA  D TRP   B 41  ? 0.7539 0.6542 0.3501 0.0844  0.0494  0.0247  50  TRP   B CA  
598  C C   A TRP   B 41  ? 0.7595 0.6614 0.3626 0.0772  0.0522  0.0269  50  TRP   B C   
599  C C   B TRP   B 41  ? 0.7555 0.6575 0.3587 0.0771  0.0521  0.0268  50  TRP   B C   
600  C C   C TRP   B 41  ? 0.7595 0.6614 0.3626 0.0772  0.0522  0.0269  50  TRP   B C   
601  C C   D TRP   B 41  ? 0.7567 0.6587 0.3598 0.0771  0.0521  0.0268  50  TRP   B C   
602  O O   A TRP   B 41  ? 0.7664 0.6554 0.3670 0.0711  0.0541  0.0243  50  TRP   B O   
603  O O   B TRP   B 41  ? 0.7624 0.6515 0.3631 0.0709  0.0540  0.0242  50  TRP   B O   
604  O O   C TRP   B 41  ? 0.7664 0.6554 0.3670 0.0711  0.0541  0.0243  50  TRP   B O   
605  O O   D TRP   B 41  ? 0.7635 0.6525 0.3642 0.0710  0.0540  0.0242  50  TRP   B O   
606  C CB  A TRP   B 41  ? 0.7627 0.6665 0.3539 0.0820  0.0435  0.0213  50  TRP   B CB  
607  C CB  B TRP   B 41  ? 0.7484 0.6523 0.3395 0.0821  0.0434  0.0212  50  TRP   B CB  
608  C CB  C TRP   B 41  ? 0.7627 0.6665 0.3539 0.0820  0.0435  0.0213  50  TRP   B CB  
609  C CB  D TRP   B 41  ? 0.7530 0.6563 0.3439 0.0820  0.0436  0.0211  50  TRP   B CB  
610  C CG  A TRP   B 41  ? 0.7797 0.6738 0.3652 0.0748  0.0431  0.0162  50  TRP   B CG  
611  C CG  B TRP   B 41  ? 0.7558 0.6523 0.3428 0.0741  0.0424  0.0164  50  TRP   B CG  
612  C CG  C TRP   B 41  ? 0.7797 0.6738 0.3652 0.0748  0.0431  0.0162  50  TRP   B CG  
613  C CG  D TRP   B 41  ? 0.7629 0.6582 0.3493 0.0741  0.0428  0.0162  50  TRP   B CG  
614  C CD1 A TRP   B 41  ? 0.7991 0.6815 0.3752 0.0749  0.0453  0.0128  50  TRP   B CD1 
615  C CD1 B TRP   B 41  ? 0.7626 0.6643 0.3550 0.0669  0.0394  0.0146  50  TRP   B CD1 
616  C CD1 C TRP   B 41  ? 0.7991 0.6815 0.3752 0.0749  0.0453  0.0128  50  TRP   B CD1 
617  C CD1 D TRP   B 41  ? 0.7710 0.6702 0.3625 0.0667  0.0401  0.0143  50  TRP   B CD1 
618  C CD2 A TRP   B 41  ? 0.7832 0.6787 0.3719 0.0668  0.0405  0.0134  50  TRP   B CD2 
619  C CD2 B TRP   B 41  ? 0.7627 0.6456 0.3396 0.0729  0.0443  0.0122  50  TRP   B CD2 
620  C CD2 C TRP   B 41  ? 0.7832 0.6787 0.3719 0.0668  0.0405  0.0134  50  TRP   B CD2 
621  C CD2 D TRP   B 41  ? 0.7711 0.6536 0.3470 0.0733  0.0444  0.0120  50  TRP   B CD2 
622  N NE1 A TRP   B 41  ? 0.8097 0.6844 0.3796 0.0694  0.0439  0.0080  50  TRP   B NE1 
623  N NE1 B TRP   B 41  ? 0.7708 0.6600 0.3548 0.0620  0.0378  0.0088  50  TRP   B NE1 
624  N NE1 C TRP   B 41  ? 0.8097 0.6844 0.3796 0.0694  0.0439  0.0080  50  TRP   B NE1 
625  N NE1 D TRP   B 41  ? 0.7802 0.6667 0.3628 0.0622  0.0386  0.0085  50  TRP   B NE1 
626  C CE2 A TRP   B 41  ? 0.8019 0.6834 0.3797 0.0640  0.0400  0.0078  50  TRP   B CE2 
627  C CE2 B TRP   B 41  ? 0.7747 0.6525 0.3479 0.0665  0.0415  0.0075  50  TRP   B CE2 
628  C CE2 C TRP   B 41  ? 0.8019 0.6834 0.3797 0.0640  0.0400  0.0078  50  TRP   B CE2 
629  C CE2 D TRP   B 41  ? 0.7841 0.6607 0.3559 0.0670  0.0419  0.0073  50  TRP   B CE2 
630  C CE3 A TRP   B 41  ? 0.7833 0.6920 0.3842 0.0615  0.0383  0.0149  50  TRP   B CE3 
631  C CE3 B TRP   B 41  ? 0.7733 0.6497 0.3447 0.0766  0.0482  0.0116  50  TRP   B CE3 
632  C CE3 C TRP   B 41  ? 0.7833 0.6920 0.3842 0.0615  0.0383  0.0149  50  TRP   B CE3 
633  C CE3 D TRP   B 41  ? 0.7819 0.6586 0.3521 0.0770  0.0478  0.0117  50  TRP   B CE3 
634  C CZ2 A TRP   B 41  ? 0.8136 0.6905 0.3903 0.0567  0.0357  0.0026  50  TRP   B CZ2 
635  C CZ2 B TRP   B 41  ? 0.7896 0.6539 0.3504 0.0658  0.0426  0.0024  50  TRP   B CZ2 
636  C CZ2 C TRP   B 41  ? 0.8136 0.6905 0.3903 0.0567  0.0357  0.0026  50  TRP   B CZ2 
637  C CZ2 D TRP   B 41  ? 0.7994 0.6632 0.3584 0.0667  0.0431  0.0024  50  TRP   B CZ2 
638  C CZ3 A TRP   B 41  ? 0.7948 0.7013 0.3981 0.0521  0.0344  0.0101  50  TRP   B CZ3 
639  C CZ3 B TRP   B 41  ? 0.7902 0.6568 0.3521 0.0748  0.0509  0.0074  50  TRP   B CZ3 
640  C CZ3 C TRP   B 41  ? 0.7948 0.7013 0.3981 0.0521  0.0344  0.0101  50  TRP   B CZ3 
641  C CZ3 D TRP   B 41  ? 0.7999 0.6672 0.3602 0.0753  0.0506  0.0077  50  TRP   B CZ3 
642  C CH2 A TRP   B 41  ? 0.8074 0.6966 0.3976 0.0501  0.0322  0.0036  50  TRP   B CH2 
643  C CH2 B TRP   B 41  ? 0.7941 0.6538 0.3490 0.0705  0.0482  0.0029  50  TRP   B CH2 
644  C CH2 C TRP   B 41  ? 0.8074 0.6966 0.3976 0.0501  0.0322  0.0036  50  TRP   B CH2 
645  C CH2 D TRP   B 41  ? 0.8033 0.6635 0.3565 0.0713  0.0484  0.0032  50  TRP   B CH2 
646  N N   . HIS   B 42  ? 0.7492 0.6666 0.3607 0.0775  0.0526  0.0315  51  HIS   B N   
647  C CA  . HIS   B 42  ? 0.7567 0.6778 0.3778 0.0677  0.0562  0.0346  51  HIS   B CA  
648  C C   . HIS   B 42  ? 0.7759 0.6801 0.3938 0.0668  0.0639  0.0391  51  HIS   B C   
649  O O   . HIS   B 42  ? 0.7793 0.6779 0.4018 0.0561  0.0669  0.0410  51  HIS   B O   
650  C CB  . HIS   B 42  ? 0.7459 0.6926 0.3791 0.0683  0.0563  0.0389  51  HIS   B CB  
651  C CG  . HIS   B 42  ? 0.7529 0.7060 0.3851 0.0791  0.0619  0.0461  51  HIS   B CG  
652  N ND1 . HIS   B 42  ? 0.7715 0.7318 0.3976 0.0926  0.0579  0.0458  51  HIS   B ND1 
653  C CD2 . HIS   B 42  ? 0.7555 0.7057 0.3890 0.0789  0.0707  0.0537  51  HIS   B CD2 
654  C CE1 . HIS   B 42  ? 0.7724 0.7358 0.3967 0.1010  0.0638  0.0522  51  HIS   B CE1 
655  N NE2 . HIS   B 42  ? 0.7646 0.7222 0.3926 0.0934  0.0722  0.0576  51  HIS   B NE2 
656  N N   . VAL   B 43  ? 0.7887 0.6824 0.3974 0.0776  0.0660  0.0399  52  VAL   B N   
657  C CA  . VAL   B 43  ? 0.8039 0.6795 0.4054 0.0807  0.0718  0.0433  52  VAL   B CA  
658  C C   . VAL   B 43  ? 0.8252 0.6797 0.4195 0.0757  0.0710  0.0373  52  VAL   B C   
659  O O   . VAL   B 43  ? 0.8402 0.6780 0.4307 0.0698  0.0745  0.0395  52  VAL   B O   
660  C CB  . VAL   B 43  ? 0.8115 0.6868 0.4066 0.0963  0.0718  0.0444  52  VAL   B CB  
661  C CG1 . VAL   B 43  ? 0.8279 0.6828 0.4126 0.1025  0.0759  0.0459  52  VAL   B CG1 
662  C CG2 . VAL   B 43  ? 0.8065 0.6987 0.4046 0.1034  0.0727  0.0502  52  VAL   B CG2 
663  N N   . THR   B 44  ? 0.8249 0.6788 0.4159 0.0785  0.0669  0.0302  53  THR   B N   
664  C CA  . THR   B 44  ? 0.8348 0.6708 0.4173 0.0770  0.0667  0.0240  53  THR   B CA  
665  C C   . THR   B 44  ? 0.8369 0.6709 0.4187 0.0669  0.0625  0.0184  53  THR   B C   
666  O O   . THR   B 44  ? 0.8471 0.6630 0.4202 0.0644  0.0621  0.0137  53  THR   B O   
667  C CB  . THR   B 44  ? 0.8376 0.6749 0.4166 0.0875  0.0666  0.0197  53  THR   B CB  
668  O OG1 . THR   B 44  ? 0.8322 0.6846 0.4155 0.0865  0.0633  0.0178  53  THR   B OG1 
669  C CG2 . THR   B 44  ? 0.8443 0.6823 0.4231 0.0991  0.0686  0.0232  53  THR   B CG2 
670  N N   . LYS   B 45  ? 0.8308 0.6820 0.4195 0.0627  0.0583  0.0182  54  LYS   B N   
671  C CA  . LYS   B 45  ? 0.8408 0.6932 0.4271 0.0562  0.0524  0.0120  54  LYS   B CA  
672  C C   . LYS   B 45  ? 0.8527 0.6957 0.4262 0.0619  0.0526  0.0060  54  LYS   B C   
673  O O   . LYS   B 45  ? 0.8575 0.6915 0.4225 0.0585  0.0494  -0.0001 54  LYS   B O   
674  C CB  . LYS   B 45  ? 0.8670 0.7102 0.4555 0.0444  0.0495  0.0095  54  LYS   B CB  
675  C CG  . LYS   B 45  ? 0.9330 0.7850 0.5355 0.0366  0.0518  0.0163  54  LYS   B CG  
676  C CD  . LYS   B 45  ? 1.0036 0.8841 0.6196 0.0363  0.0493  0.0191  54  LYS   B CD  
677  C CE  . LYS   B 45  ? 1.0695 0.9605 0.7008 0.0272  0.0534  0.0259  54  LYS   B CE  
678  N NZ  . LYS   B 45  ? 1.0956 1.0140 0.7376 0.0334  0.0556  0.0319  54  LYS   B NZ  
679  N N   . GLY   B 46  ? 0.8504 0.6963 0.4231 0.0705  0.0566  0.0075  55  GLY   B N   
680  C CA  . GLY   B 46  ? 0.8543 0.6961 0.4187 0.0752  0.0590  0.0030  55  GLY   B CA  
681  C C   . GLY   B 46  ? 0.8654 0.6917 0.4221 0.0791  0.0625  -0.0012 55  GLY   B C   
682  O O   . GLY   B 46  ? 0.8743 0.6991 0.4240 0.0836  0.0654  -0.0055 55  GLY   B O   
683  N N   . ALA   B 47  ? 0.8682 0.6820 0.4246 0.0781  0.0627  0.0002  56  ALA   B N   
684  C CA  . ALA   B 47  ? 0.8787 0.6735 0.4242 0.0838  0.0649  -0.0042 56  ALA   B CA  
685  C C   . ALA   B 47  ? 0.8840 0.6846 0.4316 0.0962  0.0694  -0.0044 56  ALA   B C   
686  O O   . ALA   B 47  ? 0.8812 0.6959 0.4391 0.0989  0.0701  0.0000  56  ALA   B O   
687  C CB  . ALA   B 47  ? 0.8856 0.6616 0.4281 0.0787  0.0637  -0.0016 56  ALA   B CB  
688  N N   . ALA   B 48  ? 0.8955 0.6855 0.4332 0.1047  0.0716  -0.0103 57  ALA   B N   
689  C CA  . ALA   B 48  ? 0.9068 0.7052 0.4485 0.1175  0.0750  -0.0120 57  ALA   B CA  
690  C C   . ALA   B 48  ? 0.9308 0.7203 0.4726 0.1234  0.0742  -0.0076 57  ALA   B C   
691  O O   . ALA   B 48  ? 0.9495 0.7205 0.4842 0.1179  0.0728  -0.0038 57  ALA   B O   
692  C CB  . ALA   B 48  ? 0.9080 0.6983 0.4381 0.1271  0.0776  -0.0200 57  ALA   B CB  
693  N N   . LEU   B 49  ? 0.9305 0.7331 0.4801 0.1341  0.0750  -0.0080 58  LEU   B N   
694  C CA  . LEU   B 49  ? 0.9543 0.7481 0.5008 0.1427  0.0738  -0.0042 58  LEU   B CA  
695  C C   . LEU   B 49  ? 0.9810 0.7707 0.5216 0.1597  0.0738  -0.0104 58  LEU   B C   
696  O O   . LEU   B 49  ? 0.9747 0.7802 0.5220 0.1651  0.0752  -0.0172 58  LEU   B O   
697  C CB  . LEU   B 49  ? 0.9430 0.7556 0.5028 0.1427  0.0719  0.0005  58  LEU   B CB  
698  C CG  . LEU   B 49  ? 0.9511 0.7707 0.5168 0.1293  0.0713  0.0062  58  LEU   B CG  
699  C CD1 . LEU   B 49  ? 0.9438 0.7813 0.5203 0.1324  0.0685  0.0089  58  LEU   B CD1 
700  C CD2 . LEU   B 49  ? 0.9673 0.7692 0.5245 0.1223  0.0724  0.0123  58  LEU   B CD2 
701  N N   . ARG   B 50  ? 1.0136 0.7829 0.5414 0.1688  0.0726  -0.0077 59  ARG   B N   
702  C CA  . ARG   B 50  ? 1.0510 0.8136 0.5701 0.1877  0.0713  -0.0135 59  ARG   B CA  
703  C C   . ARG   B 50  ? 1.0705 0.8451 0.5961 0.1995  0.0680  -0.0117 59  ARG   B C   
704  O O   . ARG   B 50  ? 1.0678 0.8411 0.5944 0.1942  0.0676  -0.0039 59  ARG   B O   
705  C CB  . ARG   B 50  ? 1.0993 0.8222 0.5927 0.1909  0.0714  -0.0122 59  ARG   B CB  
706  C CG  . ARG   B 50  ? 1.1762 0.8856 0.6546 0.2128  0.0692  -0.0184 59  ARG   B CG  
707  C CD  . ARG   B 50  ? 1.2636 0.9287 0.7134 0.2151  0.0687  -0.0180 59  ARG   B CD  
708  N NE  . ARG   B 50  ? 1.3254 0.9631 0.7645 0.2013  0.0703  -0.0069 59  ARG   B NE  
709  C CZ  . ARG   B 50  ? 1.3781 0.9971 0.8043 0.2080  0.0708  0.0009  59  ARG   B CZ  
710  N NH1 . ARG   B 50  ? 1.3746 0.9988 0.7961 0.2295  0.0680  -0.0020 59  ARG   B NH1 
711  N NH2 . ARG   B 50  ? 1.3978 0.9943 0.8160 0.1934  0.0741  0.0117  59  ARG   B NH2 
712  N N   . SER   B 51  ? 1.0859 0.8756 0.6175 0.2158  0.0652  -0.0197 60  SER   B N   
713  C CA  . SER   B 51  ? 1.1121 0.9128 0.6489 0.2291  0.0598  -0.0203 60  SER   B CA  
714  C C   . SER   B 51  ? 1.1494 0.9417 0.6744 0.2514  0.0565  -0.0278 60  SER   B C   
715  O O   . SER   B 51  ? 1.1435 0.9622 0.6842 0.2605  0.0546  -0.0374 60  SER   B O   
716  C CB  . SER   B 51  ? 1.1075 0.9459 0.6725 0.2243  0.0573  -0.0244 60  SER   B CB  
717  O OG  . SER   B 51  ? 1.1302 0.9776 0.6997 0.2362  0.0502  -0.0256 60  SER   B OG  
718  N N   . GLY   B 52  ? 1.1827 0.9377 0.6795 0.2598  0.0566  -0.0234 61  GLY   B N   
719  C CA  . GLY   B 52  ? 1.2042 0.9436 0.6834 0.2824  0.0532  -0.0302 61  GLY   B CA  
720  C C   . GLY   B 52  ? 1.2193 0.9554 0.6958 0.2800  0.0568  -0.0367 61  GLY   B C   
721  O O   . GLY   B 52  ? 1.2408 0.9525 0.7050 0.2657  0.0608  -0.0318 61  GLY   B O   
722  N N   . GLU   B 53  ? 1.2029 0.9671 0.6932 0.2929  0.0554  -0.0480 62  GLU   B N   
723  C CA  . GLU   B 53  ? 1.2054 0.9706 0.6932 0.2922  0.0598  -0.0546 62  GLU   B CA  
724  C C   . GLU   B 53  ? 1.1712 0.9734 0.6874 0.2742  0.0655  -0.0558 62  GLU   B C   
725  O O   . GLU   B 53  ? 1.1784 0.9774 0.6895 0.2689  0.0704  -0.0585 62  GLU   B O   
726  C CB  . GLU   B 53  ? 1.2526 1.0204 0.7318 0.3191  0.0567  -0.0660 62  GLU   B CB  
727  C CG  . GLU   B 53  ? 1.3861 1.1015 0.8254 0.3338  0.0531  -0.0647 62  GLU   B CG  
728  C CD  . GLU   B 53  ? 1.5452 1.2516 0.9676 0.3551  0.0521  -0.0759 62  GLU   B CD  
729  O OE1 . GLU   B 53  ? 1.5664 1.3147 1.0112 0.3630  0.0543  -0.0856 62  GLU   B OE1 
730  O OE2 . GLU   B 53  ? 1.6072 1.2641 0.9935 0.3639  0.0494  -0.0748 62  GLU   B OE2 
731  N N   . GLY   B 54  ? 1.1335 0.9659 0.6755 0.2651  0.0646  -0.0533 63  GLY   B N   
732  C CA  . GLY   B 54  ? 1.1009 0.9641 0.6671 0.2477  0.0699  -0.0530 63  GLY   B CA  
733  C C   . GLY   B 54  ? 1.0881 0.9342 0.6472 0.2264  0.0733  -0.0444 63  GLY   B C   
734  O O   . GLY   B 54  ? 1.1156 0.9330 0.6586 0.2218  0.0711  -0.0373 63  GLY   B O   
735  N N   . ARG   B 55  ? 1.0419 0.9064 0.6130 0.2133  0.0789  -0.0448 64  ARG   B N   
736  C CA  . ARG   B 55  ? 1.0229 0.8743 0.5877 0.1945  0.0811  -0.0380 64  ARG   B CA  
737  C C   . ARG   B 55  ? 0.9730 0.8487 0.5587 0.1798  0.0820  -0.0337 64  ARG   B C   
738  O O   . ARG   B 55  ? 0.9589 0.8633 0.5639 0.1800  0.0846  -0.0371 64  ARG   B O   
739  C CB  . ARG   B 55  ? 1.0459 0.8884 0.5974 0.1932  0.0861  -0.0421 64  ARG   B CB  
740  C CG  . ARG   B 55  ? 1.0863 0.9121 0.6281 0.1762  0.0862  -0.0370 64  ARG   B CG  
741  C CD  . ARG   B 55  ? 1.1377 0.9511 0.6623 0.1782  0.0893  -0.0426 64  ARG   B CD  
742  N NE  . ARG   B 55  ? 1.1719 0.9768 0.6905 0.1624  0.0888  -0.0392 64  ARG   B NE  
743  C CZ  . ARG   B 55  ? 1.2134 0.9923 0.7115 0.1603  0.0862  -0.0422 64  ARG   B CZ  
744  N NH1 . ARG   B 55  ? 1.2222 0.9776 0.7018 0.1724  0.0842  -0.0482 64  ARG   B NH1 
745  N NH2 . ARG   B 55  ? 1.2080 0.9830 0.7029 0.1468  0.0843  -0.0400 64  ARG   B NH2 
746  N N   . LEU   B 56  ? 0.9416 0.8052 0.5233 0.1670  0.0798  -0.0262 65  LEU   B N   
747  C CA  . LEU   B 56  ? 0.9038 0.7839 0.4997 0.1543  0.0797  -0.0220 65  LEU   B CA  
748  C C   . LEU   B 56  ? 0.8870 0.7576 0.4732 0.1416  0.0825  -0.0193 65  LEU   B C   
749  O O   . LEU   B 56  ? 0.8939 0.7435 0.4667 0.1378  0.0804  -0.0164 65  LEU   B O   
750  C CB  . LEU   B 56  ? 0.9033 0.7790 0.5012 0.1528  0.0737  -0.0160 65  LEU   B CB  
751  C CG  . LEU   B 56  ? 0.9141 0.7914 0.5146 0.1670  0.0689  -0.0177 65  LEU   B CG  
752  C CD1 . LEU   B 56  ? 0.9163 0.7898 0.5163 0.1649  0.0642  -0.0112 65  LEU   B CD1 
753  C CD2 . LEU   B 56  ? 0.9058 0.8098 0.5256 0.1735  0.0678  -0.0248 65  LEU   B CD2 
754  N N   . ASP   B 57  ? 0.8664 0.7520 0.4589 0.1350  0.0871  -0.0201 66  ASP   B N   
755  C CA  . ASP   B 57  ? 0.8699 0.7464 0.4509 0.1248  0.0890  -0.0181 66  ASP   B CA  
756  C C   . ASP   B 57  ? 0.8454 0.7287 0.4331 0.1137  0.0867  -0.0122 66  ASP   B C   
757  O O   . ASP   B 57  ? 0.8349 0.7341 0.4373 0.1124  0.0867  -0.0110 66  ASP   B O   
758  C CB  . ASP   B 57  ? 0.9093 0.7931 0.4856 0.1271  0.0969  -0.0225 66  ASP   B CB  
759  C CG  . ASP   B 57  ? 1.0026 0.8772 0.5683 0.1402  0.0984  -0.0293 66  ASP   B CG  
760  O OD1 . ASP   B 57  ? 1.0284 0.8787 0.5798 0.1422  0.0934  -0.0299 66  ASP   B OD1 
761  O OD2 . ASP   B 57  ? 1.0291 0.9208 0.6013 0.1485  0.1047  -0.0340 66  ASP   B OD2 
762  N N   . PRO   B 58  ? 0.8318 0.7028 0.4087 0.1060  0.0836  -0.0091 67  PRO   B N   
763  C CA  . PRO   B 58  ? 0.8117 0.6877 0.3920 0.0979  0.0806  -0.0040 67  PRO   B CA  
764  C C   . PRO   B 58  ? 0.7897 0.6755 0.3715 0.0933  0.0860  -0.0033 67  PRO   B C   
765  O O   . PRO   B 58  ? 0.7809 0.6682 0.3567 0.0946  0.0929  -0.0062 67  PRO   B O   
766  C CB  . PRO   B 58  ? 0.8322 0.6949 0.4004 0.0927  0.0761  -0.0026 67  PRO   B CB  
767  C CG  . PRO   B 58  ? 0.8508 0.7014 0.4070 0.0953  0.0783  -0.0078 67  PRO   B CG  
768  C CD  . PRO   B 58  ? 0.8349 0.6870 0.3962 0.1047  0.0815  -0.0108 67  PRO   B CD  
769  N N   . TYR   B 59  ? 0.7739 0.6654 0.3627 0.0884  0.0832  0.0007  68  TYR   B N   
770  C CA  . TYR   B 59  ? 0.7579 0.6559 0.3485 0.0820  0.0884  0.0029  68  TYR   B CA  
771  C C   . TYR   B 59  ? 0.7620 0.6493 0.3404 0.0758  0.0840  0.0078  68  TYR   B C   
772  O O   . TYR   B 59  ? 0.7738 0.6563 0.3407 0.0712  0.0889  0.0101  68  TYR   B O   
773  C CB  . TYR   B 59  ? 0.7368 0.6501 0.3483 0.0818  0.0881  0.0022  68  TYR   B CB  
774  C CG  . TYR   B 59  ? 0.7268 0.6474 0.3441 0.0726  0.0940  0.0049  68  TYR   B CG  
775  C CD1 . TYR   B 59  ? 0.7336 0.6443 0.3450 0.0650  0.0898  0.0101  68  TYR   B CD1 
776  C CD2 . TYR   B 59  ? 0.7227 0.6603 0.3518 0.0718  0.1039  0.0025  68  TYR   B CD2 
777  C CE1 . TYR   B 59  ? 0.7413 0.6546 0.3564 0.0548  0.0957  0.0136  68  TYR   B CE1 
778  C CE2 . TYR   B 59  ? 0.7298 0.6755 0.3665 0.0611  0.1108  0.0060  68  TYR   B CE2 
779  C CZ  . TYR   B 59  ? 0.7471 0.6787 0.3764 0.0517  0.1066  0.0120  68  TYR   B CZ  
780  O OH  . TYR   B 59  ? 0.7604 0.6956 0.3950 0.0395  0.1141  0.0166  68  TYR   B OH  
781  N N   . TRP   B 60  ? 0.7590 0.6424 0.3383 0.0771  0.0752  0.0096  69  TRP   B N   
782  C CA  . TRP   B 60  ? 0.7647 0.6389 0.3321 0.0742  0.0695  0.0135  69  TRP   B CA  
783  C C   . TRP   B 60  ? 0.7763 0.6490 0.3426 0.0784  0.0620  0.0133  69  TRP   B C   
784  O O   . TRP   B 60  ? 0.7810 0.6591 0.3579 0.0826  0.0605  0.0125  69  TRP   B O   
785  C CB  . TRP   B 60  ? 0.7499 0.6236 0.3220 0.0711  0.0664  0.0166  69  TRP   B CB  
786  C CG  . TRP   B 60  ? 0.7569 0.6197 0.3155 0.0719  0.0583  0.0198  69  TRP   B CG  
787  C CD1 . TRP   B 60  ? 0.7760 0.6263 0.3155 0.0693  0.0581  0.0226  69  TRP   B CD1 
788  C CD2 . TRP   B 60  ? 0.7539 0.6176 0.3147 0.0780  0.0491  0.0202  69  TRP   B CD2 
789  N NE1 . TRP   B 60  ? 0.7797 0.6239 0.3105 0.0739  0.0485  0.0240  69  TRP   B NE1 
790  C CE2 . TRP   B 60  ? 0.7693 0.6228 0.3136 0.0793  0.0434  0.0226  69  TRP   B CE2 
791  C CE3 . TRP   B 60  ? 0.7544 0.6265 0.3274 0.0842  0.0457  0.0188  69  TRP   B CE3 
792  C CZ2 . TRP   B 60  ? 0.7762 0.6307 0.3182 0.0866  0.0346  0.0231  69  TRP   B CZ2 
793  C CZ3 . TRP   B 60  ? 0.7667 0.6386 0.3363 0.0908  0.0379  0.0202  69  TRP   B CZ3 
794  C CH2 . TRP   B 60  ? 0.7736 0.6381 0.3289 0.0921  0.0325  0.0221  69  TRP   B CH2 
795  N N   . GLY   B 61  ? 0.7869 0.6535 0.3407 0.0775  0.0577  0.0143  70  GLY   B N   
796  C CA  . GLY   B 61  ? 0.7871 0.6568 0.3427 0.0800  0.0512  0.0144  70  GLY   B CA  
797  C C   . GLY   B 61  ? 0.7839 0.6502 0.3271 0.0804  0.0448  0.0153  70  GLY   B C   
798  O O   . GLY   B 61  ? 0.8006 0.6580 0.3292 0.0786  0.0458  0.0152  70  GLY   B O   
799  N N   . ASP   B 62  ? 0.7665 0.6404 0.3142 0.0838  0.0384  0.0162  71  ASP   B N   
800  C CA  . ASP   B 62  ? 0.7750 0.6495 0.3128 0.0867  0.0308  0.0162  71  ASP   B CA  
801  C C   . ASP   B 62  ? 0.7645 0.6546 0.3144 0.0887  0.0268  0.0160  71  ASP   B C   
802  O O   . ASP   B 62  ? 0.7506 0.6486 0.3095 0.0931  0.0267  0.0187  71  ASP   B O   
803  C CB  . ASP   B 62  ? 0.8177 0.6848 0.3462 0.0913  0.0271  0.0193  71  ASP   B CB  
804  C CG  . ASP   B 62  ? 0.9329 0.7946 0.4444 0.0962  0.0192  0.0191  71  ASP   B CG  
805  O OD1 . ASP   B 62  ? 0.9443 0.8188 0.4597 0.1007  0.0131  0.0173  71  ASP   B OD1 
806  O OD2 . ASP   B 62  ? 1.0044 0.8492 0.4985 0.0958  0.0192  0.0210  71  ASP   B OD2 
807  N N   . VAL   B 63  ? 0.7739 0.6694 0.3239 0.0858  0.0232  0.0126  72  VAL   B N   
808  C CA  . VAL   B 63  ? 0.7631 0.6767 0.3280 0.0851  0.0202  0.0123  72  VAL   B CA  
809  C C   . VAL   B 63  ? 0.7645 0.6913 0.3302 0.0941  0.0144  0.0144  72  VAL   B C   
810  O O   . VAL   B 63  ? 0.7697 0.7132 0.3497 0.0957  0.0156  0.0168  72  VAL   B O   
811  C CB  . VAL   B 63  ? 0.7612 0.6771 0.3269 0.0784  0.0161  0.0067  72  VAL   B CB  
812  C CG1 . VAL   B 63  ? 0.7554 0.6943 0.3369 0.0773  0.0106  0.0057  72  VAL   B CG1 
813  C CG2 . VAL   B 63  ? 0.7662 0.6711 0.3347 0.0704  0.0220  0.0049  72  VAL   B CG2 
814  N N   . LYS   B 64  ? 0.7770 0.6952 0.3259 0.1010  0.0085  0.0138  73  LYS   B N   
815  C CA  . LYS   B 64  ? 0.7726 0.7007 0.3187 0.1122  0.0017  0.0149  73  LYS   B CA  
816  C C   . LYS   B 64  ? 0.7752 0.7023 0.3242 0.1182  0.0046  0.0191  73  LYS   B C   
817  O O   . LYS   B 64  ? 0.7708 0.7155 0.3289 0.1252  0.0035  0.0206  73  LYS   B O   
818  C CB  . LYS   B 64  ? 0.7918 0.7070 0.3152 0.1193  -0.0066 0.0129  73  LYS   B CB  
819  C CG  . LYS   B 64  ? 0.8191 0.7484 0.3405 0.1328  -0.0153 0.0122  73  LYS   B CG  
820  C CD  . LYS   B 64  ? 0.8842 0.8014 0.3819 0.1411  -0.0250 0.0093  73  LYS   B CD  
821  C CE  . LYS   B 64  ? 0.9337 0.8609 0.4260 0.1573  -0.0335 0.0087  73  LYS   B CE  
822  N NZ  . LYS   B 64  ? 0.9881 0.8904 0.4488 0.1676  -0.0424 0.0079  73  LYS   B NZ  
823  N N   . GLN   B 65  ? 0.7819 0.6904 0.3243 0.1156  0.0084  0.0208  74  GLN   B N   
824  C CA  . GLN   B 65  ? 0.7869 0.6932 0.3327 0.1208  0.0099  0.0234  74  GLN   B CA  
825  C C   . GLN   B 65  ? 0.7743 0.6938 0.3375 0.1186  0.0168  0.0251  74  GLN   B C   
826  O O   . GLN   B 65  ? 0.7773 0.7000 0.3432 0.1261  0.0172  0.0272  74  GLN   B O   
827  C CB  . GLN   B 65  ? 0.8248 0.7109 0.3635 0.1162  0.0121  0.0237  74  GLN   B CB  
828  C CG  . GLN   B 65  ? 0.8991 0.7665 0.4177 0.1183  0.0061  0.0239  74  GLN   B CG  
829  C CD  . GLN   B 65  ? 0.9913 0.8421 0.5077 0.1117  0.0093  0.0250  74  GLN   B CD  
830  O OE1 . GLN   B 65  ? 1.0158 0.8679 0.5419 0.1128  0.0096  0.0248  74  GLN   B OE1 
831  N NE2 . GLN   B 65  ? 1.0040 0.8398 0.5078 0.1048  0.0117  0.0260  74  GLN   B NE2 
832  N N   . ASP   B 66  ? 0.7561 0.6794 0.3281 0.1088  0.0221  0.0242  75  ASP   B N   
833  C CA  . ASP   B 66  ? 0.7463 0.6757 0.3313 0.1047  0.0292  0.0263  75  ASP   B CA  
834  C C   . ASP   B 66  ? 0.7389 0.6571 0.3232 0.1067  0.0331  0.0272  75  ASP   B C   
835  O O   . ASP   B 66  ? 0.7343 0.6564 0.3243 0.1107  0.0368  0.0301  75  ASP   B O   
836  C CB  . ASP   B 66  ? 0.7520 0.7013 0.3474 0.1089  0.0305  0.0298  75  ASP   B CB  
837  C CG  . ASP   B 66  ? 0.7932 0.7451 0.3996 0.1024  0.0388  0.0331  75  ASP   B CG  
838  O OD1 . ASP   B 66  ? 0.8049 0.7470 0.4127 0.0925  0.0412  0.0309  75  ASP   B OD1 
839  O OD2 . ASP   B 66  ? 0.8014 0.7625 0.4123 0.1081  0.0430  0.0381  75  ASP   B OD2 
840  N N   . LEU   B 67  ? 0.7309 0.6362 0.3091 0.1033  0.0332  0.0246  76  LEU   B N   
841  C CA  . LEU   B 67  ? 0.7203 0.6187 0.3013 0.1045  0.0364  0.0240  76  LEU   B CA  
842  C C   . LEU   B 67  ? 0.7293 0.6207 0.3104 0.0969  0.0415  0.0212  76  LEU   B C   
843  O O   . LEU   B 67  ? 0.7287 0.6165 0.3031 0.0914  0.0415  0.0196  76  LEU   B O   
844  C CB  . LEU   B 67  ? 0.7199 0.6123 0.2958 0.1092  0.0310  0.0236  76  LEU   B CB  
845  C CG  . LEU   B 67  ? 0.7288 0.6256 0.3015 0.1200  0.0249  0.0254  76  LEU   B CG  
846  C CD1 . LEU   B 67  ? 0.7323 0.6178 0.2959 0.1231  0.0175  0.0241  76  LEU   B CD1 
847  C CD2 . LEU   B 67  ? 0.7344 0.6370 0.3138 0.1274  0.0275  0.0268  76  LEU   B CD2 
848  N N   . VAL   B 68  ? 0.7257 0.6154 0.3127 0.0984  0.0455  0.0200  77  VAL   B N   
849  C CA  . VAL   B 68  ? 0.7258 0.6111 0.3134 0.0940  0.0510  0.0167  77  VAL   B CA  
850  C C   . VAL   B 68  ? 0.7150 0.6029 0.3108 0.0987  0.0523  0.0148  77  VAL   B C   
851  O O   . VAL   B 68  ? 0.7145 0.6047 0.3141 0.1059  0.0497  0.0157  77  VAL   B O   
852  C CB  . VAL   B 68  ? 0.7299 0.6114 0.3162 0.0912  0.0545  0.0158  77  VAL   B CB  
853  C CG1 . VAL   B 68  ? 0.7300 0.6120 0.3208 0.0958  0.0553  0.0185  77  VAL   B CG1 
854  C CG2 . VAL   B 68  ? 0.7372 0.6129 0.3208 0.0894  0.0596  0.0115  77  VAL   B CG2 
855  N N   . SER   B 69  ? 0.7153 0.6043 0.3138 0.0951  0.0560  0.0119  78  SER   B N   
856  C CA  . SER   B 69  ? 0.7019 0.5981 0.3120 0.0986  0.0571  0.0087  78  SER   B CA  
857  C C   . SER   B 69  ? 0.7074 0.6056 0.3191 0.0990  0.0644  0.0049  78  SER   B C   
858  O O   . SER   B 69  ? 0.7201 0.6135 0.3232 0.0944  0.0689  0.0047  78  SER   B O   
859  C CB  . SER   B 69  ? 0.6913 0.5908 0.3067 0.0934  0.0551  0.0086  78  SER   B CB  
860  O OG  . SER   B 69  ? 0.6938 0.5921 0.3051 0.0848  0.0616  0.0092  78  SER   B OG  
861  N N   . TYR   B 70  ? 0.7034 0.6081 0.3242 0.1064  0.0647  0.0013  79  TYR   B N   
862  C CA  . TYR   B 70  ? 0.7129 0.6198 0.3345 0.1105  0.0707  -0.0031 79  TYR   B CA  
863  C C   . TYR   B 70  ? 0.7049 0.6298 0.3433 0.1124  0.0721  -0.0077 79  TYR   B C   
864  O O   . TYR   B 70  ? 0.6869 0.6192 0.3364 0.1152  0.0659  -0.0087 79  TYR   B O   
865  C CB  . TYR   B 70  ? 0.7253 0.6223 0.3407 0.1203  0.0690  -0.0037 79  TYR   B CB  
866  C CG  . TYR   B 70  ? 0.7445 0.6253 0.3460 0.1163  0.0693  0.0001  79  TYR   B CG  
867  C CD1 . TYR   B 70  ? 0.7490 0.6268 0.3483 0.1130  0.0653  0.0055  79  TYR   B CD1 
868  C CD2 . TYR   B 70  ? 0.7639 0.6333 0.3553 0.1161  0.0729  -0.0024 79  TYR   B CD2 
869  C CE1 . TYR   B 70  ? 0.7669 0.6344 0.3580 0.1078  0.0655  0.0085  79  TYR   B CE1 
870  C CE2 . TYR   B 70  ? 0.7873 0.6425 0.3685 0.1102  0.0719  0.0001  79  TYR   B CE2 
871  C CZ  . TYR   B 70  ? 0.7978 0.6539 0.3808 0.1053  0.0684  0.0057  79  TYR   B CZ  
872  O OH  . TYR   B 70  ? 0.8246 0.6708 0.4016 0.0983  0.0675  0.0076  79  TYR   B OH  
873  N N   . CYS   B 71  ? 0.7087 0.6418 0.3496 0.1113  0.0802  -0.0109 80  CYS   B N   
874  C CA  . CYS   B 71  ? 0.7078 0.6635 0.3676 0.1122  0.0842  -0.0156 80  CYS   B CA  
875  C C   . CYS   B 71  ? 0.7002 0.6661 0.3718 0.0993  0.0856  -0.0128 80  CYS   B C   
876  O O   . CYS   B 71  ? 0.7087 0.6948 0.3968 0.0962  0.0917  -0.0156 80  CYS   B O   
877  C CB  . CYS   B 71  ? 0.7313 0.6972 0.4036 0.1248  0.0782  -0.0213 80  CYS   B CB  
878  S SG  . CYS   B 71  ? 0.8430 0.7910 0.4976 0.1406  0.0766  -0.0235 80  CYS   B SG  
879  N N   . GLY   B 72  ? 0.6835 0.6358 0.3469 0.0921  0.0803  -0.0074 81  GLY   B N   
880  C CA  . GLY   B 72  ? 0.6672 0.6227 0.3375 0.0796  0.0809  -0.0043 81  GLY   B CA  
881  C C   . GLY   B 72  ? 0.6667 0.6025 0.3216 0.0751  0.0742  0.0013  81  GLY   B C   
882  O O   . GLY   B 72  ? 0.6618 0.5855 0.3032 0.0811  0.0697  0.0028  81  GLY   B O   
883  N N   . PRO   B 73  ? 0.6679 0.6004 0.3244 0.0642  0.0740  0.0047  82  PRO   B N   
884  C CA  . PRO   B 73  ? 0.6948 0.6074 0.3349 0.0620  0.0663  0.0094  82  PRO   B CA  
885  C C   . PRO   B 73  ? 0.7101 0.6188 0.3518 0.0707  0.0536  0.0073  82  PRO   B C   
886  O O   . PRO   B 73  ? 0.7088 0.6288 0.3664 0.0756  0.0489  0.0023  82  PRO   B O   
887  C CB  . PRO   B 73  ? 0.6980 0.6058 0.3394 0.0484  0.0694  0.0132  82  PRO   B CB  
888  C CG  . PRO   B 73  ? 0.6776 0.6083 0.3457 0.0435  0.0746  0.0090  82  PRO   B CG  
889  C CD  . PRO   B 73  ? 0.6463 0.5930 0.3203 0.0535  0.0804  0.0043  82  PRO   B CD  
890  N N   . TRP   B 74  ? 0.7259 0.6192 0.3501 0.0738  0.0476  0.0108  83  TRP   B N   
891  C CA  . TRP   B 74  ? 0.7415 0.6301 0.3629 0.0831  0.0366  0.0099  83  TRP   B CA  
892  C C   . TRP   B 74  ? 0.7578 0.6465 0.3906 0.0811  0.0283  0.0065  83  TRP   B C   
893  O O   . TRP   B 74  ? 0.7652 0.6448 0.3963 0.0707  0.0276  0.0083  83  TRP   B O   
894  C CB  . TRP   B 74  ? 0.7484 0.6227 0.3497 0.0854  0.0325  0.0143  83  TRP   B CB  
895  C CG  . TRP   B 74  ? 0.7469 0.6193 0.3437 0.0973  0.0233  0.0138  83  TRP   B CG  
896  C CD1 . TRP   B 74  ? 0.7538 0.6177 0.3469 0.1017  0.0130  0.0125  83  TRP   B CD1 
897  C CD2 . TRP   B 74  ? 0.7441 0.6233 0.3396 0.1069  0.0241  0.0144  83  TRP   B CD2 
898  N NE1 . TRP   B 74  ? 0.7583 0.6244 0.3461 0.1150  0.0078  0.0124  83  TRP   B NE1 
899  C CE2 . TRP   B 74  ? 0.7509 0.6274 0.3414 0.1177  0.0153  0.0141  83  TRP   B CE2 
900  C CE3 . TRP   B 74  ? 0.7449 0.6305 0.3419 0.1070  0.0314  0.0155  83  TRP   B CE3 
901  C CZ2 . TRP   B 74  ? 0.7555 0.6379 0.3431 0.1282  0.0156  0.0159  83  TRP   B CZ2 
902  C CZ3 . TRP   B 74  ? 0.7538 0.6430 0.3488 0.1155  0.0309  0.0173  83  TRP   B CZ3 
903  C CH2 . TRP   B 74  ? 0.7563 0.6452 0.3470 0.1258  0.0240  0.0181  83  TRP   B CH2 
904  N N   . LYS   B 75  ? 0.7589 0.6566 0.4027 0.0905  0.0221  0.0013  84  LYS   B N   
905  C CA  . LYS   B 75  ? 0.7684 0.6681 0.4251 0.0895  0.0123  -0.0041 84  LYS   B CA  
906  C C   . LYS   B 75  ? 0.8031 0.6886 0.4470 0.0999  -0.0013 -0.0052 84  LYS   B C   
907  O O   . LYS   B 75  ? 0.8124 0.6927 0.4619 0.0976  -0.0115 -0.0096 84  LYS   B O   
908  C CB  . LYS   B 75  ? 0.7679 0.6875 0.4445 0.0957  0.0121  -0.0109 84  LYS   B CB  
909  C CG  . LYS   B 75  ? 0.7608 0.6978 0.4520 0.0885  0.0245  -0.0117 84  LYS   B CG  
910  C CD  . LYS   B 75  ? 0.8008 0.7433 0.5067 0.0715  0.0275  -0.0118 84  LYS   B CD  
911  C CE  . LYS   B 75  ? 0.8388 0.7991 0.5566 0.0644  0.0420  -0.0113 84  LYS   B CE  
912  N NZ  . LYS   B 75  ? 0.8571 0.8444 0.6026 0.0674  0.0408  -0.0196 84  LYS   B NZ  
913  N N   . LEU   B 76  ? 0.8157 0.6959 0.4431 0.1115  -0.0016 -0.0018 85  LEU   B N   
914  C CA  . LEU   B 76  ? 0.8293 0.6994 0.4433 0.1248  -0.0128 -0.0028 85  LEU   B CA  
915  C C   . LEU   B 76  ? 0.8642 0.7155 0.4623 0.1215  -0.0188 -0.0002 85  LEU   B C   
916  O O   . LEU   B 76  ? 0.8622 0.7090 0.4480 0.1199  -0.0136 0.0052  85  LEU   B O   
917  C CB  . LEU   B 76  ? 0.8241 0.6992 0.4285 0.1380  -0.0086 0.0007  85  LEU   B CB  
918  C CG  . LEU   B 76  ? 0.8101 0.6981 0.4246 0.1418  -0.0015 -0.0003 85  LEU   B CG  
919  C CD1 . LEU   B 76  ? 0.8123 0.7013 0.4157 0.1516  0.0036  0.0049  85  LEU   B CD1 
920  C CD2 . LEU   B 76  ? 0.8068 0.6995 0.4308 0.1498  -0.0098 -0.0076 85  LEU   B CD2 
921  N N   . ASP   B 77  ? 0.8914 0.7301 0.4882 0.1214  -0.0311 -0.0048 86  ASP   B N   
922  C CA  . ASP   B 77  ? 0.9319 0.7474 0.5106 0.1185  -0.0379 -0.0027 86  ASP   B CA  
923  C C   . ASP   B 77  ? 0.9492 0.7489 0.5112 0.1340  -0.0533 -0.0067 86  ASP   B C   
924  O O   . ASP   B 77  ? 0.9678 0.7449 0.5120 0.1334  -0.0604 -0.0056 86  ASP   B O   
925  C CB  . ASP   B 77  ? 0.9763 0.7821 0.5638 0.0986  -0.0371 -0.0026 86  ASP   B CB  
926  C CG  . ASP   B 77  ? 1.0730 0.8833 0.6810 0.0928  -0.0452 -0.0103 86  ASP   B CG  
927  O OD1 . ASP   B 77  ? 1.0863 0.9126 0.7055 0.1037  -0.0490 -0.0160 86  ASP   B OD1 
928  O OD2 . ASP   B 77  ? 1.1183 0.9160 0.7312 0.0770  -0.0480 -0.0105 86  ASP   B OD2 
929  N N   . ALA   B 78  ? 0.9429 0.7519 0.5067 0.1494  -0.0585 -0.0111 87  ALA   B N   
930  C CA  . ALA   B 78  ? 0.9526 0.7470 0.4974 0.1671  -0.0727 -0.0152 87  ALA   B CA  
931  C C   . ALA   B 78  ? 0.9632 0.7549 0.4866 0.1793  -0.0697 -0.0094 87  ALA   B C   
932  O O   . ALA   B 78  ? 0.9506 0.7579 0.4776 0.1773  -0.0568 -0.0032 87  ALA   B O   
933  C CB  . ALA   B 78  ? 0.9436 0.7493 0.4931 0.1823  -0.0776 -0.0207 87  ALA   B CB  
934  N N   . ALA   B 79  ? 0.9784 0.7507 0.4797 0.1924  -0.0822 -0.0120 88  ALA   B N   
935  C CA  . ALA   B 79  ? 0.9925 0.7656 0.4744 0.2065  -0.0804 -0.0076 88  ALA   B CA  
936  C C   . ALA   B 79  ? 1.0070 0.7755 0.4701 0.2314  -0.0908 -0.0118 88  ALA   B C   
937  O O   . ALA   B 79  ? 1.0161 0.7685 0.4737 0.2370  -0.1044 -0.0192 88  ALA   B O   
938  C CB  . ALA   B 79  ? 1.0085 0.7607 0.4761 0.1990  -0.0836 -0.0053 88  ALA   B CB  
939  N N   . TRP   B 80  ? 1.0078 0.7912 0.4611 0.2466  -0.0847 -0.0072 89  TRP   B N   
940  C CA  . TRP   B 80  ? 1.0210 0.8030 0.4540 0.2725  -0.0921 -0.0099 89  TRP   B CA  
941  C C   . TRP   B 80  ? 1.0577 0.8082 0.4665 0.2807  -0.1092 -0.0158 89  TRP   B C   
942  O O   . TRP   B 80  ? 1.0573 0.7958 0.4603 0.2719  -0.1101 -0.0137 89  TRP   B O   
943  C CB  . TRP   B 80  ? 1.0070 0.8149 0.4378 0.2835  -0.0799 -0.0028 89  TRP   B CB  
944  C CG  . TRP   B 80  ? 1.0170 0.8280 0.4272 0.3114  -0.0846 -0.0044 89  TRP   B CG  
945  C CD1 . TRP   B 80  ? 1.0312 0.8370 0.4318 0.3270  -0.0908 -0.0088 89  TRP   B CD1 
946  C CD2 . TRP   B 80  ? 1.0185 0.8407 0.4144 0.3286  -0.0833 -0.0020 89  TRP   B CD2 
947  N NE1 . TRP   B 80  ? 1.0416 0.8525 0.4206 0.3532  -0.0928 -0.0088 89  TRP   B NE1 
948  C CE2 . TRP   B 80  ? 1.0333 0.8570 0.4110 0.3545  -0.0874 -0.0045 89  TRP   B CE2 
949  C CE3 . TRP   B 80  ? 1.0189 0.8526 0.4162 0.3258  -0.0788 0.0016  89  TRP   B CE3 
950  C CZ2 . TRP   B 80  ? 1.0379 0.8756 0.3997 0.3773  -0.0861 -0.0031 89  TRP   B CZ2 
951  C CZ3 . TRP   B 80  ? 1.0343 0.8825 0.4174 0.3484  -0.0789 0.0023  89  TRP   B CZ3 
952  C CH2 . TRP   B 80  ? 1.0364 0.8878 0.4028 0.3736  -0.0817 0.0002  89  TRP   B CH2 
953  N N   . ASP   B 81  ? 1.0840 0.8177 0.4764 0.2974  -0.1237 -0.0235 90  ASP   B N   
954  C CA  . ASP   B 81  ? 1.1261 0.8247 0.4929 0.3057  -0.1418 -0.0300 90  ASP   B CA  
955  C C   . ASP   B 81  ? 1.1615 0.8597 0.5018 0.3292  -0.1437 -0.0285 90  ASP   B C   
956  O O   . ASP   B 81  ? 1.1930 0.8595 0.5073 0.3394  -0.1593 -0.0340 90  ASP   B O   
957  C CB  . ASP   B 81  ? 1.1446 0.8218 0.5026 0.3144  -0.1594 -0.0406 90  ASP   B CB  
958  C CG  . ASP   B 81  ? 1.2039 0.8931 0.5483 0.3424  -0.1612 -0.0434 90  ASP   B CG  
959  O OD1 . ASP   B 81  ? 1.2005 0.9169 0.5436 0.3546  -0.1470 -0.0361 90  ASP   B OD1 
960  O OD2 . ASP   B 81  ? 1.2533 0.9249 0.5882 0.3522  -0.1769 -0.0531 90  ASP   B OD2 
961  N N   . GLY   B 82  ? 1.1501 0.8832 0.4977 0.3372  -0.1283 -0.0214 91  GLY   B N   
962  C CA  . GLY   B 82  ? 1.1651 0.9085 0.4941 0.3593  -0.1275 -0.0196 91  GLY   B CA  
963  C C   . GLY   B 82  ? 1.1903 0.9317 0.4952 0.3906  -0.1356 -0.0247 91  GLY   B C   
964  O O   . GLY   B 82  ? 1.2025 0.9530 0.4902 0.4124  -0.1360 -0.0244 91  GLY   B O   
965  N N   . LEU   B 83  ? 1.1924 0.9234 0.4952 0.3949  -0.1423 -0.0299 92  LEU   B N   
966  C CA  . LEU   B 83  ? 1.2052 0.9291 0.4811 0.4258  -0.1520 -0.0360 92  LEU   B CA  
967  C C   . LEU   B 83  ? 1.2010 0.9455 0.4833 0.4345  -0.1433 -0.0340 92  LEU   B C   
968  O O   . LEU   B 83  ? 1.2201 0.9781 0.4847 0.4613  -0.1397 -0.0329 92  LEU   B O   
969  C CB  . LEU   B 83  ? 1.2298 0.9072 0.4851 0.4281  -0.1764 -0.0479 92  LEU   B CB  
970  C CG  . LEU   B 83  ? 1.2660 0.9137 0.4878 0.4464  -0.1920 -0.0537 92  LEU   B CG  
971  C CD1 . LEU   B 83  ? 1.2801 0.9007 0.5051 0.4225  -0.1979 -0.0533 92  LEU   B CD1 
972  C CD2 . LEU   B 83  ? 1.2904 0.9051 0.4840 0.4666  -0.2134 -0.0658 92  LEU   B CD2 
973  N N   . SER   B 84  ? 1.1741 0.9180 0.4779 0.4150  -0.1415 -0.0344 93  SER   B N   
974  C CA  . SER   B 84  ? 1.1563 0.9116 0.4607 0.4257  -0.1371 -0.0342 93  SER   B CA  
975  C C   . SER   B 84  ? 1.1276 0.9186 0.4528 0.4179  -0.1131 -0.0220 93  SER   B C   
976  O O   . SER   B 84  ? 1.1261 0.9338 0.4721 0.3983  -0.1004 -0.0146 93  SER   B O   
977  C CB  . SER   B 84  ? 1.1707 0.9048 0.4832 0.4144  -0.1515 -0.0436 93  SER   B CB  
978  O OG  . SER   B 84  ? 1.1955 0.9077 0.5189 0.3915  -0.1624 -0.0486 93  SER   B OG  
979  N N   . GLU   B 85  ? 1.1108 0.9111 0.4276 0.4342  -0.1075 -0.0199 94  GLU   B N   
980  C CA  . GLU   B 85  ? 1.0850 0.9128 0.4175 0.4279  -0.0857 -0.0084 94  GLU   B CA  
981  C C   . GLU   B 85  ? 1.0505 0.8768 0.4105 0.4006  -0.0832 -0.0084 94  GLU   B C   
982  O O   . GLU   B 85  ? 1.0569 0.8632 0.4219 0.3914  -0.0986 -0.0180 94  GLU   B O   
983  C CB  . GLU   B 85  ? 1.1093 0.9405 0.4194 0.4548  -0.0819 -0.0064 94  GLU   B CB  
984  C CG  . GLU   B 85  ? 1.1865 1.0256 0.4701 0.4833  -0.0800 -0.0046 94  GLU   B CG  
985  C CD  . GLU   B 85  ? 1.2621 1.1119 0.5248 0.5082  -0.0688 0.0018  94  GLU   B CD  
986  O OE1 . GLU   B 85  ? 1.2767 1.1154 0.5342 0.5115  -0.0711 0.0002  94  GLU   B OE1 
987  O OE2 . GLU   B 85  ? 1.2919 1.1621 0.5431 0.5253  -0.0572 0.0087  94  GLU   B OE2 
988  N N   . VAL   B 86  ? 1.0116 0.8599 0.3901 0.3872  -0.0637 0.0023  95  VAL   B N   
989  C CA  . VAL   B 86  ? 0.9788 0.8289 0.3827 0.3627  -0.0584 0.0035  95  VAL   B CA  
990  C C   . VAL   B 86  ? 0.9721 0.8343 0.3776 0.3659  -0.0430 0.0121  95  VAL   B C   
991  O O   . VAL   B 86  ? 0.9946 0.8662 0.3841 0.3836  -0.0337 0.0190  95  VAL   B O   
992  C CB  . VAL   B 86  ? 0.9459 0.8069 0.3710 0.3387  -0.0501 0.0083  95  VAL   B CB  
993  C CG1 . VAL   B 86  ? 0.9546 0.8012 0.3731 0.3373  -0.0639 0.0017  95  VAL   B CG1 
994  C CG2 . VAL   B 86  ? 0.9276 0.8142 0.3571 0.3390  -0.0313 0.0199  95  VAL   B CG2 
995  N N   . GLN   B 87  ? 0.9476 0.8095 0.3714 0.3490  -0.0389 0.0125  96  GLN   B N   
996  C CA  . GLN   B 87  ? 0.9402 0.8090 0.3638 0.3506  -0.0241 0.0211  96  GLN   B CA  
997  C C   . GLN   B 87  ? 0.9224 0.8023 0.3695 0.3259  -0.0098 0.0283  96  GLN   B C   
998  O O   . GLN   B 87  ? 0.9175 0.7943 0.3827 0.3079  -0.0144 0.0231  96  GLN   B O   
999  C CB  . GLN   B 87  ? 0.9571 0.8117 0.3712 0.3629  -0.0335 0.0145  96  GLN   B CB  
1000 C CG  . GLN   B 87  ? 1.0041 0.8499 0.3878 0.3925  -0.0417 0.0115  96  GLN   B CG  
1001 C CD  . GLN   B 87  ? 1.0279 0.8599 0.3981 0.4087  -0.0520 0.0046  96  GLN   B CD  
1002 O OE1 . GLN   B 87  ? 1.0037 0.8342 0.3864 0.3997  -0.0509 0.0034  96  GLN   B OE1 
1003 N NE2 . GLN   B 87  ? 1.0478 0.8691 0.3904 0.4351  -0.0635 -0.0009 96  GLN   B NE2 
1004 N N   . LEU   B 88  ? 0.9055 0.7985 0.3520 0.3248  0.0078  0.0402  97  LEU   B N   
1005 C CA  . LEU   B 88  ? 0.8954 0.7959 0.3613 0.3028  0.0210  0.0469  97  LEU   B CA  
1006 C C   . LEU   B 88  ? 0.8948 0.7832 0.3550 0.3061  0.0248  0.0487  97  LEU   B C   
1007 O O   . LEU   B 88  ? 0.9154 0.8003 0.3565 0.3223  0.0315  0.0552  97  LEU   B O   
1008 C CB  . LEU   B 88  ? 0.8912 0.8110 0.3608 0.2985  0.0375  0.0586  97  LEU   B CB  
1009 C CG  . LEU   B 88  ? 0.8930 0.8176 0.3793 0.2774  0.0517  0.0663  97  LEU   B CG  
1010 C CD1 . LEU   B 88  ? 0.8842 0.8064 0.3901 0.2564  0.0458  0.0597  97  LEU   B CD1 
1011 C CD2 . LEU   B 88  ? 0.8938 0.8400 0.3857 0.2732  0.0669  0.0773  97  LEU   B CD2 
1012 N N   . LEU   B 89  ? 0.8650 0.7464 0.3391 0.2931  0.0202  0.0428  98  LEU   B N   
1013 C CA  . LEU   B 89  ? 0.8614 0.7315 0.3304 0.2966  0.0235  0.0439  98  LEU   B CA  
1014 C C   . LEU   B 89  ? 0.8647 0.7383 0.3423 0.2799  0.0404  0.0544  98  LEU   B C   
1015 O O   . LEU   B 89  ? 0.8606 0.7345 0.3553 0.2619  0.0417  0.0521  98  LEU   B O   
1016 C CB  . LEU   B 89  ? 0.8516 0.7152 0.3314 0.2936  0.0099  0.0316  98  LEU   B CB  
1017 C CG  . LEU   B 89  ? 0.8632 0.7170 0.3412 0.2964  0.0120  0.0307  98  LEU   B CG  
1018 C CD1 . LEU   B 89  ? 0.8926 0.7350 0.3446 0.3163  0.0173  0.0376  98  LEU   B CD1 
1019 C CD2 . LEU   B 89  ? 0.8651 0.7184 0.3538 0.2987  -0.0037 0.0170  98  LEU   B CD2 
1020 N N   . ALA   B 90  ? 0.8667 0.7442 0.3326 0.2855  0.0535  0.0662  99  ALA   B N   
1021 C CA  . ALA   B 90  ? 0.8617 0.7428 0.3349 0.2697  0.0701  0.0773  99  ALA   B CA  
1022 C C   . ALA   B 90  ? 0.8720 0.7327 0.3379 0.2680  0.0748  0.0799  99  ALA   B C   
1023 O O   . ALA   B 90  ? 0.8935 0.7401 0.3375 0.2864  0.0745  0.0819  99  ALA   B O   
1024 C CB  . ALA   B 90  ? 0.8517 0.7431 0.3136 0.2780  0.0831  0.0893  99  ALA   B CB  
1025 N N   . VAL   B 91  ? 0.8586 0.7161 0.3396 0.2480  0.0791  0.0801  100 VAL   B N   
1026 C CA  . VAL   B 91  ? 0.8796 0.7154 0.3522 0.2460  0.0841  0.0829  100 VAL   B CA  
1027 C C   . VAL   B 91  ? 0.9089 0.7427 0.3855 0.2283  0.0999  0.0950  100 VAL   B C   
1028 O O   . VAL   B 91  ? 0.9014 0.7375 0.3949 0.2091  0.1008  0.0928  100 VAL   B O   
1029 C CB  . VAL   B 91  ? 0.8754 0.7050 0.3588 0.2407  0.0739  0.0711  100 VAL   B CB  
1030 C CG1 . VAL   B 91  ? 0.8922 0.6979 0.3633 0.2420  0.0788  0.0738  100 VAL   B CG1 
1031 C CG2 . VAL   B 91  ? 0.8685 0.7028 0.3520 0.2555  0.0584  0.0592  100 VAL   B CG2 
1032 N N   . PRO   B 92  ? 0.9435 0.7740 0.4050 0.2342  0.1126  0.1079  101 PRO   B N   
1033 C CA  . PRO   B 92  ? 0.9504 0.7822 0.4195 0.2148  0.1279  0.1198  101 PRO   B CA  
1034 C C   . PRO   B 92  ? 0.9774 0.7790 0.4375 0.2057  0.1333  0.1238  101 PRO   B C   
1035 O O   . PRO   B 92  ? 1.0056 0.7829 0.4446 0.2208  0.1294  0.1218  101 PRO   B O   
1036 C CB  . PRO   B 92  ? 0.9567 0.7967 0.4116 0.2263  0.1404  0.1326  101 PRO   B CB  
1037 C CG  . PRO   B 92  ? 0.9654 0.8081 0.4043 0.2527  0.1295  0.1258  101 PRO   B CG  
1038 C CD  . PRO   B 92  ? 0.9485 0.7754 0.3857 0.2584  0.1138  0.1124  101 PRO   B CD  
1039 N N   . PRO   B 93  ? 0.9714 0.7726 0.4457 0.1822  0.1417  0.1291  102 PRO   B N   
1040 C CA  . PRO   B 93  ? 0.9859 0.7531 0.4486 0.1735  0.1460  0.1327  102 PRO   B CA  
1041 C C   . PRO   B 93  ? 1.0135 0.7523 0.4444 0.1872  0.1562  0.1450  102 PRO   B C   
1042 O O   . PRO   B 93  ? 1.0157 0.7628 0.4399 0.1901  0.1683  0.1573  102 PRO   B O   
1043 C CB  . PRO   B 93  ? 0.9802 0.7563 0.4650 0.1454  0.1533  0.1371  102 PRO   B CB  
1044 C CG  . PRO   B 93  ? 0.9672 0.7824 0.4787 0.1405  0.1463  0.1292  102 PRO   B CG  
1045 C CD  . PRO   B 93  ? 0.9492 0.7797 0.4504 0.1630  0.1456  0.1307  102 PRO   B CD  
1046 N N   . GLY   B 94  ? 1.0309 0.7372 0.4408 0.1981  0.1507  0.1411  103 GLY   B N   
1047 C CA  . GLY   B 94  ? 1.0557 0.7280 0.4299 0.2143  0.1577  0.1510  103 GLY   B CA  
1048 C C   . GLY   B 94  ? 1.0656 0.7447 0.4204 0.2413  0.1563  0.1528  103 GLY   B C   
1049 O O   . GLY   B 94  ? 1.0827 0.7342 0.4046 0.2570  0.1628  0.1622  103 GLY   B O   
1050 N N   . GLU   B 95  ? 1.0521 0.7654 0.4241 0.2476  0.1480  0.1445  104 GLU   B N   
1051 C CA  . GLU   B 95  ? 1.0594 0.7795 0.4127 0.2736  0.1450  0.1449  104 GLU   B CA  
1052 C C   . GLU   B 95  ? 1.0478 0.7777 0.4070 0.2892  0.1244  0.1268  104 GLU   B C   
1053 O O   . GLU   B 95  ? 1.0273 0.7700 0.4117 0.2766  0.1149  0.1154  104 GLU   B O   
1054 C CB  . GLU   B 95  ? 1.0855 0.8359 0.4493 0.2695  0.1552  0.1532  104 GLU   B CB  
1055 C CG  . GLU   B 95  ? 1.1570 0.9035 0.5205 0.2516  0.1766  0.1713  104 GLU   B CG  
1056 C CD  . GLU   B 95  ? 1.2264 1.0093 0.6061 0.2456  0.1875  0.1790  104 GLU   B CD  
1057 O OE1 . GLU   B 95  ? 1.2305 1.0414 0.6236 0.2536  0.1770  0.1689  104 GLU   B OE1 
1058 O OE2 . GLU   B 95  ? 1.2506 1.0341 0.6299 0.2327  0.2066  0.1950  104 GLU   B OE2 
1059 N N   . ARG   B 96  ? 1.0610 0.7841 0.3961 0.3164  0.1176  0.1243  105 ARG   B N   
1060 C CA  . ARG   B 96  ? 1.0779 0.8087 0.4164 0.3330  0.0973  0.1073  105 ARG   B CA  
1061 C C   . ARG   B 96  ? 1.0671 0.8300 0.4324 0.3259  0.0887  0.0984  105 ARG   B C   
1062 O O   . ARG   B 96  ? 1.0665 0.8453 0.4356 0.3211  0.0975  0.1061  105 ARG   B O   
1063 C CB  . ARG   B 96  ? 1.1284 0.8452 0.4321 0.3642  0.0934  0.1086  105 ARG   B CB  
1064 C CG  . ARG   B 96  ? 1.2080 0.9087 0.4983 0.3847  0.0772  0.0963  105 ARG   B CG  
1065 C CD  . ARG   B 96  ? 1.3145 0.9901 0.5609 0.4132  0.0802  0.1040  105 ARG   B CD  
1066 N NE  . ARG   B 96  ? 1.4059 1.0508 0.6290 0.4090  0.0975  0.1201  105 ARG   B NE  
1067 C CZ  . ARG   B 96  ? 1.4639 1.0878 0.6508 0.4224  0.1114  0.1358  105 ARG   B CZ  
1068 N NH1 . ARG   B 96  ? 1.4854 1.1171 0.6541 0.4432  0.1100  0.1372  105 ARG   B NH1 
1069 N NH2 . ARG   B 96  ? 1.4690 1.0618 0.6358 0.4154  0.1271  0.1506  105 ARG   B NH2 
1070 N N   . ALA   B 97  ? 1.0549 0.8269 0.4368 0.3272  0.0713  0.0822  106 ALA   B N   
1071 C CA  . ALA   B 97  ? 1.0492 0.8457 0.4520 0.3224  0.0613  0.0732  106 ALA   B CA  
1072 C C   . ALA   B 97  ? 1.0626 0.8628 0.4458 0.3441  0.0577  0.0744  106 ALA   B C   
1073 O O   . ALA   B 97  ? 1.0821 0.8672 0.4398 0.3669  0.0531  0.0735  106 ALA   B O   
1074 C CB  . ALA   B 97  ? 1.0426 0.8442 0.4627 0.3216  0.0443  0.0569  106 ALA   B CB  
1075 N N   . LYS   B 98  ? 1.0597 0.8787 0.4520 0.3388  0.0600  0.0765  107 LYS   B N   
1076 C CA  . LYS   B 98  ? 1.0784 0.9013 0.4503 0.3602  0.0581  0.0782  107 LYS   B CA  
1077 C C   . LYS   B 98  ? 1.0562 0.8972 0.4434 0.3573  0.0468  0.0692  107 LYS   B C   
1078 O O   . LYS   B 98  ? 1.0486 0.9045 0.4585 0.3370  0.0513  0.0706  107 LYS   B O   
1079 C CB  . LYS   B 98  ? 1.1327 0.9583 0.4923 0.3592  0.0800  0.0962  107 LYS   B CB  
1080 C CG  . LYS   B 98  ? 1.2359 1.0677 0.5723 0.3816  0.0834  0.1013  107 LYS   B CG  
1081 C CD  . LYS   B 98  ? 1.3254 1.1639 0.6548 0.3764  0.1084  0.1206  107 LYS   B CD  
1082 C CE  . LYS   B 98  ? 1.3628 1.2208 0.7252 0.3456  0.1194  0.1261  107 LYS   B CE  
1083 N NZ  . LYS   B 98  ? 1.3872 1.2699 0.7522 0.3445  0.1363  0.1384  107 LYS   B NZ  
1084 N N   . ASN   B 99  ? 1.0455 0.8828 0.4190 0.3778  0.0309  0.0592  108 ASN   B N   
1085 C CA  . ASN   B 99  ? 1.0357 0.8842 0.4192 0.3766  0.0187  0.0503  108 ASN   B CA  
1086 C C   . ASN   B 99  ? 1.0432 0.9022 0.4112 0.3894  0.0269  0.0582  108 ASN   B C   
1087 O O   . ASN   B 99  ? 1.0717 0.9236 0.4119 0.4121  0.0305  0.0629  108 ASN   B O   
1088 C CB  . ASN   B 99  ? 1.0419 0.8798 0.4196 0.3907  -0.0045 0.0343  108 ASN   B CB  
1089 C CG  . ASN   B 99  ? 1.0707 0.9049 0.4693 0.3775  -0.0143 0.0244  108 ASN   B CG  
1090 O OD1 . ASN   B 99  ? 1.1050 0.9317 0.5008 0.3790  -0.0101 0.0263  108 ASN   B OD1 
1091 N ND2 . ASN   B 99  ? 1.0410 0.8798 0.4593 0.3656  -0.0276 0.0136  108 ASN   B ND2 
1092 N N   . ILE   B 100 ? 1.0178 0.8942 0.4023 0.3765  0.0303  0.0598  109 ILE   B N   
1093 C CA  . ILE   B 100 ? 1.0149 0.9062 0.3879 0.3891  0.0378  0.0662  109 ILE   B CA  
1094 C C   . ILE   B 100 ? 1.0011 0.8949 0.3769 0.3929  0.0210  0.0546  109 ILE   B C   
1095 O O   . ILE   B 100 ? 0.9925 0.8901 0.3908 0.3731  0.0157  0.0497  109 ILE   B O   
1096 C CB  . ILE   B 100 ? 1.0182 0.9313 0.4085 0.3711  0.0588  0.0797  109 ILE   B CB  
1097 C CG1 . ILE   B 100 ? 1.0397 0.9451 0.4320 0.3593  0.0745  0.0905  109 ILE   B CG1 
1098 C CG2 . ILE   B 100 ? 1.0203 0.9532 0.3990 0.3868  0.0682  0.0868  109 ILE   B CG2 
1099 C CD1 . ILE   B 100 ? 1.0767 0.9724 0.4396 0.3795  0.0856  0.1007  109 ILE   B CD1 
1100 N N   . GLN   B 101 ? 1.0006 0.8905 0.3518 0.4186  0.0129  0.0507  110 GLN   B N   
1101 C CA  . GLN   B 101 ? 1.0018 0.8879 0.3492 0.4258  -0.0047 0.0393  110 GLN   B CA  
1102 C C   . GLN   B 101 ? 1.0013 0.9092 0.3489 0.4301  0.0038  0.0449  110 GLN   B C   
1103 O O   . GLN   B 101 ? 1.0074 0.9300 0.3414 0.4454  0.0179  0.0544  110 GLN   B O   
1104 C CB  . GLN   B 101 ? 1.0344 0.8996 0.3520 0.4536  -0.0220 0.0292  110 GLN   B CB  
1105 C CG  . GLN   B 101 ? 1.0883 0.9429 0.3968 0.4632  -0.0424 0.0166  110 GLN   B CG  
1106 C CD  . GLN   B 101 ? 1.1435 0.9725 0.4328 0.4804  -0.0645 0.0029  110 GLN   B CD  
1107 O OE1 . GLN   B 101 ? 1.1485 0.9685 0.4436 0.4756  -0.0691 -0.0007 110 GLN   B OE1 
1108 N NE2 . GLN   B 101 ? 1.1530 0.9697 0.4189 0.5014  -0.0799 -0.0060 110 GLN   B NE2 
1109 N N   . THR   B 102 ? 0.9904 0.9012 0.3527 0.4175  -0.0047 0.0390  111 THR   B N   
1110 C CA  . THR   B 102 ? 0.9936 0.9263 0.3577 0.4220  0.0012  0.0426  111 THR   B CA  
1111 C C   . THR   B 102 ? 1.0105 0.9299 0.3708 0.4237  -0.0182 0.0310  111 THR   B C   
1112 O O   . THR   B 102 ? 1.0256 0.9224 0.3907 0.4122  -0.0327 0.0222  111 THR   B O   
1113 C CB  . THR   B 102 ? 0.9929 0.9522 0.3859 0.3978  0.0204  0.0537  111 THR   B CB  
1114 O OG1 . THR   B 102 ? 0.9993 0.9868 0.3942 0.4061  0.0286  0.0584  111 THR   B OG1 
1115 C CG2 . THR   B 102 ? 0.9952 0.9474 0.4134 0.3688  0.0148  0.0493  111 THR   B CG2 
1116 N N   . LEU   B 103 ? 1.0106 0.9438 0.3619 0.4382  -0.0184 0.0310  112 LEU   B N   
1117 C CA  . LEU   B 103 ? 1.0179 0.9363 0.3644 0.4385  -0.0358 0.0211  112 LEU   B CA  
1118 C C   . LEU   B 103 ? 1.0056 0.9470 0.3782 0.4175  -0.0259 0.0266  112 LEU   B C   
1119 O O   . LEU   B 103 ? 0.9925 0.9666 0.3735 0.4211  -0.0108 0.0348  112 LEU   B O   
1120 C CB  . LEU   B 103 ? 1.0372 0.9508 0.3536 0.4700  -0.0463 0.0152  112 LEU   B CB  
1121 C CG  . LEU   B 103 ? 1.0749 0.9672 0.3848 0.4680  -0.0650 0.0055  112 LEU   B CG  
1122 C CD1 . LEU   B 103 ? 1.1005 0.9513 0.3964 0.4674  -0.0864 -0.0060 112 LEU   B CD1 
1123 C CD2 . LEU   B 103 ? 1.0975 1.0000 0.3870 0.4945  -0.0681 0.0034  112 LEU   B CD2 
1124 N N   . PRO   B 104 ? 1.0019 0.9280 0.3884 0.3950  -0.0338 0.0223  113 PRO   B N   
1125 C CA  . PRO   B 104 ? 0.9903 0.9362 0.3995 0.3758  -0.0257 0.0266  113 PRO   B CA  
1126 C C   . PRO   B 104 ? 0.9983 0.9579 0.3998 0.3896  -0.0295 0.0249  113 PRO   B C   
1127 O O   . PRO   B 104 ? 1.0190 0.9607 0.3957 0.4098  -0.0440 0.0175  113 PRO   B O   
1128 C CB  . PRO   B 104 ? 0.9984 0.9195 0.4174 0.3526  -0.0349 0.0215  113 PRO   B CB  
1129 C CG  . PRO   B 104 ? 1.0173 0.9146 0.4282 0.3550  -0.0427 0.0168  113 PRO   B CG  
1130 C CD  . PRO   B 104 ? 1.0059 0.8984 0.3896 0.3852  -0.0494 0.0136  113 PRO   B CD  
1131 N N   . GLY   B 105 ? 0.9801 0.9712 0.4031 0.3787  -0.0173 0.0309  114 GLY   B N   
1132 C CA  . GLY   B 105 ? 0.9755 0.9843 0.3975 0.3878  -0.0208 0.0289  114 GLY   B CA  
1133 C C   . GLY   B 105 ? 0.9810 0.9701 0.4068 0.3706  -0.0314 0.0239  114 GLY   B C   
1134 O O   . GLY   B 105 ? 0.9846 0.9427 0.4085 0.3562  -0.0382 0.0209  114 GLY   B O   
1135 N N   . ILE   B 106 ? 0.9794 0.9874 0.4109 0.3723  -0.0326 0.0230  115 ILE   B N   
1136 C CA  . ILE   B 106 ? 0.9952 0.9836 0.4253 0.3593  -0.0427 0.0187  115 ILE   B CA  
1137 C C   . ILE   B 106 ? 0.9851 1.0068 0.4402 0.3460  -0.0345 0.0217  115 ILE   B C   
1138 O O   . ILE   B 106 ? 0.9796 1.0399 0.4456 0.3565  -0.0278 0.0237  115 ILE   B O   
1139 C CB  . ILE   B 106 ? 1.0278 0.9923 0.4259 0.3824  -0.0604 0.0110  115 ILE   B CB  
1140 C CG1 . ILE   B 106 ? 1.0737 0.9985 0.4458 0.3932  -0.0722 0.0061  115 ILE   B CG1 
1141 C CG2 . ILE   B 106 ? 1.0446 0.9920 0.4371 0.3737  -0.0699 0.0077  115 ILE   B CG2 
1142 C CD1 . ILE   B 106 ? 1.1051 0.9972 0.4805 0.3703  -0.0761 0.0052  115 ILE   B CD1 
1143 N N   . PHE   B 107 ? 0.9856 0.9933 0.4497 0.3235  -0.0358 0.0213  116 PHE   B N   
1144 C CA  . PHE   B 107 ? 0.9712 1.0023 0.4540 0.3114  -0.0326 0.0218  116 PHE   B CA  
1145 C C   . PHE   B 107 ? 0.9969 1.0021 0.4563 0.3193  -0.0482 0.0155  116 PHE   B C   
1146 O O   . PHE   B 107 ? 1.0157 0.9828 0.4618 0.3089  -0.0545 0.0141  116 PHE   B O   
1147 C CB  . PHE   B 107 ? 0.9589 0.9839 0.4609 0.2827  -0.0248 0.0248  116 PHE   B CB  
1148 C CG  . PHE   B 107 ? 0.9404 0.9943 0.4696 0.2700  -0.0089 0.0313  116 PHE   B CG  
1149 C CD1 . PHE   B 107 ? 0.9362 1.0172 0.4713 0.2825  0.0001  0.0357  116 PHE   B CD1 
1150 C CD2 . PHE   B 107 ? 0.9402 0.9913 0.4863 0.2461  -0.0025 0.0332  116 PHE   B CD2 
1151 C CE1 . PHE   B 107 ? 0.9270 1.0298 0.4846 0.2695  0.0156  0.0429  116 PHE   B CE1 
1152 C CE2 . PHE   B 107 ? 0.9350 1.0067 0.5029 0.2341  0.0114  0.0393  116 PHE   B CE2 
1153 C CZ  . PHE   B 107 ? 0.9235 1.0197 0.4969 0.2451  0.0206  0.0446  116 PHE   B CZ  
1154 N N   . LYS   B 108 ? 0.9990 1.0232 0.4515 0.3385  -0.0545 0.0120  117 LYS   B N   
1155 C CA  . LYS   B 108 ? 1.0303 1.0277 0.4571 0.3476  -0.0698 0.0064  117 LYS   B CA  
1156 C C   . LYS   B 108 ? 1.0255 1.0361 0.4684 0.3308  -0.0683 0.0061  117 LYS   B C   
1157 O O   . LYS   B 108 ? 1.0002 1.0549 0.4678 0.3304  -0.0622 0.0063  117 LYS   B O   
1158 C CB  . LYS   B 108 ? 1.0584 1.0699 0.4677 0.3796  -0.0788 0.0016  117 LYS   B CB  
1159 C CG  . LYS   B 108 ? 1.1340 1.1264 0.5197 0.4006  -0.0836 0.0001  117 LYS   B CG  
1160 C CD  . LYS   B 108 ? 1.1975 1.2278 0.5812 0.4306  -0.0832 -0.0023 117 LYS   B CD  
1161 C CE  . LYS   B 108 ? 1.2917 1.2892 0.6342 0.4606  -0.0994 -0.0089 117 LYS   B CE  
1162 N NZ  . LYS   B 108 ? 1.3338 1.3490 0.6701 0.4842  -0.0951 -0.0088 117 LYS   B NZ  
1163 N N   . THR   B 109 ? 1.0463 1.0201 0.4764 0.3161  -0.0731 0.0058  118 THR   B N   
1164 C CA  . THR   B 109 ? 1.0589 1.0400 0.4983 0.3025  -0.0731 0.0048  118 THR   B CA  
1165 C C   . THR   B 109 ? 1.0954 1.0450 0.5009 0.3146  -0.0881 0.0005  118 THR   B C   
1166 O O   . THR   B 109 ? 1.1183 1.0379 0.4944 0.3311  -0.0978 -0.0011 118 THR   B O   
1167 C CB  . THR   B 109 ? 1.0746 1.0462 0.5307 0.2739  -0.0628 0.0089  118 THR   B CB  
1168 O OG1 . THR   B 109 ? 1.1145 1.0398 0.5474 0.2660  -0.0674 0.0095  118 THR   B OG1 
1169 C CG2 . THR   B 109 ? 1.0643 1.0519 0.5431 0.2647  -0.0501 0.0134  118 THR   B CG2 
1170 N N   . LYS   B 110 ? 1.0971 1.0506 0.5040 0.3075  -0.0909 -0.0015 119 LYS   B N   
1171 C CA  . LYS   B 110 ? 1.1253 1.0453 0.4968 0.3187  -0.1043 -0.0045 119 LYS   B CA  
1172 C C   . LYS   B 110 ? 1.1623 1.0260 0.5079 0.3058  -0.1047 -0.0002 119 LYS   B C   
1173 O O   . LYS   B 110 ? 1.1930 1.0183 0.5028 0.3160  -0.1153 -0.0009 119 LYS   B O   
1174 C CB  . LYS   B 110 ? 1.1263 1.0672 0.5052 0.3165  -0.1078 -0.0084 119 LYS   B CB  
1175 C CG  . LYS   B 110 ? 1.1549 1.0884 0.5461 0.2899  -0.0992 -0.0056 119 LYS   B CG  
1176 C CD  . LYS   B 110 ? 1.1867 1.1576 0.5995 0.2863  -0.1008 -0.0107 119 LYS   B CD  
1177 C CE  . LYS   B 110 ? 1.2472 1.1932 0.6465 0.2732  -0.1019 -0.0109 119 LYS   B CE  
1178 N NZ  . LYS   B 110 ? 1.2790 1.2105 0.6900 0.2485  -0.0885 -0.0053 119 LYS   B NZ  
1179 N N   . ASP   B 111 ? 1.1537 1.0129 0.5173 0.2839  -0.0930 0.0044  120 ASP   B N   
1180 C CA  . ASP   B 111 ? 1.1800 0.9947 0.5277 0.2690  -0.0911 0.0085  120 ASP   B CA  
1181 C C   . ASP   B 111 ? 1.1861 0.9866 0.5340 0.2694  -0.0904 0.0098  120 ASP   B C   
1182 O O   . ASP   B 111 ? 1.2036 0.9811 0.5530 0.2522  -0.0855 0.0130  120 ASP   B O   
1183 C CB  . ASP   B 111 ? 1.2021 1.0231 0.5699 0.2442  -0.0792 0.0116  120 ASP   B CB  
1184 C CG  . ASP   B 111 ? 1.2868 1.1081 0.6461 0.2419  -0.0814 0.0103  120 ASP   B CG  
1185 O OD1 . ASP   B 111 ? 1.3244 1.1159 0.6505 0.2522  -0.0909 0.0098  120 ASP   B OD1 
1186 O OD2 . ASP   B 111 ? 1.3059 1.1543 0.6894 0.2303  -0.0742 0.0094  120 ASP   B OD2 
1187 N N   . GLY   B 112 ? 1.1657 0.9819 0.5134 0.2890  -0.0951 0.0069  121 GLY   B N   
1188 C CA  . GLY   B 112 ? 1.1715 0.9731 0.5161 0.2925  -0.0965 0.0068  121 GLY   B CA  
1189 C C   . GLY   B 112 ? 1.1451 0.9846 0.5162 0.2959  -0.0879 0.0071  121 GLY   B C   
1190 O O   . GLY   B 112 ? 1.1247 1.0040 0.5214 0.2916  -0.0786 0.0085  121 GLY   B O   
1191 N N   . ASP   B 113 ? 1.1421 0.9677 0.5057 0.3039  -0.0913 0.0059  122 ASP   B N   
1192 C CA  . ASP   B 113 ? 1.1257 0.9817 0.5083 0.3097  -0.0833 0.0068  122 ASP   B CA  
1193 C C   . ASP   B 113 ? 1.1037 0.9591 0.5073 0.2884  -0.0734 0.0101  122 ASP   B C   
1194 O O   . ASP   B 113 ? 1.1194 0.9438 0.5174 0.2750  -0.0766 0.0097  122 ASP   B O   
1195 C CB  . ASP   B 113 ? 1.1695 1.0127 0.5295 0.3346  -0.0935 0.0027  122 ASP   B CB  
1196 C CG  . ASP   B 113 ? 1.2675 1.1170 0.6070 0.3610  -0.1028 -0.0011 122 ASP   B CG  
1197 O OD1 . ASP   B 113 ? 1.2724 1.1448 0.6199 0.3609  -0.1005 -0.0006 122 ASP   B OD1 
1198 O OD2 . ASP   B 113 ? 1.3257 1.1573 0.6404 0.3832  -0.1134 -0.0055 122 ASP   B OD2 
1199 N N   . ILE   B 114 ? 1.0617 0.9521 0.4897 0.2855  -0.0610 0.0134  123 ILE   B N   
1200 C CA  . ILE   B 114 ? 1.0394 0.9330 0.4866 0.2691  -0.0511 0.0164  123 ILE   B CA  
1201 C C   . ILE   B 114 ? 1.0091 0.9196 0.4588 0.2841  -0.0469 0.0176  123 ILE   B C   
1202 O O   . ILE   B 114 ? 0.9896 0.9263 0.4398 0.2995  -0.0441 0.0188  123 ILE   B O   
1203 C CB  . ILE   B 114 ? 1.0298 0.9467 0.5019 0.2501  -0.0389 0.0203  123 ILE   B CB  
1204 C CG1 . ILE   B 114 ? 1.0598 0.9639 0.5260 0.2399  -0.0430 0.0190  123 ILE   B CG1 
1205 C CG2 . ILE   B 114 ? 1.0288 0.9448 0.5176 0.2342  -0.0295 0.0229  123 ILE   B CG2 
1206 C CD1 . ILE   B 114 ? 1.0679 0.9998 0.5520 0.2312  -0.0360 0.0205  123 ILE   B CD1 
1207 N N   . GLY   B 115 ? 0.9960 0.8936 0.4475 0.2801  -0.0461 0.0173  124 GLY   B N   
1208 C CA  . GLY   B 115 ? 0.9870 0.8983 0.4386 0.2940  -0.0411 0.0191  124 GLY   B CA  
1209 C C   . GLY   B 115 ? 0.9633 0.9085 0.4378 0.2859  -0.0243 0.0263  124 GLY   B C   
1210 O O   . GLY   B 115 ? 0.9580 0.9100 0.4498 0.2662  -0.0177 0.0287  124 GLY   B O   
1211 N N   . ALA   B 116 ? 0.9499 0.9157 0.4232 0.3011  -0.0172 0.0301  125 ALA   B N   
1212 C CA  . ALA   B 116 ? 0.9353 0.9319 0.4295 0.2929  -0.0004 0.0380  125 ALA   B CA  
1213 C C   . ALA   B 116 ? 0.9396 0.9401 0.4272 0.3055  0.0074  0.0426  125 ALA   B C   
1214 O O   . ALA   B 116 ? 0.9607 0.9534 0.4277 0.3272  0.0006  0.0397  125 ALA   B O   
1215 C CB  . ALA   B 116 ? 0.9200 0.9489 0.4228 0.2982  0.0033  0.0398  125 ALA   B CB  
1216 N N   A VAL   B 117 ? 0.9322 0.9416 0.4345 0.2926  0.0211  0.0497  126 VAL   B N   
1217 N N   B VAL   B 117 ? 0.9307 0.9407 0.4332 0.2927  0.0212  0.0497  126 VAL   B N   
1218 N N   C VAL   B 117 ? 0.9322 0.9416 0.4345 0.2926  0.0211  0.0497  126 VAL   B N   
1219 N N   D VAL   B 117 ? 0.9307 0.9407 0.4332 0.2927  0.0212  0.0497  126 VAL   B N   
1220 C CA  A VAL   B 117 ? 0.9422 0.9531 0.4360 0.3041  0.0300  0.0554  126 VAL   B CA  
1221 C CA  B VAL   B 117 ? 0.9399 0.9507 0.4343 0.3033  0.0301  0.0554  126 VAL   B CA  
1222 C CA  C VAL   B 117 ? 0.9422 0.9531 0.4360 0.3041  0.0300  0.0554  126 VAL   B CA  
1223 C CA  D VAL   B 117 ? 0.9399 0.9507 0.4343 0.3033  0.0301  0.0554  126 VAL   B CA  
1224 C C   A VAL   B 117 ? 0.9324 0.9759 0.4408 0.3005  0.0486  0.0661  126 VAL   B C   
1225 C C   B VAL   B 117 ? 0.9308 0.9746 0.4395 0.3003  0.0486  0.0661  126 VAL   B C   
1226 C C   C VAL   B 117 ? 0.9324 0.9759 0.4408 0.3005  0.0486  0.0661  126 VAL   B C   
1227 C C   D VAL   B 117 ? 0.9308 0.9746 0.4395 0.3003  0.0486  0.0661  126 VAL   B C   
1228 O O   A VAL   B 117 ? 0.9214 0.9750 0.4512 0.2790  0.0573  0.0703  126 VAL   B O   
1229 O O   B VAL   B 117 ? 0.9195 0.9740 0.4498 0.2788  0.0573  0.0703  126 VAL   B O   
1230 O O   C VAL   B 117 ? 0.9214 0.9750 0.4512 0.2790  0.0573  0.0703  126 VAL   B O   
1231 O O   D VAL   B 117 ? 0.9195 0.9740 0.4498 0.2788  0.0573  0.0703  126 VAL   B O   
1232 C CB  A VAL   B 117 ? 0.9594 0.9446 0.4502 0.2969  0.0286  0.0543  126 VAL   B CB  
1233 C CB  B VAL   B 117 ? 0.9541 0.9398 0.4487 0.2925  0.0288  0.0542  126 VAL   B CB  
1234 C CB  C VAL   B 117 ? 0.9594 0.9446 0.4502 0.2969  0.0286  0.0543  126 VAL   B CB  
1235 C CB  D VAL   B 117 ? 0.9541 0.9398 0.4487 0.2925  0.0288  0.0542  126 VAL   B CB  
1236 C CG1 A VAL   B 117 ? 0.9800 0.9374 0.4534 0.3074  0.0107  0.0442  126 VAL   B CG1 
1237 C CG1 B VAL   B 117 ? 0.9590 0.9471 0.4493 0.2976  0.0418  0.0625  126 VAL   B CG1 
1238 C CG1 C VAL   B 117 ? 0.9800 0.9374 0.4534 0.3074  0.0107  0.0442  126 VAL   B CG1 
1239 C CG1 D VAL   B 117 ? 0.9590 0.9471 0.4493 0.2976  0.0418  0.0625  126 VAL   B CG1 
1240 C CG2 A VAL   B 117 ? 0.9588 0.9414 0.4704 0.2705  0.0334  0.0555  126 VAL   B CG2 
1241 C CG2 B VAL   B 117 ? 0.9739 0.9313 0.4521 0.3015  0.0112  0.0441  126 VAL   B CG2 
1242 C CG2 C VAL   B 117 ? 0.9588 0.9414 0.4704 0.2705  0.0334  0.0555  126 VAL   B CG2 
1243 C CG2 D VAL   B 117 ? 0.9739 0.9313 0.4521 0.3015  0.0112  0.0441  126 VAL   B CG2 
1244 N N   . ALA   B 118 ? 0.9316 0.9916 0.4282 0.3217  0.0546  0.0703  127 ALA   B N   
1245 C CA  . ALA   B 118 ? 0.9339 1.0278 0.4447 0.3191  0.0736  0.0814  127 ALA   B CA  
1246 C C   . ALA   B 118 ? 0.9600 1.0452 0.4637 0.3187  0.0876  0.0911  127 ALA   B C   
1247 O O   . ALA   B 118 ? 0.9694 1.0611 0.4559 0.3389  0.0953  0.0967  127 ALA   B O   
1248 C CB  . ALA   B 118 ? 0.9275 1.0488 0.4305 0.3427  0.0748  0.0815  127 ALA   B CB  
1249 N N   . LEU   B 119 ? 0.9660 1.0337 0.4797 0.2974  0.0903  0.0929  128 LEU   B N   
1250 C CA  . LEU   B 119 ? 0.9758 1.0306 0.4820 0.2949  0.1029  0.1022  128 LEU   B CA  
1251 C C   . LEU   B 119 ? 0.9681 1.0316 0.5004 0.2662  0.1144  0.1087  128 LEU   B C   
1252 O O   . LEU   B 119 ? 0.9687 1.0268 0.5161 0.2489  0.1061  0.1020  128 LEU   B O   
1253 C CB  . LEU   B 119 ? 0.9938 1.0116 0.4814 0.3011  0.0910  0.0955  128 LEU   B CB  
1254 C CG  . LEU   B 119 ? 1.0170 1.0222 0.4785 0.3285  0.0773  0.0877  128 LEU   B CG  
1255 C CD1 . LEU   B 119 ? 1.0344 1.0074 0.4860 0.3294  0.0629  0.0787  128 LEU   B CD1 
1256 C CD2 . LEU   B 119 ? 1.0308 1.0440 0.4706 0.3517  0.0885  0.0963  128 LEU   B CD2 
1257 N N   C ASP   B 120 ? 0.9621 1.0383 0.4986 0.2611  0.1334  0.1218  129 ASP   B N   
1258 N N   D ASP   B 120 ? 0.9621 1.0383 0.4986 0.2611  0.1334  0.1218  129 ASP   B N   
1259 C CA  C ASP   B 120 ? 0.9554 1.0384 0.5160 0.2332  0.1442  0.1283  129 ASP   B CA  
1260 C CA  D ASP   B 120 ? 0.9554 1.0384 0.5160 0.2332  0.1442  0.1283  129 ASP   B CA  
1261 C C   C ASP   B 120 ? 0.9672 1.0161 0.5163 0.2248  0.1496  0.1335  129 ASP   B C   
1262 C C   D ASP   B 120 ? 0.9672 1.0161 0.5163 0.2248  0.1496  0.1335  129 ASP   B C   
1263 O O   C ASP   B 120 ? 0.9820 1.0193 0.5102 0.2374  0.1595  0.1424  129 ASP   B O   
1264 O O   D ASP   B 120 ? 0.9820 1.0193 0.5102 0.2374  0.1595  0.1424  129 ASP   B O   
1265 C CB  C ASP   B 120 ? 0.9637 1.0849 0.5408 0.2288  0.1623  0.1398  129 ASP   B CB  
1266 C CB  D ASP   B 120 ? 0.9637 1.0849 0.5408 0.2288  0.1623  0.1398  129 ASP   B CB  
1267 C CG  C ASP   B 120 ? 1.0153 1.1558 0.6262 0.1995  0.1671  0.1412  129 ASP   B CG  
1268 C CG  D ASP   B 120 ? 1.0153 1.1558 0.6262 0.1995  0.1671  0.1412  129 ASP   B CG  
1269 O OD1 C ASP   B 120 ? 1.0288 1.1443 0.6442 0.1800  0.1658  0.1407  129 ASP   B OD1 
1270 O OD1 D ASP   B 120 ? 1.0288 1.1443 0.6442 0.1800  0.1658  0.1407  129 ASP   B OD1 
1271 O OD2 C ASP   B 120 ? 1.0305 1.2115 0.6633 0.1969  0.1715  0.1422  129 ASP   B OD2 
1272 O OD2 D ASP   B 120 ? 1.0305 1.2115 0.6633 0.1969  0.1715  0.1422  129 ASP   B OD2 
1273 N N   . TYR   B 121 ? 0.9618 0.9937 0.5222 0.2053  0.1431  0.1280  130 TYR   B N   
1274 C CA  . TYR   B 121 ? 0.9705 0.9687 0.5204 0.1974  0.1462  0.1311  130 TYR   B CA  
1275 C C   . TYR   B 121 ? 0.9519 0.9482 0.5239 0.1688  0.1494  0.1318  130 TYR   B C   
1276 O O   . TYR   B 121 ? 0.9383 0.9556 0.5324 0.1569  0.1439  0.1258  130 TYR   B O   
1277 C CB  . TYR   B 121 ? 0.9879 0.9596 0.5218 0.2095  0.1300  0.1197  130 TYR   B CB  
1278 C CG  . TYR   B 121 ? 1.0155 0.9765 0.5220 0.2362  0.1285  0.1210  130 TYR   B CG  
1279 C CD1 . TYR   B 121 ? 1.0422 0.9808 0.5277 0.2436  0.1374  0.1294  130 TYR   B CD1 
1280 C CD2 . TYR   B 121 ? 1.0294 1.0013 0.5283 0.2552  0.1182  0.1141  130 TYR   B CD2 
1281 C CE1 . TYR   B 121 ? 1.0687 0.9977 0.5266 0.2700  0.1357  0.1305  130 TYR   B CE1 
1282 C CE2 . TYR   B 121 ? 1.0535 1.0153 0.5256 0.2808  0.1160  0.1146  130 TYR   B CE2 
1283 C CZ  . TYR   B 121 ? 1.0801 1.0215 0.5319 0.2885  0.1247  0.1226  130 TYR   B CZ  
1284 O OH  . TYR   B 121 ? 1.1199 1.0501 0.5428 0.3155  0.1214  0.1224  130 TYR   B OH  
1285 N N   . PRO   B 122 ? 0.9500 0.9188 0.5142 0.1585  0.1569  0.1381  131 PRO   B N   
1286 C CA  . PRO   B 122 ? 0.9336 0.8971 0.5165 0.1319  0.1585  0.1377  131 PRO   B CA  
1287 C C   . PRO   B 122 ? 0.9131 0.8737 0.5070 0.1245  0.1423  0.1230  131 PRO   B C   
1288 O O   . PRO   B 122 ? 0.9185 0.8712 0.5020 0.1387  0.1307  0.1142  131 PRO   B O   
1289 C CB  . PRO   B 122 ? 0.9627 0.8887 0.5262 0.1289  0.1668  0.1457  131 PRO   B CB  
1290 C CG  . PRO   B 122 ? 0.9815 0.9027 0.5203 0.1510  0.1753  0.1550  131 PRO   B CG  
1291 C CD  . PRO   B 122 ? 0.9623 0.9021 0.4981 0.1719  0.1639  0.1459  131 PRO   B CD  
1292 N N   . ALA   B 123 ? 0.8877 0.8547 0.5022 0.1024  0.1413  0.1205  132 ALA   B N   
1293 C CA  . ALA   B 123 ? 0.8809 0.8450 0.5034 0.0958  0.1271  0.1073  132 ALA   B CA  
1294 C C   . ALA   B 123 ? 0.8814 0.8123 0.4860 0.1026  0.1196  0.1006  132 ALA   B C   
1295 O O   . ALA   B 123 ? 0.8721 0.8038 0.4764 0.1081  0.1082  0.0906  132 ALA   B O   
1296 C CB  . ALA   B 123 ? 0.8754 0.8463 0.5189 0.0717  0.1276  0.1060  132 ALA   B CB  
1297 N N   . GLY   B 124 ? 0.8802 0.7835 0.4689 0.1042  0.1265  0.1068  133 GLY   B N   
1298 C CA  . GLY   B 124 ? 0.8786 0.7529 0.4506 0.1128  0.1202  0.1007  133 GLY   B CA  
1299 C C   . GLY   B 124 ? 0.8624 0.7373 0.4219 0.1350  0.1132  0.0961  133 GLY   B C   
1300 O O   . GLY   B 124 ? 0.8675 0.7232 0.4160 0.1431  0.1073  0.0902  133 GLY   B O   
1301 N N   . THR   B 125 ? 0.8448 0.7416 0.4053 0.1457  0.1135  0.0985  134 THR   B N   
1302 C CA  . THR   B 125 ? 0.8471 0.7456 0.3967 0.1662  0.1047  0.0930  134 THR   B CA  
1303 C C   . THR   B 125 ? 0.8244 0.7338 0.3858 0.1634  0.0918  0.0813  134 THR   B C   
1304 O O   . THR   B 125 ? 0.8287 0.7352 0.3836 0.1760  0.0824  0.0747  134 THR   B O   
1305 C CB  . THR   B 125 ? 0.8774 0.7902 0.4182 0.1809  0.1111  0.1011  134 THR   B CB  
1306 O OG1 . THR   B 125 ? 0.9037 0.8050 0.4332 0.1807  0.1251  0.1134  134 THR   B OG1 
1307 C CG2 . THR   B 125 ? 0.8869 0.7962 0.4119 0.2040  0.1012  0.0954  134 THR   B CG2 
1308 N N   . SER   B 126 ? 0.8024 0.7228 0.3802 0.1466  0.0911  0.0789  135 SER   B N   
1309 C CA  . SER   B 126 ? 0.7928 0.7205 0.3789 0.1426  0.0805  0.0694  135 SER   B CA  
1310 C C   . SER   B 126 ? 0.7932 0.7046 0.3739 0.1462  0.0727  0.0611  135 SER   B C   
1311 O O   . SER   B 126 ? 0.8029 0.6987 0.3817 0.1410  0.0748  0.0599  135 SER   B O   
1312 C CB  . SER   B 126 ? 0.7940 0.7289 0.3945 0.1240  0.0816  0.0682  135 SER   B CB  
1313 O OG  . SER   B 126 ? 0.8091 0.7685 0.4202 0.1213  0.0847  0.0724  135 SER   B OG  
1314 N N   . GLY   B 127 ? 0.7783 0.6938 0.3570 0.1546  0.0636  0.0554  136 GLY   B N   
1315 C CA  . GLY   B 127 ? 0.7810 0.6858 0.3579 0.1574  0.0563  0.0477  136 GLY   B CA  
1316 C C   . GLY   B 127 ? 0.7916 0.6909 0.3586 0.1743  0.0515  0.0461  136 GLY   B C   
1317 O O   . GLY   B 127 ? 0.7993 0.6932 0.3677 0.1770  0.0444  0.0390  136 GLY   B O   
1318 N N   . SER   B 128 ? 0.7891 0.6903 0.3463 0.1861  0.0555  0.0525  137 SER   B N   
1319 C CA  . SER   B 128 ? 0.8007 0.6957 0.3448 0.2048  0.0500  0.0508  137 SER   B CA  
1320 C C   . SER   B 128 ? 0.7996 0.6988 0.3440 0.2106  0.0376  0.0434  137 SER   B C   
1321 O O   . SER   B 128 ? 0.7994 0.7084 0.3466 0.2073  0.0363  0.0442  137 SER   B O   
1322 C CB  . SER   B 128 ? 0.8177 0.7148 0.3487 0.2163  0.0584  0.0603  137 SER   B CB  
1323 O OG  . SER   B 128 ? 0.8378 0.7240 0.3639 0.2130  0.0691  0.0673  137 SER   B OG  
1324 N N   . PRO   B 129 ? 0.7954 0.6867 0.3377 0.2182  0.0275  0.0356  138 PRO   B N   
1325 C CA  . PRO   B 129 ? 0.7936 0.6846 0.3361 0.2214  0.0147  0.0283  138 PRO   B CA  
1326 C C   . PRO   B 129 ? 0.8048 0.6955 0.3313 0.2394  0.0087  0.0287  138 PRO   B C   
1327 O O   . PRO   B 129 ? 0.8084 0.6968 0.3210 0.2554  0.0109  0.0319  138 PRO   B O   
1328 C CB  . PRO   B 129 ? 0.7993 0.6840 0.3481 0.2222  0.0063  0.0196  138 PRO   B CB  
1329 C CG  . PRO   B 129 ? 0.8086 0.6886 0.3497 0.2325  0.0116  0.0224  138 PRO   B CG  
1330 C CD  . PRO   B 129 ? 0.7850 0.6671 0.3254 0.2241  0.0263  0.0324  138 PRO   B CD  
1331 N N   . ILE   B 130 ? 0.8041 0.6946 0.3297 0.2385  0.0004  0.0250  139 ILE   B N   
1332 C CA  . ILE   B 130 ? 0.8268 0.7144 0.3357 0.2565  -0.0082 0.0231  139 ILE   B CA  
1333 C C   . ILE   B 130 ? 0.8529 0.7262 0.3607 0.2588  -0.0246 0.0124  139 ILE   B C   
1334 O O   . ILE   B 130 ? 0.8427 0.7123 0.3632 0.2428  -0.0283 0.0084  139 ILE   B O   
1335 C CB  . ILE   B 130 ? 0.8248 0.7213 0.3316 0.2549  -0.0061 0.0266  139 ILE   B CB  
1336 C CG1 . ILE   B 130 ? 0.8280 0.7421 0.3411 0.2499  0.0100  0.0365  139 ILE   B CG1 
1337 C CG2 . ILE   B 130 ? 0.8324 0.7239 0.3196 0.2754  -0.0164 0.0233  139 ILE   B CG2 
1338 C CD1 . ILE   B 130 ? 0.8422 0.7667 0.3652 0.2371  0.0124  0.0379  139 ILE   B CD1 
1339 N N   . LEU   B 131 ? 0.8774 0.7426 0.3705 0.2778  -0.0342 0.0077  140 LEU   B N   
1340 C CA  . LEU   B 131 ? 0.9075 0.7598 0.4021 0.2792  -0.0510 -0.0035 140 LEU   B CA  
1341 C C   . LEU   B 131 ? 0.9316 0.7707 0.4067 0.2958  -0.0661 -0.0097 140 LEU   B C   
1342 O O   . LEU   B 131 ? 0.9484 0.7891 0.4042 0.3141  -0.0637 -0.0058 140 LEU   B O   
1343 C CB  . LEU   B 131 ? 0.9184 0.7704 0.4171 0.2852  -0.0538 -0.0081 140 LEU   B CB  
1344 C CG  . LEU   B 131 ? 0.9405 0.7991 0.4340 0.2925  -0.0399 0.0001  140 LEU   B CG  
1345 C CD1 . LEU   B 131 ? 0.9387 0.7906 0.4218 0.3107  -0.0484 -0.0059 140 LEU   B CD1 
1346 C CD2 . LEU   B 131 ? 0.9435 0.8104 0.4563 0.2722  -0.0270 0.0048  140 LEU   B CD2 
1347 N N   . ASP   B 132 ? 0.9396 0.7650 0.4194 0.2897  -0.0818 -0.0196 141 ASP   B N   
1348 C CA  . ASP   B 132 ? 0.9655 0.7726 0.4258 0.3049  -0.0996 -0.0276 141 ASP   B CA  
1349 C C   . ASP   B 132 ? 0.9963 0.7969 0.4493 0.3216  -0.1128 -0.0370 141 ASP   B C   
1350 O O   . ASP   B 132 ? 0.9940 0.8050 0.4585 0.3204  -0.1078 -0.0369 141 ASP   B O   
1351 C CB  . ASP   B 132 ? 0.9689 0.7603 0.4351 0.2884  -0.1100 -0.0326 141 ASP   B CB  
1352 C CG  . ASP   B 132 ? 0.9959 0.7867 0.4877 0.2666  -0.1142 -0.0383 141 ASP   B CG  
1353 O OD1 . ASP   B 132 ? 0.9858 0.7835 0.4882 0.2694  -0.1181 -0.0439 141 ASP   B OD1 
1354 O OD2 . ASP   B 132 ? 1.0421 0.8262 0.5427 0.2475  -0.1134 -0.0370 141 ASP   B OD2 
1355 N N   . LYS   B 133 ? 1.0243 0.8064 0.4572 0.3380  -0.1309 -0.0458 142 LYS   B N   
1356 C CA  . LYS   B 133 ? 1.0595 0.8340 0.4820 0.3567  -0.1458 -0.0560 142 LYS   B CA  
1357 C C   . LYS   B 133 ? 1.0575 0.8361 0.5073 0.3416  -0.1543 -0.0651 142 LYS   B C   
1358 O O   . LYS   B 133 ? 1.0505 0.8308 0.4969 0.3560  -0.1622 -0.0717 142 LYS   B O   
1359 C CB  . LYS   B 133 ? 1.1313 0.8821 0.5259 0.3765  -0.1656 -0.0652 142 LYS   B CB  
1360 C CG  . LYS   B 133 ? 1.2272 0.9786 0.5897 0.4030  -0.1582 -0.0582 142 LYS   B CG  
1361 C CD  . LYS   B 133 ? 1.3154 1.0504 0.6594 0.4085  -0.1661 -0.0598 142 LYS   B CD  
1362 C CE  . LYS   B 133 ? 1.3861 1.1193 0.6946 0.4418  -0.1655 -0.0580 142 LYS   B CE  
1363 N NZ  . LYS   B 133 ? 1.4349 1.1488 0.7216 0.4518  -0.1772 -0.0624 142 LYS   B NZ  
1364 N N   . CYS   B 134 ? 1.0518 0.8344 0.5285 0.3135  -0.1515 -0.0649 143 CYS   B N   
1365 C CA  . CYS   B 134 ? 1.0482 0.8407 0.5552 0.2975  -0.1569 -0.0727 143 CYS   B CA  
1366 C C   . CYS   B 134 ? 1.0191 0.8348 0.5447 0.2898  -0.1389 -0.0657 143 CYS   B C   
1367 O O   . CYS   B 134 ? 1.0117 0.8397 0.5630 0.2786  -0.1418 -0.0720 143 CYS   B O   
1368 C CB  . CYS   B 134 ? 1.0756 0.8600 0.6014 0.2720  -0.1635 -0.0765 143 CYS   B CB  
1369 S SG  . CYS   B 134 ? 1.1976 0.9483 0.7015 0.2793  -0.1883 -0.0868 143 CYS   B SG  
1370 N N   . GLY   B 135 ? 1.0029 0.8246 0.5164 0.2957  -0.1211 -0.0535 144 GLY   B N   
1371 C CA  . GLY   B 135 ? 0.9805 0.8190 0.5077 0.2881  -0.1040 -0.0462 144 GLY   B CA  
1372 C C   . GLY   B 135 ? 0.9515 0.7983 0.4993 0.2620  -0.0915 -0.0403 144 GLY   B C   
1373 O O   . GLY   B 135 ? 0.9492 0.8085 0.5098 0.2541  -0.0787 -0.0359 144 GLY   B O   
1374 N N   . ARG   B 136 ? 0.9344 0.7719 0.4830 0.2496  -0.0953 -0.0403 145 ARG   B N   
1375 C CA  . ARG   B 136 ? 0.9210 0.7637 0.4850 0.2263  -0.0839 -0.0345 145 ARG   B CA  
1376 C C   . ARG   B 136 ? 0.9005 0.7470 0.4536 0.2267  -0.0681 -0.0228 145 ARG   B C   
1377 O O   . ARG   B 136 ? 0.9128 0.7536 0.4454 0.2412  -0.0690 -0.0194 145 ARG   B O   
1378 C CB  . ARG   B 136 ? 0.9441 0.7716 0.5099 0.2133  -0.0943 -0.0385 145 ARG   B CB  
1379 C CG  . ARG   B 136 ? 0.9841 0.8122 0.5699 0.2046  -0.1074 -0.0495 145 ARG   B CG  
1380 C CD  . ARG   B 136 ? 1.0545 0.8627 0.6390 0.1913  -0.1178 -0.0525 145 ARG   B CD  
1381 N NE  . ARG   B 136 ? 1.1418 0.9270 0.6981 0.2090  -0.1319 -0.0557 145 ARG   B NE  
1382 C CZ  . ARG   B 136 ? 1.2077 0.9691 0.7481 0.2048  -0.1381 -0.0544 145 ARG   B CZ  
1383 N NH1 . ARG   B 136 ? 1.2028 0.9589 0.7517 0.1826  -0.1308 -0.0491 145 ARG   B NH1 
1384 N NH2 . ARG   B 136 ? 1.2393 0.9804 0.7522 0.2244  -0.1516 -0.0584 145 ARG   B NH2 
1385 N N   . VAL   B 137 ? 0.8711 0.7286 0.4381 0.2116  -0.0541 -0.0172 146 VAL   B N   
1386 C CA  . VAL   B 137 ? 0.8591 0.7216 0.4192 0.2097  -0.0403 -0.0073 146 VAL   B CA  
1387 C C   . VAL   B 137 ? 0.8591 0.7133 0.4128 0.2016  -0.0419 -0.0049 146 VAL   B C   
1388 O O   . VAL   B 137 ? 0.8639 0.7147 0.4275 0.1853  -0.0417 -0.0060 146 VAL   B O   
1389 C CB  . VAL   B 137 ? 0.8592 0.7334 0.4340 0.1978  -0.0266 -0.0036 146 VAL   B CB  
1390 C CG1 . VAL   B 137 ? 0.8674 0.7462 0.4360 0.1953  -0.0141 0.0056  146 VAL   B CG1 
1391 C CG2 . VAL   B 137 ? 0.8556 0.7351 0.4353 0.2068  -0.0265 -0.0069 146 VAL   B CG2 
1392 N N   . ILE   B 138 ? 0.8556 0.7063 0.3914 0.2145  -0.0437 -0.0018 147 ILE   B N   
1393 C CA  . ILE   B 138 ? 0.8505 0.6930 0.3760 0.2117  -0.0463 0.0002  147 ILE   B CA  
1394 C C   . ILE   B 138 ? 0.8321 0.6876 0.3601 0.2051  -0.0331 0.0081  147 ILE   B C   
1395 O O   . ILE   B 138 ? 0.8408 0.6916 0.3605 0.2033  -0.0349 0.0098  147 ILE   B O   
1396 C CB  . ILE   B 138 ? 0.8652 0.6971 0.3686 0.2323  -0.0579 -0.0026 147 ILE   B CB  
1397 C CG1 . ILE   B 138 ? 0.8757 0.7219 0.3705 0.2501  -0.0507 0.0022  147 ILE   B CG1 
1398 C CG2 . ILE   B 138 ? 0.8741 0.6890 0.3743 0.2366  -0.0740 -0.0120 147 ILE   B CG2 
1399 C CD1 . ILE   B 138 ? 0.9073 0.7476 0.3793 0.2716  -0.0588 0.0008  147 ILE   B CD1 
1400 N N   . GLY   B 139 ? 0.8015 0.6714 0.3400 0.2016  -0.0213 0.0123  148 GLY   B N   
1401 C CA  . GLY   B 139 ? 0.7898 0.6717 0.3328 0.1938  -0.0101 0.0186  148 GLY   B CA  
1402 C C   . GLY   B 139 ? 0.7804 0.6743 0.3299 0.1946  0.0012  0.0234  148 GLY   B C   
1403 O O   . GLY   B 139 ? 0.7744 0.6666 0.3218 0.2039  0.0007  0.0225  148 GLY   B O   
1404 N N   . LEU   B 140 ? 0.7757 0.6795 0.3321 0.1847  0.0107  0.0282  149 LEU   B N   
1405 C CA  . LEU   B 140 ? 0.7738 0.6856 0.3355 0.1829  0.0218  0.0335  149 LEU   B CA  
1406 C C   . LEU   B 140 ? 0.7809 0.7080 0.3414 0.1865  0.0276  0.0397  149 LEU   B C   
1407 O O   . LEU   B 140 ? 0.7751 0.7092 0.3358 0.1844  0.0246  0.0392  149 LEU   B O   
1408 C CB  . LEU   B 140 ? 0.7652 0.6755 0.3379 0.1666  0.0281  0.0332  149 LEU   B CB  
1409 C CG  . LEU   B 140 ? 0.7790 0.6800 0.3569 0.1610  0.0250  0.0274  149 LEU   B CG  
1410 C CD1 . LEU   B 140 ? 0.7817 0.6823 0.3675 0.1475  0.0326  0.0275  149 LEU   B CD1 
1411 C CD2 . LEU   B 140 ? 0.7814 0.6780 0.3572 0.1723  0.0218  0.0248  149 LEU   B CD2 
1412 N N   . TYR   B 141 ? 0.7835 0.7161 0.3429 0.1918  0.0362  0.0458  150 TYR   B N   
1413 C CA  . TYR   B 141 ? 0.7829 0.7330 0.3436 0.1950  0.0447  0.0532  150 TYR   B CA  
1414 C C   . TYR   B 141 ? 0.7889 0.7457 0.3636 0.1773  0.0542  0.0572  150 TYR   B C   
1415 O O   . TYR   B 141 ? 0.8056 0.7497 0.3824 0.1692  0.0576  0.0572  150 TYR   B O   
1416 C CB  . TYR   B 141 ? 0.7878 0.7353 0.3370 0.2097  0.0502  0.0584  150 TYR   B CB  
1417 C CG  . TYR   B 141 ? 0.7869 0.7522 0.3383 0.2112  0.0630  0.0683  150 TYR   B CG  
1418 C CD1 . TYR   B 141 ? 0.7973 0.7612 0.3551 0.1994  0.0753  0.0756  150 TYR   B CD1 
1419 C CD2 . TYR   B 141 ? 0.7877 0.7707 0.3344 0.2244  0.0633  0.0705  150 TYR   B CD2 
1420 C CE1 . TYR   B 141 ? 0.8086 0.7894 0.3704 0.1982  0.0883  0.0857  150 TYR   B CE1 
1421 C CE2 . TYR   B 141 ? 0.7940 0.7974 0.3448 0.2256  0.0768  0.0802  150 TYR   B CE2 
1422 C CZ  . TYR   B 141 ? 0.8074 0.8100 0.3668 0.2112  0.0898  0.0882  150 TYR   B CZ  
1423 O OH  . TYR   B 141 ? 0.8053 0.8291 0.3716 0.2092  0.1044  0.0987  150 TYR   B OH  
1424 N N   . GLY   B 142 ? 0.7783 0.7553 0.3622 0.1726  0.0581  0.0605  151 GLY   B N   
1425 C CA  . GLY   B 142 ? 0.7836 0.7671 0.3819 0.1549  0.0657  0.0636  151 GLY   B CA  
1426 C C   . GLY   B 142 ? 0.7860 0.7851 0.3966 0.1449  0.0618  0.0601  151 GLY   B C   
1427 O O   . GLY   B 142 ? 0.7941 0.7987 0.4174 0.1297  0.0667  0.0617  151 GLY   B O   
1428 N N   . ASN   B 143 ? 0.7748 0.7791 0.3803 0.1533  0.0521  0.0550  152 ASN   B N   
1429 C CA  . ASN   B 143 ? 0.7661 0.7868 0.3809 0.1471  0.0475  0.0515  152 ASN   B CA  
1430 C C   . ASN   B 143 ? 0.7747 0.8163 0.3869 0.1629  0.0440  0.0517  152 ASN   B C   
1431 O O   . ASN   B 143 ? 0.7793 0.8100 0.3756 0.1768  0.0359  0.0485  152 ASN   B O   
1432 C CB  . ASN   B 143 ? 0.7671 0.7709 0.3758 0.1409  0.0384  0.0443  152 ASN   B CB  
1433 C CG  . ASN   B 143 ? 0.7711 0.7898 0.3879 0.1342  0.0336  0.0405  152 ASN   B CG  
1434 O OD1 . ASN   B 143 ? 0.7601 0.8023 0.3930 0.1287  0.0376  0.0425  152 ASN   B OD1 
1435 N ND2 . ASN   B 143 ? 0.7695 0.7750 0.3752 0.1346  0.0248  0.0350  152 ASN   B ND2 
1436 N N   . GLY   B 144 ? 0.7770 0.8483 0.4050 0.1606  0.0499  0.0553  153 GLY   B N   
1437 C CA  . GLY   B 144 ? 0.8066 0.9027 0.4335 0.1774  0.0477  0.0554  153 GLY   B CA  
1438 C C   . GLY   B 144 ? 0.8239 0.9586 0.4737 0.1723  0.0518  0.0567  153 GLY   B C   
1439 O O   . GLY   B 144 ? 0.8191 0.9608 0.4834 0.1571  0.0489  0.0530  153 GLY   B O   
1440 N N   . VAL   B 145 ? 0.8404 1.0020 0.4936 0.1859  0.0582  0.0614  154 VAL   B N   
1441 C CA  . VAL   B 145 ? 0.8476 1.0530 0.5248 0.1838  0.0620  0.0621  154 VAL   B CA  
1442 C C   . VAL   B 145 ? 0.8680 1.1014 0.5564 0.1873  0.0789  0.0726  154 VAL   B C   
1443 O O   . VAL   B 145 ? 0.8737 1.0907 0.5452 0.1969  0.0861  0.0789  154 VAL   B O   
1444 C CB  . VAL   B 145 ? 0.8533 1.0703 0.5212 0.2030  0.0479  0.0536  154 VAL   B CB  
1445 C CG1 . VAL   B 145 ? 0.8578 1.0825 0.5088 0.2297  0.0490  0.0557  154 VAL   B CG1 
1446 C CG2 . VAL   B 145 ? 0.8431 1.0985 0.5367 0.1962  0.0446  0.0492  154 VAL   B CG2 
1447 N N   . VAL   B 146 ? 0.8734 1.1493 0.5910 0.1785  0.0854  0.0747  155 VAL   B N   
1448 C CA  . VAL   B 146 ? 0.8933 1.2032 0.6263 0.1796  0.1030  0.0852  155 VAL   B CA  
1449 C C   . VAL   B 146 ? 0.9144 1.2621 0.6488 0.2035  0.0993  0.0815  155 VAL   B C   
1450 O O   . VAL   B 146 ? 0.9010 1.2736 0.6510 0.2031  0.0891  0.0731  155 VAL   B O   
1451 C CB  . VAL   B 146 ? 0.8867 1.2199 0.6545 0.1510  0.1130  0.0899  155 VAL   B CB  
1452 C CG1 . VAL   B 146 ? 0.8786 1.2539 0.6655 0.1519  0.1323  0.1013  155 VAL   B CG1 
1453 C CG2 . VAL   B 146 ? 0.9101 1.2014 0.6718 0.1300  0.1164  0.0934  155 VAL   B CG2 
1454 N N   . ILE   B 147 ? 0.9436 1.2932 0.6585 0.2268  0.1059  0.0867  156 ILE   B N   
1455 C CA  . ILE   B 147 ? 0.9626 1.3437 0.6730 0.2539  0.1013  0.0823  156 ILE   B CA  
1456 C C   . ILE   B 147 ? 0.9604 1.4028 0.7033 0.2523  0.1176  0.0893  156 ILE   B C   
1457 O O   . ILE   B 147 ? 0.9496 1.4044 0.7158 0.2290  0.1334  0.0989  156 ILE   B O   
1458 C CB  . ILE   B 147 ? 0.9943 1.3451 0.6647 0.2824  0.0970  0.0819  156 ILE   B CB  
1459 C CG1 . ILE   B 147 ? 1.0052 1.3578 0.6678 0.2878  0.1162  0.0946  156 ILE   B CG1 
1460 C CG2 . ILE   B 147 ? 1.0282 1.3230 0.6733 0.2794  0.0812  0.0748  156 ILE   B CG2 
1461 C CD1 . ILE   B 147 ? 1.0377 1.3675 0.6620 0.3192  0.1107  0.0927  156 ILE   B CD1 
1462 N N   C LYS   B 148 ? 0.9569 1.4370 0.7016 0.2765  0.1135  0.0842  157 LYS   B N   
1463 N N   D LYS   B 148 ? 0.9569 1.4370 0.7016 0.2765  0.1135  0.0842  157 LYS   B N   
1464 C CA  C LYS   B 148 ? 0.9411 1.4867 0.7180 0.2792  0.1279  0.0892  157 LYS   B CA  
1465 C CA  D LYS   B 148 ? 0.9411 1.4867 0.7180 0.2792  0.1279  0.0892  157 LYS   B CA  
1466 C C   C LYS   B 148 ? 0.9437 1.5035 0.7268 0.2736  0.1541  0.1057  157 LYS   B C   
1467 C C   D LYS   B 148 ? 0.9437 1.5035 0.7268 0.2736  0.1541  0.1057  157 LYS   B C   
1468 O O   C LYS   B 148 ? 0.9184 1.5312 0.7362 0.2641  0.1699  0.1126  157 LYS   B O   
1469 O O   D LYS   B 148 ? 0.9184 1.5312 0.7362 0.2641  0.1699  0.1126  157 LYS   B O   
1470 C CB  C LYS   B 148 ? 0.9657 1.5417 0.7323 0.3147  0.1189  0.0809  157 LYS   B CB  
1471 C CB  D LYS   B 148 ? 0.9657 1.5417 0.7323 0.3147  0.1189  0.0809  157 LYS   B CB  
1472 C CG  C LYS   B 148 ? 1.0555 1.5873 0.7836 0.3362  0.0945  0.0683  157 LYS   B CG  
1473 C CG  D LYS   B 148 ? 1.0555 1.5873 0.7836 0.3362  0.0945  0.0683  157 LYS   B CG  
1474 C CD  C LYS   B 148 ? 1.1441 1.6352 0.8281 0.3605  0.0940  0.0708  157 LYS   B CD  
1475 C CD  D LYS   B 148 ? 1.1441 1.6352 0.8281 0.3605  0.0940  0.0708  157 LYS   B CD  
1476 C CE  C LYS   B 148 ? 1.1821 1.7107 0.8592 0.3908  0.1046  0.0745  157 LYS   B CE  
1477 C CE  D LYS   B 148 ? 1.1821 1.7107 0.8592 0.3908  0.1046  0.0745  157 LYS   B CE  
1478 N NZ  C LYS   B 148 ? 1.1987 1.7606 0.8778 0.4151  0.0918  0.0634  157 LYS   B NZ  
1479 N NZ  D LYS   B 148 ? 1.1987 1.7606 0.8778 0.4151  0.0918  0.0634  157 LYS   B NZ  
1480 N N   . ASN   B 149 ? 0.9711 1.4841 0.7206 0.2795  0.1586  0.1122  158 ASN   B N   
1481 C CA  . ASN   B 149 ? 0.9744 1.4904 0.7210 0.2762  0.1826  0.1284  158 ASN   B CA  
1482 C C   . ASN   B 149 ? 0.9598 1.4562 0.7235 0.2395  0.1935  0.1376  158 ASN   B C   
1483 O O   . ASN   B 149 ? 0.9635 1.4676 0.7314 0.2312  0.2154  0.1524  158 ASN   B O   
1484 C CB  . ASN   B 149 ? 1.0428 1.5135 0.7414 0.3020  0.1797  0.1296  158 ASN   B CB  
1485 C CG  . ASN   B 149 ? 1.1273 1.6056 0.8006 0.3399  0.1684  0.1210  158 ASN   B CG  
1486 O OD1 . ASN   B 149 ? 1.1427 1.6713 0.8321 0.3537  0.1713  0.1188  158 ASN   B OD1 
1487 N ND2 . ASN   B 149 ? 1.1675 1.5963 0.8004 0.3581  0.1551  0.1154  158 ASN   B ND2 
1488 N N   . GLY   B 150 ? 0.9478 1.4137 0.7158 0.2200  0.1783  0.1291  159 GLY   B N   
1489 C CA  . GLY   B 150 ? 0.9362 1.3736 0.7132 0.1886  0.1847  0.1354  159 GLY   B CA  
1490 C C   . GLY   B 150 ? 0.9421 1.3166 0.6823 0.1921  0.1786  0.1353  159 GLY   B C   
1491 O O   . GLY   B 150 ? 0.9586 1.3025 0.7019 0.1689  0.1782  0.1366  159 GLY   B O   
1492 N N   A SER   B 151 ? 0.9498 1.3050 0.6554 0.2216  0.1730  0.1330  160 SER   B N   
1493 N N   B SER   B 151 ? 0.9502 1.3054 0.6557 0.2216  0.1732  0.1331  160 SER   B N   
1494 N N   C SER   B 151 ? 0.9507 1.3059 0.6561 0.2218  0.1729  0.1330  160 SER   B N   
1495 N N   D SER   B 151 ? 0.9522 1.3074 0.6577 0.2217  0.1730  0.1330  160 SER   B N   
1496 C CA  A SER   B 151 ? 0.9757 1.2758 0.6477 0.2278  0.1658  0.1315  160 SER   B CA  
1497 C CA  B SER   B 151 ? 0.9760 1.2761 0.6483 0.2273  0.1661  0.1317  160 SER   B CA  
1498 C CA  C SER   B 151 ? 0.9772 1.2772 0.6493 0.2276  0.1657  0.1315  160 SER   B CA  
1499 C CA  D SER   B 151 ? 0.9800 1.2801 0.6523 0.2273  0.1659  0.1316  160 SER   B CA  
1500 C C   A SER   B 151 ? 0.9785 1.2486 0.6465 0.2209  0.1441  0.1178  160 SER   B C   
1501 C C   B SER   B 151 ? 0.9788 1.2489 0.6466 0.2211  0.1442  0.1178  160 SER   B C   
1502 C C   C SER   B 151 ? 0.9799 1.2501 0.6484 0.2203  0.1442  0.1178  160 SER   B C   
1503 C C   D SER   B 151 ? 0.9808 1.2509 0.6491 0.2206  0.1442  0.1178  160 SER   B C   
1504 O O   A SER   B 151 ? 0.9697 1.2580 0.6502 0.2214  0.1320  0.1082  160 SER   B O   
1505 O O   B SER   B 151 ? 0.9701 1.2584 0.6501 0.2220  0.1321  0.1082  160 SER   B O   
1506 O O   C SER   B 151 ? 0.9710 1.2596 0.6530 0.2198  0.1323  0.1083  160 SER   B O   
1507 O O   D SER   B 151 ? 0.9719 1.2606 0.6533 0.2206  0.1322  0.1083  160 SER   B O   
1508 C CB  A SER   B 151 ? 1.0064 1.2978 0.6444 0.2613  0.1652  0.1322  160 SER   B CB  
1509 C CB  B SER   B 151 ? 1.0078 1.2985 0.6459 0.2603  0.1664  0.1331  160 SER   B CB  
1510 C CB  C SER   B 151 ? 1.0085 1.2989 0.6462 0.2612  0.1648  0.1320  160 SER   B CB  
1511 C CB  D SER   B 151 ? 1.0147 1.3052 0.6527 0.2605  0.1658  0.1327  160 SER   B CB  
1512 O OG  A SER   B 151 ? 1.0601 1.3013 0.6683 0.2672  0.1568  0.1296  160 SER   B OG  
1513 O OG  B SER   B 151 ? 1.0303 1.3427 0.6643 0.2829  0.1547  0.1236  160 SER   B OG  
1514 O OG  C SER   B 151 ? 1.0585 1.2985 0.6667 0.2667  0.1560  0.1291  160 SER   B OG  
1515 O OG  D SER   B 151 ? 1.0408 1.3472 0.6728 0.2824  0.1516  0.1219  160 SER   B OG  
1516 N N   . TYR   B 152 ? 0.9893 1.2139 0.6389 0.2155  0.1397  0.1170  161 TYR   B N   
1517 C CA  . TYR   B 152 ? 0.9598 1.1552 0.6047 0.2084  0.1221  0.1056  161 TYR   B CA  
1518 C C   . TYR   B 152 ? 0.9427 1.1134 0.5591 0.2314  0.1065  0.0968  161 TYR   B C   
1519 O O   . TYR   B 152 ? 0.9581 1.1091 0.5514 0.2466  0.1082  0.0995  161 TYR   B O   
1520 C CB  . TYR   B 152 ? 0.9591 1.1223 0.6037 0.1880  0.1264  0.1092  161 TYR   B CB  
1521 C CG  . TYR   B 152 ? 0.9649 1.0987 0.6051 0.1797  0.1109  0.0986  161 TYR   B CG  
1522 C CD1 . TYR   B 152 ? 0.9571 1.1016 0.6157 0.1652  0.1026  0.0912  161 TYR   B CD1 
1523 C CD2 . TYR   B 152 ? 0.9880 1.0848 0.6061 0.1864  0.1049  0.0958  161 TYR   B CD2 
1524 C CE1 . TYR   B 152 ? 0.9748 1.0925 0.6272 0.1584  0.0901  0.0824  161 TYR   B CE1 
1525 C CE2 . TYR   B 152 ? 1.0020 1.0753 0.6177 0.1783  0.0927  0.0868  161 TYR   B CE2 
1526 C CZ  . TYR   B 152 ? 1.0032 1.0864 0.6350 0.1646  0.0861  0.0806  161 TYR   B CZ  
1527 O OH  . TYR   B 152 ? 1.0283 1.0884 0.6555 0.1576  0.0757  0.0726  161 TYR   B OH  
1528 N N   . VAL   B 153 ? 0.9100 1.0790 0.5271 0.2331  0.0906  0.0859  162 VAL   B N   
1529 C CA  . VAL   B 153 ? 0.8961 1.0377 0.4877 0.2502  0.0745  0.0771  162 VAL   B CA  
1530 C C   . VAL   B 153 ? 0.8668 0.9800 0.4595 0.2335  0.0633  0.0698  162 VAL   B C   
1531 O O   . VAL   B 153 ? 0.8516 0.9751 0.4589 0.2212  0.0588  0.0657  162 VAL   B O   
1532 C CB  . VAL   B 153 ? 0.8997 1.0615 0.4836 0.2726  0.0662  0.0718  162 VAL   B CB  
1533 C CG1 . VAL   B 153 ? 0.9195 1.0476 0.4775 0.2862  0.0479  0.0622  162 VAL   B CG1 
1534 C CG2 . VAL   B 153 ? 0.9038 1.0907 0.4821 0.2923  0.0780  0.0790  162 VAL   B CG2 
1535 N N   . SER   B 154 ? 0.8544 0.9337 0.4323 0.2330  0.0595  0.0682  163 SER   B N   
1536 C CA  . SER   B 154 ? 0.8400 0.8938 0.4184 0.2184  0.0511  0.0621  163 SER   B CA  
1537 C C   . SER   B 154 ? 0.8307 0.8648 0.3918 0.2293  0.0354  0.0536  163 SER   B C   
1538 O O   . SER   B 154 ? 0.8340 0.8597 0.3779 0.2475  0.0306  0.0523  163 SER   B O   
1539 C CB  . SER   B 154 ? 0.8491 0.8797 0.4236 0.2115  0.0562  0.0649  163 SER   B CB  
1540 O OG  . SER   B 154 ? 0.8504 0.8555 0.4211 0.2035  0.0473  0.0583  163 SER   B OG  
1541 N N   . ALA   B 155 ? 0.8129 0.8345 0.3764 0.2173  0.0277  0.0482  164 ALA   B N   
1542 C CA  . ALA   B 155 ? 0.8128 0.8101 0.3593 0.2236  0.0140  0.0413  164 ALA   B CA  
1543 C C   . ALA   B 155 ? 0.8122 0.7833 0.3512 0.2222  0.0119  0.0398  164 ALA   B C   
1544 O O   . ALA   B 155 ? 0.8024 0.7727 0.3496 0.2143  0.0204  0.0432  164 ALA   B O   
1545 C CB  . ALA   B 155 ? 0.8148 0.8066 0.3655 0.2099  0.0090  0.0375  164 ALA   B CB  
1546 N N   . ILE   B 156 ? 0.8192 0.7686 0.3425 0.2302  -0.0001 0.0342  165 ILE   B N   
1547 C CA  . ILE   B 156 ? 0.8246 0.7515 0.3448 0.2263  -0.0043 0.0309  165 ILE   B CA  
1548 C C   . ILE   B 156 ? 0.8176 0.7329 0.3432 0.2083  -0.0067 0.0283  165 ILE   B C   
1549 O O   . ILE   B 156 ? 0.8134 0.7149 0.3278 0.2098  -0.0160 0.0249  165 ILE   B O   
1550 C CB  . ILE   B 156 ? 0.8401 0.7497 0.3415 0.2434  -0.0168 0.0258  165 ILE   B CB  
1551 C CG1 . ILE   B 156 ? 0.8587 0.7797 0.3515 0.2632  -0.0133 0.0286  165 ILE   B CG1 
1552 C CG2 . ILE   B 156 ? 0.8483 0.7366 0.3513 0.2354  -0.0229 0.0209  165 ILE   B CG2 
1553 C CD1 . ILE   B 156 ? 0.8861 0.7921 0.3564 0.2840  -0.0270 0.0229  165 ILE   B CD1 
1554 N N   . THR   B 157 ? 0.8090 0.7300 0.3495 0.1926  0.0024  0.0306  166 THR   B N   
1555 C CA  . THR   B 157 ? 0.8131 0.7258 0.3579 0.1766  0.0025  0.0288  166 THR   B CA  
1556 C C   . THR   B 157 ? 0.8185 0.7133 0.3641 0.1694  -0.0002 0.0254  166 THR   B C   
1557 O O   . THR   B 157 ? 0.8141 0.7102 0.3684 0.1666  0.0046  0.0254  166 THR   B O   
1558 C CB  . THR   B 157 ? 0.8170 0.7430 0.3759 0.1643  0.0127  0.0318  166 THR   B CB  
1559 O OG1 . THR   B 157 ? 0.8286 0.7753 0.3917 0.1689  0.0157  0.0349  166 THR   B OG1 
1560 C CG2 . THR   B 157 ? 0.8136 0.7316 0.3738 0.1505  0.0127  0.0296  166 THR   B CG2 
1561 N N   . GLN   B 158 ? 0.8272 0.7054 0.3637 0.1665  -0.0078 0.0226  167 GLN   B N   
1562 C CA  . GLN   B 158 ? 0.8406 0.7047 0.3808 0.1575  -0.0098 0.0196  167 GLN   B CA  
1563 C C   . GLN   B 158 ? 0.8730 0.7296 0.4131 0.1425  -0.0062 0.0204  167 GLN   B C   
1564 O O   . GLN   B 158 ? 0.8617 0.7153 0.3911 0.1427  -0.0077 0.0219  167 GLN   B O   
1565 C CB  . GLN   B 158 ? 0.8393 0.6864 0.3681 0.1660  -0.0222 0.0158  167 GLN   B CB  
1566 C CG  . GLN   B 158 ? 0.8399 0.6753 0.3765 0.1559  -0.0255 0.0119  167 GLN   B CG  
1567 C CD  . GLN   B 158 ? 0.8357 0.6840 0.3897 0.1544  -0.0204 0.0099  167 GLN   B CD  
1568 O OE1 . GLN   B 158 ? 0.8495 0.7093 0.4146 0.1466  -0.0100 0.0120  167 GLN   B OE1 
1569 N NE2 . GLN   B 158 ? 0.7891 0.6338 0.3443 0.1625  -0.0289 0.0050  167 GLN   B NE2 
1570 N N   . GLY   B 159 ? 0.9071 0.7623 0.4582 0.1312  -0.0013 0.0191  168 GLY   B N   
1571 C CA  . GLY   B 159 ? 0.9616 0.8095 0.5112 0.1179  0.0035  0.0203  168 GLY   B CA  
1572 C C   . GLY   B 159 ? 1.0305 0.8587 0.5719 0.1129  -0.0028 0.0197  168 GLY   B C   
1573 O O   . GLY   B 159 ? 1.0362 0.8534 0.5690 0.1209  -0.0129 0.0180  168 GLY   B O   
1574 N N   . LYS   B 160 ? 1.0787 0.9009 0.6212 0.0996  0.0036  0.0213  169 LYS   B N   
1575 C CA  . LYS   B 160 ? 1.1353 0.9378 0.6714 0.0906  0.0004  0.0222  169 LYS   B CA  
1576 C C   . LYS   B 160 ? 1.1653 0.9780 0.7226 0.0777  0.0085  0.0209  169 LYS   B C   
1577 O O   . LYS   B 160 ? 1.1652 0.9916 0.7305 0.0734  0.0191  0.0216  169 LYS   B O   
1578 C CB  . LYS   B 160 ? 1.1841 0.9692 0.6982 0.0866  0.0024  0.0270  169 LYS   B CB  
1579 C CG  . LYS   B 160 ? 1.2666 1.0273 0.7712 0.0752  0.0012  0.0299  169 LYS   B CG  
1580 C CD  . LYS   B 160 ? 1.3462 1.0905 0.8287 0.0701  0.0070  0.0357  169 LYS   B CD  
1581 C CE  . LYS   B 160 ? 1.4169 1.1308 0.8845 0.0597  0.0052  0.0400  169 LYS   B CE  
1582 N NZ  . LYS   B 160 ? 1.4659 1.1634 0.9115 0.0536  0.0137  0.0468  169 LYS   B NZ  
1583 N N   . ARG   B 161 ? 1.1874 0.9954 0.7548 0.0725  0.0028  0.0179  170 ARG   B N   
1584 C CA  . ARG   B 161 ? 1.2035 1.0258 0.7946 0.0603  0.0100  0.0159  170 ARG   B CA  
1585 C C   . ARG   B 161 ? 1.2421 1.0502 0.8284 0.0434  0.0164  0.0211  170 ARG   B C   
1586 O O   . ARG   B 161 ? 1.2545 1.0414 0.8331 0.0376  0.0085  0.0219  170 ARG   B O   
1587 C CB  . ARG   B 161 ? 1.2067 1.0359 0.8154 0.0635  -0.0002 0.0088  170 ARG   B CB  
1588 C CG  . ARG   B 161 ? 1.2122 1.0628 0.8496 0.0531  0.0061  0.0051  170 ARG   B CG  
1589 C CD  . ARG   B 161 ? 1.2359 1.0913 0.8904 0.0548  -0.0066 -0.0030 170 ARG   B CD  
1590 N NE  . ARG   B 161 ? 1.2524 1.1327 0.9372 0.0448  -0.0007 -0.0072 170 ARG   B NE  
1591 C CZ  . ARG   B 161 ? 1.2613 1.1632 0.9656 0.0537  -0.0051 -0.0152 170 ARG   B CZ  
1592 N NH1 . ARG   B 161 ? 1.2484 1.1472 0.9430 0.0721  -0.0149 -0.0190 170 ARG   B NH1 
1593 N NH2 . ARG   B 161 ? 1.2467 1.1738 0.9793 0.0452  0.0005  -0.0194 170 ARG   B NH2 
1594 N N   . GLU   B 162 ? 1.2595 1.0767 0.8474 0.0359  0.0308  0.0249  171 GLU   B N   
1595 C CA  . GLU   B 162 ? 1.2941 1.0993 0.8756 0.0202  0.0402  0.0313  171 GLU   B CA  
1596 C C   . GLU   B 162 ? 1.2978 1.1102 0.9040 0.0050  0.0414  0.0296  171 GLU   B C   
1597 O O   . GLU   B 162 ? 1.3148 1.1052 0.9132 -0.0072 0.0395  0.0339  171 GLU   B O   
1598 C CB  . GLU   B 162 ? 1.3393 1.1565 0.9178 0.0185  0.0557  0.0345  171 GLU   B CB  
1599 C CG  . GLU   B 162 ? 1.4444 1.2477 0.9943 0.0280  0.0551  0.0376  171 GLU   B CG  
1600 C CD  . GLU   B 162 ? 1.5718 1.3450 1.0928 0.0227  0.0558  0.0451  171 GLU   B CD  
1601 O OE1 . GLU   B 162 ? 1.5895 1.3594 1.1003 0.0159  0.0683  0.0502  171 GLU   B OE1 
1602 O OE2 . GLU   B 162 ? 1.6245 1.3758 1.1303 0.0267  0.0437  0.0458  171 GLU   B OE2 
1603 S S   . DMS   C .   ? 1.3874 1.1620 0.9127 0.0602  0.0464  -0.0198 201 DMS   B S   
1604 O O   . DMS   C .   ? 1.3774 1.1705 0.9079 0.0674  0.0522  -0.0155 201 DMS   B O   
1605 C C1  . DMS   C .   ? 1.3992 1.1513 0.9179 0.0659  0.0509  -0.0196 201 DMS   B C1  
1606 C C2  . DMS   C .   ? 1.3767 1.1614 0.9216 0.0482  0.0438  -0.0127 201 DMS   B C2  
1607 N N1  . A1BXV D .   ? 1.0121 1.0721 0.6839 0.0972  0.0861  0.0740  202 A1BXV B N1  
1608 N N3  . A1BXV D .   ? 1.0073 1.1189 0.7060 0.0930  0.1090  0.0915  202 A1BXV B N3  
1609 C C4  . A1BXV D .   ? 1.0203 1.1216 0.6934 0.1132  0.1345  0.1132  202 A1BXV B C4  
1610 C C5  . A1BXV D .   ? 1.0347 1.1279 0.6902 0.1254  0.1483  0.1251  202 A1BXV B C5  
1611 C C6  . A1BXV D .   ? 1.0268 1.1005 0.6876 0.1156  0.1201  0.1025  202 A1BXV B C6  
1612 C C7  . A1BXV D .   ? 1.0416 1.0841 0.6776 0.1291  0.1170  0.1014  202 A1BXV B C7  
1613 C C8  . A1BXV D .   ? 1.0515 1.0729 0.6799 0.1297  0.1046  0.0915  202 A1BXV B C8  
1614 C C10 . A1BXV D .   ? 1.0269 1.0808 0.6884 0.1067  0.0963  0.0829  202 A1BXV B C10 
1615 C C13 . A1BXV D .   ? 1.0129 1.0402 0.6738 0.0878  0.0628  0.0538  202 A1BXV B C13 
1616 C C15 . A1BXV D .   ? 1.0062 1.0421 0.6847 0.0646  0.0514  0.0422  202 A1BXV B C15 
1617 C C17 . A1BXV D .   ? 1.0155 1.0333 0.6624 0.0856  0.0340  0.0314  202 A1BXV B C17 
1618 C C1  . A1BXV D .   ? 0.9641 1.1424 0.7089 0.0760  0.1209  0.0983  202 A1BXV B C1  
1619 C C2  . A1BXV D .   ? 0.9914 1.1311 0.7049 0.0900  0.1217  0.1007  202 A1BXV B C2  
1620 C C3  . A1BXV D .   ? 0.9996 1.1348 0.7007 0.0993  0.1357  0.1124  202 A1BXV B C3  
1621 O O1  . A1BXV D .   ? 1.0263 1.1562 0.6923 0.1310  0.1604  0.1336  202 A1BXV B O1  
1622 C C9  . A1BXV D .   ? 1.0437 1.0705 0.6843 0.1183  0.0952  0.0829  202 A1BXV B C9  
1623 C C11 . A1BXV D .   ? 1.0026 1.0703 0.6713 0.1059  0.0744  0.0660  202 A1BXV B C11 
1624 O O2  . A1BXV D .   ? 0.9989 1.0744 0.6582 0.1234  0.0711  0.0656  202 A1BXV B O2  
1625 C C12 . A1BXV D .   ? 1.0009 1.0629 0.6744 0.0940  0.0648  0.0572  202 A1BXV B C12 
1626 C C14 . A1BXV D .   ? 1.0158 1.0346 0.6756 0.0796  0.0533  0.0448  202 A1BXV B C14 
1627 C C16 . A1BXV D .   ? 1.0120 1.0374 0.6857 0.0586  0.0411  0.0327  202 A1BXV B C16 
1628 N N2  . A1BXV D .   ? 1.0217 1.0292 0.6747 0.0698  0.0356  0.0290  202 A1BXV B N2  
1629 C C18 . A1BXV D .   ? 1.0169 1.0354 0.6646 0.0916  0.0433  0.0392  202 A1BXV B C18 
1630 C C19 . A1BXV D .   ? 1.0208 1.1008 0.6949 0.1048  0.1086  0.0924  202 A1BXV B C19 
# 
