data_7HOJ
# 
_entry.id   7HOJ 
# 
_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   7HOJ         pdb_00007hoj 10.2210/pdb7hoj/pdb 
WWPDB D_1001407733 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7HOJ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B' 5067.486  1   ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'          18117.629 1   3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'           78.133    2   ?                           ?    ? ? 
4 non-polymer syn 3-bromanyl-1-methyl-pyridine   173.030   1   ?                           ?    ? ? 
5 water       nat water                          18.015    142 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'         DMS   
4 3-bromanyl-1-methyl-pyridine A1BG6 
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 
A1BG6 non-polymer         . 3-bromanyl-1-methyl-pyridine ? 'C6 H7 Br N 1'   173.030 
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        A1BG6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BG6 
_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   101 203 DMS   DMS A . 
D 3 DMS   1   201 202 DMS   DMS B . 
E 4 A1BG6 1   202 301 A1BG6 LIG B . 
F 5 HOH   1   201 83  HOH   HOH A . 
F 5 HOH   2   202 34  HOH   HOH A . 
F 5 HOH   3   203 48  HOH   HOH A . 
F 5 HOH   4   204 66  HOH   HOH A . 
F 5 HOH   5   205 80  HOH   HOH A . 
F 5 HOH   6   206 107 HOH   HOH A . 
F 5 HOH   7   207 86  HOH   HOH A . 
F 5 HOH   8   208 108 HOH   HOH A . 
F 5 HOH   9   209 26  HOH   HOH A . 
F 5 HOH   10  210 126 HOH   HOH A . 
F 5 HOH   11  211 35  HOH   HOH A . 
F 5 HOH   12  212 21  HOH   HOH A . 
F 5 HOH   13  213 79  HOH   HOH A . 
F 5 HOH   14  214 98  HOH   HOH A . 
F 5 HOH   15  215 12  HOH   HOH A . 
F 5 HOH   16  216 134 HOH   HOH A . 
F 5 HOH   17  217 15  HOH   HOH A . 
F 5 HOH   18  218 53  HOH   HOH A . 
F 5 HOH   19  219 111 HOH   HOH A . 
F 5 HOH   20  220 102 HOH   HOH A . 
F 5 HOH   21  221 28  HOH   HOH A . 
F 5 HOH   22  222 70  HOH   HOH A . 
F 5 HOH   23  223 101 HOH   HOH A . 
F 5 HOH   24  224 22  HOH   HOH A . 
F 5 HOH   25  225 82  HOH   HOH A . 
F 5 HOH   26  226 75  HOH   HOH A . 
F 5 HOH   27  227 106 HOH   HOH A . 
F 5 HOH   28  228 122 HOH   HOH A . 
F 5 HOH   29  229 128 HOH   HOH A . 
F 5 HOH   30  230 138 HOH   HOH A . 
F 5 HOH   31  231 36  HOH   HOH A . 
F 5 HOH   32  232 20  HOH   HOH A . 
F 5 HOH   33  233 81  HOH   HOH A . 
F 5 HOH   34  234 116 HOH   HOH A . 
G 5 HOH   1   301 121 HOH   HOH B . 
G 5 HOH   2   302 8   HOH   HOH B . 
G 5 HOH   3   303 6   HOH   HOH B . 
G 5 HOH   4   304 96  HOH   HOH B . 
G 5 HOH   5   305 37  HOH   HOH B . 
G 5 HOH   6   306 120 HOH   HOH B . 
G 5 HOH   7   307 54  HOH   HOH B . 
G 5 HOH   8   308 99  HOH   HOH B . 
G 5 HOH   9   309 110 HOH   HOH B . 
G 5 HOH   10  310 62  HOH   HOH B . 
G 5 HOH   11  311 63  HOH   HOH B . 
G 5 HOH   12  312 127 HOH   HOH B . 
G 5 HOH   13  313 38  HOH   HOH B . 
G 5 HOH   14  314 67  HOH   HOH B . 
G 5 HOH   15  315 57  HOH   HOH B . 
G 5 HOH   16  316 29  HOH   HOH B . 
G 5 HOH   17  317 137 HOH   HOH B . 
G 5 HOH   18  318 39  HOH   HOH B . 
G 5 HOH   19  319 52  HOH   HOH B . 
G 5 HOH   20  320 18  HOH   HOH B . 
G 5 HOH   21  321 33  HOH   HOH B . 
G 5 HOH   22  322 104 HOH   HOH B . 
G 5 HOH   23  323 123 HOH   HOH B . 
G 5 HOH   24  324 46  HOH   HOH B . 
G 5 HOH   25  325 130 HOH   HOH B . 
G 5 HOH   26  326 2   HOH   HOH B . 
G 5 HOH   27  327 10  HOH   HOH B . 
G 5 HOH   28  328 73  HOH   HOH B . 
G 5 HOH   29  329 11  HOH   HOH B . 
G 5 HOH   30  330 4   HOH   HOH B . 
G 5 HOH   31  331 103 HOH   HOH B . 
G 5 HOH   32  332 1   HOH   HOH B . 
G 5 HOH   33  333 7   HOH   HOH B . 
G 5 HOH   34  334 5   HOH   HOH B . 
G 5 HOH   35  335 124 HOH   HOH B . 
G 5 HOH   36  336 89  HOH   HOH B . 
G 5 HOH   37  337 143 HOH   HOH B . 
G 5 HOH   38  338 25  HOH   HOH B . 
G 5 HOH   39  339 64  HOH   HOH B . 
G 5 HOH   40  340 49  HOH   HOH B . 
G 5 HOH   41  341 59  HOH   HOH B . 
G 5 HOH   42  342 71  HOH   HOH B . 
G 5 HOH   43  343 51  HOH   HOH B . 
G 5 HOH   44  344 95  HOH   HOH B . 
G 5 HOH   45  345 85  HOH   HOH B . 
G 5 HOH   46  346 91  HOH   HOH B . 
G 5 HOH   47  347 77  HOH   HOH B . 
G 5 HOH   48  348 24  HOH   HOH B . 
G 5 HOH   49  349 41  HOH   HOH B . 
G 5 HOH   50  350 136 HOH   HOH B . 
G 5 HOH   51  351 125 HOH   HOH B . 
G 5 HOH   52  352 93  HOH   HOH B . 
G 5 HOH   53  353 60  HOH   HOH B . 
G 5 HOH   54  354 16  HOH   HOH B . 
G 5 HOH   55  355 142 HOH   HOH B . 
G 5 HOH   56  356 9   HOH   HOH B . 
G 5 HOH   57  357 88  HOH   HOH B . 
G 5 HOH   58  358 112 HOH   HOH B . 
G 5 HOH   59  359 23  HOH   HOH B . 
G 5 HOH   60  360 135 HOH   HOH B . 
G 5 HOH   61  361 87  HOH   HOH B . 
G 5 HOH   62  362 17  HOH   HOH B . 
G 5 HOH   63  363 27  HOH   HOH B . 
G 5 HOH   64  364 55  HOH   HOH B . 
G 5 HOH   65  365 78  HOH   HOH B . 
G 5 HOH   66  366 58  HOH   HOH B . 
G 5 HOH   67  367 43  HOH   HOH B . 
G 5 HOH   68  368 3   HOH   HOH B . 
G 5 HOH   69  369 129 HOH   HOH B . 
G 5 HOH   70  370 13  HOH   HOH B . 
G 5 HOH   71  371 84  HOH   HOH B . 
G 5 HOH   72  372 50  HOH   HOH B . 
G 5 HOH   73  373 105 HOH   HOH B . 
G 5 HOH   74  374 45  HOH   HOH B . 
G 5 HOH   75  375 132 HOH   HOH B . 
G 5 HOH   76  376 72  HOH   HOH B . 
G 5 HOH   77  377 14  HOH   HOH B . 
G 5 HOH   78  378 115 HOH   HOH B . 
G 5 HOH   79  379 109 HOH   HOH B . 
G 5 HOH   80  380 65  HOH   HOH B . 
G 5 HOH   81  381 119 HOH   HOH B . 
G 5 HOH   82  382 114 HOH   HOH B . 
G 5 HOH   83  383 117 HOH   HOH B . 
G 5 HOH   84  384 47  HOH   HOH B . 
G 5 HOH   85  385 97  HOH   HOH B . 
G 5 HOH   86  386 31  HOH   HOH B . 
G 5 HOH   87  387 90  HOH   HOH B . 
G 5 HOH   88  388 68  HOH   HOH B . 
G 5 HOH   89  389 141 HOH   HOH B . 
G 5 HOH   90  390 30  HOH   HOH B . 
G 5 HOH   91  391 100 HOH   HOH B . 
G 5 HOH   92  392 44  HOH   HOH B . 
G 5 HOH   93  393 131 HOH   HOH B . 
G 5 HOH   94  394 133 HOH   HOH B . 
G 5 HOH   95  395 113 HOH   HOH B . 
G 5 HOH   96  396 94  HOH   HOH B . 
G 5 HOH   97  397 118 HOH   HOH B . 
G 5 HOH   98  398 140 HOH   HOH B . 
G 5 HOH   99  399 76  HOH   HOH B . 
G 5 HOH   100 400 61  HOH   HOH B . 
G 5 HOH   101 401 92  HOH   HOH B . 
G 5 HOH   102 402 139 HOH   HOH B . 
G 5 HOH   103 403 19  HOH   HOH B . 
G 5 HOH   104 404 42  HOH   HOH B . 
G 5 HOH   105 405 74  HOH   HOH B . 
G 5 HOH   106 406 56  HOH   HOH B . 
G 5 HOH   107 407 32  HOH   HOH B . 
G 5 HOH   108 408 40  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (26-JUL-2023)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
'data reduction' XDS     .                      ? 5 
'data reduction' XDS     .                      ? 6 
'data reduction' XDS     .                      ? 7 
'data reduction' XDS     .                      ? 8 
# 
_cell.entry_id           7HOJ 
_cell.length_a           42.686 
_cell.length_b           42.686 
_cell.length_c           216.886 
_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                         7HOJ 
_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          7HOJ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.27 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-03-23 
_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                     7HOJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.76 
_reflns.d_resolution_high            1.39 
_reflns.number_obs                   41959 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_netI_over_sigmaI        20.3 
_reflns.pdbx_redundancy              23.3 
_reflns.pdbx_Rrim_I_all              0.053 
_reflns.pdbx_Rpim_I_all              0.011 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     979064 
_reflns.pdbx_chi_squared             0.40 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.39 
_reflns_shell.d_res_low                   1.41 
_reflns_shell.number_measured_all         31778 
_reflns_shell.number_unique_obs           2005 
_reflns_shell.Rmerge_I_obs                7.874 
_reflns_shell.pdbx_chi_squared            0.12 
_reflns_shell.pdbx_redundancy             15.8 
_reflns_shell.percent_possible_obs        99.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             8.135 
_reflns_shell.pdbx_Rpim_I_all             2.018 
_reflns_shell.pdbx_CC_half                0.347 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HOJ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     37629 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.76 
_refine.ls_d_res_high                            1.390 
_refine.ls_percent_reflns_obs                    89.8 
_refine.ls_R_factor_obs                          0.2244 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2230 
_refine.ls_R_factor_R_free                       0.2501 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.090 
_refine.ls_number_reflns_R_free                  1915 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.B_iso_mean                               45.87 
_refine.aniso_B[1][1]                            -4.77030 
_refine.aniso_B[2][2]                            -4.77030 
_refine.aniso_B[3][3]                            9.54060 
_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             0.075 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.076 
_refine.pdbx_overall_SU_R_Blow_DPI               0.080 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.080 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HOJ 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_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         16 
_refine_hist.number_atoms_solvent             142 
_refine_hist.number_atoms_total               1634 
_refine_hist.d_res_high                       1.390 
_refine_hist.d_res_low                        36.76 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  1592 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.11  ? 2.00  2169 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  535  '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  280  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1592 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.19  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.29 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  196  '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  1339 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.39 
_refine_ls_shell.d_res_low                        1.45 
_refine_ls_shell.number_reflns_R_work             702 
_refine_ls_shell.R_factor_R_work                  0.5935 
_refine_ls_shell.percent_reflns_obs               16.27 
_refine_ls_shell.R_factor_R_free                  0.4865 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.77 
_refine_ls_shell.number_reflns_R_free             51 
_refine_ls_shell.number_reflns_all                753 
_refine_ls_shell.R_factor_all                     0.5864 
# 
_struct.entry_id                  7HOJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with Z1269184291' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOJ 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HOJ A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOJ 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 7HOJ SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOJ MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOJ MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOJ LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4780 ? 
1 MORE         -22  ? 
1 'SSA (A^2)'  9720 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
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  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HOJ 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    CYS 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     80 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             72.57 
_pdbx_validate_torsion.psi             -11.78 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -14.1069 -1.2255 -19.5192 0.0415 0.0473 -0.1445 0.1747 0.0977 0.0677 2.3706 3.0225 2.6456 -1.3938 
0.9891 0.1303  0.4302 0.4372 0.2590 -0.5446 -0.3867 -0.2712 -0.0317 0.5701 -0.0435 
'X-RAY DIFFRACTION' 2 ? refined -18.6166 1.3635  -15.4760 0.0831 0.0043 -0.0189 0.1232 0.0230 0.0243 1.1727 1.1625 1.8974 -0.9359 
0.7588 -0.0338 0.2841 0.1349 0.0722 -0.2007 -0.2880 0.0526  -0.0225 0.2197 0.0039  
# 
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 
A1BG6 C4   C  Y N 1   
A1BG6 C5   C  Y N 2   
A1BG6 BR   BR N N 3   
A1BG6 C3   C  Y N 4   
A1BG6 C2   C  Y N 5   
A1BG6 C1   C  Y N 6   
A1BG6 N    N  Y N 7   
A1BG6 C    C  N N 8   
A1BG6 H6   H  N N 9   
A1BG6 H5   H  N N 10  
A1BG6 H4   H  N N 11  
A1BG6 H3   H  N N 12  
A1BG6 H1   H  N N 13  
A1BG6 H    H  N N 14  
A1BG6 H2   H  N N 15  
ALA   N    N  N N 16  
ALA   CA   C  N S 17  
ALA   C    C  N N 18  
ALA   O    O  N N 19  
ALA   CB   C  N N 20  
ALA   OXT  O  N N 21  
ALA   H    H  N N 22  
ALA   H2   H  N N 23  
ALA   HA   H  N N 24  
ALA   HB1  H  N N 25  
ALA   HB2  H  N N 26  
ALA   HB3  H  N N 27  
ALA   HXT  H  N N 28  
ARG   N    N  N N 29  
ARG   CA   C  N S 30  
ARG   C    C  N N 31  
ARG   O    O  N N 32  
ARG   CB   C  N N 33  
ARG   CG   C  N N 34  
ARG   CD   C  N N 35  
ARG   NE   N  N N 36  
ARG   CZ   C  N N 37  
ARG   NH1  N  N N 38  
ARG   NH2  N  N N 39  
ARG   OXT  O  N N 40  
ARG   H    H  N N 41  
ARG   H2   H  N N 42  
ARG   HA   H  N N 43  
ARG   HB2  H  N N 44  
ARG   HB3  H  N N 45  
ARG   HG2  H  N N 46  
ARG   HG3  H  N N 47  
ARG   HD2  H  N N 48  
ARG   HD3  H  N N 49  
ARG   HE   H  N N 50  
ARG   HH11 H  N N 51  
ARG   HH12 H  N N 52  
ARG   HH21 H  N N 53  
ARG   HH22 H  N N 54  
ARG   HXT  H  N N 55  
ASN   N    N  N N 56  
ASN   CA   C  N S 57  
ASN   C    C  N N 58  
ASN   O    O  N N 59  
ASN   CB   C  N N 60  
ASN   CG   C  N N 61  
ASN   OD1  O  N N 62  
ASN   ND2  N  N N 63  
ASN   OXT  O  N N 64  
ASN   H    H  N N 65  
ASN   H2   H  N N 66  
ASN   HA   H  N N 67  
ASN   HB2  H  N N 68  
ASN   HB3  H  N N 69  
ASN   HD21 H  N N 70  
ASN   HD22 H  N N 71  
ASN   HXT  H  N N 72  
ASP   N    N  N N 73  
ASP   CA   C  N S 74  
ASP   C    C  N N 75  
ASP   O    O  N N 76  
ASP   CB   C  N N 77  
ASP   CG   C  N N 78  
ASP   OD1  O  N N 79  
ASP   OD2  O  N N 80  
ASP   OXT  O  N N 81  
ASP   H    H  N N 82  
ASP   H2   H  N N 83  
ASP   HA   H  N N 84  
ASP   HB2  H  N N 85  
ASP   HB3  H  N N 86  
ASP   HD2  H  N N 87  
ASP   HXT  H  N N 88  
CYS   N    N  N N 89  
CYS   CA   C  N R 90  
CYS   C    C  N N 91  
CYS   O    O  N N 92  
CYS   CB   C  N N 93  
CYS   SG   S  N N 94  
CYS   OXT  O  N N 95  
CYS   H    H  N N 96  
CYS   H2   H  N N 97  
CYS   HA   H  N N 98  
CYS   HB2  H  N N 99  
CYS   HB3  H  N N 100 
CYS   HG   H  N N 101 
CYS   HXT  H  N N 102 
DMS   S    S  N N 103 
DMS   O    O  N N 104 
DMS   C1   C  N N 105 
DMS   C2   C  N N 106 
DMS   H11  H  N N 107 
DMS   H12  H  N N 108 
DMS   H13  H  N N 109 
DMS   H21  H  N N 110 
DMS   H22  H  N N 111 
DMS   H23  H  N N 112 
GLN   N    N  N N 113 
GLN   CA   C  N S 114 
GLN   C    C  N N 115 
GLN   O    O  N N 116 
GLN   CB   C  N N 117 
GLN   CG   C  N N 118 
GLN   CD   C  N N 119 
GLN   OE1  O  N N 120 
GLN   NE2  N  N N 121 
GLN   OXT  O  N N 122 
GLN   H    H  N N 123 
GLN   H2   H  N N 124 
GLN   HA   H  N N 125 
GLN   HB2  H  N N 126 
GLN   HB3  H  N N 127 
GLN   HG2  H  N N 128 
GLN   HG3  H  N N 129 
GLN   HE21 H  N N 130 
GLN   HE22 H  N N 131 
GLN   HXT  H  N N 132 
GLU   N    N  N N 133 
GLU   CA   C  N S 134 
GLU   C    C  N N 135 
GLU   O    O  N N 136 
GLU   CB   C  N N 137 
GLU   CG   C  N N 138 
GLU   CD   C  N N 139 
GLU   OE1  O  N N 140 
GLU   OE2  O  N N 141 
GLU   OXT  O  N N 142 
GLU   H    H  N N 143 
GLU   H2   H  N N 144 
GLU   HA   H  N N 145 
GLU   HB2  H  N N 146 
GLU   HB3  H  N N 147 
GLU   HG2  H  N N 148 
GLU   HG3  H  N N 149 
GLU   HE2  H  N N 150 
GLU   HXT  H  N N 151 
GLY   N    N  N N 152 
GLY   CA   C  N N 153 
GLY   C    C  N N 154 
GLY   O    O  N N 155 
GLY   OXT  O  N N 156 
GLY   H    H  N N 157 
GLY   H2   H  N N 158 
GLY   HA2  H  N N 159 
GLY   HA3  H  N N 160 
GLY   HXT  H  N N 161 
HIS   N    N  N N 162 
HIS   CA   C  N S 163 
HIS   C    C  N N 164 
HIS   O    O  N N 165 
HIS   CB   C  N N 166 
HIS   CG   C  Y N 167 
HIS   ND1  N  Y N 168 
HIS   CD2  C  Y N 169 
HIS   CE1  C  Y N 170 
HIS   NE2  N  Y N 171 
HIS   OXT  O  N N 172 
HIS   H    H  N N 173 
HIS   H2   H  N N 174 
HIS   HA   H  N N 175 
HIS   HB2  H  N N 176 
HIS   HB3  H  N N 177 
HIS   HD1  H  N N 178 
HIS   HD2  H  N N 179 
HIS   HE1  H  N N 180 
HIS   HE2  H  N N 181 
HIS   HXT  H  N N 182 
HOH   O    O  N N 183 
HOH   H1   H  N N 184 
HOH   H2   H  N N 185 
ILE   N    N  N N 186 
ILE   CA   C  N S 187 
ILE   C    C  N N 188 
ILE   O    O  N N 189 
ILE   CB   C  N S 190 
ILE   CG1  C  N N 191 
ILE   CG2  C  N N 192 
ILE   CD1  C  N N 193 
ILE   OXT  O  N N 194 
ILE   H    H  N N 195 
ILE   H2   H  N N 196 
ILE   HA   H  N N 197 
ILE   HB   H  N N 198 
ILE   HG12 H  N N 199 
ILE   HG13 H  N N 200 
ILE   HG21 H  N N 201 
ILE   HG22 H  N N 202 
ILE   HG23 H  N N 203 
ILE   HD11 H  N N 204 
ILE   HD12 H  N N 205 
ILE   HD13 H  N N 206 
ILE   HXT  H  N N 207 
LEU   N    N  N N 208 
LEU   CA   C  N S 209 
LEU   C    C  N N 210 
LEU   O    O  N N 211 
LEU   CB   C  N N 212 
LEU   CG   C  N N 213 
LEU   CD1  C  N N 214 
LEU   CD2  C  N N 215 
LEU   OXT  O  N N 216 
LEU   H    H  N N 217 
LEU   H2   H  N N 218 
LEU   HA   H  N N 219 
LEU   HB2  H  N N 220 
LEU   HB3  H  N N 221 
LEU   HG   H  N N 222 
LEU   HD11 H  N N 223 
LEU   HD12 H  N N 224 
LEU   HD13 H  N N 225 
LEU   HD21 H  N N 226 
LEU   HD22 H  N N 227 
LEU   HD23 H  N N 228 
LEU   HXT  H  N N 229 
LYS   N    N  N N 230 
LYS   CA   C  N S 231 
LYS   C    C  N N 232 
LYS   O    O  N N 233 
LYS   CB   C  N N 234 
LYS   CG   C  N N 235 
LYS   CD   C  N N 236 
LYS   CE   C  N N 237 
LYS   NZ   N  N N 238 
LYS   OXT  O  N N 239 
LYS   H    H  N N 240 
LYS   H2   H  N N 241 
LYS   HA   H  N N 242 
LYS   HB2  H  N N 243 
LYS   HB3  H  N N 244 
LYS   HG2  H  N N 245 
LYS   HG3  H  N N 246 
LYS   HD2  H  N N 247 
LYS   HD3  H  N N 248 
LYS   HE2  H  N N 249 
LYS   HE3  H  N N 250 
LYS   HZ1  H  N N 251 
LYS   HZ2  H  N N 252 
LYS   HZ3  H  N N 253 
LYS   HXT  H  N N 254 
MET   N    N  N N 255 
MET   CA   C  N S 256 
MET   C    C  N N 257 
MET   O    O  N N 258 
MET   CB   C  N N 259 
MET   CG   C  N N 260 
MET   SD   S  N N 261 
MET   CE   C  N N 262 
MET   OXT  O  N N 263 
MET   H    H  N N 264 
MET   H2   H  N N 265 
MET   HA   H  N N 266 
MET   HB2  H  N N 267 
MET   HB3  H  N N 268 
MET   HG2  H  N N 269 
MET   HG3  H  N N 270 
MET   HE1  H  N N 271 
MET   HE2  H  N N 272 
MET   HE3  H  N N 273 
MET   HXT  H  N N 274 
PHE   N    N  N N 275 
PHE   CA   C  N S 276 
PHE   C    C  N N 277 
PHE   O    O  N N 278 
PHE   CB   C  N N 279 
PHE   CG   C  Y N 280 
PHE   CD1  C  Y N 281 
PHE   CD2  C  Y N 282 
PHE   CE1  C  Y N 283 
PHE   CE2  C  Y N 284 
PHE   CZ   C  Y N 285 
PHE   OXT  O  N N 286 
PHE   H    H  N N 287 
PHE   H2   H  N N 288 
PHE   HA   H  N N 289 
PHE   HB2  H  N N 290 
PHE   HB3  H  N N 291 
PHE   HD1  H  N N 292 
PHE   HD2  H  N N 293 
PHE   HE1  H  N N 294 
PHE   HE2  H  N N 295 
PHE   HZ   H  N N 296 
PHE   HXT  H  N N 297 
PRO   N    N  N N 298 
PRO   CA   C  N S 299 
PRO   C    C  N N 300 
PRO   O    O  N N 301 
PRO   CB   C  N N 302 
PRO   CG   C  N N 303 
PRO   CD   C  N N 304 
PRO   OXT  O  N N 305 
PRO   H    H  N N 306 
PRO   HA   H  N N 307 
PRO   HB2  H  N N 308 
PRO   HB3  H  N N 309 
PRO   HG2  H  N N 310 
PRO   HG3  H  N N 311 
PRO   HD2  H  N N 312 
PRO   HD3  H  N N 313 
PRO   HXT  H  N N 314 
SER   N    N  N N 315 
SER   CA   C  N S 316 
SER   C    C  N N 317 
SER   O    O  N N 318 
SER   CB   C  N N 319 
SER   OG   O  N N 320 
SER   OXT  O  N N 321 
SER   H    H  N N 322 
SER   H2   H  N N 323 
SER   HA   H  N N 324 
SER   HB2  H  N N 325 
SER   HB3  H  N N 326 
SER   HG   H  N N 327 
SER   HXT  H  N N 328 
THR   N    N  N N 329 
THR   CA   C  N S 330 
THR   C    C  N N 331 
THR   O    O  N N 332 
THR   CB   C  N R 333 
THR   OG1  O  N N 334 
THR   CG2  C  N N 335 
THR   OXT  O  N N 336 
THR   H    H  N N 337 
THR   H2   H  N N 338 
THR   HA   H  N N 339 
THR   HB   H  N N 340 
THR   HG1  H  N N 341 
THR   HG21 H  N N 342 
THR   HG22 H  N N 343 
THR   HG23 H  N N 344 
THR   HXT  H  N N 345 
TRP   N    N  N N 346 
TRP   CA   C  N S 347 
TRP   C    C  N N 348 
TRP   O    O  N N 349 
TRP   CB   C  N N 350 
TRP   CG   C  Y N 351 
TRP   CD1  C  Y N 352 
TRP   CD2  C  Y N 353 
TRP   NE1  N  Y N 354 
TRP   CE2  C  Y N 355 
TRP   CE3  C  Y N 356 
TRP   CZ2  C  Y N 357 
TRP   CZ3  C  Y N 358 
TRP   CH2  C  Y N 359 
TRP   OXT  O  N N 360 
TRP   H    H  N N 361 
TRP   H2   H  N N 362 
TRP   HA   H  N N 363 
TRP   HB2  H  N N 364 
TRP   HB3  H  N N 365 
TRP   HD1  H  N N 366 
TRP   HE1  H  N N 367 
TRP   HE3  H  N N 368 
TRP   HZ2  H  N N 369 
TRP   HZ3  H  N N 370 
TRP   HH2  H  N N 371 
TRP   HXT  H  N N 372 
TYR   N    N  N N 373 
TYR   CA   C  N S 374 
TYR   C    C  N N 375 
TYR   O    O  N N 376 
TYR   CB   C  N N 377 
TYR   CG   C  Y N 378 
TYR   CD1  C  Y N 379 
TYR   CD2  C  Y N 380 
TYR   CE1  C  Y N 381 
TYR   CE2  C  Y N 382 
TYR   CZ   C  Y N 383 
TYR   OH   O  N N 384 
TYR   OXT  O  N N 385 
TYR   H    H  N N 386 
TYR   H2   H  N N 387 
TYR   HA   H  N N 388 
TYR   HB2  H  N N 389 
TYR   HB3  H  N N 390 
TYR   HD1  H  N N 391 
TYR   HD2  H  N N 392 
TYR   HE1  H  N N 393 
TYR   HE2  H  N N 394 
TYR   HH   H  N N 395 
TYR   HXT  H  N N 396 
VAL   N    N  N N 397 
VAL   CA   C  N S 398 
VAL   C    C  N N 399 
VAL   O    O  N N 400 
VAL   CB   C  N N 401 
VAL   CG1  C  N N 402 
VAL   CG2  C  N N 403 
VAL   OXT  O  N N 404 
VAL   H    H  N N 405 
VAL   H2   H  N N 406 
VAL   HA   H  N N 407 
VAL   HB   H  N N 408 
VAL   HG11 H  N N 409 
VAL   HG12 H  N N 410 
VAL   HG13 H  N N 411 
VAL   HG21 H  N N 412 
VAL   HG22 H  N N 413 
VAL   HG23 H  N N 414 
VAL   HXT  H  N N 415 
# 
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 
A1BG6 C   N    sing N N 1   
A1BG6 N   C1   sing Y N 2   
A1BG6 C1  C2   doub Y N 3   
A1BG6 C2  C3   sing Y N 4   
A1BG6 C3  C4   doub Y N 5   
A1BG6 C4  BR   sing N N 6   
A1BG6 C5  C4   sing Y N 7   
A1BG6 N   C5   doub Y N 8   
A1BG6 C5  H6   sing N N 9   
A1BG6 C3  H5   sing N N 10  
A1BG6 C2  H4   sing N N 11  
A1BG6 C1  H3   sing N N 12  
A1BG6 C   H1   sing N N 13  
A1BG6 C   H    sing N N 14  
A1BG6 C   H2   sing N N 15  
ALA   N   CA   sing N N 16  
ALA   N   H    sing N N 17  
ALA   N   H2   sing N N 18  
ALA   CA  C    sing N N 19  
ALA   CA  CB   sing N N 20  
ALA   CA  HA   sing N N 21  
ALA   C   O    doub N N 22  
ALA   C   OXT  sing N N 23  
ALA   CB  HB1  sing N N 24  
ALA   CB  HB2  sing N N 25  
ALA   CB  HB3  sing N N 26  
ALA   OXT HXT  sing N N 27  
ARG   N   CA   sing N N 28  
ARG   N   H    sing N N 29  
ARG   N   H2   sing N N 30  
ARG   CA  C    sing N N 31  
ARG   CA  CB   sing N N 32  
ARG   CA  HA   sing N N 33  
ARG   C   O    doub N N 34  
ARG   C   OXT  sing N N 35  
ARG   CB  CG   sing N N 36  
ARG   CB  HB2  sing N N 37  
ARG   CB  HB3  sing N N 38  
ARG   CG  CD   sing N N 39  
ARG   CG  HG2  sing N N 40  
ARG   CG  HG3  sing N N 41  
ARG   CD  NE   sing N N 42  
ARG   CD  HD2  sing N N 43  
ARG   CD  HD3  sing N N 44  
ARG   NE  CZ   sing N N 45  
ARG   NE  HE   sing N N 46  
ARG   CZ  NH1  sing N N 47  
ARG   CZ  NH2  doub N N 48  
ARG   NH1 HH11 sing N N 49  
ARG   NH1 HH12 sing N N 50  
ARG   NH2 HH21 sing N N 51  
ARG   NH2 HH22 sing N N 52  
ARG   OXT HXT  sing N N 53  
ASN   N   CA   sing N N 54  
ASN   N   H    sing N N 55  
ASN   N   H2   sing N N 56  
ASN   CA  C    sing N N 57  
ASN   CA  CB   sing N N 58  
ASN   CA  HA   sing N N 59  
ASN   C   O    doub N N 60  
ASN   C   OXT  sing N N 61  
ASN   CB  CG   sing N N 62  
ASN   CB  HB2  sing N N 63  
ASN   CB  HB3  sing N N 64  
ASN   CG  OD1  doub N N 65  
ASN   CG  ND2  sing N N 66  
ASN   ND2 HD21 sing N N 67  
ASN   ND2 HD22 sing N N 68  
ASN   OXT HXT  sing N N 69  
ASP   N   CA   sing N N 70  
ASP   N   H    sing N N 71  
ASP   N   H2   sing N N 72  
ASP   CA  C    sing N N 73  
ASP   CA  CB   sing N N 74  
ASP   CA  HA   sing N N 75  
ASP   C   O    doub N N 76  
ASP   C   OXT  sing N N 77  
ASP   CB  CG   sing N N 78  
ASP   CB  HB2  sing N N 79  
ASP   CB  HB3  sing N N 80  
ASP   CG  OD1  doub N N 81  
ASP   CG  OD2  sing N N 82  
ASP   OD2 HD2  sing N N 83  
ASP   OXT HXT  sing N N 84  
CYS   N   CA   sing N N 85  
CYS   N   H    sing N N 86  
CYS   N   H2   sing N N 87  
CYS   CA  C    sing N N 88  
CYS   CA  CB   sing N N 89  
CYS   CA  HA   sing N N 90  
CYS   C   O    doub N N 91  
CYS   C   OXT  sing N N 92  
CYS   CB  SG   sing N N 93  
CYS   CB  HB2  sing N N 94  
CYS   CB  HB3  sing N N 95  
CYS   SG  HG   sing N N 96  
CYS   OXT HXT  sing N N 97  
DMS   S   O    doub N N 98  
DMS   S   C1   sing N N 99  
DMS   S   C2   sing N N 100 
DMS   C1  H11  sing N N 101 
DMS   C1  H12  sing N N 102 
DMS   C1  H13  sing N N 103 
DMS   C2  H21  sing N N 104 
DMS   C2  H22  sing N N 105 
DMS   C2  H23  sing N N 106 
GLN   N   CA   sing N N 107 
GLN   N   H    sing N N 108 
GLN   N   H2   sing N N 109 
GLN   CA  C    sing N N 110 
GLN   CA  CB   sing N N 111 
GLN   CA  HA   sing N N 112 
GLN   C   O    doub N N 113 
GLN   C   OXT  sing N N 114 
GLN   CB  CG   sing N N 115 
GLN   CB  HB2  sing N N 116 
GLN   CB  HB3  sing N N 117 
GLN   CG  CD   sing N N 118 
GLN   CG  HG2  sing N N 119 
GLN   CG  HG3  sing N N 120 
GLN   CD  OE1  doub N N 121 
GLN   CD  NE2  sing N N 122 
GLN   NE2 HE21 sing N N 123 
GLN   NE2 HE22 sing N N 124 
GLN   OXT HXT  sing N N 125 
GLU   N   CA   sing N N 126 
GLU   N   H    sing N N 127 
GLU   N   H2   sing N N 128 
GLU   CA  C    sing N N 129 
GLU   CA  CB   sing N N 130 
GLU   CA  HA   sing N N 131 
GLU   C   O    doub N N 132 
GLU   C   OXT  sing N N 133 
GLU   CB  CG   sing N N 134 
GLU   CB  HB2  sing N N 135 
GLU   CB  HB3  sing N N 136 
GLU   CG  CD   sing N N 137 
GLU   CG  HG2  sing N N 138 
GLU   CG  HG3  sing N N 139 
GLU   CD  OE1  doub N N 140 
GLU   CD  OE2  sing N N 141 
GLU   OE2 HE2  sing N N 142 
GLU   OXT HXT  sing N N 143 
GLY   N   CA   sing N N 144 
GLY   N   H    sing N N 145 
GLY   N   H2   sing N N 146 
GLY   CA  C    sing N N 147 
GLY   CA  HA2  sing N N 148 
GLY   CA  HA3  sing N N 149 
GLY   C   O    doub N N 150 
GLY   C   OXT  sing N N 151 
GLY   OXT HXT  sing N N 152 
HIS   N   CA   sing N N 153 
HIS   N   H    sing N N 154 
HIS   N   H2   sing N N 155 
HIS   CA  C    sing N N 156 
HIS   CA  CB   sing N N 157 
HIS   CA  HA   sing N N 158 
HIS   C   O    doub N N 159 
HIS   C   OXT  sing N N 160 
HIS   CB  CG   sing N N 161 
HIS   CB  HB2  sing N N 162 
HIS   CB  HB3  sing N N 163 
HIS   CG  ND1  sing Y N 164 
HIS   CG  CD2  doub Y N 165 
HIS   ND1 CE1  doub Y N 166 
HIS   ND1 HD1  sing N N 167 
HIS   CD2 NE2  sing Y N 168 
HIS   CD2 HD2  sing N N 169 
HIS   CE1 NE2  sing Y N 170 
HIS   CE1 HE1  sing N N 171 
HIS   NE2 HE2  sing N N 172 
HIS   OXT HXT  sing N N 173 
HOH   O   H1   sing N N 174 
HOH   O   H2   sing N N 175 
ILE   N   CA   sing N N 176 
ILE   N   H    sing N N 177 
ILE   N   H2   sing N N 178 
ILE   CA  C    sing N N 179 
ILE   CA  CB   sing N N 180 
ILE   CA  HA   sing N N 181 
ILE   C   O    doub N N 182 
ILE   C   OXT  sing N N 183 
ILE   CB  CG1  sing N N 184 
ILE   CB  CG2  sing N N 185 
ILE   CB  HB   sing N N 186 
ILE   CG1 CD1  sing N N 187 
ILE   CG1 HG12 sing N N 188 
ILE   CG1 HG13 sing N N 189 
ILE   CG2 HG21 sing N N 190 
ILE   CG2 HG22 sing N N 191 
ILE   CG2 HG23 sing N N 192 
ILE   CD1 HD11 sing N N 193 
ILE   CD1 HD12 sing N N 194 
ILE   CD1 HD13 sing N N 195 
ILE   OXT HXT  sing N N 196 
LEU   N   CA   sing N N 197 
LEU   N   H    sing N N 198 
LEU   N   H2   sing N N 199 
LEU   CA  C    sing N N 200 
LEU   CA  CB   sing N N 201 
LEU   CA  HA   sing N N 202 
LEU   C   O    doub N N 203 
LEU   C   OXT  sing N N 204 
LEU   CB  CG   sing N N 205 
LEU   CB  HB2  sing N N 206 
LEU   CB  HB3  sing N N 207 
LEU   CG  CD1  sing N N 208 
LEU   CG  CD2  sing N N 209 
LEU   CG  HG   sing N N 210 
LEU   CD1 HD11 sing N N 211 
LEU   CD1 HD12 sing N N 212 
LEU   CD1 HD13 sing N N 213 
LEU   CD2 HD21 sing N N 214 
LEU   CD2 HD22 sing N N 215 
LEU   CD2 HD23 sing N N 216 
LEU   OXT HXT  sing N N 217 
LYS   N   CA   sing N N 218 
LYS   N   H    sing N N 219 
LYS   N   H2   sing N N 220 
LYS   CA  C    sing N N 221 
LYS   CA  CB   sing N N 222 
LYS   CA  HA   sing N N 223 
LYS   C   O    doub N N 224 
LYS   C   OXT  sing N N 225 
LYS   CB  CG   sing N N 226 
LYS   CB  HB2  sing N N 227 
LYS   CB  HB3  sing N N 228 
LYS   CG  CD   sing N N 229 
LYS   CG  HG2  sing N N 230 
LYS   CG  HG3  sing N N 231 
LYS   CD  CE   sing N N 232 
LYS   CD  HD2  sing N N 233 
LYS   CD  HD3  sing N N 234 
LYS   CE  NZ   sing N N 235 
LYS   CE  HE2  sing N N 236 
LYS   CE  HE3  sing N N 237 
LYS   NZ  HZ1  sing N N 238 
LYS   NZ  HZ2  sing N N 239 
LYS   NZ  HZ3  sing N N 240 
LYS   OXT HXT  sing N N 241 
MET   N   CA   sing N N 242 
MET   N   H    sing N N 243 
MET   N   H2   sing N N 244 
MET   CA  C    sing N N 245 
MET   CA  CB   sing N N 246 
MET   CA  HA   sing N N 247 
MET   C   O    doub N N 248 
MET   C   OXT  sing N N 249 
MET   CB  CG   sing N N 250 
MET   CB  HB2  sing N N 251 
MET   CB  HB3  sing N N 252 
MET   CG  SD   sing N N 253 
MET   CG  HG2  sing N N 254 
MET   CG  HG3  sing N N 255 
MET   SD  CE   sing N N 256 
MET   CE  HE1  sing N N 257 
MET   CE  HE2  sing N N 258 
MET   CE  HE3  sing N N 259 
MET   OXT HXT  sing N N 260 
PHE   N   CA   sing N N 261 
PHE   N   H    sing N N 262 
PHE   N   H2   sing N N 263 
PHE   CA  C    sing N N 264 
PHE   CA  CB   sing N N 265 
PHE   CA  HA   sing N N 266 
PHE   C   O    doub N N 267 
PHE   C   OXT  sing N N 268 
PHE   CB  CG   sing N N 269 
PHE   CB  HB2  sing N N 270 
PHE   CB  HB3  sing N N 271 
PHE   CG  CD1  doub Y N 272 
PHE   CG  CD2  sing Y N 273 
PHE   CD1 CE1  sing Y N 274 
PHE   CD1 HD1  sing N N 275 
PHE   CD2 CE2  doub Y N 276 
PHE   CD2 HD2  sing N N 277 
PHE   CE1 CZ   doub Y N 278 
PHE   CE1 HE1  sing N N 279 
PHE   CE2 CZ   sing Y N 280 
PHE   CE2 HE2  sing N N 281 
PHE   CZ  HZ   sing N N 282 
PHE   OXT HXT  sing N N 283 
PRO   N   CA   sing N N 284 
PRO   N   CD   sing N N 285 
PRO   N   H    sing N N 286 
PRO   CA  C    sing N N 287 
PRO   CA  CB   sing N N 288 
PRO   CA  HA   sing N N 289 
PRO   C   O    doub N N 290 
PRO   C   OXT  sing N N 291 
PRO   CB  CG   sing N N 292 
PRO   CB  HB2  sing N N 293 
PRO   CB  HB3  sing N N 294 
PRO   CG  CD   sing N N 295 
PRO   CG  HG2  sing N N 296 
PRO   CG  HG3  sing N N 297 
PRO   CD  HD2  sing N N 298 
PRO   CD  HD3  sing N N 299 
PRO   OXT HXT  sing N N 300 
SER   N   CA   sing N N 301 
SER   N   H    sing N N 302 
SER   N   H2   sing N N 303 
SER   CA  C    sing N N 304 
SER   CA  CB   sing N N 305 
SER   CA  HA   sing N N 306 
SER   C   O    doub N N 307 
SER   C   OXT  sing N N 308 
SER   CB  OG   sing N N 309 
SER   CB  HB2  sing N N 310 
SER   CB  HB3  sing N N 311 
SER   OG  HG   sing N N 312 
SER   OXT HXT  sing N N 313 
THR   N   CA   sing N N 314 
THR   N   H    sing N N 315 
THR   N   H2   sing N N 316 
THR   CA  C    sing N N 317 
THR   CA  CB   sing N N 318 
THR   CA  HA   sing N N 319 
THR   C   O    doub N N 320 
THR   C   OXT  sing N N 321 
THR   CB  OG1  sing N N 322 
THR   CB  CG2  sing N N 323 
THR   CB  HB   sing N N 324 
THR   OG1 HG1  sing N N 325 
THR   CG2 HG21 sing N N 326 
THR   CG2 HG22 sing N N 327 
THR   CG2 HG23 sing N N 328 
THR   OXT HXT  sing N N 329 
TRP   N   CA   sing N N 330 
TRP   N   H    sing N N 331 
TRP   N   H2   sing N N 332 
TRP   CA  C    sing N N 333 
TRP   CA  CB   sing N N 334 
TRP   CA  HA   sing N N 335 
TRP   C   O    doub N N 336 
TRP   C   OXT  sing N N 337 
TRP   CB  CG   sing N N 338 
TRP   CB  HB2  sing N N 339 
TRP   CB  HB3  sing N N 340 
TRP   CG  CD1  doub Y N 341 
TRP   CG  CD2  sing Y N 342 
TRP   CD1 NE1  sing Y N 343 
TRP   CD1 HD1  sing N N 344 
TRP   CD2 CE2  doub Y N 345 
TRP   CD2 CE3  sing Y N 346 
TRP   NE1 CE2  sing Y N 347 
TRP   NE1 HE1  sing N N 348 
TRP   CE2 CZ2  sing Y N 349 
TRP   CE3 CZ3  doub Y N 350 
TRP   CE3 HE3  sing N N 351 
TRP   CZ2 CH2  doub Y N 352 
TRP   CZ2 HZ2  sing N N 353 
TRP   CZ3 CH2  sing Y N 354 
TRP   CZ3 HZ3  sing N N 355 
TRP   CH2 HH2  sing N N 356 
TRP   OXT HXT  sing N N 357 
TYR   N   CA   sing N N 358 
TYR   N   H    sing N N 359 
TYR   N   H2   sing N N 360 
TYR   CA  C    sing N N 361 
TYR   CA  CB   sing N N 362 
TYR   CA  HA   sing N N 363 
TYR   C   O    doub N N 364 
TYR   C   OXT  sing N N 365 
TYR   CB  CG   sing N N 366 
TYR   CB  HB2  sing N N 367 
TYR   CB  HB3  sing N N 368 
TYR   CG  CD1  doub Y N 369 
TYR   CG  CD2  sing Y N 370 
TYR   CD1 CE1  sing Y N 371 
TYR   CD1 HD1  sing N N 372 
TYR   CD2 CE2  doub Y N 373 
TYR   CD2 HD2  sing N N 374 
TYR   CE1 CZ   doub Y N 375 
TYR   CE1 HE1  sing N N 376 
TYR   CE2 CZ   sing Y N 377 
TYR   CE2 HE2  sing N N 378 
TYR   CZ  OH   sing N N 379 
TYR   OH  HH   sing N N 380 
TYR   OXT HXT  sing N N 381 
VAL   N   CA   sing N N 382 
VAL   N   H    sing N N 383 
VAL   N   H2   sing N N 384 
VAL   CA  C    sing N N 385 
VAL   CA  CB   sing N N 386 
VAL   CA  HA   sing N N 387 
VAL   C   O    doub N N 388 
VAL   C   OXT  sing N N 389 
VAL   CB  CG1  sing N N 390 
VAL   CB  CG2  sing N N 391 
VAL   CB  HB   sing N N 392 
VAL   CG1 HG11 sing N N 393 
VAL   CG1 HG12 sing N N 394 
VAL   CG1 HG13 sing N N 395 
VAL   CG2 HG21 sing N N 396 
VAL   CG2 HG22 sing N N 397 
VAL   CG2 HG23 sing N N 398 
VAL   OXT HXT  sing N N 399 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002322 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HOJ 
_atom_sites.fract_transf_matrix[1][1]   0.023427 
_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]   0.023427 
_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]   0.004611 
_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 
BR 
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   ? -21.095 19.650  -7.565  1.00 53.72 ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.407 19.026  -7.719  1.00 53.21 ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.498 18.259  -9.054  1.00 50.33 ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.327 18.809  -10.158 1.00 51.67 ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.539 20.033  -7.581  1.00 57.24 ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.867 19.391  -7.251  1.00 64.57 ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -24.967 18.746  -6.174  1.00 66.80 ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -25.814 19.540  -8.060  1.00 66.51 ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.794 17.001  -8.927  1.00 45.18 ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.805 16.106  -10.075 1.00 41.43 ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -24.168 15.823  -10.613 1.00 39.13 ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -25.116 15.711  -9.836  1.00 40.11 ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -22.078 14.813  -9.703  1.00 41.59 ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.619 15.007  -9.594  1.00 43.29 ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.832 13.413  -9.191  1.00 43.66 ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -18.193 13.934  -9.161  1.00 45.67 ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -24.289 15.727  -11.949 1.00 36.78 ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.577 15.486  -12.590 1.00 36.51 ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -25.426 14.518  -13.741 1.00 36.59 ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -24.308 14.310  -14.250 1.00 37.78 ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -26.250 16.813  -13.067 1.00 37.22 ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.458 17.544  -14.126 1.00 39.24 ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.479 18.470  -13.774 1.00 41.59 ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.795 17.439  -15.472 1.00 41.01 ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.781 19.190  -14.745 1.00 43.19 ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -25.138 18.192  -16.449 1.00 42.15 ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -24.127 19.063  -16.081 1.00 44.30 ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.396 19.741  -17.050 1.00 46.66 ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.516 13.807  -14.086 1.00 35.58 ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.427 12.819  -15.198 1.00 34.36 ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -27.269 13.276  -16.400 1.00 34.82 ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -28.246 14.027  -16.246 1.00 35.59 ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.846 11.424  -14.743 1.00 34.26 ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -28.338 11.407  -14.291 1.00 35.48 ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.917 10.987  -13.593 1.00 34.08 ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.844 9.925   -13.946 1.00 35.62 ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.839 12.856  -17.607 1.00 34.69 ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.500 13.217  -18.861 1.00 36.00 ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.530 11.977  -19.734 1.00 36.83 ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.489 11.302  -19.884 1.00 35.99 ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.686 14.272  -19.637 1.00 39.73 ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.357 15.574  -18.958 1.00 48.67 ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.684 16.537  -19.926 1.00 55.36 ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.945 16.076  -20.829 1.00 58.43 ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.891 17.760  -19.772 1.00 59.83 ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.695 11.636  -20.293 1.00 36.66 ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.789 10.416  -21.105 1.00 37.28 ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.872 10.507  -22.336 1.00 37.57 ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.798 11.599  -22.944 1.00 38.95 ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -30.251 10.177  -21.555 1.00 40.78 ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.475 8.701   -21.874 1.00 44.94 ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.940 8.348   -22.042 1.00 49.83 ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -32.133 6.904   -22.219 1.00 50.01 ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -32.085 6.295   -23.404 1.00 49.81 ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.853 6.993   -24.508 1.00 51.11 ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -32.248 4.984   -23.490 1.00 47.91 ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -27.144 9.405   -22.649 1.00 36.73 ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -26.256 9.366   -23.831 1.00 38.97 ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.697 8.300   -24.859 1.00 40.42 ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -26.175 8.310   -25.975 1.00 42.30 ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.819 9.083   -23.408 1.00 39.49 ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.555 7.355   -24.474 1.00 39.05 ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -28.025 6.363   -25.430 1.00 40.13 ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.644 5.116   -24.862 1.00 40.55 ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.776 4.960   -23.651 1.00 39.85 ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -29.042 4.223   -25.754 1.00 41.24 ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.580 2.928   -25.397 1.00 40.91 ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.432 1.964   -25.261 1.00 41.81 ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -27.410 2.106   -25.953 1.00 44.12 ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.463 2.359   -26.530 1.00 43.88 ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.803 3.040   -26.740 1.00 50.76 ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -32.076 4.035   -26.055 1.00 50.45 ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.566 2.599   -27.647 1.00 55.60 ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.657 0.900   -24.511 1.00 40.81 ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.648 -0.162  -24.384 1.00 41.37 ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -28.045 -1.336  -25.283 1.00 44.20 ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.957 -2.104  -24.963 1.00 44.34 ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.543 -0.569  -22.935 1.00 41.98 ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -27.031 0.630   -22.128 1.00 42.28 ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.616 -1.780  -22.801 1.00 43.03 ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -27.217 0.493   -20.671 1.00 43.36 ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -27.398 -1.436  -26.434 0.50 45.29 ? 60  THR   A N   1 
ATOM   83   N  N   C THR   A 1 17  ? -27.398 -1.436  -26.434 0.50 45.29 ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.693 -2.479  -27.415 0.50 47.84 ? 60  THR   A CA  1 
ATOM   85   C  CA  C THR   A 1 17  ? -27.693 -2.479  -27.415 0.50 47.84 ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.419 -2.904  -28.121 0.50 49.75 ? 60  THR   A C   1 
ATOM   87   C  C   C THR   A 1 17  ? -26.419 -2.904  -28.121 0.50 49.75 ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.539 -2.074  -28.335 0.50 50.49 ? 60  THR   A O   1 
ATOM   89   O  O   C THR   A 1 17  ? -25.539 -2.074  -28.335 0.50 50.49 ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.671 -1.968  -28.505 0.50 50.98 ? 60  THR   A CB  1 
ATOM   91   C  CB  C THR   A 1 17  ? -28.671 -1.968  -28.505 0.50 50.98 ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -28.050 -0.955  -29.310 0.50 55.11 ? 60  THR   A OG1 1 
ATOM   93   O  OG1 C THR   A 1 17  ? -28.050 -0.955  -29.310 0.50 55.11 ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.985 -1.456  -27.945 0.50 49.23 ? 60  THR   A CG2 1 
ATOM   95   C  CG2 C THR   A 1 17  ? -29.985 -1.456  -27.945 0.50 49.23 ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -26.370 -4.155  -28.594 1.00 50.70 ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -25.220 -4.643  -29.371 1.00 53.64 ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -25.351 -4.083  -30.799 1.00 55.74 ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.462 -4.082  -31.335 1.00 57.64 ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -25.291 -6.165  -29.440 1.00 53.85 ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -24.206 -6.807  -30.256 1.00 54.30 ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -24.235 -7.065  -31.597 1.00 55.74 ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.983 -7.369  -29.764 1.00 54.04 ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -23.078 -7.704  -31.983 1.00 55.98 ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -22.307 -7.933  -30.870 1.00 55.16 ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -22.356 -7.393  -28.510 1.00 53.89 ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -21.058 -8.539  -30.749 1.00 55.53 ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -21.159 -8.076  -28.381 1.00 55.02 ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -20.504 -8.605  -29.495 1.00 55.52 ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -24.254 -3.577  -31.417 1.00 55.87 ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -24.342 -3.024  -32.779 1.00 57.86 ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.777 -4.052  -33.724 1.00 59.84 ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -22.625 -4.442  -33.575 1.00 58.52 ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.536 -1.700  -32.914 1.00 60.88 ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.343 -1.231  -34.359 1.00 67.95 ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -22.569 0.047   -34.627 1.00 75.43 ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -22.113 0.697   -33.658 1.00 77.14 ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -22.444 0.413   -35.819 1.00 78.86 ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -24.555 -4.460  -34.740 1.00 62.90 ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -24.053 -5.419  -35.718 1.00 67.75 ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -23.055 -4.661  -36.595 1.00 70.74 ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -23.321 -3.515  -36.957 1.00 71.01 ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -25.217 -5.952  -36.574 1.00 72.83 ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -26.033 -7.044  -35.872 1.00 80.95 ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -26.735 -7.950  -36.897 1.00 88.13 ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -28.156 -8.283  -36.502 1.00 92.83 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -29.033 -7.079  -36.512 1.00 95.14 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -21.885 -5.252  -36.850 1.00 72.81 ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.839 -4.613  -37.656 1.00 74.80 ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -20.298 -3.339  -36.986 1.00 73.32 ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -20.174 -2.298  -37.621 1.00 74.21 ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -21.268 -4.356  -39.111 1.00 80.01 ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.726 -5.591  -39.862 1.00 89.70 ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -21.083 -6.657  -39.703 1.00 93.38 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.725 -5.494  -40.610 1.00 92.78 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -20.015 -3.414  -35.676 1.00 70.68 ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -19.362 -2.314  -34.982 1.00 68.50 ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -17.857 -2.401  -35.368 1.00 67.80 ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -17.418 -3.422  -35.887 1.00 68.04 ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -19.508 -2.516  -33.487 1.00 67.70 ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -17.063 -1.353  -35.111 1.00 67.78 ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -15.620 -1.379  -35.396 1.00 68.97 ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.985 -2.411  -34.443 1.00 66.96 ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -15.313 -2.412  -33.264 1.00 63.27 ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -15.021 0.026   -35.182 1.00 75.04 ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -13.506 0.104   -35.050 1.00 84.56 ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -13.070 1.226   -34.119 1.00 94.87 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -13.775 2.262   -34.063 1.00 97.24 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -12.029 1.068   -33.441 1.00 97.81 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -14.180 -3.335  -34.973 1.00 67.97 ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -13.570 -4.417  -34.193 1.00 68.71 ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -12.073 -4.176  -33.965 1.00 68.87 ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -11.297 -4.223  -34.924 1.00 70.48 ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.805 -5.786  -34.891 1.00 70.73 ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -13.243 -6.931  -34.069 1.00 70.91 ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -15.282 -6.011  -35.189 1.00 72.19 ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -11.639 -3.991  -32.683 1.00 67.03 ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -10.218 -3.740  -32.400 1.00 66.45 ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.803  -4.157  -30.970 1.00 65.00 ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -10.641 -4.623  -30.213 1.00 64.78 ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.875  -2.261  -32.713 1.00 69.35 ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -8.454  -2.168  -32.899 1.00 71.40 ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -10.359 -1.322  -31.636 1.00 69.25 ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -8.532  -3.981  -30.612 1.00 64.37 ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -8.037  -4.323  -29.292 1.00 64.68 ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -7.455  -5.714  -29.294 1.00 64.89 ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.933  -6.583  -30.031 1.00 65.92 ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -6.396  -5.922  -28.505 1.00 63.27 ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.827  -7.241  -28.384 1.00 62.99 ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -6.398  -7.922  -27.115 1.00 59.96 ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -7.311  -7.373  -26.473 1.00 57.76 ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -4.295  -7.199  -28.474 1.00 66.53 ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -3.668  -6.534  -27.284 1.00 72.12 ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.934  -5.365  -26.987 1.00 73.84 ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.803  -7.261  -26.593 1.00 74.94 ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.901  -9.119  -26.753 1.00 58.51 ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -6.426  -9.861  -25.591 1.00 57.45 ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -5.294  -10.347 -24.680 1.00 57.83 ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.955  -11.537 -24.668 1.00 58.04 ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -7.258  -11.050 -26.063 1.00 58.05 ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.930  -10.774 -27.283 1.00 60.81 ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -4.687  -9.429  -23.913 1.00 57.02 ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -3.525  -9.819  -23.119 1.00 56.71 ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.880  -10.638 -21.900 1.00 55.12 ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.904  -10.371 -21.251 1.00 53.21 ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.901  -8.475  -22.744 1.00 58.37 ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -4.092  -7.530  -22.651 1.00 58.34 ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.952  -7.971  -23.827 1.00 56.74 ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -3.023  -11.602 -21.560 1.00 54.16 ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -3.207  -12.414 -20.347 1.00 54.94 ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -2.179  -11.915 -19.317 1.00 53.86 ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.977  -12.081 -19.508 1.00 53.43 ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -3.019  -13.923 -20.636 1.00 58.00 ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -4.164  -14.544 -21.475 1.00 63.48 ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.873  -16.019 -21.785 1.00 69.36 ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -4.769  -16.608 -22.792 1.00 73.33 ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.928  -17.200 -22.510 1.00 74.27 ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -6.365  -17.257 -21.256 1.00 75.26 ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -6.667  -17.725 -23.482 1.00 70.43 ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.652  -11.246 -18.254 1.00 52.71 ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.766  -10.601 -17.292 1.00 52.45 ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.941  -11.080 -15.881 1.00 51.20 ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -3.065  -11.135 -15.393 1.00 50.92 ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -2.070  -9.079  -17.301 1.00 52.68 ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.981  -8.405  -18.674 1.00 54.42 ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.822  -7.146  -18.730 1.00 55.30 ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.520  -8.239  -19.132 1.00 56.27 ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.824  -11.231 -15.154 1.00 50.70 ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.864  -11.564 -13.737 1.00 50.80 ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.983  -10.213 -13.021 1.00 49.40 ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? -0.173  -9.311  -13.269 1.00 49.77 ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 0.428   -12.280 -13.285 1.00 54.41 ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 0.546   -13.755 -13.673 1.00 62.52 ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? -0.461  -14.337 -14.124 1.00 63.31 ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 1.645   -14.337 -13.483 1.00 66.17 ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -2.047  -10.036 -12.225 1.00 46.54 ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -2.261  -8.765  -11.547 1.00 45.17 ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.609  -8.952  -10.068 1.00 44.03 ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -3.013  -10.035 -9.637  1.00 44.52 ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -3.318  -7.866  -12.281 1.00 45.82 ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -3.037  -7.688  -13.768 1.00 46.44 ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.734  -8.357  -12.042 1.00 46.16 ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.438  -7.884  -9.284  1.00 42.93 ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.782  -7.845  -7.865  1.00 41.98 ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.773  -6.692  -7.656  1.00 40.60 ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.726  -5.704  -8.387  1.00 40.79 ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.536  -7.645  -7.005  1.00 42.17 ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.702  -6.851  -6.715  1.00 38.73 ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.722  -5.846  -6.444  1.00 38.55 ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.558  -5.451  -4.980  1.00 39.40 ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.593  -6.335  -4.128  1.00 39.97 ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -7.132  -6.459  -6.695  1.00 38.11 ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.303  -5.561  -6.338  1.00 39.74 ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.288  -4.237  -7.131  1.00 39.43 ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.644  -6.313  -6.454  1.00 41.19 ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -5.259  -4.166  -4.697  1.00 38.51 ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -5.038  -3.754  -3.311  1.00 38.90 ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.357  -3.303  -2.644  1.00 37.76 ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.409  -3.251  -3.294  1.00 37.80 ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.879  -2.729  -3.172  1.00 39.63 ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.127  -1.333  -3.731  1.00 42.35 ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.313  -0.995  -4.010  1.00 41.98 ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.135  -0.550  -3.849  1.00 44.98 ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.300  -3.025  -1.339  1.00 38.04 ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.466  -2.624  -0.579  1.00 38.04 ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -8.065  -1.318  -1.087  1.00 38.21 ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.278  -1.143  -0.969  1.00 39.16 ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -7.097  -2.541  0.905   1.00 40.50 ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -8.278  -2.332  1.819   1.00 44.26 ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.861  -2.430  3.276   1.00 51.67 ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.582  -1.373  3.893   1.00 49.82 ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.784  -3.571  3.788   1.00 54.73 ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.258  -0.443  -1.764  1.00 36.30 ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.810  0.794   -2.315  1.00 37.05 ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.462  0.620   -3.710  1.00 35.63 ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.896  1.613   -4.311  1.00 36.02 ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.717  1.848   -2.410  1.00 40.18 ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.327  2.208   -1.097  1.00 44.56 ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.548  -0.610  -4.209  1.00 34.11 ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.178  -0.842  -5.513  1.00 34.18 ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.232  -0.569  -6.672  1.00 36.05 ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.689  -0.447  -7.816  1.00 36.54 ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.932  -0.495  -6.405  1.00 35.98 ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.963  -0.284  -7.493  1.00 37.69 ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.419  -1.627  -7.976  1.00 38.26 ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.902  -2.414  -7.168  1.00 38.06 ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.738  0.524   -7.020  1.00 41.49 ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.022  1.829   -6.335  1.00 51.47 ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -5.828  2.611   -6.868  1.00 52.49 ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -4.432  2.069   -5.252  1.00 57.43 ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.445  -1.841  -9.304  1.00 38.58 ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.803  -3.000  -9.899  1.00 39.88 ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -3.327  -2.662  -10.177 1.00 42.40 ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -3.005  -1.537  -10.570 1.00 42.83 ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.484  -3.354  -11.230 1.00 38.76 ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.791  -4.088  -11.078 1.00 37.64 ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.821  -5.393  -10.612 1.00 38.13 ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -8.001  -3.458  -11.354 1.00 36.38 ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -8.021  -6.072  -10.489 1.00 38.30 ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -9.204  -4.138  -11.220 1.00 36.88 ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -9.211  -5.450  -10.823 1.00 37.54 ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.446  -3.660  -10.053 1.00 43.56 ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -1.039  -3.492  -10.388 1.00 46.45 ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.510  -4.793  -11.042 1.00 49.02 ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -1.066  -5.860  -10.805 1.00 48.31 ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? -0.224  -3.138  -9.149  1.00 47.51 ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.271  -4.203  -8.210  1.00 49.66 ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.540   -4.709  -11.876 1.00 51.91 ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.107   -5.901  -12.514 1.00 55.24 ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 1.979   -6.682  -11.530 1.00 58.71 ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 2.749   -6.080  -10.784 1.00 59.33 ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.021   -5.497  -13.679 1.00 56.37 ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.392   -4.793  -14.857 1.00 59.12 ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 2.474   -4.465  -15.884 1.00 60.12 ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.330   -5.667  -15.512 1.00 59.85 ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 1.929   -8.011  -11.582 1.00 60.65 ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 2.782   -8.848  -10.738 1.00 63.76 ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 3.879   -9.388  -11.641 1.00 67.41 ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.566   -9.980  -12.674 1.00 67.70 ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 1.988   -10.010 -10.108 1.00 64.28 ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 2.929   -10.984 -9.393  1.00 65.17 ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 0.908   -9.486  -9.171  1.00 64.34 ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.148   -9.147  -11.304 1.00 70.16 ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.255   -9.643  -12.141 1.00 73.24 ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.221   -10.534 -11.367 1.00 75.13 ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.032   -10.765 -10.169 1.00 76.39 ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.001   -8.479  -12.816 1.00 77.02 ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.093   -7.557  -13.622 1.00 83.58 ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 6.205   -7.703  -15.127 1.00 93.62 ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 6.904   -8.636  -15.589 1.00 94.88 ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 5.597   -6.878  -15.848 1.00 97.50 ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -36.398 13.154  -12.016 1.00 63.15 ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -35.590 13.229  -13.228 1.00 63.53 ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -35.789 12.085  -14.206 1.00 63.39 ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.816 11.393  -14.158 1.00 64.10 ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -34.825 11.898  -15.136 1.00 61.61 ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -34.942 10.825  -16.120 1.00 60.47 ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -34.561 9.463   -15.546 1.00 58.95 ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -33.449 9.241   -15.070 1.00 58.91 ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -34.190 11.110  -17.433 1.00 62.62 ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -34.576 10.117  -18.525 1.00 66.07 ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -34.056 10.435  -19.914 1.00 70.79 ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -33.082 11.220  -20.000 1.00 71.55 ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -34.647 9.951   -20.913 1.00 70.40 ? 17  GLU   B OE2 1 
ATOM   325  N  N   . THR   B 2 9   ? -35.523 8.564   -15.578 1.00 57.41 ? 18  THR   B N   1 
ATOM   326  C  CA  . THR   B 2 9   ? -35.424 7.211   -15.053 1.00 56.42 ? 18  THR   B CA  1 
ATOM   327  C  C   . THR   B 2 9   ? -35.356 6.165   -16.158 1.00 53.79 ? 18  THR   B C   1 
ATOM   328  O  O   . THR   B 2 9   ? -35.209 4.986   -15.869 1.00 54.45 ? 18  THR   B O   1 
ATOM   329  C  CB  . THR   B 2 9   ? -36.638 6.961   -14.134 1.00 58.69 ? 18  THR   B CB  1 
ATOM   330  O  OG1 . THR   B 2 9   ? -37.831 6.954   -14.932 1.00 59.87 ? 18  THR   B OG1 1 
ATOM   331  C  CG2 . THR   B 2 9   ? -36.772 8.027   -13.044 1.00 59.53 ? 18  THR   B CG2 1 
ATOM   332  N  N   . THR   B 2 10  ? -35.431 6.577   -17.442 1.00 50.86 ? 19  THR   B N   1 
ATOM   333  C  CA  . THR   B 2 10  ? -35.363 5.666   -18.569 1.00 48.57 ? 19  THR   B CA  1 
ATOM   334  C  C   . THR   B 2 10  ? -34.061 4.885   -18.525 1.00 44.91 ? 19  THR   B C   1 
ATOM   335  O  O   . THR   B 2 10  ? -33.005 5.462   -18.227 1.00 44.23 ? 19  THR   B O   1 
ATOM   336  C  CB  . THR   B 2 10  ? -35.465 6.470   -19.892 1.00 50.45 ? 19  THR   B CB  1 
ATOM   337  O  OG1 . THR   B 2 10  ? -36.572 7.376   -19.793 1.00 53.41 ? 19  THR   B OG1 1 
ATOM   338  C  CG2 . THR   B 2 10  ? -35.644 5.585   -21.102 1.00 51.06 ? 19  THR   B CG2 1 
ATOM   339  N  N   . ASP   B 2 11  ? -34.139 3.576   -18.781 1.00 42.37 ? 20  ASP   B N   1 
ATOM   340  C  CA  . ASP   B 2 11  ? -33.004 2.684   -18.892 1.00 42.03 ? 20  ASP   B CA  1 
ATOM   341  C  C   . ASP   B 2 11  ? -32.061 3.245   -19.984 1.00 41.06 ? 20  ASP   B C   1 
ATOM   342  O  O   . ASP   B 2 11  ? -32.528 3.925   -20.941 1.00 41.76 ? 20  ASP   B O   1 
ATOM   343  C  CB  . ASP   B 2 11  ? -33.452 1.267   -19.350 1.00 44.48 ? 20  ASP   B CB  1 
ATOM   344  C  CG  . ASP   B 2 11  ? -33.929 0.312   -18.267 1.00 49.43 ? 20  ASP   B CG  1 
ATOM   345  O  OD1 . ASP   B 2 11  ? -34.134 0.766   -17.127 1.00 47.17 ? 20  ASP   B OD1 1 
ATOM   346  O  OD2 . ASP   B 2 11  ? -34.089 -0.908  -18.568 1.00 52.48 ? 20  ASP   B OD2 1 
ATOM   347  N  N   . GLY   B 2 12  ? -30.789 2.976   -19.832 1.00 38.13 ? 21  GLY   B N   1 
ATOM   348  C  CA  . GLY   B 2 12  ? -29.782 3.360   -20.814 1.00 37.70 ? 21  GLY   B CA  1 
ATOM   349  C  C   . GLY   B 2 12  ? -28.476 3.806   -20.209 1.00 36.43 ? 21  GLY   B C   1 
ATOM   350  O  O   . GLY   B 2 12  ? -28.236 3.621   -18.994 1.00 34.03 ? 21  GLY   B O   1 
ATOM   351  N  N   . VAL   B 2 13  ? -27.593 4.305   -21.054 1.00 34.01 ? 22  VAL   B N   1 
ATOM   352  C  CA  . VAL   B 2 13  ? -26.294 4.794   -20.657 1.00 32.43 ? 22  VAL   B CA  1 
ATOM   353  C  C   . VAL   B 2 13  ? -26.308 6.305   -20.498 1.00 32.36 ? 22  VAL   B C   1 
ATOM   354  O  O   . VAL   B 2 13  ? -26.968 7.024   -21.284 1.00 33.78 ? 22  VAL   B O   1 
ATOM   355  C  CB  . VAL   B 2 13  ? -25.187 4.286   -21.569 1.00 33.85 ? 22  VAL   B CB  1 
ATOM   356  C  CG1 . VAL   B 2 13  ? -25.362 4.802   -22.998 1.00 33.71 ? 22  VAL   B CG1 1 
ATOM   357  C  CG2 . VAL   B 2 13  ? -23.797 4.591   -21.035 1.00 36.43 ? 22  VAL   B CG2 1 
ATOM   358  N  N   . TYR   B 2 14  ? -25.655 6.808   -19.420 1.00 30.94 ? 23  TYR   B N   1 
ATOM   359  C  CA  . TYR   B 2 14  ? -25.689 8.246   -19.109 1.00 32.05 ? 23  TYR   B CA  1 
ATOM   360  C  C   . TYR   B 2 14  ? -24.288 8.788   -18.831 1.00 32.97 ? 23  TYR   B C   1 
ATOM   361  O  O   . TYR   B 2 14  ? -23.435 8.073   -18.272 1.00 32.96 ? 23  TYR   B O   1 
ATOM   362  C  CB  . TYR   B 2 14  ? -26.460 8.469   -17.763 1.00 32.32 ? 23  TYR   B CB  1 
ATOM   363  C  CG  . TYR   B 2 14  ? -27.963 8.291   -17.820 1.00 31.96 ? 23  TYR   B CG  1 
ATOM   364  C  CD1 . TYR   B 2 14  ? -28.528 7.048   -18.135 1.00 32.29 ? 23  TYR   B CD1 1 
ATOM   365  C  CD2 . TYR   B 2 14  ? -28.812 9.385   -17.722 1.00 34.09 ? 23  TYR   B CD2 1 
ATOM   366  C  CE1 . TYR   B 2 14  ? -29.900 6.886   -18.221 1.00 33.95 ? 23  TYR   B CE1 1 
ATOM   367  C  CE2 . TYR   B 2 14  ? -30.189 9.239   -17.828 1.00 35.89 ? 23  TYR   B CE2 1 
ATOM   368  C  CZ  . TYR   B 2 14  ? -30.727 7.983   -18.057 1.00 36.97 ? 23  TYR   B CZ  1 
ATOM   369  O  OH  . TYR   B 2 14  ? -32.097 7.878   -18.159 1.00 41.54 ? 23  TYR   B OH  1 
ATOM   370  N  N   . ARG   B 2 15  ? -24.069 10.080  -19.148 1.00 32.46 ? 24  ARG   B N   1 
ATOM   371  C  CA  . ARG   B 2 15  ? -22.819 10.736  -18.781 1.00 32.62 ? 24  ARG   B CA  1 
ATOM   372  C  C   . ARG   B 2 15  ? -22.993 11.237  -17.329 1.00 32.15 ? 24  ARG   B C   1 
ATOM   373  O  O   . ARG   B 2 15  ? -24.084 11.658  -16.949 1.00 32.41 ? 24  ARG   B O   1 
ATOM   374  C  CB  . ARG   B 2 15  ? -22.602 12.004  -19.653 1.00 33.78 ? 24  ARG   B CB  1 
ATOM   375  C  CG  . ARG   B 2 15  ? -22.594 11.682  -21.142 1.00 36.50 ? 24  ARG   B CG  1 
ATOM   376  C  CD  . ARG   B 2 15  ? -22.506 12.972  -21.963 1.00 36.77 ? 24  ARG   B CD  1 
ATOM   377  N  NE  . ARG   B 2 15  ? -22.752 12.725  -23.382 1.00 38.64 ? 24  ARG   B NE  1 
ATOM   378  C  CZ  . ARG   B 2 15  ? -21.833 12.312  -24.247 1.00 41.66 ? 24  ARG   B CZ  1 
ATOM   379  N  NH1 . ARG   B 2 15  ? -20.567 12.157  -23.865 1.00 37.46 ? 24  ARG   B NH1 1 
ATOM   380  N  NH2 . ARG   B 2 15  ? -22.164 12.070  -25.506 1.00 44.22 ? 24  ARG   B NH2 1 
ATOM   381  N  N   . VAL   B 2 16  ? -21.908 11.285  -16.569 1.00 32.95 ? 25  VAL   B N   1 
ATOM   382  C  CA  . VAL   B 2 16  ? -21.887 11.856  -15.233 1.00 33.09 ? 25  VAL   B CA  1 
ATOM   383  C  C   . VAL   B 2 16  ? -21.041 13.130  -15.338 1.00 33.54 ? 25  VAL   B C   1 
ATOM   384  O  O   . VAL   B 2 16  ? -19.875 13.045  -15.745 1.00 33.27 ? 25  VAL   B O   1 
ATOM   385  C  CB  . VAL   B 2 16  ? -21.240 10.897  -14.212 1.00 34.08 ? 25  VAL   B CB  1 
ATOM   386  C  CG1 . VAL   B 2 16  ? -21.191 11.585  -12.844 1.00 35.05 ? 25  VAL   B CG1 1 
ATOM   387  C  CG2 . VAL   B 2 16  ? -22.036 9.600   -14.139 1.00 32.18 ? 25  VAL   B CG2 1 
ATOM   388  N  N   . MET   B 2 17  ? -21.672 14.275  -15.113 1.00 35.25 ? 26  MET   B N   1 
ATOM   389  C  CA  . MET   B 2 17  ? -21.082 15.595  -15.287 1.00 37.13 ? 26  MET   B CA  1 
ATOM   390  C  C   . MET   B 2 17  ? -20.907 16.350  -13.984 1.00 39.61 ? 26  MET   B C   1 
ATOM   391  O  O   . MET   B 2 17  ? -21.655 16.130  -13.045 1.00 39.32 ? 26  MET   B O   1 
ATOM   392  C  CB  . MET   B 2 17  ? -22.025 16.437  -16.183 1.00 37.83 ? 26  MET   B CB  1 
ATOM   393  C  CG  . MET   B 2 17  ? -22.469 15.755  -17.477 1.00 39.23 ? 26  MET   B CG  1 
ATOM   394  S  SD  . MET   B 2 17  ? -21.144 15.481  -18.661 1.00 38.74 ? 26  MET   B SD  1 
ATOM   395  C  CE  . MET   B 2 17  ? -20.600 17.225  -18.976 1.00 41.52 ? 26  MET   B CE  1 
ATOM   396  N  N   . THR   B 2 18  ? -20.006 17.337  -13.969 1.00 42.15 ? 27  THR   B N   1 
ATOM   397  C  CA  . THR   B 2 18  ? -19.880 18.256  -12.842 1.00 45.06 ? 27  THR   B CA  1 
ATOM   398  C  C   . THR   B 2 18  ? -19.666 19.662  -13.346 1.00 45.98 ? 27  THR   B C   1 
ATOM   399  O  O   . THR   B 2 18  ? -19.066 19.874  -14.407 1.00 43.90 ? 27  THR   B O   1 
ATOM   400  C  CB  . THR   B 2 18  ? -18.761 17.872  -11.857 1.00 48.55 ? 27  THR   B CB  1 
ATOM   401  O  OG1 . THR   B 2 18  ? -18.772 18.836  -10.784 1.00 51.28 ? 27  THR   B OG1 1 
ATOM   402  C  CG2 . THR   B 2 18  ? -17.383 17.829  -12.515 1.00 48.68 ? 27  THR   B CG2 1 
ATOM   403  N  N   . ARG   B 2 19  ? -20.135 20.631  -12.566 1.00 48.78 ? 28  ARG   B N   1 
ATOM   404  C  CA  . ARG   B 2 19  ? -19.860 22.028  -12.828 1.00 52.71 ? 28  ARG   B CA  1 
ATOM   405  C  C   . ARG   B 2 19  ? -18.867 22.625  -11.799 1.00 55.44 ? 28  ARG   B C   1 
ATOM   406  O  O   . ARG   B 2 19  ? -18.632 23.826  -11.825 1.00 56.13 ? 28  ARG   B O   1 
ATOM   407  C  CB  . ARG   B 2 19  ? -21.151 22.852  -12.959 1.00 56.14 ? 28  ARG   B CB  1 
ATOM   408  C  CG  . ARG   B 2 19  ? -21.908 22.474  -14.222 1.00 61.71 ? 28  ARG   B CG  1 
ATOM   409  C  CD  . ARG   B 2 19  ? -22.884 23.520  -14.685 1.00 68.16 ? 28  ARG   B CD  1 
ATOM   410  N  NE  . ARG   B 2 19  ? -23.599 23.072  -15.880 1.00 73.92 ? 28  ARG   B NE  1 
ATOM   411  C  CZ  . ARG   B 2 19  ? -24.884 22.728  -15.901 1.00 78.74 ? 28  ARG   B CZ  1 
ATOM   412  N  NH1 . ARG   B 2 19  ? -25.617 22.799  -14.793 1.00 79.21 ? 28  ARG   B NH1 1 
ATOM   413  N  NH2 . ARG   B 2 19  ? -25.450 22.320  -17.031 1.00 79.58 ? 28  ARG   B NH2 1 
ATOM   414  N  N   . ARG   B 2 20  ? -18.243 21.789  -10.939 1.00 57.89 ? 29  ARG   B N   1 
ATOM   415  C  CA  . ARG   B 2 20  ? -17.275 22.237  -9.923  1.00 60.81 ? 29  ARG   B CA  1 
ATOM   416  C  C   . ARG   B 2 20  ? -15.997 22.803  -10.557 1.00 62.07 ? 29  ARG   B C   1 
ATOM   417  O  O   . ARG   B 2 20  ? -15.468 23.806  -10.086 1.00 62.79 ? 29  ARG   B O   1 
ATOM   418  C  CB  . ARG   B 2 20  ? -16.941 21.092  -8.956  1.00 63.95 ? 29  ARG   B CB  1 
ATOM   419  C  CG  . ARG   B 2 20  ? -15.956 21.482  -7.860  1.00 70.77 ? 29  ARG   B CG  1 
ATOM   420  C  CD  . ARG   B 2 20  ? -15.656 20.329  -6.919  1.00 76.88 ? 29  ARG   B CD  1 
ATOM   421  N  NE  . ARG   B 2 20  ? -15.132 19.161  -7.630  1.00 82.20 ? 29  ARG   B NE  1 
ATOM   422  C  CZ  . ARG   B 2 20  ? -13.841 18.939  -7.862  1.00 86.57 ? 29  ARG   B CZ  1 
ATOM   423  N  NH1 . ARG   B 2 20  ? -12.923 19.804  -7.441  1.00 87.18 ? 29  ARG   B NH1 1 
ATOM   424  N  NH2 . ARG   B 2 20  ? -13.458 17.850  -8.516  1.00 87.17 ? 29  ARG   B NH2 1 
ATOM   425  N  N   . LEU   B 2 21  ? -15.535 22.189  -11.651 1.00 61.71 ? 30  LEU   B N   1 
ATOM   426  C  CA  . LEU   B 2 21  ? -14.334 22.614  -12.365 1.00 61.64 ? 30  LEU   B CA  1 
ATOM   427  C  C   . LEU   B 2 21  ? -14.675 23.696  -13.455 1.00 59.53 ? 30  LEU   B C   1 
ATOM   428  O  O   . LEU   B 2 21  ? -15.734 24.338  -13.405 1.00 59.38 ? 30  LEU   B O   1 
ATOM   429  C  CB  . LEU   B 2 21  ? -13.695 21.339  -12.996 1.00 63.09 ? 30  LEU   B CB  1 
ATOM   430  C  CG  . LEU   B 2 21  ? -12.666 20.467  -12.219 1.00 65.85 ? 30  LEU   B CG  1 
ATOM   431  C  CD1 . LEU   B 2 21  ? -12.474 20.889  -10.750 1.00 67.18 ? 30  LEU   B CD1 1 
ATOM   432  C  CD2 . LEU   B 2 21  ? -12.999 18.982  -12.345 1.00 66.45 ? 30  LEU   B CD2 1 
ATOM   433  N  N   . LEU   B 2 22  ? -13.767 23.916  -14.416 1.00 57.45 ? 31  LEU   B N   1 
ATOM   434  C  CA  . LEU   B 2 22  ? -14.003 24.841  -15.503 1.00 55.59 ? 31  LEU   B CA  1 
ATOM   435  C  C   . LEU   B 2 22  ? -15.149 24.295  -16.385 1.00 53.06 ? 31  LEU   B C   1 
ATOM   436  O  O   . LEU   B 2 22  ? -15.205 23.076  -16.621 1.00 53.26 ? 31  LEU   B O   1 
ATOM   437  C  CB  . LEU   B 2 22  ? -12.718 24.968  -16.309 1.00 56.05 ? 31  LEU   B CB  1 
ATOM   438  C  CG  . LEU   B 2 22  ? -12.730 26.020  -17.372 1.00 56.89 ? 31  LEU   B CG  1 
ATOM   439  C  CD1 . LEU   B 2 22  ? -12.701 27.459  -16.770 1.00 57.08 ? 31  LEU   B CD1 1 
ATOM   440  C  CD2 . LEU   B 2 22  ? -11.564 25.823  -18.307 1.00 58.34 ? 31  LEU   B CD2 1 
ATOM   441  N  N   . GLY   B 2 23  ? -16.084 25.171  -16.796 1.00 49.84 ? 32  GLY   B N   1 
ATOM   442  C  CA  . GLY   B 2 23  ? -17.254 24.789  -17.592 1.00 47.77 ? 32  GLY   B CA  1 
ATOM   443  C  C   . GLY   B 2 23  ? -18.010 23.558  -17.062 1.00 45.69 ? 32  GLY   B C   1 
ATOM   444  O  O   . GLY   B 2 23  ? -18.201 23.401  -15.856 1.00 45.07 ? 32  GLY   B O   1 
ATOM   445  N  N   . SER   B 2 24  ? -18.470 22.697  -17.971 1.00 45.17 ? 33  SER   B N   1 
ATOM   446  C  CA  . SER   B 2 24  ? -19.172 21.472  -17.594 1.00 45.73 ? 33  SER   B CA  1 
ATOM   447  C  C   . SER   B 2 24  ? -18.240 20.367  -18.016 1.00 44.42 ? 33  SER   B C   1 
ATOM   448  O  O   . SER   B 2 24  ? -17.774 20.330  -19.161 1.00 45.77 ? 33  SER   B O   1 
ATOM   449  C  CB  . SER   B 2 24  ? -20.515 21.351  -18.307 1.00 48.74 ? 33  SER   B CB  1 
ATOM   450  O  OG  . SER   B 2 24  ? -21.321 22.496  -18.067 1.00 51.58 ? 33  SER   B OG  1 
ATOM   451  N  N   . THR   B 2 25  ? -17.853 19.569  -17.064 1.00 42.72 ? 34  THR   B N   1 
ATOM   452  C  CA  . THR   B 2 25  ? -16.863 18.524  -17.272 1.00 41.19 ? 34  THR   B CA  1 
ATOM   453  C  C   . THR   B 2 25  ? -17.428 17.116  -17.056 1.00 40.43 ? 34  THR   B C   1 
ATOM   454  O  O   . THR   B 2 25  ? -18.109 16.844  -16.054 1.00 39.72 ? 34  THR   B O   1 
ATOM   455  C  CB  . THR   B 2 25  ? -15.651 18.756  -16.316 1.00 43.94 ? 34  THR   B CB  1 
ATOM   456  O  OG1 . THR   B 2 25  ? -15.114 20.075  -16.498 1.00 45.75 ? 34  THR   B OG1 1 
ATOM   457  C  CG2 . THR   B 2 25  ? -14.543 17.715  -16.488 1.00 44.47 ? 34  THR   B CG2 1 
ATOM   458  N  N   . GLN   B 2 26  ? -17.129 16.220  -18.009 1.00 38.59 ? 35  GLN   B N   1 
ATOM   459  C  CA  . GLN   B 2 26  ? -17.565 14.836  -17.863 1.00 38.00 ? 35  GLN   B CA  1 
ATOM   460  C  C   . GLN   B 2 26  ? -16.547 14.030  -17.026 1.00 39.16 ? 35  GLN   B C   1 
ATOM   461  O  O   . GLN   B 2 26  ? -15.420 13.790  -17.486 1.00 39.84 ? 35  GLN   B O   1 
ATOM   462  C  CB  . GLN   B 2 26  ? -17.815 14.149  -19.219 1.00 35.57 ? 35  GLN   B CB  1 
ATOM   463  C  CG  . GLN   B 2 26  ? -18.351 12.717  -19.043 1.00 34.30 ? 35  GLN   B CG  1 
ATOM   464  C  CD  . GLN   B 2 26  ? -18.642 12.098  -20.379 1.00 37.72 ? 35  GLN   B CD  1 
ATOM   465  O  OE1 . GLN   B 2 26  ? -19.269 12.729  -21.250 1.00 38.01 ? 35  GLN   B OE1 1 
ATOM   466  N  NE2 . GLN   B 2 26  ? -18.202 10.851  -20.573 1.00 36.11 ? 35  GLN   B NE2 1 
ATOM   467  N  N   . VAL   B 2 27  ? -16.974 13.585  -15.844 1.00 38.78 ? 36  VAL   B N   1 
ATOM   468  C  CA  . VAL   B 2 27  ? -16.083 12.794  -14.974 1.00 38.53 ? 36  VAL   B CA  1 
ATOM   469  C  C   . VAL   B 2 27  ? -16.256 11.270  -15.124 1.00 36.35 ? 36  VAL   B C   1 
ATOM   470  O  O   . VAL   B 2 27  ? -15.402 10.493  -14.645 1.00 36.54 ? 36  VAL   B O   1 
ATOM   471  C  CB  . VAL   B 2 27  ? -16.191 13.217  -13.506 1.00 39.94 ? 36  VAL   B CB  1 
ATOM   472  C  CG1 . VAL   B 2 27  ? -15.712 14.658  -13.319 1.00 41.95 ? 36  VAL   B CG1 1 
ATOM   473  C  CG2 . VAL   B 2 27  ? -17.609 13.051  -13.004 1.00 40.82 ? 36  VAL   B CG2 1 
ATOM   474  N  N   . GLY   B 2 28  ? -17.350 10.837  -15.729 1.00 34.04 ? 37  GLY   B N   1 
ATOM   475  C  CA  . GLY   B 2 28  ? -17.546 9.419   -15.995 1.00 32.70 ? 37  GLY   B CA  1 
ATOM   476  C  C   . GLY   B 2 28  ? -18.859 9.133   -16.681 1.00 33.10 ? 37  GLY   B C   1 
ATOM   477  O  O   . GLY   B 2 28  ? -19.478 10.031  -17.268 1.00 32.92 ? 37  GLY   B O   1 
ATOM   478  N  N   . VAL   B 2 29  ? -19.284 7.888   -16.589 1.00 30.97 ? 38  VAL   B N   1 
ATOM   479  C  CA  . VAL   B 2 29  ? -20.445 7.314   -17.267 1.00 31.87 ? 38  VAL   B CA  1 
ATOM   480  C  C   . VAL   B 2 29  ? -21.103 6.249   -16.369 1.00 32.47 ? 38  VAL   B C   1 
ATOM   481  O  O   . VAL   B 2 29  ? -20.453 5.737   -15.442 1.00 31.21 ? 38  VAL   B O   1 
ATOM   482  C  CB  . VAL   B 2 29  ? -19.932 6.633   -18.574 1.00 32.32 ? 38  VAL   B CB  1 
ATOM   483  C  CG1 . VAL   B 2 29  ? -21.053 5.932   -19.343 1.00 31.21 ? 38  VAL   B CG1 1 
ATOM   484  C  CG2 . VAL   B 2 29  ? -19.231 7.657   -19.464 1.00 33.12 ? 38  VAL   B CG2 1 
ATOM   485  N  N   . GLY   B 2 30  ? -22.382 5.983   -16.603 1.00 31.44 ? 39  GLY   B N   1 
ATOM   486  C  CA  . GLY   B 2 30  ? -23.063 4.950   -15.826 1.00 31.67 ? 39  GLY   B CA  1 
ATOM   487  C  C   . GLY   B 2 30  ? -24.249 4.348   -16.545 1.00 31.80 ? 39  GLY   B C   1 
ATOM   488  O  O   . GLY   B 2 30  ? -24.656 4.830   -17.612 1.00 31.38 ? 39  GLY   B O   1 
ATOM   489  N  N   . VAL   B 2 31  ? -24.844 3.320   -15.940 1.00 29.53 ? 40  VAL   B N   1 
ATOM   490  C  CA  . VAL   B 2 31  ? -25.953 2.548   -16.474 1.00 29.09 ? 40  VAL   B CA  1 
ATOM   491  C  C   . VAL   B 2 31  ? -27.207 2.618   -15.613 1.00 30.32 ? 40  VAL   B C   1 
ATOM   492  O  O   . VAL   B 2 31  ? -27.166 2.292   -14.408 1.00 28.78 ? 40  VAL   B O   1 
ATOM   493  C  CB  . VAL   B 2 31  ? -25.517 1.045   -16.575 1.00 31.53 ? 40  VAL   B CB  1 
ATOM   494  C  CG1 . VAL   B 2 31  ? -26.697 0.171   -16.992 1.00 32.38 ? 40  VAL   B CG1 1 
ATOM   495  C  CG2 . VAL   B 2 31  ? -24.334 0.865   -17.533 1.00 32.15 ? 40  VAL   B CG2 1 
ATOM   496  N  N   . MET   B 2 32  ? -28.347 3.003   -16.197 1.00 29.62 ? 41  MET   B N   1 
ATOM   497  C  CA  . MET   B 2 32  ? -29.632 3.023   -15.496 1.00 30.21 ? 41  MET   B CA  1 
ATOM   498  C  C   . MET   B 2 32  ? -30.342 1.726   -15.929 1.00 31.86 ? 41  MET   B C   1 
ATOM   499  O  O   . MET   B 2 32  ? -30.497 1.459   -17.146 1.00 32.70 ? 41  MET   B O   1 
ATOM   500  C  CB  . MET   B 2 32  ? -30.464 4.286   -15.833 1.00 30.79 ? 41  MET   B CB  1 
ATOM   501  C  CG  . MET   B 2 32  ? -31.712 4.381   -15.056 1.00 33.53 ? 41  MET   B CG  1 
ATOM   502  S  SD  . MET   B 2 32  ? -31.274 5.102   -13.424 1.00 36.02 ? 41  MET   B SD  1 
ATOM   503  C  CE  . MET   B 2 32  ? -30.935 6.792   -13.891 1.00 38.78 ? 41  MET   B CE  1 
ATOM   504  N  N   . GLN   B 2 33  ? -30.679 0.885   -14.958 1.00 29.98 ? 42  GLN   B N   1 
ATOM   505  C  CA  . GLN   B 2 33  ? -31.353 -0.363  -15.214 1.00 31.63 ? 42  GLN   B CA  1 
ATOM   506  C  C   . GLN   B 2 33  ? -32.230 -0.703  -14.032 1.00 33.83 ? 42  GLN   B C   1 
ATOM   507  O  O   . GLN   B 2 33  ? -31.770 -0.619  -12.884 1.00 33.34 ? 42  GLN   B O   1 
ATOM   508  C  CB  . GLN   B 2 33  ? -30.374 -1.522  -15.501 1.00 34.26 ? 42  GLN   B CB  1 
ATOM   509  C  CG  . GLN   B 2 33  ? -31.157 -2.767  -15.904 1.00 38.52 ? 42  GLN   B CG  1 
ATOM   510  C  CD  . GLN   B 2 33  ? -30.255 -3.900  -16.298 1.00 43.18 ? 42  GLN   B CD  1 
ATOM   511  O  OE1 . GLN   B 2 33  ? -30.341 -4.995  -15.738 1.00 48.47 ? 42  GLN   B OE1 1 
ATOM   512  N  NE2 . GLN   B 2 33  ? -29.353 -3.629  -17.248 1.00 39.40 ? 42  GLN   B NE2 1 
ATOM   513  N  N   . GLU   B 2 34  ? -33.522 -0.958  -14.277 1.00 35.23 ? 43  GLU   B N   1 
ATOM   514  C  CA  . GLU   B 2 34  ? -34.485 -1.351  -13.226 1.00 37.12 ? 43  GLU   B CA  1 
ATOM   515  C  C   . GLU   B 2 34  ? -34.576 -0.323  -12.085 1.00 38.66 ? 43  GLU   B C   1 
ATOM   516  O  O   . GLU   B 2 34  ? -34.618 -0.700  -10.907 1.00 40.78 ? 43  GLU   B O   1 
ATOM   517  C  CB  . GLU   B 2 34  ? -34.117 -2.745  -12.668 1.00 39.11 ? 43  GLU   B CB  1 
ATOM   518  C  CG  . GLU   B 2 34  ? -34.251 -3.904  -13.658 1.00 42.46 ? 43  GLU   B CG  1 
ATOM   519  C  CD  . GLU   B 2 34  ? -33.459 -5.147  -13.293 1.00 51.91 ? 43  GLU   B CD  1 
ATOM   520  O  OE1 . GLU   B 2 34  ? -33.680 -5.698  -12.192 1.00 54.41 ? 43  GLU   B OE1 1 
ATOM   521  O  OE2 . GLU   B 2 34  ? -32.600 -5.563  -14.100 1.00 57.53 ? 43  GLU   B OE2 1 
ATOM   522  N  N   . GLY   B 2 35  ? -34.527 0.951   -12.451 1.00 37.22 ? 44  GLY   B N   1 
ATOM   523  C  CA  . GLY   B 2 35  ? -34.649 2.063   -11.523 1.00 37.32 ? 44  GLY   B CA  1 
ATOM   524  C  C   . GLY   B 2 35  ? -33.407 2.367   -10.706 1.00 35.31 ? 44  GLY   B C   1 
ATOM   525  O  O   . GLY   B 2 35  ? -33.475 3.230   -9.801  1.00 36.24 ? 44  GLY   B O   1 
ATOM   526  N  N   . VAL   B 2 36  ? -32.272 1.670   -11.008 1.00 31.29 ? 45  VAL   B N   1 
ATOM   527  C  CA  . VAL   B 2 36  ? -31.007 1.856   -10.273 1.00 29.46 ? 45  VAL   B CA  1 
ATOM   528  C  C   . VAL   B 2 36  ? -29.880 2.400   -11.196 1.00 28.48 ? 45  VAL   B C   1 
ATOM   529  O  O   . VAL   B 2 36  ? -29.732 1.949   -12.364 1.00 28.83 ? 45  VAL   B O   1 
ATOM   530  C  CB  . VAL   B 2 36  ? -30.605 0.499   -9.636  1.00 29.79 ? 45  VAL   B CB  1 
ATOM   531  C  CG1 . VAL   B 2 36  ? -29.220 0.598   -8.989  1.00 28.34 ? 45  VAL   B CG1 1 
ATOM   532  C  CG2 . VAL   B 2 36  ? -31.663 0.075   -8.591  1.00 30.89 ? 45  VAL   B CG2 1 
ATOM   533  N  N   . PHE   B 2 37  ? -29.115 3.388   -10.684 1.00 28.00 ? 46  PHE   B N   1 
ATOM   534  C  CA  . PHE   B 2 37  ? -27.994 3.952   -11.426 1.00 27.85 ? 46  PHE   B CA  1 
ATOM   535  C  C   . PHE   B 2 37  ? -26.693 3.297   -10.979 1.00 26.95 ? 46  PHE   B C   1 
ATOM   536  O  O   . PHE   B 2 37  ? -26.433 3.249   -9.781  1.00 26.80 ? 46  PHE   B O   1 
ATOM   537  C  CB  . PHE   B 2 37  ? -27.912 5.471   -11.334 1.00 29.12 ? 46  PHE   B CB  1 
ATOM   538  C  CG  . PHE   B 2 37  ? -26.922 6.036   -12.322 1.00 29.44 ? 46  PHE   B CG  1 
ATOM   539  C  CD1 . PHE   B 2 37  ? -27.132 5.898   -13.694 1.00 31.27 ? 46  PHE   B CD1 1 
ATOM   540  C  CD2 . PHE   B 2 37  ? -25.762 6.661   -11.885 1.00 30.36 ? 46  PHE   B CD2 1 
ATOM   541  C  CE1 . PHE   B 2 37  ? -26.220 6.423   -14.604 1.00 32.13 ? 46  PHE   B CE1 1 
ATOM   542  C  CE2 . PHE   B 2 37  ? -24.865 7.216   -12.806 1.00 30.79 ? 46  PHE   B CE2 1 
ATOM   543  C  CZ  . PHE   B 2 37  ? -25.112 7.099   -14.156 1.00 31.69 ? 46  PHE   B CZ  1 
ATOM   544  N  N   . HIS   B 2 38  ? -25.927 2.804   -11.909 1.00 25.93 ? 47  HIS   B N   1 
ATOM   545  C  CA  . HIS   B 2 38  ? -24.710 1.999   -11.627 1.00 25.62 ? 47  HIS   B CA  1 
ATOM   546  C  C   . HIS   B 2 38  ? -23.489 2.696   -12.225 1.00 27.29 ? 47  HIS   B C   1 
ATOM   547  O  O   . HIS   B 2 38  ? -23.483 2.980   -13.434 1.00 27.98 ? 47  HIS   B O   1 
ATOM   548  C  CB  . HIS   B 2 38  ? -24.781 0.597   -12.297 1.00 26.42 ? 47  HIS   B CB  1 
ATOM   549  C  CG  . HIS   B 2 38  ? -26.009 -0.197  -11.953 1.00 27.31 ? 47  HIS   B CG  1 
ATOM   550  N  ND1 . HIS   B 2 38  ? -27.254 0.085   -12.531 1.00 29.42 ? 47  HIS   B ND1 1 
ATOM   551  C  CD2 . HIS   B 2 38  ? -26.143 -1.275  -11.131 1.00 28.61 ? 47  HIS   B CD2 1 
ATOM   552  C  CE1 . HIS   B 2 38  ? -28.093 -0.822  -12.048 1.00 28.79 ? 47  HIS   B CE1 1 
ATOM   553  N  NE2 . HIS   B 2 38  ? -27.462 -1.679  -11.222 1.00 29.29 ? 47  HIS   B NE2 1 
ATOM   554  N  N   . THR   B 2 39  ? -22.459 2.917   -11.407 1.00 26.37 ? 48  THR   B N   1 
ATOM   555  C  CA  . THR   B 2 39  ? -21.221 3.539   -11.953 1.00 26.43 ? 48  THR   B CA  1 
ATOM   556  C  C   . THR   B 2 39  ? -20.015 3.063   -11.155 1.00 28.22 ? 48  THR   B C   1 
ATOM   557  O  O   . THR   B 2 39  ? -20.186 2.186   -10.281 1.00 26.52 ? 48  THR   B O   1 
ATOM   558  C  CB  . THR   B 2 39  ? -21.349 5.095   -12.074 1.00 29.03 ? 48  THR   B CB  1 
ATOM   559  O  OG1 . THR   B 2 39  ? -20.200 5.619   -12.754 1.00 29.20 ? 48  THR   B OG1 1 
ATOM   560  C  CG2 . THR   B 2 39  ? -21.404 5.764   -10.677 1.00 28.68 ? 48  THR   B CG2 1 
ATOM   561  N  N   . MET   B 2 40  ? -18.803 3.589   -11.458 1.00 27.99 ? 49  MET   B N   1 
ATOM   562  C  CA  . MET   B 2 40  ? -17.635 3.149   -10.675 1.00 28.28 ? 49  MET   B CA  1 
ATOM   563  C  C   . MET   B 2 40  ? -17.467 4.112   -9.523  1.00 28.13 ? 49  MET   B C   1 
ATOM   564  O  O   . MET   B 2 40  ? -17.756 5.330   -9.637  1.00 29.71 ? 49  MET   B O   1 
ATOM   565  C  CB  . MET   B 2 40  ? -16.387 3.099   -11.589 1.00 29.07 ? 49  MET   B CB  1 
ATOM   566  C  CG  . MET   B 2 40  ? -16.644 2.193   -12.847 1.00 29.76 ? 49  MET   B CG  1 
ATOM   567  S  SD  . MET   B 2 40  ? -15.164 1.510   -13.536 1.00 38.05 ? 49  MET   B SD  1 
ATOM   568  C  CE  . MET   B 2 40  ? -14.886 0.214   -12.404 1.00 34.69 ? 49  MET   B CE  1 
ATOM   569  N  N   A TRP   B 2 41  ? -17.019 3.599   -8.364  0.25 28.05 ? 50  TRP   B N   1 
ATOM   570  N  N   B TRP   B 2 41  ? -17.014 3.600   -8.364  0.25 27.71 ? 50  TRP   B N   1 
ATOM   571  N  N   C TRP   B 2 41  ? -17.019 3.599   -8.364  0.25 28.05 ? 50  TRP   B N   1 
ATOM   572  N  N   D TRP   B 2 41  ? -17.014 3.600   -8.364  0.25 27.71 ? 50  TRP   B N   1 
ATOM   573  C  CA  A TRP   B 2 41  ? -16.838 4.437   -7.184  0.25 29.49 ? 50  TRP   B CA  1 
ATOM   574  C  CA  B TRP   B 2 41  ? -16.824 4.435   -7.183  0.25 28.85 ? 50  TRP   B CA  1 
ATOM   575  C  CA  C TRP   B 2 41  ? -16.838 4.437   -7.184  0.25 29.49 ? 50  TRP   B CA  1 
ATOM   576  C  CA  D TRP   B 2 41  ? -16.824 4.435   -7.183  0.25 28.85 ? 50  TRP   B CA  1 
ATOM   577  C  C   A TRP   B 2 41  ? -15.913 5.629   -7.438  0.25 29.97 ? 50  TRP   B C   1 
ATOM   578  C  C   B TRP   B 2 41  ? -15.912 5.634   -7.447  0.25 29.67 ? 50  TRP   B C   1 
ATOM   579  C  C   C TRP   B 2 41  ? -15.913 5.629   -7.438  0.25 29.97 ? 50  TRP   B C   1 
ATOM   580  C  C   D TRP   B 2 41  ? -15.912 5.634   -7.447  0.25 29.67 ? 50  TRP   B C   1 
ATOM   581  O  O   A TRP   B 2 41  ? -16.227 6.725   -7.001  0.25 30.28 ? 50  TRP   B O   1 
ATOM   582  O  O   B TRP   B 2 41  ? -16.228 6.730   -7.010  0.25 29.99 ? 50  TRP   B O   1 
ATOM   583  O  O   C TRP   B 2 41  ? -16.227 6.725   -7.001  0.25 30.28 ? 50  TRP   B O   1 
ATOM   584  O  O   D TRP   B 2 41  ? -16.228 6.730   -7.010  0.25 29.99 ? 50  TRP   B O   1 
ATOM   585  C  CB  A TRP   B 2 41  ? -16.320 3.599   -6.008  0.25 29.96 ? 50  TRP   B CB  1 
ATOM   586  C  CB  B TRP   B 2 41  ? -16.252 3.599   -6.027  0.25 28.81 ? 50  TRP   B CB  1 
ATOM   587  C  CB  C TRP   B 2 41  ? -16.320 3.599   -6.008  0.25 29.96 ? 50  TRP   B CB  1 
ATOM   588  C  CB  D TRP   B 2 41  ? -16.252 3.599   -6.027  0.25 28.81 ? 50  TRP   B CB  1 
ATOM   589  C  CG  A TRP   B 2 41  ? -16.400 4.334   -4.704  0.25 30.91 ? 50  TRP   B CG  1 
ATOM   590  C  CG  B TRP   B 2 41  ? -16.053 4.412   -4.783  0.25 29.08 ? 50  TRP   B CG  1 
ATOM   591  C  CG  C TRP   B 2 41  ? -16.400 4.334   -4.704  0.25 30.91 ? 50  TRP   B CG  1 
ATOM   592  C  CG  D TRP   B 2 41  ? -16.053 4.412   -4.783  0.25 29.08 ? 50  TRP   B CG  1 
ATOM   593  C  CD1 A TRP   B 2 41  ? -17.431 4.312   -3.810  0.25 31.93 ? 50  TRP   B CD1 1 
ATOM   594  C  CD1 B TRP   B 2 41  ? -14.963 5.165   -4.458  0.25 29.99 ? 50  TRP   B CD1 1 
ATOM   595  C  CD1 C TRP   B 2 41  ? -17.431 4.312   -3.810  0.25 31.93 ? 50  TRP   B CD1 1 
ATOM   596  C  CD1 D TRP   B 2 41  ? -14.963 5.165   -4.458  0.25 29.99 ? 50  TRP   B CD1 1 
ATOM   597  C  CD2 A TRP   B 2 41  ? -15.424 5.237   -4.168  0.25 31.61 ? 50  TRP   B CD2 1 
ATOM   598  C  CD2 B TRP   B 2 41  ? -17.016 4.633   -3.746  0.25 29.55 ? 50  TRP   B CD2 1 
ATOM   599  C  CD2 C TRP   B 2 41  ? -15.424 5.237   -4.168  0.25 31.61 ? 50  TRP   B CD2 1 
ATOM   600  C  CD2 D TRP   B 2 41  ? -17.016 4.633   -3.746  0.25 29.55 ? 50  TRP   B CD2 1 
ATOM   601  N  NE1 A TRP   B 2 41  ? -17.150 5.138   -2.745  0.25 32.50 ? 50  TRP   B NE1 1 
ATOM   602  N  NE1 B TRP   B 2 41  ? -15.185 5.833   -3.277  0.25 30.22 ? 50  TRP   B NE1 1 
ATOM   603  N  NE1 C TRP   B 2 41  ? -17.150 5.138   -2.745  0.25 32.50 ? 50  TRP   B NE1 1 
ATOM   604  N  NE1 D TRP   B 2 41  ? -15.185 5.833   -3.277  0.25 30.22 ? 50  TRP   B NE1 1 
ATOM   605  C  CE2 A TRP   B 2 41  ? -15.928 5.723   -2.945  0.25 32.36 ? 50  TRP   B CE2 1 
ATOM   606  C  CE2 B TRP   B 2 41  ? -16.438 5.526   -2.820  0.25 30.20 ? 50  TRP   B CE2 1 
ATOM   607  C  CE2 C TRP   B 2 41  ? -15.928 5.723   -2.945  0.25 32.36 ? 50  TRP   B CE2 1 
ATOM   608  C  CE2 D TRP   B 2 41  ? -16.438 5.526   -2.820  0.25 30.20 ? 50  TRP   B CE2 1 
ATOM   609  C  CE3 A TRP   B 2 41  ? -14.151 5.644   -4.579  0.25 32.60 ? 50  TRP   B CE3 1 
ATOM   610  C  CE3 B TRP   B 2 41  ? -18.314 4.170   -3.515  0.25 30.51 ? 50  TRP   B CE3 1 
ATOM   611  C  CE3 C TRP   B 2 41  ? -14.151 5.644   -4.579  0.25 32.60 ? 50  TRP   B CE3 1 
ATOM   612  C  CE3 D TRP   B 2 41  ? -18.314 4.170   -3.515  0.25 30.51 ? 50  TRP   B CE3 1 
ATOM   613  C  CZ2 A TRP   B 2 41  ? -15.220 6.621   -2.156  0.25 33.98 ? 50  TRP   B CZ2 1 
ATOM   614  C  CZ2 B TRP   B 2 41  ? -17.108 5.945   -1.673  0.25 31.63 ? 50  TRP   B CZ2 1 
ATOM   615  C  CZ2 C TRP   B 2 41  ? -15.220 6.621   -2.156  0.25 33.98 ? 50  TRP   B CZ2 1 
ATOM   616  C  CZ2 D TRP   B 2 41  ? -17.108 5.945   -1.673  0.25 31.63 ? 50  TRP   B CZ2 1 
ATOM   617  C  CZ3 A TRP   B 2 41  ? -13.454 6.535   -3.792  0.25 33.85 ? 50  TRP   B CZ3 1 
ATOM   618  C  CZ3 B TRP   B 2 41  ? -18.978 4.593   -2.383  0.25 31.57 ? 50  TRP   B CZ3 1 
ATOM   619  C  CZ3 C TRP   B 2 41  ? -13.454 6.535   -3.792  0.25 33.85 ? 50  TRP   B CZ3 1 
ATOM   620  C  CZ3 D TRP   B 2 41  ? -18.978 4.593   -2.383  0.25 31.57 ? 50  TRP   B CZ3 1 
ATOM   621  C  CH2 A TRP   B 2 41  ? -13.985 7.009   -2.596  0.25 34.17 ? 50  TRP   B CH2 1 
ATOM   622  C  CH2 B TRP   B 2 41  ? -18.377 5.473   -1.476  0.25 31.62 ? 50  TRP   B CH2 1 
ATOM   623  C  CH2 C TRP   B 2 41  ? -13.985 7.009   -2.596  0.25 34.17 ? 50  TRP   B CH2 1 
ATOM   624  C  CH2 D TRP   B 2 41  ? -18.377 5.473   -1.476  0.25 31.62 ? 50  TRP   B CH2 1 
ATOM   625  N  N   . HIS   B 2 42  ? -14.804 5.434   -8.168  1.00 29.58 ? 51  HIS   B N   1 
ATOM   626  C  CA  . HIS   B 2 42  ? -13.847 6.529   -8.408  1.00 31.41 ? 51  HIS   B CA  1 
ATOM   627  C  C   . HIS   B 2 42  ? -14.429 7.690   -9.253  1.00 32.54 ? 51  HIS   B C   1 
ATOM   628  O  O   . HIS   B 2 42  ? -13.863 8.797   -9.245  1.00 33.82 ? 51  HIS   B O   1 
ATOM   629  C  CB  . HIS   B 2 42  ? -12.505 6.038   -8.956  1.00 32.28 ? 51  HIS   B CB  1 
ATOM   630  C  CG  . HIS   B 2 42  ? -12.542 5.756   -10.430 1.00 33.70 ? 51  HIS   B CG  1 
ATOM   631  N  ND1 . HIS   B 2 42  ? -12.716 4.468   -10.923 1.00 34.96 ? 51  HIS   B ND1 1 
ATOM   632  C  CD2 . HIS   B 2 42  ? -12.421 6.615   -11.474 1.00 35.61 ? 51  HIS   B CD2 1 
ATOM   633  C  CE1 . HIS   B 2 42  ? -12.642 4.576   -12.248 1.00 36.35 ? 51  HIS   B CE1 1 
ATOM   634  N  NE2 . HIS   B 2 42  ? -12.491 5.855   -12.631 1.00 35.84 ? 51  HIS   B NE2 1 
ATOM   635  N  N   . VAL   B 2 43  ? -15.577 7.460   -9.924  1.00 30.91 ? 52  VAL   B N   1 
ATOM   636  C  CA  . VAL   B 2 43  ? -16.218 8.545   -10.712 1.00 30.07 ? 52  VAL   B CA  1 
ATOM   637  C  C   . VAL   B 2 43  ? -16.925 9.541   -9.773  1.00 32.00 ? 52  VAL   B C   1 
ATOM   638  O  O   . VAL   B 2 43  ? -16.767 10.768  -9.937  1.00 33.33 ? 52  VAL   B O   1 
ATOM   639  C  CB  . VAL   B 2 43  ? -17.243 7.976   -11.724 1.00 30.54 ? 52  VAL   B CB  1 
ATOM   640  C  CG1 . VAL   B 2 43  ? -18.128 9.106   -12.348 1.00 30.46 ? 52  VAL   B CG1 1 
ATOM   641  C  CG2 . VAL   B 2 43  ? -16.524 7.200   -12.828 1.00 30.23 ? 52  VAL   B CG2 1 
ATOM   642  N  N   . THR   B 2 44  ? -17.717 9.020   -8.790  1.00 29.25 ? 53  THR   B N   1 
ATOM   643  C  CA  . THR   B 2 44  ? -18.501 9.916   -7.940  1.00 29.36 ? 53  THR   B CA  1 
ATOM   644  C  C   . THR   B 2 44  ? -17.979 10.085  -6.522  1.00 30.87 ? 53  THR   B C   1 
ATOM   645  O  O   . THR   B 2 44  ? -18.456 10.969  -5.798  1.00 31.48 ? 53  THR   B O   1 
ATOM   646  C  CB  . THR   B 2 44  ? -19.979 9.424   -7.822  1.00 30.46 ? 53  THR   B CB  1 
ATOM   647  O  OG1 . THR   B 2 44  ? -19.964 8.166   -7.115  1.00 29.47 ? 53  THR   B OG1 1 
ATOM   648  C  CG2 . THR   B 2 44  ? -20.660 9.262   -9.189  1.00 31.40 ? 53  THR   B CG2 1 
ATOM   649  N  N   . LYS   B 2 45  ? -17.061 9.222   -6.111  1.00 30.74 ? 54  LYS   B N   1 
ATOM   650  C  CA  . LYS   B 2 45  ? -16.557 9.165   -4.718  1.00 31.92 ? 54  LYS   B CA  1 
ATOM   651  C  C   . LYS   B 2 45  ? -17.736 8.971   -3.716  1.00 33.48 ? 54  LYS   B C   1 
ATOM   652  O  O   . LYS   B 2 45  ? -17.630 9.308   -2.523  1.00 35.12 ? 54  LYS   B O   1 
ATOM   653  C  CB  . LYS   B 2 45  ? -15.681 10.417  -4.370  1.00 34.85 ? 54  LYS   B CB  1 
ATOM   654  C  CG  . LYS   B 2 45  ? -14.581 10.746  -5.401  1.00 44.11 ? 54  LYS   B CG  1 
ATOM   655  C  CD  . LYS   B 2 45  ? -13.606 9.631   -5.629  1.00 51.14 ? 54  LYS   B CD  1 
ATOM   656  C  CE  . LYS   B 2 45  ? -12.391 10.067  -6.454  1.00 57.39 ? 54  LYS   B CE  1 
ATOM   657  N  NZ  . LYS   B 2 45  ? -12.761 10.860  -7.663  1.00 58.93 ? 54  LYS   B NZ  1 
ATOM   658  N  N   . GLY   B 2 46  ? -18.854 8.428   -4.194  1.00 34.04 ? 55  GLY   B N   1 
ATOM   659  C  CA  . GLY   B 2 46  ? -20.016 8.175   -3.345  1.00 34.39 ? 55  GLY   B CA  1 
ATOM   660  C  C   . GLY   B 2 46  ? -20.896 9.392   -3.134  1.00 34.86 ? 55  GLY   B C   1 
ATOM   661  O  O   . GLY   B 2 46  ? -21.740 9.379   -2.247  1.00 37.24 ? 55  GLY   B O   1 
ATOM   662  N  N   . ALA   B 2 47  ? -20.674 10.499  -3.880  1.00 34.45 ? 56  ALA   B N   1 
ATOM   663  C  CA  . ALA   B 2 47  ? -21.509 11.704  -3.709  1.00 35.45 ? 56  ALA   B CA  1 
ATOM   664  C  C   . ALA   B 2 47  ? -22.938 11.496  -4.275  1.00 35.14 ? 56  ALA   B C   1 
ATOM   665  O  O   . ALA   B 2 47  ? -23.114 10.731  -5.223  1.00 32.63 ? 56  ALA   B O   1 
ATOM   666  C  CB  . ALA   B 2 47  ? -20.872 12.875  -4.450  1.00 36.84 ? 56  ALA   B CB  1 
ATOM   667  N  N   . ALA   B 2 48  ? -23.919 12.315  -3.821  1.00 35.69 ? 57  ALA   B N   1 
ATOM   668  C  CA  . ALA   B 2 48  ? -25.262 12.284  -4.425  1.00 36.09 ? 57  ALA   B CA  1 
ATOM   669  C  C   . ALA   B 2 48  ? -25.190 12.830  -5.849  1.00 35.74 ? 57  ALA   B C   1 
ATOM   670  O  O   . ALA   B 2 48  ? -24.264 13.569  -6.181  1.00 37.50 ? 57  ALA   B O   1 
ATOM   671  C  CB  . ALA   B 2 48  ? -26.244 13.153  -3.616  1.00 36.84 ? 57  ALA   B CB  1 
ATOM   672  N  N   . LEU   B 2 49  ? -26.175 12.488  -6.690  1.00 33.80 ? 58  LEU   B N   1 
ATOM   673  C  CA  . LEU   B 2 49  ? -26.246 12.934  -8.068  1.00 35.36 ? 58  LEU   B CA  1 
ATOM   674  C  C   . LEU   B 2 49  ? -27.601 13.603  -8.312  1.00 37.38 ? 58  LEU   B C   1 
ATOM   675  O  O   . LEU   B 2 49  ? -28.576 13.299  -7.616  1.00 38.06 ? 58  LEU   B O   1 
ATOM   676  C  CB  . LEU   B 2 49  ? -26.156 11.733  -9.028  1.00 35.48 ? 58  LEU   B CB  1 
ATOM   677  C  CG  . LEU   B 2 49  ? -24.928 10.876  -8.880  1.00 36.57 ? 58  LEU   B CG  1 
ATOM   678  C  CD1 . LEU   B 2 49  ? -25.009 9.665   -9.786  1.00 36.17 ? 58  LEU   B CD1 1 
ATOM   679  C  CD2 . LEU   B 2 49  ? -23.664 11.644  -9.213  1.00 38.85 ? 58  LEU   B CD2 1 
ATOM   680  N  N   . ARG   B 2 50  ? -27.645 14.475  -9.298  1.00 37.84 ? 59  ARG   B N   1 
ATOM   681  C  CA  . ARG   B 2 50  ? -28.855 15.157  -9.716  1.00 40.17 ? 59  ARG   B CA  1 
ATOM   682  C  C   . ARG   B 2 50  ? -29.280 14.571  -11.083 1.00 41.13 ? 59  ARG   B C   1 
ATOM   683  O  O   . ARG   B 2 50  ? -28.433 14.261  -11.925 1.00 39.14 ? 59  ARG   B O   1 
ATOM   684  C  CB  . ARG   B 2 50  ? -28.530 16.659  -9.846  1.00 42.97 ? 59  ARG   B CB  1 
ATOM   685  C  CG  . ARG   B 2 50  ? -29.649 17.510  -10.394 1.00 51.28 ? 59  ARG   B CG  1 
ATOM   686  C  CD  . ARG   B 2 50  ? -29.473 19.016  -10.119 1.00 55.71 ? 59  ARG   B CD  1 
ATOM   687  N  NE  . ARG   B 2 50  ? -28.069 19.453  -10.124 1.00 57.83 ? 59  ARG   B NE  1 
ATOM   688  C  CZ  . ARG   B 2 50  ? -27.405 19.841  -11.205 1.00 58.90 ? 59  ARG   B CZ  1 
ATOM   689  N  NH1 . ARG   B 2 50  ? -28.014 19.885  -12.387 1.00 56.77 ? 59  ARG   B NH1 1 
ATOM   690  N  NH2 . ARG   B 2 50  ? -26.133 20.210  -11.112 1.00 59.32 ? 59  ARG   B NH2 1 
ATOM   691  N  N   . SER   B 2 51  ? -30.580 14.425  -11.293 1.00 43.24 ? 60  SER   B N   1 
ATOM   692  C  CA  . SER   B 2 51  ? -31.131 13.982  -12.568 1.00 46.08 ? 60  SER   B CA  1 
ATOM   693  C  C   . SER   B 2 51  ? -32.286 14.958  -12.800 1.00 48.39 ? 60  SER   B C   1 
ATOM   694  O  O   . SER   B 2 51  ? -33.331 14.796  -12.193 1.00 48.39 ? 60  SER   B O   1 
ATOM   695  C  CB  . SER   B 2 51  ? -31.642 12.550  -12.438 1.00 49.37 ? 60  SER   B CB  1 
ATOM   696  O  OG  . SER   B 2 51  ? -32.184 12.106  -13.664 1.00 53.38 ? 60  SER   B OG  1 
ATOM   697  N  N   . GLY   B 2 52  ? -32.050 16.024  -13.568 1.00 50.14 ? 61  GLY   B N   1 
ATOM   698  C  CA  . GLY   B 2 52  ? -33.040 17.080  -13.776 1.00 52.12 ? 61  GLY   B CA  1 
ATOM   699  C  C   . GLY   B 2 52  ? -33.281 17.797  -12.467 1.00 54.18 ? 61  GLY   B C   1 
ATOM   700  O  O   . GLY   B 2 52  ? -32.338 18.296  -11.848 1.00 54.66 ? 61  GLY   B O   1 
ATOM   701  N  N   . GLU   B 2 53  ? -34.529 17.785  -11.988 1.00 55.09 ? 62  GLU   B N   1 
ATOM   702  C  CA  . GLU   B 2 53  ? -34.858 18.360  -10.687 1.00 55.97 ? 62  GLU   B CA  1 
ATOM   703  C  C   . GLU   B 2 53  ? -34.788 17.330  -9.538  1.00 55.24 ? 62  GLU   B C   1 
ATOM   704  O  O   . GLU   B 2 53  ? -34.987 17.712  -8.391  1.00 55.84 ? 62  GLU   B O   1 
ATOM   705  C  CB  . GLU   B 2 53  ? -36.271 18.962  -10.716 1.00 59.92 ? 62  GLU   B CB  1 
ATOM   706  C  CG  . GLU   B 2 53  ? -36.308 20.467  -10.874 1.00 68.54 ? 62  GLU   B CG  1 
ATOM   707  C  CD  . GLU   B 2 53  ? -37.716 21.010  -10.724 1.00 80.55 ? 62  GLU   B CD  1 
ATOM   708  O  OE1 . GLU   B 2 53  ? -38.637 20.446  -11.360 1.00 84.16 ? 62  GLU   B OE1 1 
ATOM   709  O  OE2 . GLU   B 2 53  ? -37.902 21.996  -9.975  1.00 83.90 ? 62  GLU   B OE2 1 
ATOM   710  N  N   . GLY   B 2 54  ? -34.534 16.051  -9.841  1.00 53.44 ? 63  GLY   B N   1 
ATOM   711  C  CA  . GLY   B 2 54  ? -34.506 14.998  -8.836  1.00 52.12 ? 63  GLY   B CA  1 
ATOM   712  C  C   . GLY   B 2 54  ? -33.123 14.640  -8.323  1.00 49.75 ? 63  GLY   B C   1 
ATOM   713  O  O   . GLY   B 2 54  ? -32.105 15.033  -8.905  1.00 49.07 ? 63  GLY   B O   1 
ATOM   714  N  N   . ARG   B 2 55  ? -33.084 13.955  -7.184  1.00 47.39 ? 64  ARG   B N   1 
ATOM   715  C  CA  . ARG   B 2 55  ? -31.826 13.566  -6.560  1.00 45.93 ? 64  ARG   B CA  1 
ATOM   716  C  C   . ARG   B 2 55  ? -31.722 12.021  -6.499  1.00 43.46 ? 64  ARG   B C   1 
ATOM   717  O  O   . ARG   B 2 55  ? -32.706 11.324  -6.240  1.00 44.48 ? 64  ARG   B O   1 
ATOM   718  C  CB  . ARG   B 2 55  ? -31.775 14.159  -5.149  1.00 47.79 ? 64  ARG   B CB  1 
ATOM   719  C  CG  . ARG   B 2 55  ? -30.530 13.882  -4.313  1.00 50.35 ? 64  ARG   B CG  1 
ATOM   720  C  CD  . ARG   B 2 55  ? -30.826 14.377  -2.896  1.00 53.41 ? 64  ARG   B CD  1 
ATOM   721  N  NE  . ARG   B 2 55  ? -29.815 13.995  -1.918  1.00 56.51 ? 64  ARG   B NE  1 
ATOM   722  C  CZ  . ARG   B 2 55  ? -28.905 14.819  -1.406  1.00 60.81 ? 64  ARG   B CZ  1 
ATOM   723  N  NH1 . ARG   B 2 55  ? -28.895 16.103  -1.747  1.00 62.18 ? 64  ARG   B NH1 1 
ATOM   724  N  NH2 . ARG   B 2 55  ? -28.022 14.374  -0.521  1.00 58.94 ? 64  ARG   B NH2 1 
ATOM   725  N  N   . LEU   B 2 56  ? -30.522 11.508  -6.754  1.00 38.87 ? 65  LEU   B N   1 
ATOM   726  C  CA  . LEU   B 2 56  ? -30.207 10.093  -6.671  1.00 36.50 ? 65  LEU   B CA  1 
ATOM   727  C  C   . LEU   B 2 56  ? -29.231 9.942   -5.521  1.00 34.64 ? 65  LEU   B C   1 
ATOM   728  O  O   . LEU   B 2 56  ? -28.167 10.592  -5.496  1.00 35.45 ? 65  LEU   B O   1 
ATOM   729  C  CB  . LEU   B 2 56  ? -29.531 9.597   -7.955  1.00 36.08 ? 65  LEU   B CB  1 
ATOM   730  C  CG  . LEU   B 2 56  ? -30.237 9.696   -9.309  1.00 40.03 ? 65  LEU   B CG  1 
ATOM   731  C  CD1 . LEU   B 2 56  ? -29.616 8.662   -10.285 1.00 39.69 ? 65  LEU   B CD1 1 
ATOM   732  C  CD2 . LEU   B 2 56  ? -31.689 9.361   -9.250  1.00 43.08 ? 65  LEU   B CD2 1 
ATOM   733  N  N   . ASP   B 2 57  ? -29.620 9.181   -4.514  1.00 33.41 ? 66  ASP   B N   1 
ATOM   734  C  CA  . ASP   B 2 57  ? -28.767 8.979   -3.347  1.00 34.09 ? 66  ASP   B CA  1 
ATOM   735  C  C   . ASP   B 2 57  ? -28.037 7.639   -3.476  1.00 32.55 ? 66  ASP   B C   1 
ATOM   736  O  O   . ASP   B 2 57  ? -28.637 6.665   -3.933  1.00 32.01 ? 66  ASP   B O   1 
ATOM   737  C  CB  . ASP   B 2 57  ? -29.597 8.963   -2.057  1.00 38.00 ? 66  ASP   B CB  1 
ATOM   738  C  CG  . ASP   B 2 57  ? -30.251 10.306  -1.778  1.00 46.30 ? 66  ASP   B CG  1 
ATOM   739  O  OD1 . ASP   B 2 57  ? -29.632 11.343  -2.108  1.00 45.26 ? 66  ASP   B OD1 1 
ATOM   740  O  OD2 . ASP   B 2 57  ? -31.385 10.313  -1.257  1.00 49.90 ? 66  ASP   B OD2 1 
ATOM   741  N  N   . PRO   B 2 58  ? -26.802 7.548   -2.975  1.00 31.91 ? 67  PRO   B N   1 
ATOM   742  C  CA  . PRO   B 2 58  ? -26.105 6.250   -2.998  1.00 31.73 ? 67  PRO   B CA  1 
ATOM   743  C  C   . PRO   B 2 58  ? -26.838 5.249   -2.122  1.00 31.01 ? 67  PRO   B C   1 
ATOM   744  O  O   . PRO   B 2 58  ? -27.440 5.605   -1.089  1.00 32.00 ? 67  PRO   B O   1 
ATOM   745  C  CB  . PRO   B 2 58  ? -24.711 6.561   -2.447  1.00 32.22 ? 67  PRO   B CB  1 
ATOM   746  C  CG  . PRO   B 2 58  ? -24.920 7.847   -1.611  1.00 34.76 ? 67  PRO   B CG  1 
ATOM   747  C  CD  . PRO   B 2 58  ? -25.976 8.615   -2.370  1.00 33.06 ? 67  PRO   B CD  1 
ATOM   748  N  N   . TYR   B 2 59  ? -26.766 3.984   -2.558  1.00 28.04 ? 68  TYR   B N   1 
ATOM   749  C  CA  . TYR   B 2 59  ? -27.439 2.891   -1.857  1.00 27.59 ? 68  TYR   B CA  1 
ATOM   750  C  C   . TYR   B 2 59  ? -26.441 1.781   -1.455  1.00 26.67 ? 68  TYR   B C   1 
ATOM   751  O  O   . TYR   B 2 59  ? -26.529 1.259   -0.339  1.00 29.02 ? 68  TYR   B O   1 
ATOM   752  C  CB  . TYR   B 2 59  ? -28.516 2.325   -2.808  1.00 28.31 ? 68  TYR   B CB  1 
ATOM   753  C  CG  . TYR   B 2 59  ? -29.298 1.176   -2.197  1.00 28.65 ? 68  TYR   B CG  1 
ATOM   754  C  CD1 . TYR   B 2 59  ? -28.744 -0.096  -2.101  1.00 30.95 ? 68  TYR   B CD1 1 
ATOM   755  C  CD2 . TYR   B 2 59  ? -30.573 1.378   -1.658  1.00 29.61 ? 68  TYR   B CD2 1 
ATOM   756  C  CE1 . TYR   B 2 59  ? -29.452 -1.158  -1.547  1.00 32.39 ? 68  TYR   B CE1 1 
ATOM   757  C  CE2 . TYR   B 2 59  ? -31.300 0.313   -1.126  1.00 30.53 ? 68  TYR   B CE2 1 
ATOM   758  C  CZ  . TYR   B 2 59  ? -30.732 -0.951  -1.071  1.00 32.03 ? 68  TYR   B CZ  1 
ATOM   759  O  OH  . TYR   B 2 59  ? -31.424 -2.010  -0.540  1.00 32.82 ? 68  TYR   B OH  1 
ATOM   760  N  N   . TRP   B 2 60  ? -25.506 1.464   -2.310  1.00 24.97 ? 69  TRP   B N   1 
ATOM   761  C  CA  . TRP   B 2 60  ? -24.468 0.479   -1.996  1.00 25.34 ? 69  TRP   B CA  1 
ATOM   762  C  C   . TRP   B 2 60  ? -23.182 0.978   -2.684  1.00 27.33 ? 69  TRP   B C   1 
ATOM   763  O  O   . TRP   B 2 60  ? -23.222 1.471   -3.806  1.00 26.76 ? 69  TRP   B O   1 
ATOM   764  C  CB  . TRP   B 2 60  ? -24.853 -0.918  -2.533  1.00 27.03 ? 69  TRP   B CB  1 
ATOM   765  C  CG  . TRP   B 2 60  ? -23.708 -1.902  -2.518  1.00 28.21 ? 69  TRP   B CG  1 
ATOM   766  C  CD1 . TRP   B 2 60  ? -23.249 -2.603  -1.439  1.00 28.64 ? 69  TRP   B CD1 1 
ATOM   767  C  CD2 . TRP   B 2 60  ? -22.811 -2.177  -3.598  1.00 26.66 ? 69  TRP   B CD2 1 
ATOM   768  N  NE1 . TRP   B 2 60  ? -22.122 -3.324  -1.788  1.00 27.57 ? 69  TRP   B NE1 1 
ATOM   769  C  CE2 . TRP   B 2 60  ? -21.819 -3.063  -3.113  1.00 27.37 ? 69  TRP   B CE2 1 
ATOM   770  C  CE3 . TRP   B 2 60  ? -22.745 -1.754  -4.921  1.00 28.38 ? 69  TRP   B CE3 1 
ATOM   771  C  CZ2 . TRP   B 2 60  ? -20.811 -3.577  -3.918  1.00 28.86 ? 69  TRP   B CZ2 1 
ATOM   772  C  CZ3 . TRP   B 2 60  ? -21.719 -2.228  -5.704  1.00 28.98 ? 69  TRP   B CZ3 1 
ATOM   773  C  CH2 . TRP   B 2 60  ? -20.771 -3.134  -5.217  1.00 28.86 ? 69  TRP   B CH2 1 
ATOM   774  N  N   . GLY   B 2 61  ? -22.046 0.656   -2.079  1.00 27.68 ? 70  GLY   B N   1 
ATOM   775  C  CA  . GLY   B 2 61  ? -20.760 0.958   -2.714  1.00 28.72 ? 70  GLY   B CA  1 
ATOM   776  C  C   . GLY   B 2 61  ? -19.634 0.201   -2.052  1.00 26.97 ? 70  GLY   B C   1 
ATOM   777  O  O   . GLY   B 2 61  ? -19.751 -0.180  -0.879  1.00 26.85 ? 70  GLY   B O   1 
ATOM   778  N  N   . ASP   B 2 62  ? -18.535 0.055   -2.805  1.00 25.90 ? 71  ASP   B N   1 
ATOM   779  C  CA  . ASP   B 2 62  ? -17.361 -0.654  -2.324  1.00 26.60 ? 71  ASP   B CA  1 
ATOM   780  C  C   . ASP   B 2 62  ? -16.118 -0.164  -3.025  1.00 27.38 ? 71  ASP   B C   1 
ATOM   781  O  O   . ASP   B 2 62  ? -15.993 -0.294  -4.230  1.00 27.93 ? 71  ASP   B O   1 
ATOM   782  C  CB  . ASP   B 2 62  ? -17.542 -2.177  -2.432  1.00 30.60 ? 71  ASP   B CB  1 
ATOM   783  C  CG  . ASP   B 2 62  ? -16.438 -2.972  -1.719  1.00 37.13 ? 71  ASP   B CG  1 
ATOM   784  O  OD1 . ASP   B 2 62  ? -15.317 -2.981  -2.196  1.00 34.46 ? 71  ASP   B OD1 1 
ATOM   785  O  OD2 . ASP   B 2 62  ? -16.699 -3.499  -0.646  1.00 41.65 ? 71  ASP   B OD2 1 
ATOM   786  N  N   . VAL   B 2 63  ? -15.220 0.494   -2.283  1.00 27.27 ? 72  VAL   B N   1 
ATOM   787  C  CA  . VAL   B 2 63  ? -13.982 1.049   -2.882  1.00 27.37 ? 72  VAL   B CA  1 
ATOM   788  C  C   . VAL   B 2 63  ? -13.101 -0.034  -3.566  1.00 28.43 ? 72  VAL   B C   1 
ATOM   789  O  O   . VAL   B 2 63  ? -12.486 0.232   -4.628  1.00 29.87 ? 72  VAL   B O   1 
ATOM   790  C  CB  . VAL   B 2 63  ? -13.202 1.855   -1.787  1.00 28.91 ? 72  VAL   B CB  1 
ATOM   791  C  CG1 . VAL   B 2 63  ? -11.697 2.000   -2.112  1.00 30.56 ? 72  VAL   B CG1 1 
ATOM   792  C  CG2 . VAL   B 2 63  ? -13.867 3.210   -1.529  1.00 30.04 ? 72  VAL   B CG2 1 
ATOM   793  N  N   . LYS   B 2 64  ? -13.014 -1.233  -2.914  1.00 28.12 ? 73  LYS   B N   1 
ATOM   794  C  CA  . LYS   B 2 64  ? -12.123 -2.282  -3.477  1.00 29.51 ? 73  LYS   B CA  1 
ATOM   795  C  C   . LYS   B 2 64  ? -12.628 -2.827  -4.825  1.00 30.70 ? 73  LYS   B C   1 
ATOM   796  O  O   . LYS   B 2 64  ? -11.867 -2.924  -5.779  1.00 32.96 ? 73  LYS   B O   1 
ATOM   797  C  CB  . LYS   B 2 64  ? -11.860 -3.388  -2.464  1.00 31.69 ? 73  LYS   B CB  1 
ATOM   798  C  CG  . LYS   B 2 64  ? -10.832 -4.383  -3.037  1.00 34.71 ? 73  LYS   B CG  1 
ATOM   799  C  CD  . LYS   B 2 64  ? -10.568 -5.484  -2.034  1.00 37.14 ? 73  LYS   B CD  1 
ATOM   800  C  CE  . LYS   B 2 64  ? -9.624  -6.508  -2.623  1.00 40.91 ? 73  LYS   B CE  1 
ATOM   801  N  NZ  . LYS   B 2 64  ? -9.249  -7.548  -1.604  1.00 42.31 ? 73  LYS   B NZ  1 
ATOM   802  N  N   . GLN   B 2 65  ? -13.950 -3.063  -4.903  1.00 29.78 ? 74  GLN   B N   1 
ATOM   803  C  CA  . GLN   B 2 65  ? -14.584 -3.436  -6.179  1.00 29.41 ? 74  GLN   B CA  1 
ATOM   804  C  C   . GLN   B 2 65  ? -14.628 -2.238  -7.154  1.00 29.13 ? 74  GLN   B C   1 
ATOM   805  O  O   . GLN   B 2 65  ? -14.766 -2.436  -8.384  1.00 29.16 ? 74  GLN   B O   1 
ATOM   806  C  CB  . GLN   B 2 65  ? -16.032 -3.925  -5.965  1.00 30.24 ? 74  GLN   B CB  1 
ATOM   807  C  CG  . GLN   B 2 65  ? -16.120 -5.226  -5.129  1.00 35.08 ? 74  GLN   B CG  1 
ATOM   808  C  CD  . GLN   B 2 65  ? -17.553 -5.722  -4.971  1.00 43.48 ? 74  GLN   B CD  1 
ATOM   809  O  OE1 . GLN   B 2 65  ? -18.348 -5.764  -5.925  1.00 44.43 ? 74  GLN   B OE1 1 
ATOM   810  N  NE2 . GLN   B 2 65  ? -17.930 -6.163  -3.756  1.00 46.23 ? 74  GLN   B NE2 1 
ATOM   811  N  N   . ASP   B 2 66  ? -14.537 -1.014  -6.607  1.00 29.41 ? 75  ASP   B N   1 
ATOM   812  C  CA  . ASP   B 2 66  ? -14.605 0.248   -7.333  1.00 28.68 ? 75  ASP   B CA  1 
ATOM   813  C  C   . ASP   B 2 66  ? -15.993 0.353   -8.027  1.00 27.52 ? 75  ASP   B C   1 
ATOM   814  O  O   . ASP   B 2 66  ? -16.100 0.779   -9.190  1.00 27.44 ? 75  ASP   B O   1 
ATOM   815  C  CB  . ASP   B 2 66  ? -13.439 0.442   -8.383  1.00 28.72 ? 75  ASP   B CB  1 
ATOM   816  C  CG  . ASP   B 2 66  ? -13.362 1.864   -8.916  1.00 30.28 ? 75  ASP   B CG  1 
ATOM   817  O  OD1 . ASP   B 2 66  ? -13.799 2.775   -8.230  1.00 29.97 ? 75  ASP   B OD1 1 
ATOM   818  O  OD2 . ASP   B 2 66  ? -12.893 2.048   -10.067 1.00 32.39 ? 75  ASP   B OD2 1 
ATOM   819  N  N   . LEU   B 2 67  ? -17.059 0.080   -7.256  1.00 26.88 ? 76  LEU   B N   1 
ATOM   820  C  CA  . LEU   B 2 67  ? -18.430 0.156   -7.782  1.00 26.66 ? 76  LEU   B CA  1 
ATOM   821  C  C   . LEU   B 2 67  ? -19.370 0.882   -6.817  1.00 26.16 ? 76  LEU   B C   1 
ATOM   822  O  O   . LEU   B 2 67  ? -19.140 0.863   -5.605  1.00 26.48 ? 76  LEU   B O   1 
ATOM   823  C  CB  . LEU   B 2 67  ? -19.021 -1.240  -8.019  1.00 27.69 ? 76  LEU   B CB  1 
ATOM   824  C  CG  . LEU   B 2 67  ? -18.383 -2.047  -9.163  1.00 29.73 ? 76  LEU   B CG  1 
ATOM   825  C  CD1 . LEU   B 2 67  ? -19.016 -3.444  -9.239  1.00 30.57 ? 76  LEU   B CD1 1 
ATOM   826  C  CD2 . LEU   B 2 67  ? -18.592 -1.264  -10.533 1.00 28.92 ? 76  LEU   B CD2 1 
ATOM   827  N  N   . VAL   B 2 68  ? -20.466 1.409   -7.353  1.00 25.55 ? 77  VAL   B N   1 
ATOM   828  C  CA  . VAL   B 2 68  ? -21.480 2.115   -6.552  1.00 26.04 ? 77  VAL   B CA  1 
ATOM   829  C  C   . VAL   B 2 68  ? -22.826 2.027   -7.276  1.00 25.99 ? 77  VAL   B C   1 
ATOM   830  O  O   . VAL   B 2 68  ? -22.894 2.090   -8.511  1.00 26.00 ? 77  VAL   B O   1 
ATOM   831  C  CB  . VAL   B 2 68  ? -21.045 3.594   -6.218  1.00 26.23 ? 77  VAL   B CB  1 
ATOM   832  C  CG1 . VAL   B 2 68  ? -20.839 4.427   -7.485  1.00 26.98 ? 77  VAL   B CG1 1 
ATOM   833  C  CG2 . VAL   B 2 68  ? -22.052 4.302   -5.276  1.00 26.04 ? 77  VAL   B CG2 1 
ATOM   834  N  N   . SER   B 2 69  ? -23.902 1.873   -6.495  1.00 25.40 ? 78  SER   B N   1 
ATOM   835  C  CA  . SER   B 2 69  ? -25.271 1.896   -7.038  1.00 25.30 ? 78  SER   B CA  1 
ATOM   836  C  C   . SER   B 2 69  ? -26.090 2.995   -6.291  1.00 26.92 ? 78  SER   B C   1 
ATOM   837  O  O   . SER   B 2 69  ? -25.837 3.253   -5.107  1.00 26.29 ? 78  SER   B O   1 
ATOM   838  C  CB  . SER   B 2 69  ? -25.967 0.533   -6.950  1.00 25.70 ? 78  SER   B CB  1 
ATOM   839  O  OG  . SER   B 2 69  ? -26.236 0.159   -5.606  1.00 26.49 ? 78  SER   B OG  1 
ATOM   840  N  N   . TYR   B 2 70  ? -27.041 3.577   -7.001  1.00 27.63 ? 79  TYR   B N   1 
ATOM   841  C  CA  . TYR   B 2 70  ? -27.905 4.673   -6.517  1.00 27.94 ? 79  TYR   B CA  1 
ATOM   842  C  C   . TYR   B 2 70  ? -29.382 4.232   -6.647  1.00 29.06 ? 79  TYR   B C   1 
ATOM   843  O  O   . TYR   B 2 70  ? -29.755 3.664   -7.676  1.00 28.44 ? 79  TYR   B O   1 
ATOM   844  C  CB  . TYR   B 2 70  ? -27.720 5.940   -7.404  1.00 28.08 ? 79  TYR   B CB  1 
ATOM   845  C  CG  . TYR   B 2 70  ? -26.387 6.614   -7.175  1.00 27.35 ? 79  TYR   B CG  1 
ATOM   846  C  CD1 . TYR   B 2 70  ? -25.224 6.123   -7.764  1.00 27.73 ? 79  TYR   B CD1 1 
ATOM   847  C  CD2 . TYR   B 2 70  ? -26.282 7.737   -6.358  1.00 28.61 ? 79  TYR   B CD2 1 
ATOM   848  C  CE1 . TYR   B 2 70  ? -23.985 6.721   -7.518  1.00 28.22 ? 79  TYR   B CE1 1 
ATOM   849  C  CE2 . TYR   B 2 70  ? -25.053 8.329   -6.100  1.00 28.67 ? 79  TYR   B CE2 1 
ATOM   850  C  CZ  . TYR   B 2 70  ? -23.900 7.777   -6.628  1.00 29.72 ? 79  TYR   B CZ  1 
ATOM   851  O  OH  . TYR   B 2 70  ? -22.680 8.374   -6.389  1.00 31.50 ? 79  TYR   B OH  1 
ATOM   852  N  N   . CYS   B 2 71  ? -30.240 4.626   -5.657  1.00 29.27 ? 80  CYS   B N   1 
ATOM   853  C  CA  . CYS   B 2 71  ? -31.691 4.344   -5.606  1.00 31.72 ? 80  CYS   B CA  1 
ATOM   854  C  C   . CYS   B 2 71  ? -32.063 2.907   -5.291  1.00 32.36 ? 80  CYS   B C   1 
ATOM   855  O  O   . CYS   B 2 71  ? -33.232 2.642   -4.990  1.00 35.30 ? 80  CYS   B O   1 
ATOM   856  C  CB  . CYS   B 2 71  ? -32.452 4.810   -6.840  1.00 33.18 ? 80  CYS   B CB  1 
ATOM   857  S  SG  . CYS   B 2 71  ? -31.966 6.458   -7.421  1.00 38.69 ? 80  CYS   B SG  1 
ATOM   858  N  N   . GLY   B 2 72  ? -31.114 2.006   -5.326  1.00 30.68 ? 81  GLY   B N   1 
ATOM   859  C  CA  . GLY   B 2 72  ? -31.391 0.598   -5.043  1.00 30.24 ? 81  GLY   B CA  1 
ATOM   860  C  C   . GLY   B 2 72  ? -30.147 -0.245  -5.144  1.00 28.72 ? 81  GLY   B C   1 
ATOM   861  O  O   . GLY   B 2 72  ? -29.055 0.257   -5.444  1.00 28.83 ? 81  GLY   B O   1 
ATOM   862  N  N   . PRO   B 2 73  ? -30.299 -1.557  -4.900  1.00 28.78 ? 82  PRO   B N   1 
ATOM   863  C  CA  . PRO   B 2 73  ? -29.137 -2.447  -4.925  1.00 28.94 ? 82  PRO   B CA  1 
ATOM   864  C  C   . PRO   B 2 73  ? -28.643 -2.714  -6.340  1.00 29.13 ? 82  PRO   B C   1 
ATOM   865  O  O   . PRO   B 2 73  ? -29.396 -2.508  -7.298  1.00 29.80 ? 82  PRO   B O   1 
ATOM   866  C  CB  . PRO   B 2 73  ? -29.673 -3.753  -4.286  1.00 30.85 ? 82  PRO   B CB  1 
ATOM   867  C  CG  . PRO   B 2 73  ? -31.101 -3.727  -4.593  1.00 32.59 ? 82  PRO   B CG  1 
ATOM   868  C  CD  . PRO   B 2 73  ? -31.526 -2.272  -4.501  1.00 30.37 ? 82  PRO   B CD  1 
ATOM   869  N  N   . TRP   B 2 74  ? -27.389 -3.142  -6.463  1.00 28.47 ? 83  TRP   B N   1 
ATOM   870  C  CA  . TRP   B 2 74  ? -26.746 -3.432  -7.770  1.00 29.49 ? 83  TRP   B CA  1 
ATOM   871  C  C   . TRP   B 2 74  ? -27.607 -4.457  -8.524  1.00 29.71 ? 83  TRP   B C   1 
ATOM   872  O  O   . TRP   B 2 74  ? -27.937 -5.499  -7.960  1.00 31.46 ? 83  TRP   B O   1 
ATOM   873  C  CB  . TRP   B 2 74  ? -25.330 -3.983  -7.514  1.00 28.99 ? 83  TRP   B CB  1 
ATOM   874  C  CG  . TRP   B 2 74  ? -24.554 -4.211  -8.780  1.00 28.01 ? 83  TRP   B CG  1 
ATOM   875  C  CD1 . TRP   B 2 74  ? -24.498 -5.360  -9.527  1.00 29.40 ? 83  TRP   B CD1 1 
ATOM   876  C  CD2 . TRP   B 2 74  ? -23.684 -3.274  -9.418  1.00 28.50 ? 83  TRP   B CD2 1 
ATOM   877  N  NE1 . TRP   B 2 74  ? -23.710 -5.163  -10.637 1.00 29.44 ? 83  TRP   B NE1 1 
ATOM   878  C  CE2 . TRP   B 2 74  ? -23.212 -3.882  -10.608 1.00 28.51 ? 83  TRP   B CE2 1 
ATOM   879  C  CE3 . TRP   B 2 74  ? -23.341 -1.929  -9.169  1.00 27.78 ? 83  TRP   B CE3 1 
ATOM   880  C  CZ2 . TRP   B 2 74  ? -22.398 -3.207  -11.524 1.00 28.89 ? 83  TRP   B CZ2 1 
ATOM   881  C  CZ3 . TRP   B 2 74  ? -22.506 -1.275  -10.058 1.00 28.02 ? 83  TRP   B CZ3 1 
ATOM   882  C  CH2 . TRP   B 2 74  ? -22.096 -1.893  -11.261 1.00 27.60 ? 83  TRP   B CH2 1 
ATOM   883  N  N   . LYS   B 2 75  ? -27.983 -4.162  -9.766  1.00 29.45 ? 84  LYS   B N   1 
ATOM   884  C  CA  . LYS   B 2 75  ? -28.902 -5.034  -10.533 1.00 30.02 ? 84  LYS   B CA  1 
ATOM   885  C  C   . LYS   B 2 75  ? -28.234 -5.830  -11.644 1.00 32.76 ? 84  LYS   B C   1 
ATOM   886  O  O   . LYS   B 2 75  ? -28.884 -6.719  -12.191 1.00 34.28 ? 84  LYS   B O   1 
ATOM   887  C  CB  . LYS   B 2 75  ? -29.961 -4.169  -11.229 1.00 30.61 ? 84  LYS   B CB  1 
ATOM   888  C  CG  . LYS   B 2 75  ? -30.808 -3.313  -10.268 1.00 32.73 ? 84  LYS   B CG  1 
ATOM   889  C  CD  . LYS   B 2 75  ? -31.738 -4.179  -9.398  1.00 37.43 ? 84  LYS   B CD  1 
ATOM   890  C  CE  . LYS   B 2 75  ? -32.751 -3.273  -8.689  1.00 42.01 ? 84  LYS   B CE  1 
ATOM   891  N  NZ  . LYS   B 2 75  ? -33.814 -4.029  -8.010  1.00 45.06 ? 84  LYS   B NZ  1 
ATOM   892  N  N   . LEU   B 2 76  ? -27.004 -5.473  -12.020 1.00 31.95 ? 85  LEU   B N   1 
ATOM   893  C  CA  . LEU   B 2 76  ? -26.338 -6.084  -13.182 1.00 31.96 ? 85  LEU   B CA  1 
ATOM   894  C  C   . LEU   B 2 76  ? -25.668 -7.403  -12.787 1.00 33.73 ? 85  LEU   B C   1 
ATOM   895  O  O   . LEU   B 2 76  ? -24.784 -7.425  -11.933 1.00 33.93 ? 85  LEU   B O   1 
ATOM   896  C  CB  . LEU   B 2 76  ? -25.326 -5.109  -13.802 1.00 31.46 ? 85  LEU   B CB  1 
ATOM   897  C  CG  . LEU   B 2 76  ? -25.837 -3.650  -14.030 1.00 31.21 ? 85  LEU   B CG  1 
ATOM   898  C  CD1 . LEU   B 2 76  ? -24.728 -2.760  -14.566 1.00 32.45 ? 85  LEU   B CD1 1 
ATOM   899  C  CD2 . LEU   B 2 76  ? -27.080 -3.604  -14.880 1.00 33.03 ? 85  LEU   B CD2 1 
ATOM   900  N  N   . ASP   B 2 77  ? -26.080 -8.508  -13.453 1.00 36.01 ? 86  ASP   B N   1 
ATOM   901  C  CA  . ASP   B 2 77  ? -25.486 -9.801  -13.068 1.00 38.40 ? 86  ASP   B CA  1 
ATOM   902  C  C   . ASP   B 2 77  ? -24.992 -10.646 -14.215 1.00 37.81 ? 86  ASP   B C   1 
ATOM   903  O  O   . ASP   B 2 77  ? -24.530 -11.776 -13.959 1.00 38.05 ? 86  ASP   B O   1 
ATOM   904  C  CB  . ASP   B 2 77  ? -26.420 -10.638 -12.181 1.00 44.55 ? 86  ASP   B CB  1 
ATOM   905  C  CG  . ASP   B 2 77  ? -27.773 -10.959 -12.774 1.00 54.74 ? 86  ASP   B CG  1 
ATOM   906  O  OD1 . ASP   B 2 77  ? -28.122 -10.371 -13.813 1.00 56.87 ? 86  ASP   B OD1 1 
ATOM   907  O  OD2 . ASP   B 2 77  ? -28.482 -11.805 -12.197 1.00 60.75 ? 86  ASP   B OD2 1 
ATOM   908  N  N   . ALA   B 2 78  ? -25.046 -10.134 -15.447 1.00 36.73 ? 87  ALA   B N   1 
ATOM   909  C  CA  . ALA   B 2 78  ? -24.501 -10.940 -16.551 1.00 36.94 ? 87  ALA   B CA  1 
ATOM   910  C  C   . ALA   B 2 78  ? -22.993 -11.032 -16.454 1.00 37.07 ? 87  ALA   B C   1 
ATOM   911  O  O   . ALA   B 2 78  ? -22.315 -10.147 -15.929 1.00 36.02 ? 87  ALA   B O   1 
ATOM   912  C  CB  . ALA   B 2 78  ? -24.935 -10.397 -17.903 1.00 36.14 ? 87  ALA   B CB  1 
ATOM   913  N  N   . ALA   B 2 79  ? -22.439 -12.157 -16.961 1.00 37.68 ? 88  ALA   B N   1 
ATOM   914  C  CA  . ALA   B 2 79  ? -21.016 -12.392 -16.891 1.00 38.69 ? 88  ALA   B CA  1 
ATOM   915  C  C   . ALA   B 2 79  ? -20.453 -12.703 -18.253 1.00 39.13 ? 88  ALA   B C   1 
ATOM   916  O  O   . ALA   B 2 79  ? -21.107 -13.399 -19.045 1.00 40.44 ? 88  ALA   B O   1 
ATOM   917  C  CB  . ALA   B 2 79  ? -20.750 -13.594 -15.989 1.00 39.91 ? 88  ALA   B CB  1 
ATOM   918  N  N   . TRP   B 2 80  ? -19.189 -12.307 -18.502 1.00 39.15 ? 89  TRP   B N   1 
ATOM   919  C  CA  . TRP   B 2 80  ? -18.513 -12.706 -19.755 1.00 40.31 ? 89  TRP   B CA  1 
ATOM   920  C  C   . TRP   B 2 80  ? -18.397 -14.270 -19.762 1.00 41.19 ? 89  TRP   B C   1 
ATOM   921  O  O   . TRP   B 2 80  ? -18.145 -14.868 -18.725 1.00 40.93 ? 89  TRP   B O   1 
ATOM   922  C  CB  . TRP   B 2 80  ? -17.074 -12.140 -19.803 1.00 41.17 ? 89  TRP   B CB  1 
ATOM   923  C  CG  . TRP   B 2 80  ? -16.304 -12.467 -21.065 1.00 41.89 ? 89  TRP   B CG  1 
ATOM   924  C  CD1 . TRP   B 2 80  ? -16.782 -12.477 -22.343 1.00 43.38 ? 89  TRP   B CD1 1 
ATOM   925  C  CD2 . TRP   B 2 80  ? -14.932 -12.900 -21.142 1.00 42.71 ? 89  TRP   B CD2 1 
ATOM   926  N  NE1 . TRP   B 2 80  ? -15.788 -12.857 -23.217 1.00 44.31 ? 89  TRP   B NE1 1 
ATOM   927  C  CE2 . TRP   B 2 80  ? -14.651 -13.156 -22.504 1.00 44.20 ? 89  TRP   B CE2 1 
ATOM   928  C  CE3 . TRP   B 2 80  ? -13.921 -13.108 -20.192 1.00 43.92 ? 89  TRP   B CE3 1 
ATOM   929  C  CZ2 . TRP   B 2 80  ? -13.381 -13.516 -22.948 1.00 45.64 ? 89  TRP   B CZ2 1 
ATOM   930  C  CZ3 . TRP   B 2 80  ? -12.668 -13.514 -20.632 1.00 45.23 ? 89  TRP   B CZ3 1 
ATOM   931  C  CH2 . TRP   B 2 80  ? -12.413 -13.729 -21.997 1.00 45.74 ? 89  TRP   B CH2 1 
ATOM   932  N  N   . ASP   B 2 81  ? -18.699 -14.887 -20.943 1.00 43.22 ? 90  ASP   B N   1 
ATOM   933  C  CA  . ASP   B 2 81  ? -18.635 -16.351 -21.046 1.00 46.95 ? 90  ASP   B CA  1 
ATOM   934  C  C   . ASP   B 2 81  ? -17.197 -16.917 -21.130 1.00 50.77 ? 90  ASP   B C   1 
ATOM   935  O  O   . ASP   B 2 81  ? -17.022 -18.149 -21.154 1.00 52.54 ? 90  ASP   B O   1 
ATOM   936  C  CB  . ASP   B 2 81  ? -19.496 -16.836 -22.233 1.00 47.65 ? 90  ASP   B CB  1 
ATOM   937  C  CG  . ASP   B 2 81  ? -19.008 -16.430 -23.590 1.00 50.70 ? 90  ASP   B CG  1 
ATOM   938  O  OD1 . ASP   B 2 81  ? -17.885 -15.883 -23.684 1.00 49.69 ? 90  ASP   B OD1 1 
ATOM   939  O  OD2 . ASP   B 2 81  ? -19.756 -16.640 -24.583 1.00 56.35 ? 90  ASP   B OD2 1 
ATOM   940  N  N   . GLY   B 2 82  ? -16.194 -16.050 -21.257 1.00 51.38 ? 91  GLY   B N   1 
ATOM   941  C  CA  . GLY   B 2 82  ? -14.791 -16.484 -21.325 1.00 51.98 ? 91  GLY   B CA  1 
ATOM   942  C  C   . GLY   B 2 82  ? -14.315 -16.877 -22.723 1.00 54.06 ? 91  GLY   B C   1 
ATOM   943  O  O   . GLY   B 2 82  ? -13.160 -17.301 -22.887 1.00 55.52 ? 91  GLY   B O   1 
ATOM   944  N  N   . LEU   B 2 83  ? -15.185 -16.784 -23.734 1.00 53.70 ? 92  LEU   B N   1 
ATOM   945  C  CA  . LEU   B 2 83  ? -14.820 -17.197 -25.105 1.00 55.68 ? 92  LEU   B CA  1 
ATOM   946  C  C   . LEU   B 2 83  ? -15.120 -16.154 -26.197 1.00 56.20 ? 92  LEU   B C   1 
ATOM   947  O  O   . LEU   B 2 83  ? -14.393 -16.065 -27.189 1.00 56.66 ? 92  LEU   B O   1 
ATOM   948  C  CB  . LEU   B 2 83  ? -15.641 -18.438 -25.499 1.00 57.02 ? 92  LEU   B CB  1 
ATOM   949  C  CG  . LEU   B 2 83  ? -15.389 -19.760 -24.853 1.00 61.22 ? 92  LEU   B CG  1 
ATOM   950  C  CD1 . LEU   B 2 83  ? -16.107 -20.835 -25.636 1.00 62.54 ? 92  LEU   B CD1 1 
ATOM   951  C  CD2 . LEU   B 2 83  ? -13.903 -20.114 -24.877 1.00 61.76 ? 92  LEU   B CD2 1 
ATOM   952  N  N   . SER   B 2 84  ? -16.259 -15.458 -26.082 1.00 55.35 ? 93  SER   B N   1 
ATOM   953  C  CA  . SER   B 2 84  ? -16.772 -14.571 -27.124 1.00 55.18 ? 93  SER   B CA  1 
ATOM   954  C  C   . SER   B 2 84  ? -16.326 -13.123 -27.078 1.00 52.15 ? 93  SER   B C   1 
ATOM   955  O  O   . SER   B 2 84  ? -15.933 -12.622 -26.022 1.00 50.49 ? 93  SER   B O   1 
ATOM   956  C  CB  . SER   B 2 84  ? -18.300 -14.597 -27.130 1.00 57.83 ? 93  SER   B CB  1 
ATOM   957  O  OG  . SER   B 2 84  ? -18.814 -15.900 -26.904 1.00 62.00 ? 93  SER   B OG  1 
ATOM   958  N  N   . GLU   B 2 85  ? -16.364 -12.467 -28.231 1.00 49.92 ? 94  GLU   B N   1 
ATOM   959  C  CA  . GLU   B 2 85  ? -16.096 -11.040 -28.328 1.00 48.19 ? 94  GLU   B CA  1 
ATOM   960  C  C   . GLU   B 2 85  ? -17.250 -10.288 -27.601 1.00 46.40 ? 94  GLU   B C   1 
ATOM   961  O  O   . GLU   B 2 85  ? -18.348 -10.811 -27.415 1.00 46.09 ? 94  GLU   B O   1 
ATOM   962  C  CB  . GLU   B 2 85  ? -15.915 -10.561 -29.799 1.00 50.13 ? 94  GLU   B CB  1 
ATOM   963  C  CG  . GLU   B 2 85  ? -14.551 -11.005 -30.344 1.00 53.03 ? 94  GLU   B CG  1 
ATOM   964  C  CD  . GLU   B 2 85  ? -14.100 -10.369 -31.657 1.00 58.85 ? 94  GLU   B CD  1 
ATOM   965  O  OE1 . GLU   B 2 85  ? -14.946 -9.780  -32.362 1.00 58.62 ? 94  GLU   B OE1 1 
ATOM   966  O  OE2 . GLU   B 2 85  ? -12.891 -10.465 -31.976 1.00 61.30 ? 94  GLU   B OE2 1 
ATOM   967  N  N   . VAL   B 2 86  ? -16.926 -9.133  -27.086 1.00 44.35 ? 95  VAL   B N   1 
ATOM   968  C  CA  . VAL   B 2 86  ? -17.902 -8.283  -26.382 1.00 40.91 ? 95  VAL   B CA  1 
ATOM   969  C  C   . VAL   B 2 86  ? -17.838 -6.908  -27.018 1.00 41.66 ? 95  VAL   B C   1 
ATOM   970  O  O   . VAL   B 2 86  ? -17.032 -6.670  -27.938 1.00 43.71 ? 95  VAL   B O   1 
ATOM   971  C  CB  . VAL   B 2 86  ? -17.452 -8.196  -24.883 1.00 38.70 ? 95  VAL   B CB  1 
ATOM   972  C  CG1 . VAL   B 2 86  ? -17.330 -9.570  -24.254 1.00 39.08 ? 95  VAL   B CG1 1 
ATOM   973  C  CG2 . VAL   B 2 86  ? -16.150 -7.426  -24.753 1.00 39.23 ? 95  VAL   B CG2 1 
ATOM   974  N  N   . GLN   B 2 87  ? -18.722 -5.963  -26.583 1.00 40.02 ? 96  GLN   B N   1 
ATOM   975  C  CA  . GLN   B 2 87  ? -18.647 -4.617  -27.078 1.00 39.97 ? 96  GLN   B CA  1 
ATOM   976  C  C   . GLN   B 2 87  ? -18.525 -3.637  -25.920 1.00 39.72 ? 96  GLN   B C   1 
ATOM   977  O  O   . GLN   B 2 87  ? -19.288 -3.721  -24.969 1.00 39.24 ? 96  GLN   B O   1 
ATOM   978  C  CB  . GLN   B 2 87  ? -19.880 -4.273  -27.944 1.00 40.75 ? 96  GLN   B CB  1 
ATOM   979  C  CG  . GLN   B 2 87  ? -19.745 -4.891  -29.345 1.00 42.67 ? 96  GLN   B CG  1 
ATOM   980  C  CD  . GLN   B 2 87  ? -20.841 -4.487  -30.293 1.00 43.28 ? 96  GLN   B CD  1 
ATOM   981  O  OE1 . GLN   B 2 87  ? -21.748 -3.707  -30.023 1.00 40.93 ? 96  GLN   B OE1 1 
ATOM   982  N  NE2 . GLN   B 2 87  ? -20.740 -5.045  -31.512 1.00 46.84 ? 96  GLN   B NE2 1 
ATOM   983  N  N   . LEU   B 2 88  ? -17.573 -2.715  -26.006 1.00 39.66 ? 97  LEU   B N   1 
ATOM   984  C  CA  . LEU   B 2 88  ? -17.530 -1.589  -25.104 1.00 39.19 ? 97  LEU   B CA  1 
ATOM   985  C  C   . LEU   B 2 88  ? -18.470 -0.517  -25.708 1.00 38.94 ? 97  LEU   B C   1 
ATOM   986  O  O   . LEU   B 2 88  ? -18.335 -0.142  -26.885 1.00 38.84 ? 97  LEU   B O   1 
ATOM   987  C  CB  . LEU   B 2 88  ? -16.103 -1.037  -24.922 1.00 38.55 ? 97  LEU   B CB  1 
ATOM   988  C  CG  . LEU   B 2 88  ? -16.004 0.339   -24.248 1.00 39.66 ? 97  LEU   B CG  1 
ATOM   989  C  CD1 . LEU   B 2 88  ? -16.495 0.235   -22.751 1.00 37.32 ? 97  LEU   B CD1 1 
ATOM   990  C  CD2 . LEU   B 2 88  ? -14.555 0.815   -24.252 1.00 41.02 ? 97  LEU   B CD2 1 
ATOM   991  N  N   . LEU   B 2 89  ? -19.457 -0.050  -24.953 1.00 37.28 ? 98  LEU   B N   1 
ATOM   992  C  CA  . LEU   B 2 89  ? -20.309 1.031   -25.393 1.00 37.02 ? 98  LEU   B CA  1 
ATOM   993  C  C   . LEU   B 2 89  ? -19.673 2.255   -24.806 1.00 37.31 ? 98  LEU   B C   1 
ATOM   994  O  O   . LEU   B 2 89  ? -20.030 2.664   -23.694 1.00 35.09 ? 98  LEU   B O   1 
ATOM   995  C  CB  . LEU   B 2 89  ? -21.757 0.849   -24.939 1.00 38.87 ? 98  LEU   B CB  1 
ATOM   996  C  CG  . LEU   B 2 89  ? -22.782 1.921   -25.347 1.00 42.54 ? 98  LEU   B CG  1 
ATOM   997  C  CD1 . LEU   B 2 89  ? -22.748 2.224   -26.857 1.00 46.84 ? 98  LEU   B CD1 1 
ATOM   998  C  CD2 . LEU   B 2 89  ? -24.164 1.524   -24.861 1.00 43.20 ? 98  LEU   B CD2 1 
ATOM   999  N  N   . ALA   B 2 90  ? -18.605 2.737   -25.466 1.00 37.50 ? 99  ALA   B N   1 
ATOM   1000 C  CA  . ALA   B 2 90  ? -17.819 3.886   -25.032 1.00 37.87 ? 99  ALA   B CA  1 
ATOM   1001 C  C   . ALA   B 2 90  ? -18.615 5.179   -25.151 1.00 38.07 ? 99  ALA   B C   1 
ATOM   1002 O  O   . ALA   B 2 90  ? -19.130 5.498   -26.227 1.00 38.31 ? 99  ALA   B O   1 
ATOM   1003 C  CB  . ALA   B 2 90  ? -16.535 3.987   -25.866 1.00 40.03 ? 99  ALA   B CB  1 
ATOM   1004 N  N   . VAL   B 2 91  ? -18.638 5.981   -24.073 1.00 36.67 ? 100 VAL   B N   1 
ATOM   1005 C  CA  . VAL   B 2 91  ? -19.254 7.301   -24.061 1.00 36.74 ? 100 VAL   B CA  1 
ATOM   1006 C  C   . VAL   B 2 91  ? -18.154 8.324   -23.680 1.00 38.78 ? 100 VAL   B C   1 
ATOM   1007 O  O   . VAL   B 2 91  ? -18.014 8.721   -22.533 1.00 38.04 ? 100 VAL   B O   1 
ATOM   1008 C  CB  . VAL   B 2 91  ? -20.502 7.403   -23.135 1.00 36.75 ? 100 VAL   B CB  1 
ATOM   1009 C  CG1 . VAL   B 2 91  ? -21.171 8.769   -23.283 1.00 37.63 ? 100 VAL   B CG1 1 
ATOM   1010 C  CG2 . VAL   B 2 91  ? -21.519 6.274   -23.387 1.00 36.02 ? 100 VAL   B CG2 1 
ATOM   1011 N  N   . PRO   B 2 92  ? -17.326 8.754   -24.654 1.00 39.94 ? 101 PRO   B N   1 
ATOM   1012 C  CA  . PRO   B 2 92  ? -16.231 9.702   -24.342 1.00 40.44 ? 101 PRO   B CA  1 
ATOM   1013 C  C   . PRO   B 2 92  ? -16.702 11.138  -24.109 1.00 39.57 ? 101 PRO   B C   1 
ATOM   1014 O  O   . PRO   B 2 92  ? -17.715 11.532  -24.680 1.00 39.98 ? 101 PRO   B O   1 
ATOM   1015 C  CB  . PRO   B 2 92  ? -15.362 9.665   -25.620 1.00 43.13 ? 101 PRO   B CB  1 
ATOM   1016 C  CG  . PRO   B 2 92  ? -15.890 8.503   -26.441 1.00 44.39 ? 101 PRO   B CG  1 
ATOM   1017 C  CD  . PRO   B 2 92  ? -17.346 8.409   -26.088 1.00 41.39 ? 101 PRO   B CD  1 
ATOM   1018 N  N   . PRO   B 2 93  ? -15.929 11.945  -23.357 1.00 39.70 ? 102 PRO   B N   1 
ATOM   1019 C  CA  . PRO   B 2 93  ? -16.351 13.342  -23.099 1.00 40.82 ? 102 PRO   B CA  1 
ATOM   1020 C  C   . PRO   B 2 93  ? -16.541 14.160  -24.382 1.00 42.15 ? 102 PRO   B C   1 
ATOM   1021 O  O   . PRO   B 2 93  ? -15.671 14.137  -25.240 1.00 43.47 ? 102 PRO   B O   1 
ATOM   1022 C  CB  . PRO   B 2 93  ? -15.213 13.880  -22.222 1.00 41.58 ? 102 PRO   B CB  1 
ATOM   1023 C  CG  . PRO   B 2 93  ? -14.657 12.636  -21.516 1.00 42.44 ? 102 PRO   B CG  1 
ATOM   1024 C  CD  . PRO   B 2 93  ? -14.712 11.582  -22.587 1.00 41.17 ? 102 PRO   B CD  1 
ATOM   1025 N  N   . GLY   B 2 94  ? -17.695 14.817  -24.529 1.00 42.49 ? 103 GLY   B N   1 
ATOM   1026 C  CA  . GLY   B 2 94  ? -18.032 15.661  -25.682 1.00 43.05 ? 103 GLY   B CA  1 
ATOM   1027 C  C   . GLY   B 2 94  ? -18.245 14.934  -26.993 1.00 44.50 ? 103 GLY   B C   1 
ATOM   1028 O  O   . GLY   B 2 94  ? -18.304 15.574  -28.050 1.00 45.25 ? 103 GLY   B O   1 
ATOM   1029 N  N   . GLU   B 2 95  ? -18.279 13.586  -26.956 1.00 44.40 ? 104 GLU   B N   1 
ATOM   1030 C  CA  . GLU   B 2 95  ? -18.422 12.778  -28.174 1.00 44.65 ? 104 GLU   B CA  1 
ATOM   1031 C  C   . GLU   B 2 95  ? -19.592 11.789  -28.078 1.00 44.13 ? 104 GLU   B C   1 
ATOM   1032 O  O   . GLU   B 2 95  ? -19.955 11.352  -26.987 1.00 42.08 ? 104 GLU   B O   1 
ATOM   1033 C  CB  . GLU   B 2 95  ? -17.090 12.002  -28.488 1.00 45.12 ? 104 GLU   B CB  1 
ATOM   1034 C  CG  . GLU   B 2 95  ? -15.861 12.911  -28.533 1.00 49.37 ? 104 GLU   B CG  1 
ATOM   1035 C  CD  . GLU   B 2 95  ? -14.485 12.282  -28.708 1.00 55.72 ? 104 GLU   B CD  1 
ATOM   1036 O  OE1 . GLU   B 2 95  ? -14.388 11.040  -28.600 1.00 53.18 ? 104 GLU   B OE1 1 
ATOM   1037 O  OE2 . GLU   B 2 95  ? -13.510 13.028  -28.986 1.00 58.80 ? 104 GLU   B OE2 1 
ATOM   1038 N  N   . ARG   B 2 96  ? -20.156 11.402  -29.224 1.00 44.46 ? 105 ARG   B N   1 
ATOM   1039 C  CA  . ARG   B 2 96  ? -21.291 10.471  -29.280 1.00 45.71 ? 105 ARG   B CA  1 
ATOM   1040 C  C   . ARG   B 2 96  ? -20.941 9.075   -28.789 1.00 44.23 ? 105 ARG   B C   1 
ATOM   1041 O  O   . ARG   B 2 96  ? -19.799 8.633   -28.980 1.00 44.02 ? 105 ARG   B O   1 
ATOM   1042 C  CB  . ARG   B 2 96  ? -21.761 10.330  -30.734 1.00 50.93 ? 105 ARG   B CB  1 
ATOM   1043 C  CG  . ARG   B 2 96  ? -23.254 9.980   -30.858 1.00 56.65 ? 105 ARG   B CG  1 
ATOM   1044 C  CD  . ARG   B 2 96  ? -23.892 10.473  -32.152 1.00 61.85 ? 105 ARG   B CD  1 
ATOM   1045 N  NE  . ARG   B 2 96  ? -23.049 10.325  -33.337 1.00 67.92 ? 105 ARG   B NE  1 
ATOM   1046 C  CZ  . ARG   B 2 96  ? -22.661 11.337  -34.112 1.00 73.11 ? 105 ARG   B CZ  1 
ATOM   1047 N  NH1 . ARG   B 2 96  ? -23.014 12.583  -33.816 1.00 72.62 ? 105 ARG   B NH1 1 
ATOM   1048 N  NH2 . ARG   B 2 96  ? -21.920 11.111  -35.189 1.00 74.65 ? 105 ARG   B NH2 1 
ATOM   1049 N  N   . ALA   B 2 97  ? -21.937 8.362   -28.165 1.00 42.48 ? 106 ALA   B N   1 
ATOM   1050 C  CA  . ALA   B 2 97  ? -21.776 6.954   -27.747 1.00 43.35 ? 106 ALA   B CA  1 
ATOM   1051 C  C   . ALA   B 2 97  ? -21.443 6.115   -28.982 1.00 44.31 ? 106 ALA   B C   1 
ATOM   1052 O  O   . ALA   B 2 97  ? -22.072 6.293   -30.044 1.00 45.09 ? 106 ALA   B O   1 
ATOM   1053 C  CB  . ALA   B 2 97  ? -23.058 6.445   -27.116 1.00 44.06 ? 106 ALA   B CB  1 
ATOM   1054 N  N   . LYS   B 2 98  ? -20.462 5.212   -28.842 1.00 44.09 ? 107 LYS   B N   1 
ATOM   1055 C  CA  . LYS   B 2 98  ? -19.956 4.385   -29.939 1.00 46.49 ? 107 LYS   B CA  1 
ATOM   1056 C  C   . LYS   B 2 98  ? -19.634 3.007   -29.429 1.00 45.05 ? 107 LYS   B C   1 
ATOM   1057 O  O   . LYS   B 2 98  ? -19.077 2.865   -28.317 1.00 44.10 ? 107 LYS   B O   1 
ATOM   1058 C  CB  . LYS   B 2 98  ? -18.691 5.073   -30.488 1.00 52.55 ? 107 LYS   B CB  1 
ATOM   1059 C  CG  . LYS   B 2 98  ? -17.900 4.357   -31.569 1.00 62.39 ? 107 LYS   B CG  1 
ATOM   1060 C  CD  . LYS   B 2 98  ? -16.591 5.140   -31.872 1.00 69.42 ? 107 LYS   B CD  1 
ATOM   1061 C  CE  . LYS   B 2 98  ? -15.713 5.379   -30.647 1.00 73.42 ? 107 LYS   B CE  1 
ATOM   1062 N  NZ  . LYS   B 2 98  ? -15.765 6.799   -30.190 1.00 74.31 ? 107 LYS   B NZ  1 
ATOM   1063 N  N   . ASN   B 2 99  ? -20.031 1.969   -30.172 1.00 44.06 ? 108 ASN   B N   1 
ATOM   1064 C  CA  . ASN   B 2 99  ? -19.744 0.577   -29.838 1.00 44.46 ? 108 ASN   B CA  1 
ATOM   1065 C  C   . ASN   B 2 99  ? -18.432 0.112   -30.436 1.00 46.52 ? 108 ASN   B C   1 
ATOM   1066 O  O   . ASN   B 2 99  ? -18.227 0.270   -31.651 1.00 48.29 ? 108 ASN   B O   1 
ATOM   1067 C  CB  . ASN   B 2 99  ? -20.863 -0.380  -30.273 1.00 44.65 ? 108 ASN   B CB  1 
ATOM   1068 C  CG  . ASN   B 2 99  ? -22.210 -0.223  -29.638 1.00 49.27 ? 108 ASN   B CG  1 
ATOM   1069 O  OD1 . ASN   B 2 99  ? -22.887 0.798   -29.812 1.00 52.45 ? 108 ASN   B OD1 1 
ATOM   1070 N  ND2 . ASN   B 2 99  ? -22.666 -1.238  -28.905 1.00 48.34 ? 108 ASN   B ND2 1 
ATOM   1071 N  N   . ILE   B 2 100 ? -17.569 -0.511  -29.632 1.00 46.05 ? 109 ILE   B N   1 
ATOM   1072 C  CA  . ILE   B 2 100 ? -16.289 -1.067  -30.072 1.00 45.77 ? 109 ILE   B CA  1 
ATOM   1073 C  C   . ILE   B 2 100 ? -16.270 -2.522  -29.721 1.00 45.75 ? 109 ILE   B C   1 
ATOM   1074 O  O   . ILE   B 2 100 ? -16.379 -2.866  -28.540 1.00 44.30 ? 109 ILE   B O   1 
ATOM   1075 C  CB  . ILE   B 2 100 ? -15.088 -0.338  -29.460 1.00 48.07 ? 109 ILE   B CB  1 
ATOM   1076 C  CG1 . ILE   B 2 100 ? -15.221 1.188   -29.609 1.00 50.69 ? 109 ILE   B CG1 1 
ATOM   1077 C  CG2 . ILE   B 2 100 ? -13.750 -0.868  -29.976 1.00 48.76 ? 109 ILE   B CG2 1 
ATOM   1078 C  CD1 . ILE   B 2 100 ? -15.015 1.720   -30.970 1.00 53.01 ? 109 ILE   B CD1 1 
ATOM   1079 N  N   . GLN   B 2 101 ? -16.092 -3.407  -30.704 1.00 46.35 ? 110 GLN   B N   1 
ATOM   1080 C  CA  . GLN   B 2 101 ? -16.072 -4.843  -30.478 1.00 46.98 ? 110 GLN   B CA  1 
ATOM   1081 C  C   . GLN   B 2 101 ? -14.648 -5.332  -30.233 1.00 48.65 ? 110 GLN   B C   1 
ATOM   1082 O  O   . GLN   B 2 101 ? -13.723 -4.890  -30.917 1.00 51.23 ? 110 GLN   B O   1 
ATOM   1083 C  CB  . GLN   B 2 101 ? -16.680 -5.555  -31.705 1.00 49.29 ? 110 GLN   B CB  1 
ATOM   1084 C  CG  . GLN   B 2 101 ? -16.947 -7.019  -31.436 1.00 49.68 ? 110 GLN   B CG  1 
ATOM   1085 C  CD  . GLN   B 2 101 ? -17.928 -7.570  -32.440 1.00 52.85 ? 110 GLN   B CD  1 
ATOM   1086 O  OE1 . GLN   B 2 101 ? -18.935 -6.939  -32.793 1.00 52.34 ? 110 GLN   B OE1 1 
ATOM   1087 N  NE2 . GLN   B 2 101 ? -17.632 -8.791  -32.895 1.00 54.92 ? 110 GLN   B NE2 1 
ATOM   1088 N  N   . THR   B 2 102 ? -14.451 -6.267  -29.295 1.00 46.48 ? 111 THR   B N   1 
ATOM   1089 C  CA  . THR   B 2 102 ? -13.121 -6.727  -28.952 1.00 45.17 ? 111 THR   B CA  1 
ATOM   1090 C  C   . THR   B 2 102 ? -13.184 -8.103  -28.317 1.00 45.47 ? 111 THR   B C   1 
ATOM   1091 O  O   . THR   B 2 102 ? -14.220 -8.457  -27.768 1.00 47.04 ? 111 THR   B O   1 
ATOM   1092 C  CB  . THR   B 2 102 ? -12.419 -5.707  -27.997 1.00 45.51 ? 111 THR   B CB  1 
ATOM   1093 O  OG1 . THR   B 2 102 ? -10.999 -5.922  -27.960 1.00 48.15 ? 111 THR   B OG1 1 
ATOM   1094 C  CG2 . THR   B 2 102 ? -12.975 -5.738  -26.551 1.00 44.39 ? 111 THR   B CG2 1 
ATOM   1095 N  N   . LEU   B 2 103 ? -12.088 -8.891  -28.382 1.00 43.84 ? 112 LEU   B N   1 
ATOM   1096 C  CA  . LEU   B 2 103 ? -12.019 -10.149 -27.642 1.00 44.34 ? 112 LEU   B CA  1 
ATOM   1097 C  C   . LEU   B 2 103 ? -11.280 -9.839  -26.357 1.00 44.54 ? 112 LEU   B C   1 
ATOM   1098 O  O   . LEU   B 2 103 ? -10.082 -9.496  -26.363 1.00 45.74 ? 112 LEU   B O   1 
ATOM   1099 C  CB  . LEU   B 2 103 ? -11.255 -11.280 -28.413 1.00 45.97 ? 112 LEU   B CB  1 
ATOM   1100 C  CG  . LEU   B 2 103 ? -11.215 -12.556 -27.573 1.00 48.95 ? 112 LEU   B CG  1 
ATOM   1101 C  CD1 . LEU   B 2 103 ? -12.516 -13.272 -27.645 1.00 49.52 ? 112 LEU   B CD1 1 
ATOM   1102 C  CD2 . LEU   B 2 103 ? -10.069 -13.512 -28.016 1.00 52.33 ? 112 LEU   B CD2 1 
ATOM   1103 N  N   . PRO   B 2 104 ? -11.940 -10.016 -25.168 1.00 43.18 ? 113 PRO   B N   1 
ATOM   1104 C  CA  . PRO   B 2 104 ? -11.245 -9.704  -23.936 1.00 42.18 ? 113 PRO   B CA  1 
ATOM   1105 C  C   . PRO   B 2 104 ? -10.047 -10.599 -23.718 1.00 43.80 ? 113 PRO   B C   1 
ATOM   1106 O  O   . PRO   B 2 104 ? -10.016 -11.741 -24.178 1.00 45.36 ? 113 PRO   B O   1 
ATOM   1107 C  CB  . PRO   B 2 104 ? -12.295 -10.003 -22.834 1.00 41.77 ? 113 PRO   B CB  1 
ATOM   1108 C  CG  . PRO   B 2 104 ? -13.640 -9.822  -23.525 1.00 40.98 ? 113 PRO   B CG  1 
ATOM   1109 C  CD  . PRO   B 2 104 ? -13.333 -10.441 -24.943 1.00 41.65 ? 113 PRO   B CD  1 
ATOM   1110 N  N   . GLY   B 2 105 ? -9.078  -10.058 -23.001 1.00 43.84 ? 114 GLY   B N   1 
ATOM   1111 C  CA  . GLY   B 2 105 ? -7.952  -10.771 -22.409 1.00 44.66 ? 114 GLY   B CA  1 
ATOM   1112 C  C   . GLY   B 2 105 ? -8.348  -11.161 -20.988 1.00 45.28 ? 114 GLY   B C   1 
ATOM   1113 O  O   . GLY   B 2 105 ? -9.541  -11.142 -20.629 1.00 44.79 ? 114 GLY   B O   1 
ATOM   1114 N  N   . ILE   B 2 106 ? -7.363  -11.505 -20.163 1.00 45.47 ? 115 ILE   B N   1 
ATOM   1115 C  CA  . ILE   B 2 106 ? -7.628  -11.964 -18.803 1.00 46.22 ? 115 ILE   B CA  1 
ATOM   1116 C  C   . ILE   B 2 106 ? -6.741  -11.271 -17.793 1.00 45.33 ? 115 ILE   B C   1 
ATOM   1117 O  O   . ILE   B 2 106 ? -5.525  -11.242 -17.980 1.00 46.35 ? 115 ILE   B O   1 
ATOM   1118 C  CB  . ILE   B 2 106 ? -7.259  -13.506 -18.690 1.00 49.43 ? 115 ILE   B CB  1 
ATOM   1119 C  CG1 . ILE   B 2 106 ? -7.985  -14.395 -19.720 1.00 52.96 ? 115 ILE   B CG1 1 
ATOM   1120 C  CG2 . ILE   B 2 106 ? -7.454  -14.050 -17.284 1.00 50.08 ? 115 ILE   B CG2 1 
ATOM   1121 C  CD1 . ILE   B 2 106 ? -9.391  -14.446 -19.567 1.00 55.63 ? 115 ILE   B CD1 1 
ATOM   1122 N  N   . PHE   B 2 107 ? -7.291  -10.915 -16.638 1.00 43.31 ? 116 PHE   B N   1 
ATOM   1123 C  CA  . PHE   B 2 107 ? -6.488  -10.544 -15.477 1.00 43.16 ? 116 PHE   B CA  1 
ATOM   1124 C  C   . PHE   B 2 107 ? -6.458  -11.819 -14.604 1.00 45.27 ? 116 PHE   B C   1 
ATOM   1125 O  O   . PHE   B 2 107 ? -7.506  -12.250 -14.133 1.00 46.04 ? 116 PHE   B O   1 
ATOM   1126 C  CB  . PHE   B 2 107 ? -7.194  -9.427  -14.655 1.00 41.92 ? 116 PHE   B CB  1 
ATOM   1127 C  CG  . PHE   B 2 107 ? -6.952  -7.998  -15.083 1.00 40.80 ? 116 PHE   B CG  1 
ATOM   1128 C  CD1 . PHE   B 2 107 ? -6.205  -7.709  -16.218 1.00 41.39 ? 116 PHE   B CD1 1 
ATOM   1129 C  CD2 . PHE   B 2 107 ? -7.477  -6.944  -14.353 1.00 40.18 ? 116 PHE   B CD2 1 
ATOM   1130 C  CE1 . PHE   B 2 107 ? -6.028  -6.399  -16.642 1.00 41.91 ? 116 PHE   B CE1 1 
ATOM   1131 C  CE2 . PHE   B 2 107 ? -7.296  -5.634  -14.772 1.00 40.75 ? 116 PHE   B CE2 1 
ATOM   1132 C  CZ  . PHE   B 2 107 ? -6.554  -5.364  -15.903 1.00 41.69 ? 116 PHE   B CZ  1 
ATOM   1133 N  N   . LYS   B 2 108 ? -5.258  -12.408 -14.325 1.00 45.38 ? 117 LYS   B N   1 
ATOM   1134 C  CA  . LYS   B 2 108 ? -5.143  -13.565 -13.449 1.00 46.29 ? 117 LYS   B CA  1 
ATOM   1135 C  C   . LYS   B 2 108 ? -4.757  -13.059 -12.072 1.00 46.06 ? 117 LYS   B C   1 
ATOM   1136 O  O   . LYS   B 2 108 ? -3.779  -12.326 -11.955 1.00 46.63 ? 117 LYS   B O   1 
ATOM   1137 C  CB  . LYS   B 2 108 ? -4.048  -14.535 -13.978 1.00 49.78 ? 117 LYS   B CB  1 
ATOM   1138 C  CG  . LYS   B 2 108 ? -4.408  -15.051 -15.357 1.00 57.91 ? 117 LYS   B CG  1 
ATOM   1139 C  CD  . LYS   B 2 108 ? -3.274  -15.809 -16.049 1.00 65.37 ? 117 LYS   B CD  1 
ATOM   1140 C  CE  . LYS   B 2 108 ? -3.050  -17.157 -15.410 1.00 72.24 ? 117 LYS   B CE  1 
ATOM   1141 N  NZ  . LYS   B 2 108 ? -2.181  -18.034 -16.253 1.00 75.28 ? 117 LYS   B NZ  1 
ATOM   1142 N  N   . THR   B 2 109 ? -5.561  -13.352 -11.061 1.00 45.55 ? 118 THR   B N   1 
ATOM   1143 C  CA  . THR   B 2 109 ? -5.251  -12.888 -9.708  1.00 46.74 ? 118 THR   B CA  1 
ATOM   1144 C  C   . THR   B 2 109 ? -5.175  -14.072 -8.746  1.00 48.84 ? 118 THR   B C   1 
ATOM   1145 O  O   . THR   B 2 109 ? -5.619  -15.171 -9.095  1.00 50.25 ? 118 THR   B O   1 
ATOM   1146 C  CB  . THR   B 2 109 ? -6.280  -11.800 -9.220  1.00 46.05 ? 118 THR   B CB  1 
ATOM   1147 O  OG1 . THR   B 2 109 ? -7.443  -12.435 -8.696  1.00 45.87 ? 118 THR   B OG1 1 
ATOM   1148 C  CG2 . THR   B 2 109 ? -6.653  -10.794 -10.294 1.00 44.62 ? 118 THR   B CG2 1 
ATOM   1149 N  N   . LYS   B 2 110 ? -4.700  -13.833 -7.521  1.00 49.24 ? 119 LYS   B N   1 
ATOM   1150 C  CA  . LYS   B 2 110 ? -4.633  -14.883 -6.500  1.00 50.02 ? 119 LYS   B CA  1 
ATOM   1151 C  C   . LYS   B 2 110 ? -6.036  -15.410 -6.110  1.00 51.92 ? 119 LYS   B C   1 
ATOM   1152 O  O   . LYS   B 2 110 ? -6.148  -16.509 -5.546  1.00 53.36 ? 119 LYS   B O   1 
ATOM   1153 C  CB  . LYS   B 2 110 ? -3.906  -14.354 -5.262  1.00 49.79 ? 119 LYS   B CB  1 
ATOM   1154 C  CG  . LYS   B 2 110 ? -4.678  -13.261 -4.526  1.00 52.32 ? 119 LYS   B CG  1 
ATOM   1155 C  CD  . LYS   B 2 110 ? -4.007  -12.941 -3.200  1.00 55.98 ? 119 LYS   B CD  1 
ATOM   1156 C  CE  . LYS   B 2 110 ? -5.006  -12.768 -2.086  1.00 60.60 ? 119 LYS   B CE  1 
ATOM   1157 N  NZ  . LYS   B 2 110 ? -5.657  -11.442 -2.145  1.00 65.13 ? 119 LYS   B NZ  1 
ATOM   1158 N  N   . ASP   B 2 111 ? -7.082  -14.614 -6.375  1.00 51.04 ? 120 ASP   B N   1 
ATOM   1159 C  CA  . ASP   B 2 111 ? -8.467  -14.922 -6.072  1.00 52.01 ? 120 ASP   B CA  1 
ATOM   1160 C  C   . ASP   B 2 111 ? -9.309  -15.292 -7.294  1.00 52.14 ? 120 ASP   B C   1 
ATOM   1161 O  O   . ASP   B 2 111 ? -10.535 -15.296 -7.200  1.00 53.12 ? 120 ASP   B O   1 
ATOM   1162 C  CB  . ASP   B 2 111 ? -9.103  -13.747 -5.325  1.00 53.42 ? 120 ASP   B CB  1 
ATOM   1163 C  CG  . ASP   B 2 111 ? -8.422  -13.510 -3.994  1.00 58.02 ? 120 ASP   B CG  1 
ATOM   1164 O  OD1 . ASP   B 2 111 ? -8.134  -14.508 -3.286  1.00 58.94 ? 120 ASP   B OD1 1 
ATOM   1165 O  OD2 . ASP   B 2 111 ? -8.151  -12.339 -3.671  1.00 59.34 ? 120 ASP   B OD2 1 
ATOM   1166 N  N   . GLY   B 2 112 ? -8.669  -15.609 -8.415  1.00 50.90 ? 121 GLY   B N   1 
ATOM   1167 C  CA  . GLY   B 2 112 ? -9.387  -15.972 -9.619  1.00 50.59 ? 121 GLY   B CA  1 
ATOM   1168 C  C   . GLY   B 2 112 ? -9.135  -15.023 -10.776 1.00 50.29 ? 121 GLY   B C   1 
ATOM   1169 O  O   . GLY   B 2 112 ? -8.491  -13.975 -10.628 1.00 50.75 ? 121 GLY   B O   1 
ATOM   1170 N  N   . ASP   B 2 113 ? -9.638  -15.405 -11.936 1.00 48.27 ? 122 ASP   B N   1 
ATOM   1171 C  CA  . ASP   B 2 113 ? -9.452  -14.676 -13.181 1.00 47.43 ? 122 ASP   B CA  1 
ATOM   1172 C  C   . ASP   B 2 113 ? -10.652 -13.782 -13.535 1.00 46.65 ? 122 ASP   B C   1 
ATOM   1173 O  O   . ASP   B 2 113 ? -11.785 -14.134 -13.260 1.00 47.57 ? 122 ASP   B O   1 
ATOM   1174 C  CB  . ASP   B 2 113 ? -9.140  -15.662 -14.324 1.00 49.77 ? 122 ASP   B CB  1 
ATOM   1175 C  CG  . ASP   B 2 113 ? -7.839  -16.445 -14.123 1.00 57.39 ? 122 ASP   B CG  1 
ATOM   1176 O  OD1 . ASP   B 2 113 ? -7.294  -16.423 -12.997 1.00 59.51 ? 122 ASP   B OD1 1 
ATOM   1177 O  OD2 . ASP   B 2 113 ? -7.376  -17.080 -15.087 1.00 62.67 ? 122 ASP   B OD2 1 
ATOM   1178 N  N   . ILE   B 2 114 ? -10.377 -12.636 -14.161 1.00 44.21 ? 123 ILE   B N   1 
ATOM   1179 C  CA  . ILE   B 2 114 ? -11.391 -11.659 -14.562 1.00 44.48 ? 123 ILE   B CA  1 
ATOM   1180 C  C   . ILE   B 2 114 ? -11.125 -11.315 -16.039 1.00 42.85 ? 123 ILE   B C   1 
ATOM   1181 O  O   . ILE   B 2 114 ? -9.967  -11.222 -16.431 1.00 41.80 ? 123 ILE   B O   1 
ATOM   1182 C  CB  . ILE   B 2 114 ? -11.214 -10.373 -13.666 1.00 45.90 ? 123 ILE   B CB  1 
ATOM   1183 C  CG1 . ILE   B 2 114 ? -11.140 -10.717 -12.149 1.00 49.83 ? 123 ILE   B CG1 1 
ATOM   1184 C  CG2 . ILE   B 2 114 ? -12.302 -9.330  -13.938 1.00 47.76 ? 123 ILE   B CG2 1 
ATOM   1185 C  CD1 . ILE   B 2 114 ? -10.531 -9.585  -11.249 1.00 52.44 ? 123 ILE   B CD1 1 
ATOM   1186 N  N   . GLY   B 2 115 ? -12.169 -11.069 -16.841 1.00 42.05 ? 124 GLY   B N   1 
ATOM   1187 C  CA  . GLY   B 2 115 ? -11.967 -10.605 -18.210 1.00 41.01 ? 124 GLY   B CA  1 
ATOM   1188 C  C   . GLY   B 2 115 ? -11.389 -9.195  -18.188 1.00 39.37 ? 124 GLY   B C   1 
ATOM   1189 O  O   . GLY   B 2 115 ? -11.498 -8.479  -17.184 1.00 38.02 ? 124 GLY   B O   1 
ATOM   1190 N  N   . ALA   B 2 116 ? -10.709 -8.803  -19.252 1.00 39.22 ? 125 ALA   B N   1 
ATOM   1191 C  CA  . ALA   B 2 116 ? -10.106 -7.485  -19.339 1.00 40.49 ? 125 ALA   B CA  1 
ATOM   1192 C  C   . ALA   B 2 116 ? -10.161 -6.998  -20.782 1.00 41.97 ? 125 ALA   B C   1 
ATOM   1193 O  O   . ALA   B 2 116 ? -9.961  -7.799  -21.694 1.00 43.91 ? 125 ALA   B O   1 
ATOM   1194 C  CB  . ALA   B 2 116 ? -8.671  -7.542  -18.863 1.00 41.69 ? 125 ALA   B CB  1 
ATOM   1195 N  N   A VAL   B 2 117 ? -10.409 -5.703  -20.997 0.50 40.95 ? 126 VAL   B N   1 
ATOM   1196 N  N   C VAL   B 2 117 ? -10.409 -5.703  -20.997 0.50 40.95 ? 126 VAL   B N   1 
ATOM   1197 C  CA  A VAL   B 2 117 ? -10.484 -5.152  -22.354 0.50 42.74 ? 126 VAL   B CA  1 
ATOM   1198 C  CA  C VAL   B 2 117 ? -10.484 -5.152  -22.354 0.50 42.74 ? 126 VAL   B CA  1 
ATOM   1199 C  C   A VAL   B 2 117 ? -9.357  -4.149  -22.628 0.50 43.82 ? 126 VAL   B C   1 
ATOM   1200 C  C   C VAL   B 2 117 ? -9.357  -4.149  -22.628 0.50 43.82 ? 126 VAL   B C   1 
ATOM   1201 O  O   A VAL   B 2 117 ? -9.127  -3.223  -21.853 0.50 43.30 ? 126 VAL   B O   1 
ATOM   1202 O  O   C VAL   B 2 117 ? -9.127  -3.223  -21.853 0.50 43.30 ? 126 VAL   B O   1 
ATOM   1203 C  CB  A VAL   B 2 117 ? -11.875 -4.596  -22.705 0.50 44.50 ? 126 VAL   B CB  1 
ATOM   1204 C  CB  C VAL   B 2 117 ? -11.875 -4.596  -22.705 0.50 44.50 ? 126 VAL   B CB  1 
ATOM   1205 C  CG1 A VAL   B 2 117 ? -12.927 -5.694  -22.603 0.50 45.66 ? 126 VAL   B CG1 1 
ATOM   1206 C  CG1 C VAL   B 2 117 ? -12.927 -5.694  -22.603 0.50 45.66 ? 126 VAL   B CG1 1 
ATOM   1207 C  CG2 A VAL   B 2 117 ? -12.249 -3.402  -21.827 0.50 45.52 ? 126 VAL   B CG2 1 
ATOM   1208 C  CG2 C VAL   B 2 117 ? -12.249 -3.402  -21.827 0.50 45.52 ? 126 VAL   B CG2 1 
ATOM   1209 N  N   . ALA   B 2 118 ? -8.607  -4.376  -23.728 1.00 44.02 ? 127 ALA   B N   1 
ATOM   1210 C  CA  . ALA   B 2 118 ? -7.466  -3.536  -24.042 1.00 46.61 ? 127 ALA   B CA  1 
ATOM   1211 C  C   . ALA   B 2 118 ? -7.813  -2.426  -25.006 1.00 48.30 ? 127 ALA   B C   1 
ATOM   1212 O  O   . ALA   B 2 118 ? -7.515  -2.485  -26.208 1.00 49.03 ? 127 ALA   B O   1 
ATOM   1213 C  CB  . ALA   B 2 118 ? -6.297  -4.394  -24.532 1.00 48.18 ? 127 ALA   B CB  1 
ATOM   1214 N  N   . LEU   B 2 119 ? -8.534  -1.417  -24.483 1.00 47.74 ? 128 LEU   B N   1 
ATOM   1215 C  CA  . LEU   B 2 119 ? -9.016  -0.263  -25.221 1.00 48.33 ? 128 LEU   B CA  1 
ATOM   1216 C  C   . LEU   B 2 119 ? -8.703  0.989   -24.399 1.00 50.42 ? 128 LEU   B C   1 
ATOM   1217 O  O   . LEU   B 2 119 ? -8.938  0.998   -23.180 1.00 49.38 ? 128 LEU   B O   1 
ATOM   1218 C  CB  . LEU   B 2 119 ? -10.534 -0.390  -25.467 1.00 48.18 ? 128 LEU   B CB  1 
ATOM   1219 C  CG  . LEU   B 2 119 ? -10.951 -1.583  -26.341 1.00 49.76 ? 128 LEU   B CG  1 
ATOM   1220 C  CD1 . LEU   B 2 119 ? -12.435 -1.844  -26.289 1.00 49.83 ? 128 LEU   B CD1 1 
ATOM   1221 C  CD2 . LEU   B 2 119 ? -10.517 -1.379  -27.778 1.00 50.92 ? 128 LEU   B CD2 1 
ATOM   1222 N  N   . ASP   B 2 120 ? -8.189  2.036   -25.057 1.00 51.57 ? 129 ASP   B N   1 
ATOM   1223 C  CA  . ASP   B 2 120 ? -7.739  3.253   -24.384 1.00 53.11 ? 129 ASP   B CA  1 
ATOM   1224 C  C   . ASP   B 2 120 ? -8.611  4.471   -24.676 1.00 51.70 ? 129 ASP   B C   1 
ATOM   1225 O  O   . ASP   B 2 120 ? -8.568  5.035   -25.774 1.00 51.74 ? 129 ASP   B O   1 
ATOM   1226 C  CB  . ASP   B 2 120 ? -6.255  3.535   -24.761 1.00 58.05 ? 129 ASP   B CB  1 
ATOM   1227 C  CG  . ASP   B 2 120 ? -5.474  4.323   -23.720 1.00 64.97 ? 129 ASP   B CG  1 
ATOM   1228 O  OD1 . ASP   B 2 120 ? -6.078  5.210   -23.064 1.00 66.68 ? 129 ASP   B OD1 1 
ATOM   1229 O  OD2 . ASP   B 2 120 ? -4.264  4.055   -23.560 1.00 67.70 ? 129 ASP   B OD2 1 
ATOM   1230 N  N   . TYR   B 2 121 ? -9.384  4.912   -23.660 1.00 48.87 ? 130 TYR   B N   1 
ATOM   1231 C  CA  . TYR   B 2 121 ? -10.238 6.083   -23.780 1.00 48.55 ? 130 TYR   B CA  1 
ATOM   1232 C  C   . TYR   B 2 121 ? -9.918  7.120   -22.674 1.00 47.12 ? 130 TYR   B C   1 
ATOM   1233 O  O   . TYR   B 2 121 ? -9.322  6.751   -21.661 1.00 47.48 ? 130 TYR   B O   1 
ATOM   1234 C  CB  . TYR   B 2 121 ? -11.732 5.655   -23.720 1.00 49.75 ? 130 TYR   B CB  1 
ATOM   1235 C  CG  . TYR   B 2 121 ? -12.232 5.091   -25.031 1.00 51.22 ? 130 TYR   B CG  1 
ATOM   1236 C  CD1 . TYR   B 2 121 ? -12.659 5.929   -26.054 1.00 52.78 ? 130 TYR   B CD1 1 
ATOM   1237 C  CD2 . TYR   B 2 121 ? -12.248 3.724   -25.262 1.00 52.47 ? 130 TYR   B CD2 1 
ATOM   1238 C  CE1 . TYR   B 2 121 ? -13.082 5.417   -27.272 1.00 54.83 ? 130 TYR   B CE1 1 
ATOM   1239 C  CE2 . TYR   B 2 121 ? -12.695 3.200   -26.461 1.00 54.00 ? 130 TYR   B CE2 1 
ATOM   1240 C  CZ  . TYR   B 2 121 ? -13.081 4.052   -27.479 1.00 56.24 ? 130 TYR   B CZ  1 
ATOM   1241 O  OH  . TYR   B 2 121 ? -13.483 3.548   -28.686 1.00 59.79 ? 130 TYR   B OH  1 
ATOM   1242 N  N   . PRO   B 2 122 ? -10.355 8.398   -22.812 1.00 46.63 ? 131 PRO   B N   1 
ATOM   1243 C  CA  . PRO   B 2 122 ? -10.099 9.389   -21.746 1.00 45.62 ? 131 PRO   B CA  1 
ATOM   1244 C  C   . PRO   B 2 122 ? -10.661 8.942   -20.391 1.00 44.46 ? 131 PRO   B C   1 
ATOM   1245 O  O   . PRO   B 2 122 ? -11.609 8.168   -20.382 1.00 43.35 ? 131 PRO   B O   1 
ATOM   1246 C  CB  . PRO   B 2 122 ? -10.852 10.616  -22.239 1.00 47.25 ? 131 PRO   B CB  1 
ATOM   1247 C  CG  . PRO   B 2 122 ? -10.863 10.466  -23.716 1.00 47.38 ? 131 PRO   B CG  1 
ATOM   1248 C  CD  . PRO   B 2 122 ? -11.018 9.019   -23.980 1.00 45.47 ? 131 PRO   B CD  1 
ATOM   1249 N  N   . ALA   B 2 123 ? -10.051 9.380   -19.261 1.00 43.51 ? 132 ALA   B N   1 
ATOM   1250 C  CA  . ALA   B 2 123 ? -10.496 9.013   -17.900 1.00 43.50 ? 132 ALA   B CA  1 
ATOM   1251 C  C   . ALA   B 2 123 ? -12.027 9.216   -17.694 1.00 40.79 ? 132 ALA   B C   1 
ATOM   1252 O  O   . ALA   B 2 123 ? -12.680 8.406   -16.992 1.00 39.78 ? 132 ALA   B O   1 
ATOM   1253 C  CB  . ALA   B 2 123 ? -9.710  9.819   -16.863 1.00 43.98 ? 132 ALA   B CB  1 
ATOM   1254 N  N   . GLY   B 2 124 ? -12.577 10.244  -18.331 1.00 39.84 ? 133 GLY   B N   1 
ATOM   1255 C  CA  . GLY   B 2 124 ? -14.004 10.553  -18.239 1.00 39.02 ? 133 GLY   B CA  1 
ATOM   1256 C  C   . GLY   B 2 124 ? -14.931 9.520   -18.866 1.00 35.61 ? 133 GLY   B C   1 
ATOM   1257 O  O   . GLY   B 2 124 ? -16.158 9.667   -18.811 1.00 35.42 ? 133 GLY   B O   1 
ATOM   1258 N  N   . THR   B 2 125 ? -14.355 8.495   -19.502 1.00 32.98 ? 134 THR   B N   1 
ATOM   1259 C  CA  . THR   B 2 125 ? -15.120 7.395   -20.100 1.00 33.72 ? 134 THR   B CA  1 
ATOM   1260 C  C   . THR   B 2 125 ? -15.367 6.262   -19.057 1.00 34.15 ? 134 THR   B C   1 
ATOM   1261 O  O   . THR   B 2 125 ? -16.158 5.346   -19.287 1.00 34.37 ? 134 THR   B O   1 
ATOM   1262 C  CB  . THR   B 2 125 ? -14.400 6.879   -21.360 1.00 37.29 ? 134 THR   B CB  1 
ATOM   1263 O  OG1 . THR   B 2 125 ? -13.974 8.010   -22.152 1.00 37.18 ? 134 THR   B OG1 1 
ATOM   1264 C  CG2 . THR   B 2 125 ? -15.279 6.013   -22.237 1.00 39.38 ? 134 THR   B CG2 1 
ATOM   1265 N  N   . SER   B 2 126 ? -14.725 6.366   -17.889 1.00 32.69 ? 135 SER   B N   1 
ATOM   1266 C  CA  . SER   B 2 126 ? -14.924 5.364   -16.805 1.00 32.61 ? 135 SER   B CA  1 
ATOM   1267 C  C   . SER   B 2 126 ? -16.391 5.168   -16.458 1.00 30.94 ? 135 SER   B C   1 
ATOM   1268 O  O   . SER   B 2 126 ? -17.103 6.172   -16.301 1.00 31.51 ? 135 SER   B O   1 
ATOM   1269 C  CB  . SER   B 2 126 ? -14.196 5.831   -15.552 1.00 35.25 ? 135 SER   B CB  1 
ATOM   1270 O  OG  . SER   B 2 126 ? -12.792 5.743   -15.734 1.00 39.23 ? 135 SER   B OG  1 
ATOM   1271 N  N   . GLY   B 2 127 ? -16.822 3.913   -16.297 1.00 28.96 ? 136 GLY   B N   1 
ATOM   1272 C  CA  . GLY   B 2 127 ? -18.228 3.585   -16.048 1.00 30.50 ? 136 GLY   B CA  1 
ATOM   1273 C  C   . GLY   B 2 127 ? -18.963 3.179   -17.322 1.00 31.11 ? 136 GLY   B C   1 
ATOM   1274 O  O   . GLY   B 2 127 ? -20.114 2.735   -17.262 1.00 30.12 ? 136 GLY   B O   1 
ATOM   1275 N  N   . SER   B 2 128 ? -18.278 3.305   -18.514 1.00 30.95 ? 137 SER   B N   1 
ATOM   1276 C  CA  . SER   B 2 128 ? -18.959 2.890   -19.754 1.00 30.90 ? 137 SER   B CA  1 
ATOM   1277 C  C   . SER   B 2 128 ? -19.219 1.364   -19.682 1.00 31.75 ? 137 SER   B C   1 
ATOM   1278 O  O   . SER   B 2 128 ? -18.370 0.603   -19.216 1.00 32.10 ? 137 SER   B O   1 
ATOM   1279 C  CB  . SER   B 2 128 ? -18.116 3.187   -21.024 1.00 32.14 ? 137 SER   B CB  1 
ATOM   1280 O  OG  . SER   B 2 128 ? -18.095 4.594   -21.208 1.00 34.22 ? 137 SER   B OG  1 
ATOM   1281 N  N   . PRO   B 2 129 ? -20.413 0.921   -20.132 1.00 32.14 ? 138 PRO   B N   1 
ATOM   1282 C  CA  . PRO   B 2 129 ? -20.717 -0.507  -20.044 1.00 31.54 ? 138 PRO   B CA  1 
ATOM   1283 C  C   . PRO   B 2 129 ? -20.092 -1.387  -21.099 1.00 33.00 ? 138 PRO   B C   1 
ATOM   1284 O  O   . PRO   B 2 129 ? -19.965 -0.961  -22.243 1.00 34.00 ? 138 PRO   B O   1 
ATOM   1285 C  CB  . PRO   B 2 129 ? -22.227 -0.563  -20.196 1.00 33.79 ? 138 PRO   B CB  1 
ATOM   1286 C  CG  . PRO   B 2 129 ? -22.587 0.662   -21.012 1.00 33.58 ? 138 PRO   B CG  1 
ATOM   1287 C  CD  . PRO   B 2 129 ? -21.560 1.711   -20.645 1.00 33.01 ? 138 PRO   B CD  1 
ATOM   1288 N  N   . ILE   B 2 130 ? -19.764 -2.608  -20.709 1.00 32.47 ? 139 ILE   B N   1 
ATOM   1289 C  CA  . ILE   B 2 130 ? -19.256 -3.648  -21.640 1.00 34.20 ? 139 ILE   B CA  1 
ATOM   1290 C  C   . ILE   B 2 130 ? -20.438 -4.629  -21.763 1.00 34.33 ? 139 ILE   B C   1 
ATOM   1291 O  O   . ILE   B 2 130 ? -21.030 -4.994  -20.758 1.00 33.44 ? 139 ILE   B O   1 
ATOM   1292 C  CB  . ILE   B 2 130 ? -18.020 -4.326  -21.013 1.00 35.70 ? 139 ILE   B CB  1 
ATOM   1293 C  CG1 . ILE   B 2 130 ? -16.909 -3.269  -20.852 1.00 39.75 ? 139 ILE   B CG1 1 
ATOM   1294 C  CG2 . ILE   B 2 130 ? -17.517 -5.463  -21.924 1.00 35.67 ? 139 ILE   B CG2 1 
ATOM   1295 C  CD1 . ILE   B 2 130 ? -15.819 -3.618  -19.885 1.00 41.79 ? 139 ILE   B CD1 1 
ATOM   1296 N  N   . LEU   B 2 131 ? -20.834 -4.994  -22.993 1.00 35.93 ? 140 LEU   B N   1 
ATOM   1297 C  CA  . LEU   B 2 131 ? -22.020 -5.817  -23.252 1.00 38.17 ? 140 LEU   B CA  1 
ATOM   1298 C  C   . LEU   B 2 131 ? -21.702 -7.151  -23.958 1.00 39.45 ? 140 LEU   B C   1 
ATOM   1299 O  O   . LEU   B 2 131 ? -20.722 -7.265  -24.694 1.00 41.03 ? 140 LEU   B O   1 
ATOM   1300 C  CB  . LEU   B 2 131 ? -22.971 -5.078  -24.253 1.00 40.65 ? 140 LEU   B CB  1 
ATOM   1301 C  CG  . LEU   B 2 131 ? -22.976 -3.562  -24.252 1.00 43.60 ? 140 LEU   B CG  1 
ATOM   1302 C  CD1 . LEU   B 2 131 ? -23.866 -3.044  -25.371 1.00 45.55 ? 140 LEU   B CD1 1 
ATOM   1303 C  CD2 . LEU   B 2 131 ? -23.392 -3.036  -22.888 1.00 44.69 ? 140 LEU   B CD2 1 
ATOM   1304 N  N   . ASP   B 2 132 ? -22.569 -8.138  -23.740 1.00 39.30 ? 141 ASP   B N   1 
ATOM   1305 C  CA  . ASP   B 2 132 ? -22.498 -9.384  -24.498 1.00 41.01 ? 141 ASP   B CA  1 
ATOM   1306 C  C   . ASP   B 2 132 ? -23.411 -9.274  -25.737 1.00 43.17 ? 141 ASP   B C   1 
ATOM   1307 O  O   . ASP   B 2 132 ? -24.099 -8.274  -25.910 1.00 43.26 ? 141 ASP   B O   1 
ATOM   1308 C  CB  . ASP   B 2 132 ? -22.858 -10.609 -23.658 1.00 42.18 ? 141 ASP   B CB  1 
ATOM   1309 C  CG  . ASP   B 2 132 ? -24.258 -10.633 -23.072 1.00 43.19 ? 141 ASP   B CG  1 
ATOM   1310 O  OD1 . ASP   B 2 132 ? -25.157 -9.940  -23.617 1.00 44.86 ? 141 ASP   B OD1 1 
ATOM   1311 O  OD2 . ASP   B 2 132 ? -24.474 -11.383 -22.113 1.00 44.39 ? 141 ASP   B OD2 1 
ATOM   1312 N  N   . LYS   B 2 133 ? -23.485 -10.369 -26.555 1.00 45.79 ? 142 LYS   B N   1 
ATOM   1313 C  CA  . LYS   B 2 133 ? -24.280 -10.351 -27.798 1.00 47.76 ? 142 LYS   B CA  1 
ATOM   1314 C  C   . LYS   B 2 133 ? -25.794 -10.212 -27.625 1.00 49.18 ? 142 LYS   B C   1 
ATOM   1315 O  O   . LYS   B 2 133 ? -26.514 -9.855  -28.610 1.00 50.10 ? 142 LYS   B O   1 
ATOM   1316 C  CB  . LYS   B 2 133 ? -23.932 -11.617 -28.633 1.00 50.96 ? 142 LYS   B CB  1 
ATOM   1317 C  CG  . LYS   B 2 133 ? -22.476 -11.609 -29.020 1.00 57.45 ? 142 LYS   B CG  1 
ATOM   1318 C  CD  . LYS   B 2 133 ? -22.067 -12.816 -29.911 1.00 64.68 ? 142 LYS   B CD  1 
ATOM   1319 C  CE  . LYS   B 2 133 ? -20.570 -13.029 -29.861 1.00 70.65 ? 142 LYS   B CE  1 
ATOM   1320 N  NZ  . LYS   B 2 133 ? -20.169 -14.420 -30.268 1.00 75.52 ? 142 LYS   B NZ  1 
ATOM   1321 N  N   . CYS   B 2 134 ? -26.298 -10.445 -26.385 1.00 49.33 ? 143 CYS   B N   1 
ATOM   1322 C  CA  . CYS   B 2 134 ? -27.713 -10.201 -26.045 1.00 49.89 ? 143 CYS   B CA  1 
ATOM   1323 C  C   . CYS   B 2 134 ? -27.978 -8.778  -25.545 1.00 49.27 ? 143 CYS   B C   1 
ATOM   1324 O  O   . CYS   B 2 134 ? -29.114 -8.469  -25.165 1.00 50.67 ? 143 CYS   B O   1 
ATOM   1325 C  CB  . CYS   B 2 134 ? -28.246 -11.220 -25.047 1.00 52.67 ? 143 CYS   B CB  1 
ATOM   1326 S  SG  . CYS   B 2 134 ? -28.138 -12.935 -25.610 1.00 61.07 ? 143 CYS   B SG  1 
ATOM   1327 N  N   . GLY   B 2 135 ? -26.952 -7.932  -25.517 1.00 47.33 ? 144 GLY   B N   1 
ATOM   1328 C  CA  . GLY   B 2 135 ? -27.092 -6.558  -25.048 1.00 44.64 ? 144 GLY   B CA  1 
ATOM   1329 C  C   . GLY   B 2 135 ? -27.066 -6.437  -23.532 1.00 43.24 ? 144 GLY   B C   1 
ATOM   1330 O  O   . GLY   B 2 135 ? -27.340 -5.364  -23.000 1.00 43.08 ? 144 GLY   B O   1 
ATOM   1331 N  N   . ARG   B 2 136 ? -26.700 -7.515  -22.818 1.00 40.31 ? 145 ARG   B N   1 
ATOM   1332 C  CA  . ARG   B 2 136 ? -26.642 -7.473  -21.341 1.00 39.72 ? 145 ARG   B CA  1 
ATOM   1333 C  C   . ARG   B 2 136 ? -25.323 -6.885  -20.873 1.00 36.92 ? 145 ARG   B C   1 
ATOM   1334 O  O   . ARG   B 2 136 ? -24.275 -7.203  -21.422 1.00 35.97 ? 145 ARG   B O   1 
ATOM   1335 C  CB  . ARG   B 2 136 ? -26.835 -8.883  -20.754 1.00 43.05 ? 145 ARG   B CB  1 
ATOM   1336 C  CG  . ARG   B 2 136 ? -28.245 -9.451  -20.996 1.00 48.92 ? 145 ARG   B CG  1 
ATOM   1337 C  CD  . ARG   B 2 136 ? -28.357 -10.851 -20.407 1.00 55.86 ? 145 ARG   B CD  1 
ATOM   1338 N  NE  . ARG   B 2 136 ? -27.585 -11.812 -21.190 1.00 63.04 ? 145 ARG   B NE  1 
ATOM   1339 C  CZ  . ARG   B 2 136 ? -27.272 -13.041 -20.793 1.00 68.82 ? 145 ARG   B CZ  1 
ATOM   1340 N  NH1 . ARG   B 2 136 ? -27.600 -13.459 -19.573 1.00 69.02 ? 145 ARG   B NH1 1 
ATOM   1341 N  NH2 . ARG   B 2 136 ? -26.589 -13.850 -21.597 1.00 70.03 ? 145 ARG   B NH2 1 
ATOM   1342 N  N   . VAL   B 2 137 ? -25.365 -6.083  -19.769 1.00 33.42 ? 146 VAL   B N   1 
ATOM   1343 C  CA  . VAL   B 2 137 ? -24.152 -5.467  -19.286 1.00 31.77 ? 146 VAL   B CA  1 
ATOM   1344 C  C   . VAL   B 2 137 ? -23.386 -6.465  -18.438 1.00 32.09 ? 146 VAL   B C   1 
ATOM   1345 O  O   . VAL   B 2 137 ? -23.905 -6.904  -17.432 1.00 32.15 ? 146 VAL   B O   1 
ATOM   1346 C  CB  . VAL   B 2 137 ? -24.488 -4.175  -18.488 1.00 32.29 ? 146 VAL   B CB  1 
ATOM   1347 C  CG1 . VAL   B 2 137 ? -23.221 -3.590  -17.842 1.00 32.63 ? 146 VAL   B CG1 1 
ATOM   1348 C  CG2 . VAL   B 2 137 ? -25.188 -3.138  -19.394 1.00 33.40 ? 146 VAL   B CG2 1 
ATOM   1349 N  N   . ILE   B 2 138 ? -22.213 -6.870  -18.888 1.00 32.90 ? 147 ILE   B N   1 
ATOM   1350 C  CA  . ILE   B 2 138 ? -21.372 -7.837  -18.168 1.00 32.25 ? 147 ILE   B CA  1 
ATOM   1351 C  C   . ILE   B 2 138 ? -20.348 -7.191  -17.229 1.00 31.48 ? 147 ILE   B C   1 
ATOM   1352 O  O   . ILE   B 2 138 ? -19.589 -7.928  -16.555 1.00 32.11 ? 147 ILE   B O   1 
ATOM   1353 C  CB  . ILE   B 2 138 ? -20.678 -8.854  -19.147 1.00 34.03 ? 147 ILE   B CB  1 
ATOM   1354 C  CG1 . ILE   B 2 138 ? -19.943 -8.086  -20.243 1.00 35.82 ? 147 ILE   B CG1 1 
ATOM   1355 C  CG2 . ILE   B 2 138 ? -21.752 -9.693  -19.779 1.00 34.17 ? 147 ILE   B CG2 1 
ATOM   1356 C  CD1 . ILE   B 2 138 ? -18.967 -9.004  -21.169 1.00 38.62 ? 147 ILE   B CD1 1 
ATOM   1357 N  N   . GLY   B 2 139 ? -20.287 -5.860  -17.219 1.00 31.35 ? 148 GLY   B N   1 
ATOM   1358 C  CA  . GLY   B 2 139 ? -19.420 -5.087  -16.322 1.00 30.31 ? 148 GLY   B CA  1 
ATOM   1359 C  C   . GLY   B 2 139 ? -19.216 -3.674  -16.830 1.00 31.00 ? 148 GLY   B C   1 
ATOM   1360 O  O   . GLY   B 2 139 ? -19.690 -3.307  -17.917 1.00 31.47 ? 148 GLY   B O   1 
ATOM   1361 N  N   . LEU   B 2 140 ? -18.440 -2.901  -16.060 1.00 30.69 ? 149 LEU   B N   1 
ATOM   1362 C  CA  . LEU   B 2 140 ? -18.113 -1.513  -16.396 1.00 30.37 ? 149 LEU   B CA  1 
ATOM   1363 C  C   . LEU   B 2 140 ? -16.599 -1.339  -16.638 1.00 31.99 ? 149 LEU   B C   1 
ATOM   1364 O  O   . LEU   B 2 140 ? -15.752 -2.021  -16.070 1.00 31.67 ? 149 LEU   B O   1 
ATOM   1365 C  CB  . LEU   B 2 140 ? -18.555 -0.564  -15.281 1.00 29.72 ? 149 LEU   B CB  1 
ATOM   1366 C  CG  . LEU   B 2 140 ? -20.007 -0.616  -14.848 1.00 29.28 ? 149 LEU   B CG  1 
ATOM   1367 C  CD1 . LEU   B 2 140 ? -20.227 0.500   -13.800 1.00 28.79 ? 149 LEU   B CD1 1 
ATOM   1368 C  CD2 . LEU   B 2 140 ? -20.991 -0.466  -16.031 1.00 29.44 ? 149 LEU   B CD2 1 
ATOM   1369 N  N   . TYR   B 2 141 ? -16.279 -0.473  -17.588 1.00 31.71 ? 150 TYR   B N   1 
ATOM   1370 C  CA  . TYR   B 2 141 ? -14.935 -0.195  -18.018 1.00 32.97 ? 150 TYR   B CA  1 
ATOM   1371 C  C   . TYR   B 2 141 ? -14.365 0.942   -17.232 1.00 33.37 ? 150 TYR   B C   1 
ATOM   1372 O  O   . TYR   B 2 141 ? -15.073 1.929   -17.080 1.00 35.21 ? 150 TYR   B O   1 
ATOM   1373 C  CB  . TYR   B 2 141 ? -15.058 0.224   -19.528 1.00 34.86 ? 150 TYR   B CB  1 
ATOM   1374 C  CG  . TYR   B 2 141 ? -13.824 0.869   -20.128 1.00 38.39 ? 150 TYR   B CG  1 
ATOM   1375 C  CD1 . TYR   B 2 141 ? -13.693 2.251   -20.184 1.00 40.26 ? 150 TYR   B CD1 1 
ATOM   1376 C  CD2 . TYR   B 2 141 ? -12.794 0.093   -20.661 1.00 40.92 ? 150 TYR   B CD2 1 
ATOM   1377 C  CE1 . TYR   B 2 141 ? -12.557 2.849   -20.719 1.00 43.04 ? 150 TYR   B CE1 1 
ATOM   1378 C  CE2 . TYR   B 2 141 ? -11.657 0.683   -21.207 1.00 42.45 ? 150 TYR   B CE2 1 
ATOM   1379 C  CZ  . TYR   B 2 141 ? -11.524 2.060   -21.196 1.00 44.81 ? 150 TYR   B CZ  1 
ATOM   1380 O  OH  . TYR   B 2 141 ? -10.420 2.668   -21.752 1.00 48.16 ? 150 TYR   B OH  1 
ATOM   1381 N  N   . GLY   B 2 142 ? -13.096 0.889   -16.845 1.00 33.73 ? 151 GLY   B N   1 
ATOM   1382 C  CA  . GLY   B 2 142 ? -12.480 2.045   -16.207 1.00 36.00 ? 151 GLY   B CA  1 
ATOM   1383 C  C   . GLY   B 2 142 ? -11.617 1.822   -14.999 1.00 37.15 ? 151 GLY   B C   1 
ATOM   1384 O  O   . GLY   B 2 142 ? -11.101 2.803   -14.445 1.00 39.81 ? 151 GLY   B O   1 
ATOM   1385 N  N   . ASN   B 2 143 ? -11.441 0.552   -14.563 1.00 34.11 ? 152 ASN   B N   1 
ATOM   1386 C  CA  . ASN   B 2 143 ? -10.520 0.274   -13.471 1.00 34.06 ? 152 ASN   B CA  1 
ATOM   1387 C  C   . ASN   B 2 143 ? -9.578  -0.805  -14.009 1.00 36.16 ? 152 ASN   B C   1 
ATOM   1388 O  O   . ASN   B 2 143 ? -10.011 -1.919  -14.317 1.00 35.79 ? 152 ASN   B O   1 
ATOM   1389 C  CB  . ASN   B 2 143 ? -11.198 -0.227  -12.176 1.00 33.58 ? 152 ASN   B CB  1 
ATOM   1390 C  CG  . ASN   B 2 143 ? -10.233 -0.192  -10.993 1.00 34.77 ? 152 ASN   B CG  1 
ATOM   1391 O  OD1 . ASN   B 2 143 ? -9.265  0.596   -11.007 1.00 36.81 ? 152 ASN   B OD1 1 
ATOM   1392 N  ND2 . ASN   B 2 143 ? -10.426 -1.057  -10.013 1.00 34.72 ? 152 ASN   B ND2 1 
ATOM   1393 N  N   . GLY   B 2 144 ? -8.315  -0.451  -14.145 1.00 38.08 ? 153 GLY   B N   1 
ATOM   1394 C  CA  . GLY   B 2 144 ? -7.353  -1.340  -14.784 1.00 39.22 ? 153 GLY   B CA  1 
ATOM   1395 C  C   . GLY   B 2 144 ? -5.908  -1.010  -14.515 1.00 41.13 ? 153 GLY   B C   1 
ATOM   1396 O  O   . GLY   B 2 144 ? -5.559  -0.546  -13.426 1.00 40.31 ? 153 GLY   B O   1 
ATOM   1397 N  N   . VAL   B 2 145 ? -5.034  -1.260  -15.546 1.00 43.12 ? 154 VAL   B N   1 
ATOM   1398 C  CA  . VAL   B 2 145 ? -3.625  -1.108  -15.327 1.00 46.44 ? 154 VAL   B CA  1 
ATOM   1399 C  C   . VAL   B 2 145 ? -2.905  -0.612  -16.589 1.00 50.11 ? 154 VAL   B C   1 
ATOM   1400 O  O   . VAL   B 2 145 ? -3.487  -0.596  -17.668 1.00 49.61 ? 154 VAL   B O   1 
ATOM   1401 C  CB  . VAL   B 2 145 ? -3.099  -2.503  -14.854 1.00 49.25 ? 154 VAL   B CB  1 
ATOM   1402 C  CG1 . VAL   B 2 145 ? -2.942  -3.485  -16.022 1.00 49.94 ? 154 VAL   B CG1 1 
ATOM   1403 C  CG2 . VAL   B 2 145 ? -1.835  -2.390  -14.031 1.00 50.87 ? 154 VAL   B CG2 1 
ATOM   1404 N  N   . VAL   B 2 146 ? -1.644  -0.190  -16.428 1.00 53.36 ? 155 VAL   B N   1 
ATOM   1405 C  CA  . VAL   B 2 146 ? -0.839  0.252   -17.575 1.00 56.87 ? 155 VAL   B CA  1 
ATOM   1406 C  C   . VAL   B 2 146 ? 0.259   -0.761  -17.741 1.00 60.58 ? 155 VAL   B C   1 
ATOM   1407 O  O   . VAL   B 2 146 ? 1.028   -0.964  -16.813 1.00 60.74 ? 155 VAL   B O   1 
ATOM   1408 C  CB  . VAL   B 2 146 ? -0.309  1.685   -17.406 1.00 58.08 ? 155 VAL   B CB  1 
ATOM   1409 C  CG1 . VAL   B 2 146 ? 0.701   2.014   -18.507 1.00 59.25 ? 155 VAL   B CG1 1 
ATOM   1410 C  CG2 . VAL   B 2 146 ? -1.463  2.678   -17.425 1.00 58.60 ? 155 VAL   B CG2 1 
ATOM   1411 N  N   . ILE   B 2 147 ? 0.300   -1.462  -18.897 1.00 63.47 ? 156 ILE   B N   1 
ATOM   1412 C  CA  . ILE   B 2 147 ? 1.263   -2.547  -19.117 1.00 66.36 ? 156 ILE   B CA  1 
ATOM   1413 C  C   . ILE   B 2 147 ? 2.614   -2.065  -19.719 1.00 69.10 ? 156 ILE   B C   1 
ATOM   1414 O  O   . ILE   B 2 147 ? 2.719   -0.906  -20.110 1.00 69.45 ? 156 ILE   B O   1 
ATOM   1415 C  CB  . ILE   B 2 147 ? 0.586   -3.660  -19.970 1.00 67.36 ? 156 ILE   B CB  1 
ATOM   1416 C  CG1 . ILE   B 2 147 ? 0.320   -3.180  -21.402 1.00 68.08 ? 156 ILE   B CG1 1 
ATOM   1417 C  CG2 . ILE   B 2 147 ? -0.716  -4.137  -19.316 1.00 68.02 ? 156 ILE   B CG2 1 
ATOM   1418 C  CD1 . ILE   B 2 147 ? -0.088  -4.312  -22.350 1.00 69.25 ? 156 ILE   B CD1 1 
ATOM   1419 N  N   . LYS   B 2 148 ? 3.635   -2.954  -19.773 1.00 70.53 ? 157 LYS   B N   1 
ATOM   1420 C  CA  . LYS   B 2 148 ? 4.998   -2.674  -20.265 1.00 72.82 ? 157 LYS   B CA  1 
ATOM   1421 C  C   . LYS   B 2 148 ? 5.108   -1.615  -21.373 1.00 74.79 ? 157 LYS   B C   1 
ATOM   1422 O  O   . LYS   B 2 148 ? 5.753   -0.589  -21.160 1.00 76.16 ? 157 LYS   B O   1 
ATOM   1423 C  CB  . LYS   B 2 148 ? 5.697   -3.969  -20.721 1.00 74.89 ? 157 LYS   B CB  1 
ATOM   1424 C  CG  . LYS   B 2 148 ? 6.291   -4.796  -19.600 1.00 79.25 ? 157 LYS   B CG  1 
ATOM   1425 C  CD  . LYS   B 2 148 ? 6.666   -6.191  -20.091 1.00 84.78 ? 157 LYS   B CD  1 
ATOM   1426 C  CE  . LYS   B 2 148 ? 7.692   -6.194  -21.205 1.00 89.70 ? 157 LYS   B CE  1 
ATOM   1427 N  NZ  . LYS   B 2 148 ? 9.073   -5.944  -20.704 1.00 92.46 ? 157 LYS   B NZ  1 
ATOM   1428 N  N   . ASN   B 2 149 ? 4.455   -1.825  -22.530 1.00 74.64 ? 158 ASN   B N   1 
ATOM   1429 C  CA  . ASN   B 2 149 ? 4.516   -0.895  -23.666 1.00 74.69 ? 158 ASN   B CA  1 
ATOM   1430 C  C   . ASN   B 2 149 ? 3.697   0.395   -23.500 1.00 72.86 ? 158 ASN   B C   1 
ATOM   1431 O  O   . ASN   B 2 149 ? 3.411   1.068   -24.495 1.00 73.29 ? 158 ASN   B O   1 
ATOM   1432 C  CB  . ASN   B 2 149 ? 4.116   -1.606  -24.973 1.00 77.05 ? 158 ASN   B CB  1 
ATOM   1433 C  CG  . ASN   B 2 149 ? 2.908   -2.515  -24.845 1.00 81.87 ? 158 ASN   B CG  1 
ATOM   1434 O  OD1 . ASN   B 2 149 ? 2.941   -3.531  -24.142 1.00 84.24 ? 158 ASN   B OD1 1 
ATOM   1435 N  ND2 . ASN   B 2 149 ? 1.821   -2.177  -25.519 1.00 82.54 ? 158 ASN   B ND2 1 
ATOM   1436 N  N   . GLY   B 2 150 ? 3.336   0.724   -22.269 1.00 70.64 ? 159 GLY   B N   1 
ATOM   1437 C  CA  . GLY   B 2 150 ? 2.530   1.898   -21.922 1.00 68.81 ? 159 GLY   B CA  1 
ATOM   1438 C  C   . GLY   B 2 150 ? 1.040   1.853   -22.242 1.00 65.85 ? 159 GLY   B C   1 
ATOM   1439 O  O   . GLY   B 2 150 ? 0.348   2.871   -22.090 1.00 66.77 ? 159 GLY   B O   1 
ATOM   1440 N  N   A SER   B 2 151 ? 0.520   0.688   -22.670 0.50 63.77 ? 160 SER   B N   1 
ATOM   1441 N  N   C SER   B 2 151 ? 0.520   0.688   -22.670 0.50 63.77 ? 160 SER   B N   1 
ATOM   1442 C  CA  A SER   B 2 151 ? -0.899  0.582   -23.034 0.50 62.05 ? 160 SER   B CA  1 
ATOM   1443 C  CA  C SER   B 2 151 ? -0.899  0.582   -23.034 0.50 62.05 ? 160 SER   B CA  1 
ATOM   1444 C  C   A SER   B 2 151 ? -1.851  0.364   -21.844 0.50 58.92 ? 160 SER   B C   1 
ATOM   1445 C  C   C SER   B 2 151 ? -1.851  0.364   -21.844 0.50 58.92 ? 160 SER   B C   1 
ATOM   1446 O  O   A SER   B 2 151 ? -1.464  -0.270  -20.870 0.50 59.31 ? 160 SER   B O   1 
ATOM   1447 O  O   C SER   B 2 151 ? -1.464  -0.270  -20.870 0.50 59.31 ? 160 SER   B O   1 
ATOM   1448 C  CB  A SER   B 2 151 ? -1.105  -0.522  -24.063 0.50 64.21 ? 160 SER   B CB  1 
ATOM   1449 C  CB  C SER   B 2 151 ? -1.105  -0.522  -24.063 0.50 64.21 ? 160 SER   B CB  1 
ATOM   1450 O  OG  A SER   B 2 151 ? -2.355  -0.346  -24.707 0.50 67.91 ? 160 SER   B OG  1 
ATOM   1451 O  OG  C SER   B 2 151 ? -2.355  -0.346  -24.707 0.50 67.91 ? 160 SER   B OG  1 
ATOM   1452 N  N   . TYR   B 2 152 ? -3.103  0.843   -21.960 1.00 56.28 ? 161 TYR   B N   1 
ATOM   1453 C  CA  . TYR   B 2 152 ? -4.153  0.691   -20.901 1.00 52.43 ? 161 TYR   B CA  1 
ATOM   1454 C  C   . TYR   B 2 152 ? -5.029  -0.557  -21.087 1.00 48.81 ? 161 TYR   B C   1 
ATOM   1455 O  O   . TYR   B 2 152 ? -5.601  -0.756  -22.161 1.00 48.51 ? 161 TYR   B O   1 
ATOM   1456 C  CB  . TYR   B 2 152 ? -5.086  1.918   -20.845 1.00 50.89 ? 161 TYR   B CB  1 
ATOM   1457 C  CG  . TYR   B 2 152 ? -6.094  1.884   -19.696 1.00 50.71 ? 161 TYR   B CG  1 
ATOM   1458 C  CD1 . TYR   B 2 152 ? -5.680  2.017   -18.379 1.00 51.22 ? 161 TYR   B CD1 1 
ATOM   1459 C  CD2 . TYR   B 2 152 ? -7.455  1.717   -19.937 1.00 50.59 ? 161 TYR   B CD2 1 
ATOM   1460 C  CE1 . TYR   B 2 152 ? -6.592  1.983   -17.326 1.00 51.53 ? 161 TYR   B CE1 1 
ATOM   1461 C  CE2 . TYR   B 2 152 ? -8.378  1.677   -18.888 1.00 51.30 ? 161 TYR   B CE2 1 
ATOM   1462 C  CZ  . TYR   B 2 152 ? -7.939  1.808   -17.582 1.00 51.55 ? 161 TYR   B CZ  1 
ATOM   1463 O  OH  . TYR   B 2 152 ? -8.835  1.760   -16.526 1.00 51.35 ? 161 TYR   B OH  1 
ATOM   1464 N  N   . VAL   B 2 153 ? -5.208  -1.358  -20.009 1.00 45.58 ? 162 VAL   B N   1 
ATOM   1465 C  CA  . VAL   B 2 153 ? -6.079  -2.509  -20.084 1.00 42.44 ? 162 VAL   B CA  1 
ATOM   1466 C  C   . VAL   B 2 153 ? -7.039  -2.420  -18.877 1.00 38.55 ? 162 VAL   B C   1 
ATOM   1467 O  O   . VAL   B 2 153 ? -6.604  -2.375  -17.727 1.00 39.25 ? 162 VAL   B O   1 
ATOM   1468 C  CB  . VAL   B 2 153 ? -5.313  -3.834  -20.059 1.00 43.96 ? 162 VAL   B CB  1 
ATOM   1469 C  CG1 . VAL   B 2 153 ? -6.266  -5.028  -20.097 1.00 43.99 ? 162 VAL   B CG1 1 
ATOM   1470 C  CG2 . VAL   B 2 153 ? -4.280  -3.914  -21.207 1.00 45.59 ? 162 VAL   B CG2 1 
ATOM   1471 N  N   . SER   B 2 154 ? -8.340  -2.390  -19.185 1.00 37.82 ? 163 SER   B N   1 
ATOM   1472 C  CA  . SER   B 2 154 ? -9.349  -2.276  -18.109 1.00 35.97 ? 163 SER   B CA  1 
ATOM   1473 C  C   . SER   B 2 154 ? -9.879  -3.636  -17.669 1.00 35.38 ? 163 SER   B C   1 
ATOM   1474 O  O   . SER   B 2 154 ? -10.178 -4.448  -18.526 1.00 35.93 ? 163 SER   B O   1 
ATOM   1475 C  CB  . SER   B 2 154 ? -10.538 -1.477  -18.639 1.00 36.90 ? 163 SER   B CB  1 
ATOM   1476 O  OG  . SER   B 2 154 ? -11.542 -1.362  -17.626 1.00 37.24 ? 163 SER   B OG  1 
ATOM   1477 N  N   . ALA   B 2 155 ? -10.116 -3.885  -16.371 1.00 34.17 ? 164 ALA   B N   1 
ATOM   1478 C  CA  . ALA   B 2 155 ? -10.851 -5.082  -15.954 1.00 32.84 ? 164 ALA   B CA  1 
ATOM   1479 C  C   . ALA   B 2 155 ? -12.300 -4.932  -16.484 1.00 34.12 ? 164 ALA   B C   1 
ATOM   1480 O  O   . ALA   B 2 155 ? -12.780 -3.787  -16.715 1.00 34.74 ? 164 ALA   B O   1 
ATOM   1481 C  CB  . ALA   B 2 155 ? -10.922 -5.175  -14.423 1.00 32.96 ? 164 ALA   B CB  1 
ATOM   1482 N  N   . ILE   B 2 156 ? -12.988 -6.067  -16.680 1.00 33.32 ? 165 ILE   B N   1 
ATOM   1483 C  CA  . ILE   B 2 156 ? -14.432 -6.034  -16.887 1.00 33.95 ? 165 ILE   B CA  1 
ATOM   1484 C  C   . ILE   B 2 156 ? -14.974 -6.147  -15.433 1.00 32.55 ? 165 ILE   B C   1 
ATOM   1485 O  O   . ILE   B 2 156 ? -14.969 -7.237  -14.857 1.00 33.99 ? 165 ILE   B O   1 
ATOM   1486 C  CB  . ILE   B 2 156 ? -14.879 -7.269  -17.698 1.00 36.40 ? 165 ILE   B CB  1 
ATOM   1487 C  CG1 . ILE   B 2 156 ? -14.190 -7.197  -19.084 1.00 38.73 ? 165 ILE   B CG1 1 
ATOM   1488 C  CG2 . ILE   B 2 156 ? -16.419 -7.214  -17.869 1.00 36.87 ? 165 ILE   B CG2 1 
ATOM   1489 C  CD1 . ILE   B 2 156 ? -14.661 -8.279  -20.077 1.00 40.93 ? 165 ILE   B CD1 1 
ATOM   1490 N  N   . THR   B 2 157 ? -15.347 -4.988  -14.808 1.00 31.56 ? 166 THR   B N   1 
ATOM   1491 C  CA  . THR   B 2 157 ? -15.727 -5.019  -13.394 1.00 30.87 ? 166 THR   B CA  1 
ATOM   1492 C  C   . THR   B 2 157 ? -17.235 -5.231  -13.236 1.00 30.54 ? 166 THR   B C   1 
ATOM   1493 O  O   . THR   B 2 157 ? -18.031 -4.379  -13.680 1.00 30.74 ? 166 THR   B O   1 
ATOM   1494 C  CB  . THR   B 2 157 ? -15.304 -3.698  -12.737 1.00 31.67 ? 166 THR   B CB  1 
ATOM   1495 O  OG1 . THR   B 2 157 ? -13.875 -3.513  -12.806 1.00 31.85 ? 166 THR   B OG1 1 
ATOM   1496 C  CG2 . THR   B 2 157 ? -15.806 -3.609  -11.296 1.00 30.65 ? 166 THR   B CG2 1 
ATOM   1497 N  N   . GLN   B 2 158 ? -17.633 -6.328  -12.566 1.00 30.06 ? 167 GLN   B N   1 
ATOM   1498 C  CA  . GLN   B 2 158 ? -19.058 -6.590  -12.386 1.00 29.55 ? 167 GLN   B CA  1 
ATOM   1499 C  C   . GLN   B 2 158 ? -19.361 -6.741  -10.862 1.00 30.33 ? 167 GLN   B C   1 
ATOM   1500 O  O   . GLN   B 2 158 ? -18.530 -7.274  -10.117 1.00 30.41 ? 167 GLN   B O   1 
ATOM   1501 C  CB  . GLN   B 2 158 ? -19.444 -7.887  -13.139 1.00 32.16 ? 167 GLN   B CB  1 
ATOM   1502 C  CG  . GLN   B 2 158 ? -20.921 -8.278  -13.016 1.00 32.85 ? 167 GLN   B CG  1 
ATOM   1503 C  CD  . GLN   B 2 158 ? -21.887 -7.239  -13.626 1.00 32.71 ? 167 GLN   B CD  1 
ATOM   1504 O  OE1 . GLN   B 2 158 ? -22.022 -6.128  -13.078 1.00 30.63 ? 167 GLN   B OE1 1 
ATOM   1505 N  NE2 . GLN   B 2 158 ? -22.523 -7.560  -14.766 1.00 32.51 ? 167 GLN   B NE2 1 
ATOM   1506 N  N   . GLY   B 2 159 ? -20.536 -6.273  -10.473 1.00 31.46 ? 168 GLY   B N   1 
ATOM   1507 C  CA  . GLY   B 2 159 ? -20.984 -6.348  -9.078  1.00 33.77 ? 168 GLY   B CA  1 
ATOM   1508 C  C   . GLY   B 2 159 ? -21.818 -7.595  -8.832  1.00 40.57 ? 168 GLY   B C   1 
ATOM   1509 O  O   . GLY   B 2 159 ? -22.049 -8.405  -9.739  1.00 43.54 ? 168 GLY   B O   1 
ATOM   1510 N  N   . LYS   B 2 160 ? -22.233 -7.800  -7.591  1.00 42.20 ? 169 LYS   B N   1 
ATOM   1511 C  CA  . LYS   B 2 160 ? -23.057 -8.957  -7.233  1.00 43.53 ? 169 LYS   B CA  1 
ATOM   1512 C  C   . LYS   B 2 160 ? -24.507 -8.504  -7.112  1.00 44.14 ? 169 LYS   B C   1 
ATOM   1513 O  O   . LYS   B 2 160 ? -24.779 -7.468  -6.502  1.00 43.65 ? 169 LYS   B O   1 
ATOM   1514 C  CB  . LYS   B 2 160 ? -22.563 -9.533  -5.884  1.00 46.40 ? 169 LYS   B CB  1 
ATOM   1515 C  CG  . LYS   B 2 160 ? -23.541 -10.490 -5.201  1.00 54.20 ? 169 LYS   B CG  1 
ATOM   1516 C  CD  . LYS   B 2 160 ? -22.882 -11.303 -4.083  1.00 62.19 ? 169 LYS   B CD  1 
ATOM   1517 C  CE  . LYS   B 2 160 ? -23.693 -12.555 -3.798  1.00 68.51 ? 169 LYS   B CE  1 
ATOM   1518 N  NZ  . LYS   B 2 160 ? -23.108 -13.380 -2.699  1.00 72.84 ? 169 LYS   B NZ  1 
ATOM   1519 N  N   . ARG   B 2 161 ? -25.444 -9.280  -7.679  1.00 45.54 ? 170 ARG   B N   1 
ATOM   1520 C  CA  . ARG   B 2 161 ? -26.853 -8.981  -7.512  1.00 48.66 ? 170 ARG   B CA  1 
ATOM   1521 C  C   . ARG   B 2 161 ? -27.325 -9.834  -6.315  1.00 51.69 ? 170 ARG   B C   1 
ATOM   1522 O  O   . ARG   B 2 161 ? -27.329 -11.068 -6.413  1.00 52.38 ? 170 ARG   B O   1 
ATOM   1523 C  CB  . ARG   B 2 161 ? -27.648 -9.278  -8.792  1.00 50.16 ? 170 ARG   B CB  1 
ATOM   1524 C  CG  . ARG   B 2 161 ? -29.064 -8.774  -8.725  1.00 52.10 ? 170 ARG   B CG  1 
ATOM   1525 C  CD  . ARG   B 2 161 ? -29.901 -9.272  -9.883  1.00 54.89 ? 170 ARG   B CD  1 
ATOM   1526 N  NE  . ARG   B 2 161 ? -31.317 -8.948  -9.701  1.00 55.61 ? 170 ARG   B NE  1 
ATOM   1527 C  CZ  . ARG   B 2 161 ? -32.007 -8.108  -10.467 1.00 55.18 ? 170 ARG   B CZ  1 
ATOM   1528 N  NH1 . ARG   B 2 161 ? -31.424 -7.503  -11.494 1.00 50.31 ? 170 ARG   B NH1 1 
ATOM   1529 N  NH2 . ARG   B 2 161 ? -33.295 -7.897  -10.236 1.00 56.51 ? 170 ARG   B NH2 1 
ATOM   1530 N  N   . GLU   B 2 162 ? -27.600 -9.189  -5.162  1.00 53.20 ? 171 GLU   B N   1 
ATOM   1531 C  CA  . GLU   B 2 162 ? -28.014 -9.890  -3.933  1.00 56.23 ? 171 GLU   B CA  1 
ATOM   1532 C  C   . GLU   B 2 162 ? -29.354 -10.593 -4.095  1.00 58.15 ? 171 GLU   B C   1 
ATOM   1533 O  O   . GLU   B 2 162 ? -29.668 -11.479 -3.292  1.00 59.54 ? 171 GLU   B O   1 
ATOM   1534 C  CB  . GLU   B 2 162 ? -28.090 -8.927  -2.730  1.00 60.09 ? 171 GLU   B CB  1 
ATOM   1535 C  CG  . GLU   B 2 162 ? -26.864 -8.045  -2.534  1.00 67.58 ? 171 GLU   B CG  1 
ATOM   1536 C  CD  . GLU   B 2 162 ? -25.700 -8.643  -1.766  1.00 77.80 ? 171 GLU   B CD  1 
ATOM   1537 O  OE1 . GLU   B 2 162 ? -25.198 -7.961  -0.843  1.00 80.78 ? 171 GLU   B OE1 1 
ATOM   1538 O  OE2 . GLU   B 2 162 ? -25.265 -9.770  -2.098  1.00 80.83 ? 171 GLU   B OE2 1 
HETATM 1539 S  S   . DMS   C 3 .   ? -9.399  3.425   -8.818  0.84 70.01 ? 101 DMS   A S   1 
HETATM 1540 O  O   . DMS   C 3 .   ? -9.629  2.532   -7.632  0.84 69.69 ? 101 DMS   A O   1 
HETATM 1541 C  C1  . DMS   C 3 .   ? -9.055  5.081   -8.171  0.84 69.75 ? 101 DMS   A C1  1 
HETATM 1542 C  C2  . DMS   C 3 .   ? -7.714  3.117   -9.418  0.84 70.48 ? 101 DMS   A C2  1 
HETATM 1543 S  S   . DMS   D 3 .   ? -18.870 12.396  -0.302  1.00 71.20 ? 201 DMS   B S   1 
HETATM 1544 O  O   . DMS   D 3 .   ? -19.553 11.062  -0.345  1.00 70.87 ? 201 DMS   B O   1 
HETATM 1545 C  C1  . DMS   D 3 .   ? -19.908 13.698  -1.003  1.00 71.40 ? 201 DMS   B C1  1 
HETATM 1546 C  C2  . DMS   D 3 .   ? -17.679 12.513  -1.662  1.00 70.73 ? 201 DMS   B C2  1 
HETATM 1547 C  C4  . A1BG6 E 4 .   ? -9.643  5.017   -18.138 0.70 74.40 ? 202 A1BG6 B C4  1 
HETATM 1548 C  C5  . A1BG6 E 4 .   ? -9.489  5.167   -16.777 0.70 74.08 ? 202 A1BG6 B C5  1 
HETATM 1549 BR BR  . A1BG6 E 4 .   ? -11.352 4.537   -18.813 0.70 75.43 ? 202 A1BG6 B BR  1 
HETATM 1550 C  C3  . A1BG6 E 4 .   ? -8.594  5.233   -19.005 0.70 73.88 ? 202 A1BG6 B C3  1 
HETATM 1551 C  C2  . A1BG6 E 4 .   ? -7.375  5.618   -18.474 0.70 73.74 ? 202 A1BG6 B C2  1 
HETATM 1552 C  C1  . A1BG6 E 4 .   ? -7.237  5.766   -17.112 0.70 73.83 ? 202 A1BG6 B C1  1 
HETATM 1553 N  N   . A1BG6 E 4 .   ? -8.285  5.537   -16.291 0.70 74.02 1 202 A1BG6 B N   1 
HETATM 1554 C  C   . A1BG6 E 4 .   ? -8.119  5.700   -14.831 0.70 73.93 ? 202 A1BG6 B C   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -32.385 0.495   -28.935 1.00 55.27 ? 201 HOH   A O   1 
HETATM 1556 O  O   . HOH   F 5 .   ? -7.959  1.026   3.240   1.00 48.77 ? 202 HOH   A O   1 
HETATM 1557 O  O   . HOH   F 5 .   ? -24.625 9.657   -27.566 1.00 39.48 ? 203 HOH   A O   1 
HETATM 1558 O  O   . HOH   F 5 .   ? -23.868 19.411  -19.683 1.00 48.59 ? 204 HOH   A O   1 
HETATM 1559 O  O   . HOH   F 5 .   ? -4.675  -13.959 -25.625 1.00 39.08 ? 205 HOH   A O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -2.888  -4.137  -24.913 1.00 53.02 ? 206 HOH   A O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -25.625 12.847  -23.824 1.00 50.30 ? 207 HOH   A O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -8.664  -5.827  2.696   1.00 69.55 ? 208 HOH   A O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -2.218  -3.482  -6.507  1.00 44.80 ? 209 HOH   A O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -6.748  -4.045  6.244   1.00 72.03 ? 210 HOH   A O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -8.209  -1.256  6.527   1.00 47.75 ? 211 HOH   A O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -3.102  -11.202 -7.151  1.00 42.25 ? 212 HOH   A O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -9.691  -6.368  -25.501 1.00 43.16 ? 213 HOH   A O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -8.274  2.265   0.883   1.00 49.30 ? 214 HOH   A O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -29.470 16.226  -15.056 1.00 44.48 ? 215 HOH   A O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -0.925  -12.305 -23.416 1.00 64.18 ? 216 HOH   A O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -7.086  -8.648  -3.219  1.00 40.50 ? 217 HOH   A O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -27.099 -3.205  -35.340 1.00 71.09 ? 218 HOH   A O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -9.197  4.365   -3.415  1.00 56.44 ? 219 HOH   A O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? 1.699   -2.039  -11.919 1.00 54.58 ? 220 HOH   A O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -31.011 13.085  -16.427 1.00 52.09 ? 221 HOH   A O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -28.747 -5.760  -28.011 1.00 47.31 ? 222 HOH   A O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -3.224  0.981   -12.082 1.00 55.59 ? 223 HOH   A O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -4.733  -9.611  -5.625  1.00 40.01 ? 224 HOH   A O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -22.621 -9.127  -34.561 1.00 59.32 ? 225 HOH   A O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -3.825  -3.767  0.233   1.00 52.36 ? 226 HOH   A O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -28.038 2.111   -29.613 1.00 73.96 ? 227 HOH   A O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -27.188 7.237   -28.681 1.00 50.87 ? 228 HOH   A O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -12.981 -3.532  -37.893 1.00 67.58 ? 229 HOH   A O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -23.002 17.446  -4.001  1.00 73.78 ? 230 HOH   A O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -31.588 1.104   -23.099 1.00 37.28 ? 231 HOH   A O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -2.921  -8.327  -3.425  1.00 60.07 ? 232 HOH   A O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -3.973  -0.279  -0.479  1.00 57.83 ? 233 HOH   A O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -4.554  -6.270  -0.141  1.00 71.65 ? 234 HOH   A O   1 
HETATM 1589 O  O   . HOH   G 5 .   ? -20.324 -6.868  -5.450  1.00 47.50 ? 301 HOH   B O   1 
HETATM 1590 O  O   . HOH   G 5 .   ? -34.277 2.200   -15.147 1.00 48.49 ? 302 HOH   B O   1 
HETATM 1591 O  O   . HOH   G 5 .   ? -15.476 -4.148  1.433   1.00 37.15 ? 303 HOH   B O   1 
HETATM 1592 O  O   . HOH   G 5 .   ? -13.063 10.791  -13.820 1.00 52.97 ? 304 HOH   B O   1 
HETATM 1593 O  O   . HOH   G 5 .   ? -31.322 12.851  -19.255 1.00 47.72 ? 305 HOH   B O   1 
HETATM 1594 O  O   . HOH   G 5 .   ? -18.250 1.026   -34.048 1.00 62.69 ? 306 HOH   B O   1 
HETATM 1595 O  O   . HOH   G 5 .   ? -17.614 15.726  -30.480 1.00 62.68 ? 307 HOH   B O   1 
HETATM 1596 O  O   . HOH   G 5 .   ? -22.910 -10.600 -10.665 1.00 59.99 ? 308 HOH   B O   1 
HETATM 1597 O  O   . HOH   G 5 .   ? -28.461 -8.296  -29.080 1.00 59.69 ? 309 HOH   B O   1 
HETATM 1598 O  O   . HOH   G 5 .   ? -28.920 -4.051  -21.498 1.00 59.24 ? 310 HOH   B O   1 
HETATM 1599 O  O   . HOH   G 5 .   ? -19.956 -11.633 -25.583 1.00 51.88 ? 311 HOH   B O   1 
HETATM 1600 O  O   . HOH   G 5 .   ? -26.050 -7.273  1.506   1.00 68.79 ? 312 HOH   B O   1 
HETATM 1601 O  O   . HOH   G 5 .   ? -34.884 -2.311  -16.533 1.00 53.42 ? 313 HOH   B O   1 
HETATM 1602 O  O   . HOH   G 5 .   ? -35.603 4.343   -8.801  1.00 53.48 ? 314 HOH   B O   1 
HETATM 1603 O  O   . HOH   G 5 .   ? -23.341 -6.420  -1.966  1.00 57.81 ? 315 HOH   B O   1 
HETATM 1604 O  O   . HOH   G 5 .   ? -21.829 7.825   -0.079  0.50 33.58 ? 316 HOH   B O   1 
HETATM 1605 O  O   . HOH   G 5 .   ? -5.663  -17.456 -11.151 1.00 76.78 ? 317 HOH   B O   1 
HETATM 1606 O  O   . HOH   G 5 .   ? -16.844 -14.592 -16.405 1.00 43.62 ? 318 HOH   B O   1 
HETATM 1607 O  O   . HOH   G 5 .   ? -7.432  -10.378 -5.344  1.00 44.69 ? 319 HOH   B O   1 
HETATM 1608 O  O   . HOH   G 5 .   ? -16.696 -6.600  -8.275  1.00 48.90 ? 320 HOH   B O   1 
HETATM 1609 O  O   . HOH   G 5 .   ? -16.801 21.328  -14.454 1.00 49.57 ? 321 HOH   B O   1 
HETATM 1610 O  O   . HOH   G 5 .   ? -17.924 9.098   -30.856 1.00 53.56 ? 322 HOH   B O   1 
HETATM 1611 O  O   . HOH   G 5 .   ? -5.280  -9.247  -0.630  1.00 74.06 ? 323 HOH   B O   1 
HETATM 1612 O  O   . HOH   G 5 .   ? -27.713 -6.281  -5.387  1.00 41.93 ? 324 HOH   B O   1 
HETATM 1613 O  O   . HOH   G 5 .   ? -12.542 20.853  -16.767 1.00 73.09 ? 325 HOH   B O   1 
HETATM 1614 O  O   . HOH   G 5 .   ? -28.129 -5.739  -18.412 1.00 42.04 ? 326 HOH   B O   1 
HETATM 1615 O  O   . HOH   G 5 .   ? -30.260 -0.455  -19.074 1.00 41.00 ? 327 HOH   B O   1 
HETATM 1616 O  O   . HOH   G 5 .   ? -22.122 -12.052 -12.705 1.00 46.99 ? 328 HOH   B O   1 
HETATM 1617 O  O   . HOH   G 5 .   ? -6.521  0.187   -10.979 1.00 36.25 ? 329 HOH   B O   1 
HETATM 1618 O  O   . HOH   G 5 .   ? -18.328 -10.342 -16.370 1.00 35.13 ? 330 HOH   B O   1 
HETATM 1619 O  O   . HOH   G 5 .   ? -16.475 26.780  -12.426 1.00 68.50 ? 331 HOH   B O   1 
HETATM 1620 O  O   . HOH   G 5 .   ? -13.285 -1.782  -14.869 1.00 29.75 ? 332 HOH   B O   1 
HETATM 1621 O  O   . HOH   G 5 .   ? -19.484 15.263  -22.320 1.00 36.70 ? 333 HOH   B O   1 
HETATM 1622 O  O   . HOH   G 5 .   ? -26.375 -7.566  -16.392 1.00 35.52 ? 334 HOH   B O   1 
HETATM 1623 O  O   . HOH   G 5 .   ? -29.802 18.536  -14.003 1.00 78.77 ? 335 HOH   B O   1 
HETATM 1624 O  O   . HOH   G 5 .   ? -22.494 15.709  -6.074  1.00 43.72 ? 336 HOH   B O   1 
HETATM 1625 O  O   . HOH   G 5 .   ? -9.455  3.620   -12.352 1.00 58.83 ? 337 HOH   B O   1 
HETATM 1626 O  O   . HOH   G 5 .   ? -12.741 -2.961  -10.224 1.00 34.80 ? 338 HOH   B O   1 
HETATM 1627 O  O   . HOH   G 5 .   ? -15.880 -9.843  -15.252 1.00 41.61 ? 339 HOH   B O   1 
HETATM 1628 O  O   . HOH   G 5 .   ? -12.210 -17.599 -28.011 1.00 46.97 ? 340 HOH   B O   1 
HETATM 1629 O  O   . HOH   G 5 .   ? -35.592 -4.978  -9.948  1.00 52.91 ? 341 HOH   B O   1 
HETATM 1630 O  O   . HOH   G 5 .   ? -18.944 19.726  -21.629 1.00 55.91 ? 342 HOH   B O   1 
HETATM 1631 O  O   . HOH   G 5 .   ? -22.318 -13.093 -21.592 1.00 47.75 ? 343 HOH   B O   1 
HETATM 1632 O  O   . HOH   G 5 .   ? -23.200 7.667   -34.232 1.00 74.01 ? 344 HOH   B O   1 
HETATM 1633 O  O   . HOH   G 5 .   ? -23.801 -5.670  -4.578  1.00 47.09 ? 345 HOH   B O   1 
HETATM 1634 O  O   . HOH   G 5 .   ? -21.692 14.853  -34.815 1.00 62.84 ? 346 HOH   B O   1 
HETATM 1635 O  O   . HOH   G 5 .   ? -15.363 9.809   -0.924  1.00 40.78 ? 347 HOH   B O   1 
HETATM 1636 O  O   . HOH   G 5 .   ? -12.333 2.804   -5.780  1.00 36.08 ? 348 HOH   B O   1 
HETATM 1637 O  O   . HOH   G 5 .   ? -17.326 13.566  -5.589  1.00 45.27 ? 349 HOH   B O   1 
HETATM 1638 O  O   . HOH   G 5 .   ? -9.230  6.978   -27.757 1.00 54.12 ? 350 HOH   B O   1 
HETATM 1639 O  O   . HOH   G 5 .   ? -25.049 -11.718 -9.117  1.00 55.66 ? 351 HOH   B O   1 
HETATM 1640 O  O   . HOH   G 5 .   ? -2.436  -17.643 -19.075 1.00 71.04 ? 352 HOH   B O   1 
HETATM 1641 O  O   . HOH   G 5 .   ? -11.825 -4.391  -8.236  1.00 41.21 ? 353 HOH   B O   1 
HETATM 1642 O  O   . HOH   G 5 .   ? -15.608 17.000  -20.307 1.00 44.89 ? 354 HOH   B O   1 
HETATM 1643 O  O   . HOH   G 5 .   ? -7.569  2.382   -14.032 1.00 43.78 ? 355 HOH   B O   1 
HETATM 1644 O  O   . HOH   G 5 .   ? -7.607  -6.069  0.221   1.00 52.21 ? 356 HOH   B O   1 
HETATM 1645 O  O   . HOH   G 5 .   ? -11.214 -16.332 -24.760 1.00 53.56 ? 357 HOH   B O   1 
HETATM 1646 O  O   . HOH   G 5 .   ? -12.565 14.031  -17.103 1.00 77.53 ? 358 HOH   B O   1 
HETATM 1647 O  O   . HOH   G 5 .   ? -11.463 12.646  -19.499 1.00 44.26 ? 359 HOH   B O   1 
HETATM 1648 O  O   . HOH   G 5 .   ? -28.012 20.706  -15.163 1.00 84.91 ? 360 HOH   B O   1 
HETATM 1649 O  O   . HOH   G 5 .   ? -15.498 -8.188  -11.864 1.00 45.51 ? 361 HOH   B O   1 
HETATM 1650 O  O   . HOH   G 5 .   ? -32.158 7.741   -4.423  1.00 50.40 ? 362 HOH   B O   1 
HETATM 1651 O  O   . HOH   G 5 .   ? -16.475 -13.950 -30.764 1.00 54.25 ? 363 HOH   B O   1 
HETATM 1652 O  O   . HOH   G 5 .   ? -11.632 8.270   -14.228 1.00 52.13 ? 364 HOH   B O   1 
HETATM 1653 O  O   . HOH   G 5 .   ? -15.024 -11.796 -16.384 1.00 41.39 ? 365 HOH   B O   1 
HETATM 1654 O  O   . HOH   G 5 .   ? -32.647 -6.434  -6.684  1.00 47.60 ? 366 HOH   B O   1 
HETATM 1655 O  O   . HOH   G 5 .   ? -21.275 6.265   -32.920 1.00 66.29 ? 367 HOH   B O   1 
HETATM 1656 O  O   . HOH   G 5 .   ? -26.140 -4.044  -3.901  1.00 35.20 ? 368 HOH   B O   1 
HETATM 1657 O  O   . HOH   G 5 .   ? -7.512  1.665   -27.974 1.00 64.58 ? 369 HOH   B O   1 
HETATM 1658 O  O   . HOH   G 5 .   ? -1.035  0.903   -13.673 1.00 58.59 ? 370 HOH   B O   1 
HETATM 1659 O  O   . HOH   G 5 .   ? -20.896 25.299  -16.992 1.00 55.05 ? 371 HOH   B O   1 
HETATM 1660 O  O   . HOH   G 5 .   ? -24.372 -14.337 -17.807 1.00 53.41 ? 372 HOH   B O   1 
HETATM 1661 O  O   . HOH   G 5 .   ? -7.843  11.432  -19.615 1.00 58.32 ? 373 HOH   B O   1 
HETATM 1662 O  O   . HOH   G 5 .   ? -14.544 -5.877  -1.638  1.00 43.19 ? 374 HOH   B O   1 
HETATM 1663 O  O   . HOH   G 5 .   ? -23.110 14.863  -2.355  1.00 65.36 ? 375 HOH   B O   1 
HETATM 1664 O  O   . HOH   G 5 .   ? -9.004  -10.155 -7.407  1.00 54.96 ? 376 HOH   B O   1 
HETATM 1665 O  O   . HOH   G 5 .   ? -19.959 -12.979 -23.007 1.00 40.16 ? 377 HOH   B O   1 
HETATM 1666 O  O   . HOH   G 5 .   ? -35.141 4.973   -4.342  1.00 54.49 ? 378 HOH   B O   1 
HETATM 1667 O  O   . HOH   G 5 .   ? -37.009 2.455   -18.864 1.00 60.74 ? 379 HOH   B O   1 
HETATM 1668 O  O   . HOH   G 5 .   ? -10.928 -18.218 -11.916 1.00 52.84 ? 380 HOH   B O   1 
HETATM 1669 O  O   . HOH   G 5 .   ? -12.899 8.000   -30.021 1.00 59.25 ? 381 HOH   B O   1 
HETATM 1670 O  O   . HOH   G 5 .   ? -11.585 -12.763 -8.737  1.00 61.62 ? 382 HOH   B O   1 
HETATM 1671 O  O   . HOH   G 5 .   ? -12.200 9.024   -27.581 1.00 49.68 ? 383 HOH   B O   1 
HETATM 1672 O  O   . HOH   G 5 .   ? -19.700 -5.085  -0.805  1.00 39.63 ? 384 HOH   B O   1 
HETATM 1673 O  O   . HOH   G 5 .   ? -11.468 -8.649  0.345   1.00 66.71 ? 385 HOH   B O   1 
HETATM 1674 O  O   . HOH   G 5 .   ? -19.466 26.005  -14.589 1.00 60.47 ? 386 HOH   B O   1 
HETATM 1675 O  O   . HOH   G 5 .   ? -9.531  -14.869 -24.117 1.00 49.34 ? 387 HOH   B O   1 
HETATM 1676 O  O   . HOH   G 5 .   ? -30.957 5.190   -2.249  1.00 47.00 ? 388 HOH   B O   1 
HETATM 1677 O  O   . HOH   G 5 .   ? -20.004 -10.338 -34.479 1.00 61.20 ? 389 HOH   B O   1 
HETATM 1678 O  O   . HOH   G 5 .   ? -20.688 -7.199  -2.369  1.00 51.91 ? 390 HOH   B O   1 
HETATM 1679 O  O   . HOH   G 5 .   ? -35.478 2.202   -7.439  1.00 60.46 ? 391 HOH   B O   1 
HETATM 1680 O  O   . HOH   G 5 .   ? -29.897 -4.903  -0.783  1.00 43.98 ? 392 HOH   B O   1 
HETATM 1681 O  O   . HOH   G 5 .   ? -16.812 -12.493 -32.846 1.00 76.62 ? 393 HOH   B O   1 
HETATM 1682 O  O   . HOH   G 5 .   ? -18.823 -10.611 -9.835  1.00 64.22 ? 394 HOH   B O   1 
HETATM 1683 O  O   . HOH   G 5 .   ? -14.407 11.740  -31.969 1.00 68.15 ? 395 HOH   B O   1 
HETATM 1684 O  O   . HOH   G 5 .   ? -7.052  8.298   -24.131 1.00 62.46 ? 396 HOH   B O   1 
HETATM 1685 O  O   . HOH   G 5 .   ? -10.746 -10.026 -3.449  1.00 72.93 ? 397 HOH   B O   1 
HETATM 1686 O  O   . HOH   G 5 .   ? 3.223   -6.331  -19.083 1.00 70.66 ? 398 HOH   B O   1 
HETATM 1687 O  O   . HOH   G 5 .   ? -30.526 -7.152  -4.811  1.00 47.27 ? 399 HOH   B O   1 
HETATM 1688 O  O   . HOH   G 5 .   ? -1.638  -14.392 -9.847  1.00 67.52 ? 400 HOH   B O   1 
HETATM 1689 O  O   . HOH   G 5 .   ? -22.920 -13.835 -25.448 1.00 59.35 ? 401 HOH   B O   1 
HETATM 1690 O  O   . HOH   G 5 .   ? -22.121 7.927   -37.060 1.00 84.79 ? 402 HOH   B O   1 
HETATM 1691 O  O   . HOH   G 5 .   ? -17.685 17.512  -21.961 1.00 48.36 ? 403 HOH   B O   1 
HETATM 1692 O  O   . HOH   G 5 .   ? -19.095 -11.536 -13.730 1.00 41.52 ? 404 HOH   B O   1 
HETATM 1693 O  O   . HOH   G 5 .   ? -11.309 -6.582  2.119   1.00 48.62 ? 405 HOH   B O   1 
HETATM 1694 O  O   . HOH   G 5 .   ? -11.822 13.007  -14.586 1.00 60.92 ? 406 HOH   B O   1 
HETATM 1695 O  O   . HOH   G 5 .   ? -21.811 5.218   -0.569  0.50 33.76 ? 407 HOH   B O   1 
HETATM 1696 O  O   . HOH   G 5 .   ? -17.739 28.632  -14.059 1.00 53.67 ? 408 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 0.8363 0.4548 0.7499 0.0505  -0.0188 -0.0595 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.8288 0.4667 0.7264 0.0722  -0.0111 -0.0652 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.7866 0.4413 0.6843 0.0724  0.0029  -0.0432 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.8124 0.4424 0.7085 0.0697  0.0047  -0.0260 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 0.8951 0.5017 0.7782 0.0922  -0.0209 -0.0799 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 0.9816 0.6171 0.8548 0.1142  -0.0149 -0.0929 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.0007 0.6652 0.8723 0.1166  -0.0121 -0.1062 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.0100 0.6395 0.8775 0.1292  -0.0132 -0.0893 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.7084 0.4026 0.6055 0.0769  0.0121  -0.0442 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.6552 0.3678 0.5513 0.0778  0.0233  -0.0266 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.6278 0.3456 0.5134 0.0977  0.0245  -0.0300 51  MET   A C   
12   O  O   . MET   A 8   ? 0.6368 0.3662 0.5210 0.1094  0.0220  -0.0469 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.6416 0.3923 0.5462 0.0678  0.0307  -0.0235 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.6588 0.4082 0.5780 0.0482  0.0306  -0.0147 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.6457 0.4404 0.5729 0.0409  0.0378  -0.0122 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.6647 0.4563 0.6145 0.0195  0.0358  -0.0026 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.6030 0.3130 0.4813 0.1027  0.0283  -0.0142 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.6012 0.3148 0.4710 0.1225  0.0263  -0.0176 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.5993 0.3277 0.4634 0.1245  0.0328  -0.0027 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.6148 0.3430 0.4777 0.1126  0.0400  0.0132  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.6276 0.3008 0.4859 0.1360  0.0169  -0.0192 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.6683 0.3068 0.5158 0.1294  0.0183  0.0022  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.7052 0.3168 0.5582 0.1129  0.0166  0.0077  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.6997 0.3280 0.5304 0.1413  0.0196  0.0162  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7388 0.3180 0.5843 0.1052  0.0197  0.0300  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7304 0.3242 0.5471 0.1370  0.0226  0.0379  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.7626 0.3326 0.5881 0.1178  0.0239  0.0460  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.8062 0.3452 0.6214 0.1102  0.0300  0.0712  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.5810 0.3269 0.4439 0.1393  0.0302  -0.0091 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.5643 0.3222 0.4192 0.1437  0.0332  0.0022  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.5829 0.3190 0.4212 0.1631  0.0254  0.0058  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.5967 0.3199 0.4357 0.1756  0.0167  -0.0047 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.5464 0.3414 0.4140 0.1431  0.0344  -0.0064 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.5537 0.3612 0.4332 0.1557  0.0274  -0.0231 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.5345 0.3472 0.4132 0.1253  0.0414  -0.0081 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.5379 0.3822 0.4333 0.1535  0.0287  -0.0288 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.5888 0.3198 0.4096 0.1675  0.0282  0.0207  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.6205 0.3287 0.4187 0.1875  0.0203  0.0262  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.6284 0.3544 0.4166 0.1959  0.0193  0.0293  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.6147 0.3529 0.3998 0.1859  0.0297  0.0394  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.6877 0.3585 0.4633 0.1857  0.0261  0.0468  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.8076 0.4516 0.5899 0.1748  0.0266  0.0481  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.9132 0.5178 0.6725 0.1739  0.0320  0.0717  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.9556 0.5645 0.6999 0.1727  0.0429  0.0899  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 0.9830 0.5516 0.7386 0.1748  0.0257  0.0725  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.6265 0.3553 0.4112 0.2147  0.0056  0.0194  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.6325 0.3759 0.4081 0.2237  0.0007  0.0192  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.6553 0.3779 0.3945 0.2308  0.0076  0.0388  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.6908 0.3816 0.4074 0.2386  0.0088  0.0505  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.6741 0.4212 0.4542 0.2436  -0.0187 0.0043  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.7168 0.4874 0.5034 0.2463  -0.0263 -0.0030 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.7682 0.5513 0.5738 0.2600  -0.0463 -0.0203 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.7595 0.5636 0.5769 0.2587  -0.0549 -0.0279 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.7695 0.5622 0.5610 0.2745  -0.0669 -0.0271 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.8095 0.5722 0.5602 0.2931  -0.0697 -0.0177 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.7360 0.5447 0.5398 0.2724  -0.0765 -0.0354 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.6409 0.3805 0.3741 0.2281  0.0135  0.0431  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.6857 0.4116 0.3834 0.2373  0.0225  0.0614  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.7105 0.4397 0.3857 0.2590  0.0097  0.0549  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.7514 0.4663 0.3897 0.2734  0.0148  0.0683  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.6839 0.4262 0.3903 0.2184  0.0418  0.0733  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.6794 0.4276 0.3765 0.2606  -0.0058 0.0355  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.6995 0.4474 0.3777 0.2808  -0.0221 0.0269  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.6864 0.4587 0.3956 0.2751  -0.0357 0.0085  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.6587 0.4509 0.4045 0.2552  -0.0311 0.0026  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.7019 0.4704 0.3946 0.2931  -0.0532 -0.0004 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.6827 0.4694 0.4022 0.2884  -0.0683 -0.0165 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.6937 0.4891 0.4058 0.2813  -0.0577 -0.0114 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.7381 0.5235 0.4149 0.2908  -0.0456 0.0013  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7301 0.5046 0.4327 0.3131  -0.0960 -0.0300 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.8145 0.5843 0.5298 0.3237  -0.1141 -0.0403 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8030 0.5768 0.5371 0.3140  -0.1043 -0.0366 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.8825 0.6431 0.5869 0.3442  -0.1398 -0.0530 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.6651 0.4777 0.4079 0.2679  -0.0643 -0.0215 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.6723 0.4912 0.4084 0.2636  -0.0585 -0.0191 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.7166 0.5251 0.4379 0.2819  -0.0826 -0.0324 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.7070 0.5207 0.4571 0.2759  -0.1011 -0.0459 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.6601 0.5000 0.4349 0.2375  -0.0502 -0.0200 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.6589 0.5055 0.4422 0.2226  -0.0284 -0.0084 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.6739 0.5182 0.4429 0.2350  -0.0486 -0.0195 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.6543 0.5197 0.4735 0.1999  -0.0221 -0.0111 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.7505 0.5437 0.4267 0.3048  -0.0828 -0.0285 60  THR   A N   
83   N  N   C THR   A 17  ? 0.7505 0.5437 0.4267 0.3048  -0.0828 -0.0285 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.7954 0.5739 0.4485 0.3272  -0.1072 -0.0424 60  THR   A CA  
85   C  CA  C THR   A 17  ? 0.7954 0.5739 0.4485 0.3272  -0.1072 -0.0424 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.8356 0.6086 0.4462 0.3441  -0.0961 -0.0351 60  THR   A C   
87   C  C   C THR   A 17  ? 0.8356 0.6086 0.4462 0.3441  -0.0961 -0.0351 60  THR   A C   
88   O  O   A THR   A 17  ? 0.8514 0.6267 0.4404 0.3465  -0.0720 -0.0178 60  THR   A O   
89   O  O   C THR   A 17  ? 0.8514 0.6267 0.4404 0.3465  -0.0720 -0.0178 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.8492 0.6085 0.4794 0.3509  -0.1274 -0.0501 60  THR   A CB  
91   C  CB  C THR   A 17  ? 0.8492 0.6085 0.4794 0.3509  -0.1274 -0.0501 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.9206 0.6671 0.5061 0.3676  -0.1110 -0.0344 60  THR   A OG1 
93   O  OG1 C THR   A 17  ? 0.9206 0.6671 0.5061 0.3676  -0.1110 -0.0344 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.8105 0.5776 0.4823 0.3389  -0.1391 -0.0582 60  THR   A CG2 
95   C  CG2 C THR   A 17  ? 0.8105 0.5776 0.4823 0.3389  -0.1391 -0.0582 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.8552 0.6192 0.4519 0.3584  -0.1150 -0.0487 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 0.9087 0.6678 0.4614 0.3803  -0.1066 -0.0446 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 0.9599 0.6990 0.4589 0.4130  -0.1110 -0.0429 61  TRP   A C   
99   O  O   . TRP   A 18  ? 0.9913 0.7135 0.4851 0.4251  -0.1372 -0.0564 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 0.9141 0.6643 0.4678 0.3879  -0.1306 -0.0629 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 0.9370 0.6814 0.4448 0.4147  -0.1260 -0.0632 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 0.9797 0.7033 0.4350 0.4509  -0.1401 -0.0720 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 0.9276 0.6876 0.4382 0.4099  -0.1086 -0.0568 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 0.9919 0.7189 0.4160 0.4697  -0.1296 -0.0705 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 0.9621 0.7119 0.4218 0.4448  -0.1113 -0.0618 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 0.9054 0.6880 0.4542 0.3817  -0.0904 -0.0470 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 0.9653 0.7291 0.4156 0.4518  -0.0965 -0.0580 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 0.9190 0.7127 0.4589 0.3883  -0.0796 -0.0445 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 0.9435 0.7296 0.4363 0.4228  -0.0814 -0.0494 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 0.9738 0.7156 0.4335 0.4274  -0.0856 -0.0256 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.0248 0.7463 0.4275 0.4596  -0.0870 -0.0208 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.0683 0.7808 0.4244 0.4918  -0.0952 -0.0303 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.0474 0.7769 0.3990 0.4919  -0.0747 -0.0224 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.0657 0.7944 0.4531 0.4551  -0.0513 0.0078  62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.1842 0.8930 0.5045 0.4903  -0.0461 0.0178  62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.2841 0.9960 0.5859 0.4869  -0.0111 0.0486  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.2856 1.0156 0.6298 0.4551  0.0100  0.0627  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.3529 1.0470 0.5966 0.5165  -0.0060 0.0587  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.1283 0.8143 0.4474 0.5219  -0.1254 -0.0480 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.2110 0.8846 0.4785 0.5574  -0.1356 -0.0594 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.2660 0.9433 0.4785 0.5800  -0.1028 -0.0360 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.2775 0.9473 0.4734 0.5816  -0.0917 -0.0201 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.2944 0.9364 0.5366 0.5839  -0.1795 -0.0855 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.3817 1.0197 0.6744 0.5662  -0.2137 -0.1104 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.4951 1.1011 0.7523 0.6000  -0.2575 -0.1390 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.5404 1.1382 0.8485 0.5828  -0.2954 -0.1593 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.5640 1.1652 0.8859 0.5756  -0.2948 -0.1516 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.2956 0.9865 0.4845 0.5948  -0.0849 -0.0318 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.3334 1.0343 0.4742 0.6153  -0.0495 -0.0076 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.2957 1.0197 0.4704 0.5825  -0.0120 0.0233  64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.3197 1.0371 0.4629 0.5908  0.0074  0.0449  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.4344 1.1053 0.5003 0.6580  -0.0608 -0.0097 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.5785 1.2242 0.6053 0.6941  -0.0993 -0.0415 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.6209 1.2767 0.6503 0.7014  -0.1015 -0.0537 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.6391 1.2536 0.6325 0.7161  -0.1293 -0.0552 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.2329 0.9807 0.4717 0.5449  -0.0039 0.0251  65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.1863 0.9570 0.4594 0.5140  0.0299  0.0518  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.1741 0.9731 0.4287 0.5254  0.0645  0.0701  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.1854 0.9883 0.4117 0.5525  0.0592  0.0579  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.1479 0.9348 0.4895 0.4753  0.0245  0.0445  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.1607 0.9805 0.4340 0.5052  0.0991  0.0983  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.1665 1.0204 0.4337 0.5119  0.1341  0.1173  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.1170 0.9995 0.4275 0.4992  0.1303  0.1028  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.0523 0.9377 0.4140 0.4677  0.1189  0.0951  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.2310 1.0991 0.5209 0.4857  0.1681  0.1503  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.3293 1.2423 0.6414 0.4777  0.2048  0.1708  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.4355 1.3645 0.8048 0.4350  0.2244  0.1916  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.4746 1.3758 0.8441 0.4206  0.2210  0.2011  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.4448 1.4129 0.8586 0.4169  0.2412  0.1973  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.1324 1.0321 0.4179 0.5271  0.1365  0.0971  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.1232 1.0460 0.4415 0.5219  0.1301  0.0819  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.1003 1.0717 0.4449 0.5139  0.1671  0.1024  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.1267 1.1158 0.4353 0.5422  0.1898  0.1135  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.1700 1.0740 0.4437 0.5614  0.1039  0.0552  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.1557 1.0770 0.4614 0.5568  0.0940  0.0390  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.2113 1.0691 0.4624 0.5694  0.0657  0.0347  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.0479 1.0434 0.4557 0.4772  0.1725  0.1061  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.0131 1.0577 0.4541 0.4673  0.2049  0.1244  68  THR   A CA  
159  C  C   . THR   A 25  ? 0.9674 1.0336 0.4689 0.4387  0.1966  0.1151  68  THR   A C   
160  O  O   . THR   A 25  ? 0.9686 1.0099 0.4829 0.4265  0.1679  0.0964  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.0437 1.0991 0.4922 0.4501  0.2369  0.1566  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.0470 1.1521 0.5136 0.4528  0.2708  0.1751  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.0302 1.0749 0.5261 0.4075  0.2312  0.1620  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 0.9317 1.0442 0.4699 0.4285  0.2215  0.1286  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 0.9101 1.0447 0.5029 0.4039  0.2142  0.1208  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 0.9104 1.0601 0.4952 0.4303  0.2041  0.1027  69  GLY   A C   
167  O  O   . GLY   A 26  ? 0.9475 1.0721 0.4850 0.4624  0.1878  0.0868  69  GLY   A O   
168  N  N   . ASN   A 27  ? 0.8612 1.0512 0.4914 0.4186  0.2125  0.1044  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.8547 1.0578 0.4806 0.4430  0.2007  0.0864  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.8176 0.9954 0.4651 0.4244  0.1684  0.0674  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.7945 0.9454 0.4547 0.3964  0.1567  0.0678  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.8692 1.1335 0.5249 0.4502  0.2291  0.0986  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.9076 1.2032 0.6295 0.4118  0.2363  0.1085  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.9231 1.2147 0.6679 0.3805  0.2455  0.1240  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9227 1.2490 0.6755 0.4152  0.2306  0.0989  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.7962 0.9809 0.4459 0.4411  0.1538  0.0511  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.7867 0.9445 0.4515 0.4260  0.1237  0.0349  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.7672 0.9605 0.4697 0.4226  0.1241  0.0322  71  SER   A C   
179  O  O   . SER   A 28  ? 0.7757 0.9650 0.4646 0.4471  0.1089  0.0171  71  SER   A O   
180  C  CB  . SER   A 28  ? 0.8245 0.9366 0.4447 0.4519  0.0948  0.0138  71  SER   A CB  
181  O  OG  . SER   A 28  ? 0.8811 0.9714 0.4581 0.4705  0.0971  0.0145  71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.7297 0.9568 0.4799 0.3934  0.1397  0.0462  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.7003 0.9663 0.4881 0.3922  0.1404  0.0438  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.6869 0.9260 0.4815 0.3823  0.1108  0.0290  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.6747 0.8785 0.4685 0.3585  0.0972  0.0275  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.6922 0.9975 0.5280 0.3621  0.1639  0.0631  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.7072 0.9749 0.5346 0.3362  0.1616  0.0698  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.7173 0.9499 0.4888 0.3630  0.1572  0.0644  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.6663 0.9233 0.4684 0.4008  0.1018  0.0190  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.6821 0.9151 0.4904 0.3927  0.0746  0.0071  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.6368 0.9136 0.4958 0.3737  0.0810  0.0132  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.6089 0.9320 0.4893 0.3900  0.0915  0.0138  73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.7376 0.9514 0.5148 0.4285  0.0546  -0.0100 73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.8412 1.0020 0.5688 0.4449  0.0395  -0.0199 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 0.9322 1.0732 0.6302 0.4818  0.0186  -0.0377 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.0130 1.1093 0.6639 0.5035  0.0046  -0.0490 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.0498 1.0898 0.6825 0.4942  -0.0223 -0.0578 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.0609 1.0829 0.7157 0.4638  -0.0348 -0.0546 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.0269 1.0293 0.6198 0.5153  -0.0367 -0.0696 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.6197 0.8841 0.4992 0.3399  0.0750  0.0174  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.5876 0.8904 0.5148 0.3195  0.0795  0.0226  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.5775 0.8588 0.5090 0.3073  0.0551  0.0141  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.5957 0.8328 0.5063 0.2932  0.0427  0.0120  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.5802 0.8912 0.5301 0.2886  0.0972  0.0369  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.5984 0.9268 0.5424 0.2963  0.1238  0.0497  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.6158 0.9241 0.5612 0.2691  0.1328  0.0610  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.5892 0.9804 0.5682 0.3076  0.1448  0.0576  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.5487 0.8656 0.5123 0.3089  0.0503  0.0111  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.5540 0.8541 0.5220 0.2973  0.0280  0.0045  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.5226 0.8332 0.5212 0.2630  0.0347  0.0120  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.4992 0.8543 0.5375 0.2539  0.0509  0.0191  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.5811 0.9158 0.5702 0.3166  0.0176  -0.0032 75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.7013 1.0168 0.6572 0.3517  0.0034  -0.0138 75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.7410 1.0090 0.6555 0.3589  -0.0031 -0.0164 75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.7315 1.0785 0.7042 0.3722  -0.0035 -0.0205 75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.5064 0.7753 0.4865 0.2440  0.0237  0.0110  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.4801 0.7529 0.4833 0.2141  0.0282  0.0160  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.4767 0.7248 0.4713 0.2023  0.0078  0.0095  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.5033 0.7210 0.4674 0.2136  -0.0077 0.0043  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.4991 0.7510 0.4907 0.2002  0.0435  0.0243  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5001 0.7722 0.4922 0.2138  0.0640  0.0321  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.5336 0.7341 0.4861 0.1982  0.0326  0.0208  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.4504 0.7101 0.4705 0.1798  0.0077  0.0103  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.4492 0.6869 0.4591 0.1682  -0.0095 0.0044  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.4395 0.6565 0.4467 0.1448  -0.0020 0.0078  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.4299 0.6615 0.4583 0.1344  0.0136  0.0141  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.4291 0.7011 0.4721 0.1667  -0.0214 -0.0019 77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.4368 0.6190 0.4159 0.1382  -0.0119 0.0047  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.4434 0.6049 0.4166 0.1195  -0.0059 0.0062  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.4552 0.6132 0.4287 0.1100  -0.0199 -0.0012 78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.4749 0.6187 0.4249 0.1185  -0.0333 -0.0047 78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.4623 0.5861 0.3994 0.1226  -0.0035 0.0092  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.4930 0.5954 0.4217 0.1065  0.0018  0.0097  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.4772 0.5917 0.4292 0.0957  0.0155  0.0133  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.5320 0.6022 0.4308 0.1096  0.0021  0.0122  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.4309 0.6017 0.4307 0.0940  -0.0185 -0.0038 79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.4375 0.6045 0.4360 0.0872  -0.0345 -0.0135 79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.4448 0.5772 0.4128 0.0790  -0.0331 -0.0154 79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.4558 0.5704 0.4100 0.0769  -0.0200 -0.0092 79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.4207 0.6197 0.4655 0.0760  -0.0397 -0.0184 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.4469 0.6464 0.5159 0.0576  -0.0274 -0.0146 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.4593 0.6307 0.5050 0.0534  -0.0172 -0.0109 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.4562 0.6836 0.5693 0.0468  -0.0292 -0.0154 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.4550 0.5791 0.4113 0.0765  -0.0473 -0.0247 80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.4746 0.5700 0.4007 0.0717  -0.0459 -0.0276 80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.4735 0.5635 0.4146 0.0581  -0.0347 -0.0278 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.5005 0.5685 0.4187 0.0565  -0.0266 -0.0265 80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.5131 0.6034 0.4223 0.0748  -0.0645 -0.0387 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.5829 0.6451 0.4536 0.0746  -0.0621 -0.0413 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.6871 0.7431 0.5329 0.0823  -0.0809 -0.0515 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.6610 0.7178 0.5142 0.0772  -0.0915 -0.0645 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.7378 0.7862 0.5554 0.0942  -0.0866 -0.0468 80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.4292 0.5396 0.4104 0.0485  -0.0326 -0.0274 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.4377 0.5385 0.4317 0.0360  -0.0224 -0.0257 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.4213 0.5186 0.4141 0.0378  -0.0034 -0.0129 81  SER   A C   
256  O  O   . SER   A 38  ? 0.4258 0.5144 0.4282 0.0291  0.0056  -0.0096 81  SER   A O   
257  C  CB  . SER   A 38  ? 0.4566 0.5765 0.4937 0.0229  -0.0283 -0.0289 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.5139 0.6304 0.5490 0.0209  -0.0484 -0.0436 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.4055 0.5063 0.3844 0.0502  0.0008  -0.0066 82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.4098 0.5052 0.3836 0.0546  0.0156  0.0033  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.4156 0.5357 0.4185 0.0542  0.0251  0.0115  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.4246 0.5398 0.4238 0.0571  0.0380  0.0198  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.3959 0.5439 0.4272 0.0519  0.0192  0.0097  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.3972 0.5751 0.4597 0.0519  0.0310  0.0193  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.4007 0.5966 0.4567 0.0713  0.0318  0.0212  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.3962 0.6001 0.4498 0.0790  0.0176  0.0136  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4214 0.6270 0.5280 0.0382  0.0247  0.0167  83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.5502 0.7384 0.6671 0.0196  0.0178  0.0110  83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.5731 0.7393 0.6818 0.0127  0.0280  0.0167  83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.6184 0.8135 0.7501 0.0135  0.0004  -0.0003 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.4032 0.6060 0.4565 0.0806  0.0475  0.0311  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.4143 0.6369 0.4641 0.1010  0.0492  0.0324  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4155 0.6854 0.5101 0.0993  0.0558  0.0368  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4067 0.6906 0.5300 0.0839  0.0679  0.0453  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.4132 0.6222 0.4374 0.1144  0.0624  0.0396  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.4254 0.5949 0.4098 0.1211  0.0537  0.0344  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.4413 0.6011 0.4062 0.1347  0.0399  0.0273  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.4239 0.5656 0.3928 0.1129  0.0584  0.0368  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.4658 0.5901 0.3992 0.1382  0.0325  0.0243  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.4507 0.5609 0.3898 0.1177  0.0506  0.0323  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.4673 0.5692 0.3900 0.1294  0.0384  0.0268  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4197 0.7144 0.5210 0.1158  0.0489  0.0321  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4242 0.7702 0.5708 0.1176  0.0562  0.0360  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.4543 0.8190 0.5893 0.1468  0.0583  0.0346  85  SER   A C   
285  O  O   . SER   A 42  ? 0.4675 0.8037 0.5643 0.1626  0.0458  0.0271  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4193 0.7851 0.6007 0.1050  0.0385  0.0270  85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.4596 0.8112 0.6161 0.1190  0.0170  0.0146  85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4643 0.8761 0.6320 0.1546  0.0745  0.0422  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.5031 0.9355 0.6604 0.1854  0.0769  0.0393  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5347 0.9876 0.7086 0.1960  0.0554  0.0265  86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.5181 1.0003 0.7358 0.1805  0.0486  0.0244  86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.4897 0.9725 0.6796 0.1912  0.1037  0.0523  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5346 1.0044 0.7075 0.1867  0.1280  0.0674  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.5168 1.0430 0.7247 0.1936  0.1556  0.0817  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.5790 1.0046 0.6903 0.2091  0.1251  0.0629  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5747 1.0137 0.7159 0.2234  0.0440  0.0180  87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.6045 1.0609 0.7570 0.2382  0.0229  0.0063  87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.6266 1.1332 0.8013 0.2645  0.0348  0.0068  87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6441 1.1400 0.7880 0.2858  0.0458  0.0088  87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6468 1.0491 0.7464 0.2516  0.0003  -0.0029 87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6505 1.0691 0.7567 0.2726  -0.0211 -0.0139 87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6695 1.0271 0.7481 0.2268  -0.0091 -0.0027 87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.6246 1.1875 0.8535 0.2640  0.0334  0.0047  88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.6362 1.2550 0.8917 0.2904  0.0467  0.0051  88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.6460 1.2898 0.9187 0.3115  0.0230  -0.0093 88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.6754 1.2906 0.9364 0.3053  -0.0040 -0.0187 88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.6448 1.3224 0.9591 0.2730  0.0751  0.0197  88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.7426 1.3945 1.0386 0.2537  0.0985  0.0354  88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.8671 1.5397 1.1502 0.2745  0.1285  0.0468  88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.8733 1.5765 1.1551 0.3073  0.1311  0.0408  88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.9252 1.5825 1.1969 0.2598  0.1491  0.0613  88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.8513 0.7648 0.7833 0.1851  0.0017  -0.0851 16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.8685 0.7576 0.7878 0.1864  -0.0010 -0.0793 16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.8601 0.7579 0.7904 0.1864  -0.0044 -0.0777 16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.8554 0.7764 0.8037 0.1881  -0.0072 -0.0831 16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.8472 0.7268 0.7668 0.1854  -0.0049 -0.0704 17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.8288 0.7135 0.7553 0.1877  -0.0096 -0.0696 17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.7988 0.6997 0.7416 0.1736  -0.0074 -0.0651 17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.8010 0.6971 0.7402 0.1632  -0.0020 -0.0574 17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.8703 0.7315 0.7776 0.1956  -0.0115 -0.0641 17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 0.9108 0.7767 0.8229 0.2031  -0.0188 -0.0665 17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 0.9846 0.8294 0.8759 0.2154  -0.0212 -0.0625 17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 1.0053 0.8329 0.8803 0.2136  -0.0151 -0.0540 17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 0.9794 0.8251 0.8704 0.2272  -0.0294 -0.0676 17  GLU   B OE2 
325  N  N   . THR   B 9   ? 0.7667 0.6868 0.7280 0.1735  -0.0123 -0.0702 18  THR   B N   
326  C  CA  . THR   B 9   ? 0.7433 0.6787 0.7216 0.1607  -0.0120 -0.0667 18  THR   B CA  
327  C  C   . THR   B 9   ? 0.7108 0.6417 0.6913 0.1639  -0.0204 -0.0666 18  THR   B C   
328  O  O   . THR   B 9   ? 0.7126 0.6513 0.7049 0.1542  -0.0221 -0.0636 18  THR   B O   
329  C  CB  . THR   B 9   ? 0.7559 0.7182 0.7559 0.1563  -0.0113 -0.0718 18  THR   B CB  
330  O  OG1 . THR   B 9   ? 0.7649 0.7357 0.7742 0.1669  -0.0198 -0.0802 18  THR   B OG1 
331  C  CG2 . THR   B 9   ? 0.7664 0.7337 0.7619 0.1564  -0.0038 -0.0733 18  THR   B CG2 
332  N  N   . THR   B 10  ? 0.6830 0.5993 0.6502 0.1785  -0.0264 -0.0697 19  THR   B N   
333  C  CA  . THR   B 10  ? 0.6566 0.5667 0.6223 0.1849  -0.0356 -0.0708 19  THR   B CA  
334  C  C   . THR   B 10  ? 0.6151 0.5173 0.5739 0.1773  -0.0326 -0.0619 19  THR   B C   
335  O  O   . THR   B 10  ? 0.6139 0.5071 0.5597 0.1738  -0.0240 -0.0546 19  THR   B O   
336  C  CB  . THR   B 10  ? 0.6926 0.5856 0.6388 0.2037  -0.0402 -0.0741 19  THR   B CB  
337  O  OG1 . THR   B 10  ? 0.7268 0.6259 0.6767 0.2112  -0.0418 -0.0820 19  THR   B OG1 
338  C  CG2 . THR   B 10  ? 0.7026 0.5905 0.6468 0.2140  -0.0517 -0.0779 19  THR   B CG2 
339  N  N   . ASP   B 11  ? 0.5787 0.4844 0.5469 0.1746  -0.0405 -0.0629 20  ASP   B N   
340  C  CA  . ASP   B 11  ? 0.5794 0.4774 0.5403 0.1707  -0.0404 -0.0562 20  ASP   B CA  
341  C  C   . ASP   B 11  ? 0.5810 0.4619 0.5172 0.1841  -0.0387 -0.0523 20  ASP   B C   
342  O  O   . ASP   B 11  ? 0.5958 0.4690 0.5220 0.1985  -0.0423 -0.0566 20  ASP   B O   
343  C  CB  . ASP   B 11  ? 0.6065 0.5057 0.5779 0.1711  -0.0535 -0.0605 20  ASP   B CB  
344  C  CG  . ASP   B 11  ? 0.6570 0.5702 0.6509 0.1543  -0.0548 -0.0597 20  ASP   B CG  
345  O  OD1 . ASP   B 11  ? 0.6209 0.5469 0.6243 0.1435  -0.0453 -0.0571 20  ASP   B OD1 
346  O  OD2 . ASP   B 11  ? 0.6942 0.6045 0.6952 0.1524  -0.0657 -0.0615 20  ASP   B OD2 
347  N  N   . GLY   B 12  ? 0.5485 0.4249 0.4753 0.1799  -0.0329 -0.0440 21  GLY   B N   
348  C  CA  . GLY   B 12  ? 0.5543 0.4185 0.4596 0.1912  -0.0300 -0.0382 21  GLY   B CA  
349  C  C   . GLY   B 12  ? 0.5404 0.4046 0.4393 0.1822  -0.0183 -0.0279 21  GLY   B C   
350  O  O   . GLY   B 12  ? 0.5035 0.3761 0.4135 0.1674  -0.0136 -0.0258 21  GLY   B O   
351  N  N   . VAL   B 13  ? 0.5182 0.3743 0.3997 0.1910  -0.0140 -0.0212 22  VAL   B N   
352  C  CA  . VAL   B 13  ? 0.4998 0.3568 0.3757 0.1832  -0.0034 -0.0107 22  VAL   B CA  
353  C  C   . VAL   B 13  ? 0.5030 0.3526 0.3740 0.1805  0.0037  -0.0072 22  VAL   B C   
354  O  O   . VAL   B 13  ? 0.5274 0.3669 0.3893 0.1916  0.0013  -0.0099 22  VAL   B O   
355  C  CB  . VAL   B 13  ? 0.5225 0.3789 0.3846 0.1926  -0.0022 -0.0036 22  VAL   B CB  
356  C  CG1 . VAL   B 13  ? 0.5300 0.3762 0.3745 0.2109  -0.0039 -0.0026 22  VAL   B CG1 
357  C  CG2 . VAL   B 13  ? 0.5533 0.4161 0.4146 0.1824  0.0082  0.0071  22  VAL   B CG2 
358  N  N   . TYR   B 14  ? 0.4819 0.3349 0.3588 0.1658  0.0111  -0.0023 23  TYR   B N   
359  C  CA  . TYR   B 14  ? 0.5005 0.3439 0.3734 0.1618  0.0161  -0.0001 23  TYR   B CA  
360  C  C   . TYR   B 14  ? 0.5135 0.3561 0.3831 0.1521  0.0244  0.0112  23  TYR   B C   
361  O  O   . TYR   B 14  ? 0.5072 0.3613 0.3836 0.1438  0.0268  0.0147  23  TYR   B O   
362  C  CB  . TYR   B 14  ? 0.4977 0.3464 0.3839 0.1517  0.0153  -0.0076 23  TYR   B CB  
363  C  CG  . TYR   B 14  ? 0.4900 0.3417 0.3827 0.1588  0.0084  -0.0186 23  TYR   B CG  
364  C  CD1 . TYR   B 14  ? 0.4884 0.3492 0.3892 0.1627  0.0017  -0.0236 23  TYR   B CD1 
365  C  CD2 . TYR   B 14  ? 0.5205 0.3647 0.4100 0.1632  0.0074  -0.0238 23  TYR   B CD2 
366  C  CE1 . TYR   B 14  ? 0.5048 0.3708 0.4144 0.1682  -0.0051 -0.0332 23  TYR   B CE1 
367  C  CE2 . TYR   B 14  ? 0.5389 0.3892 0.4356 0.1708  0.0010  -0.0340 23  TYR   B CE2 
368  C  CZ  . TYR   B 14  ? 0.5447 0.4072 0.4529 0.1723  -0.0050 -0.0384 23  TYR   B CZ  
369  O  OH  . TYR   B 14  ? 0.5965 0.4672 0.5145 0.1787  -0.0116 -0.0481 23  TYR   B OH  
370  N  N   . ARG   B 15  ? 0.5149 0.3437 0.3749 0.1523  0.0281  0.0167  24  ARG   B N   
371  C  CA  . ARG   B 15  ? 0.5172 0.3449 0.3773 0.1405  0.0351  0.0273  24  ARG   B CA  
372  C  C   . ARG   B 15  ? 0.5082 0.3352 0.3782 0.1272  0.0345  0.0220  24  ARG   B C   
373  O  O   . ARG   B 15  ? 0.5135 0.3339 0.3838 0.1302  0.0304  0.0130  24  ARG   B O   
374  C  CB  . ARG   B 15  ? 0.5427 0.3523 0.3884 0.1448  0.0382  0.0358  24  ARG   B CB  
375  C  CG  . ARG   B 15  ? 0.5823 0.3903 0.4144 0.1609  0.0388  0.0406  24  ARG   B CG  
376  C  CD  . ARG   B 15  ? 0.5975 0.3857 0.4139 0.1655  0.0420  0.0494  24  ARG   B CD  
377  N  NE  . ARG   B 15  ? 0.6277 0.4123 0.4282 0.1841  0.0415  0.0520  24  ARG   B NE  
378  C  CZ  . ARG   B 15  ? 0.6653 0.4589 0.4587 0.1899  0.0472  0.0630  24  ARG   B CZ  
379  N  NH1 . ARG   B 15  ? 0.6044 0.4122 0.4066 0.1775  0.0545  0.0732  24  ARG   B NH1 
380  N  NH2 . ARG   B 15  ? 0.7045 0.4941 0.4814 0.2092  0.0456  0.0637  24  ARG   B NH2 
381  N  N   . VAL   B 16  ? 0.5137 0.3473 0.3907 0.1141  0.0384  0.0277  25  VAL   B N   
382  C  CA  . VAL   B 16  ? 0.5140 0.3453 0.3979 0.1023  0.0375  0.0235  25  VAL   B CA  
383  C  C   . VAL   B 16  ? 0.5260 0.3432 0.4052 0.0946  0.0401  0.0325  25  VAL   B C   
384  O  O   . VAL   B 16  ? 0.5198 0.3435 0.4007 0.0894  0.0448  0.0434  25  VAL   B O   
385  C  CB  . VAL   B 16  ? 0.5167 0.3660 0.4123 0.0928  0.0385  0.0227  25  VAL   B CB  
386  C  CG1 . VAL   B 16  ? 0.5286 0.3741 0.4289 0.0823  0.0372  0.0183  25  VAL   B CG1 
387  C  CG2 . VAL   B 16  ? 0.4872 0.3482 0.3875 0.0990  0.0356  0.0156  25  VAL   B CG2 
388  N  N   . MET   B 17  ? 0.5563 0.3542 0.4288 0.0952  0.0367  0.0283  26  MET   B N   
389  C  CA  . MET   B 17  ? 0.5889 0.3670 0.4549 0.0887  0.0370  0.0361  26  MET   B CA  
390  C  C   . MET   B 17  ? 0.6217 0.3914 0.4919 0.0775  0.0329  0.0311  26  MET   B C   
391  O  O   . MET   B 17  ? 0.6157 0.3896 0.4887 0.0796  0.0292  0.0195  26  MET   B O   
392  C  CB  . MET   B 17  ? 0.6103 0.3664 0.4605 0.1012  0.0343  0.0347  26  MET   B CB  
393  C  CG  . MET   B 17  ? 0.6286 0.3902 0.4718 0.1160  0.0362  0.0365  26  MET   B CG  
394  S  SD  . MET   B 17  ? 0.6209 0.3901 0.4611 0.1149  0.0445  0.0543  26  MET   B SD  
395  C  CE  . MET   B 17  ? 0.6693 0.4096 0.4988 0.1069  0.0459  0.0666  26  MET   B CE  
396  N  N   . THR   B 18  ? 0.6589 0.4145 0.5282 0.0666  0.0327  0.0398  27  THR   B N   
397  C  CA  . THR   B 18  ? 0.7004 0.4413 0.5706 0.0573  0.0263  0.0344  27  THR   B CA  
398  C  C   . THR   B 18  ? 0.7254 0.4365 0.5852 0.0537  0.0232  0.0416  27  THR   B C   
399  O  O   . THR   B 18  ? 0.7011 0.4086 0.5585 0.0515  0.0283  0.0554  27  THR   B O   
400  C  CB  . THR   B 18  ? 0.7343 0.4913 0.6193 0.0428  0.0267  0.0361  27  THR   B CB  
401  O  OG1 . THR   B 18  ? 0.7753 0.5147 0.6585 0.0362  0.0185  0.0291  27  THR   B OG1 
402  C  CG2 . THR   B 18  ? 0.7301 0.4961 0.6234 0.0320  0.0325  0.0519  27  THR   B CG2 
403  N  N   . ARG   B 19  ? 0.7706 0.4594 0.6233 0.0533  0.0146  0.0328  28  ARG   B N   
404  C  CA  . ARG   B 19  ? 0.8347 0.4907 0.6774 0.0476  0.0092  0.0387  28  ARG   B CA  
405  C  C   . ARG   B 19  ? 0.8687 0.5173 0.7206 0.0301  0.0030  0.0396  28  ARG   B C   
406  O  O   . ARG   B 19  ? 0.8898 0.5084 0.7345 0.0236  -0.0039 0.0431  28  ARG   B O   
407  C  CB  . ARG   B 19  ? 0.8934 0.5227 0.7170 0.0626  0.0021  0.0288  28  ARG   B CB  
408  C  CG  . ARG   B 19  ? 0.9660 0.5983 0.7803 0.0779  0.0074  0.0314  28  ARG   B CG  
409  C  CD  . ARG   B 19  ? 1.0652 0.6661 0.8587 0.0910  0.0008  0.0268  28  ARG   B CD  
410  N  NE  . ARG   B 19  ? 1.1391 0.7453 0.9243 0.1065  0.0053  0.0284  28  ARG   B NE  
411  C  CZ  . ARG   B 19  ? 1.1993 0.8125 0.9799 0.1234  0.0026  0.0151  28  ARG   B CZ  
412  N  NH1 . ARG   B 19  ? 1.2033 0.8202 0.9861 0.1273  -0.0033 0.0002  28  ARG   B NH1 
413  N  NH2 . ARG   B 19  ? 1.2107 0.8284 0.9846 0.1369  0.0056  0.0168  28  ARG   B NH2 
414  N  N   . ARG   B 20  ? 0.8856 0.5604 0.7534 0.0223  0.0048  0.0368  29  ARG   B N   
415  C  CA  . ARG   B 20  ? 0.9204 0.5917 0.7982 0.0066  -0.0018 0.0363  29  ARG   B CA  
416  C  C   . ARG   B 20  ? 0.9350 0.6010 0.8222 -0.0104 0.0000  0.0536  29  ARG   B C   
417  O  O   . ARG   B 20  ? 0.9508 0.5953 0.8396 -0.0227 -0.0090 0.0548  29  ARG   B O   
418  C  CB  . ARG   B 20  ? 0.9453 0.6479 0.8364 0.0045  0.0004  0.0297  29  ARG   B CB  
419  C  CG  . ARG   B 20  ? 1.0288 0.7298 0.9302 -0.0101 -0.0073 0.0275  29  ARG   B CG  
420  C  CD  . ARG   B 20  ? 1.0928 0.8238 1.0047 -0.0104 -0.0050 0.0211  29  ARG   B CD  
421  N  NE  . ARG   B 20  ? 1.1467 0.9073 1.0693 -0.0110 0.0061  0.0309  29  ARG   B NE  
422  C  CZ  . ARG   B 20  ? 1.1916 0.9684 1.1293 -0.0235 0.0093  0.0419  29  ARG   B CZ  
423  N  NH1 . ARG   B 20  ? 1.1997 0.9667 1.1459 -0.0384 0.0023  0.0452  29  ARG   B NH1 
424  N  NH2 . ARG   B 20  ? 1.1881 0.9914 1.1325 -0.0207 0.0189  0.0493  29  ARG   B NH2 
425  N  N   . LEU   B 21  ? 0.9223 0.6073 0.8150 -0.0106 0.0113  0.0673  30  LEU   B N   
426  C  CA  . LEU   B 21  ? 0.9175 0.6041 0.8203 -0.0257 0.0159  0.0861  30  LEU   B CA  
427  C  C   . LEU   B 21  ? 0.9067 0.5614 0.7937 -0.0235 0.0160  0.0965  30  LEU   B C   
428  O  O   . LEU   B 21  ? 0.9205 0.5465 0.7893 -0.0128 0.0089  0.0872  30  LEU   B O   
429  C  CB  . LEU   B 21  ? 0.9190 0.6447 0.8334 -0.0238 0.0285  0.0951  30  LEU   B CB  
430  C  CG  . LEU   B 21  ? 0.9362 0.6948 0.8711 -0.0333 0.0301  0.0944  30  LEU   B CG  
431  C  CD1 . LEU   B 21  ? 0.9536 0.7037 0.8952 -0.0431 0.0184  0.0825  30  LEU   B CD1 
432  C  CD2 . LEU   B 21  ? 0.9343 0.7215 0.8690 -0.0196 0.0370  0.0890  30  LEU   B CD2 
433  N  N   . LEU   B 22  ? 0.8766 0.5365 0.7699 -0.0331 0.0239  0.1163  31  LEU   B N   
434  C  CA  . LEU   B 22  ? 0.8674 0.4993 0.7452 -0.0311 0.0256  0.1286  31  LEU   B CA  
435  C  C   . LEU   B 22  ? 0.8415 0.4741 0.7003 -0.0075 0.0311  0.1240  31  LEU   B C   
436  O  O   . LEU   B 22  ? 0.8318 0.4961 0.6956 0.0020  0.0388  0.1214  31  LEU   B O   
437  C  CB  . LEU   B 22  ? 0.8639 0.5107 0.7552 -0.0460 0.0354  0.1520  31  LEU   B CB  
438  C  CG  . LEU   B 22  ? 0.8889 0.5063 0.7662 -0.0482 0.0377  0.1685  31  LEU   B CG  
439  C  CD1 . LEU   B 22  ? 0.9071 0.4811 0.7807 -0.0627 0.0235  0.1678  31  LEU   B CD1 
440  C  CD2 . LEU   B 22  ? 0.8944 0.5376 0.7846 -0.0582 0.0514  0.1922  31  LEU   B CD2 
441  N  N   . GLY   B 23  ? 0.8198 0.4170 0.6569 0.0026  0.0256  0.1211  32  GLY   B N   
442  C  CA  . GLY   B 23  ? 0.8006 0.3952 0.6192 0.0254  0.0283  0.1150  32  GLY   B CA  
443  C  C   . GLY   B 23  ? 0.7637 0.3852 0.5870 0.0386  0.0285  0.0976  32  GLY   B C   
444  O  O   . GLY   B 23  ? 0.7518 0.3777 0.5829 0.0352  0.0219  0.0839  32  GLY   B O   
445  N  N   . SER   B 24  ? 0.7535 0.3916 0.5711 0.0540  0.0356  0.0983  33  SER   B N   
446  C  CA  . SER   B 24  ? 0.7505 0.4136 0.5735 0.0654  0.0358  0.0838  33  SER   B CA  
447  C  C   . SER   B 24  ? 0.7186 0.4147 0.5543 0.0622  0.0454  0.0933  33  SER   B C   
448  O  O   . SER   B 24  ? 0.7364 0.4361 0.5666 0.0655  0.0530  0.1075  33  SER   B O   
449  C  CB  . SER   B 24  ? 0.7971 0.4514 0.6033 0.0867  0.0337  0.0752  33  SER   B CB  
450  O  OG  . SER   B 24  ? 0.8488 0.4707 0.6405 0.0914  0.0249  0.0680  33  SER   B OG  
451  N  N   . THR   B 25  ? 0.6842 0.4032 0.5360 0.0550  0.0451  0.0870  34  THR   B N   
452  C  CA  . THR   B 25  ? 0.6499 0.4006 0.5147 0.0511  0.0529  0.0948  34  THR   B CA  
453  C  C   . THR   B 25  ? 0.6317 0.4047 0.4998 0.0623  0.0529  0.0832  34  THR   B C   
454  O  O   . THR   B 25  ? 0.6214 0.3949 0.4930 0.0630  0.0471  0.0692  34  THR   B O   
455  C  CB  . THR   B 25  ? 0.6756 0.4357 0.5583 0.0308  0.0522  0.0994  34  THR   B CB  
456  O  OG1 . THR   B 25  ? 0.7064 0.4442 0.5878 0.0184  0.0509  0.1106  34  THR   B OG1 
457  C  CG2 . THR   B 25  ? 0.6661 0.4607 0.5628 0.0271  0.0600  0.1075  34  THR   B CG2 
458  N  N   . GLN   B 26  ? 0.6028 0.3942 0.4694 0.0714  0.0593  0.0897  35  GLN   B N   
459  C  CA  . GLN   B 26  ? 0.5877 0.3985 0.4576 0.0810  0.0583  0.0799  35  GLN   B CA  
460  C  C   . GLN   B 26  ? 0.5889 0.4241 0.4749 0.0704  0.0601  0.0807  35  GLN   B C   
461  O  O   . GLN   B 26  ? 0.5904 0.4419 0.4813 0.0669  0.0664  0.0924  35  GLN   B O   
462  C  CB  . GLN   B 26  ? 0.5587 0.3757 0.4173 0.0983  0.0617  0.0836  35  GLN   B CB  
463  C  CG  . GLN   B 26  ? 0.5361 0.3690 0.3980 0.1077  0.0582  0.0723  35  GLN   B CG  
464  C  CD  . GLN   B 26  ? 0.5827 0.4185 0.4321 0.1259  0.0592  0.0743  35  GLN   B CD  
465  O  OE1 . GLN   B 26  ? 0.5965 0.4158 0.4320 0.1361  0.0586  0.0757  35  GLN   B OE1 
466  N  NE2 . GLN   B 26  ? 0.5548 0.4101 0.4071 0.1316  0.0598  0.0740  35  GLN   B NE2 
467  N  N   . VAL   B 27  ? 0.5804 0.4193 0.4736 0.0668  0.0549  0.0684  36  VAL   B N   
468  C  CA  . VAL   B 27  ? 0.5657 0.4260 0.4722 0.0581  0.0556  0.0679  36  VAL   B CA  
469  C  C   . VAL   B 27  ? 0.5320 0.4103 0.4389 0.0681  0.0558  0.0632  36  VAL   B C   
470  O  O   . VAL   B 27  ? 0.5254 0.4223 0.4408 0.0636  0.0570  0.0645  36  VAL   B O   
471  C  CB  . VAL   B 27  ? 0.5832 0.4377 0.4968 0.0470  0.0501  0.0591  36  VAL   B CB  
472  C  CG1 . VAL   B 27  ? 0.6141 0.4513 0.5287 0.0352  0.0485  0.0647  36  VAL   B CG1 
473  C  CG2 . VAL   B 27  ? 0.5993 0.4446 0.5072 0.0549  0.0451  0.0456  36  VAL   B CG2 
474  N  N   . GLY   B 28  ? 0.5077 0.3798 0.4058 0.0815  0.0534  0.0571  37  GLY   B N   
475  C  CA  . GLY   B 28  ? 0.4865 0.3719 0.3839 0.0913  0.0519  0.0531  37  GLY   B CA  
476  C  C   . GLY   B 28  ? 0.4978 0.3734 0.3866 0.1049  0.0476  0.0457  37  GLY   B C   
477  O  O   . GLY   B 28  ? 0.5033 0.3636 0.3840 0.1099  0.0473  0.0460  37  GLY   B O   
478  N  N   . VAL   B 29  ? 0.4673 0.3511 0.3581 0.1108  0.0435  0.0391  38  VAL   B N   
479  C  CA  . VAL   B 29  ? 0.4823 0.3609 0.3678 0.1237  0.0378  0.0317  38  VAL   B CA  
480  C  C   . VAL   B 29  ? 0.4847 0.3697 0.3793 0.1206  0.0324  0.0225  38  VAL   B C   
481  O  O   . VAL   B 29  ? 0.4632 0.3578 0.3648 0.1115  0.0336  0.0234  38  VAL   B O   
482  C  CB  . VAL   B 29  ? 0.4898 0.3731 0.3652 0.1374  0.0382  0.0370  38  VAL   B CB  
483  C  CG1 . VAL   B 29  ? 0.4796 0.3570 0.3492 0.1518  0.0302  0.0286  38  VAL   B CG1 
484  C  CG2 . VAL   B 29  ? 0.5043 0.3834 0.3706 0.1401  0.0451  0.0484  38  VAL   B CG2 
485  N  N   . GLY   B 30  ? 0.4731 0.3532 0.3682 0.1274  0.0266  0.0142  39  GLY   B N   
486  C  CA  . GLY   B 30  ? 0.4704 0.3572 0.3755 0.1237  0.0216  0.0071  39  GLY   B CA  
487  C  C   . GLY   B 30  ? 0.4731 0.3568 0.3786 0.1339  0.0137  -0.0001 39  GLY   B C   
488  O  O   . GLY   B 30  ? 0.4732 0.3488 0.3703 0.1452  0.0118  -0.0011 39  GLY   B O   
489  N  N   . VAL   B 31  ? 0.4389 0.3286 0.3544 0.1297  0.0088  -0.0051 40  VAL   B N   
490  C  CA  . VAL   B 31  ? 0.4322 0.3208 0.3523 0.1365  -0.0003 -0.0121 40  VAL   B CA  
491  C  C   . VAL   B 31  ? 0.4407 0.3359 0.3754 0.1293  -0.0017 -0.0183 40  VAL   B C   
492  O  O   . VAL   B 31  ? 0.4156 0.3188 0.3591 0.1176  0.0014  -0.0172 40  VAL   B O   
493  C  CB  . VAL   B 31  ? 0.4627 0.3526 0.3828 0.1372  -0.0066 -0.0115 40  VAL   B CB  
494  C  CG1 . VAL   B 31  ? 0.4716 0.3595 0.3993 0.1415  -0.0178 -0.0190 40  VAL   B CG1 
495  C  CG2 . VAL   B 31  ? 0.4767 0.3630 0.3816 0.1476  -0.0059 -0.0061 40  VAL   B CG2 
496  N  N   . MET   B 32  ? 0.4314 0.3250 0.3688 0.1370  -0.0064 -0.0248 41  MET   B N   
497  C  CA  . MET   B 32  ? 0.4304 0.3342 0.3833 0.1320  -0.0080 -0.0309 41  MET   B CA  
498  C  C   . MET   B 32  ? 0.4468 0.3537 0.4100 0.1334  -0.0186 -0.0350 41  MET   B C   
499  O  O   . MET   B 32  ? 0.4624 0.3610 0.4191 0.1454  -0.0267 -0.0383 41  MET   B O   
500  C  CB  . MET   B 32  ? 0.4394 0.3408 0.3898 0.1400  -0.0074 -0.0361 41  MET   B CB  
501  C  CG  . MET   B 32  ? 0.4639 0.3796 0.4303 0.1359  -0.0079 -0.0421 41  MET   B CG  
502  S  SD  . MET   B 32  ? 0.4930 0.4153 0.4602 0.1240  0.0031  -0.0386 41  MET   B SD  
503  C  CE  . MET   B 32  ? 0.5396 0.4452 0.4888 0.1330  0.0062  -0.0391 41  MET   B CE  
504  N  N   . GLN   B 33  ? 0.4148 0.3319 0.3925 0.1214  -0.0190 -0.0342 42  GLN   B N   
505  C  CA  . GLN   B 33  ? 0.4311 0.3501 0.4207 0.1195  -0.0294 -0.0371 42  GLN   B CA  
506  C  C   . GLN   B 33  ? 0.4468 0.3823 0.4564 0.1059  -0.0270 -0.0366 42  GLN   B C   
507  O  O   . GLN   B 33  ? 0.4385 0.3799 0.4484 0.0961  -0.0181 -0.0313 42  GLN   B O   
508  C  CB  . GLN   B 33  ? 0.4709 0.3791 0.4518 0.1196  -0.0347 -0.0332 42  GLN   B CB  
509  C  CG  . GLN   B 33  ? 0.5219 0.4276 0.5141 0.1187  -0.0484 -0.0373 42  GLN   B CG  
510  C  CD  . GLN   B 33  ? 0.5893 0.4812 0.5703 0.1219  -0.0559 -0.0350 42  GLN   B CD  
511  O  OE1 . GLN   B 33  ? 0.6542 0.5445 0.6431 0.1121  -0.0611 -0.0329 42  GLN   B OE1 
512  N  NE2 . GLN   B 33  ? 0.5512 0.4332 0.5125 0.1361  -0.0562 -0.0349 42  GLN   B NE2 
513  N  N   . GLU   B 34  ? 0.4557 0.4007 0.4822 0.1060  -0.0340 -0.0422 43  GLU   B N   
514  C  CA  . GLU   B 34  ? 0.4657 0.4304 0.5144 0.0929  -0.0316 -0.0408 43  GLU   B CA  
515  C  C   . GLU   B 34  ? 0.4804 0.4591 0.5295 0.0891  -0.0182 -0.0389 43  GLU   B C   
516  O  O   . GLU   B 34  ? 0.5007 0.4909 0.5579 0.0772  -0.0117 -0.0333 43  GLU   B O   
517  C  CB  . GLU   B 34  ? 0.4901 0.4516 0.5442 0.0803  -0.0347 -0.0341 43  GLU   B CB  
518  C  CG  . GLU   B 34  ? 0.5361 0.4842 0.5928 0.0828  -0.0504 -0.0369 43  GLU   B CG  
519  C  CD  . GLU   B 34  ? 0.6617 0.5973 0.7134 0.0748  -0.0541 -0.0305 43  GLU   B CD  
520  O  OE1 . GLU   B 34  ? 0.6866 0.6310 0.7497 0.0602  -0.0498 -0.0239 43  GLU   B OE1 
521  O  OE2 . GLU   B 34  ? 0.7448 0.6617 0.7795 0.0841  -0.0612 -0.0317 43  GLU   B OE2 
522  N  N   . GLY   B 35  ? 0.4671 0.4420 0.5049 0.0999  -0.0147 -0.0432 44  GLY   B N   
523  C  CA  . GLY   B 35  ? 0.4661 0.4504 0.5014 0.0996  -0.0045 -0.0436 44  GLY   B CA  
524  C  C   . GLY   B 35  ? 0.4480 0.4244 0.4690 0.0945  0.0040  -0.0375 44  GLY   B C   
525  O  O   . GLY   B 35  ? 0.4584 0.4417 0.4768 0.0938  0.0116  -0.0380 44  GLY   B O   
526  N  N   . VAL   B 36  ? 0.4049 0.3674 0.4164 0.0919  0.0020  -0.0323 45  VAL   B N   
527  C  CA  . VAL   B 36  ? 0.3879 0.3441 0.3872 0.0868  0.0089  -0.0266 45  VAL   B CA  
528  C  C   . VAL   B 36  ? 0.3872 0.3259 0.3691 0.0944  0.0082  -0.0253 45  VAL   B C   
529  O  O   . VAL   B 36  ? 0.3959 0.3257 0.3737 0.1016  0.0015  -0.0259 45  VAL   B O   
530  C  CB  . VAL   B 36  ? 0.3897 0.3483 0.3939 0.0762  0.0081  -0.0205 45  VAL   B CB  
531  C  CG1 . VAL   B 36  ? 0.3779 0.3299 0.3690 0.0724  0.0136  -0.0153 45  VAL   B CG1 
532  C  CG2 . VAL   B 36  ? 0.3919 0.3691 0.4128 0.0672  0.0111  -0.0194 45  VAL   B CG2 
533  N  N   . PHE   B 37  ? 0.3857 0.3203 0.3578 0.0933  0.0148  -0.0233 46  PHE   B N   
534  C  CA  . PHE   B 37  ? 0.3931 0.3140 0.3510 0.0981  0.0157  -0.0201 46  PHE   B CA  
535  C  C   . PHE   B 37  ? 0.3833 0.3036 0.3371 0.0913  0.0179  -0.0136 46  PHE   B C   
536  O  O   . PHE   B 37  ? 0.3785 0.3050 0.3348 0.0829  0.0221  -0.0122 46  PHE   B O   
537  C  CB  . PHE   B 37  ? 0.4142 0.3281 0.3642 0.1011  0.0196  -0.0216 46  PHE   B CB  
538  C  CG  . PHE   B 37  ? 0.4271 0.3272 0.3642 0.1060  0.0200  -0.0170 46  PHE   B CG  
539  C  CD1 . PHE   B 37  ? 0.4543 0.3476 0.3862 0.1166  0.0157  -0.0174 46  PHE   B CD1 
540  C  CD2 . PHE   B 37  ? 0.4425 0.3377 0.3733 0.1001  0.0247  -0.0118 46  PHE   B CD2 
541  C  CE1 . PHE   B 37  ? 0.4730 0.3555 0.3924 0.1217  0.0174  -0.0116 46  PHE   B CE1 
542  C  CE2 . PHE   B 37  ? 0.4546 0.3396 0.3756 0.1035  0.0261  -0.0060 46  PHE   B CE2 
543  C  CZ  . PHE   B 37  ? 0.4701 0.3492 0.3849 0.1145  0.0231  -0.0054 46  PHE   B CZ  
544  N  N   . HIS   B 38  ? 0.3748 0.2886 0.3216 0.0961  0.0151  -0.0103 47  HIS   B N   
545  C  CA  . HIS   B 38  ? 0.3719 0.2868 0.3148 0.0920  0.0158  -0.0048 47  HIS   B CA  
546  C  C   . HIS   B 38  ? 0.3980 0.3082 0.3306 0.0955  0.0194  0.0003  47  HIS   B C   
547  O  O   . HIS   B 38  ? 0.4110 0.3150 0.3369 0.1052  0.0178  0.0008  47  HIS   B O   
548  C  CB  . HIS   B 38  ? 0.3828 0.2954 0.3256 0.0967  0.0080  -0.0050 47  HIS   B CB  
549  C  CG  . HIS   B 38  ? 0.3889 0.3050 0.3436 0.0928  0.0028  -0.0088 47  HIS   B CG  
550  N  ND1 . HIS   B 38  ? 0.4131 0.3299 0.3748 0.0976  -0.0012 -0.0145 47  HIS   B ND1 
551  C  CD2 . HIS   B 38  ? 0.4021 0.3217 0.3632 0.0845  0.0007  -0.0071 47  HIS   B CD2 
552  C  CE1 . HIS   B 38  ? 0.3991 0.3215 0.3733 0.0911  -0.0055 -0.0158 47  HIS   B CE1 
553  N  NE2 . HIS   B 38  ? 0.4053 0.3284 0.3790 0.0829  -0.0044 -0.0109 47  HIS   B NE2 
554  N  N   . THR   B 39  ? 0.3854 0.2996 0.3170 0.0879  0.0241  0.0042  48  THR   B N   
555  C  CA  . THR   B 39  ? 0.3888 0.3017 0.3136 0.0894  0.0277  0.0104  48  THR   B CA  
556  C  C   . THR   B 39  ? 0.4084 0.3296 0.3342 0.0826  0.0298  0.0143  48  THR   B C   
557  O  O   . THR   B 39  ? 0.3844 0.3096 0.3135 0.0783  0.0278  0.0122  48  THR   B O   
558  C  CB  . THR   B 39  ? 0.4250 0.3304 0.3477 0.0883  0.0313  0.0107  48  THR   B CB  
559  O  OG1 . THR   B 39  ? 0.4290 0.3338 0.3467 0.0891  0.0348  0.0184  48  THR   B OG1 
560  C  CG2 . THR   B 39  ? 0.4186 0.3251 0.3460 0.0782  0.0335  0.0079  48  THR   B CG2 
561  N  N   . MET   B 40  ? 0.4052 0.3298 0.3284 0.0816  0.0335  0.0205  49  MET   B N   
562  C  CA  . MET   B 40  ? 0.4048 0.3395 0.3301 0.0756  0.0347  0.0235  49  MET   B CA  
563  C  C   . MET   B 40  ? 0.4014 0.3359 0.3315 0.0648  0.0370  0.0221  49  MET   B C   
564  O  O   . MET   B 40  ? 0.4239 0.3506 0.3544 0.0624  0.0387  0.0218  49  MET   B O   
565  C  CB  . MET   B 40  ? 0.4132 0.3561 0.3352 0.0804  0.0371  0.0309  49  MET   B CB  
566  C  CG  . MET   B 40  ? 0.4252 0.3663 0.3392 0.0945  0.0337  0.0312  49  MET   B CG  
567  S  SD  . MET   B 40  ? 0.5271 0.4829 0.4358 0.1027  0.0351  0.0380  49  MET   B SD  
568  C  CE  . MET   B 40  ? 0.4829 0.4427 0.3926 0.0997  0.0299  0.0339  49  MET   B CE  
569  N  N   A TRP   B 41  ? 0.3974 0.3385 0.3298 0.0589  0.0363  0.0207  50  TRP   B N   
570  N  N   B TRP   B 41  ? 0.3931 0.3343 0.3255 0.0589  0.0363  0.0207  50  TRP   B N   
571  N  N   C TRP   B 41  ? 0.3974 0.3385 0.3298 0.0589  0.0363  0.0207  50  TRP   B N   
572  N  N   D TRP   B 41  ? 0.3931 0.3343 0.3255 0.0589  0.0363  0.0207  50  TRP   B N   
573  C  CA  A TRP   B 41  ? 0.4148 0.3555 0.3503 0.0501  0.0371  0.0182  50  TRP   B CA  
574  C  CA  B TRP   B 41  ? 0.4066 0.3474 0.3421 0.0501  0.0371  0.0182  50  TRP   B CA  
575  C  CA  C TRP   B 41  ? 0.4148 0.3555 0.3503 0.0501  0.0371  0.0182  50  TRP   B CA  
576  C  CA  D TRP   B 41  ? 0.4066 0.3474 0.3421 0.0501  0.0371  0.0182  50  TRP   B CA  
577  C  C   A TRP   B 41  ? 0.4200 0.3602 0.3584 0.0450  0.0389  0.0223  50  TRP   B C   
578  C  C   B TRP   B 41  ? 0.4163 0.3564 0.3546 0.0450  0.0389  0.0223  50  TRP   B C   
579  C  C   C TRP   B 41  ? 0.4200 0.3602 0.3584 0.0450  0.0389  0.0223  50  TRP   B C   
580  C  C   D TRP   B 41  ? 0.4163 0.3564 0.3546 0.0450  0.0389  0.0223  50  TRP   B C   
581  O  O   A TRP   B 41  ? 0.4268 0.3582 0.3657 0.0405  0.0384  0.0195  50  TRP   B O   
582  O  O   B TRP   B 41  ? 0.4230 0.3544 0.3620 0.0405  0.0385  0.0195  50  TRP   B O   
583  O  O   C TRP   B 41  ? 0.4268 0.3582 0.3657 0.0405  0.0384  0.0195  50  TRP   B O   
584  O  O   D TRP   B 41  ? 0.4230 0.3544 0.3620 0.0405  0.0385  0.0195  50  TRP   B O   
585  C  CB  A TRP   B 41  ? 0.4180 0.3667 0.3536 0.0465  0.0357  0.0168  50  TRP   B CB  
586  C  CB  B TRP   B 41  ? 0.4033 0.3524 0.3389 0.0464  0.0357  0.0171  50  TRP   B CB  
587  C  CB  C TRP   B 41  ? 0.4180 0.3667 0.3536 0.0465  0.0357  0.0168  50  TRP   B CB  
588  C  CB  D TRP   B 41  ? 0.4033 0.3524 0.3389 0.0464  0.0357  0.0171  50  TRP   B CB  
589  C  CG  A TRP   B 41  ? 0.4303 0.3773 0.3667 0.0399  0.0355  0.0124  50  TRP   B CG  
590  C  CG  B TRP   B 41  ? 0.4064 0.3549 0.3436 0.0391  0.0354  0.0135  50  TRP   B CG  
591  C  CG  C TRP   B 41  ? 0.4303 0.3773 0.3667 0.0399  0.0355  0.0124  50  TRP   B CG  
592  C  CG  D TRP   B 41  ? 0.4064 0.3549 0.3436 0.0391  0.0354  0.0135  50  TRP   B CG  
593  C  CD1 A TRP   B 41  ? 0.4450 0.3888 0.3794 0.0396  0.0355  0.0072  50  TRP   B CD1 
594  C  CD1 B TRP   B 41  ? 0.4157 0.3675 0.3564 0.0331  0.0348  0.0149  50  TRP   B CD1 
595  C  CD1 C TRP   B 41  ? 0.4450 0.3888 0.3794 0.0396  0.0355  0.0072  50  TRP   B CD1 
596  C  CD1 D TRP   B 41  ? 0.4157 0.3675 0.3564 0.0331  0.0348  0.0149  50  TRP   B CD1 
597  C  CD2 A TRP   B 41  ? 0.4377 0.3864 0.3770 0.0333  0.0346  0.0125  50  TRP   B CD2 
598  C  CD2 B TRP   B 41  ? 0.4145 0.3586 0.3495 0.0378  0.0352  0.0076  50  TRP   B CD2 
599  C  CD2 C TRP   B 41  ? 0.4377 0.3864 0.3770 0.0333  0.0346  0.0125  50  TRP   B CD2 
600  C  CD2 D TRP   B 41  ? 0.4145 0.3586 0.3495 0.0378  0.0352  0.0076  50  TRP   B CD2 
601  N  NE1 A TRP   B 41  ? 0.4529 0.3955 0.3864 0.0350  0.0346  0.0034  50  TRP   B NE1 
602  N  NE1 B TRP   B 41  ? 0.4205 0.3677 0.3601 0.0287  0.0329  0.0092  50  TRP   B NE1 
603  N  NE1 C TRP   B 41  ? 0.4529 0.3955 0.3864 0.0350  0.0346  0.0034  50  TRP   B NE1 
604  N  NE1 D TRP   B 41  ? 0.4205 0.3677 0.3601 0.0287  0.0329  0.0092  50  TRP   B NE1 
605  C  CE2 A TRP   B 41  ? 0.4495 0.3937 0.3863 0.0306  0.0332  0.0062  50  TRP   B CE2 
606  C  CE2 B TRP   B 41  ? 0.4231 0.3662 0.3583 0.0324  0.0337  0.0047  50  TRP   B CE2 
607  C  CE2 C TRP   B 41  ? 0.4495 0.3937 0.3863 0.0306  0.0332  0.0062  50  TRP   B CE2 
608  C  CE2 D TRP   B 41  ? 0.4231 0.3662 0.3583 0.0324  0.0337  0.0047  50  TRP   B CE2 
609  C  CE3 A TRP   B 41  ? 0.4464 0.4013 0.3909 0.0294  0.0346  0.0175  50  TRP   B CE3 
610  C  CE3 B TRP   B 41  ? 0.4278 0.3701 0.3614 0.0410  0.0361  0.0046  50  TRP   B CE3 
611  C  CE3 C TRP   B 41  ? 0.4464 0.4013 0.3909 0.0294  0.0346  0.0175  50  TRP   B CE3 
612  C  CE3 D TRP   B 41  ? 0.4278 0.3701 0.3614 0.0410  0.0361  0.0046  50  TRP   B CE3 
613  C  CZ2 A TRP   B 41  ? 0.4701 0.4127 0.4083 0.0247  0.0302  0.0035  50  TRP   B CZ2 
614  C  CZ2 B TRP   B 41  ? 0.4436 0.3833 0.3748 0.0320  0.0330  -0.0015 50  TRP   B CZ2 
615  C  CZ2 C TRP   B 41  ? 0.4701 0.4127 0.4083 0.0247  0.0302  0.0035  50  TRP   B CZ2 
616  C  CZ2 D TRP   B 41  ? 0.4436 0.3833 0.3748 0.0320  0.0330  -0.0015 50  TRP   B CZ2 
617  C  CZ3 A TRP   B 41  ? 0.4609 0.4157 0.4095 0.0216  0.0320  0.0157  50  TRP   B CZ3 
618  C  CZ3 B TRP   B 41  ? 0.4420 0.3839 0.3736 0.0396  0.0367  -0.0004 50  TRP   B CZ3 
619  C  CZ3 C TRP   B 41  ? 0.4609 0.4157 0.4095 0.0216  0.0320  0.0157  50  TRP   B CZ3 
620  C  CZ3 D TRP   B 41  ? 0.4420 0.3839 0.3736 0.0396  0.0367  -0.0004 50  TRP   B CZ3 
621  C  CH2 A TRP   B 41  ? 0.4687 0.4160 0.4135 0.0196  0.0291  0.0083  50  TRP   B CH2 
622  C  CH2 B TRP   B 41  ? 0.4440 0.3841 0.3731 0.0362  0.0353  -0.0037 50  TRP   B CH2 
623  C  CH2 C TRP   B 41  ? 0.4687 0.4160 0.4135 0.0196  0.0291  0.0083  50  TRP   B CH2 
624  C  CH2 D TRP   B 41  ? 0.4440 0.3841 0.3731 0.0362  0.0353  -0.0037 50  TRP   B CH2 
625  N  N   . HIS   B 42  ? 0.4114 0.3609 0.3515 0.0460  0.0406  0.0293  51  HIS   B N   
626  C  CA  . HIS   B 42  ? 0.4321 0.3836 0.3777 0.0391  0.0427  0.0352  51  HIS   B CA  
627  C  C   . HIS   B 42  ? 0.4522 0.3891 0.3951 0.0398  0.0443  0.0375  51  HIS   B C   
628  O  O   . HIS   B 42  ? 0.4684 0.4011 0.4155 0.0317  0.0449  0.0416  51  HIS   B O   
629  C  CB  . HIS   B 42  ? 0.4359 0.4053 0.3855 0.0401  0.0451  0.0430  51  HIS   B CB  
630  C  CG  . HIS   B 42  ? 0.4548 0.4264 0.3993 0.0503  0.0485  0.0491  51  HIS   B CG  
631  N  ND1 . HIS   B 42  ? 0.4715 0.4478 0.4090 0.0619  0.0470  0.0478  51  HIS   B ND1 
632  C  CD2 . HIS   B 42  ? 0.4804 0.4486 0.4242 0.0511  0.0525  0.0565  51  HIS   B CD2 
633  C  CE1 . HIS   B 42  ? 0.4903 0.4678 0.4230 0.0704  0.0502  0.0539  51  HIS   B CE1 
634  N  NE2 . HIS   B 42  ? 0.4843 0.4573 0.4203 0.0644  0.0542  0.0597  51  HIS   B NE2 
635  N  N   . VAL   B 43  ? 0.4369 0.3648 0.3729 0.0490  0.0441  0.0346  52  VAL   B N   
636  C  CA  . VAL   B 43  ? 0.4330 0.3455 0.3642 0.0515  0.0450  0.0360  52  VAL   B CA  
637  C  C   . VAL   B 43  ? 0.4622 0.3607 0.3930 0.0462  0.0418  0.0288  52  VAL   B C   
638  O  O   . VAL   B 43  ? 0.4837 0.3695 0.4131 0.0418  0.0414  0.0314  52  VAL   B O   
639  C  CB  . VAL   B 43  ? 0.4427 0.3509 0.3667 0.0643  0.0445  0.0339  52  VAL   B CB  
640  C  CG1 . VAL   B 43  ? 0.4498 0.3402 0.3674 0.0683  0.0441  0.0329  52  VAL   B CG1 
641  C  CG2 . VAL   B 43  ? 0.4363 0.3550 0.3574 0.0721  0.0469  0.0412  52  VAL   B CG2 
642  N  N   . THR   B 44  ? 0.4267 0.3271 0.3577 0.0473  0.0394  0.0201  53  THR   B N   
643  C  CA  . THR   B 44  ? 0.4328 0.3216 0.3612 0.0457  0.0365  0.0125  53  THR   B CA  
644  C  C   . THR   B 44  ? 0.4499 0.3420 0.3812 0.0378  0.0341  0.0086  53  THR   B C   
645  O  O   . THR   B 44  ? 0.4624 0.3438 0.3901 0.0370  0.0310  0.0023  53  THR   B O   
646  C  CB  . THR   B 44  ? 0.4473 0.3366 0.3736 0.0539  0.0358  0.0051  53  THR   B CB  
647  O  OG1 . THR   B 44  ? 0.4287 0.3320 0.3589 0.0527  0.0364  0.0037  53  THR   B OG1 
648  C  CG2 . THR   B 44  ? 0.4617 0.3468 0.3847 0.0632  0.0363  0.0068  53  THR   B CG2 
649  N  N   . LYS   B 45  ? 0.4418 0.3480 0.3779 0.0338  0.0349  0.0114  54  LYS   B N   
650  C  CA  . LYS   B 45  ? 0.4547 0.3659 0.3924 0.0280  0.0322  0.0071  54  LYS   B CA  
651  C  C   . LYS   B 45  ? 0.4766 0.3864 0.4092 0.0324  0.0314  -0.0015 54  LYS   B C   
652  O  O   . LYS   B 45  ? 0.4985 0.4073 0.4286 0.0300  0.0286  -0.0069 54  LYS   B O   
653  C  CB  . LYS   B 45  ? 0.4936 0.3966 0.4341 0.0192  0.0283  0.0076  54  LYS   B CB  
654  C  CG  . LYS   B 45  ? 0.6074 0.5134 0.5550 0.0136  0.0302  0.0178  54  LYS   B CG  
655  C  CD  . LYS   B 45  ? 0.6876 0.6142 0.6412 0.0133  0.0331  0.0236  54  LYS   B CD  
656  C  CE  . LYS   B 45  ? 0.7613 0.6954 0.7237 0.0068  0.0353  0.0340  54  LYS   B CE  
657  N  NZ  . LYS   B 45  ? 0.7860 0.7077 0.7453 0.0085  0.0383  0.0403  54  LYS   B NZ  
658  N  N   . GLY   B 46  ? 0.4838 0.3947 0.4149 0.0393  0.0338  -0.0026 55  GLY   B N   
659  C  CA  . GLY   B 46  ? 0.4880 0.4019 0.4167 0.0433  0.0343  -0.0089 55  GLY   B CA  
660  C  C   . GLY   B 46  ? 0.4992 0.4022 0.4230 0.0473  0.0326  -0.0155 55  GLY   B C   
661  O  O   . GLY   B 46  ? 0.5289 0.4362 0.4501 0.0509  0.0332  -0.0212 55  GLY   B O   
662  N  N   . ALA   B 47  ? 0.4997 0.3881 0.4212 0.0472  0.0302  -0.0146 56  ALA   B N   
663  C  CA  . ALA   B 47  ? 0.5193 0.3939 0.4338 0.0525  0.0272  -0.0215 56  ALA   B CA  
664  C  C   . ALA   B 47  ? 0.5144 0.3921 0.4287 0.0620  0.0292  -0.0246 56  ALA   B C   
665  O  O   . ALA   B 47  ? 0.4791 0.3627 0.3981 0.0637  0.0315  -0.0202 56  ALA   B O   
666  C  CB  . ALA   B 47  ? 0.5441 0.4000 0.4557 0.0492  0.0237  -0.0182 56  ALA   B CB  
667  N  N   . ALA   B 48  ? 0.5253 0.3973 0.4334 0.0694  0.0270  -0.0327 57  ALA   B N   
668  C  CA  . ALA   B 48  ? 0.5289 0.4044 0.4378 0.0790  0.0280  -0.0363 57  ALA   B CA  
669  C  C   . ALA   B 48  ? 0.5307 0.3909 0.4364 0.0819  0.0262  -0.0327 57  ALA   B C   
670  O  O   . ALA   B 48  ? 0.5599 0.4041 0.4608 0.0771  0.0239  -0.0286 57  ALA   B O   
671  C  CB  . ALA   B 48  ? 0.5416 0.4149 0.4432 0.0879  0.0258  -0.0461 57  ALA   B CB  
672  N  N   . LEU   B 49  ? 0.5036 0.3687 0.4120 0.0897  0.0269  -0.0339 58  LEU   B N   
673  C  CA  . LEU   B 49  ? 0.5295 0.3810 0.4331 0.0950  0.0252  -0.0310 58  LEU   B CA  
674  C  C   . LEU   B 49  ? 0.5580 0.4053 0.4568 0.1074  0.0222  -0.0392 58  LEU   B C   
675  O  O   . LEU   B 49  ? 0.5596 0.4226 0.4638 0.1117  0.0229  -0.0459 58  LEU   B O   
676  C  CB  . LEU   B 49  ? 0.5250 0.3870 0.4358 0.0951  0.0273  -0.0253 58  LEU   B CB  
677  C  CG  . LEU   B 49  ? 0.5349 0.4042 0.4505 0.0854  0.0300  -0.0178 58  LEU   B CG  
678  C  CD1 . LEU   B 49  ? 0.5250 0.4035 0.4456 0.0883  0.0304  -0.0142 58  LEU   B CD1 
679  C  CD2 . LEU   B 49  ? 0.5700 0.4259 0.4800 0.0797  0.0303  -0.0108 58  LEU   B CD2 
680  N  N   . ARG   B 50  ? 0.5737 0.4015 0.4626 0.1134  0.0193  -0.0382 59  ARG   B N   
681  C  CA  . ARG   B 50  ? 0.6075 0.4290 0.4899 0.1269  0.0156  -0.0458 59  ARG   B CA  
682  C  C   . ARG   B 50  ? 0.6178 0.4423 0.5025 0.1337  0.0154  -0.0432 59  ARG   B C   
683  O  O   . ARG   B 50  ? 0.5951 0.4139 0.4783 0.1299  0.0170  -0.0345 59  ARG   B O   
684  C  CB  . ARG   B 50  ? 0.6583 0.4501 0.5243 0.1294  0.0109  -0.0462 59  ARG   B CB  
685  C  CG  . ARG   B 50  ? 0.7712 0.5508 0.6263 0.1448  0.0060  -0.0535 59  ARG   B CG  
686  C  CD  . ARG   B 50  ? 0.8432 0.5927 0.6810 0.1477  -0.0002 -0.0565 59  ARG   B CD  
687  N  NE  . ARG   B 50  ? 0.8775 0.6083 0.7116 0.1341  -0.0003 -0.0468 59  ARG   B NE  
688  C  CZ  . ARG   B 50  ? 0.8994 0.6116 0.7270 0.1309  0.0000  -0.0366 59  ARG   B CZ  
689  N  NH1 . ARG   B 50  ? 0.8765 0.5832 0.6974 0.1419  -0.0001 -0.0353 59  ARG   B NH1 
690  N  NH2 . ARG   B 50  ? 0.9089 0.6086 0.7365 0.1170  0.0003  -0.0273 59  ARG   B NH2 
691  N  N   . SER   B 51  ? 0.6398 0.4748 0.5284 0.1445  0.0131  -0.0511 60  SER   B N   
692  C  CA  . SER   B 51  ? 0.6748 0.5114 0.5647 0.1533  0.0108  -0.0510 60  SER   B CA  
693  C  C   . SER   B 51  ? 0.7092 0.5384 0.5909 0.1680  0.0058  -0.0603 60  SER   B C   
694  O  O   . SER   B 51  ? 0.7000 0.5477 0.5908 0.1727  0.0050  -0.0686 60  SER   B O   
695  C  CB  . SER   B 51  ? 0.7016 0.5645 0.6097 0.1502  0.0117  -0.0523 60  SER   B CB  
696  O  OG  . SER   B 51  ? 0.7518 0.6153 0.6612 0.1592  0.0076  -0.0535 60  SER   B OG  
697  N  N   . GLY   B 52  ? 0.7463 0.5487 0.6102 0.1748  0.0028  -0.0584 61  GLY   B N   
698  C  CA  . GLY   B 52  ? 0.7793 0.5697 0.6314 0.1899  -0.0028 -0.0671 61  GLY   B CA  
699  C  C   . GLY   B 52  ? 0.8062 0.5966 0.6557 0.1897  -0.0037 -0.0741 61  GLY   B C   
700  O  O   . GLY   B 52  ? 0.8193 0.5952 0.6624 0.1802  -0.0027 -0.0698 61  GLY   B O   
701  N  N   . GLU   B 53  ? 0.8093 0.6186 0.6652 0.2000  -0.0056 -0.0849 62  GLU   B N   
702  C  CA  . GLU   B 53  ? 0.8197 0.6338 0.6731 0.2023  -0.0060 -0.0925 62  GLU   B CA  
703  C  C   . GLU   B 53  ? 0.7942 0.6389 0.6660 0.1913  0.0006  -0.0915 62  GLU   B C   
704  O  O   . GLU   B 53  ? 0.8005 0.6514 0.6698 0.1932  0.0011  -0.0969 62  GLU   B O   
705  C  CB  . GLU   B 53  ? 0.8686 0.6899 0.7181 0.2214  -0.0110 -0.1048 62  GLU   B CB  
706  C  CG  . GLU   B 53  ? 0.9976 0.7847 0.8219 0.2335  -0.0185 -0.1098 62  GLU   B CG  
707  C  CD  . GLU   B 53  ? 1.1472 0.9453 0.9678 0.2538  -0.0233 -0.1232 62  GLU   B CD  
708  O  OE1 . GLU   B 53  ? 1.1817 1.0016 1.0146 0.2615  -0.0235 -0.1267 62  GLU   B OE1 
709  O  OE2 . GLU   B 53  ? 1.1989 0.9844 1.0045 0.2627  -0.0277 -0.1308 62  GLU   B OE2 
710  N  N   . GLY   B 54  ? 0.7600 0.6222 0.6481 0.1811  0.0049  -0.0847 63  GLY   B N   
711  C  CA  . GLY   B 54  ? 0.7287 0.6182 0.6335 0.1707  0.0109  -0.0827 63  GLY   B CA  
712  C  C   . GLY   B 54  ? 0.7016 0.5835 0.6052 0.1555  0.0146  -0.0741 63  GLY   B C   
713  O  O   . GLY   B 54  ? 0.7041 0.5627 0.5976 0.1511  0.0131  -0.0681 63  GLY   B O   
714  N  N   . ARG   B 55  ? 0.6616 0.5639 0.5750 0.1481  0.0194  -0.0733 64  ARG   B N   
715  C  CA  . ARG   B 55  ? 0.6448 0.5429 0.5574 0.1348  0.0225  -0.0663 64  ARG   B CA  
716  C  C   . ARG   B 55  ? 0.6009 0.5202 0.5300 0.1249  0.0270  -0.0598 64  ARG   B C   
717  O  O   . ARG   B 55  ? 0.6018 0.5443 0.5440 0.1264  0.0292  -0.0618 64  ARG   B O   
718  C  CB  . ARG   B 55  ? 0.6701 0.5700 0.5756 0.1359  0.0233  -0.0712 64  ARG   B CB  
719  C  CG  . ARG   B 55  ? 0.7045 0.6007 0.6080 0.1238  0.0253  -0.0660 64  ARG   B CG  
720  C  CD  . ARG   B 55  ? 0.7433 0.6460 0.6399 0.1289  0.0256  -0.0730 64  ARG   B CD  
721  N  NE  . ARG   B 55  ? 0.7825 0.6866 0.6780 0.1191  0.0275  -0.0694 64  ARG   B NE  
722  C  CZ  . ARG   B 55  ? 0.8476 0.7318 0.7310 0.1169  0.0225  -0.0714 64  ARG   B CZ  
723  N  NH1 . ARG   B 55  ? 0.8774 0.7369 0.7482 0.1232  0.0153  -0.0766 64  ARG   B NH1 
724  N  NH2 . ARG   B 55  ? 0.8225 0.7108 0.7062 0.1086  0.0238  -0.0686 64  ARG   B NH2 
725  N  N   . LEU   B 56  ? 0.5458 0.4567 0.4743 0.1149  0.0279  -0.0519 65  LEU   B N   
726  C  CA  . LEU   B 56  ? 0.5072 0.4324 0.4474 0.1058  0.0308  -0.0457 65  LEU   B CA  
727  C  C   . LEU   B 56  ? 0.4843 0.4103 0.4214 0.0968  0.0339  -0.0424 65  LEU   B C   
728  O  O   . LEU   B 56  ? 0.5033 0.4129 0.4309 0.0936  0.0325  -0.0404 65  LEU   B O   
729  C  CB  . LEU   B 56  ? 0.5054 0.4202 0.4451 0.1041  0.0286  -0.0397 65  LEU   B CB  
730  C  CG  . LEU   B 56  ? 0.5571 0.4669 0.4970 0.1137  0.0243  -0.0420 65  LEU   B CG  
731  C  CD1 . LEU   B 56  ? 0.5527 0.4606 0.4950 0.1112  0.0228  -0.0357 65  LEU   B CD1 
732  C  CD2 . LEU   B 56  ? 0.5859 0.5135 0.5376 0.1194  0.0229  -0.0483 65  LEU   B CD2 
733  N  N   . ASP   B 57  ? 0.4599 0.4049 0.4046 0.0932  0.0378  -0.0420 66  ASP   B N   
734  C  CA  . ASP   B 57  ? 0.4693 0.4161 0.4098 0.0862  0.0404  -0.0395 66  ASP   B CA  
735  C  C   . ASP   B 57  ? 0.4462 0.3975 0.3930 0.0768  0.0417  -0.0315 66  ASP   B C   
736  O  O   . ASP   B 57  ? 0.4327 0.3938 0.3899 0.0756  0.0420  -0.0289 66  ASP   B O   
737  C  CB  . ASP   B 57  ? 0.5123 0.4771 0.4543 0.0891  0.0446  -0.0431 66  ASP   B CB  
738  C  CG  . ASP   B 57  ? 0.6221 0.5822 0.5550 0.1003  0.0426  -0.0522 66  ASP   B CG  
739  O  OD1 . ASP   B 57  ? 0.6201 0.5581 0.5416 0.1027  0.0377  -0.0550 66  ASP   B OD1 
740  O  OD2 . ASP   B 57  ? 0.6600 0.6388 0.5973 0.1069  0.0457  -0.0560 66  ASP   B OD2 
741  N  N   . PRO   B 58  ? 0.4421 0.3872 0.3830 0.0707  0.0419  -0.0280 67  PRO   B N   
742  C  CA  . PRO   B 58  ? 0.4370 0.3866 0.3820 0.0634  0.0427  -0.0211 67  PRO   B CA  
743  C  C   . PRO   B 58  ? 0.4200 0.3864 0.3717 0.0607  0.0464  -0.0192 67  PRO   B C   
744  O  O   . PRO   B 58  ? 0.4299 0.4059 0.3800 0.0628  0.0498  -0.0222 67  PRO   B O   
745  C  CB  . PRO   B 58  ? 0.4484 0.3904 0.3856 0.0588  0.0419  -0.0194 67  PRO   B CB  
746  C  CG  . PRO   B 58  ? 0.4846 0.4220 0.4142 0.0625  0.0413  -0.0262 67  PRO   B CG  
747  C  CD  . PRO   B 58  ? 0.4642 0.3975 0.3945 0.0702  0.0401  -0.0309 67  PRO   B CD  
748  N  N   . TYR   B 59  ? 0.3793 0.3485 0.3374 0.0562  0.0454  -0.0136 68  TYR   B N   
749  C  CA  . TYR   B 59  ? 0.3666 0.3495 0.3321 0.0516  0.0483  -0.0097 68  TYR   B CA  
750  C  C   . TYR   B 59  ? 0.3574 0.3370 0.3188 0.0451  0.0476  -0.0032 68  TYR   B C   
751  O  O   . TYR   B 59  ? 0.3850 0.3727 0.3450 0.0413  0.0515  0.0002  68  TYR   B O   
752  C  CB  . TYR   B 59  ? 0.3696 0.3576 0.3483 0.0523  0.0454  -0.0096 68  TYR   B CB  
753  C  CG  . TYR   B 59  ? 0.3657 0.3677 0.3552 0.0456  0.0477  -0.0043 68  TYR   B CG  
754  C  CD1 . TYR   B 59  ? 0.3965 0.3936 0.3857 0.0386  0.0455  0.0025  68  TYR   B CD1 
755  C  CD2 . TYR   B 59  ? 0.3681 0.3890 0.3678 0.0462  0.0523  -0.0055 68  TYR   B CD2 
756  C  CE1 . TYR   B 59  ? 0.4081 0.4155 0.4071 0.0310  0.0472  0.0087  68  TYR   B CE1 
757  C  CE2 . TYR   B 59  ? 0.3710 0.4062 0.3828 0.0383  0.0549  0.0012  68  TYR   B CE2 
758  C  CZ  . TYR   B 59  ? 0.3930 0.4199 0.4042 0.0301  0.0522  0.0087  68  TYR   B CZ  
759  O  OH  . TYR   B 59  ? 0.3953 0.4337 0.4179 0.0210  0.0544  0.0165  68  TYR   B OH  
760  N  N   . TRP   B 60  ? 0.3407 0.3091 0.2989 0.0452  0.0432  -0.0014 69  TRP   B N   
761  C  CA  . TRP   B 60  ? 0.3486 0.3132 0.3011 0.0412  0.0416  0.0037  69  TRP   B CA  
762  C  C   . TRP   B 60  ? 0.3791 0.3345 0.3250 0.0439  0.0389  0.0031  69  TRP   B C   
763  O  O   . TRP   B 60  ? 0.3731 0.3232 0.3205 0.0481  0.0368  0.0014  69  TRP   B O   
764  C  CB  . TRP   B 60  ? 0.3686 0.3314 0.3269 0.0387  0.0375  0.0081  69  TRP   B CB  
765  C  CG  . TRP   B 60  ? 0.3888 0.3440 0.3390 0.0375  0.0339  0.0124  69  TRP   B CG  
766  C  CD1 . TRP   B 60  ? 0.3960 0.3522 0.3400 0.0335  0.0353  0.0166  69  TRP   B CD1 
767  C  CD2 . TRP   B 60  ? 0.3737 0.3200 0.3193 0.0423  0.0285  0.0125  69  TRP   B CD2 
768  N  NE1 . TRP   B 60  ? 0.3878 0.3358 0.3239 0.0355  0.0304  0.0187  69  TRP   B NE1 
769  C  CE2 . TRP   B 60  ? 0.3865 0.3295 0.3238 0.0412  0.0264  0.0162  69  TRP   B CE2 
770  C  CE3 . TRP   B 60  ? 0.3967 0.3383 0.3433 0.0486  0.0254  0.0100  69  TRP   B CE3 
771  C  CZ2 . TRP   B 60  ? 0.4096 0.3464 0.3404 0.0465  0.0212  0.0171  69  TRP   B CZ2 
772  C  CZ3 . TRP   B 60  ? 0.4084 0.3442 0.3482 0.0536  0.0212  0.0116  69  TRP   B CZ3 
773  C  CH2 . TRP   B 60  ? 0.4099 0.3442 0.3424 0.0529  0.0191  0.0149  69  TRP   B CH2 
774  N  N   . GLY   B 61  ? 0.3860 0.3407 0.3251 0.0416  0.0386  0.0055  70  GLY   B N   
775  C  CA  . GLY   B 61  ? 0.4020 0.3522 0.3372 0.0432  0.0363  0.0063  70  GLY   B CA  
776  C  C   . GLY   B 61  ? 0.3812 0.3333 0.3104 0.0413  0.0350  0.0092  70  GLY   B C   
777  O  O   . GLY   B 61  ? 0.3797 0.3351 0.3053 0.0385  0.0366  0.0097  70  GLY   B O   
778  N  N   . ASP   B 62  ? 0.3685 0.3198 0.2959 0.0437  0.0325  0.0113  71  ASP   B N   
779  C  CA  . ASP   B 62  ? 0.3781 0.3327 0.3000 0.0436  0.0304  0.0136  71  ASP   B CA  
780  C  C   . ASP   B 62  ? 0.3862 0.3451 0.3092 0.0455  0.0296  0.0149  71  ASP   B C   
781  O  O   . ASP   B 62  ? 0.3931 0.3510 0.3172 0.0502  0.0287  0.0169  71  ASP   B O   
782  C  CB  . ASP   B 62  ? 0.4316 0.3822 0.3491 0.0460  0.0267  0.0167  71  ASP   B CB  
783  C  CG  . ASP   B 62  ? 0.5162 0.4690 0.4255 0.0470  0.0242  0.0185  71  ASP   B CG  
784  O  OD1 . ASP   B 62  ? 0.4814 0.4387 0.3892 0.0508  0.0222  0.0191  71  ASP   B OD1 
785  O  OD2 . ASP   B 62  ? 0.5757 0.5269 0.4800 0.0442  0.0246  0.0195  71  ASP   B OD2 
786  N  N   . VAL   B 63  ? 0.3827 0.3472 0.3063 0.0417  0.0300  0.0137  72  VAL   B N   
787  C  CA  . VAL   B 63  ? 0.3801 0.3520 0.3080 0.0414  0.0297  0.0160  72  VAL   B CA  
788  C  C   . VAL   B 63  ? 0.3921 0.3709 0.3171 0.0479  0.0275  0.0199  72  VAL   B C   
789  O  O   . VAL   B 63  ? 0.4072 0.3920 0.3357 0.0509  0.0286  0.0234  72  VAL   B O   
790  C  CB  . VAL   B 63  ? 0.3972 0.3740 0.3274 0.0352  0.0287  0.0132  72  VAL   B CB  
791  C  CG1 . VAL   B 63  ? 0.4119 0.4014 0.3479 0.0340  0.0273  0.0163  72  VAL   B CG1 
792  C  CG2 . VAL   B 63  ? 0.4132 0.3819 0.3463 0.0307  0.0298  0.0095  72  VAL   B CG2 
793  N  N   . LYS   B 64  ? 0.3911 0.3690 0.3084 0.0507  0.0244  0.0195  73  LYS   B N   
794  C  CA  . LYS   B 64  ? 0.4086 0.3920 0.3208 0.0587  0.0210  0.0221  73  LYS   B CA  
795  C  C   . LYS   B 64  ? 0.4265 0.4037 0.3361 0.0665  0.0196  0.0239  73  LYS   B C   
796  O  O   . LYS   B 64  ? 0.4526 0.4378 0.3619 0.0735  0.0193  0.0264  73  LYS   B O   
797  C  CB  . LYS   B 64  ? 0.4400 0.4211 0.3428 0.0605  0.0170  0.0212  73  LYS   B CB  
798  C  CG  . LYS   B 64  ? 0.4785 0.4655 0.3747 0.0705  0.0125  0.0230  73  LYS   B CG  
799  C  CD  . LYS   B 64  ? 0.5148 0.4967 0.3994 0.0731  0.0077  0.0222  73  LYS   B CD  
800  C  CE  . LYS   B 64  ? 0.5641 0.5500 0.4402 0.0850  0.0021  0.0231  73  LYS   B CE  
801  N  NZ  . LYS   B 64  ? 0.5883 0.5681 0.4512 0.0884  -0.0033 0.0223  73  LYS   B NZ  
802  N  N   . GLN   B 65  ? 0.4194 0.3839 0.3283 0.0653  0.0189  0.0225  74  GLN   B N   
803  C  CA  . GLN   B 65  ? 0.4176 0.3748 0.3250 0.0724  0.0165  0.0228  74  GLN   B CA  
804  C  C   . GLN   B 65  ? 0.4108 0.3717 0.3243 0.0732  0.0209  0.0238  74  GLN   B C   
805  O  O   . GLN   B 65  ? 0.4130 0.3713 0.3235 0.0818  0.0192  0.0247  74  GLN   B O   
806  C  CB  . GLN   B 65  ? 0.4320 0.3767 0.3402 0.0693  0.0142  0.0209  74  GLN   B CB  
807  C  CG  . GLN   B 65  ? 0.4981 0.4356 0.3993 0.0682  0.0094  0.0217  74  GLN   B CG  
808  C  CD  . GLN   B 65  ? 0.6067 0.5340 0.5115 0.0636  0.0074  0.0215  74  GLN   B CD  
809  O  OE1 . GLN   B 65  ? 0.6191 0.5410 0.5280 0.0665  0.0046  0.0200  74  GLN   B OE1 
810  N  NE2 . GLN   B 65  ? 0.6425 0.5678 0.5462 0.0565  0.0086  0.0234  74  GLN   B NE2 
811  N  N   . ASP   B 66  ? 0.4108 0.3758 0.3310 0.0650  0.0258  0.0235  75  ASP   B N   
812  C  CA  . ASP   B 66  ? 0.3996 0.3650 0.3250 0.0637  0.0298  0.0249  75  ASP   B CA  
813  C  C   . ASP   B 66  ? 0.3890 0.3429 0.3139 0.0671  0.0291  0.0225  75  ASP   B C   
814  O  O   . ASP   B 66  ? 0.3890 0.3407 0.3128 0.0728  0.0301  0.0244  75  ASP   B O   
815  C  CB  . ASP   B 66  ? 0.3964 0.3727 0.3220 0.0691  0.0318  0.0306  75  ASP   B CB  
816  C  CG  . ASP   B 66  ? 0.4145 0.3906 0.3456 0.0649  0.0366  0.0339  75  ASP   B CG  
817  O  OD1 . ASP   B 66  ? 0.4112 0.3810 0.3465 0.0566  0.0376  0.0313  75  ASP   B OD1 
818  O  OD2 . ASP   B 66  ? 0.4398 0.4211 0.3697 0.0710  0.0392  0.0394  75  ASP   B OD2 
819  N  N   . LEU   B 67  ? 0.3824 0.3304 0.3086 0.0633  0.0278  0.0186  76  LEU   B N   
820  C  CA  . LEU   B 67  ? 0.3815 0.3217 0.3098 0.0658  0.0266  0.0156  76  LEU   B CA  
821  C  C   . LEU   B 67  ? 0.3739 0.3131 0.3070 0.0592  0.0294  0.0119  76  LEU   B C   
822  O  O   . LEU   B 67  ? 0.3766 0.3196 0.3097 0.0533  0.0309  0.0113  76  LEU   B O   
823  C  CB  . LEU   B 67  ? 0.3967 0.3321 0.3231 0.0697  0.0207  0.0148  76  LEU   B CB  
824  C  CG  . LEU   B 67  ? 0.4257 0.3590 0.3449 0.0800  0.0158  0.0166  76  LEU   B CG  
825  C  CD1 . LEU   B 67  ? 0.4399 0.3647 0.3569 0.0826  0.0079  0.0150  76  LEU   B CD1 
826  C  CD2 . LEU   B 67  ? 0.4165 0.3476 0.3346 0.0880  0.0168  0.0166  76  LEU   B CD2 
827  N  N   . VAL   B 68  ? 0.3666 0.3013 0.3028 0.0618  0.0294  0.0089  77  VAL   B N   
828  C  CA  . VAL   B 68  ? 0.3712 0.3067 0.3116 0.0581  0.0318  0.0047  77  VAL   B CA  
829  C  C   . VAL   B 68  ? 0.3697 0.3030 0.3148 0.0629  0.0296  0.0015  77  VAL   B C   
830  O  O   . VAL   B 68  ? 0.3722 0.3001 0.3155 0.0697  0.0270  0.0016  77  VAL   B O   
831  C  CB  . VAL   B 68  ? 0.3751 0.3079 0.3135 0.0558  0.0349  0.0034  77  VAL   B CB  
832  C  CG1 . VAL   B 68  ? 0.3879 0.3133 0.3240 0.0606  0.0347  0.0049  77  VAL   B CG1 
833  C  CG2 . VAL   B 68  ? 0.3719 0.3056 0.3119 0.0543  0.0366  -0.0021 77  VAL   B CG2 
834  N  N   . SER   B 69  ? 0.3582 0.2972 0.3094 0.0598  0.0307  -0.0012 78  SER   B N   
835  C  CA  . SER   B 69  ? 0.3540 0.2947 0.3126 0.0635  0.0286  -0.0049 78  SER   B CA  
836  C  C   . SER   B 69  ? 0.3720 0.3181 0.3330 0.0635  0.0327  -0.0095 78  SER   B C   
837  O  O   . SER   B 69  ? 0.3631 0.3139 0.3218 0.0591  0.0367  -0.0094 78  SER   B O   
838  C  CB  . SER   B 69  ? 0.3548 0.3000 0.3215 0.0604  0.0250  -0.0035 78  SER   B CB  
839  O  OG  . SER   B 69  ? 0.3606 0.3150 0.3309 0.0528  0.0290  -0.0014 78  SER   B OG  
840  N  N   . TYR   B 70  ? 0.3801 0.3254 0.3444 0.0698  0.0311  -0.0140 79  TYR   B N   
841  C  CA  . TYR   B 70  ? 0.3823 0.3319 0.3475 0.0731  0.0336  -0.0196 79  TYR   B CA  
842  C  C   . TYR   B 70  ? 0.3878 0.3504 0.3660 0.0752  0.0322  -0.0228 79  TYR   B C   
843  O  O   . TYR   B 70  ? 0.3789 0.3394 0.3623 0.0781  0.0271  -0.0231 79  TYR   B O   
844  C  CB  . TYR   B 70  ? 0.3917 0.3273 0.3481 0.0806  0.0319  -0.0225 79  TYR   B CB  
845  C  CG  . TYR   B 70  ? 0.3894 0.3141 0.3358 0.0772  0.0335  -0.0194 79  TYR   B CG  
846  C  CD1 . TYR   B 70  ? 0.3969 0.3166 0.3401 0.0747  0.0328  -0.0133 79  TYR   B CD1 
847  C  CD2 . TYR   B 70  ? 0.4089 0.3291 0.3493 0.0769  0.0350  -0.0227 79  TYR   B CD2 
848  C  CE1 . TYR   B 70  ? 0.4073 0.3205 0.3444 0.0703  0.0343  -0.0099 79  TYR   B CE1 
849  C  CE2 . TYR   B 70  ? 0.4151 0.3257 0.3487 0.0721  0.0351  -0.0200 79  TYR   B CE2 
850  C  CZ  . TYR   B 70  ? 0.4289 0.3379 0.3624 0.0679  0.0352  -0.0131 79  TYR   B CZ  
851  O  OH  . TYR   B 70  ? 0.4549 0.3575 0.3845 0.0623  0.0352  -0.0100 79  TYR   B OH  
852  N  N   . CYS   B 71  ? 0.3843 0.3607 0.3672 0.0752  0.0364  -0.0259 80  CYS   B N   
853  C  CA  . CYS   B 71  ? 0.4044 0.3987 0.4021 0.0768  0.0365  -0.0287 80  CYS   B CA  
854  C  C   . CYS   B 71  ? 0.4039 0.4105 0.4152 0.0675  0.0364  -0.0229 80  CYS   B C   
855  O  O   . CYS   B 71  ? 0.4299 0.4556 0.4559 0.0662  0.0379  -0.0236 80  CYS   B O   
856  C  CB  . CYS   B 71  ? 0.4229 0.4138 0.4238 0.0861  0.0309  -0.0346 80  CYS   B CB  
857  S  SG  . CYS   B 71  ? 0.5057 0.4761 0.4883 0.0969  0.0296  -0.0397 80  CYS   B SG  
858  N  N   . GLY   B 72  ? 0.3872 0.3842 0.3944 0.0611  0.0347  -0.0170 81  GLY   B N   
859  C  CA  . GLY   B 72  ? 0.3757 0.3796 0.3938 0.0519  0.0333  -0.0109 81  GLY   B CA  
860  C  C   . GLY   B 72  ? 0.3647 0.3536 0.3731 0.0479  0.0303  -0.0057 81  GLY   B C   
861  O  O   . GLY   B 72  ? 0.3747 0.3510 0.3698 0.0519  0.0301  -0.0065 81  GLY   B O   
862  N  N   . PRO   B 73  ? 0.3627 0.3529 0.3781 0.0397  0.0277  0.0001  82  PRO   B N   
863  C  CA  . PRO   B 73  ? 0.3729 0.3487 0.3778 0.0370  0.0242  0.0049  82  PRO   B CA  
864  C  C   . PRO   B 73  ? 0.3822 0.3426 0.3821 0.0441  0.0151  0.0020  82  PRO   B C   
865  O  O   . PRO   B 73  ? 0.3883 0.3488 0.3953 0.0492  0.0101  -0.0027 82  PRO   B O   
866  C  CB  . PRO   B 73  ? 0.3924 0.3728 0.4068 0.0265  0.0230  0.0119  82  PRO   B CB  
867  C  CG  . PRO   B 73  ? 0.4037 0.3976 0.4370 0.0246  0.0216  0.0098  82  PRO   B CG  
868  C  CD  . PRO   B 73  ? 0.3716 0.3773 0.4050 0.0321  0.0281  0.0034  82  PRO   B CD  
869  N  N   . TRP   B 74  ? 0.3821 0.3307 0.3690 0.0457  0.0130  0.0046  83  TRP   B N   
870  C  CA  . TRP   B 74  ? 0.4022 0.3373 0.3811 0.0544  0.0051  0.0027  83  TRP   B CA  
871  C  C   . TRP   B 74  ? 0.4038 0.3336 0.3916 0.0545  -0.0053 0.0013  83  TRP   B C   
872  O  O   . TRP   B 74  ? 0.4241 0.3531 0.4179 0.0461  -0.0084 0.0053  83  TRP   B O   
873  C  CB  . TRP   B 74  ? 0.4028 0.3303 0.3682 0.0549  0.0047  0.0067  83  TRP   B CB  
874  C  CG  . TRP   B 74  ? 0.3972 0.3143 0.3527 0.0655  -0.0017 0.0052  83  TRP   B CG  
875  C  CD1 . TRP   B 74  ? 0.4197 0.3257 0.3716 0.0703  -0.0121 0.0048  83  TRP   B CD1 
876  C  CD2 . TRP   B 74  ? 0.4062 0.3233 0.3532 0.0732  0.0018  0.0044  83  TRP   B CD2 
877  N  NE1 . TRP   B 74  ? 0.4255 0.3264 0.3666 0.0824  -0.0148 0.0032  83  TRP   B NE1 
878  C  CE2 . TRP   B 74  ? 0.4120 0.3205 0.3508 0.0837  -0.0057 0.0037  83  TRP   B CE2 
879  C  CE3 . TRP   B 74  ? 0.3955 0.3185 0.3414 0.0726  0.0099  0.0043  83  TRP   B CE3 
880  C  CZ2 . TRP   B 74  ? 0.4199 0.3282 0.3498 0.0932  -0.0036 0.0042  83  TRP   B CZ2 
881  C  CZ3 . TRP   B 74  ? 0.4020 0.3227 0.3401 0.0801  0.0112  0.0051  83  TRP   B CZ3 
882  C  CH2 . TRP   B 74  ? 0.4011 0.3158 0.3318 0.0905  0.0053  0.0054  83  TRP   B CH2 
883  N  N   . LYS   B 75  ? 0.4017 0.3270 0.3903 0.0637  -0.0113 -0.0042 84  LYS   B N   
884  C  CA  . LYS   B 75  ? 0.4073 0.3277 0.4057 0.0646  -0.0229 -0.0073 84  LYS   B CA  
885  C  C   . LYS   B 75  ? 0.4519 0.3549 0.4381 0.0745  -0.0342 -0.0091 84  LYS   B C   
886  O  O   . LYS   B 75  ? 0.4713 0.3670 0.4642 0.0748  -0.0460 -0.0118 84  LYS   B O   
887  C  CB  . LYS   B 75  ? 0.4092 0.3370 0.4169 0.0704  -0.0239 -0.0139 84  LYS   B CB  
888  C  CG  . LYS   B 75  ? 0.4257 0.3722 0.4457 0.0638  -0.0141 -0.0139 84  LYS   B CG  
889  C  CD  . LYS   B 75  ? 0.4752 0.4335 0.5136 0.0505  -0.0145 -0.0099 84  LYS   B CD  
890  C  CE  . LYS   B 75  ? 0.5216 0.5018 0.5728 0.0478  -0.0057 -0.0114 84  LYS   B CE  
891  N  NZ  . LYS   B 75  ? 0.5479 0.5441 0.6200 0.0357  -0.0057 -0.0072 84  LYS   B NZ  
892  N  N   . LEU   B 76  ? 0.4489 0.3466 0.4182 0.0833  -0.0311 -0.0082 85  LEU   B N   
893  C  CA  . LEU   B 76  ? 0.4583 0.3423 0.4138 0.0964  -0.0407 -0.0104 85  LEU   B CA  
894  C  C   . LEU   B 76  ? 0.4865 0.3602 0.4349 0.0938  -0.0471 -0.0070 85  LEU   B C   
895  O  O   . LEU   B 76  ? 0.4899 0.3670 0.4324 0.0893  -0.0402 -0.0020 85  LEU   B O   
896  C  CB  . LEU   B 76  ? 0.4559 0.3418 0.3975 0.1073  -0.0337 -0.0096 85  LEU   B CB  
897  C  CG  . LEU   B 76  ? 0.4488 0.3425 0.3945 0.1090  -0.0259 -0.0116 85  LEU   B CG  
898  C  CD1 . LEU   B 76  ? 0.4689 0.3629 0.4010 0.1172  -0.0189 -0.0085 85  LEU   B CD1 
899  C  CD2 . LEU   B 76  ? 0.4703 0.3613 0.4233 0.1148  -0.0339 -0.0183 85  LEU   B CD2 
900  N  N   . ASP   B 77  ? 0.5202 0.3798 0.4681 0.0980  -0.0619 -0.0105 86  ASP   B N   
901  C  CA  . ASP   B 77  ? 0.5577 0.4040 0.4973 0.0960  -0.0696 -0.0075 86  ASP   B CA  
902  C  C   . ASP   B 77  ? 0.5614 0.3901 0.4851 0.1120  -0.0839 -0.0122 86  ASP   B C   
903  O  O   . ASP   B 77  ? 0.5720 0.3866 0.4869 0.1120  -0.0925 -0.0106 86  ASP   B O   
904  C  CB  . ASP   B 77  ? 0.6316 0.4746 0.5864 0.0795  -0.0739 -0.0041 86  ASP   B CB  
905  C  CG  . ASP   B 77  ? 0.7564 0.5961 0.7274 0.0765  -0.0849 -0.0088 86  ASP   B CG  
906  O  OD1 . ASP   B 77  ? 0.7826 0.6243 0.7540 0.0873  -0.0880 -0.0156 86  ASP   B OD1 
907  O  OD2 . ASP   B 77  ? 0.8297 0.6650 0.8133 0.0632  -0.0906 -0.0054 86  ASP   B OD2 
908  N  N   . ALA   B 78  ? 0.5498 0.3783 0.4675 0.1268  -0.0869 -0.0179 87  ALA   B N   
909  C  CA  . ALA   B 78  ? 0.5639 0.3764 0.4633 0.1449  -0.1005 -0.0227 87  ALA   B CA  
910  C  C   . ALA   B 78  ? 0.5708 0.3859 0.4518 0.1539  -0.0949 -0.0187 87  ALA   B C   
911  O  O   . ALA   B 78  ? 0.5520 0.3833 0.4334 0.1500  -0.0798 -0.0134 87  ALA   B O   
912  C  CB  . ALA   B 78  ? 0.5552 0.3671 0.4508 0.1602  -0.1052 -0.0295 87  ALA   B CB  
913  N  N   . ALA   B 79  ? 0.5896 0.3884 0.4538 0.1668  -0.1084 -0.0218 88  ALA   B N   
914  C  CA  . ALA   B 79  ? 0.6070 0.4093 0.4536 0.1770  -0.1048 -0.0187 88  ALA   B CA  
915  C  C   . ALA   B 79  ? 0.6215 0.4177 0.4477 0.2019  -0.1138 -0.0240 88  ALA   B C   
916  O  O   . ALA   B 79  ? 0.6457 0.4236 0.4672 0.2109  -0.1301 -0.0314 88  ALA   B O   
917  C  CB  . ALA   B 79  ? 0.6287 0.4167 0.4712 0.1700  -0.1127 -0.0167 88  ALA   B CB  
918  N  N   . TRP   B 80  ? 0.6210 0.4321 0.4344 0.2137  -0.1043 -0.0204 89  TRP   B N   
919  C  CA  . TRP   B 80  ? 0.6442 0.4520 0.4354 0.2398  -0.1121 -0.0246 89  TRP   B CA  
920  C  C   . TRP   B 80  ? 0.6684 0.4515 0.4450 0.2486  -0.1319 -0.0304 89  TRP   B C   
921  O  O   . TRP   B 80  ? 0.6662 0.4437 0.4451 0.2374  -0.1330 -0.0275 89  TRP   B O   
922  C  CB  . TRP   B 80  ? 0.6502 0.4817 0.4325 0.2486  -0.0979 -0.0179 89  TRP   B CB  
923  C  CG  . TRP   B 80  ? 0.6660 0.4999 0.4255 0.2766  -0.1030 -0.0207 89  TRP   B CG  
924  C  CD1 . TRP   B 80  ? 0.6915 0.5170 0.4398 0.2944  -0.1112 -0.0265 89  TRP   B CD1 
925  C  CD2 . TRP   B 80  ? 0.6777 0.5236 0.4214 0.2915  -0.1012 -0.0183 89  TRP   B CD2 
926  N  NE1 . TRP   B 80  ? 0.7086 0.5406 0.4343 0.3199  -0.1137 -0.0273 89  TRP   B NE1 
927  C  CE2 . TRP   B 80  ? 0.7038 0.5488 0.4268 0.3188  -0.1080 -0.0224 89  TRP   B CE2 
928  C  CE3 . TRP   B 80  ? 0.6885 0.5468 0.4334 0.2856  -0.0950 -0.0134 89  TRP   B CE3 
929  C  CZ2 . TRP   B 80  ? 0.7233 0.5830 0.4279 0.3399  -0.1065 -0.0209 89  TRP   B CZ2 
930  C  CZ3 . TRP   B 80  ? 0.7064 0.5782 0.4338 0.3062  -0.0949 -0.0126 89  TRP   B CZ3 
931  C  CH2 . TRP   B 80  ? 0.7191 0.5921 0.4268 0.3332  -0.1005 -0.0162 89  TRP   B CH2 
932  N  N   . ASP   B 81  ? 0.7047 0.4708 0.4665 0.2684  -0.1484 -0.0390 90  ASP   B N   
933  C  CA  . ASP   B 81  ? 0.7664 0.5051 0.5126 0.2782  -0.1695 -0.0456 90  ASP   B CA  
934  C  C   . ASP   B 81  ? 0.8210 0.5641 0.5438 0.2973  -0.1703 -0.0450 90  ASP   B C   
935  O  O   . ASP   B 81  ? 0.8568 0.5759 0.5637 0.3070  -0.1882 -0.0505 90  ASP   B O   
936  C  CB  . ASP   B 81  ? 0.7851 0.5021 0.5234 0.2930  -0.1892 -0.0564 90  ASP   B CB  
937  C  CG  . ASP   B 81  ? 0.8270 0.5533 0.5459 0.3207  -0.1884 -0.0602 90  ASP   B CG  
938  O  OD1 . ASP   B 81  ? 0.8094 0.5593 0.5192 0.3303  -0.1732 -0.0540 90  ASP   B OD1 
939  O  OD2 . ASP   B 81  ? 0.9056 0.6167 0.6185 0.3332  -0.2030 -0.0692 90  ASP   B OD2 
940  N  N   . GLY   B 82  ? 0.8198 0.5925 0.5398 0.3041  -0.1524 -0.0387 91  GLY   B N   
941  C  CA  . GLY   B 82  ? 0.8302 0.6139 0.5309 0.3221  -0.1511 -0.0374 91  GLY   B CA  
942  C  C   . GLY   B 82  ? 0.8658 0.6478 0.5405 0.3550  -0.1606 -0.0438 91  GLY   B C   
943  O  O   . GLY   B 82  ? 0.8867 0.6792 0.5437 0.3736  -0.1606 -0.0436 91  GLY   B O   
944  N  N   . LEU   B 83  ? 0.8666 0.6360 0.5377 0.3643  -0.1695 -0.0502 92  LEU   B N   
945  C  CA  . LEU   B 83  ? 0.9022 0.6676 0.5460 0.3979  -0.1803 -0.0575 92  LEU   B CA  
946  C  C   . LEU   B 83  ? 0.9039 0.6844 0.5471 0.4080  -0.1709 -0.0560 92  LEU   B C   
947  O  O   . LEU   B 83  ? 0.9121 0.7061 0.5345 0.4347  -0.1684 -0.0561 92  LEU   B O   
948  C  CB  . LEU   B 83  ? 0.9368 0.6617 0.5681 0.4070  -0.2087 -0.0704 92  LEU   B CB  
949  C  CG  . LEU   B 83  ? 1.0021 0.7012 0.6229 0.4072  -0.2259 -0.0749 92  LEU   B CG  
950  C  CD1 . LEU   B 83  ? 1.0371 0.6979 0.6412 0.4230  -0.2547 -0.0885 92  LEU   B CD1 
951  C  CD2 . LEU   B 83  ? 1.0107 0.7261 0.6098 0.4285  -0.2216 -0.0730 92  LEU   B CD2 
952  N  N   . SER   B 84  ? 0.8879 0.6638 0.5515 0.3892  -0.1678 -0.0556 93  SER   B N   
953  C  CA  . SER   B 84  ? 0.8840 0.6668 0.5459 0.3987  -0.1629 -0.0560 93  SER   B CA  
954  C  C   . SER   B 84  ? 0.8314 0.6458 0.5043 0.3904  -0.1372 -0.0436 93  SER   B C   
955  O  O   . SER   B 84  ? 0.7993 0.6293 0.4899 0.3689  -0.1225 -0.0348 93  SER   B O   
956  C  CB  . SER   B 84  ? 0.9199 0.6803 0.5970 0.3854  -0.1752 -0.0635 93  SER   B CB  
957  O  OG  . SER   B 84  ? 0.9839 0.7139 0.6581 0.3845  -0.1986 -0.0732 93  SER   B OG  
958  N  N   . GLU   B 85  ? 0.8044 0.6269 0.4655 0.4082  -0.1325 -0.0427 94  GLU   B N   
959  C  CA  . GLU   B 85  ? 0.7710 0.6186 0.4415 0.4005  -0.1099 -0.0307 94  GLU   B CA  
960  C  C   . GLU   B 85  ? 0.7417 0.5825 0.4388 0.3723  -0.1060 -0.0303 94  GLU   B C   
961  O  O   . GLU   B 85  ? 0.7427 0.5613 0.4474 0.3652  -0.1211 -0.0397 94  GLU   B O   
962  C  CB  . GLU   B 85  ? 0.8002 0.6556 0.4489 0.4279  -0.1065 -0.0293 94  GLU   B CB  
963  C  CG  . GLU   B 85  ? 0.8382 0.7121 0.4645 0.4528  -0.1028 -0.0252 94  GLU   B CG  
964  C  CD  . GLU   B 85  ? 0.9130 0.8038 0.5191 0.4779  -0.0929 -0.0189 94  GLU   B CD  
965  O  OE1 . GLU   B 85  ? 0.9146 0.7955 0.5174 0.4822  -0.0942 -0.0208 94  GLU   B OE1 
966  O  OE2 . GLU   B 85  ? 0.9404 0.8553 0.5334 0.4940  -0.0838 -0.0117 94  GLU   B OE2 
967  N  N   . VAL   B 86  ? 0.7043 0.5649 0.4160 0.3558  -0.0862 -0.0191 95  VAL   B N   
968  C  CA  . VAL   B 86  ? 0.6540 0.5115 0.3890 0.3311  -0.0804 -0.0179 95  VAL   B CA  
969  C  C   . VAL   B 86  ? 0.6596 0.5301 0.3933 0.3337  -0.0651 -0.0097 95  VAL   B C   
970  O  O   . VAL   B 86  ? 0.6873 0.5699 0.4035 0.3528  -0.0585 -0.0039 95  VAL   B O   
971  C  CB  . VAL   B 86  ? 0.6163 0.4837 0.3705 0.3059  -0.0711 -0.0120 95  VAL   B CB  
972  C  CG1 . VAL   B 86  ? 0.6259 0.4807 0.3781 0.3047  -0.0849 -0.0181 95  VAL   B CG1 
973  C  CG2 . VAL   B 86  ? 0.6143 0.5080 0.3682 0.3048  -0.0527 0.0003  95  VAL   B CG2 
974  N  N   . GLN   B 87  ? 0.6340 0.5017 0.3850 0.3158  -0.0595 -0.0087 96  GLN   B N   
975  C  CA  . GLN   B 87  ? 0.6306 0.5077 0.3802 0.3163  -0.0452 -0.0001 96  GLN   B CA  
976  C  C   . GLN   B 87  ? 0.6172 0.5042 0.3878 0.2901  -0.0311 0.0077  96  GLN   B C   
977  O  O   . GLN   B 87  ? 0.6078 0.4877 0.3953 0.2726  -0.0350 0.0026  96  GLN   B O   
978  C  CB  . GLN   B 87  ? 0.6474 0.5090 0.3918 0.3261  -0.0535 -0.0076 96  GLN   B CB  
979  C  CG  . GLN   B 87  ? 0.6827 0.5380 0.4008 0.3568  -0.0637 -0.0125 96  GLN   B CG  
980  C  CD  . GLN   B 87  ? 0.6977 0.5390 0.4079 0.3693  -0.0715 -0.0194 96  GLN   B CD  
981  O  OE1 . GLN   B 87  ? 0.6651 0.5017 0.3886 0.3569  -0.0694 -0.0208 96  GLN   B OE1 
982  N  NE2 . GLN   B 87  ? 0.7531 0.5880 0.4386 0.3976  -0.0815 -0.0246 96  GLN   B NE2 
983  N  N   . LEU   B 88  ? 0.6112 0.5149 0.3806 0.2877  -0.0151 0.0201  97  LEU   B N   
984  C  CA  . LEU   B 88  ? 0.5975 0.5074 0.3842 0.2652  -0.0029 0.0272  97  LEU   B CA  
985  C  C   . LEU   B 88  ? 0.5987 0.4976 0.3832 0.2670  -0.0009 0.0270  97  LEU   B C   
986  O  O   . LEU   B 88  ? 0.6031 0.5017 0.3710 0.2842  0.0018  0.0313  97  LEU   B O   
987  C  CB  . LEU   B 88  ? 0.5815 0.5132 0.3700 0.2602  0.0120  0.0407  97  LEU   B CB  
988  C  CG  . LEU   B 88  ? 0.5893 0.5251 0.3925 0.2395  0.0244  0.0491  97  LEU   B CG  
989  C  CD1 . LEU   B 88  ? 0.5551 0.4856 0.3773 0.2179  0.0211  0.0426  97  LEU   B CD1 
990  C  CD2 . LEU   B 88  ? 0.5982 0.5568 0.4035 0.2361  0.0377  0.0629  97  LEU   B CD2 
991  N  N   . LEU   B 89  ? 0.5759 0.4655 0.3750 0.2515  -0.0027 0.0219  98  LEU   B N   
992  C  CA  . LEU   B 89  ? 0.5765 0.4562 0.3740 0.2525  -0.0006 0.0216  98  LEU   B CA  
993  C  C   . LEU   B 89  ? 0.5751 0.4621 0.3803 0.2367  0.0138  0.0327  98  LEU   B C   
994  O  O   . LEU   B 89  ? 0.5423 0.4279 0.3632 0.2186  0.0154  0.0306  98  LEU   B O   
995  C  CB  . LEU   B 89  ? 0.6000 0.4677 0.4092 0.2463  -0.0112 0.0093  98  LEU   B CB  
996  C  CG  . LEU   B 89  ? 0.6503 0.5077 0.4582 0.2487  -0.0110 0.0067  98  LEU   B CG  
997  C  CD1 . LEU   B 89  ? 0.7144 0.5654 0.5000 0.2714  -0.0117 0.0091  98  LEU   B CD1 
998  C  CD2 . LEU   B 89  ? 0.6562 0.5071 0.4782 0.2433  -0.0223 -0.0059 98  LEU   B CD2 
999  N  N   . ALA   B 90  ? 0.5777 0.4745 0.3727 0.2430  0.0241  0.0451  99  ALA   B N   
1000 C  CA  . ALA   B 90  ? 0.5775 0.4818 0.3796 0.2281  0.0374  0.0576  99  ALA   B CA  
1001 C  C   . ALA   B 90  ? 0.5856 0.4742 0.3869 0.2234  0.0399  0.0587  99  ALA   B C   
1002 O  O   . ALA   B 90  ? 0.5971 0.4754 0.3831 0.2388  0.0383  0.0588  99  ALA   B O   
1003 C  CB  . ALA   B 90  ? 0.6030 0.5236 0.3944 0.2377  0.0473  0.0714  99  ALA   B CB  
1004 N  N   . VAL   B 91  ? 0.5638 0.4500 0.3796 0.2033  0.0439  0.0600  100 VAL   B N   
1005 C  CA  . VAL   B 91  ? 0.5703 0.4408 0.3849 0.1978  0.0464  0.0616  100 VAL   B CA  
1006 C  C   . VAL   B 91  ? 0.5925 0.4682 0.4129 0.1825  0.0575  0.0756  100 VAL   B C   
1007 O  O   . VAL   B 91  ? 0.5784 0.4543 0.4128 0.1649  0.0583  0.0744  100 VAL   B O   
1008 C  CB  . VAL   B 91  ? 0.5705 0.4303 0.3957 0.1898  0.0386  0.0484  100 VAL   B CB  
1009 C  CG1 . VAL   B 91  ? 0.5893 0.4313 0.4092 0.1886  0.0400  0.0493  100 VAL   B CG1 
1010 C  CG2 . VAL   B 91  ? 0.5619 0.4201 0.3866 0.2014  0.0271  0.0352  100 VAL   B CG2 
1011 N  N   . PRO   B 92  ? 0.6090 0.4897 0.4188 0.1890  0.0660  0.0897  101 PRO   B N   
1012 C  CA  . PRO   B 92  ? 0.6105 0.4977 0.4282 0.1729  0.0762  0.1044  101 PRO   B CA  
1013 C  C   . PRO   B 92  ? 0.6071 0.4720 0.4244 0.1623  0.0772  0.1072  101 PRO   B C   
1014 O  O   . PRO   B 92  ? 0.6231 0.4688 0.4273 0.1731  0.0730  0.1024  101 PRO   B O   
1015 C  CB  . PRO   B 92  ? 0.6447 0.5447 0.4494 0.1860  0.0851  0.1191  101 PRO   B CB  
1016 C  CG  . PRO   B 92  ? 0.6649 0.5668 0.4550 0.2095  0.0783  0.1099  101 PRO   B CG  
1017 C  CD  . PRO   B 92  ? 0.6338 0.5152 0.4238 0.2115  0.0666  0.0934  101 PRO   B CD  
1018 N  N   . PRO   B 93  ? 0.6039 0.4705 0.4340 0.1425  0.0820  0.1153  102 PRO   B N   
1019 C  CA  . PRO   B 93  ? 0.6270 0.4687 0.4552 0.1325  0.0812  0.1175  102 PRO   B CA  
1020 C  C   . PRO   B 93  ? 0.6557 0.4813 0.4645 0.1434  0.0855  0.1284  102 PRO   B C   
1021 O  O   . PRO   B 93  ? 0.6699 0.5081 0.4736 0.1475  0.0944  0.1432  102 PRO   B O   
1022 C  CB  . PRO   B 93  ? 0.6278 0.4784 0.4735 0.1103  0.0855  0.1263  102 PRO   B CB  
1023 C  CG  . PRO   B 93  ? 0.6254 0.5024 0.4849 0.1079  0.0844  0.1202  102 PRO   B CG  
1024 C  CD  . PRO   B 93  ? 0.6090 0.4987 0.4565 0.1284  0.0861  0.1205  102 PRO   B CD  
1025 N  N   . GLY   B 94  ? 0.6727 0.4721 0.4699 0.1498  0.0794  0.1209  103 GLY   B N   
1026 C  CA  . GLY   B 94  ? 0.6935 0.4726 0.4696 0.1613  0.0819  0.1296  103 GLY   B CA  
1027 C  C   . GLY   B 94  ? 0.7153 0.5014 0.4740 0.1849  0.0835  0.1309  103 GLY   B C   
1028 O  O   . GLY   B 94  ? 0.7356 0.5084 0.4753 0.1954  0.0876  0.1412  103 GLY   B O   
1029 N  N   . GLU   B 95  ? 0.7055 0.5121 0.4693 0.1937  0.0802  0.1215  104 GLU   B N   
1030 C  CA  . GLU   B 95  ? 0.7119 0.5257 0.4588 0.2174  0.0799  0.1212  104 GLU   B CA  
1031 C  C   . GLU   B 95  ? 0.7061 0.5178 0.4527 0.2301  0.0670  0.1008  104 GLU   B C   
1032 O  O   . GLU   B 95  ? 0.6733 0.4889 0.4369 0.2192  0.0609  0.0891  104 GLU   B O   
1033 C  CB  . GLU   B 95  ? 0.7070 0.5501 0.4575 0.2189  0.0886  0.1324  104 GLU   B CB  
1034 C  CG  . GLU   B 95  ? 0.7564 0.6073 0.5121 0.2040  0.1017  0.1536  104 GLU   B CG  
1035 C  CD  . GLU   B 95  ? 0.8234 0.7070 0.5865 0.2029  0.1112  0.1656  104 GLU   B CD  
1036 O  OE1 . GLU   B 95  ? 0.7847 0.6856 0.5505 0.2122  0.1068  0.1560  104 GLU   B OE1 
1037 O  OE2 . GLU   B 95  ? 0.8586 0.7509 0.6246 0.1933  0.1228  0.1848  104 GLU   B OE2 
1038 N  N   . ARG   B 96  ? 0.7183 0.5249 0.4460 0.2533  0.0627  0.0971  105 ARG   B N   
1039 C  CA  . ARG   B 96  ? 0.7350 0.5391 0.4625 0.2662  0.0493  0.0783  105 ARG   B CA  
1040 C  C   . ARG   B 96  ? 0.7055 0.5293 0.4459 0.2643  0.0451  0.0712  105 ARG   B C   
1041 O  O   . ARG   B 96  ? 0.6974 0.5382 0.4370 0.2648  0.0522  0.0810  105 ARG   B O   
1042 C  CB  . ARG   B 96  ? 0.8123 0.6079 0.5148 0.2930  0.0455  0.0774  105 ARG   B CB  
1043 C  CG  . ARG   B 96  ? 0.8893 0.6728 0.5904 0.3048  0.0305  0.0583  105 ARG   B CG  
1044 C  CD  . ARG   B 96  ? 0.9693 0.7360 0.6448 0.3279  0.0272  0.0583  105 ARG   B CD  
1045 N  NE  . ARG   B 96  ? 1.0518 0.8235 0.7053 0.3451  0.0343  0.0710  105 ARG   B NE  
1046 C  CZ  . ARG   B 96  ? 1.1274 0.8889 0.7613 0.3513  0.0442  0.0864  105 ARG   B CZ  
1047 N  NH1 . ARG   B 96  ? 1.1278 0.8707 0.7609 0.3411  0.0471  0.0907  105 ARG   B NH1 
1048 N  NH2 . ARG   B 96  ? 1.1511 0.9204 0.7649 0.3683  0.0510  0.0980  105 ARG   B NH2 
1049 N  N   . ALA   B 97  ? 0.6800 0.5020 0.4321 0.2628  0.0332  0.0543  106 ALA   B N   
1050 C  CA  . ALA   B 97  ? 0.6829 0.5189 0.4452 0.2625  0.0268  0.0463  106 ALA   B CA  
1051 C  C   . ALA   B 97  ? 0.6998 0.5403 0.4436 0.2855  0.0236  0.0471  106 ALA   B C   
1052 O  O   . ALA   B 97  ? 0.7192 0.5483 0.4456 0.3044  0.0188  0.0442  106 ALA   B O   
1053 C  CB  . ALA   B 97  ? 0.6894 0.5200 0.4645 0.2592  0.0144  0.0297  106 ALA   B CB  
1054 N  N   . LYS   B 98  ? 0.6908 0.5477 0.4369 0.2856  0.0256  0.0505  107 LYS   B N   
1055 C  CA  . LYS   B 98  ? 0.7251 0.5887 0.4526 0.3083  0.0233  0.0520  107 LYS   B CA  
1056 C  C   . LYS   B 98  ? 0.7010 0.5745 0.4363 0.3077  0.0155  0.0444  107 LYS   B C   
1057 O  O   . LYS   B 98  ? 0.6796 0.5635 0.4323 0.2888  0.0198  0.0467  107 LYS   B O   
1058 C  CB  . LYS   B 98  ? 0.8008 0.6774 0.5184 0.3105  0.0394  0.0711  107 LYS   B CB  
1059 C  CG  . LYS   B 98  ? 0.9277 0.8173 0.6256 0.3338  0.0411  0.0763  107 LYS   B CG  
1060 C  CD  . LYS   B 98  ? 1.0118 0.9194 0.7065 0.3299  0.0595  0.0976  107 LYS   B CD  
1061 C  CE  . LYS   B 98  ? 1.0490 0.9723 0.7682 0.3034  0.0680  0.1048  107 LYS   B CE  
1062 N  NZ  . LYS   B 98  ? 1.0599 0.9742 0.7893 0.2829  0.0767  0.1144  107 LYS   B NZ  
1063 N  N   . ASN   B 99  ? 0.6945 0.5627 0.4171 0.3280  0.0026  0.0341  108 ASN   B N   
1064 C  CA  . ASN   B 99  ? 0.6967 0.5701 0.4224 0.3308  -0.0071 0.0264  108 ASN   B CA  
1065 C  C   . ASN   B 99  ? 0.7223 0.6122 0.4330 0.3456  -0.0010 0.0352  108 ASN   B C   
1066 O  O   . ASN   B 99  ? 0.7519 0.6425 0.4406 0.3678  0.0010  0.0395  108 ASN   B O   
1067 C  CB  . ASN   B 99  ? 0.7062 0.5634 0.4269 0.3443  -0.0269 0.0097  108 ASN   B CB  
1068 C  CG  . ASN   B 99  ? 0.7628 0.6078 0.5013 0.3307  -0.0354 -0.0010 108 ASN   B CG  
1069 O  OD1 . ASN   B 99  ? 0.8051 0.6435 0.5444 0.3287  -0.0320 -0.0003 108 ASN   B OD1 
1070 N  ND2 . ASN   B 99  ? 0.7475 0.5890 0.5001 0.3217  -0.0471 -0.0109 108 ASN   B ND2 
1071 N  N   . ILE   B 100 ? 0.7085 0.6121 0.4292 0.3359  0.0014  0.0374  109 ILE   B N   
1072 C  CA  . ILE   B 100 ? 0.7026 0.6253 0.4111 0.3499  0.0065  0.0446  109 ILE   B CA  
1073 C  C   . ILE   B 100 ? 0.7039 0.6228 0.4115 0.3557  -0.0082 0.0328  109 ILE   B C   
1074 O  O   . ILE   B 100 ? 0.6801 0.5971 0.4060 0.3362  -0.0113 0.0287  109 ILE   B O   
1075 C  CB  . ILE   B 100 ? 0.7197 0.6656 0.4410 0.3332  0.0243  0.0602  109 ILE   B CB  
1076 C  CG1 . ILE   B 100 ? 0.7521 0.6964 0.4776 0.3220  0.0373  0.0718  109 ILE   B CG1 
1077 C  CG2 . ILE   B 100 ? 0.7242 0.6945 0.4339 0.3491  0.0305  0.0684  109 ILE   B CG2 
1078 C  CD1 . ILE   B 100 ? 0.7878 0.7348 0.4917 0.3423  0.0444  0.0814  109 ILE   B CD1 
1079 N  N   . GLN   B 101 ? 0.7197 0.6365 0.4049 0.3828  -0.0177 0.0274  110 GLN   B N   
1080 C  CA  . GLN   B 101 ? 0.7319 0.6408 0.4125 0.3910  -0.0340 0.0156  110 GLN   B CA  
1081 C  C   . GLN   B 101 ? 0.7465 0.6783 0.4236 0.3956  -0.0269 0.0228  110 GLN   B C   
1082 O  O   . GLN   B 101 ? 0.7758 0.7289 0.4419 0.4082  -0.0141 0.0342  110 GLN   B O   
1083 C  CB  . GLN   B 101 ? 0.7750 0.6666 0.4313 0.4201  -0.0508 0.0041  110 GLN   B CB  
1084 C  CG  . GLN   B 101 ? 0.7864 0.6617 0.4396 0.4260  -0.0716 -0.0102 110 GLN   B CG  
1085 C  CD  . GLN   B 101 ? 0.8400 0.6918 0.4764 0.4473  -0.0913 -0.0240 110 GLN   B CD  
1086 O  OE1 . GLN   B 101 ? 0.8359 0.6770 0.4760 0.4452  -0.0935 -0.0273 110 GLN   B OE1 
1087 N  NE2 . GLN   B 101 ? 0.8755 0.7184 0.4929 0.4690  -0.1073 -0.0332 110 GLN   B NE2 
1088 N  N   . THR   B 102 ? 0.7172 0.6459 0.4029 0.3866  -0.0353 0.0166  111 THR   B N   
1089 C  CA  . THR   B 102 ? 0.6939 0.6447 0.3777 0.3901  -0.0292 0.0225  111 THR   B CA  
1090 C  C   . THR   B 102 ? 0.7031 0.6394 0.3853 0.3912  -0.0462 0.0108  111 THR   B C   
1091 O  O   . THR   B 102 ? 0.7275 0.6403 0.4193 0.3784  -0.0580 0.0016  111 THR   B O   
1092 C  CB  . THR   B 102 ? 0.6829 0.6562 0.3898 0.3642  -0.0102 0.0358  111 THR   B CB  
1093 O  OG1 . THR   B 102 ? 0.7078 0.7098 0.4119 0.3713  -0.0014 0.0441  111 THR   B OG1 
1094 C  CG2 . THR   B 102 ? 0.6651 0.6265 0.3951 0.3358  -0.0137 0.0311  111 THR   B CG2 
1095 N  N   . LEU   B 103 ? 0.6819 0.6320 0.3517 0.4065  -0.0477 0.0114  112 LEU   B N   
1096 C  CA  . LEU   B 103 ? 0.6935 0.6295 0.3618 0.4056  -0.0628 0.0019  112 LEU   B CA  
1097 C  C   . LEU   B 103 ? 0.6829 0.6374 0.3719 0.3822  -0.0507 0.0098  112 LEU   B C   
1098 O  O   . LEU   B 103 ? 0.6878 0.6727 0.3775 0.3859  -0.0373 0.0195  112 LEU   B O   
1099 C  CB  . LEU   B 103 ? 0.7229 0.6608 0.3631 0.4383  -0.0738 -0.0039 112 LEU   B CB  
1100 C  CG  . LEU   B 103 ? 0.7676 0.6867 0.4057 0.4356  -0.0903 -0.0134 112 LEU   B CG  
1101 C  CD1 . LEU   B 103 ? 0.7887 0.6690 0.4239 0.4342  -0.1115 -0.0264 112 LEU   B CD1 
1102 C  CD2 . LEU   B 103 ? 0.8149 0.7450 0.4286 0.4648  -0.0965 -0.0161 112 LEU   B CD2 
1103 N  N   . PRO   B 104 ? 0.6654 0.6032 0.3719 0.3579  -0.0559 0.0057  113 PRO   B N   
1104 C  CA  . PRO   B 104 ? 0.6411 0.5958 0.3656 0.3371  -0.0452 0.0125  113 PRO   B CA  
1105 C  C   . PRO   B 104 ? 0.6609 0.6288 0.3746 0.3502  -0.0482 0.0122  113 PRO   B C   
1106 O  O   . PRO   B 104 ? 0.6923 0.6456 0.3857 0.3709  -0.0635 0.0036  113 PRO   B O   
1107 C  CB  . PRO   B 104 ? 0.6394 0.5695 0.3783 0.3146  -0.0537 0.0062  113 PRO   B CB  
1108 C  CG  . PRO   B 104 ? 0.6369 0.5454 0.3747 0.3164  -0.0615 0.0001  113 PRO   B CG  
1109 C  CD  . PRO   B 104 ? 0.6552 0.5610 0.3662 0.3489  -0.0707 -0.0044 113 PRO   B CD  
1110 N  N   . GLY   B 105 ? 0.6479 0.6426 0.3753 0.3382  -0.0345 0.0210  114 GLY   B N   
1111 C  CA  . GLY   B 105 ? 0.6544 0.6641 0.3785 0.3435  -0.0359 0.0211  114 GLY   B CA  
1112 C  C   . GLY   B 105 ? 0.6641 0.6562 0.4001 0.3218  -0.0419 0.0169  114 GLY   B C   
1113 O  O   . GLY   B 105 ? 0.6642 0.6306 0.4070 0.3076  -0.0479 0.0126  114 GLY   B O   
1114 N  N   . ILE   B 106 ? 0.6604 0.6678 0.3993 0.3194  -0.0401 0.0186  115 ILE   B N   
1115 C  CA  . ILE   B 106 ? 0.6727 0.6641 0.4193 0.3017  -0.0460 0.0151  115 ILE   B CA  
1116 C  C   . ILE   B 106 ? 0.6465 0.6647 0.4112 0.2855  -0.0333 0.0222  115 ILE   B C   
1117 O  O   . ILE   B 106 ? 0.6502 0.6976 0.4134 0.2962  -0.0275 0.0262  115 ILE   B O   
1118 C  CB  . ILE   B 106 ? 0.7261 0.7013 0.4509 0.3199  -0.0630 0.0069  115 ILE   B CB  
1119 C  CG1 . ILE   B 106 ? 0.7874 0.7340 0.4908 0.3398  -0.0795 -0.0018 115 ILE   B CG1 
1120 C  CG2 . ILE   B 106 ? 0.7382 0.6963 0.4682 0.3031  -0.0689 0.0045  115 ILE   B CG2 
1121 C  CD1 . ILE   B 106 ? 0.8294 0.7452 0.5389 0.3255  -0.0871 -0.0059 115 ILE   B CD1 
1122 N  N   . PHE   B 107 ? 0.6193 0.6270 0.3992 0.2617  -0.0313 0.0224  116 PHE   B N   
1123 C  CA  . PHE   B 107 ? 0.6066 0.6332 0.4001 0.2476  -0.0241 0.0262  116 PHE   B CA  
1124 C  C   . PHE   B 107 ? 0.6439 0.6509 0.4254 0.2504  -0.0371 0.0197  116 PHE   B C   
1125 O  O   . PHE   B 107 ? 0.6639 0.6417 0.4436 0.2412  -0.0448 0.0158  116 PHE   B O   
1126 C  CB  . PHE   B 107 ? 0.5852 0.6083 0.3995 0.2212  -0.0155 0.0294  116 PHE   B CB  
1127 C  CG  . PHE   B 107 ? 0.5586 0.6034 0.3883 0.2129  -0.0013 0.0374  116 PHE   B CG  
1128 C  CD1 . PHE   B 107 ? 0.5597 0.6270 0.3858 0.2275  0.0049  0.0429  116 PHE   B CD1 
1129 C  CD2 . PHE   B 107 ? 0.5460 0.5879 0.3927 0.1911  0.0056  0.0398  116 PHE   B CD2 
1130 C  CE1 . PHE   B 107 ? 0.5561 0.6406 0.3958 0.2188  0.0177  0.0517  116 PHE   B CE1 
1131 C  CE2 . PHE   B 107 ? 0.5438 0.6011 0.4032 0.1833  0.0171  0.0471  116 PHE   B CE2 
1132 C  CZ  . PHE   B 107 ? 0.5499 0.6280 0.4062 0.1962  0.0233  0.0537  116 PHE   B CZ  
1133 N  N   . LYS   B 108 ? 0.6422 0.6659 0.4161 0.2622  -0.0394 0.0191  117 LYS   B N   
1134 C  CA  . LYS   B 108 ? 0.6642 0.6692 0.4254 0.2651  -0.0515 0.0137  117 LYS   B CA  
1135 C  C   . LYS   B 108 ? 0.6524 0.6690 0.4288 0.2461  -0.0446 0.0166  117 LYS   B C   
1136 O  O   . LYS   B 108 ? 0.6443 0.6939 0.4334 0.2440  -0.0347 0.0209  117 LYS   B O   
1137 C  CB  . LYS   B 108 ? 0.7115 0.7273 0.4527 0.2923  -0.0593 0.0102  117 LYS   B CB  
1138 C  CG  . LYS   B 108 ? 0.8245 0.8280 0.5479 0.3138  -0.0673 0.0063  117 LYS   B CG  
1139 C  CD  . LYS   B 108 ? 0.9198 0.9403 0.6236 0.3435  -0.0729 0.0033  117 LYS   B CD  
1140 C  CE  . LYS   B 108 ? 1.0215 1.0181 0.7050 0.3538  -0.0893 -0.0040 117 LYS   B CE  
1141 N  NZ  . LYS   B 108 ? 1.0655 1.0704 0.7245 0.3869  -0.0985 -0.0093 117 LYS   B NZ  
1142 N  N   . THR   B 109 ? 0.6543 0.6453 0.4312 0.2314  -0.0492 0.0148  118 THR   B N   
1143 C  CA  . THR   B 109 ? 0.6623 0.6623 0.4511 0.2148  -0.0435 0.0168  118 THR   B CA  
1144 C  C   . THR   B 109 ? 0.7013 0.6803 0.4742 0.2179  -0.0546 0.0132  118 THR   B C   
1145 O  O   . THR   B 109 ? 0.7341 0.6862 0.4890 0.2284  -0.0668 0.0097  118 THR   B O   
1146 C  CB  . THR   B 109 ? 0.6493 0.6437 0.4565 0.1916  -0.0347 0.0198  118 THR   B CB  
1147 O  OG1 . THR   B 109 ? 0.6599 0.6223 0.4608 0.1839  -0.0417 0.0177  118 THR   B OG1 
1148 C  CG2 . THR   B 109 ? 0.6243 0.6286 0.4425 0.1900  -0.0265 0.0228  118 THR   B CG2 
1149 N  N   . LYS   B 110 ? 0.7013 0.6894 0.4803 0.2078  -0.0512 0.0142  119 LYS   B N   
1150 C  CA  . LYS   B 110 ? 0.7233 0.6907 0.4863 0.2097  -0.0608 0.0118  119 LYS   B CA  
1151 C  C   . LYS   B 110 ? 0.7618 0.6920 0.5190 0.1985  -0.0662 0.0125  119 LYS   B C   
1152 O  O   . LYS   B 110 ? 0.7939 0.6995 0.5338 0.2023  -0.0764 0.0115  119 LYS   B O   
1153 C  CB  . LYS   B 110 ? 0.7112 0.6974 0.4832 0.2005  -0.0551 0.0127  119 LYS   B CB  
1154 C  CG  . LYS   B 110 ? 0.7371 0.7236 0.5271 0.1779  -0.0454 0.0157  119 LYS   B CG  
1155 C  CD  . LYS   B 110 ? 0.7781 0.7769 0.5720 0.1711  -0.0431 0.0151  119 LYS   B CD  
1156 C  CE  . LYS   B 110 ? 0.8429 0.8221 0.6374 0.1550  -0.0409 0.0166  119 LYS   B CE  
1157 N  NZ  . LYS   B 110 ? 0.8907 0.8785 0.7054 0.1395  -0.0307 0.0185  119 LYS   B NZ  
1158 N  N   . ASP   B 111 ? 0.7466 0.6737 0.5188 0.1846  -0.0592 0.0148  120 ASP   B N   
1159 C  CA  . ASP   B 111 ? 0.7683 0.6672 0.5408 0.1722  -0.0622 0.0162  120 ASP   B CA  
1160 C  C   . ASP   B 111 ? 0.7765 0.6585 0.5461 0.1782  -0.0690 0.0143  120 ASP   B C   
1161 O  O   . ASP   B 111 ? 0.7925 0.6572 0.5685 0.1661  -0.0697 0.0156  120 ASP   B O   
1162 C  CB  . ASP   B 111 ? 0.7765 0.6850 0.5683 0.1521  -0.0500 0.0194  120 ASP   B CB  
1163 C  CG  . ASP   B 111 ? 0.8309 0.7503 0.6232 0.1462  -0.0458 0.0204  120 ASP   B CG  
1164 O  OD1 . ASP   B 111 ? 0.8526 0.7579 0.6290 0.1508  -0.0533 0.0204  120 ASP   B OD1 
1165 O  OD2 . ASP   B 111 ? 0.8355 0.7762 0.6428 0.1377  -0.0361 0.0211  120 ASP   B OD2 
1166 N  N   . GLY   B 112 ? 0.7621 0.6499 0.5219 0.1973  -0.0743 0.0109  121 GLY   B N   
1167 C  CA  . GLY   B 112 ? 0.7653 0.6370 0.5198 0.2058  -0.0821 0.0079  121 GLY   B CA  
1168 C  C   . GLY   B 112 ? 0.7508 0.6462 0.5137 0.2132  -0.0739 0.0080  121 GLY   B C   
1169 O  O   . GLY   B 112 ? 0.7427 0.6669 0.5186 0.2084  -0.0611 0.0114  121 GLY   B O   
1170 N  N   . ASP   B 113 ? 0.7324 0.6144 0.4871 0.2252  -0.0821 0.0043  122 ASP   B N   
1171 C  CA  . ASP   B 113 ? 0.7148 0.6149 0.4723 0.2360  -0.0762 0.0044  122 ASP   B CA  
1172 C  C   . ASP   B 113 ? 0.7011 0.5972 0.4741 0.2226  -0.0703 0.0057  122 ASP   B C   
1173 O  O   . ASP   B 113 ? 0.7195 0.5921 0.4957 0.2124  -0.0769 0.0038  122 ASP   B O   
1174 C  CB  . ASP   B 113 ? 0.7556 0.6451 0.4905 0.2623  -0.0897 -0.0014 122 ASP   B CB  
1175 C  CG  . ASP   B 113 ? 0.8546 0.7531 0.5730 0.2795  -0.0948 -0.0031 122 ASP   B CG  
1176 O  OD1 . ASP   B 113 ? 0.8771 0.7838 0.6002 0.2699  -0.0905 -0.0005 122 ASP   B OD1 
1177 O  OD2 . ASP   B 113 ? 0.9280 0.8253 0.6277 0.3038  -0.1035 -0.0076 122 ASP   B OD2 
1178 N  N   . ILE   B 114 ? 0.6592 0.5789 0.4418 0.2234  -0.0581 0.0092  123 ILE   B N   
1179 C  CA  . ILE   B 114 ? 0.6587 0.5769 0.4546 0.2130  -0.0517 0.0105  123 ILE   B CA  
1180 C  C   . ILE   B 114 ? 0.6370 0.5656 0.4253 0.2312  -0.0500 0.0106  123 ILE   B C   
1181 O  O   . ILE   B 114 ? 0.6184 0.5689 0.4010 0.2437  -0.0451 0.0136  123 ILE   B O   
1182 C  CB  . ILE   B 114 ? 0.6636 0.6012 0.4791 0.1934  -0.0365 0.0164  123 ILE   B CB  
1183 C  CG1 . ILE   B 114 ? 0.7136 0.6464 0.5332 0.1792  -0.0370 0.0167  123 ILE   B CG1 
1184 C  CG2 . ILE   B 114 ? 0.6839 0.6182 0.5124 0.1822  -0.0303 0.0173  123 ILE   B CG2 
1185 C  CD1 . ILE   B 114 ? 0.7342 0.6893 0.5688 0.1651  -0.0241 0.0214  123 ILE   B CD1 
1186 N  N   . GLY   B 115 ? 0.6311 0.5467 0.4200 0.2329  -0.0531 0.0080  124 GLY   B N   
1187 C  CA  . GLY   B 115 ? 0.6171 0.5429 0.3983 0.2497  -0.0500 0.0090  124 GLY   B CA  
1188 C  C   . GLY   B 115 ? 0.5828 0.5357 0.3774 0.2410  -0.0320 0.0180  124 GLY   B C   
1189 O  O   . GLY   B 115 ? 0.5584 0.5165 0.3695 0.2206  -0.0240 0.0214  124 GLY   B O   
1190 N  N   . ALA   B 116 ? 0.5776 0.5481 0.3646 0.2565  -0.0259 0.0223  125 ALA   B N   
1191 C  CA  . ALA   B 116 ? 0.5812 0.5768 0.3806 0.2484  -0.0095 0.0322  125 ALA   B CA  
1192 C  C   . ALA   B 116 ? 0.6014 0.6026 0.3909 0.2646  -0.0054 0.0357  125 ALA   B C   
1193 O  O   . ALA   B 116 ? 0.6330 0.6320 0.4035 0.2877  -0.0130 0.0321  125 ALA   B O   
1194 C  CB  . ALA   B 116 ? 0.5861 0.6090 0.3890 0.2491  -0.0029 0.0377  125 ALA   B CB  
1195 N  N   A VAL   B 117 ? 0.5829 0.5901 0.3831 0.2539  0.0061  0.0427  126 VAL   B N   
1196 N  N   C VAL   B 117 ? 0.5829 0.5901 0.3831 0.2539  0.0061  0.0427  126 VAL   B N   
1197 C  CA  A VAL   B 117 ? 0.6075 0.6191 0.3973 0.2688  0.0110  0.0475  126 VAL   B CA  
1198 C  CA  C VAL   B 117 ? 0.6075 0.6191 0.3973 0.2688  0.0110  0.0475  126 VAL   B CA  
1199 C  C   A VAL   B 117 ? 0.6086 0.6506 0.4056 0.2660  0.0276  0.0614  126 VAL   B C   
1200 C  C   C VAL   B 117 ? 0.6086 0.6506 0.4056 0.2660  0.0276  0.0614  126 VAL   B C   
1201 O  O   A VAL   B 117 ? 0.5932 0.6435 0.4086 0.2449  0.0366  0.0676  126 VAL   B O   
1202 O  O   C VAL   B 117 ? 0.5932 0.6435 0.4086 0.2449  0.0366  0.0676  126 VAL   B O   
1203 C  CB  A VAL   B 117 ? 0.6372 0.6257 0.4279 0.2642  0.0080  0.0434  126 VAL   B CB  
1204 C  CB  C VAL   B 117 ? 0.6372 0.6257 0.4279 0.2642  0.0080  0.0434  126 VAL   B CB  
1205 C  CG1 A VAL   B 117 ? 0.6631 0.6248 0.4471 0.2690  -0.0092 0.0303  126 VAL   B CG1 
1206 C  CG1 C VAL   B 117 ? 0.6631 0.6248 0.4471 0.2690  -0.0092 0.0303  126 VAL   B CG1 
1207 C  CG2 A VAL   B 117 ? 0.6438 0.6314 0.4545 0.2389  0.0169  0.0477  126 VAL   B CG2 
1208 C  CG2 C VAL   B 117 ? 0.6438 0.6314 0.4545 0.2389  0.0169  0.0477  126 VAL   B CG2 
1209 N  N   . ALA   B 118 ? 0.6102 0.6700 0.3925 0.2882  0.0311  0.0666  127 ALA   B N   
1210 C  CA  . ALA   B 118 ? 0.6297 0.7220 0.4194 0.2864  0.0471  0.0813  127 ALA   B CA  
1211 C  C   . ALA   B 118 ? 0.6523 0.7437 0.4391 0.2877  0.0568  0.0906  127 ALA   B C   
1212 O  O   . ALA   B 118 ? 0.6636 0.7655 0.4338 0.3091  0.0606  0.0959  127 ALA   B O   
1213 C  CB  . ALA   B 118 ? 0.6447 0.7634 0.4226 0.3085  0.0474  0.0833  127 ALA   B CB  
1214 N  N   . LEU   B 119 ? 0.6458 0.7218 0.4465 0.2659  0.0599  0.0920  128 LEU   B N   
1215 C  CA  . LEU   B 119 ? 0.6564 0.7251 0.4550 0.2638  0.0679  0.1000  128 LEU   B CA  
1216 C  C   . LEU   B 119 ? 0.6733 0.7481 0.4944 0.2364  0.0781  0.1094  128 LEU   B C   
1217 O  O   . LEU   B 119 ? 0.6580 0.7246 0.4937 0.2182  0.0736  0.1029  128 LEU   B O   
1218 C  CB  . LEU   B 119 ? 0.6690 0.7039 0.4579 0.2681  0.0566  0.0881  128 LEU   B CB  
1219 C  CG  . LEU   B 119 ? 0.7000 0.7244 0.4663 0.2950  0.0440  0.0778  128 LEU   B CG  
1220 C  CD1 . LEU   B 119 ? 0.7124 0.7054 0.4756 0.2946  0.0306  0.0644  128 LEU   B CD1 
1221 C  CD2 . LEU   B 119 ? 0.7171 0.7537 0.4639 0.3182  0.0508  0.0865  128 LEU   B CD2 
1222 N  N   . ASP   B 120 ? 0.6829 0.7707 0.5059 0.2339  0.0910  0.1246  129 ASP   B N   
1223 C  CA  . ASP   B 120 ? 0.6931 0.7875 0.5372 0.2085  0.1002  0.1350  129 ASP   B CA  
1224 C  C   . ASP   B 120 ? 0.6840 0.7540 0.5263 0.1997  0.1030  0.1389  129 ASP   B C   
1225 O  O   . ASP   B 120 ? 0.6879 0.7591 0.5188 0.2093  0.1106  0.1497  129 ASP   B O   
1226 C  CB  . ASP   B 120 ? 0.7403 0.8726 0.5926 0.2084  0.1134  0.1518  129 ASP   B CB  
1227 C  CG  . ASP   B 120 ? 0.8144 0.9607 0.6936 0.1814  0.1188  0.1590  129 ASP   B CG  
1228 O  OD1 . ASP   B 120 ? 0.8403 0.9642 0.7290 0.1621  0.1169  0.1572  129 ASP   B OD1 
1229 O  OD2 . ASP   B 120 ? 0.8340 1.0137 0.7245 0.1805  0.1242  0.1659  129 ASP   B OD2 
1230 N  N   . TYR   B 121 ? 0.6520 0.7001 0.5049 0.1819  0.0969  0.1304  130 TYR   B N   
1231 C  CA  . TYR   B 121 ? 0.6565 0.6800 0.5081 0.1732  0.0980  0.1323  130 TYR   B CA  
1232 C  C   . TYR   B 121 ? 0.6323 0.6536 0.5045 0.1465  0.1008  0.1363  130 TYR   B C   
1233 O  O   . TYR   B 121 ? 0.6276 0.6621 0.5145 0.1356  0.0988  0.1329  130 TYR   B O   
1234 C  CB  . TYR   B 121 ? 0.6845 0.6800 0.5258 0.1811  0.0861  0.1160  130 TYR   B CB  
1235 C  CG  . TYR   B 121 ? 0.7123 0.7023 0.5315 0.2065  0.0831  0.1137  130 TYR   B CG  
1236 C  CD1 . TYR   B 121 ? 0.7406 0.7185 0.5464 0.2147  0.0874  0.1206  130 TYR   B CD1 
1237 C  CD2 . TYR   B 121 ? 0.7294 0.7248 0.5395 0.2233  0.0750  0.1046  130 TYR   B CD2 
1238 C  CE1 . TYR   B 121 ? 0.7754 0.7485 0.5594 0.2396  0.0841  0.1181  130 TYR   B CE1 
1239 C  CE2 . TYR   B 121 ? 0.7579 0.7469 0.5468 0.2477  0.0705  0.1013  130 TYR   B CE2 
1240 C  CZ  . TYR   B 121 ? 0.7939 0.7731 0.5697 0.2563  0.0754  0.1082  130 TYR   B CZ  
1241 O  OH  . TYR   B 121 ? 0.8483 0.8217 0.6016 0.2820  0.0705  0.1048  130 TYR   B OH  
1242 N  N   . PRO   B 122 ? 0.6325 0.6348 0.5046 0.1367  0.1037  0.1421  131 PRO   B N   
1243 C  CA  . PRO   B 122 ? 0.6157 0.6120 0.5057 0.1124  0.1039  0.1442  131 PRO   B CA  
1244 C  C   . PRO   B 122 ? 0.6011 0.5883 0.4996 0.1040  0.0939  0.1279  131 PRO   B C   
1245 O  O   . PRO   B 122 ? 0.5938 0.5704 0.4830 0.1153  0.0868  0.1155  131 PRO   B O   
1246 C  CB  . PRO   B 122 ? 0.6484 0.6174 0.5294 0.1099  0.1051  0.1487  131 PRO   B CB  
1247 C  CG  . PRO   B 122 ? 0.6549 0.6277 0.5176 0.1294  0.1112  0.1576  131 PRO   B CG  
1248 C  CD  . PRO   B 122 ? 0.6296 0.6144 0.4838 0.1484  0.1065  0.1475  131 PRO   B CD  
1249 N  N   . ALA   B 123 ? 0.5814 0.5742 0.4977 0.0846  0.0933  0.1283  132 ALA   B N   
1250 C  CA  . ALA   B 123 ? 0.5812 0.5668 0.5048 0.0766  0.0847  0.1140  132 ALA   B CA  
1251 C  C   . ALA   B 123 ? 0.5596 0.5166 0.4735 0.0803  0.0778  0.1020  132 ALA   B C   
1252 O  O   . ALA   B 123 ? 0.5481 0.5018 0.4616 0.0832  0.0711  0.0895  132 ALA   B O   
1253 C  CB  . ALA   B 123 ? 0.5798 0.5699 0.5212 0.0556  0.0847  0.1173  132 ALA   B CB  
1254 N  N   . GLY   B 124 ? 0.5566 0.4946 0.4627 0.0810  0.0795  0.1063  133 GLY   B N   
1255 C  CA  . GLY   B 124 ? 0.5575 0.4704 0.4546 0.0857  0.0733  0.0957  133 GLY   B CA  
1256 C  C   . GLY   B 124 ? 0.5188 0.4298 0.4043 0.1040  0.0693  0.0871  133 GLY   B C   
1257 O  O   . GLY   B 124 ? 0.5240 0.4179 0.4038 0.1088  0.0638  0.0776  133 GLY   B O   
1258 N  N   . THR   B 125 ? 0.4808 0.4095 0.3626 0.1150  0.0713  0.0902  134 THR   B N   
1259 C  CA  . THR   B 125 ? 0.4944 0.4212 0.3655 0.1326  0.0655  0.0817  134 THR   B CA  
1260 C  C   . THR   B 125 ? 0.4955 0.4276 0.3744 0.1295  0.0584  0.0703  134 THR   B C   
1261 O  O   . THR   B 125 ? 0.5019 0.4290 0.3750 0.1401  0.0514  0.0614  134 THR   B O   
1262 C  CB  . THR   B 125 ? 0.5388 0.4794 0.3987 0.1484  0.0701  0.0904  134 THR   B CB  
1263 O  OG1 . THR   B 125 ? 0.5398 0.4783 0.3947 0.1475  0.0787  0.1041  134 THR   B OG1 
1264 C  CG2 . THR   B 125 ? 0.5728 0.5055 0.4178 0.1687  0.0630  0.0821  134 THR   B CG2 
1265 N  N   . SER   B 126 ? 0.4699 0.4104 0.3617 0.1143  0.0596  0.0706  135 SER   B N   
1266 C  CA  . SER   B 126 ? 0.4656 0.4099 0.3637 0.1105  0.0537  0.0611  135 SER   B CA  
1267 C  C   . SER   B 126 ? 0.4500 0.3786 0.3468 0.1121  0.0469  0.0498  135 SER   B C   
1268 O  O   . SER   B 126 ? 0.4614 0.3771 0.3589 0.1075  0.0472  0.0479  135 SER   B O   
1269 C  CB  . SER   B 126 ? 0.4924 0.4437 0.4033 0.0936  0.0556  0.0624  135 SER   B CB  
1270 O  OG  . SER   B 126 ? 0.5347 0.5057 0.4502 0.0918  0.0607  0.0717  135 SER   B OG  
1271 N  N   . GLY   B 127 ? 0.4250 0.3548 0.3205 0.1180  0.0405  0.0428  136 GLY   B N   
1272 C  CA  . GLY   B 127 ? 0.4479 0.3664 0.3445 0.1196  0.0340  0.0330  136 GLY   B CA  
1273 C  C   . GLY   B 127 ? 0.4614 0.3722 0.3482 0.1354  0.0289  0.0300  136 GLY   B C   
1274 O  O   . GLY   B 127 ? 0.4507 0.3542 0.3395 0.1379  0.0221  0.0218  136 GLY   B O   
1275 N  N   . SER   B 128 ? 0.4621 0.3759 0.3381 0.1469  0.0320  0.0370  137 SER   B N   
1276 C  CA  . SER   B 128 ? 0.4680 0.3737 0.3322 0.1642  0.0261  0.0334  137 SER   B CA  
1277 C  C   . SER   B 128 ? 0.4789 0.3849 0.3424 0.1705  0.0161  0.0258  137 SER   B C   
1278 O  O   . SER   B 128 ? 0.4799 0.3951 0.3448 0.1682  0.0161  0.0277  137 SER   B O   
1279 C  CB  . SER   B 128 ? 0.4866 0.3973 0.3372 0.1774  0.0316  0.0428  137 SER   B CB  
1280 O  OG  . SER   B 128 ? 0.5149 0.4203 0.3649 0.1720  0.0392  0.0497  137 SER   B OG  
1281 N  N   . PRO   B 129 ? 0.4882 0.3831 0.3500 0.1782  0.0066  0.0171  138 PRO   B N   
1282 C  CA  . PRO   B 129 ? 0.4814 0.3734 0.3435 0.1824  -0.0044 0.0101  138 PRO   B CA  
1283 C  C   . PRO   B 129 ? 0.5052 0.3971 0.3517 0.2007  -0.0099 0.0105  138 PRO   B C   
1284 O  O   . PRO   B 129 ? 0.5225 0.4131 0.3563 0.2150  -0.0083 0.0130  138 PRO   B O   
1285 C  CB  . PRO   B 129 ? 0.5115 0.3930 0.3795 0.1834  -0.0130 0.0010  138 PRO   B CB  
1286 C  CG  . PRO   B 129 ? 0.5124 0.3896 0.3739 0.1906  -0.0085 0.0026  138 PRO   B CG  
1287 C  CD  . PRO   B 129 ? 0.5030 0.3874 0.3638 0.1823  0.0047  0.0128  138 PRO   B CD  
1288 N  N   . ILE   B 130 ? 0.4986 0.3906 0.3447 0.2011  -0.0170 0.0077  139 ILE   B N   
1289 C  CA  . ILE   B 130 ? 0.5268 0.4162 0.3565 0.2203  -0.0255 0.0056  139 ILE   B CA  
1290 C  C   . ILE   B 130 ? 0.5334 0.4061 0.3650 0.2233  -0.0417 -0.0053 139 ILE   B C   
1291 O  O   . ILE   B 130 ? 0.5186 0.3876 0.3644 0.2080  -0.0450 -0.0083 139 ILE   B O   
1292 C  CB  . ILE   B 130 ? 0.5428 0.4428 0.3707 0.2181  -0.0231 0.0098  139 ILE   B CB  
1293 C  CG1 . ILE   B 130 ? 0.5871 0.5058 0.4174 0.2127  -0.0074 0.0208  139 ILE   B CG1 
1294 C  CG2 . ILE   B 130 ? 0.5499 0.4463 0.3591 0.2398  -0.0332 0.0066  139 ILE   B CG2 
1295 C  CD1 . ILE   B 130 ? 0.6069 0.5388 0.4423 0.2041  -0.0031 0.0250  139 ILE   B CD1 
1296 N  N   . LEU   B 131 ? 0.5613 0.4241 0.3796 0.2424  -0.0518 -0.0110 140 LEU   B N   
1297 C  CA  . LEU   B 131 ? 0.5941 0.4406 0.4156 0.2455  -0.0687 -0.0219 140 LEU   B CA  
1298 C  C   . LEU   B 131 ? 0.6197 0.4547 0.4246 0.2635  -0.0842 -0.0278 140 LEU   B C   
1299 O  O   . LEU   B 131 ? 0.6443 0.4841 0.4305 0.2811  -0.0820 -0.0248 140 LEU   B O   
1300 C  CB  . LEU   B 131 ? 0.6283 0.4694 0.4468 0.2557  -0.0714 -0.0264 140 LEU   B CB  
1301 C  CG  . LEU   B 131 ? 0.6617 0.5117 0.4831 0.2506  -0.0561 -0.0196 140 LEU   B CG  
1302 C  CD1 . LEU   B 131 ? 0.6917 0.5334 0.5056 0.2651  -0.0616 -0.0251 140 LEU   B CD1 
1303 C  CD2 . LEU   B 131 ? 0.6664 0.5225 0.5092 0.2267  -0.0486 -0.0177 140 LEU   B CD2 
1304 N  N   . ASP   B 132 ? 0.6205 0.4401 0.4326 0.2593  -0.1001 -0.0363 141 ASP   B N   
1305 C  CA  . ASP   B 132 ? 0.6530 0.4561 0.4491 0.2772  -0.1186 -0.0442 141 ASP   B CA  
1306 C  C   . ASP   B 132 ? 0.6862 0.4786 0.4755 0.2936  -0.1305 -0.0532 141 ASP   B C   
1307 O  O   . ASP   B 132 ? 0.6826 0.4808 0.4805 0.2896  -0.1239 -0.0528 141 ASP   B O   
1308 C  CB  . ASP   B 132 ? 0.6693 0.4583 0.4750 0.2645  -0.1318 -0.0481 141 ASP   B CB  
1309 C  CG  . ASP   B 132 ? 0.6758 0.4593 0.5059 0.2452  -0.1375 -0.0519 141 ASP   B CG  
1310 O  OD1 . ASP   B 132 ? 0.6939 0.4797 0.5311 0.2473  -0.1381 -0.0559 141 ASP   B OD1 
1311 O  OD2 . ASP   B 132 ? 0.6893 0.4666 0.5309 0.2293  -0.1422 -0.0509 141 ASP   B OD2 
1312 N  N   . LYS   B 133 ? 0.7306 0.5051 0.5040 0.3122  -0.1502 -0.0625 142 LYS   B N   
1313 C  CA  . LYS   B 133 ? 0.7626 0.5256 0.5265 0.3310  -0.1637 -0.0724 142 LYS   B CA  
1314 C  C   . LYS   B 133 ? 0.7750 0.5319 0.5619 0.3174  -0.1727 -0.0795 142 LYS   B C   
1315 O  O   . LYS   B 133 ? 0.7900 0.5420 0.5717 0.3315  -0.1803 -0.0868 142 LYS   B O   
1316 C  CB  . LYS   B 133 ? 0.8172 0.5612 0.5577 0.3547  -0.1843 -0.0814 142 LYS   B CB  
1317 C  CG  . LYS   B 133 ? 0.9041 0.6588 0.6199 0.3732  -0.1745 -0.0748 142 LYS   B CG  
1318 C  CD  . LYS   B 133 ? 1.0109 0.7475 0.6992 0.4011  -0.1947 -0.0844 142 LYS   B CD  
1319 C  CE  . LYS   B 133 ? 1.0881 0.8383 0.7580 0.4132  -0.1846 -0.0768 142 LYS   B CE  
1320 N  NZ  . LYS   B 133 ? 1.1639 0.8942 0.8113 0.4339  -0.2057 -0.0863 142 LYS   B NZ  
1321 N  N   . CYS   B 134 ? 0.7677 0.5266 0.5799 0.2909  -0.1712 -0.0772 143 CYS   B N   
1322 C  CA  . CYS   B 134 ? 0.7657 0.5258 0.6040 0.2750  -0.1760 -0.0818 143 CYS   B CA  
1323 C  C   . CYS   B 134 ? 0.7468 0.5268 0.5984 0.2630  -0.1559 -0.0751 143 CYS   B C   
1324 O  O   . CYS   B 134 ? 0.7555 0.5407 0.6292 0.2499  -0.1574 -0.0781 143 CYS   B O   
1325 C  CB  . CYS   B 134 ? 0.7966 0.5490 0.6555 0.2538  -0.1859 -0.0826 143 CYS   B CB  
1326 S  SG  . CYS   B 134 ? 0.9175 0.6405 0.7625 0.2661  -0.2137 -0.0919 143 CYS   B SG  
1327 N  N   . GLY   B 135 ? 0.7227 0.5140 0.5616 0.2671  -0.1379 -0.0659 144 GLY   B N   
1328 C  CA  . GLY   B 135 ? 0.6801 0.4870 0.5288 0.2565  -0.1198 -0.0594 144 GLY   B CA  
1329 C  C   . GLY   B 135 ? 0.6522 0.4698 0.5210 0.2311  -0.1089 -0.0528 144 GLY   B C   
1330 O  O   . GLY   B 135 ? 0.6430 0.4718 0.5220 0.2208  -0.0961 -0.0489 144 GLY   B O   
1331 N  N   . ARG   B 136 ? 0.6155 0.4283 0.4877 0.2221  -0.1141 -0.0514 145 ARG   B N   
1332 C  CA  . ARG   B 136 ? 0.5992 0.4216 0.4883 0.1991  -0.1040 -0.0448 145 ARG   B CA  
1333 C  C   . ARG   B 136 ? 0.5635 0.3964 0.4429 0.1976  -0.0876 -0.0354 145 ARG   B C   
1334 O  O   . ARG   B 136 ? 0.5584 0.3888 0.4195 0.2112  -0.0881 -0.0334 145 ARG   B O   
1335 C  CB  . ARG   B 136 ? 0.6428 0.4541 0.5389 0.1898  -0.1167 -0.0465 145 ARG   B CB  
1336 C  CG  . ARG   B 136 ? 0.7143 0.5177 0.6269 0.1853  -0.1326 -0.0547 145 ARG   B CG  
1337 C  CD  . ARG   B 136 ? 0.8045 0.5944 0.7233 0.1747  -0.1453 -0.0546 145 ARG   B CD  
1338 N  NE  . ARG   B 136 ? 0.9095 0.6801 0.8056 0.1922  -0.1591 -0.0585 145 ARG   B NE  
1339 C  CZ  . ARG   B 136 ? 0.9895 0.7440 0.8814 0.1882  -0.1700 -0.0579 145 ARG   B CZ  
1340 N  NH1 . ARG   B 136 ? 0.9859 0.7418 0.8948 0.1660  -0.1672 -0.0517 145 ARG   B NH1 
1341 N  NH2 . ARG   B 136 ? 1.0185 0.7550 0.8873 0.2074  -0.1836 -0.0629 145 ARG   B NH2 
1342 N  N   . VAL   B 137 ? 0.5105 0.3562 0.4033 0.1806  -0.0737 -0.0298 146 VAL   B N   
1343 C  CA  . VAL   B 137 ? 0.4884 0.3442 0.3745 0.1777  -0.0594 -0.0214 146 VAL   B CA  
1344 C  C   . VAL   B 137 ? 0.4933 0.3480 0.3780 0.1708  -0.0609 -0.0181 146 VAL   B C   
1345 O  O   . VAL   B 137 ? 0.4898 0.3440 0.3876 0.1560  -0.0623 -0.0179 146 VAL   B O   
1346 C  CB  . VAL   B 137 ? 0.4870 0.3543 0.3855 0.1643  -0.0459 -0.0180 146 VAL   B CB  
1347 C  CG1 . VAL   B 137 ? 0.4895 0.3666 0.3837 0.1587  -0.0327 -0.0096 146 VAL   B CG1 
1348 C  CG2 . VAL   B 137 ? 0.5020 0.3683 0.3987 0.1733  -0.0448 -0.0212 146 VAL   B CG2 
1349 N  N   . ILE   B 138 ? 0.5092 0.3635 0.3775 0.1829  -0.0614 -0.0156 147 ILE   B N   
1350 C  CA  . ILE   B 138 ? 0.5031 0.3557 0.3667 0.1795  -0.0637 -0.0130 147 ILE   B CA  
1351 C  C   . ILE   B 138 ? 0.4872 0.3555 0.3533 0.1700  -0.0490 -0.0052 147 ILE   B C   
1352 O  O   . ILE   B 138 ? 0.4965 0.3650 0.3584 0.1674  -0.0501 -0.0029 147 ILE   B O   
1353 C  CB  . ILE   B 138 ? 0.5356 0.3784 0.3789 0.2001  -0.0753 -0.0162 147 ILE   B CB  
1354 C  CG1 . ILE   B 138 ? 0.5594 0.4124 0.3892 0.2172  -0.0681 -0.0137 147 ILE   B CG1 
1355 C  CG2 . ILE   B 138 ? 0.5438 0.3675 0.3869 0.2059  -0.0930 -0.0250 147 ILE   B CG2 
1356 C  CD1 . ILE   B 138 ? 0.6038 0.4532 0.4103 0.2407  -0.0766 -0.0155 147 ILE   B CD1 
1357 N  N   . GLY   B 139 ? 0.4800 0.3599 0.3514 0.1658  -0.0366 -0.0015 148 GLY   B N   
1358 C  CA  . GLY   B 139 ? 0.4605 0.3545 0.3365 0.1552  -0.0236 0.0052  148 GLY   B CA  
1359 C  C   . GLY   B 139 ? 0.4664 0.3688 0.3428 0.1567  -0.0131 0.0092  148 GLY   B C   
1360 O  O   . GLY   B 139 ? 0.4758 0.3734 0.3467 0.1673  -0.0151 0.0073  148 GLY   B O   
1361 N  N   . LEU   B 140 ? 0.4569 0.3709 0.3385 0.1465  -0.0027 0.0149  149 LEU   B N   
1362 C  CA  . LEU   B 140 ? 0.4502 0.3709 0.3330 0.1449  0.0073  0.0201  149 LEU   B CA  
1363 C  C   . LEU   B 140 ? 0.4675 0.4027 0.3452 0.1487  0.0141  0.0280  149 LEU   B C   
1364 O  O   . LEU   B 140 ? 0.4609 0.4041 0.3383 0.1472  0.0134  0.0293  149 LEU   B O   
1365 C  CB  . LEU   B 140 ? 0.4375 0.3590 0.3326 0.1286  0.0132  0.0200  149 LEU   B CB  
1366 C  CG  . LEU   B 140 ? 0.4324 0.3451 0.3352 0.1233  0.0087  0.0131  149 LEU   B CG  
1367 C  CD1 . LEU   B 140 ? 0.4221 0.3378 0.3339 0.1102  0.0158  0.0136  149 LEU   B CD1 
1368 C  CD2 . LEU   B 140 ? 0.4387 0.3425 0.3376 0.1345  0.0036  0.0089  149 LEU   B CD2 
1369 N  N   . TYR   B 141 ? 0.4643 0.4034 0.3372 0.1551  0.0201  0.0337  150 TYR   B N   
1370 C  CA  . TYR   B 141 ? 0.4760 0.4314 0.3454 0.1593  0.0276  0.0427  150 TYR   B CA  
1371 C  C   . TYR   B 141 ? 0.4742 0.4381 0.3557 0.1429  0.0366  0.0488  150 TYR   B C   
1372 O  O   . TYR   B 141 ? 0.4994 0.4533 0.3853 0.1351  0.0389  0.0483  150 TYR   B O   
1373 C  CB  . TYR   B 141 ? 0.5047 0.4579 0.3618 0.1749  0.0297  0.0465  150 TYR   B CB  
1374 C  CG  . TYR   B 141 ? 0.5443 0.5153 0.3991 0.1780  0.0403  0.0587  150 TYR   B CG  
1375 C  CD1 . TYR   B 141 ? 0.5658 0.5376 0.4265 0.1680  0.0494  0.0668  150 TYR   B CD1 
1376 C  CD2 . TYR   B 141 ? 0.5736 0.5610 0.4202 0.1914  0.0409  0.0624  150 TYR   B CD2 
1377 C  CE1 . TYR   B 141 ? 0.5951 0.5844 0.4559 0.1687  0.0595  0.0796  150 TYR   B CE1 
1378 C  CE2 . TYR   B 141 ? 0.5861 0.5941 0.4326 0.1938  0.0517  0.0748  150 TYR   B CE2 
1379 C  CZ  . TYR   B 141 ? 0.6126 0.6222 0.4678 0.1809  0.0613  0.0840  150 TYR   B CZ  
1380 O  OH  . TYR   B 141 ? 0.6475 0.6780 0.5045 0.1814  0.0723  0.0978  150 TYR   B OH  
1381 N  N   . GLY   B 142 ? 0.4713 0.4529 0.3573 0.1388  0.0412  0.0547  151 GLY   B N   
1382 C  CA  . GLY   B 142 ? 0.4933 0.4829 0.3916 0.1232  0.0487  0.0609  151 GLY   B CA  
1383 C  C   . GLY   B 142 ? 0.5003 0.5026 0.4087 0.1122  0.0488  0.0607  151 GLY   B C   
1384 O  O   . GLY   B 142 ? 0.5284 0.5363 0.4477 0.0988  0.0535  0.0650  151 GLY   B O   
1385 N  N   . ASN   B 143 ? 0.4622 0.4675 0.3665 0.1178  0.0428  0.0554  152 ASN   B N   
1386 C  CA  . ASN   B 143 ? 0.4546 0.4731 0.3665 0.1098  0.0425  0.0553  152 ASN   B CA  
1387 C  C   . ASN   B 143 ? 0.4787 0.5127 0.3827 0.1244  0.0407  0.0571  152 ASN   B C   
1388 O  O   . ASN   B 143 ? 0.4811 0.5055 0.3731 0.1366  0.0335  0.0517  152 ASN   B O   
1389 C  CB  . ASN   B 143 ? 0.4523 0.4583 0.3655 0.1019  0.0366  0.0469  152 ASN   B CB  
1390 C  CG  . ASN   B 143 ? 0.4602 0.4793 0.3816 0.0924  0.0371  0.0472  152 ASN   B CG  
1391 O  OD1 . ASN   B 143 ? 0.4777 0.5125 0.4083 0.0865  0.0422  0.0531  152 ASN   B OD1 
1392 N  ND2 . ASN   B 143 ? 0.4626 0.4761 0.3805 0.0912  0.0316  0.0415  152 ASN   B ND2 
1393 N  N   . GLY   B 144 ? 0.4927 0.5505 0.4036 0.1235  0.0467  0.0646  153 GLY   B N   
1394 C  CA  . GLY   B 144 ? 0.5034 0.5802 0.4067 0.1395  0.0462  0.0672  153 GLY   B CA  
1395 C  C   . GLY   B 144 ? 0.5133 0.6204 0.4291 0.1348  0.0521  0.0743  153 GLY   B C   
1396 O  O   . GLY   B 144 ? 0.4970 0.6086 0.4260 0.1194  0.0523  0.0735  153 GLY   B O   
1397 N  N   . VAL   B 145 ? 0.5321 0.6624 0.4437 0.1493  0.0567  0.0813  154 VAL   B N   
1398 C  CA  . VAL   B 145 ? 0.5588 0.7225 0.4832 0.1467  0.0618  0.0879  154 VAL   B CA  
1399 C  C   . VAL   B 145 ? 0.5961 0.7852 0.5225 0.1547  0.0723  0.1007  154 VAL   B C   
1400 O  O   . VAL   B 145 ? 0.5976 0.7766 0.5106 0.1665  0.0743  0.1030  154 VAL   B O   
1401 C  CB  . VAL   B 145 ? 0.5953 0.7660 0.5101 0.1599  0.0534  0.0802  154 VAL   B CB  
1402 C  CG1 . VAL   B 145 ? 0.6087 0.7849 0.5040 0.1859  0.0513  0.0799  154 VAL   B CG1 
1403 C  CG2 . VAL   B 145 ? 0.6007 0.8004 0.5316 0.1521  0.0551  0.0825  154 VAL   B CG2 
1404 N  N   . VAL   B 146 ? 0.6203 0.8432 0.5639 0.1481  0.0790  0.1093  155 VAL   B N   
1405 C  CA  . VAL   B 146 ? 0.6535 0.9062 0.6010 0.1551  0.0903  0.1234  155 VAL   B CA  
1406 C  C   . VAL   B 146 ? 0.6907 0.9761 0.6349 0.1728  0.0898  0.1232  155 VAL   B C   
1407 O  O   . VAL   B 146 ? 0.6827 0.9852 0.6399 0.1657  0.0868  0.1204  155 VAL   B O   
1408 C  CB  . VAL   B 146 ? 0.6560 0.9228 0.6281 0.1320  0.0995  0.1359  155 VAL   B CB  
1409 C  CG1 . VAL   B 146 ? 0.6561 0.9605 0.6346 0.1390  0.1121  0.1522  155 VAL   B CG1 
1410 C  CG2 . VAL   B 146 ? 0.6747 0.9065 0.6452 0.1188  0.0996  0.1360  155 VAL   B CG2 
1411 N  N   . ILE   B 147 ? 0.7316 1.0241 0.6561 0.1980  0.0911  0.1247  156 ILE   B N   
1412 C  CA  . ILE   B 147 ? 0.7613 1.0824 0.6778 0.2196  0.0890  0.1226  156 ILE   B CA  
1413 C  C   . ILE   B 147 ? 0.7738 1.1458 0.7060 0.2219  0.1025  0.1381  156 ILE   B C   
1414 O  O   . ILE   B 147 ? 0.7700 1.1516 0.7171 0.2074  0.1137  0.1514  156 ILE   B O   
1415 C  CB  . ILE   B 147 ? 0.7914 1.0915 0.6764 0.2475  0.0808  0.1140  156 ILE   B CB  
1416 C  CG1 . ILE   B 147 ? 0.8031 1.1061 0.6774 0.2595  0.0898  0.1237  156 ILE   B CG1 
1417 C  CG2 . ILE   B 147 ? 0.8192 1.0722 0.6929 0.2424  0.0676  0.1000  156 ILE   B CG2 
1418 C  CD1 . ILE   B 147 ? 0.8328 1.1227 0.6757 0.2910  0.0814  0.1156  156 ILE   B CD1 
1419 N  N   . LYS   B 148 ? 0.7820 1.1867 0.7112 0.2400  0.1011  0.1365  157 LYS   B N   
1420 C  CA  . LYS   B 148 ? 0.7875 1.2468 0.7327 0.2446  0.1133  0.1502  157 LYS   B CA  
1421 C  C   . LYS   B 148 ? 0.8043 1.2808 0.7567 0.2405  0.1293  0.1687  157 LYS   B C   
1422 O  O   . LYS   B 148 ? 0.8039 1.3051 0.7846 0.2186  0.1390  0.1817  157 LYS   B O   
1423 C  CB  . LYS   B 148 ? 0.8120 1.2955 0.7382 0.2771  0.1092  0.1448  157 LYS   B CB  
1424 C  CG  . LYS   B 148 ? 0.8633 1.3545 0.7933 0.2787  0.0983  0.1331  157 LYS   B CG  
1425 C  CD  . LYS   B 148 ? 0.9395 1.4395 0.8422 0.3141  0.0905  0.1244  157 LYS   B CD  
1426 C  CE  . LYS   B 148 ? 0.9846 1.5360 0.8876 0.3350  0.1027  0.1364  157 LYS   B CE  
1427 N  NZ  . LYS   B 148 ? 0.9918 1.5975 0.9237 0.3276  0.1096  0.1436  157 LYS   B NZ  
1428 N  N   . ASN   B 149 ? 0.8160 1.2770 0.7429 0.2604  0.1313  0.1701  158 ASN   B N   
1429 C  CA  . ASN   B 149 ? 0.8113 1.2865 0.7400 0.2601  0.1466  0.1880  158 ASN   B CA  
1430 C  C   . ASN   B 149 ? 0.7946 1.2392 0.7347 0.2328  0.1502  0.1942  158 ASN   B C   
1431 O  O   . ASN   B 149 ? 0.8032 1.2451 0.7363 0.2354  0.1600  0.2064  158 ASN   B O   
1432 C  CB  . ASN   B 149 ? 0.8546 1.3236 0.7493 0.2940  0.1464  0.1863  158 ASN   B CB  
1433 C  CG  . ASN   B 149 ? 0.9412 1.3607 0.8087 0.3070  0.1292  0.1666  158 ASN   B CG  
1434 O  OD1 . ASN   B 149 ? 0.9762 1.3872 0.8372 0.3142  0.1162  0.1521  158 ASN   B OD1 
1435 N  ND2 . ASN   B 149 ? 0.9662 1.3523 0.8176 0.3100  0.1284  0.1661  158 ASN   B ND2 
1436 N  N   . GLY   B 150 ? 0.7690 1.1907 0.7242 0.2087  0.1421  0.1859  159 GLY   B N   
1437 C  CA  . GLY   B 150 ? 0.7532 1.1428 0.7183 0.1832  0.1428  0.1887  159 GLY   B CA  
1438 C  C   . GLY   B 150 ? 0.7398 1.0807 0.6813 0.1893  0.1359  0.1794  159 GLY   B C   
1439 O  O   . GLY   B 150 ? 0.7582 1.0733 0.7056 0.1710  0.1371  0.1825  159 GLY   B O   
1440 N  N   A SER   B 151 ? 0.7270 1.0540 0.6421 0.2149  0.1275  0.1676  160 SER   B N   
1441 N  N   C SER   B 151 ? 0.7270 1.0540 0.6421 0.2149  0.1275  0.1676  160 SER   B N   
1442 C  CA  A SER   B 151 ? 0.7268 1.0101 0.6207 0.2218  0.1200  0.1584  160 SER   B CA  
1443 C  CA  C SER   B 151 ? 0.7268 1.0101 0.6207 0.2218  0.1200  0.1584  160 SER   B CA  
1444 C  C   A SER   B 151 ? 0.6985 0.9456 0.5947 0.2079  0.1069  0.1426  160 SER   B C   
1445 C  C   C SER   B 151 ? 0.6985 0.9456 0.5947 0.2079  0.1069  0.1426  160 SER   B C   
1446 O  O   A SER   B 151 ? 0.6992 0.9520 0.6022 0.2042  0.1000  0.1344  160 SER   B O   
1447 O  O   C SER   B 151 ? 0.6992 0.9520 0.6022 0.2042  0.1000  0.1344  160 SER   B O   
1448 C  CB  A SER   B 151 ? 0.7644 1.0461 0.6293 0.2547  0.1153  0.1525  160 SER   B CB  
1449 C  CB  C SER   B 151 ? 0.7644 1.0461 0.6293 0.2547  0.1153  0.1525  160 SER   B CB  
1450 O  OG  A SER   B 151 ? 0.8289 1.0753 0.6760 0.2611  0.1114  0.1482  160 SER   B OG  
1451 O  OG  C SER   B 151 ? 0.8289 1.0753 0.6760 0.2611  0.1114  0.1482  160 SER   B OG  
1452 N  N   . TYR   B 152 ? 0.6795 0.8907 0.5683 0.2024  0.1035  0.1384  161 TYR   B N   
1453 C  CA  . TYR   B 152 ? 0.6417 0.8187 0.5319 0.1900  0.0921  0.1242  161 TYR   B CA  
1454 C  C   . TYR   B 152 ? 0.6108 0.7644 0.4795 0.2086  0.0794  0.1098  161 TYR   B C   
1455 O  O   . TYR   B 152 ? 0.6165 0.7591 0.4673 0.2258  0.0781  0.1092  161 TYR   B O   
1456 C  CB  . TYR   B 152 ? 0.6289 0.7804 0.5243 0.1733  0.0946  0.1267  161 TYR   B CB  
1457 C  CG  . TYR   B 152 ? 0.6351 0.7572 0.5344 0.1598  0.0847  0.1136  161 TYR   B CG  
1458 C  CD1 . TYR   B 152 ? 0.6344 0.7614 0.5505 0.1421  0.0825  0.1105  161 TYR   B CD1 
1459 C  CD2 . TYR   B 152 ? 0.6482 0.7395 0.5345 0.1656  0.0777  0.1046  161 TYR   B CD2 
1460 C  CE1 . TYR   B 152 ? 0.6458 0.7481 0.5641 0.1312  0.0745  0.0993  161 TYR   B CE1 
1461 C  CE2 . TYR   B 152 ? 0.6634 0.7317 0.5541 0.1537  0.0698  0.0937  161 TYR   B CE2 
1462 C  CZ  . TYR   B 152 ? 0.6595 0.7336 0.5655 0.1369  0.0687  0.0914  161 TYR   B CZ  
1463 O  OH  . TYR   B 152 ? 0.6628 0.7162 0.5719 0.1264  0.0619  0.0814  161 TYR   B OH  
1464 N  N   . VAL   B 153 ? 0.5727 0.7159 0.4434 0.2041  0.0691  0.0983  162 VAL   B N   
1465 C  CA  . VAL   B 153 ? 0.5471 0.6655 0.3999 0.2180  0.0561  0.0854  162 VAL   B CA  
1466 C  C   . VAL   B 153 ? 0.5037 0.5960 0.3651 0.1992  0.0493  0.0766  162 VAL   B C   
1467 O  O   . VAL   B 153 ? 0.5062 0.6049 0.3803 0.1850  0.0491  0.0754  162 VAL   B O   
1468 C  CB  . VAL   B 153 ? 0.5658 0.6970 0.4077 0.2358  0.0492  0.0803  162 VAL   B CB  
1469 C  CG1 . VAL   B 153 ? 0.5823 0.6830 0.4060 0.2482  0.0339  0.0671  162 VAL   B CG1 
1470 C  CG2 . VAL   B 153 ? 0.5788 0.7411 0.4125 0.2560  0.0569  0.0894  162 VAL   B CG2 
1471 N  N   . SER   B 154 ? 0.5062 0.5708 0.3600 0.2005  0.0439  0.0706  163 SER   B N   
1472 C  CA  . SER   B 154 ? 0.4876 0.5297 0.3494 0.1838  0.0384  0.0629  163 SER   B CA  
1473 C  C   . SER   B 154 ? 0.4887 0.5141 0.3414 0.1902  0.0254  0.0521  163 SER   B C   
1474 O  O   . SER   B 154 ? 0.5038 0.5204 0.3410 0.2080  0.0181  0.0479  163 SER   B O   
1475 C  CB  . SER   B 154 ? 0.5062 0.5289 0.3668 0.1810  0.0393  0.0622  163 SER   B CB  
1476 O  OG  . SER   B 154 ? 0.5141 0.5183 0.3827 0.1664  0.0346  0.0550  163 SER   B OG  
1477 N  N   . ALA   B 155 ? 0.4733 0.4910 0.3340 0.1762  0.0217  0.0473  164 ALA   B N   
1478 C  CA  . ALA   B 155 ? 0.4659 0.4631 0.3187 0.1794  0.0096  0.0383  164 ALA   B CA  
1479 C  C   . ALA   B 155 ? 0.4902 0.4654 0.3409 0.1798  0.0051  0.0337  164 ALA   B C   
1480 O  O   . ALA   B 155 ? 0.4957 0.4704 0.3538 0.1724  0.0120  0.0367  164 ALA   B O   
1481 C  CB  . ALA   B 155 ? 0.4654 0.4590 0.3280 0.1625  0.0086  0.0359  164 ALA   B CB  
1482 N  N   . ILE   B 156 ? 0.4895 0.4462 0.3303 0.1883  -0.0072 0.0264  165 ILE   B N   
1483 C  CA  . ILE   B 156 ? 0.5034 0.4402 0.3465 0.1850  -0.0131 0.0210  165 ILE   B CA  
1484 C  C   . ILE   B 156 ? 0.4837 0.4138 0.3390 0.1659  -0.0137 0.0190  165 ILE   B C   
1485 O  O   . ILE   B 156 ? 0.5064 0.4277 0.3576 0.1656  -0.0218 0.0160  165 ILE   B O   
1486 C  CB  . ILE   B 156 ? 0.5449 0.4648 0.3735 0.2016  -0.0276 0.0140  165 ILE   B CB  
1487 C  CG1 . ILE   B 156 ? 0.5761 0.5054 0.3898 0.2233  -0.0264 0.0162  165 ILE   B CG1 
1488 C  CG2 . ILE   B 156 ? 0.5549 0.4564 0.3895 0.1965  -0.0343 0.0082  165 ILE   B CG2 
1489 C  CD1 . ILE   B 156 ? 0.6158 0.5271 0.4124 0.2431  -0.0418 0.0083  165 ILE   B CD1 
1490 N  N   . THR   B 157 ? 0.4652 0.3999 0.3339 0.1508  -0.0047 0.0214  166 THR   B N   
1491 C  CA  . THR   B 157 ? 0.4542 0.3861 0.3326 0.1346  -0.0038 0.0203  166 THR   B CA  
1492 C  C   . THR   B 157 ? 0.4531 0.3701 0.3373 0.1289  -0.0092 0.0153  166 THR   B C   
1493 O  O   . THR   B 157 ? 0.4544 0.3695 0.3440 0.1276  -0.0064 0.0141  166 THR   B O   
1494 C  CB  . THR   B 157 ? 0.4568 0.4012 0.3454 0.1225  0.0073  0.0244  166 THR   B CB  
1495 O  OG1 . THR   B 157 ? 0.4540 0.4152 0.3408 0.1257  0.0122  0.0296  166 THR   B OG1 
1496 C  CG2 . THR   B 157 ? 0.4419 0.3835 0.3391 0.1076  0.0085  0.0226  166 THR   B CG2 
1497 N  N   . GLN   B 158 ? 0.4505 0.3575 0.3342 0.1249  -0.0167 0.0130  167 GLN   B N   
1498 C  CA  . GLN   B 158 ? 0.4450 0.3409 0.3370 0.1181  -0.0218 0.0094  167 GLN   B CA  
1499 C  C   . GLN   B 158 ? 0.4517 0.3489 0.3517 0.1025  -0.0184 0.0114  167 GLN   B C   
1500 O  O   . GLN   B 158 ? 0.4542 0.3528 0.3485 0.1007  -0.0183 0.0139  167 GLN   B O   
1501 C  CB  . GLN   B 158 ? 0.4861 0.3658 0.3702 0.1279  -0.0360 0.0054  167 GLN   B CB  
1502 C  CG  . GLN   B 158 ? 0.4946 0.3637 0.3897 0.1200  -0.0429 0.0021  167 GLN   B CG  
1503 C  CD  . GLN   B 158 ? 0.4882 0.3618 0.3929 0.1201  -0.0396 -0.0009 167 GLN   B CD  
1504 O  OE1 . GLN   B 158 ? 0.4554 0.3403 0.3681 0.1122  -0.0286 0.0011  167 GLN   B OE1 
1505 N  NE2 . GLN   B 158 ? 0.4896 0.3536 0.3919 0.1305  -0.0497 -0.0062 167 GLN   B NE2 
1506 N  N   . GLY   B 159 ? 0.4619 0.3596 0.3740 0.0932  -0.0158 0.0101  168 GLY   B N   
1507 C  CA  . GLY   B 159 ? 0.4876 0.3883 0.4072 0.0797  -0.0117 0.0123  168 GLY   B CA  
1508 C  C   . GLY   B 159 ? 0.5763 0.4660 0.4991 0.0750  -0.0203 0.0126  168 GLY   B C   
1509 O  O   . GLY   B 159 ? 0.6191 0.4968 0.5384 0.0820  -0.0310 0.0101  168 GLY   B O   
1510 N  N   . LYS   B 160 ? 0.5942 0.4868 0.5226 0.0632  -0.0163 0.0161  169 LYS   B N   
1511 C  CA  . LYS   B 160 ? 0.6126 0.4955 0.5460 0.0558  -0.0234 0.0186  169 LYS   B CA  
1512 C  C   . LYS   B 160 ? 0.6115 0.5030 0.5627 0.0476  -0.0204 0.0179  169 LYS   B C   
1513 O  O   . LYS   B 160 ? 0.5985 0.5042 0.5557 0.0437  -0.0100 0.0179  169 LYS   B O   
1514 C  CB  . LYS   B 160 ? 0.6514 0.5331 0.5783 0.0484  -0.0200 0.0247  169 LYS   B CB  
1515 C  CG  . LYS   B 160 ? 0.7498 0.6251 0.6843 0.0367  -0.0233 0.0301  169 LYS   B CG  
1516 C  CD  . LYS   B 160 ? 0.8574 0.7256 0.7799 0.0326  -0.0227 0.0365  169 LYS   B CD  
1517 C  CE  . LYS   B 160 ? 0.9407 0.7949 0.8675 0.0231  -0.0303 0.0426  169 LYS   B CE  
1518 N  NZ  . LYS   B 160 ? 1.0033 0.8479 0.9165 0.0193  -0.0300 0.0498  169 LYS   B NZ  
1519 N  N   . ARG   B 161 ? 0.6291 0.5121 0.5889 0.0456  -0.0303 0.0168  170 ARG   B N   
1520 C  CA  . ARG   B 161 ? 0.6585 0.5525 0.6377 0.0371  -0.0281 0.0165  170 ARG   B CA  
1521 C  C   . ARG   B 161 ? 0.6944 0.5892 0.6803 0.0228  -0.0264 0.0248  170 ARG   B C   
1522 O  O   . ARG   B 161 ? 0.7094 0.5879 0.6931 0.0194  -0.0368 0.0278  170 ARG   B O   
1523 C  CB  . ARG   B 161 ? 0.6772 0.5640 0.6645 0.0422  -0.0401 0.0105  170 ARG   B CB  
1524 C  CG  . ARG   B 161 ? 0.6895 0.5919 0.6980 0.0355  -0.0374 0.0089  170 ARG   B CG  
1525 C  CD  . ARG   B 161 ? 0.7243 0.6189 0.7425 0.0390  -0.0515 0.0030  170 ARG   B CD  
1526 N  NE  . ARG   B 161 ? 0.7197 0.6318 0.7613 0.0309  -0.0496 0.0022  170 ARG   B NE  
1527 C  CZ  . ARG   B 161 ? 0.7086 0.6299 0.7580 0.0384  -0.0504 -0.0053 170 ARG   B CZ  
1528 N  NH1 . ARG   B 161 ? 0.6547 0.5675 0.6894 0.0537  -0.0528 -0.0117 170 ARG   B NH1 
1529 N  NH2 . ARG   B 161 ? 0.7119 0.6514 0.7837 0.0310  -0.0491 -0.0060 170 ARG   B NH2 
1530 N  N   . GLU   B 162 ? 0.7062 0.6181 0.6972 0.0156  -0.0135 0.0288  171 GLU   B N   
1531 C  CA  . GLU   B 162 ? 0.7417 0.6573 0.7375 0.0028  -0.0093 0.0381  171 GLU   B CA  
1532 C  C   . GLU   B 162 ? 0.7584 0.6765 0.7745 -0.0078 -0.0150 0.0414  171 GLU   B C   
1533 O  O   . GLU   B 162 ? 0.7756 0.6913 0.7955 -0.0193 -0.0147 0.0508  171 GLU   B O   
1534 C  CB  . GLU   B 162 ? 0.7838 0.7194 0.7799 0.0000  0.0058  0.0405  171 GLU   B CB  
1535 C  CG  . GLU   B 162 ? 0.8842 0.8198 0.8637 0.0092  0.0112  0.0364  171 GLU   B CG  
1536 C  CD  . GLU   B 162 ? 1.0228 0.9485 0.9849 0.0094  0.0114  0.0410  171 GLU   B CD  
1537 O  OE1 . GLU   B 162 ? 1.0601 0.9945 1.0146 0.0105  0.0200  0.0412  171 GLU   B OE1 
1538 O  OE2 . GLU   B 162 ? 1.0693 0.9776 1.0241 0.0097  0.0021  0.0435  171 GLU   B OE2 
1539 S  S   . DMS   C .   ? 0.8937 0.9174 0.8491 0.0494  0.0446  0.0506  101 DMS   A S   
1540 O  O   . DMS   C .   ? 0.8922 0.9127 0.8430 0.0498  0.0394  0.0429  101 DMS   A O   
1541 C  C1  . DMS   C .   ? 0.8872 0.9077 0.8554 0.0325  0.0453  0.0521  101 DMS   A C1  
1542 C  C2  . DMS   C .   ? 0.8873 0.9409 0.8499 0.0529  0.0480  0.0594  101 DMS   A C2  
1543 S  S   . DMS   D .   ? 0.9735 0.8476 0.8840 0.0355  0.0155  -0.0295 201 DMS   B S   
1544 O  O   . DMS   D .   ? 0.9627 0.8543 0.8756 0.0399  0.0225  -0.0272 201 DMS   B O   
1545 C  C1  . DMS   D .   ? 0.9854 0.8389 0.8887 0.0423  0.0128  -0.0336 201 DMS   B C1  
1546 C  C2  . DMS   D .   ? 0.9652 0.8366 0.8857 0.0260  0.0161  -0.0184 201 DMS   B C2  
1547 C  C4  . A1BG6 E .   ? 0.9615 0.9926 0.8727 0.1134  0.0776  0.1007  202 A1BG6 B C4  
1548 C  C5  . A1BG6 E .   ? 0.9532 0.9838 0.8776 0.0975  0.0743  0.0955  202 A1BG6 B C5  
1549 BR BR  . A1BG6 E .   ? 0.9901 0.9930 0.8829 0.1292  0.0699  0.0896  202 A1BG6 B BR  
1550 C  C3  . A1BG6 E .   ? 0.9474 1.0003 0.8593 0.1181  0.0863  0.1139  202 A1BG6 B C3  
1551 C  C2  . A1BG6 E .   ? 0.9324 1.0080 0.8613 0.1048  0.0913  0.1219  202 A1BG6 B C2  
1552 C  C1  . A1BG6 E .   ? 0.9296 1.0032 0.8722 0.0886  0.0865  0.1155  202 A1BG6 B C1  
1553 N  N   . A1BG6 E .   ? 0.9409 0.9917 0.8798 0.0859  0.0783  0.1025  202 A1BG6 B N   
1554 C  C   . A1BG6 E .   ? 0.9361 0.9855 0.8875 0.0705  0.0735  0.0959  202 A1BG6 B C   
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