data_7I9M
# 
_entry.id   7I9M 
# 
_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   7I9M         pdb_00007i9m 10.2210/pdb7i9m/pdb 
WWPDB D_1001408489 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.entry_id                        7I9M 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_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 
_audit_author.identifier_ORCID 
'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                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_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    1  ? ?    ? ? 
4 non-polymer syn 'benzyl [3-({4-[(1R)-1-aminoethyl]phenyl}carbamoyl)-5-chlorophenyl]carbamate' 423.892   1  ? ?    ? ? 
5 water       nat water                                                                         18.015    76 ? ?    ? ? 
# 
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 'benzyl [3-({4-[(1R)-1-aminoethyl]phenyl}carbamoyl)-5-chlorophenyl]carbamate' A1B86 
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 
A1B86 non-polymer         . 'benzyl [3-({4-[(1R)-1-aminoethyl]phenyl}carbamoyl)-5-chlorophenyl]carbamate' ? 'C23 H22 Cl N3 O3' 
423.892 
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 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1B86 1  202 301 A1B86 LIG B . 
E 5 HOH   1  101 98  HOH   HOH A . 
E 5 HOH   2  102 48  HOH   HOH A . 
E 5 HOH   3  103 34  HOH   HOH A . 
E 5 HOH   4  104 16  HOH   HOH A . 
E 5 HOH   5  105 117 HOH   HOH A . 
E 5 HOH   6  106 118 HOH   HOH A . 
E 5 HOH   7  107 49  HOH   HOH A . 
E 5 HOH   8  108 65  HOH   HOH A . 
E 5 HOH   9  109 36  HOH   HOH A . 
E 5 HOH   10 110 120 HOH   HOH A . 
E 5 HOH   11 111 105 HOH   HOH A . 
E 5 HOH   12 112 50  HOH   HOH A . 
E 5 HOH   13 113 29  HOH   HOH A . 
E 5 HOH   14 114 110 HOH   HOH A . 
E 5 HOH   15 115 40  HOH   HOH A . 
E 5 HOH   16 116 119 HOH   HOH A . 
E 5 HOH   17 117 27  HOH   HOH A . 
F 5 HOH   1  301 11  HOH   HOH B . 
F 5 HOH   2  302 57  HOH   HOH B . 
F 5 HOH   3  303 14  HOH   HOH B . 
F 5 HOH   4  304 92  HOH   HOH B . 
F 5 HOH   5  305 51  HOH   HOH B . 
F 5 HOH   6  306 90  HOH   HOH B . 
F 5 HOH   7  307 46  HOH   HOH B . 
F 5 HOH   8  308 24  HOH   HOH B . 
F 5 HOH   9  309 9   HOH   HOH B . 
F 5 HOH   10 310 58  HOH   HOH B . 
F 5 HOH   11 311 126 HOH   HOH B . 
F 5 HOH   12 312 1   HOH   HOH B . 
F 5 HOH   13 313 79  HOH   HOH B . 
F 5 HOH   14 314 69  HOH   HOH B . 
F 5 HOH   15 315 2   HOH   HOH B . 
F 5 HOH   16 316 4   HOH   HOH B . 
F 5 HOH   17 317 5   HOH   HOH B . 
F 5 HOH   18 318 32  HOH   HOH B . 
F 5 HOH   19 319 63  HOH   HOH B . 
F 5 HOH   20 320 20  HOH   HOH B . 
F 5 HOH   21 321 42  HOH   HOH B . 
F 5 HOH   22 322 127 HOH   HOH B . 
F 5 HOH   23 323 56  HOH   HOH B . 
F 5 HOH   24 324 12  HOH   HOH B . 
F 5 HOH   25 325 10  HOH   HOH B . 
F 5 HOH   26 326 60  HOH   HOH B . 
F 5 HOH   27 327 80  HOH   HOH B . 
F 5 HOH   28 328 28  HOH   HOH B . 
F 5 HOH   29 329 67  HOH   HOH B . 
F 5 HOH   30 330 3   HOH   HOH B . 
F 5 HOH   31 331 30  HOH   HOH B . 
F 5 HOH   32 332 115 HOH   HOH B . 
F 5 HOH   33 333 23  HOH   HOH B . 
F 5 HOH   34 334 39  HOH   HOH B . 
F 5 HOH   35 335 43  HOH   HOH B . 
F 5 HOH   36 336 13  HOH   HOH B . 
F 5 HOH   37 337 102 HOH   HOH B . 
F 5 HOH   38 338 35  HOH   HOH B . 
F 5 HOH   39 339 116 HOH   HOH B . 
F 5 HOH   40 340 21  HOH   HOH B . 
F 5 HOH   41 341 107 HOH   HOH B . 
F 5 HOH   42 342 18  HOH   HOH B . 
F 5 HOH   43 343 82  HOH   HOH B . 
F 5 HOH   44 344 72  HOH   HOH B . 
F 5 HOH   45 345 108 HOH   HOH B . 
F 5 HOH   46 346 64  HOH   HOH B . 
F 5 HOH   47 347 62  HOH   HOH B . 
F 5 HOH   48 348 112 HOH   HOH B . 
F 5 HOH   49 349 26  HOH   HOH B . 
F 5 HOH   50 350 125 HOH   HOH B . 
F 5 HOH   51 351 123 HOH   HOH B . 
F 5 HOH   52 352 124 HOH   HOH B . 
F 5 HOH   53 353 61  HOH   HOH B . 
F 5 HOH   54 354 17  HOH   HOH B . 
F 5 HOH   55 355 87  HOH   HOH B . 
F 5 HOH   56 356 59  HOH   HOH B . 
F 5 HOH   57 357 109 HOH   HOH B . 
F 5 HOH   58 358 44  HOH   HOH B . 
F 5 HOH   59 359 75  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      '2.10.4 (20-OCT-2021)' ?               program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     .                      ?               program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 PDB_EXTRACT 3.23                   'SEP. 23, 2016' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
4 XDS         .                      ?               program ?                 ?                                'data reduction'  
?                                                   ?   ? 
5 PHASER      .                      ?               program ?                 ?                                phasing           
?                                                   ?   ? 
# 
_cell.entry_id           7I9M 
_cell.length_a           42.530 
_cell.length_b           42.530 
_cell.length_c           218.130 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I9M 
_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          7I9M 
_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   42.18 
_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   2024-02-27 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I9M 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.443 
_reflns.d_resolution_high            1.854 
_reflns.number_obs                   14741 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         92.500 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.700 
_reflns.B_iso_Wilson_estimate        43.510 
_reflns.pdbx_redundancy              24.300 
_reflns.pdbx_Rrim_I_all              0.183 
_reflns.pdbx_Rpim_I_all              0.037 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     357471 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.854 1.972  ? 17948 ? ? ? ? ? ? 24.400 ? 1.400  ? 737 ? ? ? ? 67.200  3.244 0.652 0.656 ? 
1 2 5.745 54.443 ? 15030 ? ? ? ? ? ? 20.400 ? 29.300 ? 737 ? ? ? ? 100.000 0.093 0.021 0.995 ? 
# 
_refine.entry_id                                 7I9M 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.8600 
_refine.ls_d_res_low                             42.5300 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     17894 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2371 
_refine.ls_R_factor_R_work                       0.2359 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2609 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.9500 
_refine.ls_number_reflns_R_free                  885 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               59.4700 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -5.3973 
_refine.aniso_B[2][2]                            -5.3973 
_refine.aniso_B[3][3]                            10.7946 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9430 
_refine.correlation_coeff_Fo_to_Fc_free          0.9370 
_refine.overall_SU_R_Cruickshank_DPI             0.1640 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.1450 
_refine.pdbx_overall_SU_R_Blow_DPI               0.1750 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1500 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      5GPI 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                115.620 
_refine.B_iso_min                                34.620 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7I9M 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.300 
_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.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8600 
_refine_hist.d_res_low                        42.5300 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             76 
_refine_hist.number_atoms_total               1586 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           86.18 
_refine_hist.pdbx_B_iso_mean_solvent          60.76 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        536  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              294  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1570 ?      ? 10.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 195  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' 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      1133 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1570 0.008  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2135 0.950  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.370  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    15.180 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.8600 
_refine_ls_shell.d_res_low                        1.8800 
_refine_ls_shell.pdbx_total_number_of_bins_used   45 
_refine_ls_shell.percent_reflns_obs               98.0500 
_refine_ls_shell.number_reflns_R_work             380 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.4234 
_refine_ls_shell.R_factor_R_free                  0.4430 
_refine_ls_shell.percent_reflns_R_free            6.6300 
_refine_ls_shell.number_reflns_R_free             27 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                407 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7I9M 
_struct.title                     
;Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0017733-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I9M 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, XChemExplorer, ASAP Discovery Consortium, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I9M A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I9M 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 7I9M SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I9M MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I9M MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I9M LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_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)' 4210 ? 
1 MORE         -27  ? 
1 'SSA (A^2)'  9860 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N SER B 128 ? N SER B 137 O TYR B 141 ? O TYR B 150 
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                   7I9M 
_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     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS B 80  ? ? 75.44   -10.94 
2 1 VAL B 100 ? ? -117.79 79.90  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 334 ? F HOH . 
2 1 B HOH 358 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.5203 -1.4941 -19.3880 -0.0086 -0.0755 -0.2518 0.2198 0.1464 0.1106 4.1525 4.1479 4.7238 
-2.3595 0.1356 1.1607 0.6014 -0.4871 -0.1142 0.4671 0.3537 -0.3794 -0.6378 0.0130 0.4452 
'X-RAY DIFFRACTION' 2 ? refined -18.3656 1.0981  -15.8137 0.0786  0.0020  -0.0798 0.1788 0.0385 0.0430 1.6159 1.8102 2.5445 
-1.6309 0.3775 0.0301 0.4845 -0.4047 -0.0797 0.1530 0.1856 0.0297  -0.2141 0.1455 0.2221 
# 
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.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 50 A 88  '{ A|* }' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 B 171 '{ B|* }' ? ? ? ? ? 
# 
_phasing.method   MR 
# 
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 
A1B86 N1   N  N N 1   
A1B86 C4   C  Y N 2   
A1B86 C5   C  Y N 3   
A1B86 C6   C  N N 4   
A1B86 C7   C  Y N 5   
A1B86 C8   C  Y N 6   
A1B86 C10  C  Y N 7   
A1B86 C13  C  N N 8   
A1B86 C15  C  Y N 9   
A1B86 C17  C  Y N 10  
A1B86 C20  C  Y N 11  
A1B86 C21  C  Y N 12  
A1B86 C22  C  Y N 13  
A1B86 O1   O  N N 14  
A1B86 C12  C  N N 15  
A1B86 O2   O  N N 16  
A1B86 C14  C  Y N 17  
A1B86 C19  C  Y N 18  
A1B86 C18  C  Y N 19  
A1B86 C16  C  Y N 20  
A1B86 N2   N  N N 21  
A1B86 C11  C  Y N 22  
A1B86 C9   C  Y N 23  
A1B86 CL   CL N N 24  
A1B86 O    O  N N 25  
A1B86 C3   C  Y N 26  
A1B86 C2   C  Y N 27  
A1B86 C1   C  N R 28  
A1B86 N    N  N N 29  
A1B86 C    C  N N 30  
A1B86 H8   H  N N 31  
A1B86 H7   H  N N 32  
A1B86 H9   H  N N 33  
A1B86 H10  H  N N 34  
A1B86 H12  H  N N 35  
A1B86 H13  H  N N 36  
A1B86 H14  H  N N 37  
A1B86 H16  H  N N 38  
A1B86 H19  H  N N 39  
A1B86 H20  H  N N 40  
A1B86 H21  H  N N 41  
A1B86 H18  H  N N 42  
A1B86 H17  H  N N 43  
A1B86 H15  H  N N 44  
A1B86 H11  H  N N 45  
A1B86 H6   H  N N 46  
A1B86 H    H  N N 47  
A1B86 H22  H  N N 48  
A1B86 H4   H  N N 49  
A1B86 H3   H  N N 50  
A1B86 H2   H  N N 51  
A1B86 H1   H  N N 52  
ALA   N    N  N N 53  
ALA   CA   C  N S 54  
ALA   C    C  N N 55  
ALA   O    O  N N 56  
ALA   CB   C  N N 57  
ALA   OXT  O  N N 58  
ALA   H    H  N N 59  
ALA   H2   H  N N 60  
ALA   HA   H  N N 61  
ALA   HB1  H  N N 62  
ALA   HB2  H  N N 63  
ALA   HB3  H  N N 64  
ALA   HXT  H  N N 65  
ARG   N    N  N N 66  
ARG   CA   C  N S 67  
ARG   C    C  N N 68  
ARG   O    O  N N 69  
ARG   CB   C  N N 70  
ARG   CG   C  N N 71  
ARG   CD   C  N N 72  
ARG   NE   N  N N 73  
ARG   CZ   C  N N 74  
ARG   NH1  N  N N 75  
ARG   NH2  N  N N 76  
ARG   OXT  O  N N 77  
ARG   H    H  N N 78  
ARG   H2   H  N N 79  
ARG   HA   H  N N 80  
ARG   HB2  H  N N 81  
ARG   HB3  H  N N 82  
ARG   HG2  H  N N 83  
ARG   HG3  H  N N 84  
ARG   HD2  H  N N 85  
ARG   HD3  H  N N 86  
ARG   HE   H  N N 87  
ARG   HH11 H  N N 88  
ARG   HH12 H  N N 89  
ARG   HH21 H  N N 90  
ARG   HH22 H  N N 91  
ARG   HXT  H  N N 92  
ASN   N    N  N N 93  
ASN   CA   C  N S 94  
ASN   C    C  N N 95  
ASN   O    O  N N 96  
ASN   CB   C  N N 97  
ASN   CG   C  N N 98  
ASN   OD1  O  N N 99  
ASN   ND2  N  N N 100 
ASN   OXT  O  N N 101 
ASN   H    H  N N 102 
ASN   H2   H  N N 103 
ASN   HA   H  N N 104 
ASN   HB2  H  N N 105 
ASN   HB3  H  N N 106 
ASN   HD21 H  N N 107 
ASN   HD22 H  N N 108 
ASN   HXT  H  N N 109 
ASP   N    N  N N 110 
ASP   CA   C  N S 111 
ASP   C    C  N N 112 
ASP   O    O  N N 113 
ASP   CB   C  N N 114 
ASP   CG   C  N N 115 
ASP   OD1  O  N N 116 
ASP   OD2  O  N N 117 
ASP   OXT  O  N N 118 
ASP   H    H  N N 119 
ASP   H2   H  N N 120 
ASP   HA   H  N N 121 
ASP   HB2  H  N N 122 
ASP   HB3  H  N N 123 
ASP   HD2  H  N N 124 
ASP   HXT  H  N N 125 
CYS   N    N  N N 126 
CYS   CA   C  N R 127 
CYS   C    C  N N 128 
CYS   O    O  N N 129 
CYS   CB   C  N N 130 
CYS   SG   S  N N 131 
CYS   OXT  O  N N 132 
CYS   H    H  N N 133 
CYS   H2   H  N N 134 
CYS   HA   H  N N 135 
CYS   HB2  H  N N 136 
CYS   HB3  H  N N 137 
CYS   HG   H  N N 138 
CYS   HXT  H  N N 139 
DMS   S    S  N N 140 
DMS   O    O  N N 141 
DMS   C1   C  N N 142 
DMS   C2   C  N N 143 
DMS   H11  H  N N 144 
DMS   H12  H  N N 145 
DMS   H13  H  N N 146 
DMS   H21  H  N N 147 
DMS   H22  H  N N 148 
DMS   H23  H  N N 149 
GLN   N    N  N N 150 
GLN   CA   C  N S 151 
GLN   C    C  N N 152 
GLN   O    O  N N 153 
GLN   CB   C  N N 154 
GLN   CG   C  N N 155 
GLN   CD   C  N N 156 
GLN   OE1  O  N N 157 
GLN   NE2  N  N N 158 
GLN   OXT  O  N N 159 
GLN   H    H  N N 160 
GLN   H2   H  N N 161 
GLN   HA   H  N N 162 
GLN   HB2  H  N N 163 
GLN   HB3  H  N N 164 
GLN   HG2  H  N N 165 
GLN   HG3  H  N N 166 
GLN   HE21 H  N N 167 
GLN   HE22 H  N N 168 
GLN   HXT  H  N N 169 
GLU   N    N  N N 170 
GLU   CA   C  N S 171 
GLU   C    C  N N 172 
GLU   O    O  N N 173 
GLU   CB   C  N N 174 
GLU   CG   C  N N 175 
GLU   CD   C  N N 176 
GLU   OE1  O  N N 177 
GLU   OE2  O  N N 178 
GLU   OXT  O  N N 179 
GLU   H    H  N N 180 
GLU   H2   H  N N 181 
GLU   HA   H  N N 182 
GLU   HB2  H  N N 183 
GLU   HB3  H  N N 184 
GLU   HG2  H  N N 185 
GLU   HG3  H  N N 186 
GLU   HE2  H  N N 187 
GLU   HXT  H  N N 188 
GLY   N    N  N N 189 
GLY   CA   C  N N 190 
GLY   C    C  N N 191 
GLY   O    O  N N 192 
GLY   OXT  O  N N 193 
GLY   H    H  N N 194 
GLY   H2   H  N N 195 
GLY   HA2  H  N N 196 
GLY   HA3  H  N N 197 
GLY   HXT  H  N N 198 
HIS   N    N  N N 199 
HIS   CA   C  N S 200 
HIS   C    C  N N 201 
HIS   O    O  N N 202 
HIS   CB   C  N N 203 
HIS   CG   C  Y N 204 
HIS   ND1  N  Y N 205 
HIS   CD2  C  Y N 206 
HIS   CE1  C  Y N 207 
HIS   NE2  N  Y N 208 
HIS   OXT  O  N N 209 
HIS   H    H  N N 210 
HIS   H2   H  N N 211 
HIS   HA   H  N N 212 
HIS   HB2  H  N N 213 
HIS   HB3  H  N N 214 
HIS   HD1  H  N N 215 
HIS   HD2  H  N N 216 
HIS   HE1  H  N N 217 
HIS   HE2  H  N N 218 
HIS   HXT  H  N N 219 
HOH   O    O  N N 220 
HOH   H1   H  N N 221 
HOH   H2   H  N N 222 
ILE   N    N  N N 223 
ILE   CA   C  N S 224 
ILE   C    C  N N 225 
ILE   O    O  N N 226 
ILE   CB   C  N S 227 
ILE   CG1  C  N N 228 
ILE   CG2  C  N N 229 
ILE   CD1  C  N N 230 
ILE   OXT  O  N N 231 
ILE   H    H  N N 232 
ILE   H2   H  N N 233 
ILE   HA   H  N N 234 
ILE   HB   H  N N 235 
ILE   HG12 H  N N 236 
ILE   HG13 H  N N 237 
ILE   HG21 H  N N 238 
ILE   HG22 H  N N 239 
ILE   HG23 H  N N 240 
ILE   HD11 H  N N 241 
ILE   HD12 H  N N 242 
ILE   HD13 H  N N 243 
ILE   HXT  H  N N 244 
LEU   N    N  N N 245 
LEU   CA   C  N S 246 
LEU   C    C  N N 247 
LEU   O    O  N N 248 
LEU   CB   C  N N 249 
LEU   CG   C  N N 250 
LEU   CD1  C  N N 251 
LEU   CD2  C  N N 252 
LEU   OXT  O  N N 253 
LEU   H    H  N N 254 
LEU   H2   H  N N 255 
LEU   HA   H  N N 256 
LEU   HB2  H  N N 257 
LEU   HB3  H  N N 258 
LEU   HG   H  N N 259 
LEU   HD11 H  N N 260 
LEU   HD12 H  N N 261 
LEU   HD13 H  N N 262 
LEU   HD21 H  N N 263 
LEU   HD22 H  N N 264 
LEU   HD23 H  N N 265 
LEU   HXT  H  N N 266 
LYS   N    N  N N 267 
LYS   CA   C  N S 268 
LYS   C    C  N N 269 
LYS   O    O  N N 270 
LYS   CB   C  N N 271 
LYS   CG   C  N N 272 
LYS   CD   C  N N 273 
LYS   CE   C  N N 274 
LYS   NZ   N  N N 275 
LYS   OXT  O  N N 276 
LYS   H    H  N N 277 
LYS   H2   H  N N 278 
LYS   HA   H  N N 279 
LYS   HB2  H  N N 280 
LYS   HB3  H  N N 281 
LYS   HG2  H  N N 282 
LYS   HG3  H  N N 283 
LYS   HD2  H  N N 284 
LYS   HD3  H  N N 285 
LYS   HE2  H  N N 286 
LYS   HE3  H  N N 287 
LYS   HZ1  H  N N 288 
LYS   HZ2  H  N N 289 
LYS   HZ3  H  N N 290 
LYS   HXT  H  N N 291 
MET   N    N  N N 292 
MET   CA   C  N S 293 
MET   C    C  N N 294 
MET   O    O  N N 295 
MET   CB   C  N N 296 
MET   CG   C  N N 297 
MET   SD   S  N N 298 
MET   CE   C  N N 299 
MET   OXT  O  N N 300 
MET   H    H  N N 301 
MET   H2   H  N N 302 
MET   HA   H  N N 303 
MET   HB2  H  N N 304 
MET   HB3  H  N N 305 
MET   HG2  H  N N 306 
MET   HG3  H  N N 307 
MET   HE1  H  N N 308 
MET   HE2  H  N N 309 
MET   HE3  H  N N 310 
MET   HXT  H  N N 311 
PHE   N    N  N N 312 
PHE   CA   C  N S 313 
PHE   C    C  N N 314 
PHE   O    O  N N 315 
PHE   CB   C  N N 316 
PHE   CG   C  Y N 317 
PHE   CD1  C  Y N 318 
PHE   CD2  C  Y N 319 
PHE   CE1  C  Y N 320 
PHE   CE2  C  Y N 321 
PHE   CZ   C  Y N 322 
PHE   OXT  O  N N 323 
PHE   H    H  N N 324 
PHE   H2   H  N N 325 
PHE   HA   H  N N 326 
PHE   HB2  H  N N 327 
PHE   HB3  H  N N 328 
PHE   HD1  H  N N 329 
PHE   HD2  H  N N 330 
PHE   HE1  H  N N 331 
PHE   HE2  H  N N 332 
PHE   HZ   H  N N 333 
PHE   HXT  H  N N 334 
PRO   N    N  N N 335 
PRO   CA   C  N S 336 
PRO   C    C  N N 337 
PRO   O    O  N N 338 
PRO   CB   C  N N 339 
PRO   CG   C  N N 340 
PRO   CD   C  N N 341 
PRO   OXT  O  N N 342 
PRO   H    H  N N 343 
PRO   HA   H  N N 344 
PRO   HB2  H  N N 345 
PRO   HB3  H  N N 346 
PRO   HG2  H  N N 347 
PRO   HG3  H  N N 348 
PRO   HD2  H  N N 349 
PRO   HD3  H  N N 350 
PRO   HXT  H  N N 351 
SER   N    N  N N 352 
SER   CA   C  N S 353 
SER   C    C  N N 354 
SER   O    O  N N 355 
SER   CB   C  N N 356 
SER   OG   O  N N 357 
SER   OXT  O  N N 358 
SER   H    H  N N 359 
SER   H2   H  N N 360 
SER   HA   H  N N 361 
SER   HB2  H  N N 362 
SER   HB3  H  N N 363 
SER   HG   H  N N 364 
SER   HXT  H  N N 365 
THR   N    N  N N 366 
THR   CA   C  N S 367 
THR   C    C  N N 368 
THR   O    O  N N 369 
THR   CB   C  N R 370 
THR   OG1  O  N N 371 
THR   CG2  C  N N 372 
THR   OXT  O  N N 373 
THR   H    H  N N 374 
THR   H2   H  N N 375 
THR   HA   H  N N 376 
THR   HB   H  N N 377 
THR   HG1  H  N N 378 
THR   HG21 H  N N 379 
THR   HG22 H  N N 380 
THR   HG23 H  N N 381 
THR   HXT  H  N N 382 
TRP   N    N  N N 383 
TRP   CA   C  N S 384 
TRP   C    C  N N 385 
TRP   O    O  N N 386 
TRP   CB   C  N N 387 
TRP   CG   C  Y N 388 
TRP   CD1  C  Y N 389 
TRP   CD2  C  Y N 390 
TRP   NE1  N  Y N 391 
TRP   CE2  C  Y N 392 
TRP   CE3  C  Y N 393 
TRP   CZ2  C  Y N 394 
TRP   CZ3  C  Y N 395 
TRP   CH2  C  Y N 396 
TRP   OXT  O  N N 397 
TRP   H    H  N N 398 
TRP   H2   H  N N 399 
TRP   HA   H  N N 400 
TRP   HB2  H  N N 401 
TRP   HB3  H  N N 402 
TRP   HD1  H  N N 403 
TRP   HE1  H  N N 404 
TRP   HE3  H  N N 405 
TRP   HZ2  H  N N 406 
TRP   HZ3  H  N N 407 
TRP   HH2  H  N N 408 
TRP   HXT  H  N N 409 
TYR   N    N  N N 410 
TYR   CA   C  N S 411 
TYR   C    C  N N 412 
TYR   O    O  N N 413 
TYR   CB   C  N N 414 
TYR   CG   C  Y N 415 
TYR   CD1  C  Y N 416 
TYR   CD2  C  Y N 417 
TYR   CE1  C  Y N 418 
TYR   CE2  C  Y N 419 
TYR   CZ   C  Y N 420 
TYR   OH   O  N N 421 
TYR   OXT  O  N N 422 
TYR   H    H  N N 423 
TYR   H2   H  N N 424 
TYR   HA   H  N N 425 
TYR   HB2  H  N N 426 
TYR   HB3  H  N N 427 
TYR   HD1  H  N N 428 
TYR   HD2  H  N N 429 
TYR   HE1  H  N N 430 
TYR   HE2  H  N N 431 
TYR   HH   H  N N 432 
TYR   HXT  H  N N 433 
VAL   N    N  N N 434 
VAL   CA   C  N S 435 
VAL   C    C  N N 436 
VAL   O    O  N N 437 
VAL   CB   C  N N 438 
VAL   CG1  C  N N 439 
VAL   CG2  C  N N 440 
VAL   OXT  O  N N 441 
VAL   H    H  N N 442 
VAL   H2   H  N N 443 
VAL   HA   H  N N 444 
VAL   HB   H  N N 445 
VAL   HG11 H  N N 446 
VAL   HG12 H  N N 447 
VAL   HG13 H  N N 448 
VAL   HG21 H  N N 449 
VAL   HG22 H  N N 450 
VAL   HG23 H  N N 451 
VAL   HXT  H  N N 452 
# 
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 
A1B86 C   C1   sing N N 1   
A1B86 N   C1   sing N N 2   
A1B86 C1  C2   sing N N 3   
A1B86 C2  C3   sing Y N 4   
A1B86 C3  C4   doub Y N 5   
A1B86 C4  C5   sing Y N 6   
A1B86 C5  N1   sing N N 7   
A1B86 N1  C6   sing N N 8   
A1B86 O   C6   doub N N 9   
A1B86 C6  C7   sing N N 10  
A1B86 C7  C8   sing Y N 11  
A1B86 C8  C9   doub Y N 12  
A1B86 CL  C9   sing N N 13  
A1B86 C9  C10  sing Y N 14  
A1B86 C10 C11  doub Y N 15  
A1B86 C11 N2   sing N N 16  
A1B86 N2  C12  sing N N 17  
A1B86 C12 O1   doub N N 18  
A1B86 O2  C12  sing N N 19  
A1B86 C13 O2   sing N N 20  
A1B86 C14 C13  sing N N 21  
A1B86 C14 C15  doub Y N 22  
A1B86 C15 C16  sing Y N 23  
A1B86 C16 C17  doub Y N 24  
A1B86 C17 C18  sing Y N 25  
A1B86 C18 C19  doub Y N 26  
A1B86 C19 C14  sing Y N 27  
A1B86 C20 C11  sing Y N 28  
A1B86 C7  C20  doub Y N 29  
A1B86 C21 C5   doub Y N 30  
A1B86 C22 C21  sing Y N 31  
A1B86 C2  C22  doub Y N 32  
A1B86 N1  H8   sing N N 33  
A1B86 C4  H7   sing N N 34  
A1B86 C8  H9   sing N N 35  
A1B86 C10 H10  sing N N 36  
A1B86 C13 H12  sing N N 37  
A1B86 C13 H13  sing N N 38  
A1B86 C15 H14  sing N N 39  
A1B86 C17 H16  sing N N 40  
A1B86 C20 H19  sing N N 41  
A1B86 C21 H20  sing N N 42  
A1B86 C22 H21  sing N N 43  
A1B86 C19 H18  sing N N 44  
A1B86 C18 H17  sing N N 45  
A1B86 C16 H15  sing N N 46  
A1B86 N2  H11  sing N N 47  
A1B86 C3  H6   sing N N 48  
A1B86 C1  H    sing N N 49  
A1B86 N   H22  sing N N 50  
A1B86 N   H4   sing N N 51  
A1B86 C   H3   sing N N 52  
A1B86 C   H2   sing N N 53  
A1B86 C   H1   sing N N 54  
ALA   N   CA   sing N N 55  
ALA   N   H    sing N N 56  
ALA   N   H2   sing N N 57  
ALA   CA  C    sing N N 58  
ALA   CA  CB   sing N N 59  
ALA   CA  HA   sing N N 60  
ALA   C   O    doub N N 61  
ALA   C   OXT  sing N N 62  
ALA   CB  HB1  sing N N 63  
ALA   CB  HB2  sing N N 64  
ALA   CB  HB3  sing N N 65  
ALA   OXT HXT  sing N N 66  
ARG   N   CA   sing N N 67  
ARG   N   H    sing N N 68  
ARG   N   H2   sing N N 69  
ARG   CA  C    sing N N 70  
ARG   CA  CB   sing N N 71  
ARG   CA  HA   sing N N 72  
ARG   C   O    doub N N 73  
ARG   C   OXT  sing N N 74  
ARG   CB  CG   sing N N 75  
ARG   CB  HB2  sing N N 76  
ARG   CB  HB3  sing N N 77  
ARG   CG  CD   sing N N 78  
ARG   CG  HG2  sing N N 79  
ARG   CG  HG3  sing N N 80  
ARG   CD  NE   sing N N 81  
ARG   CD  HD2  sing N N 82  
ARG   CD  HD3  sing N N 83  
ARG   NE  CZ   sing N N 84  
ARG   NE  HE   sing N N 85  
ARG   CZ  NH1  sing N N 86  
ARG   CZ  NH2  doub N N 87  
ARG   NH1 HH11 sing N N 88  
ARG   NH1 HH12 sing N N 89  
ARG   NH2 HH21 sing N N 90  
ARG   NH2 HH22 sing N N 91  
ARG   OXT HXT  sing N N 92  
ASN   N   CA   sing N N 93  
ASN   N   H    sing N N 94  
ASN   N   H2   sing N N 95  
ASN   CA  C    sing N N 96  
ASN   CA  CB   sing N N 97  
ASN   CA  HA   sing N N 98  
ASN   C   O    doub N N 99  
ASN   C   OXT  sing N N 100 
ASN   CB  CG   sing N N 101 
ASN   CB  HB2  sing N N 102 
ASN   CB  HB3  sing N N 103 
ASN   CG  OD1  doub N N 104 
ASN   CG  ND2  sing N N 105 
ASN   ND2 HD21 sing N N 106 
ASN   ND2 HD22 sing N N 107 
ASN   OXT HXT  sing N N 108 
ASP   N   CA   sing N N 109 
ASP   N   H    sing N N 110 
ASP   N   H2   sing N N 111 
ASP   CA  C    sing N N 112 
ASP   CA  CB   sing N N 113 
ASP   CA  HA   sing N N 114 
ASP   C   O    doub N N 115 
ASP   C   OXT  sing N N 116 
ASP   CB  CG   sing N N 117 
ASP   CB  HB2  sing N N 118 
ASP   CB  HB3  sing N N 119 
ASP   CG  OD1  doub N N 120 
ASP   CG  OD2  sing N N 121 
ASP   OD2 HD2  sing N N 122 
ASP   OXT HXT  sing N N 123 
CYS   N   CA   sing N N 124 
CYS   N   H    sing N N 125 
CYS   N   H2   sing N N 126 
CYS   CA  C    sing N N 127 
CYS   CA  CB   sing N N 128 
CYS   CA  HA   sing N N 129 
CYS   C   O    doub N N 130 
CYS   C   OXT  sing N N 131 
CYS   CB  SG   sing N N 132 
CYS   CB  HB2  sing N N 133 
CYS   CB  HB3  sing N N 134 
CYS   SG  HG   sing N N 135 
CYS   OXT HXT  sing N N 136 
DMS   S   O    doub N N 137 
DMS   S   C1   sing N N 138 
DMS   S   C2   sing N N 139 
DMS   C1  H11  sing N N 140 
DMS   C1  H12  sing N N 141 
DMS   C1  H13  sing N N 142 
DMS   C2  H21  sing N N 143 
DMS   C2  H22  sing N N 144 
DMS   C2  H23  sing N N 145 
GLN   N   CA   sing N N 146 
GLN   N   H    sing N N 147 
GLN   N   H2   sing N N 148 
GLN   CA  C    sing N N 149 
GLN   CA  CB   sing N N 150 
GLN   CA  HA   sing N N 151 
GLN   C   O    doub N N 152 
GLN   C   OXT  sing N N 153 
GLN   CB  CG   sing N N 154 
GLN   CB  HB2  sing N N 155 
GLN   CB  HB3  sing N N 156 
GLN   CG  CD   sing N N 157 
GLN   CG  HG2  sing N N 158 
GLN   CG  HG3  sing N N 159 
GLN   CD  OE1  doub N N 160 
GLN   CD  NE2  sing N N 161 
GLN   NE2 HE21 sing N N 162 
GLN   NE2 HE22 sing N N 163 
GLN   OXT HXT  sing N N 164 
GLU   N   CA   sing N N 165 
GLU   N   H    sing N N 166 
GLU   N   H2   sing N N 167 
GLU   CA  C    sing N N 168 
GLU   CA  CB   sing N N 169 
GLU   CA  HA   sing N N 170 
GLU   C   O    doub N N 171 
GLU   C   OXT  sing N N 172 
GLU   CB  CG   sing N N 173 
GLU   CB  HB2  sing N N 174 
GLU   CB  HB3  sing N N 175 
GLU   CG  CD   sing N N 176 
GLU   CG  HG2  sing N N 177 
GLU   CG  HG3  sing N N 178 
GLU   CD  OE1  doub N N 179 
GLU   CD  OE2  sing N N 180 
GLU   OE2 HE2  sing N N 181 
GLU   OXT HXT  sing N N 182 
GLY   N   CA   sing N N 183 
GLY   N   H    sing N N 184 
GLY   N   H2   sing N N 185 
GLY   CA  C    sing N N 186 
GLY   CA  HA2  sing N N 187 
GLY   CA  HA3  sing N N 188 
GLY   C   O    doub N N 189 
GLY   C   OXT  sing N N 190 
GLY   OXT HXT  sing N N 191 
HIS   N   CA   sing N N 192 
HIS   N   H    sing N N 193 
HIS   N   H2   sing N N 194 
HIS   CA  C    sing N N 195 
HIS   CA  CB   sing N N 196 
HIS   CA  HA   sing N N 197 
HIS   C   O    doub N N 198 
HIS   C   OXT  sing N N 199 
HIS   CB  CG   sing N N 200 
HIS   CB  HB2  sing N N 201 
HIS   CB  HB3  sing N N 202 
HIS   CG  ND1  sing Y N 203 
HIS   CG  CD2  doub Y N 204 
HIS   ND1 CE1  doub Y N 205 
HIS   ND1 HD1  sing N N 206 
HIS   CD2 NE2  sing Y N 207 
HIS   CD2 HD2  sing N N 208 
HIS   CE1 NE2  sing Y N 209 
HIS   CE1 HE1  sing N N 210 
HIS   NE2 HE2  sing N N 211 
HIS   OXT HXT  sing N N 212 
HOH   O   H1   sing N N 213 
HOH   O   H2   sing N N 214 
ILE   N   CA   sing N N 215 
ILE   N   H    sing N N 216 
ILE   N   H2   sing N N 217 
ILE   CA  C    sing N N 218 
ILE   CA  CB   sing N N 219 
ILE   CA  HA   sing N N 220 
ILE   C   O    doub N N 221 
ILE   C   OXT  sing N N 222 
ILE   CB  CG1  sing N N 223 
ILE   CB  CG2  sing N N 224 
ILE   CB  HB   sing N N 225 
ILE   CG1 CD1  sing N N 226 
ILE   CG1 HG12 sing N N 227 
ILE   CG1 HG13 sing N N 228 
ILE   CG2 HG21 sing N N 229 
ILE   CG2 HG22 sing N N 230 
ILE   CG2 HG23 sing N N 231 
ILE   CD1 HD11 sing N N 232 
ILE   CD1 HD12 sing N N 233 
ILE   CD1 HD13 sing N N 234 
ILE   OXT HXT  sing N N 235 
LEU   N   CA   sing N N 236 
LEU   N   H    sing N N 237 
LEU   N   H2   sing N N 238 
LEU   CA  C    sing N N 239 
LEU   CA  CB   sing N N 240 
LEU   CA  HA   sing N N 241 
LEU   C   O    doub N N 242 
LEU   C   OXT  sing N N 243 
LEU   CB  CG   sing N N 244 
LEU   CB  HB2  sing N N 245 
LEU   CB  HB3  sing N N 246 
LEU   CG  CD1  sing N N 247 
LEU   CG  CD2  sing N N 248 
LEU   CG  HG   sing N N 249 
LEU   CD1 HD11 sing N N 250 
LEU   CD1 HD12 sing N N 251 
LEU   CD1 HD13 sing N N 252 
LEU   CD2 HD21 sing N N 253 
LEU   CD2 HD22 sing N N 254 
LEU   CD2 HD23 sing N N 255 
LEU   OXT HXT  sing N N 256 
LYS   N   CA   sing N N 257 
LYS   N   H    sing N N 258 
LYS   N   H2   sing N N 259 
LYS   CA  C    sing N N 260 
LYS   CA  CB   sing N N 261 
LYS   CA  HA   sing N N 262 
LYS   C   O    doub N N 263 
LYS   C   OXT  sing N N 264 
LYS   CB  CG   sing N N 265 
LYS   CB  HB2  sing N N 266 
LYS   CB  HB3  sing N N 267 
LYS   CG  CD   sing N N 268 
LYS   CG  HG2  sing N N 269 
LYS   CG  HG3  sing N N 270 
LYS   CD  CE   sing N N 271 
LYS   CD  HD2  sing N N 272 
LYS   CD  HD3  sing N N 273 
LYS   CE  NZ   sing N N 274 
LYS   CE  HE2  sing N N 275 
LYS   CE  HE3  sing N N 276 
LYS   NZ  HZ1  sing N N 277 
LYS   NZ  HZ2  sing N N 278 
LYS   NZ  HZ3  sing N N 279 
LYS   OXT HXT  sing N N 280 
MET   N   CA   sing N N 281 
MET   N   H    sing N N 282 
MET   N   H2   sing N N 283 
MET   CA  C    sing N N 284 
MET   CA  CB   sing N N 285 
MET   CA  HA   sing N N 286 
MET   C   O    doub N N 287 
MET   C   OXT  sing N N 288 
MET   CB  CG   sing N N 289 
MET   CB  HB2  sing N N 290 
MET   CB  HB3  sing N N 291 
MET   CG  SD   sing N N 292 
MET   CG  HG2  sing N N 293 
MET   CG  HG3  sing N N 294 
MET   SD  CE   sing N N 295 
MET   CE  HE1  sing N N 296 
MET   CE  HE2  sing N N 297 
MET   CE  HE3  sing N N 298 
MET   OXT HXT  sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
_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_1002345 
_pdbx_deposit_group.group_description   
;XDomainX of XOrganismX None screened against the XXX Fragment Library by X-ray Crystallography at the XChem facility of Diamond Light Source beamline I04-1
;
_pdbx_deposit_group.group_title         
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7I9M 
_atom_sites.fract_transf_matrix[1][1]   0.023513 
_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]   0.023513 
_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]   0.004584 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? -21.550 19.455  -7.412  1.00 63.64  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.757 18.704  -7.721  1.00 63.63  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.647 17.952  -9.043  1.00 62.01  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.549 18.553  -10.117 1.00 62.89  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -24.009 19.590  -7.686  1.00 66.72  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.840 19.346  -6.442  1.00 74.91  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.364 20.346  -5.862  1.00 77.57  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.947 18.167  -6.021  1.00 77.38  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.640 16.640  -8.956  1.00 59.34  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.566 15.806  -10.142 1.00 56.93  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.946 15.539  -10.702 1.00 55.37  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.933 15.504  -9.956  1.00 55.72  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.832 14.516  -9.852  1.00 56.32  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.369 14.704  -9.737  1.00 57.10  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.576 13.114  -9.389  1.00 59.01  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.875 13.667  -9.241  1.00 61.14  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -24.029 15.437  -12.022 1.00 53.56  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.292 15.199  -12.711 1.00 53.41  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -25.127 14.220  -13.850 1.00 52.22  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -24.015 14.039  -14.354 1.00 52.02  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.948 16.508  -13.179 1.00 54.31  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.180 17.272  -14.238 1.00 56.73  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.284 18.272  -13.887 1.00 58.35  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.426 17.065  -15.591 1.00 58.61  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.633 19.033  -14.854 1.00 60.05  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.759 17.800  -16.568 1.00 60.04  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.860 18.784  -16.195 1.00 61.53  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.161 19.496  -17.148 1.00 64.13  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.229 13.578  -14.272 1.00 51.07  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.157 12.599  -15.360 1.00 50.37  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.943 13.055  -16.613 1.00 51.06  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.919 13.806  -16.490 1.00 50.62  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.589 11.195  -14.883 1.00 49.66  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -28.070 11.174  -14.427 1.00 50.20  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.653 10.664  -13.800 1.00 49.61  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.583 9.736   -14.088 1.00 51.37  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.497 12.613  -17.810 1.00 51.27  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.126 12.935  -19.105 1.00 51.95  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.200 11.656  -19.919 1.00 52.51  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.168 10.976  -20.036 1.00 52.01  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.253 13.915  -19.911 1.00 54.06  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.235 15.345  -19.418 1.00 60.93  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.425 16.280  -20.306 1.00 68.92  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.596 15.794  -21.111 1.00 72.19  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.595 17.512  -20.170 1.00 70.50  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.357 11.350  -20.556 1.00 53.07  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.436 10.115  -21.364 1.00 54.28  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.496 10.128  -22.574 1.00 54.26  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.342 11.168  -23.220 1.00 54.36  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.877 9.778   -21.782 1.00 57.33  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.066 8.273   -22.054 1.00 61.86  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.533 7.852   -22.118 1.00 65.72  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.661 6.410   -22.373 1.00 68.02  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.744 5.877   -23.592 1.00 69.53  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.710 6.652   -24.666 1.00 69.90  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.830 4.560   -23.744 1.00 68.18  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.840 8.987   -22.868 1.00 54.03  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.930 8.913   -24.003 1.00 55.41  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.294 7.843   -25.046 1.00 56.63  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.723 7.865   -26.132 1.00 58.03  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.492 8.734   -23.540 1.00 55.92  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.233 6.944   -24.745 1.00 55.87  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.658 5.944   -25.722 1.00 55.82  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.285 4.697   -25.137 1.00 55.89  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.403 4.574   -23.922 1.00 55.52  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.737 3.786   -26.014 1.00 56.08  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.320 2.501   -25.644 1.00 56.74  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.181 1.509   -25.458 1.00 58.53  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -27.143 1.659   -26.101 1.00 59.49  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.204 1.951   -26.785 1.00 57.23  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.572 2.587   -26.906 1.00 63.22  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.823 3.580   -26.212 1.00 62.28  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.379 2.126   -27.768 1.00 66.49  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.394 0.457   -24.659 1.00 58.65  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.376 -0.577  -24.506 1.00 59.90  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.744 -1.747  -25.402 1.00 61.20  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.658 -2.513  -25.084 1.00 60.94  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.213 -0.960  -23.042 1.00 60.35  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.602 0.220   -22.282 1.00 60.98  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.371 -2.238  -22.884 1.00 60.98  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.702 0.105   -20.862 1.00 61.75  ? 59  ILE   A CD1 1 
ATOM   82   N  N   . THR   A 1 17  ? -27.110 -1.817  -26.583 1.00 62.61  ? 60  THR   A N   1 
ATOM   83   C  CA  . THR   A 1 17  ? -27.373 -2.872  -27.563 1.00 64.84  ? 60  THR   A CA  1 
ATOM   84   C  C   . THR   A 1 17  ? -26.118 -3.315  -28.313 1.00 67.58  ? 60  THR   A C   1 
ATOM   85   O  O   . THR   A 1 17  ? -25.215 -2.511  -28.563 1.00 67.98  ? 60  THR   A O   1 
ATOM   86   C  CB  . THR   A 1 17  ? -28.524 -2.516  -28.565 1.00 66.24  ? 60  THR   A CB  1 
ATOM   87   O  OG1 . THR   A 1 17  ? -28.042 -1.788  -29.708 1.00 69.14  ? 60  THR   A OG1 1 
ATOM   88   C  CG2 . THR   A 1 17  ? -29.702 -1.791  -27.938 1.00 64.37  ? 60  THR   A CG2 1 
ATOM   89   N  N   . TRP   A 1 18  ? -26.094 -4.581  -28.729 1.00 69.42  ? 61  TRP   A N   1 
ATOM   90   C  CA  . TRP   A 1 18  ? -24.994 -5.084  -29.541 1.00 72.57  ? 61  TRP   A CA  1 
ATOM   91   C  C   . TRP   A 1 18  ? -25.164 -4.524  -30.956 1.00 76.50  ? 61  TRP   A C   1 
ATOM   92   O  O   . TRP   A 1 18  ? -26.286 -4.497  -31.477 1.00 77.28  ? 61  TRP   A O   1 
ATOM   93   C  CB  . TRP   A 1 18  ? -25.036 -6.611  -29.588 1.00 72.29  ? 61  TRP   A CB  1 
ATOM   94   C  CG  . TRP   A 1 18  ? -23.946 -7.240  -30.397 1.00 73.00  ? 61  TRP   A CG  1 
ATOM   95   C  CD1 . TRP   A 1 18  ? -24.007 -7.608  -31.709 1.00 74.16  ? 61  TRP   A CD1 1 
ATOM   96   C  CD2 . TRP   A 1 18  ? -22.690 -7.722  -29.902 1.00 73.32  ? 61  TRP   A CD2 1 
ATOM   97   N  NE1 . TRP   A 1 18  ? -22.846 -8.250  -32.074 1.00 74.74  ? 61  TRP   A NE1 1 
ATOM   98   C  CE2 . TRP   A 1 18  ? -22.023 -8.339  -30.979 1.00 74.26  ? 61  TRP   A CE2 1 
ATOM   99   C  CE3 . TRP   A 1 18  ? -22.043 -7.652  -28.663 1.00 73.60  ? 61  TRP   A CE3 1 
ATOM   100  C  CZ2 . TRP   A 1 18  ? -20.758 -8.911  -30.842 1.00 74.84  ? 61  TRP   A CZ2 1 
ATOM   101  C  CZ3 . TRP   A 1 18  ? -20.797 -8.226  -28.529 1.00 74.35  ? 61  TRP   A CZ3 1 
ATOM   102  C  CH2 . TRP   A 1 18  ? -20.163 -8.838  -29.610 1.00 74.56  ? 61  TRP   A CH2 1 
ATOM   103  N  N   . GLU   A 1 19  ? -24.073 -4.044  -31.566 1.00 78.86  ? 62  GLU   A N   1 
ATOM   104  C  CA  . GLU   A 1 19  ? -24.153 -3.519  -32.922 1.00 82.10  ? 62  GLU   A CA  1 
ATOM   105  C  C   . GLU   A 1 19  ? -23.423 -4.428  -33.896 1.00 85.74  ? 62  GLU   A C   1 
ATOM   106  O  O   . GLU   A 1 19  ? -22.228 -4.677  -33.736 1.00 85.67  ? 62  GLU   A O   1 
ATOM   107  C  CB  . GLU   A 1 19  ? -23.665 -2.070  -33.006 1.00 84.40  ? 62  GLU   A CB  1 
ATOM   108  C  CG  . GLU   A 1 19  ? -24.396 -1.132  -32.053 1.00 89.93  ? 62  GLU   A CG  1 
ATOM   109  C  CD  . GLU   A 1 19  ? -25.863 -0.826  -32.303 1.00 99.88  ? 62  GLU   A CD  1 
ATOM   110  O  OE1 . GLU   A 1 19  ? -26.328 -0.993  -33.455 1.00 103.61 ? 62  GLU   A OE1 1 
ATOM   111  O  OE2 . GLU   A 1 19  ? -26.542 -0.380  -31.348 1.00 101.38 ? 62  GLU   A OE2 1 
ATOM   112  N  N   . LYS   A 1 20  ? -24.162 -4.967  -34.874 1.00 88.77  ? 63  LYS   A N   1 
ATOM   113  C  CA  . LYS   A 1 20  ? -23.595 -5.853  -35.884 1.00 92.26  ? 63  LYS   A CA  1 
ATOM   114  C  C   . LYS   A 1 20  ? -22.647 -5.055  -36.758 1.00 94.07  ? 63  LYS   A C   1 
ATOM   115  O  O   . LYS   A 1 20  ? -22.958 -3.918  -37.108 1.00 94.41  ? 63  LYS   A O   1 
ATOM   116  C  CB  . LYS   A 1 20  ? -24.708 -6.446  -36.766 1.00 96.43  ? 63  LYS   A CB  1 
ATOM   117  C  CG  . LYS   A 1 20  ? -25.440 -7.631  -36.144 1.00 102.93 ? 63  LYS   A CG  1 
ATOM   118  C  CD  . LYS   A 1 20  ? -26.650 -8.013  -36.997 1.00 108.58 ? 63  LYS   A CD  1 
ATOM   119  C  CE  . LYS   A 1 20  ? -27.473 -9.125  -36.396 1.00 113.01 ? 63  LYS   A CE  1 
ATOM   120  N  NZ  . LYS   A 1 20  ? -28.660 -9.434  -37.238 1.00 115.62 ? 63  LYS   A NZ  1 
ATOM   121  N  N   . ASP   A 1 21  ? -21.503 -5.650  -37.124 1.00 94.93  ? 64  ASP   A N   1 
ATOM   122  C  CA  . ASP   A 1 21  ? -20.505 -4.977  -37.959 1.00 95.99  ? 64  ASP   A CA  1 
ATOM   123  C  C   . ASP   A 1 21  ? -20.013 -3.662  -37.331 1.00 94.92  ? 64  ASP   A C   1 
ATOM   124  O  O   . ASP   A 1 21  ? -20.041 -2.607  -37.964 1.00 94.96  ? 64  ASP   A O   1 
ATOM   125  C  CB  . ASP   A 1 21  ? -20.988 -4.781  -39.410 1.00 99.95  ? 64  ASP   A CB  1 
ATOM   126  C  CG  . ASP   A 1 21  ? -21.091 -6.074  -40.192 1.00 107.91 ? 64  ASP   A CG  1 
ATOM   127  O  OD1 . ASP   A 1 21  ? -20.157 -6.912  -40.085 1.00 110.38 ? 64  ASP   A OD1 1 
ATOM   128  O  OD2 . ASP   A 1 21  ? -22.099 -6.254  -40.910 1.00 110.09 ? 64  ASP   A OD2 1 
ATOM   129  N  N   . ALA   A 1 22  ? -19.608 -3.739  -36.057 1.00 93.44  ? 65  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 22  ? -19.000 -2.627  -35.331 1.00 92.15  ? 65  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 22  ? -17.473 -2.697  -35.616 1.00 90.81  ? 65  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 22  ? -16.990 -3.717  -36.128 1.00 90.67  ? 65  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 22  ? -19.259 -2.793  -33.841 1.00 92.36  ? 65  ALA   A CB  1 
ATOM   134  N  N   . GLU   A 1 23  ? -16.712 -1.631  -35.303 1.00 89.62  ? 66  GLU   A N   1 
ATOM   135  C  CA  . GLU   A 1 23  ? -15.261 -1.648  -35.522 1.00 89.01  ? 66  GLU   A CA  1 
ATOM   136  C  C   . GLU   A 1 23  ? -14.625 -2.718  -34.612 1.00 87.07  ? 66  GLU   A C   1 
ATOM   137  O  O   . GLU   A 1 23  ? -14.846 -2.688  -33.415 1.00 85.96  ? 66  GLU   A O   1 
ATOM   138  C  CB  . GLU   A 1 23  ? -14.653 -0.276  -35.204 1.00 92.38  ? 66  GLU   A CB  1 
ATOM   139  C  CG  . GLU   A 1 23  ? -13.145 -0.247  -35.375 1.00 99.58  ? 66  GLU   A CG  1 
ATOM   140  C  CD  . GLU   A 1 23  ? -12.415 0.729   -34.475 1.00 108.76 ? 66  GLU   A CD  1 
ATOM   141  O  OE1 . GLU   A 1 23  ? -13.076 1.635   -33.918 1.00 111.02 ? 66  GLU   A OE1 1 
ATOM   142  O  OE2 . GLU   A 1 23  ? -11.177 0.596   -34.338 1.00 111.60 ? 66  GLU   A OE2 1 
ATOM   143  N  N   . VAL   A 1 24  ? -13.888 -3.682  -35.186 1.00 86.15  ? 67  VAL   A N   1 
ATOM   144  C  CA  . VAL   A 1 24  ? -13.265 -4.747  -34.391 1.00 85.57  ? 67  VAL   A CA  1 
ATOM   145  C  C   . VAL   A 1 24  ? -11.783 -4.443  -34.171 1.00 84.70  ? 67  VAL   A C   1 
ATOM   146  O  O   . VAL   A 1 24  ? -11.043 -4.368  -35.142 1.00 84.94  ? 67  VAL   A O   1 
ATOM   147  C  CB  . VAL   A 1 24  ? -13.435 -6.136  -35.055 1.00 86.53  ? 67  VAL   A CB  1 
ATOM   148  C  CG1 . VAL   A 1 24  ? -12.969 -7.237  -34.121 1.00 86.80  ? 67  VAL   A CG1 1 
ATOM   149  C  CG2 . VAL   A 1 24  ? -14.877 -6.378  -35.490 1.00 87.40  ? 67  VAL   A CG2 1 
ATOM   150  N  N   . THR   A 1 25  ? -11.339 -4.261  -32.907 1.00 83.60  ? 68  THR   A N   1 
ATOM   151  C  CA  . THR   A 1 25  ? -9.927  -3.968  -32.618 1.00 82.79  ? 68  THR   A CA  1 
ATOM   152  C  C   . THR   A 1 25  ? -9.513  -4.434  -31.190 1.00 81.33  ? 68  THR   A C   1 
ATOM   153  O  O   . THR   A 1 25  ? -10.329 -5.001  -30.488 1.00 81.06  ? 68  THR   A O   1 
ATOM   154  C  CB  . THR   A 1 25  ? -9.612  -2.484  -32.904 1.00 84.40  ? 68  THR   A CB  1 
ATOM   155  O  OG1 . THR   A 1 25  ? -8.194  -2.368  -32.989 1.00 85.75  ? 68  THR   A OG1 1 
ATOM   156  C  CG2 . THR   A 1 25  ? -10.171 -1.555  -31.842 1.00 84.59  ? 68  THR   A CG2 1 
ATOM   157  N  N   . GLY   A 1 26  ? -8.252  -4.250  -30.801 1.00 80.49  ? 69  GLY   A N   1 
ATOM   158  C  CA  . GLY   A 1 26  ? -7.776  -4.644  -29.484 1.00 80.38  ? 69  GLY   A CA  1 
ATOM   159  C  C   . GLY   A 1 26  ? -7.218  -6.050  -29.410 1.00 79.91  ? 69  GLY   A C   1 
ATOM   160  O  O   . GLY   A 1 26  ? -7.800  -6.988  -29.960 1.00 80.26  ? 69  GLY   A O   1 
ATOM   161  N  N   . ASN   A 1 27  ? -6.087  -6.207  -28.718 1.00 78.58  ? 70  ASN   A N   1 
ATOM   162  C  CA  . ASN   A 1 27  ? -5.480  -7.518  -28.520 1.00 77.70  ? 70  ASN   A CA  1 
ATOM   163  C  C   . ASN   A 1 27  ? -6.021  -8.188  -27.205 1.00 75.60  ? 70  ASN   A C   1 
ATOM   164  O  O   . ASN   A 1 27  ? -6.874  -7.605  -26.535 1.00 75.01  ? 70  ASN   A O   1 
ATOM   165  C  CB  . ASN   A 1 27  ? -3.945  -7.415  -28.585 1.00 79.74  ? 70  ASN   A CB  1 
ATOM   166  C  CG  . ASN   A 1 27  ? -3.308  -6.796  -27.370 1.00 84.42  ? 70  ASN   A CG  1 
ATOM   167  O  OD1 . ASN   A 1 27  ? -3.708  -5.720  -26.906 1.00 86.53  ? 70  ASN   A OD1 1 
ATOM   168  N  ND2 . ASN   A 1 27  ? -2.290  -7.460  -26.829 1.00 85.01  ? 70  ASN   A ND2 1 
ATOM   169  N  N   . SER   A 1 28  ? -5.582  -9.421  -26.868 1.00 74.14  ? 71  SER   A N   1 
ATOM   170  C  CA  . SER   A 1 28  ? -6.056  -10.180 -25.695 1.00 73.40  ? 71  SER   A CA  1 
ATOM   171  C  C   . SER   A 1 28  ? -4.880  -10.626 -24.801 1.00 72.05  ? 71  SER   A C   1 
ATOM   172  O  O   . SER   A 1 28  ? -4.522  -11.806 -24.786 1.00 72.30  ? 71  SER   A O   1 
ATOM   173  C  CB  . SER   A 1 28  ? -6.847  -11.409 -26.149 1.00 75.64  ? 71  SER   A CB  1 
ATOM   174  O  OG  . SER   A 1 28  ? -7.636  -11.181 -27.305 1.00 79.86  ? 71  SER   A OG  1 
ATOM   175  N  N   . PRO   A 1 29  ? -4.244  -9.709  -24.057 1.00 70.53  ? 72  PRO   A N   1 
ATOM   176  C  CA  . PRO   A 1 29  ? -3.061  -10.107 -23.269 1.00 69.40  ? 72  PRO   A CA  1 
ATOM   177  C  C   . PRO   A 1 29  ? -3.380  -10.885 -21.994 1.00 67.60  ? 72  PRO   A C   1 
ATOM   178  O  O   . PRO   A 1 29  ? -4.406  -10.628 -21.363 1.00 66.82  ? 72  PRO   A O   1 
ATOM   179  C  CB  . PRO   A 1 29  ? -2.387  -8.769  -22.969 1.00 70.46  ? 72  PRO   A CB  1 
ATOM   180  C  CG  . PRO   A 1 29  ? -3.555  -7.798  -22.868 1.00 71.12  ? 72  PRO   A CG  1 
ATOM   181  C  CD  . PRO   A 1 29  ? -4.532  -8.264  -23.924 1.00 69.80  ? 72  PRO   A CD  1 
ATOM   182  N  N   . ARG   A 1 30  ? -2.514  -11.851 -21.619 1.00 66.68  ? 73  ARG   A N   1 
ATOM   183  C  CA  . ARG   A 1 30  ? -2.694  -12.601 -20.371 1.00 67.12  ? 73  ARG   A CA  1 
ATOM   184  C  C   . ARG   A 1 30  ? -1.673  -12.041 -19.380 1.00 65.92  ? 73  ARG   A C   1 
ATOM   185  O  O   . ARG   A 1 30  ? -0.473  -12.202 -19.580 1.00 65.95  ? 73  ARG   A O   1 
ATOM   186  C  CB  . ARG   A 1 30  ? -2.520  -14.120 -20.565 1.00 70.17  ? 73  ARG   A CB  1 
ATOM   187  C  CG  . ARG   A 1 30  ? -3.575  -14.746 -21.486 1.00 75.73  ? 73  ARG   A CG  1 
ATOM   188  C  CD  . ARG   A 1 30  ? -3.439  -16.266 -21.577 1.00 81.33  ? 73  ARG   A CD  1 
ATOM   189  N  NE  . ARG   A 1 30  ? -4.146  -16.822 -22.740 1.00 85.85  ? 73  ARG   A NE  1 
ATOM   190  C  CZ  . ARG   A 1 30  ? -5.417  -17.217 -22.730 1.00 87.58  ? 73  ARG   A CZ  1 
ATOM   191  N  NH1 . ARG   A 1 30  ? -6.140  -17.127 -21.620 1.00 88.51  ? 73  ARG   A NH1 1 
ATOM   192  N  NH2 . ARG   A 1 30  ? -5.974  -17.711 -23.830 1.00 85.11  ? 73  ARG   A NH2 1 
ATOM   193  N  N   . LEU   A 1 31  ? -2.150  -11.335 -18.347 1.00 64.52  ? 74  LEU   A N   1 
ATOM   194  C  CA  . LEU   A 1 31  ? -1.292  -10.630 -17.398 1.00 64.12  ? 74  LEU   A CA  1 
ATOM   195  C  C   . LEU   A 1 31  ? -1.428  -11.101 -15.952 1.00 63.23  ? 74  LEU   A C   1 
ATOM   196  O  O   . LEU   A 1 31  ? -2.547  -11.235 -15.470 1.00 63.13  ? 74  LEU   A O   1 
ATOM   197  C  CB  . LEU   A 1 31  ? -1.654  -9.122  -17.447 1.00 64.35  ? 74  LEU   A CB  1 
ATOM   198  C  CG  . LEU   A 1 31  ? -1.617  -8.454  -18.825 1.00 65.66  ? 74  LEU   A CG  1 
ATOM   199  C  CD1 . LEU   A 1 31  ? -2.113  -7.026  -18.752 1.00 65.90  ? 74  LEU   A CD1 1 
ATOM   200  C  CD2 . LEU   A 1 31  ? -0.217  -8.504  -19.420 1.00 66.28  ? 74  LEU   A CD2 1 
ATOM   201  N  N   . ASP   A 1 32  ? -0.304  -11.246 -15.222 1.00 62.36  ? 75  ASP   A N   1 
ATOM   202  C  CA  . ASP   A 1 32  ? -0.361  -11.593 -13.803 1.00 61.92  ? 75  ASP   A CA  1 
ATOM   203  C  C   . ASP   A 1 32  ? -0.532  -10.294 -13.030 1.00 59.86  ? 75  ASP   A C   1 
ATOM   204  O  O   . ASP   A 1 32  ? 0.344   -9.437  -13.113 1.00 59.81  ? 75  ASP   A O   1 
ATOM   205  C  CB  . ASP   A 1 32  ? 0.938   -12.269 -13.346 1.00 65.01  ? 75  ASP   A CB  1 
ATOM   206  C  CG  . ASP   A 1 32  ? 1.134   -13.682 -13.865 1.00 73.52  ? 75  ASP   A CG  1 
ATOM   207  O  OD1 . ASP   A 1 32  ? 0.152   -14.277 -14.362 1.00 75.35  ? 75  ASP   A OD1 1 
ATOM   208  O  OD2 . ASP   A 1 32  ? 2.271   -14.197 -13.768 1.00 77.42  ? 75  ASP   A OD2 1 
ATOM   209  N  N   . VAL   A 1 33  ? -1.655  -10.123 -12.301 1.00 57.98  ? 76  VAL   A N   1 
ATOM   210  C  CA  . VAL   A 1 33  ? -1.899  -8.882  -11.559 1.00 56.95  ? 76  VAL   A CA  1 
ATOM   211  C  C   . VAL   A 1 33  ? -2.227  -9.137  -10.069 1.00 56.67  ? 76  VAL   A C   1 
ATOM   212  O  O   . VAL   A 1 33  ? -2.514  -10.270 -9.663  1.00 57.17  ? 76  VAL   A O   1 
ATOM   213  C  CB  . VAL   A 1 33  ? -3.008  -7.995  -12.228 1.00 56.90  ? 76  VAL   A CB  1 
ATOM   214  C  CG1 . VAL   A 1 33  ? -2.676  -7.641  -13.668 1.00 57.56  ? 76  VAL   A CG1 1 
ATOM   215  C  CG2 . VAL   A 1 33  ? -4.370  -8.652  -12.128 1.00 56.48  ? 76  VAL   A CG2 1 
ATOM   216  N  N   . ALA   A 1 34  ? -2.161  -8.065  -9.256  1.00 55.42  ? 77  ALA   A N   1 
ATOM   217  C  CA  . ALA   A 1 34  ? -2.498  -8.056  -7.847  1.00 54.76  ? 77  ALA   A CA  1 
ATOM   218  C  C   . ALA   A 1 34  ? -3.479  -6.916  -7.602  1.00 53.78  ? 77  ALA   A C   1 
ATOM   219  O  O   . ALA   A 1 34  ? -3.371  -5.865  -8.230  1.00 53.90  ? 77  ALA   A O   1 
ATOM   220  C  CB  . ALA   A 1 34  ? -1.249  -7.856  -7.003  1.00 55.10  ? 77  ALA   A CB  1 
ATOM   221  N  N   . LEU   A 1 35  ? -4.437  -7.124  -6.703  1.00 52.62  ? 78  LEU   A N   1 
ATOM   222  C  CA  . LEU   A 1 35  ? -5.423  -6.112  -6.367  1.00 52.13  ? 78  LEU   A CA  1 
ATOM   223  C  C   . LEU   A 1 35  ? -5.246  -5.763  -4.887  1.00 52.36  ? 78  LEU   A C   1 
ATOM   224  O  O   . LEU   A 1 35  ? -5.166  -6.669  -4.023  1.00 53.01  ? 78  LEU   A O   1 
ATOM   225  C  CB  . LEU   A 1 35  ? -6.826  -6.654  -6.660  1.00 51.76  ? 78  LEU   A CB  1 
ATOM   226  C  CG  . LEU   A 1 35  ? -7.987  -5.755  -6.305  1.00 52.41  ? 78  LEU   A CG  1 
ATOM   227  C  CD1 . LEU   A 1 35  ? -7.983  -4.489  -7.155  1.00 52.72  ? 78  LEU   A CD1 1 
ATOM   228  C  CD2 . LEU   A 1 35  ? -9.293  -6.493  -6.486  1.00 52.69  ? 78  LEU   A CD2 1 
ATOM   229  N  N   . ASP   A 1 36  ? -5.066  -4.471  -4.597  1.00 51.40  ? 79  ASP   A N   1 
ATOM   230  C  CA  . ASP   A 1 36  ? -4.851  -4.054  -3.214  1.00 51.51  ? 79  ASP   A CA  1 
ATOM   231  C  C   . ASP   A 1 36  ? -6.164  -3.597  -2.549  1.00 51.74  ? 79  ASP   A C   1 
ATOM   232  O  O   . ASP   A 1 36  ? -7.186  -3.446  -3.224  1.00 51.81  ? 79  ASP   A O   1 
ATOM   233  C  CB  . ASP   A 1 36  ? -3.711  -3.015  -3.098  1.00 52.52  ? 79  ASP   A CB  1 
ATOM   234  C  CG  . ASP   A 1 36  ? -3.978  -1.637  -3.690  1.00 55.61  ? 79  ASP   A CG  1 
ATOM   235  O  OD1 . ASP   A 1 36  ? -5.156  -1.340  -4.020  1.00 54.29  ? 79  ASP   A OD1 1 
ATOM   236  O  OD2 . ASP   A 1 36  ? -3.011  -0.850  -3.818  1.00 58.33  ? 79  ASP   A OD2 1 
ATOM   237  N  N   . GLU   A 1 37  ? -6.132  -3.416  -1.232  1.00 52.04  ? 80  GLU   A N   1 
ATOM   238  C  CA  . GLU   A 1 37  ? -7.267  -2.980  -0.433  1.00 52.36  ? 80  GLU   A CA  1 
ATOM   239  C  C   . GLU   A 1 37  ? -7.847  -1.642  -0.936  1.00 51.31  ? 80  GLU   A C   1 
ATOM   240  O  O   . GLU   A 1 37  ? -9.030  -1.401  -0.751  1.00 51.61  ? 80  GLU   A O   1 
ATOM   241  C  CB  . GLU   A 1 37  ? -6.854  -2.910  1.046   1.00 55.67  ? 80  GLU   A CB  1 
ATOM   242  C  CG  . GLU   A 1 37  ? -8.029  -2.901  2.010   1.00 63.64  ? 80  GLU   A CG  1 
ATOM   243  C  CD  . GLU   A 1 37  ? -7.661  -2.891  3.481   1.00 71.05  ? 80  GLU   A CD  1 
ATOM   244  O  OE1 . GLU   A 1 37  ? -7.572  -1.787  4.064   1.00 70.96  ? 80  GLU   A OE1 1 
ATOM   245  O  OE2 . GLU   A 1 37  ? -7.451  -3.989  4.049   1.00 74.85  ? 80  GLU   A OE2 1 
ATOM   246  N  N   . SER   A 1 38  ? -7.054  -0.811  -1.634  1.00 50.49  ? 81  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 38  ? -7.556  0.450   -2.195  1.00 50.56  ? 81  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 38  ? -8.233  0.302   -3.572  1.00 49.17  ? 81  SER   A C   1 
ATOM   249  O  O   . SER   A 1 38  ? -8.676  1.304   -4.142  1.00 48.88  ? 81  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 38  ? -6.444  1.486   -2.285  1.00 53.54  ? 81  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 38  ? -6.011  1.870   -0.990  1.00 58.78  ? 81  SER   A OG  1 
ATOM   252  N  N   . GLY   A 1 39  ? -8.316  -0.921  -4.098  1.00 48.11  ? 82  GLY   A N   1 
ATOM   253  C  CA  . GLY   A 1 39  ? -8.951  -1.153  -5.396  1.00 48.51  ? 82  GLY   A CA  1 
ATOM   254  C  C   . GLY   A 1 39  ? -8.065  -0.865  -6.596  1.00 49.46  ? 82  GLY   A C   1 
ATOM   255  O  O   . GLY   A 1 39  ? -8.562  -0.755  -7.713  1.00 49.60  ? 82  GLY   A O   1 
ATOM   256  N  N   . ASP   A 1 40  ? -6.742  -0.789  -6.391  1.00 49.92  ? 83  ASP   A N   1 
ATOM   257  C  CA  . ASP   A 1 40  ? -5.785  -0.528  -7.455  1.00 51.15  ? 83  ASP   A CA  1 
ATOM   258  C  C   . ASP   A 1 40  ? -5.122  -1.814  -7.936  1.00 52.01  ? 83  ASP   A C   1 
ATOM   259  O  O   . ASP   A 1 40  ? -4.570  -2.577  -7.127  1.00 52.28  ? 83  ASP   A O   1 
ATOM   260  C  CB  . ASP   A 1 40  ? -4.684  0.435   -6.966  1.00 53.70  ? 83  ASP   A CB  1 
ATOM   261  C  CG  . ASP   A 1 40  ? -5.196  1.830   -6.716  1.00 60.67  ? 83  ASP   A CG  1 
ATOM   262  O  OD1 . ASP   A 1 40  ? -6.030  2.296   -7.502  1.00 61.99  ? 83  ASP   A OD1 1 
ATOM   263  O  OD2 . ASP   A 1 40  ? -4.760  2.453   -5.734  1.00 64.22  ? 83  ASP   A OD2 1 
ATOM   264  N  N   . PHE   A 1 41  ? -5.113  -2.017  -9.257  1.00 52.08  ? 84  PHE   A N   1 
ATOM   265  C  CA  . PHE   A 1 41  ? -4.458  -3.170  -9.852  1.00 53.09  ? 84  PHE   A CA  1 
ATOM   266  C  C   . PHE   A 1 41  ? -3.009  -2.827  -10.140 1.00 56.30  ? 84  PHE   A C   1 
ATOM   267  O  O   . PHE   A 1 41  ? -2.702  -1.703  -10.545 1.00 56.43  ? 84  PHE   A O   1 
ATOM   268  C  CB  . PHE   A 1 41  ? -5.148  -3.581  -11.160 1.00 51.24  ? 84  PHE   A CB  1 
ATOM   269  C  CG  . PHE   A 1 41  ? -6.441  -4.348  -11.015 1.00 49.92  ? 84  PHE   A CG  1 
ATOM   270  C  CD1 . PHE   A 1 41  ? -6.434  -5.698  -10.696 1.00 49.80  ? 84  PHE   A CD1 1 
ATOM   271  C  CD2 . PHE   A 1 41  ? -7.659  -3.737  -11.258 1.00 49.13  ? 84  PHE   A CD2 1 
ATOM   272  C  CE1 . PHE   A 1 41  ? -7.621  -6.416  -10.618 1.00 49.93  ? 84  PHE   A CE1 1 
ATOM   273  C  CE2 . PHE   A 1 41  ? -8.847  -4.455  -11.172 1.00 49.41  ? 84  PHE   A CE2 1 
ATOM   274  C  CZ  . PHE   A 1 41  ? -8.824  -5.788  -10.856 1.00 49.36  ? 84  PHE   A CZ  1 
ATOM   275  N  N   . SER   A 1 42  ? -2.113  -3.784  -9.935  1.00 58.70  ? 85  SER   A N   1 
ATOM   276  C  CA  . SER   A 1 42  ? -0.704  -3.593  -10.259 1.00 61.68  ? 85  SER   A CA  1 
ATOM   277  C  C   . SER   A 1 42  ? -0.158  -4.841  -10.949 1.00 64.45  ? 85  SER   A C   1 
ATOM   278  O  O   . SER   A 1 42  ? -0.681  -5.940  -10.737 1.00 64.05  ? 85  SER   A O   1 
ATOM   279  C  CB  . SER   A 1 42  ? 0.106   -3.258  -9.013  1.00 63.82  ? 85  SER   A CB  1 
ATOM   280  O  OG  . SER   A 1 42  ? 0.013   -4.283  -8.035  1.00 66.92  ? 85  SER   A OG  1 
ATOM   281  N  N   . LEU   A 1 43  ? 0.877   -4.680  -11.790 1.00 67.09  ? 86  LEU   A N   1 
ATOM   282  C  CA  . LEU   A 1 43  ? 1.468   -5.824  -12.480 1.00 70.35  ? 86  LEU   A CA  1 
ATOM   283  C  C   . LEU   A 1 43  ? 2.416   -6.585  -11.555 1.00 73.40  ? 86  LEU   A C   1 
ATOM   284  O  O   . LEU   A 1 43  ? 3.272   -5.983  -10.910 1.00 73.44  ? 86  LEU   A O   1 
ATOM   285  C  CB  . LEU   A 1 43  ? 2.239   -5.387  -13.734 1.00 71.13  ? 86  LEU   A CB  1 
ATOM   286  C  CG  . LEU   A 1 43  ? 1.420   -5.042  -14.973 1.00 73.35  ? 86  LEU   A CG  1 
ATOM   287  C  CD1 . LEU   A 1 43  ? 2.340   -4.684  -16.129 1.00 74.09  ? 86  LEU   A CD1 1 
ATOM   288  C  CD2 . LEU   A 1 43  ? 0.558   -6.217  -15.403 1.00 74.35  ? 86  LEU   A CD2 1 
ATOM   289  N  N   . VAL   A 1 44  ? 2.287   -7.913  -11.528 1.00 75.57  ? 87  VAL   A N   1 
ATOM   290  C  CA  . VAL   A 1 44  ? 3.143   -8.790  -10.738 1.00 78.00  ? 87  VAL   A CA  1 
ATOM   291  C  C   . VAL   A 1 44  ? 4.141   -9.416  -11.692 1.00 80.85  ? 87  VAL   A C   1 
ATOM   292  O  O   . VAL   A 1 44  ? 3.726   -9.972  -12.711 1.00 81.45  ? 87  VAL   A O   1 
ATOM   293  C  CB  . VAL   A 1 44  ? 2.298   -9.893  -10.065 1.00 78.66  ? 87  VAL   A CB  1 
ATOM   294  C  CG1 . VAL   A 1 44  ? 3.185   -10.961 -9.429  1.00 79.49  ? 87  VAL   A CG1 1 
ATOM   295  C  CG2 . VAL   A 1 44  ? 1.342   -9.297  -9.048  1.00 78.97  ? 87  VAL   A CG2 1 
ATOM   296  N  N   . GLU   A 1 45  ? 5.441   -9.316  -11.404 1.00 82.79  ? 88  GLU   A N   1 
ATOM   297  C  CA  . GLU   A 1 45  ? 6.442   -9.918  -12.288 1.00 85.04  ? 88  GLU   A CA  1 
ATOM   298  C  C   . GLU   A 1 45  ? 7.455   -10.777 -11.535 1.00 86.34  ? 88  GLU   A C   1 
ATOM   299  O  O   . GLU   A 1 45  ? 7.076   -11.543 -10.647 1.00 87.01  ? 88  GLU   A O   1 
ATOM   300  C  CB  . GLU   A 1 45  ? 7.126   -8.862  -13.174 1.00 88.55  ? 88  GLU   A CB  1 
ATOM   301  C  CG  . GLU   A 1 45  ? 6.168   -8.107  -14.089 1.00 94.00  ? 88  GLU   A CG  1 
ATOM   302  C  CD  . GLU   A 1 45  ? 6.746   -7.722  -15.437 1.00 101.19 ? 88  GLU   A CD  1 
ATOM   303  O  OE1 . GLU   A 1 45  ? 7.787   -8.302  -15.828 1.00 102.76 ? 88  GLU   A OE1 1 
ATOM   304  O  OE2 . GLU   A 1 45  ? 6.156   -6.840  -16.103 1.00 102.96 ? 88  GLU   A OE2 1 
ATOM   305  N  N   . GLY   B 2 7   ? -36.452 12.588  -12.120 1.00 68.46  ? 16  GLY   B N   1 
ATOM   306  C  CA  . GLY   B 2 7   ? -35.569 12.693  -13.274 1.00 69.15  ? 16  GLY   B CA  1 
ATOM   307  C  C   . GLY   B 2 7   ? -35.671 11.523  -14.235 1.00 69.31  ? 16  GLY   B C   1 
ATOM   308  O  O   . GLY   B 2 7   ? -36.560 10.674  -14.085 1.00 69.93  ? 16  GLY   B O   1 
ATOM   309  N  N   . GLU   B 2 8   ? -34.764 11.459  -15.232 1.00 68.20  ? 17  GLU   B N   1 
ATOM   310  C  CA  . GLU   B 2 8   ? -34.805 10.372  -16.205 1.00 67.66  ? 17  GLU   B CA  1 
ATOM   311  C  C   . GLU   B 2 8   ? -34.353 9.035   -15.635 1.00 66.36  ? 17  GLU   B C   1 
ATOM   312  O  O   . GLU   B 2 8   ? -33.236 8.895   -15.149 1.00 66.78  ? 17  GLU   B O   1 
ATOM   313  C  CB  . GLU   B 2 8   ? -34.044 10.703  -17.497 1.00 70.70  ? 17  GLU   B CB  1 
ATOM   314  C  CG  . GLU   B 2 8   ? -34.353 9.703   -18.598 1.00 76.45  ? 17  GLU   B CG  1 
ATOM   315  C  CD  . GLU   B 2 8   ? -33.740 10.017  -19.946 1.00 83.72  ? 17  GLU   B CD  1 
ATOM   316  O  OE1 . GLU   B 2 8   ? -32.709 10.727  -19.972 1.00 84.62  ? 17  GLU   B OE1 1 
ATOM   317  O  OE2 . GLU   B 2 8   ? -34.307 9.581   -20.976 1.00 86.43  ? 17  GLU   B OE2 1 
ATOM   318  N  N   A THR   B 2 9   ? -35.239 8.050   -15.695 0.50 65.52  ? 18  THR   B N   1 
ATOM   319  N  N   B THR   B 2 9   ? -35.240 8.043   -15.681 0.50 65.28  ? 18  THR   B N   1 
ATOM   320  C  CA  A THR   B 2 9   ? -34.961 6.712   -15.173 0.50 64.94  ? 18  THR   B CA  1 
ATOM   321  C  CA  B THR   B 2 9   ? -34.933 6.702   -15.187 0.50 64.47  ? 18  THR   B CA  1 
ATOM   322  C  C   A THR   B 2 9   ? -34.972 5.631   -16.273 0.50 63.44  ? 18  THR   B C   1 
ATOM   323  C  C   B THR   B 2 9   ? -34.941 5.634   -16.279 0.50 63.21  ? 18  THR   B C   1 
ATOM   324  O  O   A THR   B 2 9   ? -34.861 4.446   -15.956 0.50 63.54  ? 18  THR   B O   1 
ATOM   325  O  O   B THR   B 2 9   ? -34.803 4.452   -15.962 0.50 63.30  ? 18  THR   B O   1 
ATOM   326  C  CB  A THR   B 2 9   ? -35.898 6.342   -13.982 0.50 66.79  ? 18  THR   B CB  1 
ATOM   327  C  CB  B THR   B 2 9   ? -35.895 6.312   -14.070 0.50 65.74  ? 18  THR   B CB  1 
ATOM   328  O  OG1 A THR   B 2 9   ? -36.653 7.471   -13.513 0.50 68.43  ? 18  THR   B OG1 1 
ATOM   329  O  OG1 B THR   B 2 9   ? -37.234 6.460   -14.550 0.50 66.70  ? 18  THR   B OG1 1 
ATOM   330  C  CG2 A THR   B 2 9   ? -35.143 5.710   -12.817 0.50 67.20  ? 18  THR   B CG2 1 
ATOM   331  C  CG2 B THR   B 2 9   ? -35.675 7.127   -12.805 0.50 66.17  ? 18  THR   B CG2 1 
ATOM   332  N  N   . THR   B 2 10  ? -35.095 6.032   -17.559 1.00 61.91  ? 19  THR   B N   1 
ATOM   333  C  CA  . THR   B 2 10  ? -35.105 5.117   -18.693 1.00 59.35  ? 19  THR   B CA  1 
ATOM   334  C  C   . THR   B 2 10  ? -33.783 4.368   -18.749 1.00 56.58  ? 19  THR   B C   1 
ATOM   335  O  O   . THR   B 2 10  ? -32.724 4.980   -18.569 1.00 55.99  ? 19  THR   B O   1 
ATOM   336  C  CB  . THR   B 2 10  ? -35.294 5.926   -20.009 1.00 60.16  ? 19  THR   B CB  1 
ATOM   337  O  OG1 . THR   B 2 10  ? -36.411 6.812   -19.889 1.00 61.73  ? 19  THR   B OG1 1 
ATOM   338  C  CG2 . THR   B 2 10  ? -35.485 5.035   -21.218 1.00 59.60  ? 19  THR   B CG2 1 
ATOM   339  N  N   . ASP   B 2 11  ? -33.842 3.041   -18.942 1.00 54.93  ? 20  ASP   B N   1 
ATOM   340  C  CA  . ASP   B 2 11  ? -32.674 2.177   -19.104 1.00 54.90  ? 20  ASP   B CA  1 
ATOM   341  C  C   . ASP   B 2 11  ? -31.748 2.748   -20.200 1.00 54.05  ? 20  ASP   B C   1 
ATOM   342  O  O   . ASP   B 2 11  ? -32.244 3.360   -21.155 1.00 55.27  ? 20  ASP   B O   1 
ATOM   343  C  CB  . ASP   B 2 11  ? -33.117 0.766   -19.550 1.00 57.27  ? 20  ASP   B CB  1 
ATOM   344  C  CG  . ASP   B 2 11  ? -33.644 -0.142  -18.455 1.00 63.25  ? 20  ASP   B CG  1 
ATOM   345  O  OD1 . ASP   B 2 11  ? -33.902 0.360   -17.346 1.00 63.12  ? 20  ASP   B OD1 1 
ATOM   346  O  OD2 . ASP   B 2 11  ? -33.799 -1.364  -18.716 1.00 66.53  ? 20  ASP   B OD2 1 
ATOM   347  N  N   . GLY   B 2 12  ? -30.449 2.597   -20.031 1.00 51.59  ? 21  GLY   B N   1 
ATOM   348  C  CA  . GLY   B 2 12  ? -29.488 3.090   -21.004 1.00 50.21  ? 21  GLY   B CA  1 
ATOM   349  C  C   . GLY   B 2 12  ? -28.140 3.429   -20.402 1.00 48.63  ? 21  GLY   B C   1 
ATOM   350  O  O   . GLY   B 2 12  ? -27.895 3.171   -19.221 1.00 48.16  ? 21  GLY   B O   1 
ATOM   351  N  N   . VAL   B 2 13  ? -27.238 3.984   -21.229 1.00 47.12  ? 22  VAL   B N   1 
ATOM   352  C  CA  . VAL   B 2 13  ? -25.923 4.420   -20.784 1.00 45.36  ? 22  VAL   B CA  1 
ATOM   353  C  C   . VAL   B 2 13  ? -25.987 5.951   -20.572 1.00 44.91  ? 22  VAL   B C   1 
ATOM   354  O  O   . VAL   B 2 13  ? -26.685 6.652   -21.309 1.00 45.94  ? 22  VAL   B O   1 
ATOM   355  C  CB  . VAL   B 2 13  ? -24.810 3.965   -21.744 1.00 45.25  ? 22  VAL   B CB  1 
ATOM   356  C  CG1 . VAL   B 2 13  ? -24.973 4.578   -23.153 1.00 45.90  ? 22  VAL   B CG1 1 
ATOM   357  C  CG2 . VAL   B 2 13  ? -23.432 4.251   -21.166 1.00 44.79  ? 22  VAL   B CG2 1 
ATOM   358  N  N   . TYR   B 2 14  ? -25.323 6.461   -19.532 1.00 43.35  ? 23  TYR   B N   1 
ATOM   359  C  CA  . TYR   B 2 14  ? -25.376 7.875   -19.174 1.00 43.40  ? 23  TYR   B CA  1 
ATOM   360  C  C   . TYR   B 2 14  ? -23.998 8.451   -18.902 1.00 43.46  ? 23  TYR   B C   1 
ATOM   361  O  O   . TYR   B 2 14  ? -23.151 7.766   -18.350 1.00 43.48  ? 23  TYR   B O   1 
ATOM   362  C  CB  . TYR   B 2 14  ? -26.203 8.036   -17.883 1.00 43.18  ? 23  TYR   B CB  1 
ATOM   363  C  CG  . TYR   B 2 14  ? -27.701 7.895   -18.062 1.00 44.00  ? 23  TYR   B CG  1 
ATOM   364  C  CD1 . TYR   B 2 14  ? -28.279 6.654   -18.290 1.00 44.37  ? 23  TYR   B CD1 1 
ATOM   365  C  CD2 . TYR   B 2 14  ? -28.544 8.988   -17.913 1.00 45.06  ? 23  TYR   B CD2 1 
ATOM   366  C  CE1 . TYR   B 2 14  ? -29.647 6.513   -18.443 1.00 45.43  ? 23  TYR   B CE1 1 
ATOM   367  C  CE2 . TYR   B 2 14  ? -29.919 8.860   -18.063 1.00 46.51  ? 23  TYR   B CE2 1 
ATOM   368  C  CZ  . TYR   B 2 14  ? -30.468 7.616   -18.312 1.00 47.94  ? 23  TYR   B CZ  1 
ATOM   369  O  OH  . TYR   B 2 14  ? -31.823 7.461   -18.458 1.00 51.10  ? 23  TYR   B OH  1 
ATOM   370  N  N   . ARG   B 2 15  ? -23.798 9.727   -19.199 1.00 43.11  ? 24  ARG   B N   1 
ATOM   371  C  CA  . ARG   B 2 15  ? -22.559 10.422  -18.860 1.00 43.76  ? 24  ARG   B CA  1 
ATOM   372  C  C   . ARG   B 2 15  ? -22.678 10.958  -17.417 1.00 43.79  ? 24  ARG   B C   1 
ATOM   373  O  O   . ARG   B 2 15  ? -23.756 11.393  -17.026 1.00 44.13  ? 24  ARG   B O   1 
ATOM   374  C  CB  . ARG   B 2 15  ? -22.350 11.644  -19.787 1.00 45.06  ? 24  ARG   B CB  1 
ATOM   375  C  CG  . ARG   B 2 15  ? -22.244 11.326  -21.270 1.00 46.25  ? 24  ARG   B CG  1 
ATOM   376  C  CD  . ARG   B 2 15  ? -22.115 12.626  -22.086 1.00 48.89  ? 24  ARG   B CD  1 
ATOM   377  N  NE  . ARG   B 2 15  ? -22.350 12.369  -23.505 1.00 50.62  ? 24  ARG   B NE  1 
ATOM   378  C  CZ  . ARG   B 2 15  ? -21.429 11.944  -24.361 1.00 53.22  ? 24  ARG   B CZ  1 
ATOM   379  N  NH1 . ARG   B 2 15  ? -20.169 11.785  -23.968 1.00 50.94  ? 24  ARG   B NH1 1 
ATOM   380  N  NH2 . ARG   B 2 15  ? -21.753 11.694  -25.625 1.00 55.31  ? 24  ARG   B NH2 1 
ATOM   381  N  N   . VAL   B 2 16  ? -21.572 11.008  -16.667 1.00 43.66  ? 25  VAL   B N   1 
ATOM   382  C  CA  . VAL   B 2 16  ? -21.520 11.590  -15.323 1.00 45.04  ? 25  VAL   B CA  1 
ATOM   383  C  C   . VAL   B 2 16  ? -20.704 12.871  -15.432 1.00 46.30  ? 25  VAL   B C   1 
ATOM   384  O  O   . VAL   B 2 16  ? -19.526 12.827  -15.792 1.00 46.51  ? 25  VAL   B O   1 
ATOM   385  C  CB  . VAL   B 2 16  ? -20.891 10.651  -14.275 1.00 46.23  ? 25  VAL   B CB  1 
ATOM   386  C  CG1 . VAL   B 2 16  ? -20.836 11.342  -12.910 1.00 46.49  ? 25  VAL   B CG1 1 
ATOM   387  C  CG2 . VAL   B 2 16  ? -21.650 9.320   -14.198 1.00 46.76  ? 25  VAL   B CG2 1 
ATOM   388  N  N   . MET   B 2 17  ? -21.321 14.005  -15.156 1.00 47.17  ? 26  MET   B N   1 
ATOM   389  C  CA  . MET   B 2 17  ? -20.696 15.305  -15.332 1.00 48.80  ? 26  MET   B CA  1 
ATOM   390  C  C   . MET   B 2 17  ? -20.539 16.085  -14.027 1.00 51.64  ? 26  MET   B C   1 
ATOM   391  O  O   . MET   B 2 17  ? -21.291 15.859  -13.085 1.00 51.61  ? 26  MET   B O   1 
ATOM   392  C  CB  . MET   B 2 17  ? -21.590 16.154  -16.262 1.00 49.10  ? 26  MET   B CB  1 
ATOM   393  C  CG  . MET   B 2 17  ? -22.055 15.450  -17.546 1.00 50.22  ? 26  MET   B CG  1 
ATOM   394  S  SD  . MET   B 2 17  ? -20.751 15.294  -18.766 1.00 49.87  ? 26  MET   B SD  1 
ATOM   395  C  CE  . MET   B 2 17  ? -20.334 17.058  -19.045 1.00 46.33  ? 26  MET   B CE  1 
ATOM   396  N  N   . THR   B 2 18  ? -19.639 17.085  -14.011 1.00 53.34  ? 27  THR   B N   1 
ATOM   397  C  CA  . THR   B 2 18  ? -19.499 17.986  -12.872 1.00 56.13  ? 27  THR   B CA  1 
ATOM   398  C  C   . THR   B 2 18  ? -19.258 19.429  -13.357 1.00 58.64  ? 27  THR   B C   1 
ATOM   399  O  O   . THR   B 2 18  ? -18.617 19.637  -14.393 1.00 58.01  ? 27  THR   B O   1 
ATOM   400  C  CB  . THR   B 2 18  ? -18.385 17.514  -11.911 1.00 58.01  ? 27  THR   B CB  1 
ATOM   401  O  OG1 . THR   B 2 18  ? -18.274 18.474  -10.847 1.00 59.77  ? 27  THR   B OG1 1 
ATOM   402  C  CG2 . THR   B 2 18  ? -17.035 17.378  -12.599 1.00 58.08  ? 27  THR   B CG2 1 
ATOM   403  N  N   . ARG   B 2 19  ? -19.738 20.422  -12.598 1.00 61.19  ? 28  ARG   B N   1 
ATOM   404  C  CA  . ARG   B 2 19  ? -19.485 21.826  -12.917 1.00 64.34  ? 28  ARG   B CA  1 
ATOM   405  C  C   . ARG   B 2 19  ? -18.548 22.517  -11.901 1.00 66.62  ? 28  ARG   B C   1 
ATOM   406  O  O   . ARG   B 2 19  ? -18.462 23.746  -11.884 1.00 66.80  ? 28  ARG   B O   1 
ATOM   407  C  CB  . ARG   B 2 19  ? -20.795 22.611  -13.062 1.00 67.14  ? 28  ARG   B CB  1 
ATOM   408  C  CG  . ARG   B 2 19  ? -21.641 22.112  -14.217 1.00 72.35  ? 28  ARG   B CG  1 
ATOM   409  C  CD  . ARG   B 2 19  ? -22.260 23.244  -15.007 1.00 76.78  ? 28  ARG   B CD  1 
ATOM   410  N  NE  . ARG   B 2 19  ? -23.298 22.753  -15.913 1.00 81.57  ? 28  ARG   B NE  1 
ATOM   411  C  CZ  . ARG   B 2 19  ? -24.572 22.570  -15.571 1.00 85.54  ? 28  ARG   B CZ  1 
ATOM   412  N  NH1 . ARG   B 2 19  ? -24.981 22.840  -14.335 1.00 85.90  ? 28  ARG   B NH1 1 
ATOM   413  N  NH2 . ARG   B 2 19  ? -25.445 22.113  -16.459 1.00 85.93  ? 28  ARG   B NH2 1 
ATOM   414  N  N   . ARG   B 2 20  ? -17.853 21.734  -11.068 1.00 68.18  ? 29  ARG   B N   1 
ATOM   415  C  CA  . ARG   B 2 20  ? -16.962 22.237  -10.023 1.00 70.29  ? 29  ARG   B CA  1 
ATOM   416  C  C   . ARG   B 2 20  ? -15.693 22.808  -10.631 1.00 70.71  ? 29  ARG   B C   1 
ATOM   417  O  O   . ARG   B 2 20  ? -15.239 23.880  -10.227 1.00 71.51  ? 29  ARG   B O   1 
ATOM   418  C  CB  . ARG   B 2 20  ? -16.625 21.098  -9.036  1.00 73.49  ? 29  ARG   B CB  1 
ATOM   419  C  CG  . ARG   B 2 20  ? -15.769 21.527  -7.850  1.00 79.65  ? 29  ARG   B CG  1 
ATOM   420  C  CD  . ARG   B 2 20  ? -15.508 20.363  -6.910  1.00 85.08  ? 29  ARG   B CD  1 
ATOM   421  N  NE  . ARG   B 2 20  ? -14.547 19.405  -7.465  1.00 90.00  ? 29  ARG   B NE  1 
ATOM   422  C  CZ  . ARG   B 2 20  ? -13.306 19.239  -7.012  1.00 93.81  ? 29  ARG   B CZ  1 
ATOM   423  N  NH1 . ARG   B 2 20  ? -12.862 19.962  -5.989  1.00 93.99  ? 29  ARG   B NH1 1 
ATOM   424  N  NH2 . ARG   B 2 20  ? -12.501 18.348  -7.578  1.00 94.07  ? 29  ARG   B NH2 1 
ATOM   425  N  N   . LEU   B 2 21  ? -15.145 22.106  -11.627 1.00 69.86  ? 30  LEU   B N   1 
ATOM   426  C  CA  . LEU   B 2 21  ? -13.926 22.485  -12.336 1.00 69.50  ? 30  LEU   B CA  1 
ATOM   427  C  C   . LEU   B 2 21  ? -14.272 23.482  -13.491 1.00 68.63  ? 30  LEU   B C   1 
ATOM   428  O  O   . LEU   B 2 21  ? -15.359 24.073  -13.477 1.00 68.63  ? 30  LEU   B O   1 
ATOM   429  C  CB  . LEU   B 2 21  ? -13.269 21.186  -12.866 1.00 69.93  ? 30  LEU   B CB  1 
ATOM   430  C  CG  . LEU   B 2 21  ? -12.429 20.334  -11.896 1.00 71.92  ? 30  LEU   B CG  1 
ATOM   431  C  CD1 . LEU   B 2 21  ? -13.134 20.086  -10.581 1.00 72.53  ? 30  LEU   B CD1 1 
ATOM   432  C  CD2 . LEU   B 2 21  ? -12.096 18.988  -12.514 1.00 72.65  ? 30  LEU   B CD2 1 
ATOM   433  N  N   . LEU   B 2 22  ? -13.356 23.693  -14.469 1.00 67.53  ? 31  LEU   B N   1 
ATOM   434  C  CA  . LEU   B 2 22  ? -13.610 24.587  -15.600 1.00 66.53  ? 31  LEU   B CA  1 
ATOM   435  C  C   . LEU   B 2 22  ? -14.737 24.035  -16.476 1.00 65.01  ? 31  LEU   B C   1 
ATOM   436  O  O   . LEU   B 2 22  ? -14.701 22.854  -16.834 1.00 65.15  ? 31  LEU   B O   1 
ATOM   437  C  CB  . LEU   B 2 22  ? -12.340 24.731  -16.435 1.00 67.06  ? 31  LEU   B CB  1 
ATOM   438  C  CG  . LEU   B 2 22  ? -12.408 25.776  -17.519 1.00 68.46  ? 31  LEU   B CG  1 
ATOM   439  C  CD1 . LEU   B 2 22  ? -12.280 27.167  -16.941 1.00 68.69  ? 31  LEU   B CD1 1 
ATOM   440  C  CD2 . LEU   B 2 22  ? -11.349 25.523  -18.567 1.00 69.23  ? 31  LEU   B CD2 1 
ATOM   441  N  N   . GLY   B 2 23  ? -15.733 24.876  -16.776 1.00 63.17  ? 32  GLY   B N   1 
ATOM   442  C  CA  . GLY   B 2 23  ? -16.896 24.499  -17.577 1.00 61.84  ? 32  GLY   B CA  1 
ATOM   443  C  C   . GLY   B 2 23  ? -17.621 23.255  -17.088 1.00 60.21  ? 32  GLY   B C   1 
ATOM   444  O  O   . GLY   B 2 23  ? -17.769 23.050  -15.880 1.00 60.18  ? 32  GLY   B O   1 
ATOM   445  N  N   . SER   B 2 24  ? -18.076 22.406  -18.023 1.00 58.76  ? 33  SER   B N   1 
ATOM   446  C  CA  . SER   B 2 24  ? -18.755 21.154  -17.681 1.00 58.31  ? 33  SER   B CA  1 
ATOM   447  C  C   . SER   B 2 24  ? -17.819 20.037  -18.056 1.00 56.57  ? 33  SER   B C   1 
ATOM   448  O  O   . SER   B 2 24  ? -17.440 19.938  -19.219 1.00 56.21  ? 33  SER   B O   1 
ATOM   449  C  CB  . SER   B 2 24  ? -20.054 21.010  -18.466 1.00 60.82  ? 33  SER   B CB  1 
ATOM   450  O  OG  . SER   B 2 24  ? -20.997 21.981  -18.043 1.00 63.69  ? 33  SER   B OG  1 
ATOM   451  N  N   . THR   B 2 25  ? -17.406 19.220  -17.077 1.00 55.08  ? 34  THR   B N   1 
ATOM   452  C  CA  . THR   B 2 25  ? -16.431 18.175  -17.310 1.00 54.42  ? 34  THR   B CA  1 
ATOM   453  C  C   . THR   B 2 25  ? -17.020 16.788  -17.111 1.00 53.22  ? 34  THR   B C   1 
ATOM   454  O  O   . THR   B 2 25  ? -17.751 16.570  -16.144 1.00 53.06  ? 34  THR   B O   1 
ATOM   455  C  CB  . THR   B 2 25  ? -15.214 18.423  -16.401 1.00 55.85  ? 34  THR   B CB  1 
ATOM   456  O  OG1 . THR   B 2 25  ? -14.690 19.739  -16.654 1.00 57.28  ? 34  THR   B OG1 1 
ATOM   457  C  CG2 . THR   B 2 25  ? -14.114 17.399  -16.609 1.00 55.89  ? 34  THR   B CG2 1 
ATOM   458  N  N   . GLN   B 2 26  ? -16.716 15.850  -18.023 1.00 51.82  ? 35  GLN   B N   1 
ATOM   459  C  CA  . GLN   B 2 26  ? -17.218 14.490  -17.879 1.00 50.86  ? 35  GLN   B CA  1 
ATOM   460  C  C   . GLN   B 2 26  ? -16.231 13.706  -17.025 1.00 50.60  ? 35  GLN   B C   1 
ATOM   461  O  O   . GLN   B 2 26  ? -15.085 13.496  -17.452 1.00 51.14  ? 35  GLN   B O   1 
ATOM   462  C  CB  . GLN   B 2 26  ? -17.415 13.793  -19.240 1.00 50.43  ? 35  GLN   B CB  1 
ATOM   463  C  CG  . GLN   B 2 26  ? -17.918 12.348  -19.084 1.00 49.86  ? 35  GLN   B CG  1 
ATOM   464  C  CD  . GLN   B 2 26  ? -18.225 11.683  -20.399 1.00 49.43  ? 35  GLN   B CD  1 
ATOM   465  O  OE1 . GLN   B 2 26  ? -18.866 12.265  -21.265 1.00 49.62  ? 35  GLN   B OE1 1 
ATOM   466  N  NE2 . GLN   B 2 26  ? -17.788 10.445  -20.577 1.00 47.88  ? 35  GLN   B NE2 1 
ATOM   467  N  N   . VAL   B 2 27  ? -16.655 13.292  -15.823 1.00 48.79  ? 36  VAL   B N   1 
ATOM   468  C  CA  . VAL   B 2 27  ? -15.777 12.513  -14.929 1.00 47.48  ? 36  VAL   B CA  1 
ATOM   469  C  C   . VAL   B 2 27  ? -15.910 10.993  -15.112 1.00 45.98  ? 36  VAL   B C   1 
ATOM   470  O  O   . VAL   B 2 27  ? -15.039 10.243  -14.668 1.00 46.58  ? 36  VAL   B O   1 
ATOM   471  C  CB  . VAL   B 2 27  ? -15.950 12.910  -13.449 1.00 47.98  ? 36  VAL   B CB  1 
ATOM   472  C  CG1 . VAL   B 2 27  ? -15.345 14.277  -13.182 1.00 49.13  ? 36  VAL   B CG1 1 
ATOM   473  C  CG2 . VAL   B 2 27  ? -17.418 12.881  -13.040 1.00 48.01  ? 36  VAL   B CG2 1 
ATOM   474  N  N   . GLY   B 2 28  ? -16.979 10.545  -15.757 1.00 43.82  ? 37  GLY   B N   1 
ATOM   475  C  CA  . GLY   B 2 28  ? -17.193 9.124   -15.998 1.00 41.71  ? 37  GLY   B CA  1 
ATOM   476  C  C   . GLY   B 2 28  ? -18.514 8.848   -16.685 1.00 41.38  ? 37  GLY   B C   1 
ATOM   477  O  O   . GLY   B 2 28  ? -19.142 9.761   -17.245 1.00 41.52  ? 37  GLY   B O   1 
ATOM   478  N  N   . VAL   B 2 29  ? -18.938 7.580   -16.656 1.00 40.43  ? 38  VAL   B N   1 
ATOM   479  C  CA  . VAL   B 2 29  ? -20.099 7.017   -17.353 1.00 41.90  ? 38  VAL   B CA  1 
ATOM   480  C  C   . VAL   B 2 29  ? -20.797 5.975   -16.427 1.00 41.72  ? 38  VAL   B C   1 
ATOM   481  O  O   . VAL   B 2 29  ? -20.166 5.445   -15.521 1.00 41.38  ? 38  VAL   B O   1 
ATOM   482  C  CB  . VAL   B 2 29  ? -19.614 6.319   -18.683 1.00 43.71  ? 38  VAL   B CB  1 
ATOM   483  C  CG1 . VAL   B 2 29  ? -20.770 5.721   -19.474 1.00 44.52  ? 38  VAL   B CG1 1 
ATOM   484  C  CG2 . VAL   B 2 29  ? -18.809 7.269   -19.579 1.00 43.57  ? 38  VAL   B CG2 1 
ATOM   485  N  N   . GLY   B 2 30  ? -22.070 5.689   -16.673 1.00 40.66  ? 39  GLY   B N   1 
ATOM   486  C  CA  . GLY   B 2 30  ? -22.785 4.677   -15.912 1.00 40.95  ? 39  GLY   B CA  1 
ATOM   487  C  C   . GLY   B 2 30  ? -23.954 4.057   -16.650 1.00 41.61  ? 39  GLY   B C   1 
ATOM   488  O  O   . GLY   B 2 30  ? -24.329 4.521   -17.737 1.00 42.11  ? 39  GLY   B O   1 
ATOM   489  N  N   . VAL   B 2 31  ? -24.532 2.997   -16.069 1.00 40.10  ? 40  VAL   B N   1 
ATOM   490  C  CA  . VAL   B 2 31  ? -25.665 2.254   -16.621 1.00 40.15  ? 40  VAL   B CA  1 
ATOM   491  C  C   . VAL   B 2 31  ? -26.922 2.367   -15.755 1.00 40.59  ? 40  VAL   B C   1 
ATOM   492  O  O   . VAL   B 2 31  ? -26.885 2.047   -14.560 1.00 40.67  ? 40  VAL   B O   1 
ATOM   493  C  CB  . VAL   B 2 31  ? -25.293 0.754   -16.732 1.00 41.12  ? 40  VAL   B CB  1 
ATOM   494  C  CG1 . VAL   B 2 31  ? -26.471 -0.057  -17.261 1.00 42.27  ? 40  VAL   B CG1 1 
ATOM   495  C  CG2 . VAL   B 2 31  ? -24.059 0.569   -17.605 1.00 40.98  ? 40  VAL   B CG2 1 
ATOM   496  N  N   . MET   B 2 32  ? -28.045 2.696   -16.369 1.00 40.32  ? 41  MET   B N   1 
ATOM   497  C  CA  . MET   B 2 32  ? -29.322 2.728   -15.685 1.00 41.01  ? 41  MET   B CA  1 
ATOM   498  C  C   . MET   B 2 32  ? -30.036 1.426   -16.095 1.00 42.47  ? 41  MET   B C   1 
ATOM   499  O  O   . MET   B 2 32  ? -30.178 1.162   -17.285 1.00 42.77  ? 41  MET   B O   1 
ATOM   500  C  CB  . MET   B 2 32  ? -30.132 3.951   -16.133 1.00 41.40  ? 41  MET   B CB  1 
ATOM   501  C  CG  . MET   B 2 32  ? -31.386 4.189   -15.307 1.00 43.68  ? 41  MET   B CG  1 
ATOM   502  S  SD  . MET   B 2 32  ? -31.022 4.773   -13.625 1.00 46.75  ? 41  MET   B SD  1 
ATOM   503  C  CE  . MET   B 2 32  ? -30.678 6.523   -13.959 1.00 49.43  ? 41  MET   B CE  1 
ATOM   504  N  N   . GLN   B 2 33  ? -30.399 0.576   -15.135 1.00 43.04  ? 42  GLN   B N   1 
ATOM   505  C  CA  . GLN   B 2 33  ? -31.113 -0.662  -15.419 1.00 44.35  ? 42  GLN   B CA  1 
ATOM   506  C  C   . GLN   B 2 33  ? -31.994 -0.973  -14.230 1.00 46.22  ? 42  GLN   B C   1 
ATOM   507  O  O   . GLN   B 2 33  ? -31.501 -0.975  -13.102 1.00 46.59  ? 42  GLN   B O   1 
ATOM   508  C  CB  . GLN   B 2 33  ? -30.153 -1.836  -15.657 1.00 45.89  ? 42  GLN   B CB  1 
ATOM   509  C  CG  . GLN   B 2 33  ? -30.921 -3.127  -15.957 1.00 50.93  ? 42  GLN   B CG  1 
ATOM   510  C  CD  . GLN   B 2 33  ? -30.062 -4.248  -16.485 1.00 57.70  ? 42  GLN   B CD  1 
ATOM   511  O  OE1 . GLN   B 2 33  ? -30.150 -5.390  -16.010 1.00 60.66  ? 42  GLN   B OE1 1 
ATOM   512  N  NE2 . GLN   B 2 33  ? -29.206 -3.947  -17.466 1.00 56.55  ? 42  GLN   B NE2 1 
ATOM   513  N  N   . GLU   B 2 34  ? -33.286 -1.213  -14.471 1.00 46.91  ? 43  GLU   B N   1 
ATOM   514  C  CA  . GLU   B 2 34  ? -34.295 -1.545  -13.458 1.00 48.14  ? 43  GLU   B CA  1 
ATOM   515  C  C   . GLU   B 2 34  ? -34.445 -0.494  -12.361 1.00 49.00  ? 43  GLU   B C   1 
ATOM   516  O  O   . GLU   B 2 34  ? -34.712 -0.844  -11.217 1.00 50.55  ? 43  GLU   B O   1 
ATOM   517  C  CB  . GLU   B 2 34  ? -34.043 -2.942  -12.857 1.00 51.25  ? 43  GLU   B CB  1 
ATOM   518  C  CG  . GLU   B 2 34  ? -34.000 -4.049  -13.899 1.00 56.18  ? 43  GLU   B CG  1 
ATOM   519  C  CD  . GLU   B 2 34  ? -33.436 -5.377  -13.430 1.00 64.25  ? 43  GLU   B CD  1 
ATOM   520  O  OE1 . GLU   B 2 34  ? -33.965 -5.932  -12.441 1.00 66.24  ? 43  GLU   B OE1 1 
ATOM   521  O  OE2 . GLU   B 2 34  ? -32.472 -5.873  -14.059 1.00 67.03  ? 43  GLU   B OE2 1 
ATOM   522  N  N   . GLY   B 2 35  ? -34.282 0.782   -12.700 1.00 47.39  ? 44  GLY   B N   1 
ATOM   523  C  CA  . GLY   B 2 35  ? -34.411 1.853   -11.720 1.00 46.28  ? 44  GLY   B CA  1 
ATOM   524  C  C   . GLY   B 2 35  ? -33.184 2.093   -10.849 1.00 44.78  ? 44  GLY   B C   1 
ATOM   525  O  O   . GLY   B 2 35  ? -33.234 2.930   -9.941  1.00 44.92  ? 44  GLY   B O   1 
ATOM   526  N  N   . VAL   B 2 36  ? -32.064 1.396   -11.134 1.00 42.58  ? 45  VAL   B N   1 
ATOM   527  C  CA  . VAL   B 2 36  ? -30.800 1.525   -10.390 1.00 41.19  ? 45  VAL   B CA  1 
ATOM   528  C  C   . VAL   B 2 36  ? -29.675 2.082   -11.306 1.00 39.73  ? 45  VAL   B C   1 
ATOM   529  O  O   . VAL   B 2 36  ? -29.542 1.632   -12.452 1.00 40.04  ? 45  VAL   B O   1 
ATOM   530  C  CB  . VAL   B 2 36  ? -30.418 0.147   -9.739  1.00 41.83  ? 45  VAL   B CB  1 
ATOM   531  C  CG1 . VAL   B 2 36  ? -28.998 0.160   -9.149  1.00 41.84  ? 45  VAL   B CG1 1 
ATOM   532  C  CG2 . VAL   B 2 36  ? -31.436 -0.221  -8.649  1.00 42.40  ? 45  VAL   B CG2 1 
ATOM   533  N  N   . PHE   B 2 37  ? -28.901 3.076   -10.830 1.00 37.78  ? 46  PHE   B N   1 
ATOM   534  C  CA  . PHE   B 2 37  ? -27.796 3.642   -11.606 1.00 37.72  ? 46  PHE   B CA  1 
ATOM   535  C  C   . PHE   B 2 37  ? -26.506 2.982   -11.130 1.00 37.33  ? 46  PHE   B C   1 
ATOM   536  O  O   . PHE   B 2 37  ? -26.268 2.930   -9.930  1.00 36.43  ? 46  PHE   B O   1 
ATOM   537  C  CB  . PHE   B 2 37  ? -27.705 5.177   -11.434 1.00 38.17  ? 46  PHE   B CB  1 
ATOM   538  C  CG  . PHE   B 2 37  ? -26.714 5.765   -12.410 1.00 39.28  ? 46  PHE   B CG  1 
ATOM   539  C  CD1 . PHE   B 2 37  ? -26.914 5.654   -13.776 1.00 39.88  ? 46  PHE   B CD1 1 
ATOM   540  C  CD2 . PHE   B 2 37  ? -25.567 6.399   -11.962 1.00 40.79  ? 46  PHE   B CD2 1 
ATOM   541  C  CE1 . PHE   B 2 37  ? -25.980 6.157   -14.677 1.00 41.05  ? 46  PHE   B CE1 1 
ATOM   542  C  CE2 . PHE   B 2 37  ? -24.629 6.895   -12.863 1.00 41.18  ? 46  PHE   B CE2 1 
ATOM   543  C  CZ  . PHE   B 2 37  ? -24.857 6.798   -14.213 1.00 41.20  ? 46  PHE   B CZ  1 
ATOM   544  N  N   . HIS   B 2 38  ? -25.721 2.418   -12.040 1.00 37.23  ? 47  HIS   B N   1 
ATOM   545  C  CA  . HIS   B 2 38  ? -24.504 1.655   -11.726 1.00 36.80  ? 47  HIS   B CA  1 
ATOM   546  C  C   . HIS   B 2 38  ? -23.277 2.380   -12.298 1.00 37.56  ? 47  HIS   B C   1 
ATOM   547  O  O   . HIS   B 2 38  ? -23.265 2.704   -13.489 1.00 38.37  ? 47  HIS   B O   1 
ATOM   548  C  CB  . HIS   B 2 38  ? -24.559 0.264   -12.390 1.00 36.95  ? 47  HIS   B CB  1 
ATOM   549  C  CG  . HIS   B 2 38  ? -25.762 -0.558  -12.055 1.00 38.37  ? 47  HIS   B CG  1 
ATOM   550  N  ND1 . HIS   B 2 38  ? -27.016 -0.246  -12.555 1.00 40.38  ? 47  HIS   B ND1 1 
ATOM   551  C  CD2 . HIS   B 2 38  ? -25.865 -1.673  -11.294 1.00 39.08  ? 47  HIS   B CD2 1 
ATOM   552  C  CE1 . HIS   B 2 38  ? -27.846 -1.151  -12.054 1.00 40.29  ? 47  HIS   B CE1 1 
ATOM   553  N  NE2 . HIS   B 2 38  ? -27.195 -2.041  -11.308 1.00 40.28  ? 47  HIS   B NE2 1 
ATOM   554  N  N   . THR   B 2 39  ? -22.234 2.619   -11.479 1.00 36.59  ? 48  THR   B N   1 
ATOM   555  C  CA  . THR   B 2 39  ? -21.014 3.244   -11.999 1.00 36.88  ? 48  THR   B CA  1 
ATOM   556  C  C   . THR   B 2 39  ? -19.793 2.750   -11.174 1.00 37.32  ? 48  THR   B C   1 
ATOM   557  O  O   . THR   B 2 39  ? -19.933 1.831   -10.344 1.00 37.23  ? 48  THR   B O   1 
ATOM   558  C  CB  . THR   B 2 39  ? -21.162 4.799   -12.142 1.00 36.92  ? 48  THR   B CB  1 
ATOM   559  O  OG1 . THR   B 2 39  ? -19.966 5.303   -12.752 1.00 37.73  ? 48  THR   B OG1 1 
ATOM   560  C  CG2 . THR   B 2 39  ? -21.418 5.486   -10.812 1.00 36.74  ? 48  THR   B CG2 1 
ATOM   561  N  N   . MET   B 2 40  ? -18.592 3.292   -11.459 1.00 36.49  ? 49  MET   B N   1 
ATOM   562  C  CA  . MET   B 2 40  ? -17.394 2.931   -10.730 1.00 36.86  ? 49  MET   B CA  1 
ATOM   563  C  C   . MET   B 2 40  ? -17.215 3.883   -9.558  1.00 38.03  ? 49  MET   B C   1 
ATOM   564  O  O   . MET   B 2 40  ? -17.513 5.093   -9.657  1.00 37.39  ? 49  MET   B O   1 
ATOM   565  C  CB  . MET   B 2 40  ? -16.177 2.936   -11.667 1.00 37.27  ? 49  MET   B CB  1 
ATOM   566  C  CG  . MET   B 2 40  ? -16.412 2.111   -12.938 1.00 40.44  ? 49  MET   B CG  1 
ATOM   567  S  SD  . MET   B 2 40  ? -14.922 1.310   -13.554 1.00 48.94  ? 49  MET   B SD  1 
ATOM   568  C  CE  . MET   B 2 40  ? -14.797 -0.082  -12.418 1.00 41.99  ? 49  MET   B CE  1 
ATOM   569  N  N   . TRP   B 2 41  ? -16.721 3.359   -8.422  1.00 38.56  ? 50  TRP   B N   1 
ATOM   570  C  CA  A TRP   B 2 41  ? -16.537 4.189   -7.230  0.50 40.20  ? 50  TRP   B CA  1 
ATOM   571  C  CA  B TRP   B 2 41  ? -16.526 4.177   -7.228  0.50 38.82  ? 50  TRP   B CA  1 
ATOM   572  C  C   . TRP   B 2 41  ? -15.642 5.402   -7.496  1.00 40.12  ? 50  TRP   B C   1 
ATOM   573  O  O   . TRP   B 2 41  ? -15.935 6.467   -6.993  1.00 39.84  ? 50  TRP   B O   1 
ATOM   574  C  CB  A TRP   B 2 41  ? -16.001 3.366   -6.037  0.50 41.29  ? 50  TRP   B CB  1 
ATOM   575  C  CB  B TRP   B 2 41  ? -15.937 3.334   -6.075  0.50 37.91  ? 50  TRP   B CB  1 
ATOM   576  C  CG  A TRP   B 2 41  ? -16.123 4.073   -4.721  0.50 43.73  ? 50  TRP   B CG  1 
ATOM   577  C  CG  B TRP   B 2 41  ? -15.764 4.109   -4.811  0.50 37.58  ? 50  TRP   B CG  1 
ATOM   578  C  CD1 A TRP   B 2 41  ? -17.189 4.044   -3.871  0.50 45.09  ? 50  TRP   B CD1 1 
ATOM   579  C  CD1 B TRP   B 2 41  ? -14.729 4.934   -4.487  0.50 38.09  ? 50  TRP   B CD1 1 
ATOM   580  C  CD2 A TRP   B 2 41  ? -15.160 4.956   -4.129  0.50 44.72  ? 50  TRP   B CD2 1 
ATOM   581  C  CD2 B TRP   B 2 41  ? -16.685 4.170   -3.717  0.50 37.02  ? 50  TRP   B CD2 1 
ATOM   582  N  NE1 A TRP   B 2 41  ? -16.955 4.867   -2.795  0.50 46.05  ? 50  TRP   B NE1 1 
ATOM   583  N  NE1 B TRP   B 2 41  ? -14.978 5.552   -3.287  0.50 38.02  ? 50  TRP   B NE1 1 
ATOM   584  C  CE2 A TRP   B 2 41  ? -15.714 5.436   -2.927  0.50 45.87  ? 50  TRP   B CE2 1 
ATOM   585  C  CE2 B TRP   B 2 41  ? -16.163 5.086   -2.782  0.50 37.75  ? 50  TRP   B CE2 1 
ATOM   586  C  CE3 A TRP   B 2 41  ? -13.881 5.388   -4.500  0.50 45.69  ? 50  TRP   B CE3 1 
ATOM   587  C  CE3 B TRP   B 2 41  ? -17.927 3.583   -3.462  0.50 37.38  ? 50  TRP   B CE3 1 
ATOM   588  C  CZ2 A TRP   B 2 41  ? -15.027 6.308   -2.085  0.50 47.23  ? 50  TRP   B CZ2 1 
ATOM   589  C  CZ2 B TRP   B 2 41  ? -16.822 5.394   -1.591  0.50 38.10  ? 50  TRP   B CZ2 1 
ATOM   590  C  CZ3 A TRP   B 2 41  ? -13.210 6.269   -3.673  0.50 46.98  ? 50  TRP   B CZ3 1 
ATOM   591  C  CZ3 B TRP   B 2 41  ? -18.557 3.855   -2.261  0.50 38.56  ? 50  TRP   B CZ3 1 
ATOM   592  C  CH2 A TRP   B 2 41  ? -13.778 6.713   -2.478  0.50 47.58  ? 50  TRP   B CH2 1 
ATOM   593  C  CH2 B TRP   B 2 41  ? -18.011 4.760   -1.347  0.50 38.46  ? 50  TRP   B CH2 1 
ATOM   594  N  N   . HIS   B 2 42  ? -14.530 5.236   -8.246  1.00 40.87  ? 51  HIS   B N   1 
ATOM   595  C  CA  . HIS   B 2 42  ? -13.623 6.369   -8.473  1.00 42.08  ? 51  HIS   B CA  1 
ATOM   596  C  C   . HIS   B 2 42  ? -14.252 7.511   -9.296  1.00 43.51  ? 51  HIS   B C   1 
ATOM   597  O  O   . HIS   B 2 42  ? -13.711 8.620   -9.282  1.00 44.22  ? 51  HIS   B O   1 
ATOM   598  C  CB  . HIS   B 2 42  ? -12.271 5.931   -9.048  1.00 42.04  ? 51  HIS   B CB  1 
ATOM   599  C  CG  . HIS   B 2 42  ? -12.312 5.542   -10.489 1.00 43.69  ? 51  HIS   B CG  1 
ATOM   600  N  ND1 . HIS   B 2 42  ? -12.447 4.213   -10.882 1.00 44.62  ? 51  HIS   B ND1 1 
ATOM   601  C  CD2 . HIS   B 2 42  ? -12.237 6.325   -11.595 1.00 44.15  ? 51  HIS   B CD2 1 
ATOM   602  C  CE1 . HIS   B 2 42  ? -12.431 4.233   -12.208 1.00 44.93  ? 51  HIS   B CE1 1 
ATOM   603  N  NE2 . HIS   B 2 42  ? -12.302 5.484   -12.679 1.00 44.91  ? 51  HIS   B NE2 1 
ATOM   604  N  N   . VAL   B 2 43  ? -15.396 7.264   -9.985  1.00 42.86  ? 52  VAL   B N   1 
ATOM   605  C  CA  . VAL   B 2 43  ? -16.066 8.312   -10.750 1.00 42.58  ? 52  VAL   B CA  1 
ATOM   606  C  C   . VAL   B 2 43  ? -16.761 9.314   -9.809  1.00 43.46  ? 52  VAL   B C   1 
ATOM   607  O  O   . VAL   B 2 43  ? -16.574 10.529  -9.944  1.00 43.86  ? 52  VAL   B O   1 
ATOM   608  C  CB  . VAL   B 2 43  ? -17.083 7.717   -11.762 1.00 42.69  ? 52  VAL   B CB  1 
ATOM   609  C  CG1 . VAL   B 2 43  ? -17.940 8.822   -12.422 1.00 42.66  ? 52  VAL   B CG1 1 
ATOM   610  C  CG2 . VAL   B 2 43  ? -16.381 6.861   -12.815 1.00 42.37  ? 52  VAL   B CG2 1 
ATOM   611  N  N   . THR   B 2 44  ? -17.587 8.815   -8.868  1.00 42.43  ? 53  THR   B N   1 
ATOM   612  C  CA  . THR   B 2 44  ? -18.361 9.691   -7.993  1.00 42.77  ? 53  THR   B CA  1 
ATOM   613  C  C   . THR   B 2 44  ? -17.836 9.814   -6.569  1.00 43.69  ? 53  THR   B C   1 
ATOM   614  O  O   . THR   B 2 44  ? -18.273 10.715  -5.837  1.00 44.30  ? 53  THR   B O   1 
ATOM   615  C  CB  . THR   B 2 44  ? -19.820 9.201   -7.947  1.00 42.92  ? 53  THR   B CB  1 
ATOM   616  O  OG1 . THR   B 2 44  ? -19.903 7.961   -7.229  1.00 42.56  ? 53  THR   B OG1 1 
ATOM   617  C  CG2 . THR   B 2 44  ? -20.420 9.015   -9.350  1.00 43.17  ? 53  THR   B CG2 1 
ATOM   618  N  N   . LYS   B 2 45  ? -16.960 8.883   -6.140  1.00 43.76  ? 54  LYS   B N   1 
ATOM   619  C  CA  . LYS   B 2 45  ? -16.500 8.803   -4.742  1.00 45.29  ? 54  LYS   B CA  1 
ATOM   620  C  C   . LYS   B 2 45  ? -17.701 8.544   -3.779  1.00 46.27  ? 54  LYS   B C   1 
ATOM   621  O  O   . LYS   B 2 45  ? -17.631 8.888   -2.604  1.00 46.87  ? 54  LYS   B O   1 
ATOM   622  C  CB  . LYS   B 2 45  ? -15.746 10.076  -4.297  1.00 48.27  ? 54  LYS   B CB  1 
ATOM   623  C  CG  . LYS   B 2 45  ? -14.630 10.538  -5.228  1.00 54.33  ? 54  LYS   B CG  1 
ATOM   624  C  CD  . LYS   B 2 45  ? -13.448 9.622   -5.202  1.00 60.86  ? 54  LYS   B CD  1 
ATOM   625  C  CE  . LYS   B 2 45  ? -12.241 10.291  -5.838  1.00 66.41  ? 54  LYS   B CE  1 
ATOM   626  N  NZ  . LYS   B 2 45  ? -12.454 10.625  -7.280  1.00 69.13  ? 54  LYS   B NZ  1 
ATOM   627  N  N   . GLY   B 2 46  ? -18.798 7.982   -4.284  1.00 46.38  ? 55  GLY   B N   1 
ATOM   628  C  CA  . GLY   B 2 46  ? -19.978 7.715   -3.474  1.00 46.95  ? 55  GLY   B CA  1 
ATOM   629  C  C   . GLY   B 2 46  ? -20.875 8.923   -3.259  1.00 47.96  ? 55  GLY   B C   1 
ATOM   630  O  O   . GLY   B 2 46  ? -21.866 8.816   -2.546  1.00 47.94  ? 55  GLY   B O   1 
ATOM   631  N  N   . ALA   B 2 47  ? -20.568 10.080  -3.886  1.00 48.10  ? 56  ALA   B N   1 
ATOM   632  C  CA  . ALA   B 2 47  ? -21.394 11.281  -3.715  1.00 47.96  ? 56  ALA   B CA  1 
ATOM   633  C  C   . ALA   B 2 47  ? -22.757 11.173  -4.411  1.00 47.85  ? 56  ALA   B C   1 
ATOM   634  O  O   . ALA   B 2 47  ? -22.901 10.412  -5.357  1.00 47.51  ? 56  ALA   B O   1 
ATOM   635  C  CB  . ALA   B 2 47  ? -20.645 12.509  -4.222  1.00 48.25  ? 56  ALA   B CB  1 
ATOM   636  N  N   . ALA   B 2 48  ? -23.749 11.953  -3.954  1.00 47.67  ? 57  ALA   B N   1 
ATOM   637  C  CA  . ALA   B 2 48  ? -25.090 11.992  -4.540  1.00 47.96  ? 57  ALA   B CA  1 
ATOM   638  C  C   . ALA   B 2 48  ? -25.056 12.546  -5.963  1.00 47.68  ? 57  ALA   B C   1 
ATOM   639  O  O   . ALA   B 2 48  ? -24.150 13.298  -6.320  1.00 48.15  ? 57  ALA   B O   1 
ATOM   640  C  CB  . ALA   B 2 48  ? -26.020 12.850  -3.679  1.00 48.17  ? 57  ALA   B CB  1 
ATOM   641  N  N   . LEU   B 2 49  ? -26.043 12.173  -6.777  1.00 46.50  ? 58  LEU   B N   1 
ATOM   642  C  CA  . LEU   B 2 49  ? -26.111 12.581  -8.172  1.00 47.10  ? 58  LEU   B CA  1 
ATOM   643  C  C   . LEU   B 2 49  ? -27.425 13.284  -8.470  1.00 49.85  ? 58  LEU   B C   1 
ATOM   644  O  O   . LEU   B 2 49  ? -28.430 13.050  -7.806  1.00 50.42  ? 58  LEU   B O   1 
ATOM   645  C  CB  . LEU   B 2 49  ? -25.979 11.356  -9.103  1.00 45.95  ? 58  LEU   B CB  1 
ATOM   646  C  CG  . LEU   B 2 49  ? -24.666 10.585  -9.043  1.00 46.20  ? 58  LEU   B CG  1 
ATOM   647  C  CD1 . LEU   B 2 49  ? -24.710 9.381   -9.959  1.00 45.85  ? 58  LEU   B CD1 1 
ATOM   648  C  CD2 . LEU   B 2 49  ? -23.525 11.435  -9.455  1.00 46.83  ? 58  LEU   B CD2 1 
ATOM   649  N  N   . ARG   B 2 50  ? -27.420 14.132  -9.470  1.00 51.40  ? 59  ARG   B N   1 
ATOM   650  C  CA  . ARG   B 2 50  ? -28.596 14.854  -9.897  1.00 54.25  ? 59  ARG   B CA  1 
ATOM   651  C  C   . ARG   B 2 50  ? -29.050 14.305  -11.269 1.00 55.75  ? 59  ARG   B C   1 
ATOM   652  O  O   . ARG   B 2 50  ? -28.216 13.989  -12.123 1.00 55.25  ? 59  ARG   B O   1 
ATOM   653  C  CB  . ARG   B 2 50  ? -28.231 16.341  -9.977  1.00 57.44  ? 59  ARG   B CB  1 
ATOM   654  C  CG  . ARG   B 2 50  ? -29.377 17.259  -10.286 1.00 63.79  ? 59  ARG   B CG  1 
ATOM   655  C  CD  . ARG   B 2 50  ? -29.035 18.729  -10.044 1.00 69.46  ? 59  ARG   B CD  1 
ATOM   656  N  NE  . ARG   B 2 50  ? -27.822 19.184  -10.739 1.00 73.21  ? 59  ARG   B NE  1 
ATOM   657  C  CZ  . ARG   B 2 50  ? -27.785 19.567  -12.012 1.00 77.25  ? 59  ARG   B CZ  1 
ATOM   658  N  NH1 . ARG   B 2 50  ? -28.878 19.503  -12.765 1.00 77.08  ? 59  ARG   B NH1 1 
ATOM   659  N  NH2 . ARG   B 2 50  ? -26.647 19.988  -12.551 1.00 78.60  ? 59  ARG   B NH2 1 
ATOM   660  N  N   . SER   B 2 51  ? -30.357 14.127  -11.458 1.00 57.21  ? 60  SER   B N   1 
ATOM   661  C  CA  . SER   B 2 51  ? -30.902 13.700  -12.747 1.00 59.77  ? 60  SER   B CA  1 
ATOM   662  C  C   . SER   B 2 51  ? -32.029 14.665  -13.032 1.00 62.69  ? 60  SER   B C   1 
ATOM   663  O  O   . SER   B 2 51  ? -33.146 14.477  -12.547 1.00 62.89  ? 60  SER   B O   1 
ATOM   664  C  CB  . SER   B 2 51  ? -31.442 12.279  -12.682 1.00 60.85  ? 60  SER   B CB  1 
ATOM   665  O  OG  . SER   B 2 51  ? -31.892 11.887  -13.967 1.00 63.30  ? 60  SER   B OG  1 
ATOM   666  N  N   . GLY   B 2 52  ? -31.710 15.764  -13.703 1.00 64.41  ? 61  GLY   B N   1 
ATOM   667  C  CA  . GLY   B 2 52  ? -32.682 16.824  -13.935 1.00 66.16  ? 61  GLY   B CA  1 
ATOM   668  C  C   . GLY   B 2 52  ? -32.972 17.495  -12.613 1.00 68.12  ? 61  GLY   B C   1 
ATOM   669  O  O   . GLY   B 2 52  ? -32.042 17.937  -11.935 1.00 69.11  ? 61  GLY   B O   1 
ATOM   670  N  N   . GLU   B 2 53  ? -34.234 17.449  -12.175 1.00 68.29  ? 62  GLU   B N   1 
ATOM   671  C  CA  . GLU   B 2 53  ? -34.631 17.985  -10.876 1.00 68.92  ? 62  GLU   B CA  1 
ATOM   672  C  C   . GLU   B 2 53  ? -34.667 16.917  -9.756  1.00 68.11  ? 62  GLU   B C   1 
ATOM   673  O  O   . GLU   B 2 53  ? -34.950 17.259  -8.610  1.00 68.76  ? 62  GLU   B O   1 
ATOM   674  C  CB  . GLU   B 2 53  ? -36.013 18.635  -10.986 1.00 72.95  ? 62  GLU   B CB  1 
ATOM   675  C  CG  . GLU   B 2 53  ? -36.093 20.040  -10.418 1.00 80.66  ? 62  GLU   B CG  1 
ATOM   676  C  CD  . GLU   B 2 53  ? -37.507 20.592  -10.333 1.00 91.22  ? 62  GLU   B CD  1 
ATOM   677  O  OE1 . GLU   B 2 53  ? -38.415 20.019  -10.981 1.00 93.44  ? 62  GLU   B OE1 1 
ATOM   678  O  OE2 . GLU   B 2 53  ? -37.706 21.600  -9.616  1.00 94.46  ? 62  GLU   B OE2 1 
ATOM   679  N  N   . GLY   B 2 54  ? -34.414 15.652  -10.088 1.00 66.55  ? 63  GLY   B N   1 
ATOM   680  C  CA  . GLY   B 2 54  ? -34.445 14.568  -9.116  1.00 65.46  ? 63  GLY   B CA  1 
ATOM   681  C  C   . GLY   B 2 54  ? -33.084 14.251  -8.535  1.00 63.98  ? 63  GLY   B C   1 
ATOM   682  O  O   . GLY   B 2 54  ? -32.055 14.612  -9.114  1.00 64.54  ? 63  GLY   B O   1 
ATOM   683  N  N   . ARG   B 2 55  ? -33.064 13.577  -7.390  1.00 61.64  ? 64  ARG   B N   1 
ATOM   684  C  CA  . ARG   B 2 55  ? -31.816 13.223  -6.725  1.00 59.73  ? 64  ARG   B CA  1 
ATOM   685  C  C   . ARG   B 2 55  ? -31.600 11.697  -6.747  1.00 56.54  ? 64  ARG   B C   1 
ATOM   686  O  O   . ARG   B 2 55  ? -32.548 10.935  -6.561  1.00 56.98  ? 64  ARG   B O   1 
ATOM   687  C  CB  . ARG   B 2 55  ? -31.854 13.728  -5.267  1.00 61.70  ? 64  ARG   B CB  1 
ATOM   688  C  CG  . ARG   B 2 55  ? -30.504 13.683  -4.554  1.00 65.42  ? 64  ARG   B CG  1 
ATOM   689  C  CD  . ARG   B 2 55  ? -30.600 14.213  -3.132  1.00 68.84  ? 64  ARG   B CD  1 
ATOM   690  N  NE  . ARG   B 2 55  ? -29.396 13.917  -2.352  1.00 71.64  ? 64  ARG   B NE  1 
ATOM   691  C  CZ  . ARG   B 2 55  ? -28.772 14.795  -1.571  1.00 74.79  ? 64  ARG   B CZ  1 
ATOM   692  N  NH1 . ARG   B 2 55  ? -29.229 16.038  -1.459  1.00 74.54  ? 64  ARG   B NH1 1 
ATOM   693  N  NH2 . ARG   B 2 55  ? -27.683 14.439  -0.899  1.00 74.77  ? 64  ARG   B NH2 1 
ATOM   694  N  N   . LEU   B 2 56  ? -30.362 11.256  -6.958  1.00 52.86  ? 65  LEU   B N   1 
ATOM   695  C  CA  . LEU   B 2 56  ? -30.031 9.842   -6.891  1.00 50.66  ? 65  LEU   B CA  1 
ATOM   696  C  C   . LEU   B 2 56  ? -29.133 9.670   -5.670  1.00 48.54  ? 65  LEU   B C   1 
ATOM   697  O  O   . LEU   B 2 56  ? -28.039 10.235  -5.635  1.00 48.89  ? 65  LEU   B O   1 
ATOM   698  C  CB  . LEU   B 2 56  ? -29.286 9.345   -8.142  1.00 50.72  ? 65  LEU   B CB  1 
ATOM   699  C  CG  . LEU   B 2 56  ? -29.909 9.519   -9.539  1.00 52.88  ? 65  LEU   B CG  1 
ATOM   700  C  CD1 . LEU   B 2 56  ? -29.173 8.642   -10.554 1.00 52.68  ? 65  LEU   B CD1 1 
ATOM   701  C  CD2 . LEU   B 2 56  ? -31.385 9.135   -9.553  1.00 54.34  ? 65  LEU   B CD2 1 
ATOM   702  N  N   . ASP   B 2 57  ? -29.575 8.904   -4.680  1.00 46.48  ? 66  ASP   B N   1 
ATOM   703  C  CA  . ASP   B 2 57  ? -28.776 8.661   -3.490  1.00 45.86  ? 66  ASP   B CA  1 
ATOM   704  C  C   . ASP   B 2 57  ? -28.060 7.319   -3.564  1.00 44.56  ? 66  ASP   B C   1 
ATOM   705  O  O   . ASP   B 2 57  ? -28.619 6.326   -4.064  1.00 44.27  ? 66  ASP   B O   1 
ATOM   706  C  CB  . ASP   B 2 57  ? -29.648 8.747   -2.236  1.00 49.73  ? 66  ASP   B CB  1 
ATOM   707  C  CG  . ASP   B 2 57  ? -30.181 10.152  -2.029  1.00 56.90  ? 66  ASP   B CG  1 
ATOM   708  O  OD1 . ASP   B 2 57  ? -29.415 11.114  -2.251  1.00 58.27  ? 66  ASP   B OD1 1 
ATOM   709  O  OD2 . ASP   B 2 57  ? -31.366 10.290  -1.681  1.00 60.06  ? 66  ASP   B OD2 1 
ATOM   710  N  N   . PRO   B 2 58  ? -26.793 7.268   -3.102  1.00 42.76  ? 67  PRO   B N   1 
ATOM   711  C  CA  . PRO   B 2 58  ? -26.071 5.983   -3.094  1.00 41.28  ? 67  PRO   B CA  1 
ATOM   712  C  C   . PRO   B 2 58  ? -26.816 4.931   -2.265  1.00 39.96  ? 67  PRO   B C   1 
ATOM   713  O  O   . PRO   B 2 58  ? -27.530 5.270   -1.310  1.00 39.95  ? 67  PRO   B O   1 
ATOM   714  C  CB  . PRO   B 2 58  ? -24.712 6.343   -2.482  1.00 42.35  ? 67  PRO   B CB  1 
ATOM   715  C  CG  . PRO   B 2 58  ? -24.975 7.616   -1.684  1.00 43.48  ? 67  PRO   B CG  1 
ATOM   716  C  CD  . PRO   B 2 58  ? -25.998 8.353   -2.493  1.00 42.34  ? 67  PRO   B CD  1 
ATOM   717  N  N   . TYR   B 2 59  ? -26.694 3.672   -2.639  1.00 38.29  ? 68  TYR   B N   1 
ATOM   718  C  CA  . TYR   B 2 59  ? -27.376 2.582   -1.947  1.00 37.51  ? 68  TYR   B CA  1 
ATOM   719  C  C   . TYR   B 2 59  ? -26.367 1.534   -1.504  1.00 37.25  ? 68  TYR   B C   1 
ATOM   720  O  O   . TYR   B 2 59  ? -26.487 1.000   -0.408  1.00 37.41  ? 68  TYR   B O   1 
ATOM   721  C  CB  . TYR   B 2 59  ? -28.402 1.930   -2.896  1.00 37.05  ? 68  TYR   B CB  1 
ATOM   722  C  CG  . TYR   B 2 59  ? -29.244 0.842   -2.259  1.00 37.72  ? 68  TYR   B CG  1 
ATOM   723  C  CD1 . TYR   B 2 59  ? -28.783 -0.467  -2.179  1.00 38.02  ? 68  TYR   B CD1 1 
ATOM   724  C  CD2 . TYR   B 2 59  ? -30.506 1.119   -1.755  1.00 38.66  ? 68  TYR   B CD2 1 
ATOM   725  C  CE1 . TYR   B 2 59  ? -29.563 -1.475  -1.634  1.00 39.39  ? 68  TYR   B CE1 1 
ATOM   726  C  CE2 . TYR   B 2 59  ? -31.294 0.118   -1.197  1.00 39.78  ? 68  TYR   B CE2 1 
ATOM   727  C  CZ  . TYR   B 2 59  ? -30.822 -1.182  -1.152  1.00 40.85  ? 68  TYR   B CZ  1 
ATOM   728  O  OH  . TYR   B 2 59  ? -31.585 -2.167  -0.574  1.00 43.07  ? 68  TYR   B OH  1 
ATOM   729  N  N   . TRP   B 2 60  ? -25.397 1.217   -2.349  1.00 37.01  ? 69  TRP   B N   1 
ATOM   730  C  CA  . TRP   B 2 60  ? -24.362 0.223   -2.011  1.00 37.41  ? 69  TRP   B CA  1 
ATOM   731  C  C   . TRP   B 2 60  ? -23.067 0.663   -2.684  1.00 37.60  ? 69  TRP   B C   1 
ATOM   732  O  O   . TRP   B 2 60  ? -23.115 1.233   -3.761  1.00 38.30  ? 69  TRP   B O   1 
ATOM   733  C  CB  . TRP   B 2 60  ? -24.745 -1.201  -2.516  1.00 37.32  ? 69  TRP   B CB  1 
ATOM   734  C  CG  . TRP   B 2 60  ? -23.589 -2.187  -2.512  1.00 39.05  ? 69  TRP   B CG  1 
ATOM   735  C  CD1 . TRP   B 2 60  ? -23.161 -2.948  -1.459  1.00 40.63  ? 69  TRP   B CD1 1 
ATOM   736  C  CD2 . TRP   B 2 60  ? -22.687 -2.465  -3.600  1.00 39.83  ? 69  TRP   B CD2 1 
ATOM   737  N  NE1 . TRP   B 2 60  ? -22.052 -3.696  -1.834  1.00 40.89  ? 69  TRP   B NE1 1 
ATOM   738  C  CE2 . TRP   B 2 60  ? -21.741 -3.408  -3.137  1.00 40.67  ? 69  TRP   B CE2 1 
ATOM   739  C  CE3 . TRP   B 2 60  ? -22.590 -2.008  -4.927  1.00 40.80  ? 69  TRP   B CE3 1 
ATOM   740  C  CZ2 . TRP   B 2 60  ? -20.704 -3.882  -3.945  1.00 41.41  ? 69  TRP   B CZ2 1 
ATOM   741  C  CZ3 . TRP   B 2 60  ? -21.569 -2.487  -5.725  1.00 41.58  ? 69  TRP   B CZ3 1 
ATOM   742  C  CH2 . TRP   B 2 60  ? -20.661 -3.438  -5.244  1.00 41.52  ? 69  TRP   B CH2 1 
ATOM   743  N  N   . GLY   B 2 61  ? -21.924 0.299   -2.113  1.00 37.38  ? 70  GLY   B N   1 
ATOM   744  C  CA  . GLY   B 2 61  ? -20.638 0.613   -2.743  1.00 37.69  ? 70  GLY   B CA  1 
ATOM   745  C  C   . GLY   B 2 61  ? -19.494 -0.107  -2.061  1.00 37.33  ? 70  GLY   B C   1 
ATOM   746  O  O   . GLY   B 2 61  ? -19.634 -0.522  -0.912  1.00 37.40  ? 70  GLY   B O   1 
ATOM   747  N  N   . ASP   B 2 62  ? -18.357 -0.221  -2.733  1.00 37.30  ? 71  ASP   B N   1 
ATOM   748  C  CA  . ASP   B 2 62  ? -17.197 -0.925  -2.200  1.00 38.75  ? 71  ASP   B CA  1 
ATOM   749  C  C   . ASP   B 2 62  ? -15.952 -0.454  -2.938  1.00 38.27  ? 71  ASP   B C   1 
ATOM   750  O  O   . ASP   B 2 62  ? -15.835 -0.638  -4.139  1.00 38.27  ? 71  ASP   B O   1 
ATOM   751  C  CB  . ASP   B 2 62  ? -17.390 -2.443  -2.349  1.00 41.65  ? 71  ASP   B CB  1 
ATOM   752  C  CG  . ASP   B 2 62  ? -16.346 -3.260  -1.618  1.00 50.12  ? 71  ASP   B CG  1 
ATOM   753  O  OD1 . ASP   B 2 62  ? -15.168 -3.190  -1.992  1.00 51.84  ? 71  ASP   B OD1 1 
ATOM   754  O  OD2 . ASP   B 2 62  ? -16.707 -3.955  -0.671  1.00 55.17  ? 71  ASP   B OD2 1 
ATOM   755  N  N   . VAL   B 2 63  ? -15.037 0.209   -2.228  1.00 38.73  ? 72  VAL   B N   1 
ATOM   756  C  CA  . VAL   B 2 63  ? -13.797 0.759   -2.812  1.00 38.20  ? 72  VAL   B CA  1 
ATOM   757  C  C   . VAL   B 2 63  ? -12.921 -0.347  -3.431  1.00 39.02  ? 72  VAL   B C   1 
ATOM   758  O  O   . VAL   B 2 63  ? -12.285 -0.121  -4.472  1.00 40.02  ? 72  VAL   B O   1 
ATOM   759  C  CB  . VAL   B 2 63  ? -13.054 1.587   -1.713  1.00 38.59  ? 72  VAL   B CB  1 
ATOM   760  C  CG1 . VAL   B 2 63  ? -11.577 1.784   -2.030  1.00 40.05  ? 72  VAL   B CG1 1 
ATOM   761  C  CG2 . VAL   B 2 63  ? -13.733 2.932   -1.483  1.00 38.12  ? 72  VAL   B CG2 1 
ATOM   762  N  N   . LYS   B 2 64  ? -12.923 -1.557  -2.848  1.00 39.70  ? 73  LYS   B N   1 
ATOM   763  C  CA  . LYS   B 2 64  ? -12.047 -2.625  -3.389  1.00 40.46  ? 73  LYS   B CA  1 
ATOM   764  C  C   . LYS   B 2 64  ? -12.558 -3.147  -4.725  1.00 40.63  ? 73  LYS   B C   1 
ATOM   765  O  O   . LYS   B 2 64  ? -11.781 -3.288  -5.678  1.00 41.31  ? 73  LYS   B O   1 
ATOM   766  C  CB  . LYS   B 2 64  ? -11.786 -3.753  -2.360  1.00 40.05  ? 73  LYS   B CB  1 
ATOM   767  C  CG  . LYS   B 2 64  ? -10.661 -4.675  -2.868  1.00 43.95  ? 73  LYS   B CG  1 
ATOM   768  C  CD  . LYS   B 2 64  ? -10.257 -5.704  -1.830  1.00 46.32  ? 73  LYS   B CD  1 
ATOM   769  C  CE  . LYS   B 2 64  ? -9.350  -6.733  -2.465  1.00 49.56  ? 73  LYS   B CE  1 
ATOM   770  N  NZ  . LYS   B 2 64  ? -8.941  -7.753  -1.462  1.00 53.66  ? 73  LYS   B NZ  1 
ATOM   771  N  N   . GLN   B 2 65  ? -13.875 -3.350  -4.842  1.00 40.44  ? 74  GLN   B N   1 
ATOM   772  C  CA  . GLN   B 2 65  ? -14.449 -3.741  -6.136  1.00 40.10  ? 74  GLN   B CA  1 
ATOM   773  C  C   . GLN   B 2 65  ? -14.464 -2.529  -7.111  1.00 39.45  ? 74  GLN   B C   1 
ATOM   774  O  O   . GLN   B 2 65  ? -14.515 -2.739  -8.320  1.00 39.70  ? 74  GLN   B O   1 
ATOM   775  C  CB  . GLN   B 2 65  ? -15.877 -4.262  -5.960  1.00 42.20  ? 74  GLN   B CB  1 
ATOM   776  C  CG  . GLN   B 2 65  ? -15.969 -5.468  -5.030  1.00 46.71  ? 74  GLN   B CG  1 
ATOM   777  C  CD  . GLN   B 2 65  ? -17.378 -5.999  -5.016  1.00 53.64  ? 74  GLN   B CD  1 
ATOM   778  O  OE1 . GLN   B 2 65  ? -18.034 -6.120  -6.068  1.00 56.28  ? 74  GLN   B OE1 1 
ATOM   779  N  NE2 . GLN   B 2 65  ? -17.871 -6.337  -3.837  1.00 55.03  ? 74  GLN   B NE2 1 
ATOM   780  N  N   . ASP   B 2 66  ? -14.385 -1.283  -6.577  1.00 37.74  ? 75  ASP   B N   1 
ATOM   781  C  CA  . ASP   B 2 66  ? -14.444 -0.007  -7.305  1.00 37.30  ? 75  ASP   B CA  1 
ATOM   782  C  C   . ASP   B 2 66  ? -15.793 0.144   -7.992  1.00 37.17  ? 75  ASP   B C   1 
ATOM   783  O  O   . ASP   B 2 66  ? -15.856 0.667   -9.108  1.00 36.40  ? 75  ASP   B O   1 
ATOM   784  C  CB  . ASP   B 2 66  ? -13.273 0.187   -8.303  1.00 38.32  ? 75  ASP   B CB  1 
ATOM   785  C  CG  . ASP   B 2 66  ? -13.196 1.592   -8.892  1.00 42.98  ? 75  ASP   B CG  1 
ATOM   786  O  OD1 . ASP   B 2 66  ? -13.575 2.543   -8.204  1.00 43.84  ? 75  ASP   B OD1 1 
ATOM   787  O  OD2 . ASP   B 2 66  ? -12.747 1.730   -10.031 1.00 47.57  ? 75  ASP   B OD2 1 
ATOM   788  N  N   . LEU   B 2 67  ? -16.890 -0.261  -7.307  1.00 36.61  ? 76  LEU   B N   1 
ATOM   789  C  CA  . LEU   B 2 67  ? -18.252 -0.141  -7.849  1.00 36.69  ? 76  LEU   B CA  1 
ATOM   790  C  C   . LEU   B 2 67  ? -19.184 0.578   -6.870  1.00 36.95  ? 76  LEU   B C   1 
ATOM   791  O  O   . LEU   B 2 67  ? -18.931 0.566   -5.662  1.00 37.13  ? 76  LEU   B O   1 
ATOM   792  C  CB  . LEU   B 2 67  ? -18.818 -1.539  -8.112  1.00 37.08  ? 76  LEU   B CB  1 
ATOM   793  C  CG  . LEU   B 2 67  ? -18.114 -2.298  -9.218  1.00 38.17  ? 76  LEU   B CG  1 
ATOM   794  C  CD1 . LEU   B 2 67  ? -18.590 -3.743  -9.248  1.00 39.47  ? 76  LEU   B CD1 1 
ATOM   795  C  CD2 . LEU   B 2 67  ? -18.309 -1.591  -10.573 1.00 38.00  ? 76  LEU   B CD2 1 
ATOM   796  N  N   . VAL   B 2 68  ? -20.295 1.145   -7.381  1.00 35.74  ? 77  VAL   B N   1 
ATOM   797  C  CA  . VAL   B 2 68  ? -21.318 1.802   -6.552  1.00 35.37  ? 77  VAL   B CA  1 
ATOM   798  C  C   . VAL   B 2 68  ? -22.673 1.752   -7.310  1.00 35.19  ? 77  VAL   B C   1 
ATOM   799  O  O   . VAL   B 2 68  ? -22.674 1.879   -8.535  1.00 35.10  ? 77  VAL   B O   1 
ATOM   800  C  CB  . VAL   B 2 68  ? -20.903 3.261   -6.189  1.00 36.04  ? 77  VAL   B CB  1 
ATOM   801  C  CG1 . VAL   B 2 68  ? -20.568 4.064   -7.439  1.00 37.11  ? 77  VAL   B CG1 1 
ATOM   802  C  CG2 . VAL   B 2 68  ? -21.981 3.983   -5.353  1.00 36.62  ? 77  VAL   B CG2 1 
ATOM   803  N  N   . SER   B 2 69  ? -23.803 1.595   -6.588  1.00 34.62  ? 78  SER   B N   1 
ATOM   804  C  CA  . SER   B 2 69  ? -25.165 1.617   -7.155  1.00 34.96  ? 78  SER   B CA  1 
ATOM   805  C  C   . SER   B 2 69  ? -25.977 2.707   -6.440  1.00 35.08  ? 78  SER   B C   1 
ATOM   806  O  O   . SER   B 2 69  ? -25.738 3.023   -5.264  1.00 35.19  ? 78  SER   B O   1 
ATOM   807  C  CB  . SER   B 2 69  ? -25.867 0.260   -7.029  1.00 36.24  ? 78  SER   B CB  1 
ATOM   808  O  OG  . SER   B 2 69  ? -26.197 -0.062  -5.684  1.00 39.70  ? 78  SER   B OG  1 
ATOM   809  N  N   . TYR   B 2 70  ? -26.933 3.286   -7.151  1.00 35.20  ? 79  TYR   B N   1 
ATOM   810  C  CA  . TYR   B 2 70  ? -27.763 4.370   -6.651  1.00 36.47  ? 79  TYR   B CA  1 
ATOM   811  C  C   . TYR   B 2 70  ? -29.228 3.943   -6.789  1.00 37.97  ? 79  TYR   B C   1 
ATOM   812  O  O   . TYR   B 2 70  ? -29.577 3.304   -7.794  1.00 38.06  ? 79  TYR   B O   1 
ATOM   813  C  CB  . TYR   B 2 70  ? -27.515 5.609   -7.544  1.00 36.58  ? 79  TYR   B CB  1 
ATOM   814  C  CG  . TYR   B 2 70  ? -26.185 6.278   -7.271  1.00 37.03  ? 79  TYR   B CG  1 
ATOM   815  C  CD1 . TYR   B 2 70  ? -25.025 5.833   -7.881  1.00 37.33  ? 79  TYR   B CD1 1 
ATOM   816  C  CD2 . TYR   B 2 70  ? -26.096 7.374   -6.420  1.00 38.46  ? 79  TYR   B CD2 1 
ATOM   817  C  CE1 . TYR   B 2 70  ? -23.793 6.416   -7.607  1.00 38.09  ? 79  TYR   B CE1 1 
ATOM   818  C  CE2 . TYR   B 2 70  ? -24.874 7.979   -6.148  1.00 38.98  ? 79  TYR   B CE2 1 
ATOM   819  C  CZ  . TYR   B 2 70  ? -23.726 7.507   -6.761  1.00 39.24  ? 79  TYR   B CZ  1 
ATOM   820  O  OH  . TYR   B 2 70  ? -22.510 8.090   -6.495  1.00 39.64  ? 79  TYR   B OH  1 
ATOM   821  N  N   . CYS   B 2 71  ? -30.073 4.277   -5.789  1.00 38.43  ? 80  CYS   B N   1 
ATOM   822  C  CA  . CYS   B 2 71  ? -31.514 3.998   -5.750  1.00 40.66  ? 80  CYS   B CA  1 
ATOM   823  C  C   . CYS   B 2 71  ? -31.881 2.551   -5.447  1.00 41.69  ? 80  CYS   B C   1 
ATOM   824  O  O   . CYS   B 2 71  ? -33.069 2.279   -5.202  1.00 43.25  ? 80  CYS   B O   1 
ATOM   825  C  CB  . CYS   B 2 71  ? -32.223 4.475   -7.010  1.00 43.57  ? 80  CYS   B CB  1 
ATOM   826  S  SG  . CYS   B 2 71  ? -31.811 6.175   -7.502  1.00 51.90  ? 80  CYS   B SG  1 
ATOM   827  N  N   . GLY   B 2 72  ? -30.912 1.635   -5.466  1.00 39.88  ? 81  GLY   B N   1 
ATOM   828  C  CA  . GLY   B 2 72  ? -31.215 0.244   -5.162  1.00 39.41  ? 81  GLY   B CA  1 
ATOM   829  C  C   . GLY   B 2 72  ? -29.998 -0.634  -5.271  1.00 39.85  ? 81  GLY   B C   1 
ATOM   830  O  O   . GLY   B 2 72  ? -28.892 -0.156  -5.543  1.00 39.12  ? 81  GLY   B O   1 
ATOM   831  N  N   . PRO   B 2 73  ? -30.176 -1.933  -5.000  1.00 40.05  ? 82  PRO   B N   1 
ATOM   832  C  CA  . PRO   B 2 73  ? -29.028 -2.837  -5.048  1.00 40.91  ? 82  PRO   B CA  1 
ATOM   833  C  C   . PRO   B 2 73  ? -28.525 -3.115  -6.464  1.00 41.15  ? 82  PRO   B C   1 
ATOM   834  O  O   . PRO   B 2 73  ? -29.284 -2.978  -7.430  1.00 41.58  ? 82  PRO   B O   1 
ATOM   835  C  CB  . PRO   B 2 73  ? -29.544 -4.104  -4.343  1.00 41.90  ? 82  PRO   B CB  1 
ATOM   836  C  CG  . PRO   B 2 73  ? -31.016 -4.093  -4.638  1.00 42.18  ? 82  PRO   B CG  1 
ATOM   837  C  CD  . PRO   B 2 73  ? -31.416 -2.630  -4.619  1.00 39.98  ? 82  PRO   B CD  1 
ATOM   838  N  N   . TRP   B 2 74  ? -27.258 -3.534  -6.583  1.00 40.62  ? 83  TRP   B N   1 
ATOM   839  C  CA  . TRP   B 2 74  ? -26.605 -3.854  -7.857  1.00 41.28  ? 83  TRP   B CA  1 
ATOM   840  C  C   . TRP   B 2 74  ? -27.430 -4.891  -8.636  1.00 42.38  ? 83  TRP   B C   1 
ATOM   841  O  O   . TRP   B 2 74  ? -27.707 -5.972  -8.111  1.00 42.39  ? 83  TRP   B O   1 
ATOM   842  C  CB  . TRP   B 2 74  ? -25.180 -4.391  -7.604  1.00 40.82  ? 83  TRP   B CB  1 
ATOM   843  C  CG  . TRP   B 2 74  ? -24.383 -4.609  -8.857  1.00 40.51  ? 83  TRP   B CG  1 
ATOM   844  C  CD1 . TRP   B 2 74  ? -24.319 -5.750  -9.605  1.00 40.75  ? 83  TRP   B CD1 1 
ATOM   845  C  CD2 . TRP   B 2 74  ? -23.561 -3.636  -9.533  1.00 40.29  ? 83  TRP   B CD2 1 
ATOM   846  N  NE1 . TRP   B 2 74  ? -23.492 -5.558  -10.690 1.00 40.92  ? 83  TRP   B NE1 1 
ATOM   847  C  CE2 . TRP   B 2 74  ? -23.019 -4.266  -10.674 1.00 40.55  ? 83  TRP   B CE2 1 
ATOM   848  C  CE3 . TRP   B 2 74  ? -23.192 -2.310  -9.254  1.00 40.39  ? 83  TRP   B CE3 1 
ATOM   849  C  CZ2 . TRP   B 2 74  ? -22.160 -3.605  -11.558 1.00 40.85  ? 83  TRP   B CZ2 1 
ATOM   850  C  CZ3 . TRP   B 2 74  ? -22.370 -1.642  -10.147 1.00 40.67  ? 83  TRP   B CZ3 1 
ATOM   851  C  CH2 . TRP   B 2 74  ? -21.860 -2.287  -11.283 1.00 41.14  ? 83  TRP   B CH2 1 
ATOM   852  N  N   . LYS   B 2 75  ? -27.800 -4.561  -9.886  1.00 42.39  ? 84  LYS   B N   1 
ATOM   853  C  CA  . LYS   B 2 75  ? -28.678 -5.402  -10.713 1.00 43.71  ? 84  LYS   B CA  1 
ATOM   854  C  C   . LYS   B 2 75  ? -27.994 -6.194  -11.819 1.00 46.25  ? 84  LYS   B C   1 
ATOM   855  O  O   . LYS   B 2 75  ? -28.626 -7.078  -12.389 1.00 47.98  ? 84  LYS   B O   1 
ATOM   856  C  CB  . LYS   B 2 75  ? -29.756 -4.530  -11.382 1.00 43.73  ? 84  LYS   B CB  1 
ATOM   857  C  CG  . LYS   B 2 75  ? -30.581 -3.644  -10.443 1.00 45.66  ? 84  LYS   B CG  1 
ATOM   858  C  CD  . LYS   B 2 75  ? -31.556 -4.482  -9.613  1.00 50.35  ? 84  LYS   B CD  1 
ATOM   859  C  CE  . LYS   B 2 75  ? -32.638 -3.641  -8.999  1.00 54.79  ? 84  LYS   B CE  1 
ATOM   860  N  NZ  . LYS   B 2 75  ? -33.609 -4.462  -8.249  1.00 59.56  ? 84  LYS   B NZ  1 
ATOM   861  N  N   . LEU   B 2 76  ? -26.764 -5.843  -12.191 1.00 46.28  ? 85  LEU   B N   1 
ATOM   862  C  CA  . LEU   B 2 76  ? -26.105 -6.448  -13.342 1.00 46.90  ? 85  LEU   B CA  1 
ATOM   863  C  C   . LEU   B 2 76  ? -25.415 -7.741  -12.937 1.00 48.41  ? 85  LEU   B C   1 
ATOM   864  O  O   . LEU   B 2 76  ? -24.497 -7.696  -12.124 1.00 47.38  ? 85  LEU   B O   1 
ATOM   865  C  CB  . LEU   B 2 76  ? -25.106 -5.461  -13.969 1.00 46.57  ? 85  LEU   B CB  1 
ATOM   866  C  CG  . LEU   B 2 76  ? -25.583 -3.990  -14.134 1.00 47.01  ? 85  LEU   B CG  1 
ATOM   867  C  CD1 . LEU   B 2 76  ? -24.507 -3.128  -14.744 1.00 47.37  ? 85  LEU   B CD1 1 
ATOM   868  C  CD2 . LEU   B 2 76  ? -26.837 -3.900  -14.975 1.00 47.48  ? 85  LEU   B CD2 1 
ATOM   869  N  N   . ASP   B 2 77  ? -25.861 -8.888  -13.481 1.00 50.47  ? 86  ASP   B N   1 
ATOM   870  C  CA  . ASP   B 2 77  ? -25.249 -10.158 -13.087 1.00 53.75  ? 86  ASP   B CA  1 
ATOM   871  C  C   . ASP   B 2 77  ? -24.781 -11.041 -14.237 1.00 55.15  ? 86  ASP   B C   1 
ATOM   872  O  O   . ASP   B 2 77  ? -24.413 -12.184 -13.979 1.00 56.46  ? 86  ASP   B O   1 
ATOM   873  C  CB  . ASP   B 2 77  ? -26.156 -10.954 -12.142 1.00 58.08  ? 86  ASP   B CB  1 
ATOM   874  C  CG  . ASP   B 2 77  ? -27.531 -11.281 -12.689 1.00 67.52  ? 86  ASP   B CG  1 
ATOM   875  O  OD1 . ASP   B 2 77  ? -27.901 -10.727 -13.746 1.00 69.82  ? 86  ASP   B OD1 1 
ATOM   876  O  OD2 . ASP   B 2 77  ? -28.238 -12.095 -12.060 1.00 71.59  ? 86  ASP   B OD2 1 
ATOM   877  N  N   . ALA   B 2 78  ? -24.712 -10.519 -15.466 1.00 54.34  ? 87  ALA   B N   1 
ATOM   878  C  CA  . ALA   B 2 78  ? -24.195 -11.301 -16.583 1.00 54.40  ? 87  ALA   B CA  1 
ATOM   879  C  C   . ALA   B 2 78  ? -22.666 -11.410 -16.473 1.00 54.65  ? 87  ALA   B C   1 
ATOM   880  O  O   . ALA   B 2 78  ? -22.009 -10.526 -15.921 1.00 53.28  ? 87  ALA   B O   1 
ATOM   881  C  CB  . ALA   B 2 78  ? -24.588 -10.671 -17.911 1.00 54.00  ? 87  ALA   B CB  1 
ATOM   882  N  N   . ALA   B 2 79  ? -22.104 -12.500 -17.000 1.00 55.52  ? 88  ALA   B N   1 
ATOM   883  C  CA  . ALA   B 2 79  ? -20.664 -12.722 -16.958 1.00 56.62  ? 88  ALA   B CA  1 
ATOM   884  C  C   . ALA   B 2 79  ? -20.118 -13.082 -18.340 1.00 57.18  ? 88  ALA   B C   1 
ATOM   885  O  O   . ALA   B 2 79  ? -20.825 -13.701 -19.137 1.00 56.86  ? 88  ALA   B O   1 
ATOM   886  C  CB  . ALA   B 2 79  ? -20.351 -13.848 -15.983 1.00 57.17  ? 88  ALA   B CB  1 
ATOM   887  N  N   . TRP   B 2 80  ? -18.856 -12.702 -18.630 1.00 57.98  ? 89  TRP   B N   1 
ATOM   888  C  CA  . TRP   B 2 80  ? -18.168 -13.061 -19.882 1.00 59.64  ? 89  TRP   B CA  1 
ATOM   889  C  C   . TRP   B 2 80  ? -18.043 -14.595 -19.907 1.00 61.46  ? 89  TRP   B C   1 
ATOM   890  O  O   . TRP   B 2 80  ? -17.766 -15.167 -18.871 1.00 60.43  ? 89  TRP   B O   1 
ATOM   891  C  CB  . TRP   B 2 80  ? -16.756 -12.439 -19.909 1.00 59.52  ? 89  TRP   B CB  1 
ATOM   892  C  CG  . TRP   B 2 80  ? -15.977 -12.777 -21.148 1.00 60.08  ? 89  TRP   B CG  1 
ATOM   893  C  CD1 . TRP   B 2 80  ? -16.432 -12.759 -22.435 1.00 60.99  ? 89  TRP   B CD1 1 
ATOM   894  C  CD2 . TRP   B 2 80  ? -14.615 -13.233 -21.210 1.00 59.94  ? 89  TRP   B CD2 1 
ATOM   895  N  NE1 . TRP   B 2 80  ? -15.449 -13.206 -23.290 1.00 61.34  ? 89  TRP   B NE1 1 
ATOM   896  C  CE2 . TRP   B 2 80  ? -14.312 -13.467 -22.568 1.00 60.82  ? 89  TRP   B CE2 1 
ATOM   897  C  CE3 . TRP   B 2 80  ? -13.619 -13.443 -20.254 1.00 60.36  ? 89  TRP   B CE3 1 
ATOM   898  C  CZ2 . TRP   B 2 80  ? -13.055 -13.894 -22.990 1.00 61.53  ? 89  TRP   B CZ2 1 
ATOM   899  C  CZ3 . TRP   B 2 80  ? -12.378 -13.894 -20.675 1.00 61.15  ? 89  TRP   B CZ3 1 
ATOM   900  C  CH2 . TRP   B 2 80  ? -12.105 -14.106 -22.028 1.00 61.11  ? 89  TRP   B CH2 1 
ATOM   901  N  N   . ASP   B 2 81  ? -18.321 -15.263 -21.050 1.00 63.85  ? 90  ASP   B N   1 
ATOM   902  C  CA  . ASP   B 2 81  ? -18.263 -16.737 -21.083 1.00 66.01  ? 90  ASP   B CA  1 
ATOM   903  C  C   . ASP   B 2 81  ? -16.837 -17.321 -21.128 1.00 68.79  ? 90  ASP   B C   1 
ATOM   904  O  O   . ASP   B 2 81  ? -16.676 -18.537 -20.990 1.00 69.71  ? 90  ASP   B O   1 
ATOM   905  C  CB  . ASP   B 2 81  ? -19.119 -17.299 -22.234 1.00 67.11  ? 90  ASP   B CB  1 
ATOM   906  C  CG  . ASP   B 2 81  ? -18.709 -16.843 -23.615 1.00 71.64  ? 90  ASP   B CG  1 
ATOM   907  O  OD1 . ASP   B 2 81  ? -17.633 -16.216 -23.743 1.00 71.10  ? 90  ASP   B OD1 1 
ATOM   908  O  OD2 . ASP   B 2 81  ? -19.468 -17.108 -24.580 1.00 76.09  ? 90  ASP   B OD2 1 
ATOM   909  N  N   . GLY   B 2 82  ? -15.833 -16.474 -21.348 1.00 70.10  ? 91  GLY   B N   1 
ATOM   910  C  CA  . GLY   B 2 82  ? -14.440 -16.906 -21.427 1.00 72.08  ? 91  GLY   B CA  1 
ATOM   911  C  C   . GLY   B 2 82  ? -13.978 -17.300 -22.823 1.00 74.22  ? 91  GLY   B C   1 
ATOM   912  O  O   . GLY   B 2 82  ? -12.819 -17.691 -23.006 1.00 75.18  ? 91  GLY   B O   1 
ATOM   913  N  N   . LEU   B 2 83  ? -14.870 -17.222 -23.819 1.00 74.50  ? 92  LEU   B N   1 
ATOM   914  C  CA  . LEU   B 2 83  ? -14.531 -17.609 -25.188 1.00 75.51  ? 92  LEU   B CA  1 
ATOM   915  C  C   . LEU   B 2 83  ? -14.799 -16.532 -26.220 1.00 74.54  ? 92  LEU   B C   1 
ATOM   916  O  O   . LEU   B 2 83  ? -14.026 -16.387 -27.161 1.00 74.94  ? 92  LEU   B O   1 
ATOM   917  C  CB  . LEU   B 2 83  ? -15.370 -18.821 -25.630 1.00 77.00  ? 92  LEU   B CB  1 
ATOM   918  C  CG  . LEU   B 2 83  ? -15.256 -20.114 -24.884 1.00 80.09  ? 92  LEU   B CG  1 
ATOM   919  C  CD1 . LEU   B 2 83  ? -16.171 -21.138 -25.531 1.00 81.18  ? 92  LEU   B CD1 1 
ATOM   920  C  CD2 . LEU   B 2 83  ? -13.837 -20.619 -24.898 1.00 81.17  ? 92  LEU   B CD2 1 
ATOM   921  N  N   . SER   B 2 84  ? -15.962 -15.879 -26.126 1.00 73.09  ? 93  SER   B N   1 
ATOM   922  C  CA  . SER   B 2 84  ? -16.497 -14.979 -27.132 1.00 72.12  ? 93  SER   B CA  1 
ATOM   923  C  C   . SER   B 2 84  ? -15.999 -13.541 -27.109 1.00 70.27  ? 93  SER   B C   1 
ATOM   924  O  O   . SER   B 2 84  ? -15.513 -13.052 -26.088 1.00 70.44  ? 93  SER   B O   1 
ATOM   925  C  CB  . SER   B 2 84  ? -18.023 -14.969 -27.043 1.00 73.87  ? 93  SER   B CB  1 
ATOM   926  O  OG  . SER   B 2 84  ? -18.551 -16.265 -26.821 1.00 76.30  ? 93  SER   B OG  1 
ATOM   927  N  N   . GLU   B 2 85  ? -16.155 -12.858 -28.247 1.00 68.15  ? 94  GLU   B N   1 
ATOM   928  C  CA  . GLU   B 2 85  ? -15.826 -11.452 -28.359 1.00 66.77  ? 94  GLU   B CA  1 
ATOM   929  C  C   . GLU   B 2 85  ? -16.952 -10.658 -27.667 1.00 64.35  ? 94  GLU   B C   1 
ATOM   930  O  O   . GLU   B 2 85  ? -18.066 -11.153 -27.468 1.00 64.24  ? 94  GLU   B O   1 
ATOM   931  C  CB  . GLU   B 2 85  ? -15.650 -11.016 -29.834 1.00 69.41  ? 94  GLU   B CB  1 
ATOM   932  C  CG  . GLU   B 2 85  ? -14.315 -11.463 -30.426 1.00 76.15  ? 94  GLU   B CG  1 
ATOM   933  C  CD  . GLU   B 2 85  ? -13.951 -10.894 -31.788 1.00 82.64  ? 94  GLU   B CD  1 
ATOM   934  O  OE1 . GLU   B 2 85  ? -14.812 -10.240 -32.416 1.00 82.29  ? 94  GLU   B OE1 1 
ATOM   935  O  OE2 . GLU   B 2 85  ? -12.795 -11.096 -32.224 1.00 85.46  ? 94  GLU   B OE2 1 
ATOM   936  N  N   . VAL   B 2 86  ? -16.624 -9.453  -27.238 1.00 61.80  ? 95  VAL   B N   1 
ATOM   937  C  CA  . VAL   B 2 86  ? -17.540 -8.567  -26.519 1.00 58.52  ? 95  VAL   B CA  1 
ATOM   938  C  C   . VAL   B 2 86  ? -17.459 -7.192  -27.164 1.00 57.51  ? 95  VAL   B C   1 
ATOM   939  O  O   . VAL   B 2 86  ? -16.554 -6.950  -27.964 1.00 58.73  ? 95  VAL   B O   1 
ATOM   940  C  CB  . VAL   B 2 86  ? -17.128 -8.471  -25.010 1.00 56.85  ? 95  VAL   B CB  1 
ATOM   941  C  CG1 . VAL   B 2 86  ? -17.021 -9.846  -24.363 1.00 56.53  ? 95  VAL   B CG1 1 
ATOM   942  C  CG2 . VAL   B 2 86  ? -15.827 -7.683  -24.839 1.00 56.25  ? 95  VAL   B CG2 1 
ATOM   943  N  N   . GLN   B 2 87  ? -18.350 -6.263  -26.773 1.00 54.82  ? 96  GLN   B N   1 
ATOM   944  C  CA  . GLN   B 2 87  ? -18.265 -4.907  -27.242 1.00 54.35  ? 96  GLN   B CA  1 
ATOM   945  C  C   . GLN   B 2 87  ? -18.168 -3.932  -26.063 1.00 53.78  ? 96  GLN   B C   1 
ATOM   946  O  O   . GLN   B 2 87  ? -18.916 -4.058  -25.109 1.00 53.50  ? 96  GLN   B O   1 
ATOM   947  C  CB  . GLN   B 2 87  ? -19.482 -4.563  -28.129 1.00 55.95  ? 96  GLN   B CB  1 
ATOM   948  C  CG  . GLN   B 2 87  ? -19.288 -5.112  -29.531 1.00 59.13  ? 96  GLN   B CG  1 
ATOM   949  C  CD  . GLN   B 2 87  ? -20.390 -4.759  -30.489 1.00 62.41  ? 96  GLN   B CD  1 
ATOM   950  O  OE1 . GLN   B 2 87  ? -21.251 -3.916  -30.229 1.00 61.08  ? 96  GLN   B OE1 1 
ATOM   951  N  NE2 . GLN   B 2 87  ? -20.372 -5.426  -31.638 1.00 65.04  ? 96  GLN   B NE2 1 
ATOM   952  N  N   . LEU   B 2 88  ? -17.253 -2.972  -26.144 1.00 53.11  ? 97  LEU   B N   1 
ATOM   953  C  CA  . LEU   B 2 88  ? -17.160 -1.896  -25.191 1.00 53.16  ? 97  LEU   B CA  1 
ATOM   954  C  C   . LEU   B 2 88  ? -18.031 -0.802  -25.784 1.00 53.50  ? 97  LEU   B C   1 
ATOM   955  O  O   . LEU   B 2 88  ? -17.747 -0.317  -26.891 1.00 54.56  ? 97  LEU   B O   1 
ATOM   956  C  CB  . LEU   B 2 88  ? -15.710 -1.389  -25.045 1.00 53.26  ? 97  LEU   B CB  1 
ATOM   957  C  CG  . LEU   B 2 88  ? -15.547 -0.017  -24.358 1.00 54.41  ? 97  LEU   B CG  1 
ATOM   958  C  CD1 . LEU   B 2 88  ? -16.066 -0.063  -22.903 1.00 54.00  ? 97  LEU   B CD1 1 
ATOM   959  C  CD2 . LEU   B 2 88  ? -14.112 0.455   -24.406 1.00 55.29  ? 97  LEU   B CD2 1 
ATOM   960  N  N   . LEU   B 2 89  ? -19.085 -0.405  -25.075 1.00 51.93  ? 98  LEU   B N   1 
ATOM   961  C  CA  . LEU   B 2 89  ? -19.928 0.680   -25.530 1.00 51.95  ? 98  LEU   B CA  1 
ATOM   962  C  C   . LEU   B 2 89  ? -19.281 1.932   -24.943 1.00 52.26  ? 98  LEU   B C   1 
ATOM   963  O  O   . LEU   B 2 89  ? -19.673 2.419   -23.878 1.00 51.42  ? 98  LEU   B O   1 
ATOM   964  C  CB  . LEU   B 2 89  ? -21.382 0.462   -25.067 1.00 52.48  ? 98  LEU   B CB  1 
ATOM   965  C  CG  . LEU   B 2 89  ? -22.406 1.609   -25.258 1.00 54.96  ? 98  LEU   B CG  1 
ATOM   966  C  CD1 . LEU   B 2 89  ? -22.319 2.240   -26.605 1.00 56.73  ? 98  LEU   B CD1 1 
ATOM   967  C  CD2 . LEU   B 2 89  ? -23.820 1.126   -25.015 1.00 56.02  ? 98  LEU   B CD2 1 
ATOM   968  N  N   . ALA   B 2 90  ? -18.223 2.412   -25.618 1.00 52.15  ? 99  ALA   B N   1 
ATOM   969  C  CA  . ALA   B 2 90  ? -17.437 3.554   -25.157 1.00 51.93  ? 99  ALA   B CA  1 
ATOM   970  C  C   . ALA   B 2 90  ? -18.162 4.857   -25.267 1.00 51.26  ? 99  ALA   B C   1 
ATOM   971  O  O   . ALA   B 2 90  ? -18.612 5.192   -26.357 1.00 52.23  ? 99  ALA   B O   1 
ATOM   972  C  CB  . ALA   B 2 90  ? -16.133 3.640   -25.930 1.00 52.05  ? 99  ALA   B CB  1 
ATOM   973  N  N   . VAL   B 2 91  ? -18.243 5.627   -24.160 1.00 49.66  ? 100 VAL   B N   1 
ATOM   974  C  CA  . VAL   B 2 91  ? -18.868 6.957   -24.163 1.00 48.82  ? 100 VAL   B CA  1 
ATOM   975  C  C   . VAL   B 2 91  ? -17.762 7.975   -23.783 1.00 49.44  ? 100 VAL   B C   1 
ATOM   976  O  O   . VAL   B 2 91  ? -17.649 8.339   -22.617 1.00 49.03  ? 100 VAL   B O   1 
ATOM   977  C  CB  . VAL   B 2 91  ? -20.107 7.021   -23.226 1.00 48.74  ? 100 VAL   B CB  1 
ATOM   978  C  CG1 . VAL   B 2 91  ? -20.799 8.392   -23.290 1.00 48.91  ? 100 VAL   B CG1 1 
ATOM   979  C  CG2 . VAL   B 2 91  ? -21.097 5.910   -23.568 1.00 48.88  ? 100 VAL   B CG2 1 
ATOM   980  N  N   . PRO   B 2 92  ? -16.876 8.381   -24.740 1.00 49.91  ? 101 PRO   B N   1 
ATOM   981  C  CA  . PRO   B 2 92  ? -15.774 9.298   -24.386 1.00 49.72  ? 101 PRO   B CA  1 
ATOM   982  C  C   . PRO   B 2 92  ? -16.246 10.727  -24.174 1.00 50.73  ? 101 PRO   B C   1 
ATOM   983  O  O   . PRO   B 2 92  ? -17.269 11.125  -24.728 1.00 51.41  ? 101 PRO   B O   1 
ATOM   984  C  CB  . PRO   B 2 92  ? -14.800 9.181   -25.583 1.00 50.94  ? 101 PRO   B CB  1 
ATOM   985  C  CG  . PRO   B 2 92  ? -15.377 8.104   -26.507 1.00 51.37  ? 101 PRO   B CG  1 
ATOM   986  C  CD  . PRO   B 2 92  ? -16.845 8.033   -26.175 1.00 49.46  ? 101 PRO   B CD  1 
ATOM   987  N  N   . PRO   B 2 93  ? -15.491 11.541  -23.418 1.00 51.03  ? 102 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 93  ? -15.948 12.917  -23.150 1.00 51.87  ? 102 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 93  ? -16.109 13.729  -24.431 1.00 53.44  ? 102 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 93  ? -15.305 13.603  -25.344 1.00 53.30  ? 102 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 93  ? -14.858 13.478  -22.227 1.00 52.10  ? 102 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 93  ? -14.273 12.244  -21.550 1.00 52.14  ? 102 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 93  ? -14.265 11.218  -22.660 1.00 50.61  ? 102 PRO   B CD  1 
ATOM   994  N  N   . GLY   B 2 94  ? -17.208 14.455  -24.525 1.00 53.63  ? 103 GLY   B N   1 
ATOM   995  C  CA  . GLY   B 2 94  ? -17.542 15.285  -25.676 1.00 54.61  ? 103 GLY   B CA  1 
ATOM   996  C  C   . GLY   B 2 94  ? -17.774 14.539  -26.975 1.00 55.22  ? 103 GLY   B C   1 
ATOM   997  O  O   . GLY   B 2 94  ? -17.916 15.167  -28.016 1.00 55.10  ? 103 GLY   B O   1 
ATOM   998  N  N   . GLU   B 2 95  ? -17.754 13.196  -26.949 1.00 55.88  ? 104 GLU   B N   1 
ATOM   999  C  CA  . GLU   B 2 95  ? -17.896 12.410  -28.179 1.00 56.85  ? 104 GLU   B CA  1 
ATOM   1000 C  C   . GLU   B 2 95  ? -19.070 11.442  -28.107 1.00 58.55  ? 104 GLU   B C   1 
ATOM   1001 O  O   . GLU   B 2 95  ? -19.450 11.006  -27.020 1.00 58.15  ? 104 GLU   B O   1 
ATOM   1002 C  CB  . GLU   B 2 95  ? -16.586 11.659  -28.506 1.00 57.34  ? 104 GLU   B CB  1 
ATOM   1003 C  CG  . GLU   B 2 95  ? -15.390 12.581  -28.696 1.00 58.28  ? 104 GLU   B CG  1 
ATOM   1004 C  CD  . GLU   B 2 95  ? -14.053 11.886  -28.892 1.00 62.95  ? 104 GLU   B CD  1 
ATOM   1005 O  OE1 . GLU   B 2 95  ? -13.979 10.665  -28.631 1.00 61.87  ? 104 GLU   B OE1 1 
ATOM   1006 O  OE2 . GLU   B 2 95  ? -13.080 12.559  -29.308 1.00 64.85  ? 104 GLU   B OE2 1 
ATOM   1007 N  N   . ARG   B 2 96  ? -19.638 11.098  -29.273 1.00 59.49  ? 105 ARG   B N   1 
ATOM   1008 C  CA  . ARG   B 2 96  ? -20.779 10.190  -29.377 1.00 61.27  ? 105 ARG   B CA  1 
ATOM   1009 C  C   . ARG   B 2 96  ? -20.478 8.797   -28.840 1.00 60.59  ? 105 ARG   B C   1 
ATOM   1010 O  O   . ARG   B 2 96  ? -19.336 8.354   -28.955 1.00 60.83  ? 105 ARG   B O   1 
ATOM   1011 C  CB  . ARG   B 2 96  ? -21.210 10.079  -30.851 1.00 65.36  ? 105 ARG   B CB  1 
ATOM   1012 C  CG  . ARG   B 2 96  ? -22.425 9.177   -31.084 1.00 72.30  ? 105 ARG   B CG  1 
ATOM   1013 C  CD  . ARG   B 2 96  ? -23.429 9.715   -32.093 1.00 78.46  ? 105 ARG   B CD  1 
ATOM   1014 N  NE  . ARG   B 2 96  ? -22.819 10.229  -33.321 1.00 84.08  ? 105 ARG   B NE  1 
ATOM   1015 C  CZ  . ARG   B 2 96  ? -22.382 9.476   -34.325 1.00 88.48  ? 105 ARG   B CZ  1 
ATOM   1016 N  NH1 . ARG   B 2 96  ? -22.463 8.151   -34.256 1.00 87.94  ? 105 ARG   B NH1 1 
ATOM   1017 N  NH2 . ARG   B 2 96  ? -21.852 10.041  -35.404 1.00 90.26  ? 105 ARG   B NH2 1 
ATOM   1018 N  N   . ALA   B 2 97  ? -21.498 8.087   -28.289 1.00 59.93  ? 106 ALA   B N   1 
ATOM   1019 C  CA  . ALA   B 2 97  ? -21.363 6.693   -27.836 1.00 60.55  ? 106 ALA   B CA  1 
ATOM   1020 C  C   . ALA   B 2 97  ? -20.972 5.832   -29.049 1.00 61.59  ? 106 ALA   B C   1 
ATOM   1021 O  O   . ALA   B 2 97  ? -21.540 6.013   -30.126 1.00 62.11  ? 106 ALA   B O   1 
ATOM   1022 C  CB  . ALA   B 2 97  ? -22.683 6.200   -27.283 1.00 60.53  ? 106 ALA   B CB  1 
ATOM   1023 N  N   . LYS   B 2 98  ? -20.021 4.924   -28.891 1.00 61.78  ? 107 LYS   B N   1 
ATOM   1024 C  CA  . LYS   B 2 98  ? -19.520 4.115   -30.002 1.00 63.28  ? 107 LYS   B CA  1 
ATOM   1025 C  C   . LYS   B 2 98  ? -19.210 2.693   -29.542 1.00 62.43  ? 107 LYS   B C   1 
ATOM   1026 O  O   . LYS   B 2 98  ? -18.484 2.547   -28.561 1.00 63.07  ? 107 LYS   B O   1 
ATOM   1027 C  CB  . LYS   B 2 98  ? -18.216 4.771   -30.474 1.00 67.22  ? 107 LYS   B CB  1 
ATOM   1028 C  CG  . LYS   B 2 98  ? -17.588 4.192   -31.729 1.00 75.00  ? 107 LYS   B CG  1 
ATOM   1029 C  CD  . LYS   B 2 98  ? -16.283 4.928   -32.075 1.00 81.72  ? 107 LYS   B CD  1 
ATOM   1030 C  CE  . LYS   B 2 98  ? -15.332 5.041   -30.892 1.00 85.88  ? 107 LYS   B CE  1 
ATOM   1031 N  NZ  . LYS   B 2 98  ? -13.906 4.984   -31.312 1.00 88.30  ? 107 LYS   B NZ  1 
ATOM   1032 N  N   . ASN   B 2 99  ? -19.747 1.648   -30.211 1.00 61.26  ? 108 ASN   B N   1 
ATOM   1033 C  CA  . ASN   B 2 99  ? -19.438 0.262   -29.808 1.00 61.90  ? 108 ASN   B CA  1 
ATOM   1034 C  C   . ASN   B 2 99  ? -18.150 -0.191  -30.474 1.00 62.89  ? 108 ASN   B C   1 
ATOM   1035 O  O   . ASN   B 2 99  ? -17.991 0.013   -31.680 1.00 63.41  ? 108 ASN   B O   1 
ATOM   1036 C  CB  . ASN   B 2 99  ? -20.530 -0.711  -30.255 1.00 63.00  ? 108 ASN   B CB  1 
ATOM   1037 C  CG  . ASN   B 2 99  ? -21.885 -0.477  -29.670 1.00 66.17  ? 108 ASN   B CG  1 
ATOM   1038 O  OD1 . ASN   B 2 99  ? -22.488 0.568   -29.875 1.00 66.91  ? 108 ASN   B OD1 1 
ATOM   1039 N  ND2 . ASN   B 2 99  ? -22.412 -1.467  -28.956 1.00 66.26  ? 108 ASN   B ND2 1 
ATOM   1040 N  N   . ILE   B 2 100 ? -17.268 -0.869  -29.734 1.00 62.70  ? 109 ILE   B N   1 
ATOM   1041 C  CA  . ILE   B 2 100 ? -16.007 -1.382  -30.250 1.00 63.13  ? 109 ILE   B CA  1 
ATOM   1042 C  C   . ILE   B 2 100 ? -15.931 -2.852  -29.884 1.00 63.26  ? 109 ILE   B C   1 
ATOM   1043 O  O   . ILE   B 2 100 ? -15.960 -3.181  -28.704 1.00 63.62  ? 109 ILE   B O   1 
ATOM   1044 C  CB  . ILE   B 2 100 ? -14.819 -0.646  -29.604 1.00 64.19  ? 109 ILE   B CB  1 
ATOM   1045 C  CG1 . ILE   B 2 100 ? -14.953 0.875   -29.716 1.00 65.41  ? 109 ILE   B CG1 1 
ATOM   1046 C  CG2 . ILE   B 2 100 ? -13.484 -1.160  -30.150 1.00 65.17  ? 109 ILE   B CG2 1 
ATOM   1047 C  CD1 . ILE   B 2 100 ? -14.926 1.387   -31.092 1.00 66.62  ? 109 ILE   B CD1 1 
ATOM   1048 N  N   . GLN   B 2 101 ? -15.781 -3.736  -30.864 1.00 62.97  ? 110 GLN   B N   1 
ATOM   1049 C  CA  . GLN   B 2 101 ? -15.716 -5.172  -30.617 1.00 63.41  ? 110 GLN   B CA  1 
ATOM   1050 C  C   . GLN   B 2 101 ? -14.283 -5.621  -30.373 1.00 63.99  ? 110 GLN   B C   1 
ATOM   1051 O  O   . GLN   B 2 101 ? -13.387 -5.150  -31.072 1.00 64.90  ? 110 GLN   B O   1 
ATOM   1052 C  CB  . GLN   B 2 101 ? -16.309 -5.918  -31.820 1.00 65.49  ? 110 GLN   B CB  1 
ATOM   1053 C  CG  . GLN   B 2 101 ? -16.401 -7.423  -31.628 1.00 68.64  ? 110 GLN   B CG  1 
ATOM   1054 C  CD  . GLN   B 2 101 ? -17.486 -8.013  -32.491 1.00 71.70  ? 110 GLN   B CD  1 
ATOM   1055 O  OE1 . GLN   B 2 101 ? -18.514 -7.379  -32.773 1.00 70.73  ? 110 GLN   B OE1 1 
ATOM   1056 N  NE2 . GLN   B 2 101 ? -17.264 -9.249  -32.925 1.00 72.80  ? 110 GLN   B NE2 1 
ATOM   1057 N  N   . THR   B 2 102 ? -14.058 -6.539  -29.391 1.00 63.31  ? 111 THR   B N   1 
ATOM   1058 C  CA  . THR   B 2 102 ? -12.735 -7.021  -29.036 1.00 63.20  ? 111 THR   B CA  1 
ATOM   1059 C  C   . THR   B 2 102 ? -12.771 -8.406  -28.381 1.00 62.92  ? 111 THR   B C   1 
ATOM   1060 O  O   . THR   B 2 102 ? -13.797 -8.786  -27.822 1.00 63.88  ? 111 THR   B O   1 
ATOM   1061 C  CB  . THR   B 2 102 ? -12.012 -5.986  -28.134 1.00 65.10  ? 111 THR   B CB  1 
ATOM   1062 O  OG1 . THR   B 2 102 ? -10.621 -6.331  -28.065 1.00 67.09  ? 111 THR   B OG1 1 
ATOM   1063 C  CG2 . THR   B 2 102 ? -12.617 -5.870  -26.725 1.00 65.72  ? 111 THR   B CG2 1 
ATOM   1064 N  N   . LEU   B 2 103 ? -11.666 -9.166  -28.441 1.00 61.74  ? 112 LEU   B N   1 
ATOM   1065 C  CA  . LEU   B 2 103 ? -11.602 -10.435 -27.724 1.00 61.50  ? 112 LEU   B CA  1 
ATOM   1066 C  C   . LEU   B 2 103 ? -10.862 -10.119 -26.446 1.00 61.87  ? 112 LEU   B C   1 
ATOM   1067 O  O   . LEU   B 2 103 ? -9.687  -9.730  -26.481 1.00 61.98  ? 112 LEU   B O   1 
ATOM   1068 C  CB  . LEU   B 2 103 ? -10.874 -11.588 -28.466 1.00 62.02  ? 112 LEU   B CB  1 
ATOM   1069 C  CG  . LEU   B 2 103 ? -10.801 -12.870 -27.611 1.00 64.13  ? 112 LEU   B CG  1 
ATOM   1070 C  CD1 . LEU   B 2 103 ? -12.112 -13.595 -27.585 1.00 64.75  ? 112 LEU   B CD1 1 
ATOM   1071 C  CD2 . LEU   B 2 103 ? -9.705  -13.794 -28.051 1.00 66.13  ? 112 LEU   B CD2 1 
ATOM   1072 N  N   . PRO   B 2 104 ? -11.513 -10.322 -25.292 1.00 61.66  ? 113 PRO   B N   1 
ATOM   1073 C  CA  . PRO   B 2 104 ? -10.843 -10.017 -24.031 1.00 61.49  ? 113 PRO   B CA  1 
ATOM   1074 C  C   . PRO   B 2 104 ? -9.679  -10.929 -23.700 1.00 62.37  ? 113 PRO   B C   1 
ATOM   1075 O  O   . PRO   B 2 104 ? -9.736  -12.133 -23.919 1.00 62.91  ? 113 PRO   B O   1 
ATOM   1076 C  CB  . PRO   B 2 104 ? -11.951 -10.206 -22.986 1.00 62.11  ? 113 PRO   B CB  1 
ATOM   1077 C  CG  . PRO   B 2 104 ? -13.244 -10.106 -23.739 1.00 62.46  ? 113 PRO   B CG  1 
ATOM   1078 C  CD  . PRO   B 2 104 ? -12.914 -10.734 -25.079 1.00 61.01  ? 113 PRO   B CD  1 
ATOM   1079 N  N   . GLY   B 2 105 ? -8.658  -10.341 -23.093 1.00 62.10  ? 114 GLY   B N   1 
ATOM   1080 C  CA  . GLY   B 2 105 ? -7.551  -11.068 -22.500 1.00 61.85  ? 114 GLY   B CA  1 
ATOM   1081 C  C   . GLY   B 2 105 ? -7.941  -11.484 -21.087 1.00 61.87  ? 114 GLY   B C   1 
ATOM   1082 O  O   . GLY   B 2 105 ? -9.132  -11.457 -20.733 1.00 61.52  ? 114 GLY   B O   1 
ATOM   1083 N  N   . ILE   B 2 106 ? -6.941  -11.834 -20.242 1.00 61.40  ? 115 ILE   B N   1 
ATOM   1084 C  CA  . ILE   B 2 106 ? -7.140  -12.314 -18.872 1.00 62.27  ? 115 ILE   B CA  1 
ATOM   1085 C  C   . ILE   B 2 106 ? -6.246  -11.608 -17.849 1.00 61.56  ? 115 ILE   B C   1 
ATOM   1086 O  O   . ILE   B 2 106 ? -5.042  -11.499 -18.056 1.00 62.55  ? 115 ILE   B O   1 
ATOM   1087 C  CB  . ILE   B 2 106 ? -6.794  -13.848 -18.828 1.00 64.63  ? 115 ILE   B CB  1 
ATOM   1088 C  CG1 . ILE   B 2 106 ? -7.689  -14.692 -19.739 1.00 67.81  ? 115 ILE   B CG1 1 
ATOM   1089 C  CG2 . ILE   B 2 106 ? -6.777  -14.418 -17.432 1.00 65.51  ? 115 ILE   B CG2 1 
ATOM   1090 C  CD1 . ILE   B 2 106 ? -9.102  -14.586 -19.437 1.00 70.23  ? 115 ILE   B CD1 1 
ATOM   1091 N  N   . PHE   B 2 107 ? -6.809  -11.246 -16.688 1.00 59.77  ? 116 PHE   B N   1 
ATOM   1092 C  CA  . PHE   B 2 107 ? -6.062  -10.772 -15.537 1.00 58.66  ? 116 PHE   B CA  1 
ATOM   1093 C  C   . PHE   B 2 107 ? -5.984  -12.027 -14.651 1.00 59.46  ? 116 PHE   B C   1 
ATOM   1094 O  O   . PHE   B 2 107 ? -7.031  -12.517 -14.224 1.00 59.56  ? 116 PHE   B O   1 
ATOM   1095 C  CB  . PHE   B 2 107 ? -6.857  -9.687  -14.765 1.00 57.37  ? 116 PHE   B CB  1 
ATOM   1096 C  CG  . PHE   B 2 107 ? -6.588  -8.247  -15.137 1.00 56.59  ? 116 PHE   B CG  1 
ATOM   1097 C  CD1 . PHE   B 2 107 ? -5.852  -7.929  -16.267 1.00 56.41  ? 116 PHE   B CD1 1 
ATOM   1098 C  CD2 . PHE   B 2 107 ? -7.091  -7.209  -14.366 1.00 56.26  ? 116 PHE   B CD2 1 
ATOM   1099 C  CE1 . PHE   B 2 107 ? -5.635  -6.600  -16.622 1.00 56.54  ? 116 PHE   B CE1 1 
ATOM   1100 C  CE2 . PHE   B 2 107 ? -6.861  -5.886  -14.717 1.00 56.11  ? 116 PHE   B CE2 1 
ATOM   1101 C  CZ  . PHE   B 2 107 ? -6.132  -5.589  -15.835 1.00 56.05  ? 116 PHE   B CZ  1 
ATOM   1102 N  N   . LYS   B 2 108 ? -4.785  -12.558 -14.382 1.00 59.82  ? 117 LYS   B N   1 
ATOM   1103 C  CA  . LYS   B 2 108 ? -4.639  -13.717 -13.504 1.00 61.00  ? 117 LYS   B CA  1 
ATOM   1104 C  C   . LYS   B 2 108 ? -4.280  -13.207 -12.114 1.00 61.08  ? 117 LYS   B C   1 
ATOM   1105 O  O   . LYS   B 2 108 ? -3.269  -12.522 -11.978 1.00 61.38  ? 117 LYS   B O   1 
ATOM   1106 C  CB  . LYS   B 2 108 ? -3.515  -14.658 -14.001 1.00 64.40  ? 117 LYS   B CB  1 
ATOM   1107 C  CG  . LYS   B 2 108 ? -3.726  -15.161 -15.424 1.00 71.69  ? 117 LYS   B CG  1 
ATOM   1108 C  CD  . LYS   B 2 108 ? -2.629  -16.139 -15.846 1.00 79.21  ? 117 LYS   B CD  1 
ATOM   1109 C  CE  . LYS   B 2 108 ? -2.934  -16.781 -17.179 1.00 86.29  ? 117 LYS   B CE  1 
ATOM   1110 N  NZ  . LYS   B 2 108 ? -1.844  -17.698 -17.636 1.00 90.59  ? 117 LYS   B NZ  1 
ATOM   1111 N  N   . THR   B 2 109 ? -5.091  -13.519 -11.089 1.00 60.74  ? 118 THR   B N   1 
ATOM   1112 C  CA  . THR   B 2 109 ? -4.836  -13.058 -9.721  1.00 61.75  ? 118 THR   B CA  1 
ATOM   1113 C  C   . THR   B 2 109 ? -4.704  -14.246 -8.742  1.00 63.35  ? 118 THR   B C   1 
ATOM   1114 O  O   . THR   B 2 109 ? -5.092  -15.369 -9.074  1.00 63.72  ? 118 THR   B O   1 
ATOM   1115 C  CB  . THR   B 2 109 ? -5.946  -12.059 -9.238  1.00 62.52  ? 118 THR   B CB  1 
ATOM   1116 O  OG1 . THR   B 2 109 ? -7.106  -12.773 -8.811  1.00 63.59  ? 118 THR   B OG1 1 
ATOM   1117 C  CG2 . THR   B 2 109 ? -6.331  -11.019 -10.284 1.00 62.19  ? 118 THR   B CG2 1 
ATOM   1118 N  N   . LYS   B 2 110 ? -4.206  -13.989 -7.524  1.00 64.03  ? 119 LYS   B N   1 
ATOM   1119 C  CA  . LYS   B 2 110 ? -4.092  -15.038 -6.503  1.00 65.25  ? 119 LYS   B CA  1 
ATOM   1120 C  C   . LYS   B 2 110 ? -5.482  -15.604 -6.098  1.00 66.80  ? 119 LYS   B C   1 
ATOM   1121 O  O   . LYS   B 2 110 ? -5.550  -16.696 -5.525  1.00 67.37  ? 119 LYS   B O   1 
ATOM   1122 C  CB  . LYS   B 2 110 ? -3.347  -14.495 -5.274  1.00 66.31  ? 119 LYS   B CB  1 
ATOM   1123 C  CG  . LYS   B 2 110 ? -4.149  -13.458 -4.490  1.00 70.09  ? 119 LYS   B CG  1 
ATOM   1124 C  CD  . LYS   B 2 110 ? -3.390  -12.975 -3.261  1.00 74.97  ? 119 LYS   B CD  1 
ATOM   1125 C  CE  . LYS   B 2 110 ? -4.308  -12.594 -2.124  1.00 78.51  ? 119 LYS   B CE  1 
ATOM   1126 N  NZ  . LYS   B 2 110 ? -5.096  -11.380 -2.431  1.00 80.70  ? 119 LYS   B NZ  1 
ATOM   1127 N  N   . ASP   B 2 111 ? -6.579  -14.880 -6.441  1.00 66.71  ? 120 ASP   B N   1 
ATOM   1128 C  CA  . ASP   B 2 111 ? -7.957  -15.251 -6.139  1.00 67.39  ? 120 ASP   B CA  1 
ATOM   1129 C  C   . ASP   B 2 111 ? -8.783  -15.623 -7.369  1.00 67.62  ? 120 ASP   B C   1 
ATOM   1130 O  O   . ASP   B 2 111 ? -10.009 -15.630 -7.273  1.00 68.53  ? 120 ASP   B O   1 
ATOM   1131 C  CB  . ASP   B 2 111 ? -8.668  -14.095 -5.419  1.00 69.11  ? 120 ASP   B CB  1 
ATOM   1132 C  CG  . ASP   B 2 111 ? -8.118  -13.792 -4.043  1.00 74.67  ? 120 ASP   B CG  1 
ATOM   1133 O  OD1 . ASP   B 2 111 ? -7.770  -14.756 -3.313  1.00 75.91  ? 120 ASP   B OD1 1 
ATOM   1134 O  OD2 . ASP   B 2 111 ? -8.050  -12.596 -3.683  1.00 76.54  ? 120 ASP   B OD2 1 
ATOM   1135 N  N   . GLY   B 2 112 ? -8.148  -15.887 -8.506  1.00 66.74  ? 121 GLY   B N   1 
ATOM   1136 C  CA  . GLY   B 2 112 ? -8.877  -16.257 -9.712  1.00 66.45  ? 121 GLY   B CA  1 
ATOM   1137 C  C   . GLY   B 2 112 ? -8.698  -15.318 -10.890 1.00 65.94  ? 121 GLY   B C   1 
ATOM   1138 O  O   . GLY   B 2 112 ? -8.161  -14.216 -10.748 1.00 66.15  ? 121 GLY   B O   1 
ATOM   1139 N  N   . ASP   B 2 113 ? -9.163  -15.749 -12.064 1.00 65.08  ? 122 ASP   B N   1 
ATOM   1140 C  CA  . ASP   B 2 113 ? -9.026  -14.969 -13.291 1.00 64.62  ? 122 ASP   B CA  1 
ATOM   1141 C  C   . ASP   B 2 113 ? -10.219 -14.055 -13.566 1.00 63.66  ? 122 ASP   B C   1 
ATOM   1142 O  O   . ASP   B 2 113 ? -11.347 -14.358 -13.182 1.00 63.83  ? 122 ASP   B O   1 
ATOM   1143 C  CB  . ASP   B 2 113 ? -8.751  -15.885 -14.491 1.00 66.72  ? 122 ASP   B CB  1 
ATOM   1144 C  CG  . ASP   B 2 113 ? -7.500  -16.748 -14.365 1.00 73.02  ? 122 ASP   B CG  1 
ATOM   1145 O  OD1 . ASP   B 2 113 ? -6.726  -16.536 -13.418 1.00 74.56  ? 122 ASP   B OD1 1 
ATOM   1146 O  OD2 . ASP   B 2 113 ? -7.295  -17.627 -15.228 1.00 76.54  ? 122 ASP   B OD2 1 
ATOM   1147 N  N   . ILE   B 2 114 ? -9.947  -12.922 -14.224 1.00 61.95  ? 123 ILE   B N   1 
ATOM   1148 C  CA  . ILE   B 2 114 ? -10.931 -11.904 -14.574 1.00 61.32  ? 123 ILE   B CA  1 
ATOM   1149 C  C   . ILE   B 2 114 ? -10.706 -11.540 -16.047 1.00 59.47  ? 123 ILE   B C   1 
ATOM   1150 O  O   . ILE   B 2 114 ? -9.556  -11.425 -16.466 1.00 58.86  ? 123 ILE   B O   1 
ATOM   1151 C  CB  . ILE   B 2 114 ? -10.736 -10.614 -13.702 1.00 62.30  ? 123 ILE   B CB  1 
ATOM   1152 C  CG1 . ILE   B 2 114 ? -10.505 -10.918 -12.218 1.00 64.34  ? 123 ILE   B CG1 1 
ATOM   1153 C  CG2 . ILE   B 2 114 ? -11.882 -9.634  -13.891 1.00 63.25  ? 123 ILE   B CG2 1 
ATOM   1154 C  CD1 . ILE   B 2 114 ? -10.226 -9.663  -11.319 1.00 66.08  ? 123 ILE   B CD1 1 
ATOM   1155 N  N   . GLY   B 2 115 ? -11.780 -11.278 -16.804 1.00 57.86  ? 124 GLY   B N   1 
ATOM   1156 C  CA  . GLY   B 2 115 ? -11.631 -10.827 -18.179 1.00 57.63  ? 124 GLY   B CA  1 
ATOM   1157 C  C   . GLY   B 2 115 ? -10.984 -9.455  -18.208 1.00 57.43  ? 124 GLY   B C   1 
ATOM   1158 O  O   . GLY   B 2 115 ? -11.022 -8.725  -17.208 1.00 57.40  ? 124 GLY   B O   1 
ATOM   1159 N  N   . ALA   B 2 116 ? -10.332 -9.117  -19.308 1.00 56.97  ? 125 ALA   B N   1 
ATOM   1160 C  CA  . ALA   B 2 116 ? -9.690  -7.811  -19.442 1.00 57.60  ? 125 ALA   B CA  1 
ATOM   1161 C  C   . ALA   B 2 116 ? -9.821  -7.288  -20.874 1.00 58.38  ? 125 ALA   B C   1 
ATOM   1162 O  O   . ALA   B 2 116 ? -9.749  -8.063  -21.811 1.00 58.73  ? 125 ALA   B O   1 
ATOM   1163 C  CB  . ALA   B 2 116 ? -8.229  -7.896  -19.023 1.00 57.57  ? 125 ALA   B CB  1 
ATOM   1164 N  N   . VAL   B 2 117 ? -10.029 -5.977  -21.046 1.00 58.33  ? 126 VAL   B N   1 
ATOM   1165 C  CA  A VAL   B 2 117 ? -10.139 -5.394  -22.380 0.50 59.09  ? 126 VAL   B CA  1 
ATOM   1166 C  CA  B VAL   B 2 117 ? -10.199 -5.346  -22.343 0.50 59.22  ? 126 VAL   B CA  1 
ATOM   1167 C  C   . VAL   B 2 117 ? -9.027  -4.385  -22.624 1.00 59.64  ? 126 VAL   B C   1 
ATOM   1168 O  O   . VAL   B 2 117 ? -8.782  -3.478  -21.819 1.00 59.03  ? 126 VAL   B O   1 
ATOM   1169 C  CB  A VAL   B 2 117 ? -11.536 -4.849  -22.747 0.50 59.74  ? 126 VAL   B CB  1 
ATOM   1170 C  CB  B VAL   B 2 117 ? -11.577 -4.645  -22.329 0.50 60.01  ? 126 VAL   B CB  1 
ATOM   1171 C  CG1 A VAL   B 2 117 ? -12.512 -5.998  -22.978 0.50 60.20  ? 126 VAL   B CG1 1 
ATOM   1172 C  CG1 B VAL   B 2 117 ? -11.716 -3.637  -23.453 0.50 60.42  ? 126 VAL   B CG1 1 
ATOM   1173 C  CG2 A VAL   B 2 117 ? -12.059 -3.886  -21.686 0.50 60.07  ? 126 VAL   B CG2 1 
ATOM   1174 C  CG2 B VAL   B 2 117 ? -12.704 -5.672  -22.369 0.50 60.53  ? 126 VAL   B CG2 1 
ATOM   1175 N  N   . ALA   B 2 118 ? -8.289  -4.596  -23.741 1.00 59.76  ? 127 ALA   B N   1 
ATOM   1176 C  CA  . ALA   B 2 118 ? -7.146  -3.768  -24.078 1.00 61.12  ? 127 ALA   B CA  1 
ATOM   1177 C  C   . ALA   B 2 118 ? -7.498  -2.674  -25.061 1.00 62.70  ? 127 ALA   B C   1 
ATOM   1178 O  O   . ALA   B 2 118 ? -7.086  -2.704  -26.222 1.00 63.87  ? 127 ALA   B O   1 
ATOM   1179 C  CB  . ALA   B 2 118 ? -5.995  -4.635  -24.597 1.00 61.76  ? 127 ALA   B CB  1 
ATOM   1180 N  N   . LEU   B 2 119 ? -8.321  -1.713  -24.611 1.00 62.38  ? 128 LEU   B N   1 
ATOM   1181 C  CA  . LEU   B 2 119 ? -8.716  -0.601  -25.444 1.00 63.09  ? 128 LEU   B CA  1 
ATOM   1182 C  C   . LEU   B 2 119 ? -8.364  0.689   -24.702 1.00 64.91  ? 128 LEU   B C   1 
ATOM   1183 O  O   . LEU   B 2 119 ? -8.614  0.806   -23.502 1.00 64.99  ? 128 LEU   B O   1 
ATOM   1184 C  CB  . LEU   B 2 119 ? -10.215 -0.677  -25.775 1.00 62.94  ? 128 LEU   B CB  1 
ATOM   1185 C  CG  . LEU   B 2 119 ? -10.663 -1.903  -26.577 1.00 63.23  ? 128 LEU   B CG  1 
ATOM   1186 C  CD1 . LEU   B 2 119 ? -12.176 -1.997  -26.640 1.00 63.33  ? 128 LEU   B CD1 1 
ATOM   1187 C  CD2 . LEU   B 2 119 ? -10.061 -1.904  -27.981 1.00 63.81  ? 128 LEU   B CD2 1 
ATOM   1188 N  N   . ASP   B 2 120 ? -7.799  1.657   -25.432 1.00 66.13  ? 129 ASP   B N   1 
ATOM   1189 C  CA  . ASP   B 2 120 ? -7.297  2.937   -24.939 1.00 67.18  ? 129 ASP   B CA  1 
ATOM   1190 C  C   . ASP   B 2 120 ? -8.307  4.047   -25.011 1.00 66.07  ? 129 ASP   B C   1 
ATOM   1191 O  O   . ASP   B 2 120 ? -8.622  4.474   -26.112 1.00 67.20  ? 129 ASP   B O   1 
ATOM   1192 C  CB  . ASP   B 2 120 ? -6.102  3.355   -25.823 1.00 71.86  ? 129 ASP   B CB  1 
ATOM   1193 C  CG  . ASP   B 2 120 ? -4.793  3.549   -25.079 1.00 80.83  ? 129 ASP   B CG  1 
ATOM   1194 O  OD1 . ASP   B 2 120 ? -4.801  3.463   -23.823 1.00 82.62  ? 129 ASP   B OD1 1 
ATOM   1195 O  OD2 . ASP   B 2 120 ? -3.758  3.797   -25.750 1.00 84.12  ? 129 ASP   B OD2 1 
ATOM   1196 N  N   . TYR   B 2 121 ? -8.749  4.594   -23.870 1.00 64.30  ? 130 TYR   B N   1 
ATOM   1197 C  CA  . TYR   B 2 121 ? -9.695  5.713   -23.880 1.00 62.93  ? 130 TYR   B CA  1 
ATOM   1198 C  C   . TYR   B 2 121 ? -9.375  6.723   -22.762 1.00 61.51  ? 130 TYR   B C   1 
ATOM   1199 O  O   . TYR   B 2 121 ? -8.772  6.339   -21.756 1.00 61.62  ? 130 TYR   B O   1 
ATOM   1200 C  CB  . TYR   B 2 121 ? -11.138 5.188   -23.744 1.00 63.25  ? 130 TYR   B CB  1 
ATOM   1201 C  CG  . TYR   B 2 121 ? -11.743 4.742   -25.055 1.00 64.42  ? 130 TYR   B CG  1 
ATOM   1202 C  CD1 . TYR   B 2 121 ? -12.315 5.657   -25.926 1.00 65.71  ? 130 TYR   B CD1 1 
ATOM   1203 C  CD2 . TYR   B 2 121 ? -11.709 3.409   -25.441 1.00 65.45  ? 130 TYR   B CD2 1 
ATOM   1204 C  CE1 . TYR   B 2 121 ? -12.839 5.256   -27.148 1.00 67.23  ? 130 TYR   B CE1 1 
ATOM   1205 C  CE2 . TYR   B 2 121 ? -12.208 3.001   -26.671 1.00 66.92  ? 130 TYR   B CE2 1 
ATOM   1206 C  CZ  . TYR   B 2 121 ? -12.785 3.925   -27.516 1.00 68.76  ? 130 TYR   B CZ  1 
ATOM   1207 O  OH  . TYR   B 2 121 ? -13.286 3.523   -28.732 1.00 71.96  ? 130 TYR   B OH  1 
ATOM   1208 N  N   . PRO   B 2 122 ? -9.804  8.003   -22.870 1.00 60.10  ? 131 PRO   B N   1 
ATOM   1209 C  CA  . PRO   B 2 122 ? -9.557  8.949   -21.763 1.00 59.21  ? 131 PRO   B CA  1 
ATOM   1210 C  C   . PRO   B 2 122 ? -10.168 8.474   -20.431 1.00 57.30  ? 131 PRO   B C   1 
ATOM   1211 O  O   . PRO   B 2 122 ? -11.131 7.709   -20.444 1.00 56.60  ? 131 PRO   B O   1 
ATOM   1212 C  CB  . PRO   B 2 122 ? -10.218 10.243  -22.249 1.00 60.46  ? 131 PRO   B CB  1 
ATOM   1213 C  CG  . PRO   B 2 122 ? -10.274 10.107  -23.751 1.00 61.22  ? 131 PRO   B CG  1 
ATOM   1214 C  CD  . PRO   B 2 122 ? -10.528 8.651   -23.982 1.00 59.75  ? 131 PRO   B CD  1 
ATOM   1215 N  N   . ALA   B 2 123 ? -9.601  8.925   -19.283 1.00 55.86  ? 132 ALA   B N   1 
ATOM   1216 C  CA  . ALA   B 2 123 ? -10.031 8.549   -17.932 1.00 54.73  ? 132 ALA   B CA  1 
ATOM   1217 C  C   . ALA   B 2 123 ? -11.515 8.836   -17.640 1.00 52.14  ? 132 ALA   B C   1 
ATOM   1218 O  O   . ALA   B 2 123 ? -12.159 8.096   -16.882 1.00 51.44  ? 132 ALA   B O   1 
ATOM   1219 C  CB  . ALA   B 2 123 ? -9.143  9.217   -16.890 1.00 55.38  ? 132 ALA   B CB  1 
ATOM   1220 N  N   . GLY   B 2 124 ? -12.053 9.857   -18.298 1.00 49.98  ? 133 GLY   B N   1 
ATOM   1221 C  CA  . GLY   B 2 124 ? -13.460 10.210  -18.173 1.00 48.14  ? 133 GLY   B CA  1 
ATOM   1222 C  C   . GLY   B 2 124 ? -14.404 9.251   -18.883 1.00 45.86  ? 133 GLY   B C   1 
ATOM   1223 O  O   . GLY   B 2 124 ? -15.611 9.457   -18.847 1.00 45.75  ? 133 GLY   B O   1 
ATOM   1224 N  N   . THR   B 2 125 ? -13.878 8.205   -19.545 1.00 43.72  ? 134 THR   B N   1 
ATOM   1225 C  CA  . THR   B 2 125 ? -14.687 7.145   -20.168 1.00 43.52  ? 134 THR   B CA  1 
ATOM   1226 C  C   . THR   B 2 125 ? -15.005 6.010   -19.103 1.00 42.72  ? 134 THR   B C   1 
ATOM   1227 O  O   . THR   B 2 125 ? -15.711 5.062   -19.437 1.00 42.47  ? 134 THR   B O   1 
ATOM   1228 C  CB  . THR   B 2 125 ? -13.920 6.536   -21.393 1.00 45.50  ? 134 THR   B CB  1 
ATOM   1229 O  OG1 . THR   B 2 125 ? -13.389 7.577   -22.221 1.00 47.83  ? 134 THR   B OG1 1 
ATOM   1230 C  CG2 . THR   B 2 125 ? -14.764 5.598   -22.257 1.00 45.20  ? 134 THR   B CG2 1 
ATOM   1231 N  N   . SER   B 2 126 ? -14.416 6.074   -17.874 1.00 41.91  ? 135 SER   B N   1 
ATOM   1232 C  CA  . SER   B 2 126 ? -14.587 5.072   -16.805 1.00 41.55  ? 135 SER   B CA  1 
ATOM   1233 C  C   . SER   B 2 126 ? -16.056 4.873   -16.478 1.00 41.04  ? 135 SER   B C   1 
ATOM   1234 O  O   . SER   B 2 126 ? -16.749 5.852   -16.305 1.00 40.53  ? 135 SER   B O   1 
ATOM   1235 C  CB  . SER   B 2 126 ? -13.872 5.531   -15.541 1.00 41.90  ? 135 SER   B CB  1 
ATOM   1236 O  OG  . SER   B 2 126 ? -12.467 5.442   -15.704 1.00 43.43  ? 135 SER   B OG  1 
ATOM   1237 N  N   . GLY   B 2 127 ? -16.503 3.620   -16.387 1.00 40.53  ? 136 GLY   B N   1 
ATOM   1238 C  CA  . GLY   B 2 127 ? -17.899 3.276   -16.151 1.00 41.74  ? 136 GLY   B CA  1 
ATOM   1239 C  C   . GLY   B 2 127 ? -18.649 2.842   -17.404 1.00 42.71  ? 136 GLY   B C   1 
ATOM   1240 O  O   . GLY   B 2 127 ? -19.817 2.441   -17.327 1.00 43.21  ? 136 GLY   B O   1 
ATOM   1241 N  N   . SER   B 2 128 ? -18.022 2.964   -18.588 1.00 41.96  ? 137 SER   B N   1 
ATOM   1242 C  CA  . SER   B 2 128 ? -18.644 2.543   -19.852 1.00 41.95  ? 137 SER   B CA  1 
ATOM   1243 C  C   . SER   B 2 128 ? -18.893 1.039   -19.803 1.00 42.58  ? 137 SER   B C   1 
ATOM   1244 O  O   . SER   B 2 128 ? -18.035 0.296   -19.347 1.00 42.14  ? 137 SER   B O   1 
ATOM   1245 C  CB  . SER   B 2 128 ? -17.717 2.841   -21.035 1.00 42.76  ? 137 SER   B CB  1 
ATOM   1246 O  OG  . SER   B 2 128 ? -17.801 4.214   -21.369 1.00 44.10  ? 137 SER   B OG  1 
ATOM   1247 N  N   . PRO   B 2 129 ? -20.077 0.587   -20.223 1.00 43.18  ? 138 PRO   B N   1 
ATOM   1248 C  CA  . PRO   B 2 129 ? -20.384 -0.840  -20.137 1.00 43.69  ? 138 PRO   B CA  1 
ATOM   1249 C  C   . PRO   B 2 129 ? -19.768 -1.709  -21.226 1.00 46.08  ? 138 PRO   B C   1 
ATOM   1250 O  O   . PRO   B 2 129 ? -19.649 -1.301  -22.390 1.00 46.46  ? 138 PRO   B O   1 
ATOM   1251 C  CB  . PRO   B 2 129 ? -21.909 -0.871  -20.236 1.00 44.69  ? 138 PRO   B CB  1 
ATOM   1252 C  CG  . PRO   B 2 129 ? -22.260 0.324   -21.073 1.00 44.81  ? 138 PRO   B CG  1 
ATOM   1253 C  CD  . PRO   B 2 129 ? -21.223 1.373   -20.731 1.00 43.10  ? 138 PRO   B CD  1 
ATOM   1254 N  N   . ILE   B 2 130 ? -19.460 -2.948  -20.850 1.00 46.95  ? 139 ILE   B N   1 
ATOM   1255 C  CA  . ILE   B 2 130 ? -18.966 -3.989  -21.752 1.00 48.15  ? 139 ILE   B CA  1 
ATOM   1256 C  C   . ILE   B 2 130 ? -20.142 -4.965  -21.888 1.00 49.84  ? 139 ILE   B C   1 
ATOM   1257 O  O   . ILE   B 2 130 ? -20.731 -5.348  -20.874 1.00 49.36  ? 139 ILE   B O   1 
ATOM   1258 C  CB  . ILE   B 2 130 ? -17.726 -4.654  -21.135 1.00 48.90  ? 139 ILE   B CB  1 
ATOM   1259 C  CG1 . ILE   B 2 130 ? -16.579 -3.630  -21.043 1.00 50.37  ? 139 ILE   B CG1 1 
ATOM   1260 C  CG2 . ILE   B 2 130 ? -17.312 -5.897  -21.939 1.00 49.15  ? 139 ILE   B CG2 1 
ATOM   1261 C  CD1 . ILE   B 2 130 ? -15.571 -3.917  -19.969 1.00 52.11  ? 139 ILE   B CD1 1 
ATOM   1262 N  N   . LEU   B 2 131 ? -20.527 -5.313  -23.137 1.00 51.34  ? 140 LEU   B N   1 
ATOM   1263 C  CA  . LEU   B 2 131 ? -21.701 -6.131  -23.443 1.00 53.78  ? 140 LEU   B CA  1 
ATOM   1264 C  C   . LEU   B 2 131 ? -21.396 -7.471  -24.076 1.00 55.33  ? 140 LEU   B C   1 
ATOM   1265 O  O   . LEU   B 2 131 ? -20.465 -7.570  -24.872 1.00 56.48  ? 140 LEU   B O   1 
ATOM   1266 C  CB  . LEU   B 2 131 ? -22.608 -5.391  -24.466 1.00 55.71  ? 140 LEU   B CB  1 
ATOM   1267 C  CG  . LEU   B 2 131 ? -22.656 -3.875  -24.431 1.00 58.30  ? 140 LEU   B CG  1 
ATOM   1268 C  CD1 . LEU   B 2 131 ? -23.533 -3.333  -25.536 1.00 60.14  ? 140 LEU   B CD1 1 
ATOM   1269 C  CD2 . LEU   B 2 131 ? -23.115 -3.399  -23.081 1.00 59.45  ? 140 LEU   B CD2 1 
ATOM   1270 N  N   . ASP   B 2 132 ? -22.248 -8.474  -23.822 1.00 55.62  ? 141 ASP   B N   1 
ATOM   1271 C  CA  . ASP   B 2 132 ? -22.153 -9.745  -24.547 1.00 57.80  ? 141 ASP   B CA  1 
ATOM   1272 C  C   . ASP   B 2 132 ? -23.046 -9.644  -25.821 1.00 61.28  ? 141 ASP   B C   1 
ATOM   1273 O  O   . ASP   B 2 132 ? -23.699 -8.603  -26.035 1.00 61.98  ? 141 ASP   B O   1 
ATOM   1274 C  CB  . ASP   B 2 132 ? -22.520 -10.953 -23.650 1.00 57.79  ? 141 ASP   B CB  1 
ATOM   1275 C  CG  . ASP   B 2 132 ? -23.926 -10.968 -23.081 1.00 58.61  ? 141 ASP   B CG  1 
ATOM   1276 O  OD1 . ASP   B 2 132 ? -24.791 -10.231 -23.599 1.00 57.91  ? 141 ASP   B OD1 1 
ATOM   1277 O  OD2 . ASP   B 2 132 ? -24.164 -11.721 -22.127 1.00 60.27  ? 141 ASP   B OD2 1 
ATOM   1278 N  N   . LYS   B 2 133 ? -23.095 -10.711 -26.653 1.00 63.21  ? 142 LYS   B N   1 
ATOM   1279 C  CA  . LYS   B 2 133 ? -23.865 -10.732 -27.897 1.00 65.99  ? 142 LYS   B CA  1 
ATOM   1280 C  C   . LYS   B 2 133 ? -25.372 -10.567 -27.687 1.00 67.16  ? 142 LYS   B C   1 
ATOM   1281 O  O   . LYS   B 2 133 ? -26.071 -10.152 -28.615 1.00 67.59  ? 142 LYS   B O   1 
ATOM   1282 C  CB  . LYS   B 2 133 ? -23.544 -11.991 -28.736 1.00 70.10  ? 142 LYS   B CB  1 
ATOM   1283 C  CG  . LYS   B 2 133 ? -22.054 -12.139 -29.055 1.00 76.98  ? 142 LYS   B CG  1 
ATOM   1284 C  CD  . LYS   B 2 133 ? -21.690 -13.525 -29.644 1.00 83.33  ? 142 LYS   B CD  1 
ATOM   1285 C  CE  . LYS   B 2 133 ? -20.194 -13.706 -29.799 1.00 88.10  ? 142 LYS   B CE  1 
ATOM   1286 N  NZ  . LYS   B 2 133 ? -19.820 -15.091 -30.233 1.00 91.20  ? 142 LYS   B NZ  1 
ATOM   1287 N  N   . CYS   B 2 134 ? -25.874 -10.851 -26.472 1.00 67.23  ? 143 CYS   B N   1 
ATOM   1288 C  CA  . CYS   B 2 134 ? -27.291 -10.627 -26.158 1.00 67.46  ? 143 CYS   B CA  1 
ATOM   1289 C  C   . CYS   B 2 134 ? -27.579 -9.196  -25.678 1.00 65.86  ? 143 CYS   B C   1 
ATOM   1290 O  O   . CYS   B 2 134 ? -28.722 -8.899  -25.348 1.00 66.24  ? 143 CYS   B O   1 
ATOM   1291 C  CB  . CYS   B 2 134 ? -27.798 -11.651 -25.149 1.00 70.08  ? 143 CYS   B CB  1 
ATOM   1292 S  SG  . CYS   B 2 134 ? -27.887 -13.343 -25.787 1.00 78.61  ? 143 CYS   B SG  1 
ATOM   1293 N  N   . GLY   B 2 135 ? -26.570 -8.327  -25.644 1.00 64.03  ? 144 GLY   B N   1 
ATOM   1294 C  CA  . GLY   B 2 135 ? -26.730 -6.956  -25.171 1.00 62.60  ? 144 GLY   B CA  1 
ATOM   1295 C  C   . GLY   B 2 135 ? -26.718 -6.819  -23.657 1.00 60.81  ? 144 GLY   B C   1 
ATOM   1296 O  O   . GLY   B 2 135 ? -26.992 -5.739  -23.135 1.00 60.90  ? 144 GLY   B O   1 
ATOM   1297 N  N   . ARG   B 2 136 ? -26.402 -7.907  -22.927 1.00 58.41  ? 145 ARG   B N   1 
ATOM   1298 C  CA  . ARG   B 2 136 ? -26.379 -7.878  -21.468 1.00 56.69  ? 145 ARG   B CA  1 
ATOM   1299 C  C   . ARG   B 2 136 ? -25.064 -7.286  -20.968 1.00 53.32  ? 145 ARG   B C   1 
ATOM   1300 O  O   . ARG   B 2 136 ? -24.016 -7.536  -21.569 1.00 52.93  ? 145 ARG   B O   1 
ATOM   1301 C  CB  . ARG   B 2 136 ? -26.598 -9.289  -20.900 1.00 59.38  ? 145 ARG   B CB  1 
ATOM   1302 C  CG  . ARG   B 2 136 ? -28.003 -9.829  -21.164 1.00 63.61  ? 145 ARG   B CG  1 
ATOM   1303 C  CD  . ARG   B 2 136 ? -28.147 -11.244 -20.655 1.00 68.58  ? 145 ARG   B CD  1 
ATOM   1304 N  NE  . ARG   B 2 136 ? -27.340 -12.169 -21.449 1.00 74.30  ? 145 ARG   B NE  1 
ATOM   1305 C  CZ  . ARG   B 2 136 ? -26.970 -13.381 -21.052 1.00 78.04  ? 145 ARG   B CZ  1 
ATOM   1306 N  NH1 . ARG   B 2 136 ? -27.307 -13.826 -19.846 1.00 77.94  ? 145 ARG   B NH1 1 
ATOM   1307 N  NH2 . ARG   B 2 136 ? -26.235 -14.147 -21.846 1.00 78.84  ? 145 ARG   B NH2 1 
ATOM   1308 N  N   . VAL   B 2 137 ? -25.116 -6.478  -19.890 1.00 50.31  ? 146 VAL   B N   1 
ATOM   1309 C  CA  . VAL   B 2 137 ? -23.922 -5.847  -19.346 1.00 48.55  ? 146 VAL   B CA  1 
ATOM   1310 C  C   . VAL   B 2 137 ? -23.118 -6.830  -18.513 1.00 48.52  ? 146 VAL   B C   1 
ATOM   1311 O  O   . VAL   B 2 137 ? -23.575 -7.273  -17.465 1.00 48.82  ? 146 VAL   B O   1 
ATOM   1312 C  CB  . VAL   B 2 137 ? -24.255 -4.550  -18.566 1.00 48.11  ? 146 VAL   B CB  1 
ATOM   1313 C  CG1 . VAL   B 2 137 ? -22.991 -3.942  -17.973 1.00 48.06  ? 146 VAL   B CG1 1 
ATOM   1314 C  CG2 . VAL   B 2 137 ? -24.962 -3.545  -19.479 1.00 47.88  ? 146 VAL   B CG2 1 
ATOM   1315 N  N   . ILE   B 2 138 ? -21.952 -7.243  -19.022 1.00 47.74  ? 147 ILE   B N   1 
ATOM   1316 C  CA  . ILE   B 2 138 ? -21.100 -8.192  -18.306 1.00 46.85  ? 147 ILE   B CA  1 
ATOM   1317 C  C   . ILE   B 2 138 ? -20.073 -7.517  -17.390 1.00 45.07  ? 147 ILE   B C   1 
ATOM   1318 O  O   . ILE   B 2 138 ? -19.348 -8.207  -16.674 1.00 44.52  ? 147 ILE   B O   1 
ATOM   1319 C  CB  . ILE   B 2 138 ? -20.423 -9.178  -19.307 1.00 47.95  ? 147 ILE   B CB  1 
ATOM   1320 C  CG1 . ILE   B 2 138 ? -19.648 -8.405  -20.371 1.00 49.29  ? 147 ILE   B CG1 1 
ATOM   1321 C  CG2 . ILE   B 2 138 ? -21.453 -10.105 -19.950 1.00 48.42  ? 147 ILE   B CG2 1 
ATOM   1322 C  CD1 . ILE   B 2 138 ? -18.658 -9.277  -21.148 1.00 52.02  ? 147 ILE   B CD1 1 
ATOM   1323 N  N   . GLY   B 2 139 ? -20.040 -6.187  -17.362 1.00 44.32  ? 148 GLY   B N   1 
ATOM   1324 C  CA  . GLY   B 2 139 ? -19.139 -5.462  -16.463 1.00 43.16  ? 148 GLY   B CA  1 
ATOM   1325 C  C   . GLY   B 2 139 ? -18.871 -4.047  -16.934 1.00 42.70  ? 148 GLY   B C   1 
ATOM   1326 O  O   . GLY   B 2 139 ? -19.320 -3.663  -18.013 1.00 42.50  ? 148 GLY   B O   1 
ATOM   1327 N  N   . LEU   B 2 140 ? -18.141 -3.261  -16.147 1.00 42.04  ? 149 LEU   B N   1 
ATOM   1328 C  CA  . LEU   B 2 140 ? -17.822 -1.886  -16.518 1.00 41.95  ? 149 LEU   B CA  1 
ATOM   1329 C  C   . LEU   B 2 140 ? -16.328 -1.739  -16.771 1.00 43.13  ? 149 LEU   B C   1 
ATOM   1330 O  O   . LEU   B 2 140 ? -15.505 -2.398  -16.124 1.00 42.93  ? 149 LEU   B O   1 
ATOM   1331 C  CB  . LEU   B 2 140 ? -18.252 -0.891  -15.433 1.00 40.90  ? 149 LEU   B CB  1 
ATOM   1332 C  CG  . LEU   B 2 140 ? -19.706 -0.921  -14.971 1.00 41.78  ? 149 LEU   B CG  1 
ATOM   1333 C  CD1 . LEU   B 2 140 ? -19.973 0.181   -13.920 1.00 41.52  ? 149 LEU   B CD1 1 
ATOM   1334 C  CD2 . LEU   B 2 140 ? -20.686 -0.803  -16.160 1.00 42.61  ? 149 LEU   B CD2 1 
ATOM   1335 N  N   . TYR   B 2 141 ? -15.992 -0.828  -17.682 1.00 43.83  ? 150 TYR   B N   1 
ATOM   1336 C  CA  . TYR   B 2 141 ? -14.628 -0.533  -18.091 1.00 45.36  ? 150 TYR   B CA  1 
ATOM   1337 C  C   . TYR   B 2 141 ? -14.104 0.659   -17.313 1.00 45.91  ? 150 TYR   B C   1 
ATOM   1338 O  O   . TYR   B 2 141 ? -14.841 1.627   -17.168 1.00 46.59  ? 150 TYR   B O   1 
ATOM   1339 C  CB  . TYR   B 2 141 ? -14.687 -0.207  -19.602 1.00 46.35  ? 150 TYR   B CB  1 
ATOM   1340 C  CG  . TYR   B 2 141 ? -13.462 0.451   -20.191 1.00 47.48  ? 150 TYR   B CG  1 
ATOM   1341 C  CD1 . TYR   B 2 141 ? -13.373 1.832   -20.292 1.00 48.45  ? 150 TYR   B CD1 1 
ATOM   1342 C  CD2 . TYR   B 2 141 ? -12.405 -0.309  -20.676 1.00 48.97  ? 150 TYR   B CD2 1 
ATOM   1343 C  CE1 . TYR   B 2 141 ? -12.259 2.443   -20.858 1.00 50.19  ? 150 TYR   B CE1 1 
ATOM   1344 C  CE2 . TYR   B 2 141 ? -11.304 0.290   -21.287 1.00 49.88  ? 150 TYR   B CE2 1 
ATOM   1345 C  CZ  . TYR   B 2 141 ? -11.228 1.668   -21.362 1.00 51.82  ? 150 TYR   B CZ  1 
ATOM   1346 O  OH  . TYR   B 2 141 ? -10.146 2.281   -21.964 1.00 55.24  ? 150 TYR   B OH  1 
ATOM   1347 N  N   . GLY   B 2 142 ? -12.844 0.640   -16.895 1.00 45.66  ? 151 GLY   B N   1 
ATOM   1348 C  CA  . GLY   B 2 142 ? -12.278 1.801   -16.209 1.00 46.63  ? 151 GLY   B CA  1 
ATOM   1349 C  C   . GLY   B 2 142 ? -11.285 1.555   -15.098 1.00 47.90  ? 151 GLY   B C   1 
ATOM   1350 O  O   . GLY   B 2 142 ? -10.701 2.522   -14.595 1.00 49.24  ? 151 GLY   B O   1 
ATOM   1351 N  N   . ASN   B 2 143 ? -11.104 0.290   -14.664 1.00 46.81  ? 152 ASN   B N   1 
ATOM   1352 C  CA  . ASN   B 2 143 ? -10.143 0.002   -13.608 1.00 47.62  ? 152 ASN   B CA  1 
ATOM   1353 C  C   . ASN   B 2 143 ? -9.223  -1.093  -14.094 1.00 49.19  ? 152 ASN   B C   1 
ATOM   1354 O  O   . ASN   B 2 143 ? -9.654  -2.226  -14.314 1.00 48.20  ? 152 ASN   B O   1 
ATOM   1355 C  CB  . ASN   B 2 143 ? -10.832 -0.413  -12.290 1.00 47.94  ? 152 ASN   B CB  1 
ATOM   1356 C  CG  . ASN   B 2 143 ? -9.902  -0.534  -11.087 1.00 50.80  ? 152 ASN   B CG  1 
ATOM   1357 O  OD1 . ASN   B 2 143 ? -8.776  -0.021  -11.066 1.00 51.02  ? 152 ASN   B OD1 1 
ATOM   1358 N  ND2 . ASN   B 2 143 ? -10.333 -1.259  -10.063 1.00 50.40  ? 152 ASN   B ND2 1 
ATOM   1359 N  N   . GLY   B 2 144 ? -7.967  -0.745  -14.265 1.00 51.52  ? 153 GLY   B N   1 
ATOM   1360 C  CA  . GLY   B 2 144 ? -6.988  -1.697  -14.757 1.00 53.99  ? 153 GLY   B CA  1 
ATOM   1361 C  C   . GLY   B 2 144 ? -5.567  -1.254  -14.555 1.00 56.66  ? 153 GLY   B C   1 
ATOM   1362 O  O   . GLY   B 2 144 ? -5.248  -0.612  -13.555 1.00 56.36  ? 153 GLY   B O   1 
ATOM   1363 N  N   . VAL   B 2 145 ? -4.699  -1.583  -15.529 1.00 58.68  ? 154 VAL   B N   1 
ATOM   1364 C  CA  . VAL   B 2 145 ? -3.286  -1.313  -15.382 1.00 61.31  ? 154 VAL   B CA  1 
ATOM   1365 C  C   . VAL   B 2 145 ? -2.640  -0.714  -16.650 1.00 64.12  ? 154 VAL   B C   1 
ATOM   1366 O  O   . VAL   B 2 145 ? -3.221  -0.745  -17.736 1.00 63.53  ? 154 VAL   B O   1 
ATOM   1367 C  CB  . VAL   B 2 145 ? -2.639  -2.653  -14.950 1.00 62.37  ? 154 VAL   B CB  1 
ATOM   1368 C  CG1 . VAL   B 2 145 ? -2.384  -3.566  -16.143 1.00 62.28  ? 154 VAL   B CG1 1 
ATOM   1369 C  CG2 . VAL   B 2 145 ? -1.381  -2.438  -14.131 1.00 63.67  ? 154 VAL   B CG2 1 
ATOM   1370 N  N   . VAL   B 2 146 ? -1.452  -0.135  -16.492 1.00 66.86  ? 155 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 146 ? -0.704  0.441   -17.604 1.00 70.15  ? 155 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 146 ? 0.408   -0.542  -17.915 1.00 72.96  ? 155 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 146 ? 1.143   -0.914  -17.006 1.00 73.14  ? 155 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 146 ? -0.142  1.839   -17.261 1.00 71.54  ? 155 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 146 ? 0.437   2.492   -18.506 1.00 72.71  ? 155 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 146 ? -1.222  2.732   -16.651 1.00 72.15  ? 155 VAL   B CG2 1 
ATOM   1377 N  N   . ILE   B 2 147 ? 0.501   -1.024  -19.166 1.00 75.30  ? 156 ILE   B N   1 
ATOM   1378 C  CA  . ILE   B 2 147 ? 1.518   -2.023  -19.514 1.00 78.26  ? 156 ILE   B CA  1 
ATOM   1379 C  C   . ILE   B 2 147 ? 2.785   -1.384  -20.154 1.00 81.00  ? 156 ILE   B C   1 
ATOM   1380 O  O   . ILE   B 2 147 ? 2.802   -0.175  -20.367 1.00 81.75  ? 156 ILE   B O   1 
ATOM   1381 C  CB  . ILE   B 2 147 ? 0.888   -3.151  -20.369 1.00 79.39  ? 156 ILE   B CB  1 
ATOM   1382 C  CG1 . ILE   B 2 147 ? 0.350   -2.622  -21.697 1.00 81.05  ? 156 ILE   B CG1 1 
ATOM   1383 C  CG2 . ILE   B 2 147 ? -0.201  -3.877  -19.582 1.00 79.86  ? 156 ILE   B CG2 1 
ATOM   1384 C  CD1 . ILE   B 2 147 ? -0.045  -3.723  -22.675 1.00 82.71  ? 156 ILE   B CD1 1 
ATOM   1385 N  N   . LYS   B 2 148 ? 3.853   -2.176  -20.410 1.00 82.38  ? 157 LYS   B N   1 
ATOM   1386 C  CA  . LYS   B 2 148 ? 5.128   -1.696  -20.977 1.00 84.40  ? 157 LYS   B CA  1 
ATOM   1387 C  C   . LYS   B 2 148 ? 5.007   -0.655  -22.103 1.00 86.09  ? 157 LYS   B C   1 
ATOM   1388 O  O   . LYS   B 2 148 ? 5.696   0.367   -22.078 1.00 86.72  ? 157 LYS   B O   1 
ATOM   1389 C  CB  . LYS   B 2 148 ? 6.003   -2.871  -21.461 1.00 86.62  ? 157 LYS   B CB  1 
ATOM   1390 C  CG  . LYS   B 2 148 ? 6.089   -4.031  -20.480 1.00 91.93  ? 157 LYS   B CG  1 
ATOM   1391 C  CD  . LYS   B 2 148 ? 7.246   -4.985  -20.805 1.00 98.08  ? 157 LYS   B CD  1 
ATOM   1392 C  CE  . LYS   B 2 148 ? 8.590   -4.426  -20.398 1.00 102.71 ? 157 LYS   B CE  1 
ATOM   1393 N  NZ  . LYS   B 2 148 ? 9.688   -5.417  -20.576 1.00 105.49 ? 157 LYS   B NZ  1 
ATOM   1394 N  N   . ASN   B 2 149 ? 4.125   -0.901  -23.077 1.00 86.37  ? 158 ASN   B N   1 
ATOM   1395 C  CA  . ASN   B 2 149 ? 3.945   -0.015  -24.225 1.00 87.12  ? 158 ASN   B CA  1 
ATOM   1396 C  C   . ASN   B 2 149 ? 3.130   1.265   -23.932 1.00 86.64  ? 158 ASN   B C   1 
ATOM   1397 O  O   . ASN   B 2 149 ? 2.773   1.983   -24.871 1.00 87.14  ? 158 ASN   B O   1 
ATOM   1398 C  CB  . ASN   B 2 149 ? 3.358   -0.765  -25.451 1.00 89.38  ? 158 ASN   B CB  1 
ATOM   1399 C  CG  . ASN   B 2 149 ? 2.604   -2.061  -25.175 1.00 93.78  ? 158 ASN   B CG  1 
ATOM   1400 O  OD1 . ASN   B 2 149 ? 3.099   -2.984  -24.523 1.00 94.88  ? 158 ASN   B OD1 1 
ATOM   1401 N  ND2 . ASN   B 2 149 ? 1.393   -2.168  -25.702 1.00 95.25  ? 158 ASN   B ND2 1 
ATOM   1402 N  N   . GLY   B 2 150 ? 2.856   1.538   -22.656 1.00 85.09  ? 159 GLY   B N   1 
ATOM   1403 C  CA  . GLY   B 2 150 ? 2.124   2.721   -22.221 1.00 83.67  ? 159 GLY   B CA  1 
ATOM   1404 C  C   . GLY   B 2 150 ? 0.615   2.625   -22.328 1.00 81.71  ? 159 GLY   B C   1 
ATOM   1405 O  O   . GLY   B 2 150 ? -0.096  3.446   -21.747 1.00 81.62  ? 159 GLY   B O   1 
ATOM   1406 N  N   . SER   B 2 151 ? 0.110   1.620   -23.076 1.00 79.56  ? 160 SER   B N   1 
ATOM   1407 C  CA  A SER   B 2 151 ? -1.322  1.385   -23.278 0.50 78.59  ? 160 SER   B CA  1 
ATOM   1408 C  CA  B SER   B 2 151 ? -1.328  1.428   -23.264 0.50 78.44  ? 160 SER   B CA  1 
ATOM   1409 C  C   . SER   B 2 151 ? -2.043  0.996   -21.968 1.00 77.01  ? 160 SER   B C   1 
ATOM   1410 O  O   . SER   B 2 151 ? -1.396  0.577   -21.005 1.00 76.98  ? 160 SER   B O   1 
ATOM   1411 C  CB  A SER   B 2 151 ? -1.522  0.294   -24.330 0.50 79.97  ? 160 SER   B CB  1 
ATOM   1412 C  CB  B SER   B 2 151 ? -1.592  0.437   -24.396 0.50 79.40  ? 160 SER   B CB  1 
ATOM   1413 O  OG  A SER   B 2 151 ? -2.885  -0.058  -24.494 0.50 82.38  ? 160 SER   B OG  1 
ATOM   1414 O  OG  B SER   B 2 151 ? -0.839  -0.753  -24.236 0.50 81.10  ? 160 SER   B OG  1 
ATOM   1415 N  N   . TYR   B 2 152 ? -3.384  1.128   -21.933 1.00 73.94  ? 161 TYR   B N   1 
ATOM   1416 C  CA  . TYR   B 2 152 ? -4.179  0.769   -20.758 1.00 71.22  ? 161 TYR   B CA  1 
ATOM   1417 C  C   . TYR   B 2 152 ? -4.924  -0.552  -20.979 1.00 67.14  ? 161 TYR   B C   1 
ATOM   1418 O  O   . TYR   B 2 152 ? -5.469  -0.783  -22.053 1.00 67.19  ? 161 TYR   B O   1 
ATOM   1419 C  CB  . TYR   B 2 152 ? -5.192  1.883   -20.439 1.00 71.63  ? 161 TYR   B CB  1 
ATOM   1420 C  CG  . TYR   B 2 152 ? -5.725  1.864   -19.017 1.00 72.81  ? 161 TYR   B CG  1 
ATOM   1421 C  CD1 . TYR   B 2 152 ? -4.946  2.305   -17.958 1.00 73.65  ? 161 TYR   B CD1 1 
ATOM   1422 C  CD2 . TYR   B 2 152 ? -7.041  1.513   -18.750 1.00 73.89  ? 161 TYR   B CD2 1 
ATOM   1423 C  CE1 . TYR   B 2 152 ? -5.439  2.335   -16.660 1.00 74.74  ? 161 TYR   B CE1 1 
ATOM   1424 C  CE2 . TYR   B 2 152 ? -7.549  1.540   -17.455 1.00 74.79  ? 161 TYR   B CE2 1 
ATOM   1425 C  CZ  . TYR   B 2 152 ? -6.741  1.944   -16.407 1.00 75.72  ? 161 TYR   B CZ  1 
ATOM   1426 O  OH  . TYR   B 2 152 ? -7.226  1.985   -15.112 1.00 77.00  ? 161 TYR   B OH  1 
ATOM   1427 N  N   . VAL   B 2 153 ? -4.954  -1.415  -19.961 1.00 63.26  ? 162 VAL   B N   1 
ATOM   1428 C  CA  . VAL   B 2 153 ? -5.716  -2.657  -20.023 1.00 59.72  ? 162 VAL   B CA  1 
ATOM   1429 C  C   . VAL   B 2 153 ? -6.661  -2.683  -18.809 1.00 55.32  ? 162 VAL   B C   1 
ATOM   1430 O  O   . VAL   B 2 153 ? -6.210  -2.783  -17.674 1.00 54.21  ? 162 VAL   B O   1 
ATOM   1431 C  CB  . VAL   B 2 153 ? -4.838  -3.922  -20.115 1.00 60.28  ? 162 VAL   B CB  1 
ATOM   1432 C  CG1 . VAL   B 2 153 ? -5.691  -5.185  -19.993 1.00 60.42  ? 162 VAL   B CG1 1 
ATOM   1433 C  CG2 . VAL   B 2 153 ? -4.046  -3.934  -21.424 1.00 61.04  ? 162 VAL   B CG2 1 
ATOM   1434 N  N   . SER   B 2 154 ? -7.954  -2.557  -19.055 1.00 52.39  ? 163 SER   B N   1 
ATOM   1435 C  CA  . SER   B 2 154 ? -8.950  -2.518  -17.987 1.00 50.36  ? 163 SER   B CA  1 
ATOM   1436 C  C   . SER   B 2 154 ? -9.525  -3.899  -17.689 1.00 49.28  ? 163 SER   B C   1 
ATOM   1437 O  O   . SER   B 2 154 ? -9.781  -4.652  -18.613 1.00 49.73  ? 163 SER   B O   1 
ATOM   1438 C  CB  . SER   B 2 154 ? -10.094 -1.592  -18.406 1.00 49.98  ? 163 SER   B CB  1 
ATOM   1439 O  OG  . SER   B 2 154 ? -11.224 -1.694  -17.552 1.00 50.19  ? 163 SER   B OG  1 
ATOM   1440 N  N   . ALA   B 2 155 ? -9.850  -4.177  -16.431 1.00 48.10  ? 164 ALA   B N   1 
ATOM   1441 C  CA  . ALA   B 2 155 ? -10.549 -5.400  -16.046 1.00 47.26  ? 164 ALA   B CA  1 
ATOM   1442 C  C   . ALA   B 2 155 ? -12.009 -5.266  -16.523 1.00 47.45  ? 164 ALA   B C   1 
ATOM   1443 O  O   . ALA   B 2 155 ? -12.501 -4.146  -16.747 1.00 47.95  ? 164 ALA   B O   1 
ATOM   1444 C  CB  . ALA   B 2 155 ? -10.549 -5.532  -14.511 1.00 47.27  ? 164 ALA   B CB  1 
ATOM   1445 N  N   . ILE   B 2 156 ? -12.702 -6.392  -16.682 1.00 46.64  ? 165 ILE   B N   1 
ATOM   1446 C  CA  . ILE   B 2 156 ? -14.135 -6.364  -16.943 1.00 46.67  ? 165 ILE   B CA  1 
ATOM   1447 C  C   . ILE   B 2 156 ? -14.676 -6.431  -15.490 1.00 45.73  ? 165 ILE   B C   1 
ATOM   1448 O  O   . ILE   B 2 156 ? -14.680 -7.519  -14.887 1.00 45.05  ? 165 ILE   B O   1 
ATOM   1449 C  CB  . ILE   B 2 156 ? -14.622 -7.571  -17.774 1.00 47.75  ? 165 ILE   B CB  1 
ATOM   1450 C  CG1 . ILE   B 2 156 ? -13.879 -7.639  -19.141 1.00 49.94  ? 165 ILE   B CG1 1 
ATOM   1451 C  CG2 . ILE   B 2 156 ? -16.145 -7.492  -17.962 1.00 47.67  ? 165 ILE   B CG2 1 
ATOM   1452 C  CD1 . ILE   B 2 156 ? -14.277 -8.769  -20.060 1.00 51.46  ? 165 ILE   B CD1 1 
ATOM   1453 N  N   . THR   B 2 157 ? -14.975 -5.260  -14.872 1.00 44.76  ? 166 THR   B N   1 
ATOM   1454 C  CA  . THR   B 2 157 ? -15.401 -5.257  -13.458 1.00 44.57  ? 166 THR   B CA  1 
ATOM   1455 C  C   . THR   B 2 157 ? -16.897 -5.490  -13.290 1.00 43.86  ? 166 THR   B C   1 
ATOM   1456 O  O   . THR   B 2 157 ? -17.686 -4.661  -13.718 1.00 43.00  ? 166 THR   B O   1 
ATOM   1457 C  CB  . THR   B 2 157 ? -15.014 -3.948  -12.768 1.00 46.04  ? 166 THR   B CB  1 
ATOM   1458 O  OG1 . THR   B 2 157 ? -13.602 -3.752  -12.854 1.00 47.20  ? 166 THR   B OG1 1 
ATOM   1459 C  CG2 . THR   B 2 157 ? -15.447 -3.924  -11.308 1.00 46.16  ? 166 THR   B CG2 1 
ATOM   1460 N  N   . GLN   B 2 158 ? -17.294 -6.582  -12.632 1.00 43.47  ? 167 GLN   B N   1 
ATOM   1461 C  CA  . GLN   B 2 158 ? -18.722 -6.876  -12.434 1.00 44.19  ? 167 GLN   B CA  1 
ATOM   1462 C  C   . GLN   B 2 158 ? -19.067 -7.013  -10.920 1.00 45.43  ? 167 GLN   B C   1 
ATOM   1463 O  O   . GLN   B 2 158 ? -18.246 -7.504  -10.155 1.00 44.04  ? 167 GLN   B O   1 
ATOM   1464 C  CB  . GLN   B 2 158 ? -19.075 -8.172  -13.207 1.00 44.47  ? 167 GLN   B CB  1 
ATOM   1465 C  CG  . GLN   B 2 158 ? -20.544 -8.620  -13.174 1.00 45.57  ? 167 GLN   B CG  1 
ATOM   1466 C  CD  . GLN   B 2 158 ? -21.512 -7.584  -13.719 1.00 45.73  ? 167 GLN   B CD  1 
ATOM   1467 O  OE1 . GLN   B 2 158 ? -21.722 -6.513  -13.127 1.00 46.46  ? 167 GLN   B OE1 1 
ATOM   1468 N  NE2 . GLN   B 2 158 ? -22.161 -7.886  -14.826 1.00 41.93  ? 167 GLN   B NE2 1 
ATOM   1469 N  N   . GLY   B 2 159 ? -20.260 -6.569  -10.516 1.00 47.18  ? 168 GLY   B N   1 
ATOM   1470 C  CA  . GLY   B 2 159 ? -20.721 -6.706  -9.143  1.00 50.75  ? 168 GLY   B CA  1 
ATOM   1471 C  C   . GLY   B 2 159 ? -21.439 -8.027  -8.920  1.00 55.77  ? 168 GLY   B C   1 
ATOM   1472 O  O   . GLY   B 2 159 ? -21.357 -8.944  -9.741  1.00 55.84  ? 168 GLY   B O   1 
ATOM   1473 N  N   . LYS   B 2 160 ? -22.145 -8.145  -7.797  1.00 59.54  ? 169 LYS   B N   1 
ATOM   1474 C  CA  . LYS   B 2 160 ? -22.908 -9.352  -7.476  1.00 62.93  ? 169 LYS   B CA  1 
ATOM   1475 C  C   . LYS   B 2 160 ? -24.378 -8.956  -7.280  1.00 65.58  ? 169 LYS   B C   1 
ATOM   1476 O  O   . LYS   B 2 160 ? -24.655 -7.948  -6.628  1.00 65.73  ? 169 LYS   B O   1 
ATOM   1477 C  CB  . LYS   B 2 160 ? -22.353 -9.996  -6.195  1.00 66.15  ? 169 LYS   B CB  1 
ATOM   1478 C  CG  . LYS   B 2 160 ? -22.977 -11.342 -5.864  1.00 72.18  ? 169 LYS   B CG  1 
ATOM   1479 C  CD  . LYS   B 2 160 ? -22.369 -11.928 -4.598  1.00 77.70  ? 169 LYS   B CD  1 
ATOM   1480 C  CE  . LYS   B 2 160 ? -22.750 -13.374 -4.401  1.00 82.14  ? 169 LYS   B CE  1 
ATOM   1481 N  NZ  . LYS   B 2 160 ? -22.064 -13.959 -3.216  1.00 84.98  ? 169 LYS   B NZ  1 
ATOM   1482 N  N   . ARG   B 2 161 ? -25.317 -9.717  -7.860  1.00 67.49  ? 170 ARG   B N   1 
ATOM   1483 C  CA  . ARG   B 2 161 ? -26.738 -9.413  -7.700  1.00 70.09  ? 170 ARG   B CA  1 
ATOM   1484 C  C   . ARG   B 2 161 ? -27.292 -10.255 -6.547  1.00 72.69  ? 170 ARG   B C   1 
ATOM   1485 O  O   . ARG   B 2 161 ? -27.376 -11.477 -6.658  1.00 72.88  ? 170 ARG   B O   1 
ATOM   1486 C  CB  . ARG   B 2 161 ? -27.517 -9.665  -9.006  1.00 71.41  ? 170 ARG   B CB  1 
ATOM   1487 C  CG  . ARG   B 2 161 ? -28.964 -9.196  -8.967  1.00 73.97  ? 170 ARG   B CG  1 
ATOM   1488 C  CD  . ARG   B 2 161 ? -29.774 -9.683  -10.159 1.00 77.21  ? 170 ARG   B CD  1 
ATOM   1489 N  NE  . ARG   B 2 161 ? -31.184 -9.310  -10.028 1.00 80.44  ? 170 ARG   B NE  1 
ATOM   1490 C  CZ  . ARG   B 2 161 ? -31.800 -8.410  -10.788 1.00 83.10  ? 170 ARG   B CZ  1 
ATOM   1491 N  NH1 . ARG   B 2 161 ? -31.153 -7.814  -11.780 1.00 82.51  ? 170 ARG   B NH1 1 
ATOM   1492 N  NH2 . ARG   B 2 161 ? -33.079 -8.123  -10.583 1.00 83.72  ? 170 ARG   B NH2 1 
ATOM   1493 N  N   . GLU   B 2 162 ? -27.615 -9.601  -5.425  1.00 74.32  ? 171 GLU   B N   1 
ATOM   1494 C  CA  . GLU   B 2 162 ? -28.150 -10.250 -4.231  1.00 76.58  ? 171 GLU   B CA  1 
ATOM   1495 C  C   . GLU   B 2 162 ? -29.568 -10.785 -4.455  1.00 77.71  ? 171 GLU   B C   1 
ATOM   1496 O  O   . GLU   B 2 162 ? -29.742 -11.957 -4.799  1.00 78.50  ? 171 GLU   B O   1 
ATOM   1497 C  CB  . GLU   B 2 162 ? -28.132 -9.268  -3.047  1.00 80.19  ? 171 GLU   B CB  1 
ATOM   1498 C  CG  . GLU   B 2 162 ? -26.733 -8.886  -2.593  1.00 87.19  ? 171 GLU   B CG  1 
ATOM   1499 C  CD  . GLU   B 2 162 ? -25.905 -10.052 -2.086  1.00 96.63  ? 171 GLU   B CD  1 
ATOM   1500 O  OE1 . GLU   B 2 162 ? -26.149 -10.503 -0.942  1.00 99.07  ? 171 GLU   B OE1 1 
ATOM   1501 O  OE2 . GLU   B 2 162 ? -25.012 -10.518 -2.834  1.00 99.02  ? 171 GLU   B OE2 1 
HETATM 1502 S  S   . DMS   C 3 .   ? -18.681 11.977  -0.293  1.00 99.18  ? 201 DMS   B S   1 
HETATM 1503 O  O   . DMS   C 3 .   ? -19.561 10.820  -0.528  1.00 99.05  ? 201 DMS   B O   1 
HETATM 1504 C  C1  . DMS   C 3 .   ? -19.625 13.404  -0.703  1.00 99.18  ? 201 DMS   B C1  1 
HETATM 1505 C  C2  . DMS   C 3 .   ? -17.609 12.100  -1.698  1.00 99.08  ? 201 DMS   B C2  1 
HETATM 1506 N  N1  . A1B86 D 4 .   ? -8.764  4.675   -13.620 1.00 80.71  ? 202 A1B86 B N1  1 
HETATM 1507 C  C4  . A1B86 D 4 .   ? -8.886  5.598   -11.333 1.00 80.08  ? 202 A1B86 B C4  1 
HETATM 1508 C  C5  . A1B86 D 4 .   ? -8.764  4.526   -12.211 1.00 80.35  ? 202 A1B86 B C5  1 
HETATM 1509 C  C6  . A1B86 D 4 .   ? -8.074  5.583   -14.350 1.00 81.14  ? 202 A1B86 B C6  1 
HETATM 1510 C  C7  . A1B86 D 4 .   ? -8.135  5.410   -15.834 1.00 81.45  ? 202 A1B86 B C7  1 
HETATM 1511 C  C8  . A1B86 D 4 .   ? -9.269  4.958   -16.504 1.00 80.83  ? 202 A1B86 B C8  1 
HETATM 1512 C  C10 . A1B86 D 4 .   ? -8.114  5.168   -18.614 1.00 81.67  ? 202 A1B86 B C10 1 
HETATM 1513 C  C13 . A1B86 D 4 .   ? -2.440  6.063   -19.498 1.00 91.17  ? 202 A1B86 B C13 1 
HETATM 1514 C  C15 . A1B86 D 4 .   ? -2.743  5.653   -21.949 1.00 93.34  ? 202 A1B86 B C15 1 
HETATM 1515 C  C17 . A1B86 D 4 .   ? -1.065  6.234   -23.556 1.00 93.95  ? 202 A1B86 B C17 1 
HETATM 1516 C  C20 . A1B86 D 4 .   ? -6.997  5.744   -16.560 1.00 82.36  ? 202 A1B86 B C20 1 
HETATM 1517 C  C21 . A1B86 D 4 .   ? -8.651  3.243   -11.694 1.00 80.18  ? 202 A1B86 B C21 1 
HETATM 1518 C  C22 . A1B86 D 4 .   ? -8.671  3.038   -10.327 1.00 79.99  ? 202 A1B86 B C22 1 
HETATM 1519 O  O1  . A1B86 D 4 .   ? -4.085  5.668   -17.372 1.00 87.90  ? 202 A1B86 B O1  1 
HETATM 1520 C  C12 . A1B86 D 4 .   ? -4.580  5.922   -18.451 1.00 87.75  ? 202 A1B86 B C12 1 
HETATM 1521 O  O2  . A1B86 D 4 .   ? -3.884  6.128   -19.585 1.00 89.61  ? 202 A1B86 B O2  1 
HETATM 1522 C  C14 . A1B86 D 4 .   ? -1.956  6.142   -20.915 1.00 92.74  ? 202 A1B86 B C14 1 
HETATM 1523 C  C19 . A1B86 D 4 .   ? -0.720  6.690   -21.227 1.00 93.46  ? 202 A1B86 B C19 1 
HETATM 1524 C  C18 . A1B86 D 4 .   ? -0.277  6.732   -22.540 1.00 93.85  ? 202 A1B86 B C18 1 
HETATM 1525 C  C16 . A1B86 D 4 .   ? -2.299  5.699   -23.261 1.00 93.67  ? 202 A1B86 B C16 1 
HETATM 1526 N  N2  . A1B86 D 4 .   ? -5.898  6.084   -18.720 1.00 85.51  ? 202 A1B86 B N2  1 
HETATM 1527 C  C11 . A1B86 D 4 .   ? -6.988  5.634   -17.945 1.00 83.11  ? 202 A1B86 B C11 1 
HETATM 1528 C  C9  . A1B86 D 4 .   ? -9.241  4.858   -17.882 1.00 80.32  ? 202 A1B86 B C9  1 
HETATM 1529 CL CL  . A1B86 D 4 .   ? -10.695 4.409   -18.729 1.00 78.59  ? 202 A1B86 B CL  1 
HETATM 1530 O  O   . A1B86 D 4 .   ? -7.380  6.464   -13.847 1.00 81.25  ? 202 A1B86 B O   1 
HETATM 1531 C  C3  . A1B86 D 4 .   ? -8.899  5.381   -9.966  1.00 79.78  ? 202 A1B86 B C3  1 
HETATM 1532 C  C2  . A1B86 D 4 .   ? -8.798  4.099   -9.444  1.00 79.82  ? 202 A1B86 B C2  1 
HETATM 1533 C  C1  . A1B86 D 4 .   ? -8.809  3.861   -7.943  1.00 79.70  ? 202 A1B86 B C1  1 
HETATM 1534 N  N   . A1B86 D 4 .   ? -9.631  2.667   -7.680  1.00 79.42  ? 202 A1B86 B N   1 
HETATM 1535 C  C   . A1B86 D 4 .   ? -9.261  5.050   -7.103  1.00 79.92  ? 202 A1B86 B C   1 
HETATM 1536 O  O   . HOH   E 5 .   ? -23.620 19.117  -19.711 1.00 60.95  ? 101 HOH   A O   1 
HETATM 1537 O  O   . HOH   E 5 .   ? -8.113  0.691   3.473   1.00 64.25  ? 102 HOH   A O   1 
HETATM 1538 O  O   . HOH   E 5 .   ? -2.038  -3.611  -6.437  1.00 55.76  ? 103 HOH   A O   1 
HETATM 1539 O  O   . HOH   E 5 .   ? -29.215 15.774  -15.182 1.00 61.85  ? 104 HOH   A O   1 
HETATM 1540 O  O   . HOH   E 5 .   ? -9.190  -6.539  -25.645 1.00 57.40  ? 105 HOH   A O   1 
HETATM 1541 O  O   . HOH   E 5 .   ? -4.318  -14.395 -25.637 1.00 47.71  ? 106 HOH   A O   1 
HETATM 1542 O  O   . HOH   E 5 .   ? -8.006  -1.593  6.777   1.00 65.15  ? 107 HOH   A O   1 
HETATM 1543 O  O   . HOH   E 5 .   ? -24.078 9.386   -27.735 1.00 47.68  ? 108 HOH   A O   1 
HETATM 1544 O  O   . HOH   E 5 .   ? -30.677 12.968  -16.699 1.00 62.91  ? 109 HOH   A O   1 
HETATM 1545 O  O   . HOH   E 5 .   ? -22.591 -9.534  -34.660 1.00 61.17  ? 110 HOH   A O   1 
HETATM 1546 O  O   . HOH   E 5 .   ? -28.495 -6.098  -28.038 1.00 59.00  ? 111 HOH   A O   1 
HETATM 1547 O  O   . HOH   E 5 .   ? -30.878 0.451   -23.111 1.00 61.01  ? 112 HOH   A O   1 
HETATM 1548 O  O   . HOH   E 5 .   ? -4.685  -9.902  -5.575  1.00 53.83  ? 113 HOH   A O   1 
HETATM 1549 O  O   . HOH   E 5 .   ? -3.664  -4.094  0.360   1.00 69.15  ? 114 HOH   A O   1 
HETATM 1550 O  O   . HOH   E 5 .   ? -4.613  2.289   -10.172 1.00 69.73  ? 115 HOH   A O   1 
HETATM 1551 O  O   . HOH   E 5 .   ? -3.863  -0.449  -0.266  1.00 62.01  ? 116 HOH   A O   1 
HETATM 1552 O  O   . HOH   E 5 .   ? -2.699  -8.762  -3.467  1.00 59.56  ? 117 HOH   A O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? -34.204 1.905   -15.468 1.00 58.29  ? 301 HOH   B O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -16.422 26.133  -12.478 1.00 75.23  ? 302 HOH   B O   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -6.258  -0.185  -11.183 1.00 46.67  ? 303 HOH   B O   1 
HETATM 1556 O  O   . HOH   F 5 .   ? -15.673 -9.863  -15.104 1.00 58.58  ? 304 HOH   B O   1 
HETATM 1557 O  O   . HOH   F 5 .   ? -30.978 12.564  -19.509 1.00 61.45  ? 305 HOH   B O   1 
HETATM 1558 O  O   . HOH   F 5 .   ? -19.432 -12.085 -25.504 1.00 63.77  ? 306 HOH   B O   1 
HETATM 1559 O  O   . HOH   F 5 .   ? -16.408 21.095  -14.338 1.00 55.19  ? 307 HOH   B O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -16.397 -7.037  -8.291  1.00 77.66  ? 308 HOH   B O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -15.054 -4.422  1.382   1.00 47.63  ? 309 HOH   B O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -17.297 13.210  -5.690  1.00 59.10  ? 310 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -5.536  2.982   -13.235 1.00 80.96  ? 311 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -12.998 -2.068  -14.902 1.00 42.18  ? 312 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -23.153 -6.165  -5.227  1.00 75.33  ? 313 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -7.013  -10.576 -5.236  1.00 55.08  ? 314 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -27.856 -6.087  -18.580 1.00 56.94  ? 315 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -17.938 -10.605 -16.587 1.00 49.47  ? 316 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -26.147 -7.880  -16.591 1.00 44.52  ? 317 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -12.453 -3.189  -10.147 1.00 46.46  ? 318 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -27.493 -6.711  -5.426  1.00 73.22  ? 319 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -6.914  -8.854  -3.062  1.00 51.03  ? 320 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -20.598 -7.053  -5.382  1.00 71.35  ? 321 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -22.147 15.272  -6.210  1.00 53.49  ? 322 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -16.219 -14.581 -16.592 1.00 57.15  ? 323 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -7.387  -6.435  0.496   1.00 61.72  ? 324 HOH   B O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -18.875 14.993  -22.307 1.00 48.26  ? 325 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -20.915 6.061   -33.077 1.00 67.84  ? 326 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -32.553 -6.766  -6.897  1.00 62.90  ? 327 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -2.785  -11.504 -7.043  1.00 50.85  ? 328 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -23.834 -14.689 -17.930 1.00 66.05  ? 329 HOH   B O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -25.961 -4.229  -4.024  1.00 44.82  ? 330 HOH   B O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -10.922 12.439  -19.175 1.00 62.15  ? 331 HOH   B O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -15.523 9.508   -0.627  1.00 54.21  ? 332 HOH   B O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -32.238 7.578   -4.806  1.00 66.43  ? 333 HOH   B O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -21.265 7.385   -0.000  0.50 52.27  ? 334 HOH   B O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -18.716 25.635  -14.719 1.00 69.81  ? 335 HOH   B O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -29.516 -1.406  -19.015 1.00 66.01  ? 336 HOH   B O   1 
HETATM 1589 O  O   . HOH   F 5 .   ? -30.616 4.811   -2.363  1.00 60.72  ? 337 HOH   B O   1 
HETATM 1590 O  O   . HOH   F 5 .   ? -16.278 -14.375 -30.868 1.00 66.08  ? 338 HOH   B O   1 
HETATM 1591 O  O   . HOH   F 5 .   ? -14.675 -12.287 -16.514 1.00 53.08  ? 339 HOH   B O   1 
HETATM 1592 O  O   . HOH   F 5 .   ? -15.037 16.696  -20.466 1.00 61.93  ? 340 HOH   B O   1 
HETATM 1593 O  O   . HOH   F 5 .   ? -8.631  -10.436 -7.492  1.00 77.05  ? 341 HOH   B O   1 
HETATM 1594 O  O   . HOH   F 5 .   ? -19.603 -13.376 -23.226 1.00 51.50  ? 342 HOH   B O   1 
HETATM 1595 O  O   . HOH   F 5 .   ? -11.643 -4.948  -8.370  1.00 54.76  ? 343 HOH   B O   1 
HETATM 1596 O  O   . HOH   F 5 .   ? -17.431 14.902  -31.152 1.00 65.42  ? 344 HOH   B O   1 
HETATM 1597 O  O   . HOH   F 5 .   ? -21.374 -12.122 -13.012 1.00 54.43  ? 345 HOH   B O   1 
HETATM 1598 O  O   . HOH   F 5 .   ? -19.505 -5.627  -0.756  1.00 58.03  ? 346 HOH   B O   1 
HETATM 1599 O  O   . HOH   F 5 .   ? -14.613 -6.380  -1.510  1.00 69.44  ? 347 HOH   B O   1 
HETATM 1600 O  O   . HOH   F 5 .   ? -30.246 -7.492  -5.346  1.00 73.84  ? 348 HOH   B O   1 
HETATM 1601 O  O   . HOH   F 5 .   ? -17.206 16.774  -22.075 1.00 60.23  ? 349 HOH   B O   1 
HETATM 1602 O  O   . HOH   F 5 .   ? -30.687 -10.015 -27.973 1.00 66.72  ? 350 HOH   B O   1 
HETATM 1603 O  O   . HOH   F 5 .   ? -10.092 -16.083 -24.537 1.00 59.80  ? 351 HOH   B O   1 
HETATM 1604 O  O   . HOH   F 5 .   ? -35.411 1.090   -7.549  1.00 72.84  ? 352 HOH   B O   1 
HETATM 1605 O  O   . HOH   F 5 .   ? -29.710 -5.241  -0.851  1.00 53.45  ? 353 HOH   B O   1 
HETATM 1606 O  O   . HOH   F 5 .   ? -0.214  0.586   -13.136 1.00 70.31  ? 354 HOH   B O   1 
HETATM 1607 O  O   . HOH   F 5 .   ? -0.720  -14.380 -10.082 1.00 70.32  ? 355 HOH   B O   1 
HETATM 1608 O  O   . HOH   F 5 .   ? -18.921 -11.792 -13.567 1.00 55.52  ? 356 HOH   B O   1 
HETATM 1609 O  O   . HOH   F 5 .   ? -11.329 -6.838  1.957   1.00 63.80  ? 357 HOH   B O   1 
HETATM 1610 O  O   . HOH   F 5 .   ? -21.265 4.345   -0.000  0.50 67.86  ? 358 HOH   B O   1 
HETATM 1611 O  O   . HOH   F 5 .   ? -11.469 14.377  -14.001 1.00 76.93  ? 359 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   ? 0.9793 0.5150 0.9238 0.1494  0.1030  -0.1227 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.9742 0.5536 0.8900 0.1773  0.1026  -0.1153 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.9542 0.5415 0.8605 0.1775  0.1156  -0.0774 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.9864 0.5208 0.8822 0.1863  0.1265  -0.0531 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.0299 0.5822 0.9231 0.2149  0.0968  -0.1298 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.1175 0.7234 1.0054 0.2288  0.0849  -0.1639 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.1632 0.7403 1.0437 0.2502  0.0768  -0.1905 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.1256 0.7995 1.0151 0.2190  0.0850  -0.1641 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.8995 0.5493 0.8061 0.1691  0.1145  -0.0724 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.8684 0.5309 0.7640 0.1713  0.1236  -0.0419 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.8504 0.5320 0.7214 0.2039  0.1189  -0.0398 51  MET   A C   
12   O  O   . MET   A 8   ? 0.8446 0.5583 0.7142 0.2176  0.1095  -0.0628 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.8395 0.5526 0.7479 0.1474  0.1235  -0.0380 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.8457 0.5430 0.7810 0.1186  0.1297  -0.0328 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.8459 0.6051 0.7911 0.0987  0.1267  -0.0293 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.8646 0.6066 0.8517 0.0677  0.1323  -0.0295 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.8403 0.5027 0.6921 0.2187  0.1256  -0.0137 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.8395 0.5208 0.6692 0.2522  0.1179  -0.0127 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.8234 0.5218 0.6387 0.2552  0.1208  0.0099  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.8277 0.5061 0.6426 0.2383  0.1332  0.0312  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.8763 0.5028 0.6846 0.2861  0.1165  -0.0116 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.9380 0.4913 0.7260 0.2901  0.1314  0.0198  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.9741 0.4680 0.7750 0.2707  0.1424  0.0230  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.9772 0.5182 0.7315 0.3160  0.1347  0.0451  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 1.0251 0.4478 0.8089 0.2730  0.1605  0.0547  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 1.0270 0.4981 0.7561 0.3226  0.1525  0.0777  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 1.0604 0.4716 0.8058 0.2993  0.1675  0.0843  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.1239 0.4647 0.8482 0.3012  0.1902  0.1200  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.7987 0.5371 0.6045 0.2774  0.1089  0.0034  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.7893 0.5448 0.5795 0.2833  0.1074  0.0194  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.8168 0.5508 0.5726 0.3262  0.1005  0.0286  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.8139 0.5438 0.5656 0.3528  0.0913  0.0152  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.7514 0.5734 0.5619 0.2675  0.0976  0.0040  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.7387 0.6053 0.5632 0.2840  0.0840  -0.0215 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.7386 0.5749 0.5715 0.2300  0.1047  0.0008  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.7251 0.6546 0.5722 0.2665  0.0769  -0.0337 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.8332 0.5538 0.5613 0.3363  0.1046  0.0508  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.8627 0.5626 0.5484 0.3808  0.0971  0.0620  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.8608 0.5991 0.5353 0.3860  0.0869  0.0620  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.8537 0.5921 0.5302 0.3622  0.0989  0.0751  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.9269 0.5513 0.5759 0.3918  0.1187  0.0966  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 1.0327 0.5997 0.6827 0.3947  0.1279  0.0997  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.1725 0.6600 0.7859 0.4046  0.1521  0.1378  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.2214 0.7039 0.8176 0.3985  0.1678  0.1628  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.2161 0.6441 0.8186 0.4179  0.1573  0.1430  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.8620 0.6309 0.5238 0.4196  0.0640  0.0467  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.8695 0.6719 0.5209 0.4252  0.0509  0.0423  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.9008 0.6599 0.5010 0.4421  0.0644  0.0731  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.9330 0.6399 0.4925 0.4702  0.0754  0.0960  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8909 0.7407 0.5466 0.4561  0.0204  0.0145  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.9259 0.8254 0.5992 0.4427  0.0037  -0.0034 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.9447 0.9051 0.6472 0.4589  -0.0263 -0.0384 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.9542 0.9539 0.6764 0.4420  -0.0419 -0.0561 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.9843 0.9841 0.6733 0.4701  -0.0609 -0.0608 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 1.0203 0.9849 0.6506 0.5179  -0.0647 -0.0463 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.9501 0.9801 0.6602 0.4516  -0.0756 -0.0795 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.8916 0.6693 0.4919 0.4259  0.0659  0.0752  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.9362 0.6807 0.4882 0.4432  0.0809  0.1030  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.9527 0.7237 0.4754 0.4698  0.0592  0.0909  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.9965 0.7407 0.4678 0.4960  0.0696  0.1125  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.9409 0.6722 0.5115 0.4050  0.1086  0.1221  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.9155 0.7374 0.4699 0.4641  0.0305  0.0564  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.9144 0.7606 0.4457 0.4890  0.0052  0.0386  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.8808 0.7793 0.4636 0.4614  -0.0181 0.0037  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.8523 0.7706 0.4868 0.4229  -0.0124 -0.0045 57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.8813 0.8008 0.4485 0.4826  -0.0450 -0.0179 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.8596 0.8223 0.4738 0.4569  -0.0681 -0.0514 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8880 0.8346 0.5012 0.4290  -0.0544 -0.0416 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.9270 0.8401 0.4934 0.4453  -0.0373 -0.0172 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.8641 0.8510 0.4595 0.4942  -0.1058 -0.0816 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.9224 0.9445 0.5351 0.5201  -0.1301 -0.1044 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.9052 0.9262 0.5350 0.5156  -0.1158 -0.0935 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.9567 1.0072 0.5625 0.5499  -0.1655 -0.1348 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.8652 0.8358 0.5273 0.3904  -0.0620 -0.0605 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8879 0.8414 0.5466 0.3688  -0.0532 -0.0539 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.9057 0.8668 0.5530 0.3839  -0.0831 -0.0816 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8786 0.8672 0.5695 0.3644  -0.1048 -0.1107 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.8738 0.8365 0.5828 0.3197  -0.0396 -0.0517 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8857 0.8347 0.5965 0.3098  -0.0111 -0.0253 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.8874 0.8344 0.5950 0.3002  -0.0378 -0.0508 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8760 0.8396 0.6306 0.2708  -0.0011 -0.0265 59  ILE   A CD1 
82   N  N   . THR   A 17  ? 0.9509 0.8889 0.5391 0.4214  -0.0848 -0.0742 60  THR   A N   
83   C  CA  . THR   A 17  ? 0.9855 0.9259 0.5521 0.4437  -0.1152 -0.1028 60  THR   A CA  
84   C  C   . THR   A 17  ? 1.0491 0.9582 0.5606 0.4653  -0.1030 -0.0875 60  THR   A C   
85   O  O   . THR   A 17  ? 1.0731 0.9623 0.5474 0.4811  -0.0736 -0.0537 60  THR   A O   
86   C  CB  . THR   A 17  ? 1.0025 0.9649 0.5494 0.4863  -0.1478 -0.1283 60  THR   A CB  
87   O  OG1 . THR   A 17  ? 1.0725 1.0113 0.5433 0.5384  -0.1404 -0.1082 60  THR   A OG1 
88   C  CG2 . THR   A 17  ? 0.9511 0.9486 0.5463 0.4756  -0.1556 -0.1392 60  THR   A CG2 
89   N  N   . TRP   A 18  ? 1.0753 0.9804 0.5819 0.4679  -0.1258 -0.1137 61  TRP   A N   
90   C  CA  . TRP   A 18  ? 1.1420 1.0217 0.5935 0.4954  -0.1181 -0.1051 61  TRP   A CA  
91   C  C   . TRP   A 18  ? 1.2157 1.0931 0.5979 0.5548  -0.1274 -0.1058 61  TRP   A C   
92   O  O   . TRP   A 18  ? 1.2200 1.1158 0.6004 0.5758  -0.1606 -0.1348 61  TRP   A O   
93   C  CB  . TRP   A 18  ? 1.1369 1.0084 0.6016 0.4844  -0.1443 -0.1379 61  TRP   A CB  
94   C  CG  . TRP   A 18  ? 1.1724 1.0195 0.5817 0.5153  -0.1392 -0.1346 61  TRP   A CG  
95   C  CD1 . TRP   A 18  ? 1.2085 1.0496 0.5597 0.5647  -0.1613 -0.1557 61  TRP   A CD1 
96   C  CD2 . TRP   A 18  ? 1.1824 1.0112 0.5921 0.4999  -0.1141 -0.1144 61  TRP   A CD2 
97   N  NE1 . TRP   A 18  ? 1.2352 1.0552 0.5492 0.5816  -0.1484 -0.1484 61  TRP   A NE1 
98   C  CE2 . TRP   A 18  ? 1.2188 1.0323 0.5704 0.5422  -0.1199 -0.1233 61  TRP   A CE2 
99   C  CE3 . TRP   A 18  ? 1.1731 0.9996 0.6239 0.4585  -0.0879 -0.0904 61  TRP   A CE3 
100  C  CZ2 . TRP   A 18  ? 1.2353 1.0339 0.5743 0.5432  -0.1000 -0.1095 61  TRP   A CZ2 
101  C  CZ3 . TRP   A 18  ? 1.1917 1.0033 0.6298 0.4597  -0.0710 -0.0776 61  TRP   A CZ3 
102  C  CH2 . TRP   A 18  ? 1.2164 1.0154 0.6011 0.5015  -0.0763 -0.0867 61  TRP   A CH2 
103  N  N   . GLU   A 19  ? 1.2709 1.1286 0.5970 0.5829  -0.0973 -0.0732 62  GLU   A N   
104  C  CA  . GLU   A 19  ? 1.3397 1.1903 0.5895 0.6426  -0.1012 -0.0683 62  GLU   A CA  
105  C  C   . GLU   A 19  ? 1.4086 1.2471 0.6018 0.6779  -0.1060 -0.0782 62  GLU   A C   
106  O  O   . GLU   A 19  ? 1.4136 1.2411 0.6005 0.6694  -0.0759 -0.0560 62  GLU   A O   
107  C  CB  . GLU   A 19  ? 1.3831 1.2190 0.6049 0.6543  -0.0613 -0.0211 62  GLU   A CB  
108  C  CG  . GLU   A 19  ? 1.4328 1.2773 0.7068 0.6241  -0.0584 -0.0142 62  GLU   A CG  
109  C  CD  . GLU   A 19  ? 1.5510 1.4150 0.8290 0.6449  -0.0951 -0.0422 62  GLU   A CD  
110  O  OE1 . GLU   A 19  ? 1.6158 1.4821 0.8388 0.6951  -0.1213 -0.0603 62  GLU   A OE1 
111  O  OE2 . GLU   A 19  ? 1.5458 1.4257 0.8807 0.6139  -0.0977 -0.0466 62  GLU   A OE2 
112  N  N   . LYS   A 20  ? 1.4576 1.3016 0.6135 0.7179  -0.1468 -0.1160 63  LYS   A N   
113  C  CA  . LYS   A 20  ? 1.5259 1.3582 0.6212 0.7587  -0.1575 -0.1328 63  LYS   A CA  
114  C  C   . LYS   A 20  ? 1.5800 1.3987 0.5956 0.8042  -0.1182 -0.0907 63  LYS   A C   
115  O  O   . LYS   A 20  ? 1.5956 1.4120 0.5798 0.8268  -0.1059 -0.0662 63  LYS   A O   
116  C  CB  . LYS   A 20  ? 1.5831 1.4265 0.6544 0.7952  -0.2135 -0.1856 63  LYS   A CB  
117  C  CG  . LYS   A 20  ? 1.6385 1.4904 0.7819 0.7543  -0.2536 -0.2341 63  LYS   A CG  
118  C  CD  . LYS   A 20  ? 1.7084 1.5786 0.8386 0.7879  -0.3104 -0.2879 63  LYS   A CD  
119  C  CE  . LYS   A 20  ? 1.7343 1.6144 0.9453 0.7426  -0.3492 -0.3363 63  LYS   A CE  
120  N  NZ  . LYS   A 20  ? 1.7605 1.6655 0.9671 0.7741  -0.4062 -0.3918 63  LYS   A NZ  
121  N  N   . ASP   A 21  ? 1.6052 1.4142 0.5873 0.8191  -0.0975 -0.0816 64  ASP   A N   
122  C  CA  . ASP   A 21  ? 1.6457 1.4461 0.5554 0.8601  -0.0540 -0.0396 64  ASP   A CA  
123  C  C   . ASP   A 21  ? 1.6246 1.4210 0.5609 0.8304  -0.0044 0.0144  64  ASP   A C   
124  O  O   . ASP   A 21  ? 1.6460 1.4309 0.5312 0.8611  0.0172  0.0458  64  ASP   A O   
125  C  CB  . ASP   A 21  ? 1.7296 1.5252 0.5429 0.9328  -0.0732 -0.0504 64  ASP   A CB  
126  C  CG  . ASP   A 21  ? 1.8434 1.6400 0.6166 0.9701  -0.1133 -0.0998 64  ASP   A CG  
127  O  OD1 . ASP   A 21  ? 1.8739 1.6677 0.6524 0.9632  -0.1006 -0.1033 64  ASP   A OD1 
128  O  OD2 . ASP   A 21  ? 1.8816 1.6821 0.6191 1.0077  -0.1595 -0.1376 64  ASP   A OD2 
129  N  N   . ALA   A 22  ? 1.5770 1.3796 0.5935 0.7705  0.0108  0.0230  65  ALA   A N   
130  C  CA  . ALA   A 22  ? 1.5496 1.3493 0.6025 0.7357  0.0557  0.0681  65  ALA   A CA  
131  C  C   . ALA   A 22  ? 1.5374 1.3410 0.5720 0.7428  0.1017  0.0994  65  ALA   A C   
132  O  O   . ALA   A 22  ? 1.5427 1.3532 0.5492 0.7672  0.0938  0.0809  65  ALA   A O   
133  C  CB  . ALA   A 22  ? 1.5189 1.3278 0.6624 0.6727  0.0463  0.0569  65  ALA   A CB  
134  N  N   . GLU   A 23  ? 1.5170 1.3179 0.5703 0.7219  0.1492  0.1443  66  GLU   A N   
135  C  CA  . GLU   A 23  ? 1.5062 1.3200 0.5557 0.7238  0.1952  0.1736  66  GLU   A CA  
136  C  C   . GLU   A 23  ? 1.4536 1.2899 0.5647 0.6895  0.1857  0.1517  66  GLU   A C   
137  O  O   . GLU   A 23  ? 1.4160 1.2552 0.5949 0.6417  0.1743  0.1436  66  GLU   A O   
138  C  CB  . GLU   A 23  ? 1.5427 1.3493 0.6180 0.6975  0.2447  0.2221  66  GLU   A CB  
139  C  CG  . GLU   A 23  ? 1.6228 1.4517 0.7091 0.6932  0.2943  0.2517  66  GLU   A CG  
140  C  CD  . GLU   A 23  ? 1.7136 1.5473 0.8714 0.6414  0.3324  0.2834  66  GLU   A CD  
141  O  OE1 . GLU   A 23  ? 1.7425 1.5518 0.9238 0.6167  0.3278  0.2912  66  GLU   A OE1 
142  O  OE2 . GLU   A 23  ? 1.7282 1.5920 0.9200 0.6269  0.3659  0.2983  66  GLU   A OE2 
143  N  N   . VAL   A 24  ? 1.4472 1.2971 0.5292 0.7183  0.1879  0.1403  67  VAL   A N   
144  C  CA  . VAL   A 24  ? 1.4177 1.2838 0.5496 0.6934  0.1772  0.1196  67  VAL   A CA  
145  C  C   . VAL   A 24  ? 1.3866 1.2822 0.5495 0.6807  0.2259  0.1513  67  VAL   A C   
146  O  O   . VAL   A 24  ? 1.4005 1.3093 0.5175 0.7182  0.2565  0.1692  67  VAL   A O   
147  C  CB  . VAL   A 24  ? 1.4470 1.3069 0.5338 0.7328  0.1418  0.0793  67  VAL   A CB  
148  C  CG1 . VAL   A 24  ? 1.4315 1.2966 0.5698 0.7055  0.1255  0.0571  67  VAL   A CG1 
149  C  CG2 . VAL   A 24  ? 1.4770 1.3134 0.5303 0.7512  0.0946  0.0462  67  VAL   A CG2 
150  N  N   . THR   A 25  ? 1.3418 1.2519 0.5830 0.6294  0.2336  0.1577  68  THR   A N   
151  C  CA  . THR   A 25  ? 1.3056 1.2516 0.5885 0.6140  0.2762  0.1833  68  THR   A CA  
152  C  C   . THR   A 25  ? 1.2557 1.2186 0.6159 0.5692  0.2626  0.1694  68  THR   A C   
153  O  O   . THR   A 25  ? 1.2547 1.1971 0.6283 0.5523  0.2238  0.1433  68  THR   A O   
154  C  CB  . THR   A 25  ? 1.3239 1.2715 0.6115 0.6036  0.3228  0.2269  68  THR   A CB  
155  O  OG1 . THR   A 25  ? 1.3175 1.3064 0.6343 0.6009  0.3661  0.2487  68  THR   A OG1 
156  C  CG2 . THR   A 25  ? 1.3131 1.2449 0.6558 0.5541  0.3180  0.2341  68  THR   A CG2 
157  N  N   . GLY   A 26  ? 1.2160 1.2179 0.6242 0.5533  0.2940  0.1859  69  GLY   A N   
158  C  CA  . GLY   A 26  ? 1.1857 1.2069 0.6615 0.5171  0.2814  0.1737  69  GLY   A CA  
159  C  C   . GLY   A 26  ? 1.1774 1.2116 0.6471 0.5399  0.2621  0.1489  69  GLY   A C   
160  O  O   . GLY   A 26  ? 1.2084 1.2152 0.6257 0.5715  0.2344  0.1258  69  GLY   A O   
161  N  N   . ASN   A 27  ? 1.1287 1.2038 0.6529 0.5252  0.2747  0.1514  70  ASN   A N   
162  C  CA  . ASN   A 27  ? 1.1145 1.2011 0.6366 0.5476  0.2558  0.1286  70  ASN   A CA  
163  C  C   . ASN   A 27  ? 1.0889 1.1473 0.6363 0.5194  0.2150  0.1072  70  ASN   A C   
164  O  O   . ASN   A 27  ? 1.0832 1.1188 0.6479 0.4846  0.2041  0.1098  70  ASN   A O   
165  C  CB  . ASN   A 27  ? 1.1052 1.2567 0.6678 0.5562  0.2907  0.1412  70  ASN   A CB  
166  C  CG  . ASN   A 27  ? 1.1250 1.3130 0.7696 0.5118  0.2988  0.1489  70  ASN   A CG  
167  O  OD1 . ASN   A 27  ? 1.1442 1.3241 0.8195 0.4731  0.3066  0.1628  70  ASN   A OD1 
168  N  ND2 . ASN   A 27  ? 1.1065 1.3361 0.7875 0.5195  0.2951  0.1376  70  ASN   A ND2 
169  N  N   . SER   A 28  ? 1.0725 1.1282 0.6162 0.5374  0.1931  0.0868  71  SER   A N   
170  C  CA  . SER   A 28  ? 1.0700 1.0922 0.6268 0.5163  0.1570  0.0696  71  SER   A CA  
171  C  C   . SER   A 28  ? 1.0271 1.0847 0.6257 0.5155  0.1568  0.0674  71  SER   A C   
172  O  O   . SER   A 28  ? 1.0421 1.0855 0.6194 0.5438  0.1378  0.0506  71  SER   A O   
173  C  CB  . SER   A 28  ? 1.1353 1.1015 0.6370 0.5417  0.1232  0.0442  71  SER   A CB  
174  O  OG  . SER   A 28  ? 1.2109 1.1570 0.6662 0.5604  0.1232  0.0408  71  SER   A OG  
175  N  N   . PRO   A 29  ? 0.9728 1.0763 0.6308 0.4858  0.1756  0.0820  72  PRO   A N   
176  C  CA  . PRO   A 29  ? 0.9302 1.0768 0.6299 0.4899  0.1735  0.0771  72  PRO   A CA  
177  C  C   . PRO   A 29  ? 0.9193 1.0306 0.6185 0.4780  0.1377  0.0639  72  PRO   A C   
178  O  O   . PRO   A 29  ? 0.9240 0.9960 0.6187 0.4474  0.1236  0.0649  72  PRO   A O   
179  C  CB  . PRO   A 29  ? 0.9022 1.1072 0.6676 0.4585  0.2037  0.0945  72  PRO   A CB  
180  C  CG  . PRO   A 29  ? 0.9252 1.0926 0.6843 0.4241  0.2053  0.1049  72  PRO   A CG  
181  C  CD  . PRO   A 29  ? 0.9477 1.0659 0.6384 0.4496  0.1982  0.1014  72  PRO   A CD  
182  N  N   . ARG   A 30  ? 0.9027 1.0271 0.6037 0.5048  0.1240  0.0525  73  ARG   A N   
183  C  CA  . ARG   A 30  ? 0.9216 1.0112 0.6176 0.4975  0.0926  0.0440  73  ARG   A CA  
184  C  C   . ARG   A 30  ? 0.8648 1.0184 0.6216 0.4840  0.0975  0.0469  73  ARG   A C   
185  O  O   . ARG   A 30  ? 0.8372 1.0479 0.6207 0.5097  0.1066  0.0427  73  ARG   A O   
186  C  CB  . ARG   A 30  ? 0.9900 1.0373 0.6387 0.5396  0.0690  0.0285  73  ARG   A CB  
187  C  CG  . ARG   A 30  ? 1.1022 1.0818 0.6932 0.5513  0.0579  0.0197  73  ARG   A CG  
188  C  CD  . ARG   A 30  ? 1.2060 1.1328 0.7515 0.5897  0.0316  0.0022  73  ARG   A CD  
189  N  NE  . ARG   A 30  ? 1.2957 1.1748 0.7915 0.6105  0.0238  -0.0121 73  ARG   A NE  
190  C  CZ  . ARG   A 30  ? 1.3497 1.1598 0.8180 0.5912  0.0036  -0.0197 73  ARG   A CZ  
191  N  NH1 . ARG   A 30  ? 1.3664 1.1465 0.8499 0.5505  -0.0070 -0.0113 73  ARG   A NH1 
192  N  NH2 . ARG   A 30  ? 1.3446 1.1183 0.7711 0.6132  -0.0063 -0.0373 73  ARG   A NH2 
193  N  N   . LEU   A 31  ? 0.8404 0.9896 0.6215 0.4445  0.0918  0.0521  74  LEU   A N   
194  C  CA  . LEU   A 31  ? 0.7949 1.0051 0.6364 0.4271  0.0945  0.0515  74  LEU   A CA  
195  C  C   . LEU   A 31  ? 0.7938 0.9812 0.6274 0.4207  0.0645  0.0452  74  LEU   A C   
196  O  O   . LEU   A 31  ? 0.8234 0.9517 0.6235 0.4017  0.0522  0.0489  74  LEU   A O   
197  C  CB  . LEU   A 31  ? 0.7776 1.0087 0.6588 0.3853  0.1173  0.0624  74  LEU   A CB  
198  C  CG  . LEU   A 31  ? 0.7868 1.0355 0.6726 0.3876  0.1512  0.0745  74  LEU   A CG  
199  C  CD1 . LEU   A 31  ? 0.7784 1.0303 0.6950 0.3469  0.1700  0.0865  74  LEU   A CD1 
200  C  CD2 . LEU   A 31  ? 0.7585 1.0785 0.6815 0.4124  0.1721  0.0736  74  LEU   A CD2 
201  N  N   . ASP   A 32  ? 0.7541 0.9936 0.6216 0.4351  0.0542  0.0362  75  ASP   A N   
202  C  CA  . ASP   A 32  ? 0.7579 0.9804 0.6145 0.4324  0.0262  0.0313  75  ASP   A CA  
203  C  C   . ASP   A 32  ? 0.7063 0.9598 0.6085 0.3907  0.0312  0.0312  75  ASP   A C   
204  O  O   . ASP   A 32  ? 0.6600 0.9856 0.6269 0.3810  0.0443  0.0254  75  ASP   A O   
205  C  CB  . ASP   A 32  ? 0.7760 1.0455 0.6487 0.4705  0.0094  0.0188  75  ASP   A CB  
206  C  CG  . ASP   A 32  ? 0.9145 1.1439 0.7351 0.5176  -0.0024 0.0162  75  ASP   A CG  
207  O  OD1 . ASP   A 32  ? 0.9820 1.1341 0.7470 0.5180  -0.0039 0.0229  75  ASP   A OD1 
208  O  OD2 . ASP   A 32  ? 0.9426 1.2187 0.7801 0.5550  -0.0116 0.0052  75  ASP   A OD2 
209  N  N   . VAL   A 33  ? 0.7099 0.9109 0.5821 0.3655  0.0222  0.0367  76  VAL   A N   
210  C  CA  . VAL   A 33  ? 0.6766 0.9010 0.5864 0.3285  0.0256  0.0342  76  VAL   A CA  
211  C  C   . VAL   A 33  ? 0.6897 0.8910 0.5726 0.3255  0.0002  0.0300  76  VAL   A C   
212  O  O   . VAL   A 33  ? 0.7304 0.8833 0.5583 0.3471  -0.0164 0.0348  76  VAL   A O   
213  C  CB  . VAL   A 33  ? 0.6861 0.8813 0.5946 0.2965  0.0472  0.0447  76  VAL   A CB  
214  C  CG1 . VAL   A 33  ? 0.6803 0.8976 0.6089 0.3013  0.0741  0.0514  76  VAL   A CG1 
215  C  CG2 . VAL   A 33  ? 0.7262 0.8461 0.5736 0.2929  0.0388  0.0527  76  VAL   A CG2 
216  N  N   . ALA   A 34  ? 0.6505 0.8845 0.5706 0.3000  -0.0020 0.0212  77  ALA   A N   
217  C  CA  . ALA   A 34  ? 0.6553 0.8743 0.5510 0.2957  -0.0229 0.0161  77  ALA   A CA  
218  C  C   . ALA   A 34  ? 0.6443 0.8490 0.5502 0.2577  -0.0117 0.0169  77  ALA   A C   
219  O  O   . ALA   A 34  ? 0.6202 0.8526 0.5751 0.2354  0.0063  0.0141  77  ALA   A O   
220  C  CB  . ALA   A 34  ? 0.6248 0.9094 0.5594 0.3099  -0.0432 -0.0038 77  ALA   A CB  
221  N  N   . LEU   A 35  ? 0.6602 0.8204 0.5187 0.2517  -0.0204 0.0219  78  LEU   A N   
222  C  CA  . LEU   A 35  ? 0.6570 0.8037 0.5200 0.2207  -0.0115 0.0210  78  LEU   A CA  
223  C  C   . LEU   A 35  ? 0.6558 0.8205 0.5130 0.2213  -0.0312 0.0066  78  LEU   A C   
224  O  O   . LEU   A 35  ? 0.6857 0.8330 0.4954 0.2441  -0.0485 0.0099  78  LEU   A O   
225  C  CB  . LEU   A 35  ? 0.6900 0.7732 0.5036 0.2132  -0.0016 0.0382  78  LEU   A CB  
226  C  CG  . LEU   A 35  ? 0.7036 0.7713 0.5163 0.1858  0.0078  0.0379  78  LEU   A CG  
227  C  CD1 . LEU   A 35  ? 0.6835 0.7738 0.5459 0.1658  0.0243  0.0330  78  LEU   A CD1 
228  C  CD2 . LEU   A 35  ? 0.7404 0.7535 0.5082 0.1810  0.0146  0.0530  78  LEU   A CD2 
229  N  N   . ASP   A 36  ? 0.6162 0.8160 0.5207 0.1998  -0.0302 -0.0103 79  ASP   A N   
230  C  CA  . ASP   A 36  ? 0.6119 0.8328 0.5125 0.2022  -0.0517 -0.0294 79  ASP   A CA  
231  C  C   . ASP   A 36  ? 0.6397 0.8228 0.5035 0.1863  -0.0461 -0.0265 79  ASP   A C   
232  O  O   . ASP   A 36  ? 0.6550 0.8035 0.5100 0.1698  -0.0257 -0.0121 79  ASP   A O   
233  C  CB  . ASP   A 36  ? 0.5776 0.8639 0.5540 0.1920  -0.0606 -0.0565 79  ASP   A CB  
234  C  CG  . ASP   A 36  ? 0.5969 0.8887 0.6274 0.1568  -0.0412 -0.0623 79  ASP   A CG  
235  O  OD1 . ASP   A 36  ? 0.6038 0.8502 0.6086 0.1420  -0.0239 -0.0485 79  ASP   A OD1 
236  O  OD2 . ASP   A 36  ? 0.5915 0.9328 0.6918 0.1442  -0.0432 -0.0808 79  ASP   A OD2 
237  N  N   . GLU   A 37  ? 0.6480 0.8408 0.4885 0.1948  -0.0651 -0.0411 80  GLU   A N   
238  C  CA  . GLU   A 37  ? 0.6731 0.8393 0.4772 0.1850  -0.0609 -0.0415 80  GLU   A CA  
239  C  C   . GLU   A 37  ? 0.6449 0.8120 0.4929 0.1545  -0.0450 -0.0507 80  GLU   A C   
240  O  O   . GLU   A 37  ? 0.6676 0.8052 0.4883 0.1447  -0.0326 -0.0438 80  GLU   A O   
241  C  CB  . GLU   A 37  ? 0.7173 0.9048 0.4931 0.2047  -0.0870 -0.0609 80  GLU   A CB  
242  C  CG  . GLU   A 37  ? 0.8494 1.0047 0.5639 0.2059  -0.0812 -0.0545 80  GLU   A CG  
243  C  CD  . GLU   A 37  ? 0.9510 1.1243 0.6244 0.2312  -0.1065 -0.0721 80  GLU   A CD  
244  O  OE1 . GLU   A 37  ? 0.9331 1.1335 0.6297 0.2247  -0.1183 -0.1020 80  GLU   A OE1 
245  O  OE2 . GLU   A 37  ? 1.0239 1.1812 0.6390 0.2596  -0.1155 -0.0567 80  GLU   A OE2 
246  N  N   . SER   A 38  ? 0.6014 0.7999 0.5170 0.1400  -0.0429 -0.0637 81  SER   A N   
247  C  CA  . SER   A 38  ? 0.5920 0.7825 0.5466 0.1128  -0.0264 -0.0689 81  SER   A CA  
248  C  C   . SER   A 38  ? 0.5848 0.7442 0.5391 0.1035  0.0001  -0.0434 81  SER   A C   
249  O  O   . SER   A 38  ? 0.5766 0.7238 0.5568 0.0850  0.0149  -0.0438 81  SER   A O   
250  C  CB  . SER   A 38  ? 0.5914 0.8235 0.6194 0.0982  -0.0332 -0.0927 81  SER   A CB  
251  O  OG  . SER   A 38  ? 0.6479 0.9065 0.6789 0.1040  -0.0602 -0.1230 81  SER   A OG  
252  N  N   . GLY   A 39  ? 0.5873 0.7310 0.5098 0.1183  0.0045  -0.0229 82  GLY   A N   
253  C  CA  . GLY   A 39  ? 0.6032 0.7190 0.5209 0.1136  0.0252  -0.0025 82  GLY   A CA  
254  C  C   . GLY   A 39  ? 0.5931 0.7298 0.5564 0.1107  0.0376  0.0016  82  GLY   A C   
255  O  O   . GLY   A 39  ? 0.6021 0.7182 0.5643 0.1067  0.0555  0.0157  82  GLY   A O   
256  N  N   . ASP   A 40  ? 0.5711 0.7520 0.5737 0.1151  0.0284  -0.0106 83  ASP   A N   
257  C  CA  . ASP   A 40  ? 0.5607 0.7708 0.6121 0.1121  0.0433  -0.0065 83  ASP   A CA  
258  C  C   . ASP   A 40  ? 0.5727 0.7952 0.6083 0.1386  0.0402  0.0025  83  ASP   A C   
259  O  O   . ASP   A 40  ? 0.5750 0.8148 0.5968 0.1575  0.0188  -0.0064 83  ASP   A O   
260  C  CB  . ASP   A 40  ? 0.5537 0.8139 0.6730 0.0970  0.0366  -0.0289 83  ASP   A CB  
261  C  CG  . ASP   A 40  ? 0.6390 0.8833 0.7827 0.0698  0.0425  -0.0387 83  ASP   A CG  
262  O  OD1 . ASP   A 40  ? 0.6726 0.8791 0.8038 0.0604  0.0630  -0.0226 83  ASP   A OD1 
263  O  OD2 . ASP   A 40  ? 0.6659 0.9346 0.8397 0.0604  0.0247  -0.0642 83  ASP   A OD2 
264  N  N   . PHE   A 41  ? 0.5759 0.7904 0.6124 0.1433  0.0610  0.0188  84  PHE   A N   
265  C  CA  . PHE   A 41  ? 0.5895 0.8153 0.6124 0.1708  0.0600  0.0255  84  PHE   A CA  
266  C  C   . PHE   A 41  ? 0.5871 0.8778 0.6744 0.1722  0.0666  0.0172  84  PHE   A C   
267  O  O   . PHE   A 41  ? 0.5642 0.8770 0.7029 0.1490  0.0855  0.0170  84  PHE   A O   
268  C  CB  . PHE   A 41  ? 0.5899 0.7780 0.5789 0.1790  0.0780  0.0440  84  PHE   A CB  
269  C  CG  . PHE   A 41  ? 0.6128 0.7432 0.5406 0.1839  0.0689  0.0508  84  PHE   A CG  
270  C  CD1 . PHE   A 41  ? 0.6322 0.7412 0.5187 0.2063  0.0524  0.0518  84  PHE   A CD1 
271  C  CD2 . PHE   A 41  ? 0.6186 0.7157 0.5325 0.1666  0.0779  0.0564  84  PHE   A CD2 
272  C  CE1 . PHE   A 41  ? 0.6682 0.7234 0.5056 0.2063  0.0469  0.0587  84  PHE   A CE1 
273  C  CE2 . PHE   A 41  ? 0.6527 0.7046 0.5201 0.1688  0.0708  0.0611  84  PHE   A CE2 
274  C  CZ  . PHE   A 41  ? 0.6709 0.7019 0.5026 0.1861  0.0564  0.0624  84  PHE   A CZ  
275  N  N   . SER   A 42  ? 0.6073 0.9287 0.6944 0.1994  0.0521  0.0105  85  SER   A N   
276  C  CA  . SER   A 42  ? 0.5995 0.9922 0.7520 0.2045  0.0588  0.0015  85  SER   A CA  
277  C  C   . SER   A 42  ? 0.6398 1.0409 0.7682 0.2425  0.0591  0.0079  85  SER   A C   
278  O  O   . SER   A 42  ? 0.6717 1.0264 0.7355 0.2663  0.0428  0.0127  85  SER   A O   
279  C  CB  . SER   A 42  ? 0.5946 1.0390 0.7913 0.2004  0.0334  -0.0243 85  SER   A CB  
280  O  OG  . SER   A 42  ? 0.6570 1.0846 0.8012 0.2286  0.0021  -0.0309 85  SER   A OG  
281  N  N   . LEU   A 43  ? 0.6370 1.0952 0.8171 0.2484  0.0792  0.0083  86  LEU   A N   
282  C  CA  . LEU   A 43  ? 0.6806 1.1522 0.8401 0.2885  0.0804  0.0115  86  LEU   A CA  
283  C  C   . LEU   A 43  ? 0.7012 1.2156 0.8721 0.3172  0.0495  -0.0079 86  LEU   A C   
284  O  O   . LEU   A 43  ? 0.6579 1.2378 0.8947 0.3059  0.0409  -0.0260 86  LEU   A O   
285  C  CB  . LEU   A 43  ? 0.6572 1.1797 0.8657 0.2880  0.1167  0.0200  86  LEU   A CB  
286  C  CG  . LEU   A 43  ? 0.7116 1.1882 0.8870 0.2800  0.1478  0.0430  86  LEU   A CG  
287  C  CD1 . LEU   A 43  ? 0.6870 1.2204 0.9076 0.2853  0.1852  0.0526  86  LEU   A CD1 
288  C  CD2 . LEU   A 43  ? 0.7760 1.1841 0.8647 0.3100  0.1358  0.0498  86  LEU   A CD2 
289  N  N   . VAL   A 44  ? 0.7619 1.2392 0.8701 0.3560  0.0320  -0.0054 87  VAL   A N   
290  C  CA  . VAL   A 44  ? 0.7839 1.2910 0.8886 0.3928  0.0017  -0.0208 87  VAL   A CA  
291  C  C   . VAL   A 44  ? 0.7977 1.3518 0.9226 0.4284  0.0132  -0.0232 87  VAL   A C   
292  O  O   . VAL   A 44  ? 0.8338 1.3456 0.9156 0.4436  0.0287  -0.0098 87  VAL   A O   
293  C  CB  . VAL   A 44  ? 0.8508 1.2728 0.8652 0.4137  -0.0239 -0.0134 87  VAL   A CB  
294  C  CG1 . VAL   A 44  ? 0.8614 1.3013 0.8577 0.4615  -0.0537 -0.0248 87  VAL   A CG1 
295  C  CG2 . VAL   A 44  ? 0.8742 1.2578 0.8687 0.3817  -0.0337 -0.0116 87  VAL   A CG2 
296  N  N   . GLU   A 45  ? 0.7699 1.4144 0.9613 0.4431  0.0057  -0.0421 88  GLU   A N   
297  C  CA  . GLU   A 45  ? 0.7725 1.4715 0.9873 0.4806  0.0180  -0.0460 88  GLU   A CA  
298  C  C   . GLU   A 45  ? 0.7713 1.5163 0.9929 0.5272  -0.0162 -0.0667 88  GLU   A C   
299  O  O   . GLU   A 45  ? 0.8203 1.5082 0.9774 0.5490  -0.0493 -0.0678 88  GLU   A O   
300  C  CB  . GLU   A 45  ? 0.7602 1.5403 1.0639 0.4538  0.0578  -0.0448 88  GLU   A CB  
301  C  CG  . GLU   A 45  ? 0.8520 1.5816 1.1380 0.4180  0.0934  -0.0210 88  GLU   A CG  
302  C  CD  . GLU   A 45  ? 0.9122 1.6927 1.2397 0.4180  0.1383  -0.0096 88  GLU   A CD  
303  O  OE1 . GLU   A 45  ? 0.9009 1.7470 1.2563 0.4537  0.1433  -0.0187 88  GLU   A OE1 
304  O  OE2 . GLU   A 45  ? 0.9426 1.6974 1.2721 0.3847  0.1696  0.0093  88  GLU   A OE2 
305  N  N   . GLY   B 7   ? 0.8784 0.8941 0.8288 0.2032  0.0846  -0.0555 16  GLY   B N   
306  C  CA  . GLY   B 7   ? 0.9005 0.8900 0.8367 0.2117  0.0818  -0.0503 16  GLY   B CA  
307  C  C   . GLY   B 7   ? 0.8959 0.8957 0.8417 0.2129  0.0700  -0.0505 16  GLY   B C   
308  O  O   . GLY   B 7   ? 0.8879 0.9153 0.8539 0.2073  0.0626  -0.0559 16  GLY   B O   
309  N  N   . GLU   B 8   ? 0.8941 0.8716 0.8257 0.2204  0.0679  -0.0445 17  GLU   B N   
310  C  CA  . GLU   B 8   ? 0.8838 0.8672 0.8198 0.2251  0.0551  -0.0457 17  GLU   B CA  
311  C  C   . GLU   B 8   ? 0.8610 0.8511 0.8093 0.2032  0.0494  -0.0433 17  GLU   B C   
312  O  O   . GLU   B 8   ? 0.8735 0.8491 0.8148 0.1913  0.0548  -0.0357 17  GLU   B O   
313  C  CB  . GLU   B 8   ? 0.9375 0.8970 0.8517 0.2445  0.0551  -0.0396 17  GLU   B CB  
314  C  CG  . GLU   B 8   ? 1.0075 0.9743 0.9229 0.2562  0.0396  -0.0442 17  GLU   B CG  
315  C  CD  . GLU   B 8   ? 1.1146 1.0605 1.0058 0.2805  0.0396  -0.0384 17  GLU   B CD  
316  O  OE1 . GLU   B 8   ? 1.1382 1.0625 1.0146 0.2813  0.0527  -0.0269 17  GLU   B OE1 
317  O  OE2 . GLU   B 8   ? 1.1483 1.0999 1.0357 0.2994  0.0266  -0.0452 17  GLU   B OE2 
318  N  N   A THR   B 9   ? 0.8368 0.8486 0.8039 0.1982  0.0380  -0.0501 18  THR   B N   
319  N  N   B THR   B 9   ? 0.8337 0.8456 0.8010 0.1979  0.0380  -0.0500 18  THR   B N   
320  C  CA  A THR   B 9   ? 0.8242 0.8403 0.8029 0.1777  0.0316  -0.0480 18  THR   B CA  
321  C  CA  B THR   B 9   ? 0.8186 0.8341 0.7968 0.1778  0.0316  -0.0478 18  THR   B CA  
322  C  C   A THR   B 9   ? 0.8062 0.8189 0.7852 0.1845  0.0146  -0.0516 18  THR   B C   
323  C  C   B THR   B 9   ? 0.8037 0.8157 0.7822 0.1846  0.0147  -0.0514 18  THR   B C   
324  O  O   A THR   B 9   ? 0.8041 0.8179 0.7924 0.1690  0.0069  -0.0509 18  THR   B O   
325  O  O   B THR   B 9   ? 0.8018 0.8144 0.7889 0.1691  0.0071  -0.0506 18  THR   B O   
326  C  CB  A THR   B 9   ? 0.8309 0.8732 0.8337 0.1593  0.0344  -0.0506 18  THR   B CB  
327  C  CB  B THR   B 9   ? 0.8180 0.8596 0.8204 0.1601  0.0335  -0.0507 18  THR   B CB  
328  O  OG1 A THR   B 9   ? 0.8458 0.9022 0.8518 0.1663  0.0441  -0.0540 18  THR   B OG1 
329  O  OG1 B THR   B 9   ? 0.8162 0.8822 0.8357 0.1700  0.0268  -0.0602 18  THR   B OG1 
330  C  CG2 A THR   B 9   ? 0.8383 0.8745 0.8406 0.1374  0.0405  -0.0429 18  THR   B CG2 
331  C  CG2 B THR   B 9   ? 0.8246 0.8666 0.8228 0.1518  0.0492  -0.0467 18  THR   B CG2 
332  N  N   . THR   B 10  ? 0.7932 0.7992 0.7597 0.2091  0.0082  -0.0554 19  THR   B N   
333  C  CA  . THR   B 10  ? 0.7640 0.7648 0.7262 0.2208  -0.0093 -0.0605 19  THR   B CA  
334  C  C   . THR   B 10  ? 0.7414 0.7204 0.6878 0.2152  -0.0104 -0.0520 19  THR   B C   
335  O  O   . THR   B 10  ? 0.7442 0.7085 0.6746 0.2162  0.0028  -0.0419 19  THR   B O   
336  C  CB  . THR   B 10  ? 0.7826 0.7767 0.7264 0.2527  -0.0120 -0.0639 19  THR   B CB  
337  O  OG1 . THR   B 10  ? 0.7928 0.8056 0.7472 0.2603  -0.0087 -0.0710 19  THR   B OG1 
338  C  CG2 . THR   B 10  ? 0.7786 0.7693 0.7166 0.2692  -0.0324 -0.0720 19  THR   B CG2 
339  N  N   . ASP   B 11  ? 0.7191 0.6966 0.6714 0.2084  -0.0262 -0.0562 20  ASP   B N   
340  C  CA  . ASP   B 11  ? 0.7311 0.6883 0.6666 0.2067  -0.0306 -0.0499 20  ASP   B CA  
341  C  C   . ASP   B 11  ? 0.7353 0.6759 0.6423 0.2329  -0.0269 -0.0441 20  ASP   B C   
342  O  O   . ASP   B 11  ? 0.7526 0.6948 0.6524 0.2555  -0.0296 -0.0486 20  ASP   B O   
343  C  CB  . ASP   B 11  ? 0.7598 0.7143 0.7021 0.2044  -0.0529 -0.0589 20  ASP   B CB  
344  C  CG  . ASP   B 11  ? 0.8245 0.7876 0.7912 0.1753  -0.0561 -0.0601 20  ASP   B CG  
345  O  OD1 . ASP   B 11  ? 0.8135 0.7904 0.7942 0.1586  -0.0413 -0.0554 20  ASP   B OD1 
346  O  OD2 . ASP   B 11  ? 0.8676 0.8220 0.8381 0.1702  -0.0737 -0.0654 20  ASP   B OD2 
347  N  N   . GLY   B 12  ? 0.7138 0.6407 0.6057 0.2304  -0.0195 -0.0335 21  GLY   B N   
348  C  CA  . GLY   B 12  ? 0.7088 0.6228 0.5762 0.2533  -0.0135 -0.0253 21  GLY   B CA  
349  C  C   . GLY   B 12  ? 0.6929 0.6007 0.5540 0.2434  0.0022  -0.0119 21  GLY   B C   
350  O  O   . GLY   B 12  ? 0.6819 0.5934 0.5545 0.2200  0.0064  -0.0103 21  GLY   B O   
351  N  N   . VAL   B 13  ? 0.6827 0.5819 0.5256 0.2622  0.0110  -0.0019 22  VAL   B N   
352  C  CA  . VAL   B 13  ? 0.6623 0.5587 0.5025 0.2540  0.0263  0.0111  22  VAL   B CA  
353  C  C   . VAL   B 13  ? 0.6551 0.5505 0.5008 0.2521  0.0437  0.0167  22  VAL   B C   
354  O  O   . VAL   B 13  ? 0.6712 0.5634 0.5108 0.2692  0.0452  0.0148  22  VAL   B O   
355  C  CB  . VAL   B 13  ? 0.6699 0.5599 0.4896 0.2735  0.0257  0.0201  22  VAL   B CB  
356  C  CG1 . VAL   B 13  ? 0.6863 0.5700 0.4876 0.3045  0.0283  0.0239  22  VAL   B CG1 
357  C  CG2 . VAL   B 13  ? 0.6622 0.5548 0.4848 0.2617  0.0398  0.0327  22  VAL   B CG2 
358  N  N   . TYR   B 14  ? 0.6313 0.5280 0.4877 0.2318  0.0554  0.0222  23  TYR   B N   
359  C  CA  . TYR   B 14  ? 0.6316 0.5237 0.4939 0.2269  0.0699  0.0258  23  TYR   B CA  
360  C  C   . TYR   B 14  ? 0.6329 0.5209 0.4975 0.2183  0.0834  0.0382  23  TYR   B C   
361  O  O   . TYR   B 14  ? 0.6295 0.5240 0.4986 0.2062  0.0813  0.0403  23  TYR   B O   
362  C  CB  . TYR   B 14  ? 0.6211 0.5205 0.4991 0.2069  0.0686  0.0160  23  TYR   B CB  
363  C  CG  . TYR   B 14  ? 0.6276 0.5346 0.5095 0.2138  0.0595  0.0045  23  TYR   B CG  
364  C  CD1 . TYR   B 14  ? 0.6286 0.5440 0.5133 0.2148  0.0441  -0.0031 23  TYR   B CD1 
365  C  CD2 . TYR   B 14  ? 0.6403 0.5468 0.5249 0.2177  0.0656  0.0005  23  TYR   B CD2 
366  C  CE1 . TYR   B 14  ? 0.6355 0.5617 0.5288 0.2193  0.0350  -0.0139 23  TYR   B CE1 
367  C  CE2 . TYR   B 14  ? 0.6527 0.5712 0.5434 0.2246  0.0571  -0.0104 23  TYR   B CE2 
368  C  CZ  . TYR   B 14  ? 0.6646 0.5949 0.5620 0.2242  0.0419  -0.0176 23  TYR   B CZ  
369  O  OH  . TYR   B 14  ? 0.6957 0.6415 0.6042 0.2292  0.0327  -0.0287 23  TYR   B OH  
370  N  N   . ARG   B 15  ? 0.6324 0.5099 0.4958 0.2229  0.0968  0.0458  24  ARG   B N   
371  C  CA  . ARG   B 15  ? 0.6390 0.5129 0.5106 0.2110  0.1098  0.0570  24  ARG   B CA  
372  C  C   . ARG   B 15  ? 0.6345 0.5080 0.5213 0.1869  0.1111  0.0494  24  ARG   B C   
373  O  O   . ARG   B 15  ? 0.6400 0.5097 0.5270 0.1863  0.1090  0.0401  24  ARG   B O   
374  C  CB  . ARG   B 15  ? 0.6633 0.5216 0.5273 0.2251  0.1243  0.0693  24  ARG   B CB  
375  C  CG  . ARG   B 15  ? 0.6853 0.5418 0.5302 0.2533  0.1256  0.0783  24  ARG   B CG  
376  C  CD  . ARG   B 15  ? 0.7278 0.5660 0.5638 0.2669  0.1420  0.0917  24  ARG   B CD  
377  N  NE  . ARG   B 15  ? 0.7586 0.5936 0.5711 0.2989  0.1417  0.0975  24  ARG   B NE  
378  C  CZ  . ARG   B 15  ? 0.7929 0.6334 0.5960 0.3132  0.1471  0.1110  24  ARG   B CZ  
379  N  NH1 . ARG   B 15  ? 0.7554 0.6067 0.5735 0.2974  0.1546  0.1211  24  ARG   B NH1 
380  N  NH2 . ARG   B 15  ? 0.8289 0.6656 0.6071 0.3453  0.1450  0.1142  24  ARG   B NH2 
381  N  N   . VAL   B 16  ? 0.6274 0.5054 0.5263 0.1694  0.1147  0.0531  25  VAL   B N   
382  C  CA  . VAL   B 16  ? 0.6414 0.5174 0.5526 0.1488  0.1156  0.0459  25  VAL   B CA  
383  C  C   . VAL   B 16  ? 0.6589 0.5218 0.5783 0.1432  0.1279  0.0550  25  VAL   B C   
384  O  O   . VAL   B 16  ? 0.6574 0.5257 0.5842 0.1407  0.1336  0.0660  25  VAL   B O   
385  C  CB  . VAL   B 16  ? 0.6490 0.5397 0.5678 0.1329  0.1080  0.0411  25  VAL   B CB  
386  C  CG1 . VAL   B 16  ? 0.6501 0.5376 0.5788 0.1149  0.1085  0.0328  25  VAL   B CG1 
387  C  CG2 . VAL   B 16  ? 0.6551 0.5555 0.5660 0.1372  0.0963  0.0340  25  VAL   B CG2 
388  N  N   . MET   B 17  ? 0.6761 0.5216 0.5945 0.1417  0.1322  0.0509  26  MET   B N   
389  C  CA  . MET   B 17  ? 0.7009 0.5275 0.6257 0.1369  0.1436  0.0595  26  MET   B CA  
390  C  C   . MET   B 17  ? 0.7364 0.5535 0.6722 0.1173  0.1416  0.0499  26  MET   B C   
391  O  O   . MET   B 17  ? 0.7357 0.5570 0.6682 0.1134  0.1332  0.0361  26  MET   B O   
392  C  CB  . MET   B 17  ? 0.7171 0.5228 0.6257 0.1562  0.1504  0.0632  26  MET   B CB  
393  C  CG  . MET   B 17  ? 0.7342 0.5468 0.6270 0.1804  0.1497  0.0688  26  MET   B CG  
394  S  SD  . MET   B 17  ? 0.7286 0.5446 0.6215 0.1893  0.1612  0.0901  26  MET   B SD  
395  C  CE  . MET   B 17  ? 0.6931 0.4780 0.5892 0.1858  0.1791  0.1035  26  MET   B CE  
396  N  N   . THR   B 18  ? 0.7586 0.5611 0.7069 0.1063  0.1495  0.0573  27  THR   B N   
397  C  CA  . THR   B 18  ? 0.7960 0.5836 0.7531 0.0896  0.1463  0.0472  27  THR   B CA  
398  C  C   . THR   B 18  ? 0.8376 0.5935 0.7971 0.0881  0.1570  0.0560  27  THR   B C   
399  O  O   . THR   B 18  ? 0.8289 0.5817 0.7934 0.0918  0.1684  0.0732  27  THR   B O   
400  C  CB  . THR   B 18  ? 0.8070 0.6133 0.7837 0.0697  0.1393  0.0426  27  THR   B CB  
401  O  OG1 . THR   B 18  ? 0.8329 0.6217 0.8165 0.0555  0.1347  0.0313  27  THR   B OG1 
402  C  CG2 . THR   B 18  ? 0.7977 0.6162 0.7929 0.0635  0.1468  0.0582  27  THR   B CG2 
403  N  N   . ARG   B 19  ? 0.8796 0.6109 0.8345 0.0833  0.1537  0.0450  28  ARG   B N   
404  C  CA  . ARG   B 19  ? 0.9309 0.6263 0.8875 0.0797  0.1623  0.0521  28  ARG   B CA  
405  C  C   . ARG   B 19  ? 0.9562 0.6406 0.9343 0.0548  0.1567  0.0452  28  ARG   B C   
406  O  O   . ARG   B 19  ? 0.9700 0.6193 0.9487 0.0493  0.1602  0.0464  28  ARG   B O   
407  C  CB  . ARG   B 19  ? 0.9842 0.6518 0.9149 0.0975  0.1633  0.0460  28  ARG   B CB  
408  C  CG  . ARG   B 19  ? 1.0539 0.7296 0.9655 0.1227  0.1688  0.0535  28  ARG   B CG  
409  C  CD  . ARG   B 19  ? 1.1287 0.7685 1.0201 0.1397  0.1781  0.0601  28  ARG   B CD  
410  N  NE  . ARG   B 19  ? 1.1928 0.8428 1.0636 0.1664  0.1791  0.0615  28  ARG   B NE  
411  C  CZ  . ARG   B 19  ? 1.2453 0.9030 1.1017 0.1799  0.1708  0.0468  28  ARG   B CZ  
412  N  NH1 . ARG   B 19  ? 1.2501 0.9060 1.1078 0.1709  0.1623  0.0308  28  ARG   B NH1 
413  N  NH2 . ARG   B 19  ? 1.2514 0.9205 1.0928 0.2034  0.1706  0.0479  28  ARG   B NH2 
414  N  N   . ARG   B 20  ? 0.9612 0.6735 0.9557 0.0408  0.1472  0.0375  29  ARG   B N   
415  C  CA  . ARG   B 20  ? 0.9826 0.6900 0.9981 0.0184  0.1385  0.0277  29  ARG   B CA  
416  C  C   . ARG   B 20  ? 0.9801 0.6827 1.0238 0.0026  0.1477  0.0437  29  ARG   B C   
417  O  O   . ARG   B 20  ? 0.9946 0.6707 1.0518 -0.0128 0.1457  0.0404  29  ARG   B O   
418  C  CB  . ARG   B 20  ? 1.0093 0.7516 1.0312 0.0120  0.1259  0.0158  29  ARG   B CB  
419  C  CG  . ARG   B 20  ? 1.0817 0.8221 1.1226 -0.0081 0.1137  0.0022  29  ARG   B CG  
420  C  CD  . ARG   B 20  ? 1.1392 0.9127 1.1806 -0.0101 0.1020  -0.0090 29  ARG   B CD  
421  N  NE  . ARG   B 20  ? 1.1848 0.9914 1.2434 -0.0137 0.1059  0.0033  29  ARG   B NE  
422  C  CZ  . ARG   B 20  ? 1.2179 1.0442 1.3021 -0.0292 0.0997  0.0012  29  ARG   B CZ  
423  N  NH1 . ARG   B 20  ? 1.2197 1.0353 1.3163 -0.0435 0.0880  -0.0137 29  ARG   B NH1 
424  N  NH2 . ARG   B 20  ? 1.2066 1.0640 1.3035 -0.0289 0.1040  0.0130  29  ARG   B NH2 
425  N  N   . LEU   B 21  ? 0.9582 0.6856 1.0106 0.0070  0.1582  0.0614  30  LEU   B N   
426  C  CA  . LEU   B 21  ? 0.9429 0.6744 1.0234 -0.0057 0.1702  0.0805  30  LEU   B CA  
427  C  C   . LEU   B 21  ? 0.9470 0.6438 1.0168 0.0042  0.1875  0.0985  30  LEU   B C   
428  O  O   . LEU   B 21  ? 0.9662 0.6316 1.0097 0.0167  0.1866  0.0918  30  LEU   B O   
429  C  CB  . LEU   B 21  ? 0.9309 0.7066 1.0196 0.0000  0.1736  0.0908  30  LEU   B CB  
430  C  CG  . LEU   B 21  ? 0.9378 0.7487 1.0461 -0.0137 0.1602  0.0793  30  LEU   B CG  
431  C  CD1 . LEU   B 21  ? 0.9519 0.7588 1.0452 -0.0146 0.1426  0.0549  30  LEU   B CD1 
432  C  CD2 . LEU   B 21  ? 0.9360 0.7839 1.0405 -0.0008 0.1631  0.0886  30  LEU   B CD2 
433  N  N   . LEU   B 22  ? 0.9248 0.6273 1.0138 -0.0002 0.2038  0.1218  31  LEU   B N   
434  C  CA  . LEU   B 22  ? 0.9269 0.5967 1.0040 0.0106  0.2221  0.1416  31  LEU   B CA  
435  C  C   . LEU   B 22  ? 0.9208 0.5901 0.9592 0.0434  0.2266  0.1450  31  LEU   B C   
436  O  O   . LEU   B 22  ? 0.9128 0.6169 0.9459 0.0557  0.2250  0.1467  31  LEU   B O   
437  C  CB  . LEU   B 22  ? 0.9189 0.6035 1.0257 0.0002  0.2397  0.1673  31  LEU   B CB  
438  C  CG  . LEU   B 22  ? 0.9515 0.5994 1.0504 0.0071  0.2606  0.1905  31  LEU   B CG  
439  C  CD1 . LEU   B 22  ? 0.9646 0.5680 1.0775 -0.0153 0.2588  0.1864  31  LEU   B CD1 
440  C  CD2 . LEU   B 22  ? 0.9456 0.6198 1.0651 0.0074  0.2807  0.2188  31  LEU   B CD2 
441  N  N   . GLY   B 23  ? 0.9196 0.5493 0.9312 0.0576  0.2303  0.1443  32  GLY   B N   
442  C  CA  . GLY   B 23  ? 0.9159 0.5426 0.8912 0.0894  0.2328  0.1452  32  GLY   B CA  
443  C  C   . GLY   B 23  ? 0.8885 0.5469 0.8522 0.0994  0.2171  0.1269  32  GLY   B C   
444  O  O   . GLY   B 23  ? 0.8832 0.5492 0.8541 0.0860  0.2023  0.1076  32  GLY   B O   
445  N  N   . SER   B 24  ? 0.8705 0.5467 0.8157 0.1235  0.2199  0.1330  33  SER   B N   
446  C  CA  . SER   B 24  ? 0.8581 0.5636 0.7940 0.1325  0.2054  0.1176  33  SER   B CA  
447  C  C   . SER   B 24  ? 0.8201 0.5605 0.7687 0.1311  0.2065  0.1267  33  SER   B C   
448  O  O   . SER   B 24  ? 0.8165 0.5599 0.7593 0.1457  0.2186  0.1448  33  SER   B O   
449  C  CB  . SER   B 24  ? 0.9027 0.6009 0.8075 0.1619  0.2047  0.1150  33  SER   B CB  
450  O  OG  . SER   B 24  ? 0.9532 0.6221 0.8446 0.1653  0.2024  0.1047  33  SER   B OG  
451  N  N   . THR   B 25  ? 0.7875 0.5535 0.7517 0.1152  0.1943  0.1148  34  THR   B N   
452  C  CA  . THR   B 25  ? 0.7642 0.5630 0.7406 0.1132  0.1941  0.1222  34  THR   B CA  
453  C  C   . THR   B 25  ? 0.7459 0.5672 0.7088 0.1236  0.1803  0.1100  34  THR   B C   
454  O  O   . THR   B 25  ? 0.7454 0.5662 0.7045 0.1175  0.1681  0.0926  34  THR   B O   
455  C  CB  . THR   B 25  ? 0.7679 0.5777 0.7765 0.0854  0.1927  0.1213  34  THR   B CB  
456  O  OG1 . THR   B 25  ? 0.7890 0.5750 0.8124 0.0743  0.2055  0.1333  34  THR   B OG1 
457  C  CG2 . THR   B 25  ? 0.7517 0.5975 0.7744 0.0840  0.1931  0.1295  34  THR   B CG2 
458  N  N   . GLN   B 26  ? 0.7249 0.5646 0.6796 0.1399  0.1821  0.1195  35  GLN   B N   
459  C  CA  . GLN   B 26  ? 0.7109 0.5685 0.6530 0.1489  0.1681  0.1085  35  GLN   B CA  
460  C  C   . GLN   B 26  ? 0.6938 0.5757 0.6529 0.1323  0.1609  0.1046  35  GLN   B C   
461  O  O   . GLN   B 26  ? 0.6916 0.5898 0.6617 0.1321  0.1677  0.1173  35  GLN   B O   
462  C  CB  . GLN   B 26  ? 0.7107 0.5735 0.6320 0.1767  0.1703  0.1179  35  GLN   B CB  
463  C  CG  . GLN   B 26  ? 0.7025 0.5803 0.6118 0.1843  0.1538  0.1056  35  GLN   B CG  
464  C  CD  . GLN   B 26  ? 0.7040 0.5835 0.5907 0.2131  0.1525  0.1113  35  GLN   B CD  
465  O  OE1 . GLN   B 26  ? 0.7163 0.5808 0.5884 0.2311  0.1581  0.1157  35  GLN   B OE1 
466  N  NE2 . GLN   B 26  ? 0.6807 0.5768 0.5616 0.2199  0.1439  0.1106  35  GLN   B NE2 
467  N  N   . VAL   B 27  ? 0.6691 0.5546 0.6300 0.1198  0.1481  0.0877  36  VAL   B N   
468  C  CA  . VAL   B 27  ? 0.6411 0.5482 0.6145 0.1060  0.1400  0.0825  36  VAL   B CA  
469  C  C   . VAL   B 27  ? 0.6221 0.5447 0.5803 0.1180  0.1300  0.0795  36  VAL   B C   
470  O  O   . VAL   B 27  ? 0.6214 0.5624 0.5859 0.1123  0.1249  0.0789  36  VAL   B O   
471  C  CB  . VAL   B 27  ? 0.6460 0.5483 0.6287 0.0864  0.1322  0.0672  36  VAL   B CB  
472  C  CG1 . VAL   B 27  ? 0.6579 0.5481 0.6606 0.0712  0.1397  0.0703  36  VAL   B CG1 
473  C  CG2 . VAL   B 27  ? 0.6563 0.5453 0.6225 0.0914  0.1259  0.0547  36  VAL   B CG2 
474  N  N   . GLY   B 28  ? 0.6039 0.5184 0.5425 0.1347  0.1262  0.0771  37  GLY   B N   
475  C  CA  . GLY   B 28  ? 0.5791 0.5031 0.5027 0.1460  0.1153  0.0736  37  GLY   B CA  
476  C  C   . GLY   B 28  ? 0.5844 0.4974 0.4905 0.1624  0.1101  0.0688  37  GLY   B C   
477  O  O   . GLY   B 28  ? 0.5915 0.4915 0.4944 0.1703  0.1170  0.0712  37  GLY   B O   
478  N  N   . VAL   B 29  ? 0.5746 0.4920 0.4694 0.1679  0.0973  0.0618  38  VAL   B N   
479  C  CA  . VAL   B 29  ? 0.6002 0.5112 0.4806 0.1834  0.0884  0.0559  38  VAL   B CA  
480  C  C   . VAL   B 29  ? 0.5971 0.5108 0.4775 0.1723  0.0749  0.0436  38  VAL   B C   
481  O  O   . VAL   B 29  ? 0.5892 0.5093 0.4737 0.1591  0.0721  0.0422  38  VAL   B O   
482  C  CB  . VAL   B 29  ? 0.6283 0.5408 0.4919 0.2074  0.0860  0.0640  38  VAL   B CB  
483  C  CG1 . VAL   B 29  ? 0.6460 0.5511 0.4945 0.2250  0.0742  0.0562  38  VAL   B CG1 
484  C  CG2 . VAL   B 29  ? 0.6265 0.5387 0.4901 0.2187  0.1019  0.0795  38  VAL   B CG2 
485  N  N   . GLY   B 30  ? 0.5864 0.4960 0.4627 0.1780  0.0670  0.0353  39  GLY   B N   
486  C  CA  . GLY   B 30  ? 0.5885 0.5007 0.4667 0.1675  0.0555  0.0258  39  GLY   B CA  
487  C  C   . GLY   B 30  ? 0.5994 0.5089 0.4726 0.1790  0.0438  0.0186  39  GLY   B C   
488  O  O   . GLY   B 30  ? 0.6091 0.5150 0.4759 0.1972  0.0443  0.0194  39  GLY   B O   
489  N  N   . VAL   B 31  ? 0.5788 0.4897 0.4550 0.1688  0.0329  0.0117  40  VAL   B N   
490  C  CA  . VAL   B 31  ? 0.5797 0.4894 0.4564 0.1751  0.0192  0.0034  40  VAL   B CA  
491  C  C   . VAL   B 31  ? 0.5761 0.4953 0.4707 0.1596  0.0190  -0.0040 40  VAL   B C   
492  O  O   . VAL   B 31  ? 0.5737 0.4964 0.4753 0.1411  0.0218  -0.0037 40  VAL   B O   
493  C  CB  . VAL   B 31  ? 0.5982 0.4997 0.4643 0.1754  0.0051  0.0024  40  VAL   B CB  
494  C  CG1 . VAL   B 31  ? 0.6126 0.5112 0.4823 0.1792  -0.0112 -0.0075 40  VAL   B CG1 
495  C  CG2 . VAL   B 31  ? 0.6050 0.5002 0.4520 0.1937  0.0051  0.0097  40  VAL   B CG2 
496  N  N   . MET   B 32  ? 0.5687 0.4932 0.4700 0.1687  0.0148  -0.0107 41  MET   B N   
497  C  CA  . MET   B 32  ? 0.5665 0.5047 0.4869 0.1565  0.0138  -0.0178 41  MET   B CA  
498  C  C   . MET   B 32  ? 0.5828 0.5214 0.5094 0.1552  -0.0039 -0.0247 41  MET   B C   
499  O  O   . MET   B 32  ? 0.5911 0.5241 0.5097 0.1731  -0.0153 -0.0290 41  MET   B O   
500  C  CB  . MET   B 32  ? 0.5674 0.5134 0.4924 0.1688  0.0195  -0.0216 41  MET   B CB  
501  C  CG  . MET   B 32  ? 0.5833 0.5480 0.5286 0.1573  0.0219  -0.0279 41  MET   B CG  
502  S  SD  . MET   B 32  ? 0.6195 0.5880 0.5689 0.1375  0.0378  -0.0231 41  MET   B SD  
503  C  CE  . MET   B 32  ? 0.6601 0.6196 0.5984 0.1521  0.0504  -0.0211 41  MET   B CE  
504  N  N   . GLN   B 33  ? 0.5846 0.5273 0.5234 0.1349  -0.0066 -0.0252 42  GLN   B N   
505  C  CA  . GLN   B 33  ? 0.5986 0.5396 0.5468 0.1297  -0.0233 -0.0313 42  GLN   B CA  
506  C  C   . GLN   B 33  ? 0.6096 0.5655 0.5809 0.1064  -0.0187 -0.0311 42  GLN   B C   
507  O  O   . GLN   B 33  ? 0.6157 0.5704 0.5839 0.0930  -0.0074 -0.0238 42  GLN   B O   
508  C  CB  . GLN   B 33  ? 0.6317 0.5505 0.5613 0.1309  -0.0338 -0.0283 42  GLN   B CB  
509  C  CG  . GLN   B 33  ? 0.6946 0.6067 0.6338 0.1245  -0.0530 -0.0356 42  GLN   B CG  
510  C  CD  . GLN   B 33  ? 0.7967 0.6829 0.7128 0.1325  -0.0670 -0.0351 42  GLN   B CD  
511  O  OE1 . GLN   B 33  ? 0.8380 0.7110 0.7557 0.1181  -0.0755 -0.0347 42  GLN   B OE1 
512  N  NE2 . GLN   B 33  ? 0.7929 0.6702 0.6855 0.1566  -0.0690 -0.0344 42  GLN   B NE2 
513  N  N   . GLU   B 34  ? 0.6053 0.5769 0.6001 0.1026  -0.0270 -0.0387 43  GLU   B N   
514  C  CA  . GLU   B 34  ? 0.6055 0.5964 0.6272 0.0811  -0.0224 -0.0378 43  GLU   B CA  
515  C  C   . GLU   B 34  ? 0.6090 0.6174 0.6352 0.0755  -0.0022 -0.0328 43  GLU   B C   
516  O  O   . GLU   B 34  ? 0.6227 0.6392 0.6590 0.0576  0.0064  -0.0268 43  GLU   B O   
517  C  CB  . GLU   B 34  ? 0.6499 0.6253 0.6720 0.0622  -0.0281 -0.0323 43  GLU   B CB  
518  C  CG  . GLU   B 34  ? 0.7202 0.6761 0.7384 0.0671  -0.0505 -0.0389 43  GLU   B CG  
519  C  CD  . GLU   B 34  ? 0.8346 0.7647 0.8420 0.0536  -0.0568 -0.0329 43  GLU   B CD  
520  O  OE1 . GLU   B 34  ? 0.8525 0.7877 0.8767 0.0314  -0.0511 -0.0270 43  GLU   B OE1 
521  O  OE2 . GLU   B 34  ? 0.8873 0.7917 0.8680 0.0664  -0.0669 -0.0336 43  GLU   B OE2 
522  N  N   . GLY   B 35  ? 0.5905 0.6026 0.6076 0.0916  0.0053  -0.0349 44  GLY   B N   
523  C  CA  . GLY   B 35  ? 0.5718 0.5966 0.5899 0.0891  0.0226  -0.0319 44  GLY   B CA  
524  C  C   . GLY   B 35  ? 0.5647 0.5738 0.5629 0.0838  0.0333  -0.0241 44  GLY   B C   
525  O  O   . GLY   B 35  ? 0.5642 0.5812 0.5614 0.0815  0.0462  -0.0226 44  GLY   B O   
526  N  N   . VAL   B 36  ? 0.5496 0.5370 0.5311 0.0839  0.0272  -0.0201 45  VAL   B N   
527  C  CA  . VAL   B 36  ? 0.5424 0.5166 0.5061 0.0798  0.0350  -0.0136 45  VAL   B CA  
528  C  C   . VAL   B 36  ? 0.5347 0.4939 0.4811 0.0951  0.0339  -0.0124 45  VAL   B C   
529  O  O   . VAL   B 36  ? 0.5430 0.4942 0.4841 0.1063  0.0234  -0.0139 45  VAL   B O   
530  C  CB  . VAL   B 36  ? 0.5551 0.5196 0.5144 0.0657  0.0305  -0.0084 45  VAL   B CB  
531  C  CG1 . VAL   B 36  ? 0.5666 0.5176 0.5056 0.0650  0.0352  -0.0030 45  VAL   B CG1 
532  C  CG2 . VAL   B 36  ? 0.5517 0.5318 0.5276 0.0497  0.0367  -0.0063 45  VAL   B CG2 
533  N  N   . PHE   B 37  ? 0.5136 0.4697 0.4521 0.0962  0.0446  -0.0098 46  PHE   B N   
534  C  CA  . PHE   B 37  ? 0.5209 0.4652 0.4469 0.1079  0.0461  -0.0065 46  PHE   B CA  
535  C  C   . PHE   B 37  ? 0.5224 0.4584 0.4375 0.1016  0.0451  -0.0011 46  PHE   B C   
536  O  O   . PHE   B 37  ? 0.5101 0.4487 0.4252 0.0895  0.0498  -0.0004 46  PHE   B O   
537  C  CB  . PHE   B 37  ? 0.5266 0.4709 0.4530 0.1120  0.0574  -0.0069 46  PHE   B CB  
538  C  CG  . PHE   B 37  ? 0.5475 0.4804 0.4646 0.1242  0.0599  -0.0017 46  PHE   B CG  
539  C  CD1 . PHE   B 37  ? 0.5581 0.4871 0.4700 0.1409  0.0547  -0.0010 46  PHE   B CD1 
540  C  CD2 . PHE   B 37  ? 0.5697 0.4966 0.4837 0.1192  0.0673  0.0027  46  PHE   B CD2 
541  C  CE1 . PHE   B 37  ? 0.5793 0.4989 0.4816 0.1533  0.0590  0.0061  46  PHE   B CE1 
542  C  CE2 . PHE   B 37  ? 0.5790 0.4979 0.4876 0.1290  0.0711  0.0096  46  PHE   B CE2 
543  C  CZ  . PHE   B 37  ? 0.5827 0.4980 0.4848 0.1463  0.0682  0.0122  46  PHE   B CZ  
544  N  N   . HIS   B 38  ? 0.5276 0.4549 0.4322 0.1113  0.0385  0.0023  47  HIS   B N   
545  C  CA  . HIS   B 38  ? 0.5280 0.4491 0.4210 0.1086  0.0358  0.0070  47  HIS   B CA  
546  C  C   . HIS   B 38  ? 0.5399 0.4599 0.4275 0.1182  0.0416  0.0126  47  HIS   B C   
547  O  O   . HIS   B 38  ? 0.5520 0.4695 0.4364 0.1331  0.0412  0.0147  47  HIS   B O   
548  C  CB  . HIS   B 38  ? 0.5362 0.4479 0.4197 0.1145  0.0220  0.0067  47  HIS   B CB  
549  C  CG  . HIS   B 38  ? 0.5516 0.4629 0.4434 0.1047  0.0147  0.0022  47  HIS   B CG  
550  N  ND1 . HIS   B 38  ? 0.5700 0.4887 0.4756 0.1070  0.0122  -0.0034 47  HIS   B ND1 
551  C  CD2 . HIS   B 38  ? 0.5636 0.4684 0.4527 0.0927  0.0097  0.0033  47  HIS   B CD2 
552  C  CE1 . HIS   B 38  ? 0.5656 0.4850 0.4804 0.0943  0.0063  -0.0055 47  HIS   B CE1 
553  N  NE2 . HIS   B 38  ? 0.5724 0.4814 0.4768 0.0852  0.0050  -0.0009 47  HIS   B NE2 
554  N  N   . THR   B 39  ? 0.5268 0.4497 0.4138 0.1103  0.0469  0.0154  48  THR   B N   
555  C  CA  . THR   B 39  ? 0.5297 0.4550 0.4164 0.1170  0.0526  0.0216  48  THR   B CA  
556  C  C   . THR   B 39  ? 0.5349 0.4653 0.4179 0.1101  0.0513  0.0235  48  THR   B C   
557  O  O   . THR   B 39  ? 0.5367 0.4650 0.4129 0.1032  0.0453  0.0205  48  THR   B O   
558  C  CB  . THR   B 39  ? 0.5265 0.4521 0.4241 0.1166  0.0636  0.0223  48  THR   B CB  
559  O  OG1 . THR   B 39  ? 0.5354 0.4633 0.4349 0.1222  0.0697  0.0305  48  THR   B OG1 
560  C  CG2 . THR   B 39  ? 0.5209 0.4483 0.4267 0.1017  0.0680  0.0163  48  THR   B CG2 
561  N  N   . MET   B 40  ? 0.5204 0.4580 0.4080 0.1130  0.0567  0.0292  49  MET   B N   
562  C  CA  . MET   B 40  ? 0.5223 0.4690 0.4093 0.1078  0.0551  0.0301  49  MET   B CA  
563  C  C   . MET   B 40  ? 0.5314 0.4825 0.4311 0.0929  0.0599  0.0249  49  MET   B C   
564  O  O   . MET   B 40  ? 0.5202 0.4687 0.4318 0.0890  0.0673  0.0242  49  MET   B O   
565  C  CB  . MET   B 40  ? 0.5238 0.4805 0.4117 0.1192  0.0578  0.0391  49  MET   B CB  
566  C  CG  . MET   B 40  ? 0.5715 0.5217 0.4435 0.1382  0.0526  0.0434  49  MET   B CG  
567  S  SD  . MET   B 40  ? 0.6782 0.6413 0.5400 0.1538  0.0501  0.0517  49  MET   B SD  
568  C  CE  . MET   B 40  ? 0.5973 0.5550 0.4430 0.1484  0.0371  0.0445  49  MET   B CE  
569  N  N   . TRP   B 41  ? 0.5381 0.4939 0.4332 0.0858  0.0551  0.0206  50  TRP   B N   
570  C  CA  A TRP   B 41  ? 0.5547 0.5139 0.4588 0.0737  0.0573  0.0136  50  TRP   B CA  
571  C  CA  B TRP   B 41  ? 0.5373 0.4966 0.4413 0.0737  0.0572  0.0136  50  TRP   B CA  
572  C  C   . TRP   B 41  ? 0.5447 0.5115 0.4683 0.0695  0.0630  0.0154  50  TRP   B C   
573  O  O   . TRP   B 41  ? 0.5396 0.5014 0.4727 0.0615  0.0664  0.0100  50  TRP   B O   
574  C  CB  A TRP   B 41  ? 0.5707 0.5345 0.4637 0.0704  0.0504  0.0090  50  TRP   B CB  
575  C  CB  B TRP   B 41  ? 0.5277 0.4921 0.4207 0.0708  0.0502  0.0093  50  TRP   B CB  
576  C  CG  A TRP   B 41  ? 0.6004 0.5645 0.4965 0.0608  0.0508  -0.0001 50  TRP   B CG  
577  C  CG  B TRP   B 41  ? 0.5206 0.4880 0.4193 0.0611  0.0503  0.0005  50  TRP   B CG  
578  C  CD1 A TRP   B 41  ? 0.6232 0.5794 0.5106 0.0574  0.0519  -0.0051 50  TRP   B CD1 
579  C  CD1 B TRP   B 41  ? 0.5186 0.4963 0.4324 0.0557  0.0499  -0.0032 50  TRP   B CD1 
580  C  CD2 A TRP   B 41  ? 0.6055 0.5787 0.5149 0.0544  0.0498  -0.0058 50  TRP   B CD2 
581  C  CD2 B TRP   B 41  ? 0.5190 0.4790 0.4087 0.0566  0.0505  -0.0063 50  TRP   B CD2 
582  N  NE1 A TRP   B 41  ? 0.6336 0.5919 0.5243 0.0516  0.0515  -0.0138 50  TRP   B NE1 
583  N  NE1 B TRP   B 41  ? 0.5190 0.4934 0.4323 0.0488  0.0482  -0.0134 50  TRP   B NE1 
584  C  CE2 A TRP   B 41  ? 0.6235 0.5912 0.5282 0.0490  0.0491  -0.0153 50  TRP   B CE2 
585  C  CE2 B TRP   B 41  ? 0.5244 0.4886 0.4214 0.0505  0.0493  -0.0150 50  TRP   B CE2 
586  C  CE3 A TRP   B 41  ? 0.6076 0.5946 0.5339 0.0527  0.0493  -0.0038 50  TRP   B CE3 
587  C  CE3 B TRP   B 41  ? 0.5303 0.4817 0.4083 0.0571  0.0520  -0.0056 50  TRP   B CE3 
588  C  CZ2 A TRP   B 41  ? 0.6361 0.6083 0.5501 0.0428  0.0456  -0.0247 50  TRP   B CZ2 
589  C  CZ2 B TRP   B 41  ? 0.5334 0.4925 0.4216 0.0479  0.0494  -0.0231 50  TRP   B CZ2 
590  C  CZ3 A TRP   B 41  ? 0.6172 0.6106 0.5573 0.0438  0.0464  -0.0124 50  TRP   B CZ3 
591  C  CZ3 B TRP   B 41  ? 0.5481 0.4974 0.4197 0.0532  0.0539  -0.0118 50  TRP   B CZ3 
592  C  CH2 A TRP   B 41  ? 0.6302 0.6147 0.5631 0.0393  0.0435  -0.0236 50  TRP   B CH2 
593  C  CH2 B TRP   B 41  ? 0.5446 0.4973 0.4194 0.0501  0.0527  -0.0206 50  TRP   B CH2 
594  N  N   . HIS   B 42  ? 0.5480 0.5269 0.4780 0.0751  0.0641  0.0232  51  HIS   B N   
595  C  CA  . HIS   B 42  ? 0.5528 0.5407 0.5055 0.0687  0.0705  0.0265  51  HIS   B CA  
596  C  C   . HIS   B 42  ? 0.5723 0.5473 0.5336 0.0690  0.0803  0.0313  51  HIS   B C   
597  O  O   . HIS   B 42  ? 0.5746 0.5504 0.5551 0.0601  0.0859  0.0328  51  HIS   B O   
598  C  CB  . HIS   B 42  ? 0.5429 0.5515 0.5030 0.0746  0.0709  0.0350  51  HIS   B CB  
599  C  CG  . HIS   B 42  ? 0.5662 0.5749 0.5188 0.0905  0.0760  0.0470  51  HIS   B CG  
600  N  ND1 . HIS   B 42  ? 0.5861 0.5933 0.5161 0.1050  0.0691  0.0486  51  HIS   B ND1 
601  C  CD2 . HIS   B 42  ? 0.5690 0.5768 0.5316 0.0954  0.0870  0.0577  51  HIS   B CD2 
602  C  CE1 . HIS   B 42  ? 0.5911 0.5982 0.5178 0.1193  0.0750  0.0590  51  HIS   B CE1 
603  N  NE2 . HIS   B 42  ? 0.5842 0.5924 0.5297 0.1145  0.0867  0.0655  51  HIS   B NE2 
604  N  N   . VAL   B 43  ? 0.5730 0.5351 0.5204 0.0790  0.0817  0.0332  52  VAL   B N   
605  C  CA  . VAL   B 43  ? 0.5725 0.5214 0.5241 0.0823  0.0903  0.0370  52  VAL   B CA  
606  C  C   . VAL   B 43  ? 0.5862 0.5228 0.5424 0.0713  0.0910  0.0270  52  VAL   B C   
607  O  O   . VAL   B 43  ? 0.5901 0.5180 0.5582 0.0661  0.0977  0.0288  52  VAL   B O   
608  C  CB  . VAL   B 43  ? 0.5818 0.5229 0.5171 0.0983  0.0894  0.0400  52  VAL   B CB  
609  C  CG1 . VAL   B 43  ? 0.5860 0.5124 0.5223 0.1035  0.0972  0.0418  52  VAL   B CG1 
610  C  CG2 . VAL   B 43  ? 0.5773 0.5273 0.5052 0.1127  0.0886  0.0498  52  VAL   B CG2 
611  N  N   . THR   B 44  ? 0.5773 0.5119 0.5230 0.0686  0.0846  0.0172  53  THR   B N   
612  C  CA  . THR   B 44  ? 0.5849 0.5090 0.5310 0.0622  0.0853  0.0076  53  THR   B CA  
613  C  C   . THR   B 44  ? 0.5945 0.5226 0.5430 0.0511  0.0796  -0.0022 53  THR   B C   
614  O  O   . THR   B 44  ? 0.6054 0.5235 0.5541 0.0467  0.0799  -0.0107 53  THR   B O   
615  C  CB  . THR   B 44  ? 0.5921 0.5130 0.5256 0.0687  0.0839  0.0038  53  THR   B CB  
616  O  OG1 . THR   B 44  ? 0.5876 0.5173 0.5122 0.0665  0.0772  0.0011  53  THR   B OG1 
617  C  CG2 . THR   B 44  ? 0.5976 0.5152 0.5275 0.0817  0.0867  0.0111  53  THR   B CG2 
618  N  N   . LYS   B 45  ? 0.5914 0.5331 0.5384 0.0488  0.0736  -0.0021 54  LYS   B N   
619  C  CA  . LYS   B 45  ? 0.6097 0.5565 0.5546 0.0416  0.0666  -0.0123 54  LYS   B CA  
620  C  C   . LYS   B 45  ? 0.6297 0.5703 0.5579 0.0433  0.0652  -0.0198 54  LYS   B C   
621  O  O   . LYS   B 45  ? 0.6391 0.5785 0.5631 0.0396  0.0614  -0.0297 54  LYS   B O   
622  C  CB  . LYS   B 45  ? 0.6429 0.5866 0.6047 0.0317  0.0656  -0.0187 54  LYS   B CB  
623  C  CG  . LYS   B 45  ? 0.7101 0.6607 0.6936 0.0275  0.0695  -0.0098 54  LYS   B CG  
624  C  CD  . LYS   B 45  ? 0.7839 0.7566 0.7720 0.0280  0.0647  -0.0065 54  LYS   B CD  
625  C  CE  . LYS   B 45  ? 0.8413 0.8254 0.8566 0.0209  0.0686  0.0007  54  LYS   B CE  
626  N  NZ  . LYS   B 45  ? 0.8762 0.8541 0.8963 0.0268  0.0807  0.0154  54  LYS   B NZ  
627  N  N   . GLY   B 46  ? 0.6350 0.5727 0.5547 0.0495  0.0684  -0.0154 55  GLY   B N   
628  C  CA  . GLY   B 46  ? 0.6467 0.5826 0.5546 0.0507  0.0693  -0.0200 55  GLY   B CA  
629  C  C   . GLY   B 46  ? 0.6616 0.5891 0.5715 0.0518  0.0740  -0.0261 55  GLY   B C   
630  O  O   . GLY   B 46  ? 0.6637 0.5929 0.5651 0.0538  0.0759  -0.0298 55  GLY   B O   
631  N  N   . ALA   B 47  ? 0.6630 0.5812 0.5835 0.0514  0.0766  -0.0262 56  ALA   B N   
632  C  CA  . ALA   B 47  ? 0.6656 0.5718 0.5850 0.0543  0.0805  -0.0323 56  ALA   B CA  
633  C  C   . ALA   B 47  ? 0.6649 0.5719 0.5810 0.0632  0.0856  -0.0289 56  ALA   B C   
634  O  O   . ALA   B 47  ? 0.6580 0.5706 0.5764 0.0667  0.0860  -0.0212 56  ALA   B O   
635  C  CB  . ALA   B 47  ? 0.6701 0.5621 0.6010 0.0507  0.0819  -0.0322 56  ALA   B CB  
636  N  N   . ALA   B 48  ? 0.6663 0.5682 0.5769 0.0684  0.0885  -0.0356 57  ALA   B N   
637  C  CA  . ALA   B 48  ? 0.6690 0.5748 0.5784 0.0779  0.0929  -0.0342 57  ALA   B CA  
638  C  C   . ALA   B 48  ? 0.6673 0.5626 0.5818 0.0845  0.0958  -0.0283 57  ALA   B C   
639  O  O   . ALA   B 48  ? 0.6769 0.5576 0.5950 0.0818  0.0969  -0.0262 57  ALA   B O   
640  C  CB  . ALA   B 48  ? 0.6752 0.5786 0.5765 0.0839  0.0955  -0.0433 57  ALA   B CB  
641  N  N   . LEU   B 49  ? 0.6495 0.5525 0.5647 0.0935  0.0972  -0.0254 58  LEU   B N   
642  C  CA  . LEU   B 49  ? 0.6598 0.5538 0.5760 0.1035  0.0996  -0.0196 58  LEU   B CA  
643  C  C   . LEU   B 49  ? 0.6963 0.5893 0.6085 0.1166  0.1025  -0.0241 58  LEU   B C   
644  O  O   . LEU   B 49  ? 0.6987 0.6061 0.6110 0.1180  0.1021  -0.0300 58  LEU   B O   
645  C  CB  . LEU   B 49  ? 0.6408 0.5453 0.5600 0.1059  0.0956  -0.0126 58  LEU   B CB  
646  C  CG  . LEU   B 49  ? 0.6426 0.5490 0.5639 0.0971  0.0926  -0.0070 58  LEU   B CG  
647  C  CD1 . LEU   B 49  ? 0.6359 0.5500 0.5561 0.1027  0.0874  -0.0017 58  LEU   B CD1 
648  C  CD2 . LEU   B 49  ? 0.6538 0.5474 0.5781 0.0957  0.0969  -0.0017 58  LEU   B CD2 
649  N  N   . ARG   B 50  ? 0.7226 0.5997 0.6308 0.1273  0.1062  -0.0206 59  ARG   B N   
650  C  CA  . ARG   B 50  ? 0.7617 0.6360 0.6636 0.1429  0.1086  -0.0247 59  ARG   B CA  
651  C  C   . ARG   B 50  ? 0.7781 0.6598 0.6805 0.1560  0.1065  -0.0198 59  ARG   B C   
652  O  O   . ARG   B 50  ? 0.7740 0.6492 0.6760 0.1568  0.1066  -0.0113 59  ARG   B O   
653  C  CB  . ARG   B 50  ? 0.8149 0.6598 0.7078 0.1473  0.1142  -0.0246 59  ARG   B CB  
654  C  CG  . ARG   B 50  ? 0.9015 0.7387 0.7835 0.1653  0.1168  -0.0296 59  ARG   B CG  
655  C  CD  . ARG   B 50  ? 0.9882 0.7919 0.8591 0.1673  0.1211  -0.0313 59  ARG   B CD  
656  N  NE  . ARG   B 50  ? 1.0431 0.8228 0.9158 0.1614  0.1255  -0.0206 59  ARG   B NE  
657  C  CZ  . ARG   B 50  ? 1.1012 0.8665 0.9673 0.1740  0.1311  -0.0110 59  ARG   B CZ  
658  N  NH1 . ARG   B 50  ? 1.0998 0.8725 0.9565 0.1942  0.1311  -0.0123 59  ARG   B NH1 
659  N  NH2 . ARG   B 50  ? 1.1239 0.8692 0.9935 0.1673  0.1370  0.0004  59  ARG   B NH2 
660  N  N   . SER   B 51  ? 0.7907 0.6885 0.6945 0.1668  0.1038  -0.0257 60  SER   B N   
661  C  CA  . SER   B 51  ? 0.8210 0.7255 0.7245 0.1817  0.0996  -0.0240 60  SER   B CA  
662  C  C   . SER   B 51  ? 0.8607 0.7641 0.7572 0.1998  0.1018  -0.0301 60  SER   B C   
663  O  O   . SER   B 51  ? 0.8533 0.7788 0.7575 0.2018  0.0992  -0.0380 60  SER   B O   
664  C  CB  . SER   B 51  ? 0.8216 0.7522 0.7383 0.1755  0.0908  -0.0268 60  SER   B CB  
665  O  OG  . SER   B 51  ? 0.8517 0.7863 0.7672 0.1908  0.0843  -0.0267 60  SER   B OG  
666  N  N   . GLY   B 52  ? 0.8961 0.7732 0.7778 0.2126  0.1077  -0.0258 61  GLY   B N   
667  C  CA  . GLY   B 52  ? 0.9245 0.7946 0.7947 0.2318  0.1104  -0.0313 61  GLY   B CA  
668  C  C   . GLY   B 52  ? 0.9503 0.8186 0.8194 0.2249  0.1136  -0.0386 61  GLY   B C   
669  O  O   . GLY   B 52  ? 0.9703 0.8189 0.8366 0.2117  0.1173  -0.0362 61  GLY   B O   
670  N  N   . GLU   B 53  ? 0.9429 0.8356 0.8163 0.2326  0.1112  -0.0479 62  GLU   B N   
671  C  CA  . GLU   B 53  ? 0.9506 0.8466 0.8215 0.2292  0.1141  -0.0553 62  GLU   B CA  
672  C  C   . GLU   B 53  ? 0.9254 0.8496 0.8129 0.2102  0.1122  -0.0570 62  GLU   B C   
673  O  O   . GLU   B 53  ? 0.9332 0.8621 0.8174 0.2077  0.1149  -0.0625 62  GLU   B O   
674  C  CB  . GLU   B 53  ? 0.9995 0.9082 0.8641 0.2514  0.1144  -0.0638 62  GLU   B CB  
675  C  CG  . GLU   B 53  ? 1.1136 0.9944 0.9566 0.2624  0.1192  -0.0687 62  GLU   B CG  
676  C  CD  . GLU   B 53  ? 1.2433 1.1424 1.0801 0.2851  0.1194  -0.0780 62  GLU   B CD  
677  O  OE1 . GLU   B 53  ? 1.2566 1.1876 1.1061 0.2948  0.1157  -0.0801 62  GLU   B OE1 
678  O  OE2 . GLU   B 53  ? 1.2959 1.1780 1.1151 0.2942  0.1223  -0.0841 62  GLU   B OE2 
679  N  N   . GLY   B 54  ? 0.8949 0.8361 0.7976 0.1988  0.1076  -0.0523 63  GLY   B N   
680  C  CA  . GLY   B 54  ? 0.8685 0.8333 0.7854 0.1813  0.1062  -0.0521 63  GLY   B CA  
681  C  C   . GLY   B 54  ? 0.8562 0.8047 0.7701 0.1638  0.1066  -0.0471 63  GLY   B C   
682  O  O   . GLY   B 54  ? 0.8737 0.7977 0.7806 0.1629  0.1067  -0.0422 63  GLY   B O   
683  N  N   . ARG   B 55  ? 0.8196 0.7831 0.7391 0.1507  0.1073  -0.0477 64  ARG   B N   
684  C  CA  . ARG   B 55  ? 0.8006 0.7520 0.7167 0.1356  0.1066  -0.0443 64  ARG   B CA  
685  C  C   . ARG   B 55  ? 0.7513 0.7184 0.6787 0.1229  0.1023  -0.0386 64  ARG   B C   
686  O  O   . ARG   B 55  ? 0.7453 0.7361 0.6837 0.1210  0.1019  -0.0387 64  ARG   B O   
687  C  CB  . ARG   B 55  ? 0.8286 0.7798 0.7359 0.1332  0.1103  -0.0501 64  ARG   B CB  
688  C  CG  . ARG   B 55  ? 0.8832 0.8182 0.7842 0.1209  0.1082  -0.0495 64  ARG   B CG  
689  C  CD  . ARG   B 55  ? 0.9307 0.8648 0.8201 0.1220  0.1101  -0.0571 64  ARG   B CD  
690  N  NE  . ARG   B 55  ? 0.9706 0.8958 0.8557 0.1103  0.1064  -0.0575 64  ARG   B NE  
691  C  CZ  . ARG   B 55  ? 1.0204 0.9271 0.8942 0.1106  0.1038  -0.0654 64  ARG   B CZ  
692  N  NH1 . ARG   B 55  ? 1.0256 0.9173 0.8894 0.1219  0.1047  -0.0731 64  ARG   B NH1 
693  N  NH2 . ARG   B 55  ? 1.0222 0.9246 0.8940 0.1004  0.0989  -0.0666 64  ARG   B NH2 
694  N  N   . LEU   B 56  ? 0.7099 0.6637 0.6350 0.1143  0.0992  -0.0335 65  LEU   B N   
695  C  CA  . LEU   B 56  ? 0.6769 0.6401 0.6079 0.1034  0.0945  -0.0284 65  LEU   B CA  
696  C  C   . LEU   B 56  ? 0.6539 0.6125 0.5778 0.0925  0.0956  -0.0283 65  LEU   B C   
697  O  O   . LEU   B 56  ? 0.6657 0.6082 0.5837 0.0906  0.0952  -0.0283 65  LEU   B O   
698  C  CB  . LEU   B 56  ? 0.6807 0.6343 0.6120 0.1056  0.0890  -0.0228 65  LEU   B CB  
699  C  CG  . LEU   B 56  ? 0.7072 0.6609 0.6411 0.1197  0.0861  -0.0228 65  LEU   B CG  
700  C  CD1 . LEU   B 56  ? 0.7073 0.6549 0.6393 0.1214  0.0794  -0.0169 65  LEU   B CD1 
701  C  CD2 . LEU   B 56  ? 0.7147 0.6900 0.6600 0.1229  0.0837  -0.0275 65  LEU   B CD2 
702  N  N   . ASP   B 57  ? 0.6227 0.5957 0.5477 0.0856  0.0971  -0.0278 66  ASP   B N   
703  C  CA  . ASP   B 57  ? 0.6194 0.5886 0.5345 0.0778  0.0976  -0.0280 66  ASP   B CA  
704  C  C   . ASP   B 57  ? 0.6032 0.5718 0.5179 0.0689  0.0925  -0.0214 66  ASP   B C   
705  O  O   . ASP   B 57  ? 0.5944 0.5709 0.5168 0.0662  0.0900  -0.0168 66  ASP   B O   
706  C  CB  . ASP   B 57  ? 0.6650 0.6482 0.5763 0.0788  0.1040  -0.0307 66  ASP   B CB  
707  C  CG  . ASP   B 57  ? 0.7584 0.7388 0.6649 0.0900  0.1080  -0.0386 66  ASP   B CG  
708  O  OD1 . ASP   B 57  ? 0.7844 0.7449 0.6847 0.0929  0.1055  -0.0431 66  ASP   B OD1 
709  O  OD2 . ASP   B 57  ? 0.7915 0.7893 0.7011 0.0959  0.1137  -0.0400 66  ASP   B OD2 
710  N  N   . PRO   B 58  ? 0.5868 0.5453 0.4924 0.0648  0.0896  -0.0215 67  PRO   B N   
711  C  CA  . PRO   B 58  ? 0.5698 0.5270 0.4714 0.0587  0.0845  -0.0156 67  PRO   B CA  
712  C  C   . PRO   B 58  ? 0.5511 0.5177 0.4497 0.0534  0.0870  -0.0117 67  PRO   B C   
713  O  O   . PRO   B 58  ? 0.5488 0.5240 0.4449 0.0541  0.0937  -0.0138 67  PRO   B O   
714  C  CB  . PRO   B 58  ? 0.5889 0.5383 0.4820 0.0568  0.0818  -0.0188 67  PRO   B CB  
715  C  CG  . PRO   B 58  ? 0.6048 0.5524 0.4950 0.0598  0.0857  -0.0271 67  PRO   B CG  
716  C  CD  . PRO   B 58  ? 0.5871 0.5356 0.4861 0.0658  0.0898  -0.0280 67  PRO   B CD  
717  N  N   . TYR   B 59  ? 0.5308 0.4950 0.4292 0.0489  0.0822  -0.0053 68  TYR   B N   
718  C  CA  . TYR   B 59  ? 0.5195 0.4891 0.4164 0.0421  0.0849  0.0006  68  TYR   B CA  
719  C  C   . TYR   B 59  ? 0.5256 0.4835 0.4064 0.0388  0.0803  0.0052  68  TYR   B C   
720  O  O   . TYR   B 59  ? 0.5309 0.4894 0.4010 0.0354  0.0849  0.0091  68  TYR   B O   
721  C  CB  . TYR   B 59  ? 0.5064 0.4814 0.4198 0.0390  0.0818  0.0037  68  TYR   B CB  
722  C  CG  . TYR   B 59  ? 0.5113 0.4926 0.4291 0.0292  0.0854  0.0109  68  TYR   B CG  
723  C  CD1 . TYR   B 59  ? 0.5230 0.4901 0.4316 0.0228  0.0800  0.0175  68  TYR   B CD1 
724  C  CD2 . TYR   B 59  ? 0.5121 0.5131 0.4435 0.0266  0.0945  0.0119  68  TYR   B CD2 
725  C  CE1 . TYR   B 59  ? 0.5377 0.5074 0.4514 0.0122  0.0838  0.0257  68  TYR   B CE1 
726  C  CE2 . TYR   B 59  ? 0.5212 0.5299 0.4605 0.0159  0.0994  0.0205  68  TYR   B CE2 
727  C  CZ  . TYR   B 59  ? 0.5433 0.5346 0.4742 0.0077  0.0940  0.0278  68  TYR   B CZ  
728  O  OH  . TYR   B 59  ? 0.5674 0.5631 0.5061 -0.0042 0.0998  0.0378  68  TYR   B OH  
729  N  N   . TRP   B 60  ? 0.5271 0.4746 0.4044 0.0415  0.0717  0.0055  69  TRP   B N   
730  C  CA  . TRP   B 60  ? 0.5415 0.4781 0.4018 0.0412  0.0662  0.0093  69  TRP   B CA  
731  C  C   . TRP   B 60  ? 0.5455 0.4791 0.4041 0.0476  0.0603  0.0061  69  TRP   B C   
732  O  O   . TRP   B 60  ? 0.5502 0.4852 0.4200 0.0515  0.0591  0.0047  69  TRP   B O   
733  C  CB  . TRP   B 60  ? 0.5443 0.4708 0.4027 0.0373  0.0604  0.0161  69  TRP   B CB  
734  C  CG  . TRP   B 60  ? 0.5775 0.4895 0.4165 0.0408  0.0524  0.0193  69  TRP   B CG  
735  C  CD1 . TRP   B 60  ? 0.6067 0.5106 0.4263 0.0396  0.0532  0.0233  69  TRP   B CD1 
736  C  CD2 . TRP   B 60  ? 0.5912 0.4961 0.4262 0.0488  0.0430  0.0186  69  TRP   B CD2 
737  N  NE1 . TRP   B 60  ? 0.6192 0.5112 0.4232 0.0463  0.0439  0.0245  69  TRP   B NE1 
738  C  CE2 . TRP   B 60  ? 0.6127 0.5064 0.4264 0.0521  0.0378  0.0218  69  TRP   B CE2 
739  C  CE3 . TRP   B 60  ? 0.5992 0.5065 0.4447 0.0556  0.0389  0.0163  69  TRP   B CE3 
740  C  CZ2 . TRP   B 60  ? 0.6275 0.5147 0.4314 0.0619  0.0288  0.0222  69  TRP   B CZ2 
741  C  CZ3 . TRP   B 60  ? 0.6146 0.5152 0.4501 0.0652  0.0308  0.0177  69  TRP   B CZ3 
742  C  CH2 . TRP   B 60  ? 0.6236 0.5149 0.4391 0.0682  0.0256  0.0204  69  TRP   B CH2 
743  N  N   . GLY   B 61  ? 0.5486 0.4788 0.3929 0.0496  0.0567  0.0061  70  GLY   B N   
744  C  CA  . GLY   B 61  ? 0.5516 0.4832 0.3972 0.0551  0.0515  0.0044  70  GLY   B CA  
745  C  C   . GLY   B 61  ? 0.5534 0.4831 0.3820 0.0580  0.0462  0.0048  70  GLY   B C   
746  O  O   . GLY   B 61  ? 0.5597 0.4867 0.3745 0.0564  0.0476  0.0047  70  GLY   B O   
747  N  N   . ASP   B 62  ? 0.5518 0.4846 0.3807 0.0639  0.0406  0.0056  71  ASP   B N   
748  C  CA  . ASP   B 62  ? 0.5751 0.5090 0.3883 0.0692  0.0344  0.0055  71  ASP   B CA  
749  C  C   . ASP   B 62  ? 0.5609 0.5079 0.3853 0.0744  0.0314  0.0048  71  ASP   B C   
750  O  O   . ASP   B 62  ? 0.5596 0.5060 0.3885 0.0798  0.0303  0.0096  71  ASP   B O   
751  C  CB  . ASP   B 62  ? 0.6239 0.5419 0.4168 0.0734  0.0292  0.0120  71  ASP   B CB  
752  C  CG  . ASP   B 62  ? 0.7391 0.6551 0.5102 0.0806  0.0231  0.0120  71  ASP   B CG  
753  O  OD1 . ASP   B 62  ? 0.7568 0.6838 0.5292 0.0881  0.0182  0.0105  71  ASP   B OD1 
754  O  OD2 . ASP   B 62  ? 0.8129 0.7176 0.5657 0.0794  0.0240  0.0139  71  ASP   B OD2 
755  N  N   . VAL   B 63  ? 0.5604 0.5204 0.3907 0.0728  0.0302  -0.0015 72  VAL   B N   
756  C  CA  . VAL   B 63  ? 0.5426 0.5196 0.3892 0.0751  0.0284  -0.0018 72  VAL   B CA  
757  C  C   . VAL   B 63  ? 0.5555 0.5366 0.3903 0.0869  0.0224  0.0041  72  VAL   B C   
758  O  O   . VAL   B 63  ? 0.5603 0.5526 0.4076 0.0916  0.0237  0.0089  72  VAL   B O   
759  C  CB  . VAL   B 63  ? 0.5403 0.5301 0.3959 0.0698  0.0257  -0.0118 72  VAL   B CB  
760  C  CG1 . VAL   B 63  ? 0.5466 0.5581 0.4171 0.0722  0.0214  -0.0124 72  VAL   B CG1 
761  C  CG2 . VAL   B 63  ? 0.5302 0.5164 0.4018 0.0601  0.0313  -0.0174 72  VAL   B CG2 
762  N  N   . LYS   B 64  ? 0.5764 0.5467 0.3851 0.0931  0.0166  0.0047  73  LYS   B N   
763  C  CA  . LYS   B 64  ? 0.5905 0.5626 0.3841 0.1068  0.0097  0.0093  73  LYS   B CA  
764  C  C   . LYS   B 64  ? 0.5981 0.5578 0.3877 0.1133  0.0097  0.0167  73  LYS   B C   
765  O  O   . LYS   B 64  ? 0.6024 0.5726 0.3945 0.1241  0.0080  0.0208  73  LYS   B O   
766  C  CB  . LYS   B 64  ? 0.5989 0.5604 0.3626 0.1135  0.0029  0.0079  73  LYS   B CB  
767  C  CG  . LYS   B 64  ? 0.6513 0.6185 0.4001 0.1299  -0.0050 0.0110  73  LYS   B CG  
768  C  CD  . LYS   B 64  ? 0.6949 0.6521 0.4127 0.1387  -0.0121 0.0091  73  LYS   B CD  
769  C  CE  . LYS   B 64  ? 0.7426 0.6994 0.4410 0.1572  -0.0202 0.0129  73  LYS   B CE  
770  N  NZ  . LYS   B 64  ? 0.8099 0.7542 0.4745 0.1679  -0.0273 0.0113  73  LYS   B NZ  
771  N  N   . GLN   B 65  ? 0.6036 0.5435 0.3895 0.1073  0.0117  0.0181  74  GLN   B N   
772  C  CA  . GLN   B 65  ? 0.6037 0.5321 0.3880 0.1135  0.0100  0.0229  74  GLN   B CA  
773  C  C   . GLN   B 65  ? 0.5826 0.5250 0.3914 0.1130  0.0172  0.0242  74  GLN   B C   
774  O  O   . GLN   B 65  ? 0.5874 0.5267 0.3945 0.1235  0.0155  0.0283  74  GLN   B O   
775  C  CB  . GLN   B 65  ? 0.6396 0.5462 0.4177 0.1057  0.0094  0.0231  74  GLN   B CB  
776  C  CG  . GLN   B 65  ? 0.7109 0.5994 0.4646 0.1050  0.0042  0.0243  74  GLN   B CG  
777  C  CD  . GLN   B 65  ? 0.8054 0.6744 0.5582 0.0958  0.0043  0.0263  74  GLN   B CD  
778  O  OE1 . GLN   B 65  ? 0.8386 0.7009 0.5987 0.0972  0.0009  0.0268  74  GLN   B OE1 
779  N  NE2 . GLN   B 65  ? 0.8285 0.6894 0.5732 0.0870  0.0079  0.0276  74  GLN   B NE2 
780  N  N   . ASP   B 66  ? 0.5496 0.5054 0.3788 0.1023  0.0246  0.0206  75  ASP   B N   
781  C  CA  . ASP   B 66  ? 0.5334 0.4985 0.3854 0.0995  0.0327  0.0221  75  ASP   B CA  
782  C  C   . ASP   B 66  ? 0.5359 0.4870 0.3893 0.0993  0.0352  0.0230  75  ASP   B C   
783  O  O   . ASP   B 66  ? 0.5227 0.4758 0.3844 0.1057  0.0392  0.0272  75  ASP   B O   
784  C  CB  . ASP   B 66  ? 0.5381 0.5195 0.3982 0.1099  0.0346  0.0287  75  ASP   B CB  
785  C  CG  . ASP   B 66  ? 0.5861 0.5763 0.4706 0.1051  0.0448  0.0318  75  ASP   B CG  
786  O  OD1 . ASP   B 66  ? 0.5932 0.5818 0.4906 0.0923  0.0488  0.0265  75  ASP   B OD1 
787  O  OD2 . ASP   B 66  ? 0.6405 0.6377 0.5292 0.1154  0.0489  0.0400  75  ASP   B OD2 
788  N  N   . LEU   B 67  ? 0.5352 0.4741 0.3817 0.0921  0.0336  0.0194  76  LEU   B N   
789  C  CA  . LEU   B 67  ? 0.5378 0.4674 0.3887 0.0908  0.0350  0.0189  76  LEU   B CA  
790  C  C   . LEU   B 67  ? 0.5378 0.4684 0.3976 0.0787  0.0412  0.0140  76  LEU   B C   
791  O  O   . LEU   B 67  ? 0.5408 0.4739 0.3962 0.0722  0.0422  0.0110  76  LEU   B O   
792  C  CB  . LEU   B 67  ? 0.5530 0.4676 0.3884 0.0945  0.0260  0.0203  76  LEU   B CB  
793  C  CG  . LEU   B 67  ? 0.5725 0.4824 0.3954 0.1099  0.0183  0.0241  76  LEU   B CG  
794  C  CD1 . LEU   B 67  ? 0.6015 0.4916 0.4065 0.1120  0.0073  0.0240  76  LEU   B CD1 
795  C  CD2 . LEU   B 67  ? 0.5660 0.4797 0.3980 0.1201  0.0209  0.0259  76  LEU   B CD2 
796  N  N   . VAL   B 68  ? 0.5197 0.4488 0.3896 0.0781  0.0449  0.0127  77  VAL   B N   
797  C  CA  . VAL   B 68  ? 0.5116 0.4431 0.3890 0.0695  0.0509  0.0082  77  VAL   B CA  
798  C  C   . VAL   B 68  ? 0.5076 0.4373 0.3922 0.0717  0.0506  0.0077  77  VAL   B C   
799  O  O   . VAL   B 68  ? 0.5063 0.4338 0.3933 0.0812  0.0482  0.0093  77  VAL   B O   
800  C  CB  . VAL   B 68  ? 0.5150 0.4521 0.4022 0.0670  0.0578  0.0044  77  VAL   B CB  
801  C  CG1 . VAL   B 68  ? 0.5257 0.4624 0.4218 0.0743  0.0605  0.0074  77  VAL   B CG1 
802  C  CG2 . VAL   B 68  ? 0.5203 0.4591 0.4119 0.0616  0.0636  -0.0011 77  VAL   B CG2 
803  N  N   . SER   B 69  ? 0.4981 0.4308 0.3866 0.0643  0.0532  0.0057  78  SER   B N   
804  C  CA  . SER   B 69  ? 0.4973 0.4338 0.3973 0.0651  0.0528  0.0040  78  SER   B CA  
805  C  C   . SER   B 69  ? 0.4924 0.4393 0.4014 0.0620  0.0622  -0.0002 78  SER   B C   
806  O  O   . SER   B 69  ? 0.4945 0.4439 0.3986 0.0568  0.0676  -0.0014 78  SER   B O   
807  C  CB  . SER   B 69  ? 0.5147 0.4479 0.4144 0.0587  0.0467  0.0063  78  SER   B CB  
808  O  OG  . SER   B 69  ? 0.5580 0.4948 0.4557 0.0481  0.0525  0.0083  78  SER   B OG  
809  N  N   . TYR   B 70  ? 0.4883 0.4410 0.4082 0.0674  0.0633  -0.0031 79  TYR   B N   
810  C  CA  . TYR   B 70  ? 0.4989 0.4611 0.4258 0.0682  0.0714  -0.0076 79  TYR   B CA  
811  C  C   . TYR   B 70  ? 0.5085 0.4847 0.4493 0.0666  0.0707  -0.0088 79  TYR   B C   
812  O  O   . TYR   B 70  ? 0.5080 0.4835 0.4548 0.0696  0.0625  -0.0087 79  TYR   B O   
813  C  CB  . TYR   B 70  ? 0.5021 0.4582 0.4295 0.0793  0.0735  -0.0099 79  TYR   B CB  
814  C  CG  . TYR   B 70  ? 0.5138 0.4595 0.4336 0.0784  0.0761  -0.0090 79  TYR   B CG  
815  C  CD1 . TYR   B 70  ? 0.5214 0.4602 0.4366 0.0800  0.0719  -0.0041 79  TYR   B CD1 
816  C  CD2 . TYR   B 70  ? 0.5331 0.4768 0.4514 0.0766  0.0820  -0.0136 79  TYR   B CD2 
817  C  CE1 . TYR   B 70  ? 0.5334 0.4672 0.4466 0.0775  0.0742  -0.0031 79  TYR   B CE1 
818  C  CE2 . TYR   B 70  ? 0.5436 0.4784 0.4589 0.0738  0.0827  -0.0139 79  TYR   B CE2 
819  C  CZ  . TYR   B 70  ? 0.5482 0.4796 0.4630 0.0734  0.0791  -0.0083 79  TYR   B CZ  
820  O  OH  . TYR   B 70  ? 0.5543 0.4812 0.4707 0.0693  0.0797  -0.0084 79  TYR   B OH  
821  N  N   . CYS   B 71  ? 0.5079 0.4980 0.4541 0.0625  0.0786  -0.0103 80  CYS   B N   
822  C  CA  . CYS   B 71  ? 0.5237 0.5338 0.4874 0.0600  0.0803  -0.0111 80  CYS   B CA  
823  C  C   . CYS   B 71  ? 0.5328 0.5469 0.5043 0.0470  0.0770  -0.0051 80  CYS   B C   
824  O  O   . CYS   B 71  ? 0.5400 0.5739 0.5294 0.0416  0.0802  -0.0043 80  CYS   B O   
825  C  CB  . CYS   B 71  ? 0.5550 0.5708 0.5297 0.0710  0.0753  -0.0163 80  CYS   B CB  
826  S  SG  . CYS   B 71  ? 0.6677 0.6729 0.6313 0.0871  0.0796  -0.0214 80  CYS   B SG  
827  N  N   . GLY   B 72  ? 0.5200 0.5162 0.4791 0.0421  0.0710  -0.0007 81  GLY   B N   
828  C  CA  . GLY   B 72  ? 0.5133 0.5073 0.4769 0.0297  0.0676  0.0055  81  GLY   B CA  
829  C  C   . GLY   B 72  ? 0.5330 0.5037 0.4775 0.0288  0.0599  0.0092  81  GLY   B C   
830  O  O   . GLY   B 72  ? 0.5320 0.4924 0.4621 0.0373  0.0580  0.0072  81  GLY   B O   
831  N  N   . PRO   B 73  ? 0.5383 0.5006 0.4827 0.0182  0.0561  0.0153  82  PRO   B N   
832  C  CA  . PRO   B 73  ? 0.5643 0.5028 0.4872 0.0191  0.0484  0.0188  82  PRO   B CA  
833  C  C   . PRO   B 73  ? 0.5732 0.4985 0.4920 0.0291  0.0341  0.0144  82  PRO   B C   
834  O  O   . PRO   B 73  ? 0.5713 0.5030 0.5057 0.0325  0.0278  0.0093  82  PRO   B O   
835  C  CB  . PRO   B 73  ? 0.5789 0.5101 0.5030 0.0049  0.0492  0.0271  82  PRO   B CB  
836  C  CG  . PRO   B 73  ? 0.5662 0.5162 0.5203 -0.0035 0.0502  0.0261  82  PRO   B CG  
837  C  CD  . PRO   B 73  ? 0.5271 0.5009 0.4912 0.0048  0.0589  0.0199  82  PRO   B CD  
838  N  N   . TRP   B 74  ? 0.5794 0.4877 0.4763 0.0357  0.0288  0.0161  83  TRP   B N   
839  C  CA  . TRP   B 74  ? 0.5951 0.4906 0.4828 0.0483  0.0163  0.0133  83  TRP   B CA  
840  C  C   . TRP   B 74  ? 0.6100 0.4949 0.5052 0.0456  0.0029  0.0113  83  TRP   B C   
841  O  O   . TRP   B 74  ? 0.6151 0.4875 0.5081 0.0343  -0.0005 0.0155  83  TRP   B O   
842  C  CB  . TRP   B 74  ? 0.6025 0.4833 0.4653 0.0542  0.0133  0.0169  83  TRP   B CB  
843  C  CG  . TRP   B 74  ? 0.6055 0.4769 0.4568 0.0702  0.0028  0.0150  83  TRP   B CG  
844  C  CD1 . TRP   B 74  ? 0.6188 0.4710 0.4585 0.0762  -0.0115 0.0145  83  TRP   B CD1 
845  C  CD2 . TRP   B 74  ? 0.6002 0.4808 0.4500 0.0833  0.0061  0.0140  83  TRP   B CD2 
846  N  NE1 . TRP   B 74  ? 0.6251 0.4757 0.4541 0.0945  -0.0169 0.0131  83  TRP   B NE1 
847  C  CE2 . TRP   B 74  ? 0.6119 0.4808 0.4482 0.0984  -0.0053 0.0138  83  TRP   B CE2 
848  C  CE3 . TRP   B 74  ? 0.5936 0.4896 0.4516 0.0837  0.0177  0.0137  83  TRP   B CE3 
849  C  CZ2 . TRP   B 74  ? 0.6149 0.4903 0.4469 0.1141  -0.0034 0.0149  83  TRP   B CZ2 
850  C  CZ3 . TRP   B 74  ? 0.5963 0.4964 0.4523 0.0968  0.0189  0.0146  83  TRP   B CZ3 
851  C  CH2 . TRP   B 74  ? 0.6094 0.5009 0.4530 0.1119  0.0096  0.0161  83  TRP   B CH2 
852  N  N   . LYS   B 75  ? 0.6063 0.4948 0.5096 0.0565  -0.0051 0.0048  84  LYS   B N   
853  C  CA  . LYS   B 75  ? 0.6221 0.5031 0.5357 0.0553  -0.0202 -0.0002 84  LYS   B CA  
854  C  C   . LYS   B 75  ? 0.6685 0.5267 0.5621 0.0704  -0.0370 -0.0034 84  LYS   B C   
855  O  O   . LYS   B 75  ? 0.6927 0.5390 0.5915 0.0686  -0.0522 -0.0082 84  LYS   B O   
856  C  CB  . LYS   B 75  ? 0.6077 0.5097 0.5441 0.0597  -0.0200 -0.0075 84  LYS   B CB  
857  C  CG  . LYS   B 75  ? 0.6170 0.5443 0.5737 0.0488  -0.0043 -0.0060 84  LYS   B CG  
858  C  CD  . LYS   B 75  ? 0.6683 0.6009 0.6438 0.0281  -0.0032 -0.0023 84  LYS   B CD  
859  C  CE  . LYS   B 75  ? 0.7065 0.6691 0.7060 0.0211  0.0097  -0.0025 84  LYS   B CE  
860  N  NZ  . LYS   B 75  ? 0.7571 0.7283 0.7776 0.0009  0.0125  0.0030  84  LYS   B NZ  
861  N  N   . LEU   B 76  ? 0.6774 0.5312 0.5500 0.0863  -0.0351 -0.0013 85  LEU   B N   
862  C  CA  . LEU   B 76  ? 0.6978 0.5341 0.5499 0.1055  -0.0496 -0.0042 85  LEU   B CA  
863  C  C   . LEU   B 76  ? 0.7325 0.5441 0.5628 0.1032  -0.0580 -0.0006 85  LEU   B C   
864  O  O   . LEU   B 76  ? 0.7234 0.5354 0.5415 0.1011  -0.0489 0.0059  85  LEU   B O   
865  C  CB  . LEU   B 76  ? 0.6941 0.5401 0.5352 0.1244  -0.0420 -0.0019 85  LEU   B CB  
866  C  CG  . LEU   B 76  ? 0.6864 0.5543 0.5453 0.1260  -0.0294 -0.0030 85  LEU   B CG  
867  C  CD1 . LEU   B 76  ? 0.6929 0.5662 0.5407 0.1429  -0.0215 0.0016  85  LEU   B CD1 
868  C  CD2 . LEU   B 76  ? 0.6864 0.5582 0.5593 0.1306  -0.0384 -0.0113 85  LEU   B CD2 
869  N  N   . ASP   B 77  ? 0.7678 0.5569 0.5929 0.1040  -0.0762 -0.0055 86  ASP   B N   
870  C  CA  . ASP   B 77  ? 0.8267 0.5872 0.6284 0.1025  -0.0849 -0.0020 86  ASP   B CA  
871  C  C   . ASP   B 77  ? 0.8614 0.5963 0.6379 0.1236  -0.1053 -0.0079 86  ASP   B C   
872  O  O   . ASP   B 77  ? 0.8943 0.6007 0.6503 0.1228  -0.1154 -0.0064 86  ASP   B O   
873  C  CB  . ASP   B 77  ? 0.8808 0.6298 0.6961 0.0772  -0.0854 0.0010  86  ASP   B CB  
874  C  CG  . ASP   B 77  ? 0.9922 0.7399 0.8332 0.0671  -0.0976 -0.0066 86  ASP   B CG  
875  O  OD1 . ASP   B 77  ? 1.0144 0.7740 0.8644 0.0800  -0.1046 -0.0154 86  ASP   B OD1 
876  O  OD2 . ASP   B 77  ? 1.0440 0.7794 0.8968 0.0465  -0.1001 -0.0035 86  ASP   B OD2 
877  N  N   . ALA   B 78  ? 0.8493 0.5923 0.6229 0.1447  -0.1109 -0.0139 87  ALA   B N   
878  C  CA  . ALA   B 78  ? 0.8672 0.5872 0.6127 0.1694  -0.1299 -0.0195 87  ALA   B CA  
879  C  C   . ALA   B 78  ? 0.8809 0.5987 0.5968 0.1861  -0.1241 -0.0121 87  ALA   B C   
880  O  O   . ALA   B 78  ? 0.8539 0.5954 0.5753 0.1837  -0.1055 -0.0044 87  ALA   B O   
881  C  CB  . ALA   B 78  ? 0.8572 0.5880 0.6065 0.1895  -0.1364 -0.0274 87  ALA   B CB  
882  N  N   . ALA   B 79  ? 0.9116 0.6013 0.5965 0.2036  -0.1411 -0.0150 88  ALA   B N   
883  C  CA  . ALA   B 79  ? 0.9357 0.6243 0.5913 0.2222  -0.1377 -0.0087 88  ALA   B CA  
884  C  C   . ALA   B 79  ? 0.9557 0.6339 0.5830 0.2566  -0.1521 -0.0136 88  ALA   B C   
885  O  O   . ALA   B 79  ? 0.9614 0.6168 0.5821 0.2644  -0.1719 -0.0238 88  ALA   B O   
886  C  CB  . ALA   B 79  ? 0.9574 0.6192 0.5956 0.2116  -0.1430 -0.0056 88  ALA   B CB  
887  N  N   . TRP   B 80  ? 0.9654 0.6613 0.5762 0.2779  -0.1426 -0.0065 89  TRP   B N   
888  C  CA  . TRP   B 80  ? 0.9991 0.6882 0.5788 0.3143  -0.1536 -0.0088 89  TRP   B CA  
889  C  C   . TRP   B 80  ? 1.0472 0.6943 0.5938 0.3236  -0.1766 -0.0154 89  TRP   B C   
890  O  O   . TRP   B 80  ? 1.0399 0.6748 0.5815 0.3087  -0.1752 -0.0118 89  TRP   B O   
891  C  CB  . TRP   B 80  ? 0.9897 0.7095 0.5622 0.3305  -0.1362 0.0027  89  TRP   B CB  
892  C  CG  . TRP   B 80  ? 1.0083 0.7260 0.5485 0.3697  -0.1443 0.0028  89  TRP   B CG  
893  C  CD1 . TRP   B 80  ? 1.0264 0.7362 0.5548 0.3932  -0.1552 -0.0035 89  TRP   B CD1 
894  C  CD2 . TRP   B 80  ? 1.0132 0.7374 0.5266 0.3924  -0.1428 0.0092  89  TRP   B CD2 
895  N  NE1 . TRP   B 80  ? 1.0427 0.7516 0.5364 0.4299  -0.1605 -0.0012 89  TRP   B NE1 
896  C  CE2 . TRP   B 80  ? 1.0351 0.7552 0.5206 0.4299  -0.1521 0.0072  89  TRP   B CE2 
897  C  CE3 . TRP   B 80  ? 1.0161 0.7514 0.5258 0.3866  -0.1347 0.0160  89  TRP   B CE3 
898  C  CZ2 . TRP   B 80  ? 1.0513 0.7797 0.5069 0.4611  -0.1521 0.0129  89  TRP   B CZ2 
899  C  CZ3 . TRP   B 80  ? 1.0329 0.7765 0.5141 0.4169  -0.1360 0.0207  89  TRP   B CZ3 
900  C  CH2 . TRP   B 80  ? 1.0420 0.7831 0.4970 0.4535  -0.1440 0.0196  89  TRP   B CH2 
901  N  N   . ASP   B 81  ? 1.0936 0.7155 0.6168 0.3476  -0.1984 -0.0256 90  ASP   B N   
902  C  CA  . ASP   B 81  ? 1.1473 0.7233 0.6377 0.3561  -0.2224 -0.0331 90  ASP   B CA  
903  C  C   . ASP   B 81  ? 1.1972 0.7685 0.6480 0.3837  -0.2232 -0.0276 90  ASP   B C   
904  O  O   . ASP   B 81  ? 1.2322 0.7637 0.6527 0.3907  -0.2416 -0.0326 90  ASP   B O   
905  C  CB  . ASP   B 81  ? 1.1746 0.7216 0.6538 0.3714  -0.2490 -0.0485 90  ASP   B CB  
906  C  CG  . ASP   B 81  ? 1.2333 0.7953 0.6936 0.4102  -0.2514 -0.0510 90  ASP   B CG  
907  O  OD1 . ASP   B 81  ? 1.2190 0.8114 0.6710 0.4277  -0.2329 -0.0395 90  ASP   B OD1 
908  O  OD2 . ASP   B 81  ? 1.2975 0.8417 0.7519 0.4236  -0.2718 -0.0644 90  ASP   B OD2 
909  N  N   . GLY   B 82  ? 1.2002 0.8114 0.6519 0.3996  -0.2042 -0.0175 91  GLY   B N   
910  C  CA  . GLY   B 82  ? 1.2344 0.8510 0.6533 0.4272  -0.2027 -0.0115 91  GLY   B CA  
911  C  C   . GLY   B 82  ? 1.2764 0.8848 0.6587 0.4712  -0.2165 -0.0161 91  GLY   B C   
912  O  O   . GLY   B 82  ? 1.2964 0.9110 0.6490 0.4987  -0.2161 -0.0113 91  GLY   B O   
913  N  N   . LEU   B 83  ? 1.2843 0.8796 0.6667 0.4805  -0.2293 -0.0258 92  LEU   B N   
914  C  CA  . LEU   B 83  ? 1.3132 0.8980 0.6577 0.5251  -0.2442 -0.0316 92  LEU   B CA  
915  C  C   . LEU   B 83  ? 1.2871 0.9011 0.6440 0.5408  -0.2340 -0.0292 92  LEU   B C   
916  O  O   . LEU   B 83  ? 1.2957 0.9247 0.6271 0.5787  -0.2306 -0.0243 92  LEU   B O   
917  C  CB  . LEU   B 83  ? 1.3592 0.8879 0.6787 0.5315  -0.2784 -0.0499 92  LEU   B CB  
918  C  CG  . LEU   B 83  ? 1.4208 0.9051 0.7171 0.5233  -0.2958 -0.0549 92  LEU   B CG  
919  C  CD1 . LEU   B 83  ? 1.4594 0.8900 0.7351 0.5310  -0.3302 -0.0738 92  LEU   B CD1 
920  C  CD2 . LEU   B 83  ? 1.4465 0.9343 0.7031 0.5549  -0.2934 -0.0479 92  LEU   B CD2 
921  N  N   . SER   B 84  ? 1.2559 0.8737 0.6475 0.5152  -0.2317 -0.0338 93  SER   B N   
922  C  CA  . SER   B 84  ? 1.2348 0.8700 0.6355 0.5295  -0.2274 -0.0351 93  SER   B CA  
923  C  C   . SER   B 84  ? 1.1869 0.8701 0.6130 0.5260  -0.1951 -0.0182 93  SER   B C   
924  O  O   . SER   B 84  ? 1.1732 0.8792 0.6238 0.5005  -0.1750 -0.0071 93  SER   B O   
925  C  CB  . SER   B 84  ? 1.2545 0.8715 0.6808 0.5046  -0.2418 -0.0492 93  SER   B CB  
926  O  OG  . SER   B 84  ? 1.3044 0.8769 0.7177 0.4963  -0.2696 -0.0634 93  SER   B OG  
927  N  N   . GLU   B 85  ? 1.1578 0.8541 0.5776 0.5521  -0.1909 -0.0168 94  GLU   B N   
928  C  CA  . GLU   B 85  ? 1.1190 0.8553 0.5626 0.5493  -0.1612 -0.0008 94  GLU   B CA  
929  C  C   . GLU   B 85  ? 1.0723 0.8141 0.5586 0.5104  -0.1542 -0.0042 94  GLU   B C   
930  O  O   . GLU   B 85  ? 1.0763 0.7940 0.5706 0.4946  -0.1735 -0.0193 94  GLU   B O   
931  C  CB  . GLU   B 85  ? 1.1578 0.9031 0.5764 0.5926  -0.1584 0.0030  94  GLU   B CB  
932  C  CG  . GLU   B 85  ? 1.2520 1.0067 0.6346 0.6306  -0.1547 0.0129  94  GLU   B CG  
933  C  CD  . GLU   B 85  ? 1.3365 1.1075 0.6959 0.6735  -0.1446 0.0224  94  GLU   B CD  
934  O  OE1 . GLU   B 85  ? 1.3310 1.0999 0.6959 0.6787  -0.1446 0.0186  94  GLU   B OE1 
935  O  OE2 . GLU   B 85  ? 1.3748 1.1623 0.7101 0.7033  -0.1358 0.0342  94  GLU   B OE2 
936  N  N   . VAL   B 86  ? 1.0198 0.7938 0.5345 0.4941  -0.1268 0.0101  95  VAL   B N   
937  C  CA  . VAL   B 86  ? 0.9623 0.7452 0.5160 0.4593  -0.1167 0.0090  95  VAL   B CA  
938  C  C   . VAL   B 86  ? 0.9377 0.7454 0.5020 0.4698  -0.0949 0.0206  95  VAL   B C   
939  O  O   . VAL   B 86  ? 0.9551 0.7759 0.5003 0.4988  -0.0845 0.0321  95  VAL   B O   
940  C  CB  . VAL   B 86  ? 0.9290 0.7230 0.5081 0.4229  -0.1041 0.0151  95  VAL   B CB  
941  C  CG1 . VAL   B 86  ? 0.9387 0.7070 0.5024 0.4156  -0.1229 0.0070  95  VAL   B CG1 
942  C  CG2 . VAL   B 86  ? 0.9083 0.7344 0.4944 0.4260  -0.0792 0.0328  95  VAL   B CG2 
943  N  N   . GLN   B 87  ? 0.8911 0.7061 0.4856 0.4463  -0.0860 0.0192  96  GLN   B N   
944  C  CA  . GLN   B 87  ? 0.8750 0.7100 0.4802 0.4528  -0.0639 0.0312  96  GLN   B CA  
945  C  C   . GLN   B 87  ? 0.8496 0.7026 0.4911 0.4166  -0.0431 0.0394  96  GLN   B C   
946  O  O   . GLN   B 87  ? 0.8413 0.6885 0.5031 0.3878  -0.0489 0.0304  96  GLN   B O   
947  C  CB  . GLN   B 87  ? 0.9000 0.7248 0.5010 0.4673  -0.0738 0.0209  96  GLN   B CB  
948  C  CG  . GLN   B 87  ? 0.9571 0.7708 0.5187 0.5120  -0.0869 0.0180  96  GLN   B CG  
949  C  CD  . GLN   B 87  ? 1.0041 0.8092 0.5579 0.5317  -0.0974 0.0075  96  GLN   B CD  
950  O  OE1 . GLN   B 87  ? 0.9773 0.7884 0.5551 0.5151  -0.0910 0.0051  96  GLN   B OE1 
951  N  NE2 . GLN   B 87  ? 1.0544 0.8451 0.5717 0.5706  -0.1152 0.0002  96  GLN   B NE2 
952  N  N   . LEU   B 88  ? 0.8313 0.7057 0.4809 0.4190  -0.0194 0.0563  97  LEU   B N   
953  C  CA  . LEU   B 88  ? 0.8160 0.7055 0.4983 0.3886  -0.0002 0.0636  97  LEU   B CA  
954  C  C   . LEU   B 88  ? 0.8188 0.7063 0.5074 0.3938  0.0077  0.0643  97  LEU   B C   
955  O  O   . LEU   B 88  ? 0.8365 0.7270 0.5095 0.4212  0.0167  0.0741  97  LEU   B O   
956  C  CB  . LEU   B 88  ? 0.8068 0.7201 0.4969 0.3883  0.0204  0.0814  97  LEU   B CB  
957  C  CG  . LEU   B 88  ? 0.8056 0.7334 0.5283 0.3624  0.0419  0.0905  97  LEU   B CG  
958  C  CD1 . LEU   B 88  ? 0.7942 0.7183 0.5393 0.3269  0.0367  0.0796  97  LEU   B CD1 
959  C  CD2 . LEU   B 88  ? 0.8055 0.7578 0.5374 0.3648  0.0610  0.1083  97  LEU   B CD2 
960  N  N   . LEU   B 89  ? 0.7937 0.6763 0.5030 0.3700  0.0053  0.0549  98  LEU   B N   
961  C  CA  . LEU   B 89  ? 0.7924 0.6735 0.5081 0.3742  0.0130  0.0550  98  LEU   B CA  
962  C  C   . LEU   B 89  ? 0.7848 0.6789 0.5221 0.3561  0.0376  0.0691  98  LEU   B C   
963  O  O   . LEU   B 89  ? 0.7657 0.6619 0.5263 0.3280  0.0417  0.0650  98  LEU   B O   
964  C  CB  . LEU   B 89  ? 0.7979 0.6703 0.5258 0.3591  -0.0023 0.0375  98  LEU   B CB  
965  C  CG  . LEU   B 89  ? 0.8255 0.6983 0.5644 0.3585  0.0047  0.0350  98  LEU   B CG  
966  C  CD1 . LEU   B 89  ? 0.8559 0.7256 0.5738 0.3915  0.0118  0.0428  98  LEU   B CD1 
967  C  CD2 . LEU   B 89  ? 0.8374 0.7054 0.5858 0.3500  -0.0141 0.0168  98  LEU   B CD2 
968  N  N   . ALA   B 90  ? 0.7828 0.6860 0.5125 0.3723  0.0538  0.0861  99  ALA   B N   
969  C  CA  . ALA   B 90  ? 0.7688 0.6842 0.5203 0.3556  0.0767  0.1009  99  ALA   B CA  
970  C  C   . ALA   B 90  ? 0.7597 0.6671 0.5207 0.3511  0.0884  0.1034  99  ALA   B C   
971  O  O   . ALA   B 90  ? 0.7810 0.6798 0.5236 0.3770  0.0906  0.1066  99  ALA   B O   
972  C  CB  . ALA   B 90  ? 0.7685 0.6980 0.5111 0.3750  0.0911  0.1197  99  ALA   B CB  
973  N  N   . VAL   B 91  ? 0.7303 0.6393 0.5173 0.3209  0.0961  0.1020  100 VAL   B N   
974  C  CA  . VAL   B 91  ? 0.7201 0.6191 0.5157 0.3156  0.1079  0.1045  100 VAL   B CA  
975  C  C   . VAL   B 91  ? 0.7189 0.6248 0.5347 0.2993  0.1287  0.1204  100 VAL   B C   
976  O  O   . VAL   B 91  ? 0.7056 0.6140 0.5435 0.2714  0.1301  0.1157  100 VAL   B O   
977  C  CB  . VAL   B 91  ? 0.7176 0.6098 0.5244 0.2967  0.0970  0.0869  100 VAL   B CB  
978  C  CG1 . VAL   B 91  ? 0.7222 0.6026 0.5336 0.2956  0.1081  0.0886  100 VAL   B CG1 
979  C  CG2 . VAL   B 91  ? 0.7252 0.6140 0.5180 0.3095  0.0757  0.0717  100 VAL   B CG2 
980  N  N   . PRO   B 92  ? 0.7255 0.6360 0.5347 0.3165  0.1447  0.1396  101 PRO   B N   
981  C  CA  . PRO   B 92  ? 0.7121 0.6315 0.5456 0.2985  0.1640  0.1554  101 PRO   B CA  
982  C  C   . PRO   B 92  ? 0.7273 0.6282 0.5719 0.2862  0.1761  0.1585  101 PRO   B C   
983  O  O   . PRO   B 92  ? 0.7478 0.6304 0.5751 0.3017  0.1750  0.1550  101 PRO   B O   
984  C  CB  . PRO   B 92  ? 0.7277 0.6590 0.5488 0.3240  0.1774  0.1758  101 PRO   B CB  
985  C  CG  . PRO   B 92  ? 0.7460 0.6733 0.5327 0.3570  0.1623  0.1682  101 PRO   B CG  
986  C  CD  . PRO   B 92  ? 0.7302 0.6388 0.5104 0.3534  0.1459  0.1480  101 PRO   B CD  
987  N  N   . PRO   B 93  ? 0.7206 0.6251 0.5932 0.2598  0.1873  0.1651  102 PRO   B N   
988  C  CA  . PRO   B 93  ? 0.7357 0.6178 0.6173 0.2475  0.1971  0.1668  102 PRO   B CA  
989  C  C   . PRO   B 93  ? 0.7672 0.6322 0.6310 0.2714  0.2135  0.1839  102 PRO   B C   
990  O  O   . PRO   B 93  ? 0.7637 0.6392 0.6221 0.2875  0.2257  0.2021  102 PRO   B O   
991  C  CB  . PRO   B 93  ? 0.7240 0.6159 0.6395 0.2167  0.2047  0.1718  102 PRO   B CB  
992  C  CG  . PRO   B 93  ? 0.7132 0.6316 0.6364 0.2085  0.1913  0.1627  102 PRO   B CG  
993  C  CD  . PRO   B 93  ? 0.6991 0.6271 0.5965 0.2392  0.1883  0.1681  102 PRO   B CD  
994  N  N   . GLY   B 94  ? 0.7821 0.6222 0.6334 0.2774  0.2127  0.1775  103 GLY   B N   
995  C  CA  . GLY   B 94  ? 0.8088 0.6276 0.6386 0.3020  0.2270  0.1917  103 GLY   B CA  
996  C  C   . GLY   B 94  ? 0.8252 0.6492 0.6236 0.3398  0.2247  0.1964  103 GLY   B C   
997  O  O   . GLY   B 94  ? 0.8359 0.6441 0.6136 0.3640  0.2379  0.2106  103 GLY   B O   
998  N  N   . GLU   B 95  ? 0.8286 0.6730 0.6214 0.3466  0.2080  0.1854  104 GLU   B N   
999  C  CA  . GLU   B 95  ? 0.8498 0.6986 0.6115 0.3838  0.2032  0.1883  104 GLU   B CA  
1000 C  C   . GLU   B 95  ? 0.8764 0.7247 0.6234 0.3940  0.1774  0.1640  104 GLU   B C   
1001 O  O   . GLU   B 95  ? 0.8638 0.7176 0.6280 0.3697  0.1632  0.1470  104 GLU   B O   
1002 C  CB  . GLU   B 95  ? 0.8470 0.7200 0.6116 0.3891  0.2089  0.2017  104 GLU   B CB  
1003 C  CG  . GLU   B 95  ? 0.8513 0.7295 0.6337 0.3801  0.2357  0.2279  104 GLU   B CG  
1004 C  CD  . GLU   B 95  ? 0.8976 0.8058 0.6885 0.3829  0.2422  0.2413  104 GLU   B CD  
1005 O  OE1 . GLU   B 95  ? 0.8806 0.8042 0.6660 0.3862  0.2242  0.2280  104 GLU   B OE1 
1006 O  OE2 . GLU   B 95  ? 0.9149 0.8312 0.7180 0.3820  0.2657  0.2655  104 GLU   B OE2 
1007 N  N   . ARG   B 96  ? 0.9009 0.7431 0.6163 0.4303  0.1710  0.1624  105 ARG   B N   
1008 C  CA  . ARG   B 96  ? 0.9281 0.7697 0.6302 0.4425  0.1454  0.1394  105 ARG   B CA  
1009 C  C   . ARG   B 96  ? 0.9118 0.7693 0.6211 0.4315  0.1273  0.1276  105 ARG   B C   
1010 O  O   . ARG   B 96  ? 0.9106 0.7802 0.6203 0.4327  0.1337  0.1392  105 ARG   B O   
1011 C  CB  . ARG   B 96  ? 0.9953 0.8280 0.6602 0.4872  0.1424  0.1417  105 ARG   B CB  
1012 C  CG  . ARG   B 96  ? 1.0876 0.9197 0.7399 0.5017  0.1142  0.1169  105 ARG   B CG  
1013 C  CD  . ARG   B 96  ? 1.1791 0.9973 0.8048 0.5354  0.1112  0.1128  105 ARG   B CD  
1014 N  NE  . ARG   B 96  ? 1.2630 1.0726 0.8589 0.5699  0.1291  0.1339  105 ARG   B NE  
1015 C  CZ  . ARG   B 96  ? 1.3269 1.1400 0.8949 0.6026  0.1240  0.1380  105 ARG   B CZ  
1016 N  NH1 . ARG   B 96  ? 1.3175 1.1401 0.8836 0.6044  0.1000  0.1214  105 ARG   B NH1 
1017 N  NH2 . ARG   B 96  ? 1.3611 1.1668 0.9015 0.6346  0.1432  0.1592  105 ARG   B NH2 
1018 N  N   . ALA   B 97  ? 0.9016 0.7594 0.6162 0.4222  0.1050  0.1052  106 ALA   B N   
1019 C  CA  . ALA   B 97  ? 0.9051 0.7726 0.6230 0.4137  0.0859  0.0931  106 ALA   B CA  
1020 C  C   . ALA   B 97  ? 0.9286 0.7959 0.6158 0.4492  0.0778  0.0960  106 ALA   B C   
1021 O  O   . ALA   B 97  ? 0.9461 0.8044 0.6096 0.4802  0.0745  0.0946  106 ALA   B O   
1022 C  CB  . ALA   B 97  ? 0.9026 0.7679 0.6292 0.4024  0.0652  0.0708  106 ALA   B CB  
1023 N  N   . LYS   B 98  ? 0.9284 0.8051 0.6138 0.4473  0.0743  0.0993  107 LYS   B N   
1024 C  CA  . LYS   B 98  ? 0.9577 0.8347 0.6120 0.4825  0.0676  0.1030  107 LYS   B CA  
1025 C  C   . LYS   B 98  ? 0.9466 0.8265 0.5988 0.4759  0.0480  0.0918  107 LYS   B C   
1026 O  O   . LYS   B 98  ? 0.9445 0.8351 0.6170 0.4494  0.0537  0.0958  107 LYS   B O   
1027 C  CB  . LYS   B 98  ? 1.0048 0.8931 0.6563 0.4926  0.0940  0.1288  107 LYS   B CB  
1028 C  CG  . LYS   B 98  ? 1.1139 1.0049 0.7306 0.5344  0.0939  0.1380  107 LYS   B CG  
1029 C  CD  . LYS   B 98  ? 1.1921 1.0994 0.8134 0.5394  0.1236  0.1662  107 LYS   B CD  
1030 C  CE  . LYS   B 98  ? 1.2267 1.1526 0.8837 0.5019  0.1334  0.1726  107 LYS   B CE  
1031 N  NZ  . LYS   B 98  ? 1.2500 1.1990 0.9061 0.5141  0.1514  0.1944  107 LYS   B NZ  
1032 N  N   . ASN   B 99  ? 0.9438 0.8128 0.5712 0.4996  0.0242  0.0772  108 ASN   B N   
1033 C  CA  . ASN   B 99  ? 0.9545 0.8210 0.5764 0.4947  0.0048  0.0669  108 ASN   B CA  
1034 C  C   . ASN   B 99  ? 0.9724 0.8468 0.5704 0.5210  0.0111  0.0806  108 ASN   B C   
1035 O  O   . ASN   B 99  ? 0.9885 0.8614 0.5593 0.5576  0.0154  0.0880  108 ASN   B O   
1036 C  CB  . ASN   B 99  ? 0.9798 0.8284 0.5856 0.5084  -0.0255 0.0447  108 ASN   B CB  
1037 C  CG  . ASN   B 99  ? 1.0136 0.8575 0.6430 0.4852  -0.0355 0.0293  108 ASN   B CG  
1038 O  OD1 . ASN   B 99  ? 1.0195 0.8662 0.6566 0.4866  -0.0252 0.0314  108 ASN   B OD1 
1039 N  ND2 . ASN   B 99  ? 1.0136 0.8501 0.6540 0.4649  -0.0557 0.0137  108 ASN   B ND2 
1040 N  N   . ILE   B 100 ? 0.9649 0.8477 0.5697 0.5061  0.0105  0.0831  109 ILE   B N   
1041 C  CA  . ILE   B 100 ? 0.9736 0.8677 0.5575 0.5303  0.0157  0.0952  109 ILE   B CA  
1042 C  C   . ILE   B 100 ? 0.9840 0.8659 0.5535 0.5305  -0.0092 0.0804  109 ILE   B C   
1043 O  O   . ILE   B 100 ? 0.9818 0.8632 0.5723 0.4980  -0.0139 0.0740  109 ILE   B O   
1044 C  CB  . ILE   B 100 ? 0.9693 0.8899 0.5795 0.5103  0.0422  0.1150  109 ILE   B CB  
1045 C  CG1 . ILE   B 100 ? 0.9757 0.9034 0.6061 0.5011  0.0666  0.1289  109 ILE   B CG1 
1046 C  CG2 . ILE   B 100 ? 0.9822 0.9206 0.5734 0.5363  0.0490  0.1286  109 ILE   B CG2 
1047 C  CD1 . ILE   B 100 ? 0.9999 0.9261 0.6052 0.5384  0.0774  0.1412  109 ILE   B CD1 
1048 N  N   . GLN   B 101 ? 0.9967 0.8674 0.5284 0.5678  -0.0247 0.0756  110 GLN   B N   
1049 C  CA  . GLN   B 101 ? 1.0144 0.8676 0.5273 0.5715  -0.0502 0.0611  110 GLN   B CA  
1050 C  C   . GLN   B 101 ? 1.0186 0.8891 0.5235 0.5784  -0.0414 0.0734  110 GLN   B C   
1051 O  O   . GLN   B 101 ? 1.0263 0.9183 0.5215 0.6025  -0.0227 0.0909  110 GLN   B O   
1052 C  CB  . GLN   B 101 ? 1.0618 0.8910 0.5354 0.6107  -0.0746 0.0472  110 GLN   B CB  
1053 C  CG  . GLN   B 101 ? 1.1176 0.9207 0.5699 0.6147  -0.1045 0.0299  110 GLN   B CG  
1054 C  CD  . GLN   B 101 ? 1.1737 0.9480 0.6028 0.6369  -0.1336 0.0093  110 GLN   B CD  
1055 O  OE1 . GLN   B 101 ? 1.1578 0.9301 0.5997 0.6329  -0.1354 0.0026  110 GLN   B OE1 
1056 N  NE2 . GLN   B 101 ? 1.2071 0.9582 0.6009 0.6617  -0.1581 -0.0020 110 GLN   B NE2 
1057 N  N   . THR   B 102 ? 1.0114 0.8739 0.5200 0.5585  -0.0541 0.0650  111 THR   B N   
1058 C  CA  . THR   B 102 ? 1.0066 0.8863 0.5086 0.5637  -0.0477 0.0746  111 THR   B CA  
1059 C  C   . THR   B 102 ? 1.0167 0.8715 0.5026 0.5576  -0.0723 0.0598  111 THR   B C   
1060 O  O   . THR   B 102 ? 1.0343 0.8639 0.5289 0.5347  -0.0884 0.0449  111 THR   B O   
1061 C  CB  . THR   B 102 ? 1.0061 0.9193 0.5483 0.5332  -0.0204 0.0904  111 THR   B CB  
1062 O  OG1 . THR   B 102 ? 1.0253 0.9632 0.5607 0.5462  -0.0117 0.1021  111 THR   B OG1 
1063 C  CG2 . THR   B 102 ? 1.0058 0.9117 0.5797 0.4881  -0.0236 0.0811  111 THR   B CG2 
1064 N  N   . LEU   B 103 ? 1.0073 0.8689 0.4698 0.5783  -0.0747 0.0644  112 LEU   B N   
1065 C  CA  . LEU   B 103 ? 1.0179 0.8546 0.4644 0.5716  -0.0959 0.0521  112 LEU   B CA  
1066 C  C   . LEU   B 103 ? 1.0042 0.8660 0.4805 0.5408  -0.0800 0.0608  112 LEU   B C   
1067 O  O   . LEU   B 103 ? 0.9920 0.8890 0.4738 0.5504  -0.0620 0.0755  112 LEU   B O   
1068 C  CB  . LEU   B 103 ? 1.0448 0.8688 0.4430 0.6142  -0.1119 0.0493  112 LEU   B CB  
1069 C  CG  . LEU   B 103 ? 1.0869 0.8811 0.4687 0.6043  -0.1331 0.0374  112 LEU   B CG  
1070 C  CD1 . LEU   B 103 ? 1.1132 0.8602 0.4867 0.5933  -0.1599 0.0179  112 LEU   B CD1 
1071 C  CD2 . LEU   B 103 ? 1.1264 0.9199 0.4665 0.6426  -0.1411 0.0393  112 LEU   B CD2 
1072 N  N   . PRO   B 104 ? 1.0008 0.8461 0.4961 0.5047  -0.0869 0.0517  113 PRO   B N   
1073 C  CA  . PRO   B 104 ? 0.9822 0.8501 0.5038 0.4769  -0.0733 0.0583  113 PRO   B CA  
1074 C  C   . PRO   B 104 ? 0.9992 0.8724 0.4982 0.4920  -0.0784 0.0604  113 PRO   B C   
1075 O  O   . PRO   B 104 ? 1.0284 0.8705 0.4915 0.5105  -0.0996 0.0511  113 PRO   B O   
1076 C  CB  . PRO   B 104 ? 0.9930 0.8355 0.5313 0.4409  -0.0827 0.0468  113 PRO   B CB  
1077 C  CG  . PRO   B 104 ? 1.0054 0.8254 0.5422 0.4436  -0.0933 0.0376  113 PRO   B CG  
1078 C  CD  . PRO   B 104 ? 1.0038 0.8129 0.5013 0.4870  -0.1056 0.0359  113 PRO   B CD  
1079 N  N   . GLY   B 105 ? 0.9754 0.8869 0.4974 0.4820  -0.0601 0.0717  114 GLY   B N   
1080 C  CA  . GLY   B 105 ? 0.9729 0.8955 0.4815 0.4899  -0.0631 0.0732  114 GLY   B CA  
1081 C  C   . GLY   B 105 ? 0.9771 0.8797 0.4938 0.4583  -0.0713 0.0642  114 GLY   B C   
1082 O  O   . GLY   B 105 ? 0.9793 0.8538 0.5043 0.4358  -0.0782 0.0558  114 GLY   B O   
1083 N  N   . ILE   B 106 ? 0.9660 0.8856 0.4813 0.4568  -0.0697 0.0663  115 ILE   B N   
1084 C  CA  . ILE   B 106 ? 0.9825 0.8843 0.4992 0.4323  -0.0768 0.0591  115 ILE   B CA  
1085 C  C   . ILE   B 106 ? 0.9496 0.8924 0.4970 0.4144  -0.0617 0.0648  115 ILE   B C   
1086 O  O   . ILE   B 106 ? 0.9495 0.9286 0.4986 0.4318  -0.0545 0.0721  115 ILE   B O   
1087 C  CB  . ILE   B 106 ? 1.0390 0.9085 0.5080 0.4561  -0.0975 0.0525  115 ILE   B CB  
1088 C  CG1 . ILE   B 106 ? 1.1061 0.9285 0.5421 0.4730  -0.1171 0.0440  115 ILE   B CG1 
1089 C  CG2 . ILE   B 106 ? 1.0572 0.9099 0.5217 0.4365  -0.1034 0.0475  115 ILE   B CG2 
1090 C  CD1 . ILE   B 106 ? 1.1421 0.9336 0.5926 0.4450  -0.1227 0.0366  115 ILE   B CD1 
1091 N  N   . PHE   B 107 ? 0.9219 0.8581 0.4909 0.3815  -0.0590 0.0605  116 PHE   B N   
1092 C  CA  . PHE   B 107 ? 0.8902 0.8565 0.4823 0.3646  -0.0501 0.0619  116 PHE   B CA  
1093 C  C   . PHE   B 107 ? 0.9212 0.8579 0.4802 0.3680  -0.0656 0.0547  116 PHE   B C   
1094 O  O   . PHE   B 107 ? 0.9396 0.8362 0.4872 0.3542  -0.0743 0.0486  116 PHE   B O   
1095 C  CB  . PHE   B 107 ? 0.8605 0.8301 0.4893 0.3291  -0.0397 0.0602  116 PHE   B CB  
1096 C  CG  . PHE   B 107 ? 0.8251 0.8316 0.4936 0.3193  -0.0215 0.0679  116 PHE   B CG  
1097 C  CD1 . PHE   B 107 ? 0.8127 0.8459 0.4846 0.3407  -0.0132 0.0778  116 PHE   B CD1 
1098 C  CD2 . PHE   B 107 ? 0.8081 0.8207 0.5088 0.2896  -0.0123 0.0660  116 PHE   B CD2 
1099 C  CE1 . PHE   B 107 ? 0.7922 0.8556 0.5005 0.3304  0.0047  0.0866  116 PHE   B CE1 
1100 C  CE2 . PHE   B 107 ? 0.7851 0.8262 0.5207 0.2802  0.0037  0.0731  116 PHE   B CE2 
1101 C  CZ  . PHE   B 107 ? 0.7747 0.8403 0.5147 0.2995  0.0125  0.0839  116 PHE   B CZ  
1102 N  N   . LYS   B 108 ? 0.9246 0.8803 0.4681 0.3866  -0.0687 0.0559  117 LYS   B N   
1103 C  CA  . LYS   B 108 ? 0.9603 0.8874 0.4699 0.3918  -0.0825 0.0498  117 LYS   B CA  
1104 C  C   . LYS   B 108 ? 0.9465 0.8957 0.4786 0.3699  -0.0756 0.0479  117 LYS   B C   
1105 O  O   . LYS   B 108 ? 0.9260 0.9231 0.4830 0.3716  -0.0664 0.0511  117 LYS   B O   
1106 C  CB  . LYS   B 108 ? 1.0130 0.9468 0.4871 0.4293  -0.0916 0.0511  117 LYS   B CB  
1107 C  CG  . LYS   B 108 ? 1.1201 1.0352 0.5684 0.4567  -0.0992 0.0524  117 LYS   B CG  
1108 C  CD  . LYS   B 108 ? 1.2269 1.1467 0.6359 0.4962  -0.1090 0.0529  117 LYS   B CD  
1109 C  CE  . LYS   B 108 ? 1.3373 1.2291 0.7124 0.5258  -0.1203 0.0518  117 LYS   B CE  
1110 N  NZ  . LYS   B 108 ? 1.4032 1.3010 0.7379 0.5678  -0.1296 0.0524  117 LYS   B NZ  
1111 N  N   . THR   B 109 ? 0.9557 0.8719 0.4803 0.3499  -0.0800 0.0429  118 THR   B N   
1112 C  CA  . THR   B 109 ? 0.9572 0.8905 0.4986 0.3311  -0.0746 0.0400  118 THR   B CA  
1113 C  C   . THR   B 109 ? 1.0014 0.9029 0.5028 0.3389  -0.0863 0.0362  118 THR   B C   
1114 O  O   . THR   B 109 ? 1.0329 0.8909 0.4971 0.3515  -0.0979 0.0359  118 THR   B O   
1115 C  CB  . THR   B 109 ? 0.9575 0.8866 0.5314 0.2982  -0.0648 0.0388  118 THR   B CB  
1116 O  OG1 . THR   B 109 ? 0.9939 0.8751 0.5470 0.2876  -0.0713 0.0367  118 THR   B OG1 
1117 C  CG2 . THR   B 109 ? 0.9367 0.8837 0.5424 0.2915  -0.0546 0.0428  118 THR   B CG2 
1118 N  N   . LYS   B 110 ? 1.0016 0.9215 0.5097 0.3311  -0.0836 0.0330  119 LYS   B N   
1119 C  CA  . LYS   B 110 ? 1.0401 0.9298 0.5092 0.3387  -0.0930 0.0303  119 LYS   B CA  
1120 C  C   . LYS   B 110 ? 1.0842 0.9185 0.5356 0.3218  -0.0953 0.0314  119 LYS   B C   
1121 O  O   . LYS   B 110 ? 1.1171 0.9134 0.5292 0.3303  -0.1038 0.0317  119 LYS   B O   
1122 C  CB  . LYS   B 110 ? 1.0376 0.9612 0.5208 0.3330  -0.0892 0.0257  119 LYS   B CB  
1123 C  CG  . LYS   B 110 ? 1.0729 1.0017 0.5885 0.3022  -0.0790 0.0236  119 LYS   B CG  
1124 C  CD  . LYS   B 110 ? 1.1207 1.0808 0.6469 0.2994  -0.0781 0.0170  119 LYS   B CD  
1125 C  CE  . LYS   B 110 ? 1.1707 1.1123 0.6998 0.2778  -0.0731 0.0145  119 LYS   B CE  
1126 N  NZ  . LYS   B 110 ? 1.1816 1.1334 0.7513 0.2529  -0.0623 0.0150  119 LYS   B NZ  
1127 N  N   . ASP   B 111 ? 1.0746 0.9047 0.5553 0.2987  -0.0876 0.0327  120 ASP   B N   
1128 C  CA  . ASP   B 111 ? 1.0997 0.8866 0.5742 0.2797  -0.0879 0.0343  120 ASP   B CA  
1129 C  C   . ASP   B 111 ? 1.1125 0.8724 0.5844 0.2811  -0.0941 0.0354  120 ASP   B C   
1130 O  O   . ASP   B 111 ? 1.1291 0.8647 0.6102 0.2612  -0.0924 0.0362  120 ASP   B O   
1131 C  CB  . ASP   B 111 ? 1.1032 0.9084 0.6145 0.2517  -0.0746 0.0336  120 ASP   B CB  
1132 C  CG  . ASP   B 111 ? 1.1679 0.9906 0.6787 0.2479  -0.0701 0.0311  120 ASP   B CG  
1133 O  OD1 . ASP   B 111 ? 1.2031 1.0030 0.6780 0.2590  -0.0765 0.0318  120 ASP   B OD1 
1134 O  OD2 . ASP   B 111 ? 1.1691 1.0257 0.7134 0.2347  -0.0609 0.0280  120 ASP   B OD2 
1135 N  N   . GLY   B 112 ? 1.1028 0.8694 0.5636 0.3048  -0.1012 0.0350  121 GLY   B N   
1136 C  CA  . GLY   B 112 ? 1.1097 0.8504 0.5646 0.3101  -0.1093 0.0343  121 GLY   B CA  
1137 C  C   . GLY   B 112 ? 1.0829 0.8581 0.5642 0.3169  -0.1031 0.0351  121 GLY   B C   
1138 O  O   . GLY   B 112 ? 1.0606 0.8803 0.5725 0.3111  -0.0900 0.0372  121 GLY   B O   
1139 N  N   . ASP   B 113 ? 1.0837 0.8366 0.5525 0.3295  -0.1128 0.0334  122 ASP   B N   
1140 C  CA  . ASP   B 113 ? 1.0627 0.8432 0.5494 0.3407  -0.1075 0.0351  122 ASP   B CA  
1141 C  C   . ASP   B 113 ? 1.0386 0.8213 0.5590 0.3178  -0.0999 0.0344  122 ASP   B C   
1142 O  O   . ASP   B 113 ? 1.0500 0.8026 0.5726 0.2987  -0.1046 0.0310  122 ASP   B O   
1143 C  CB  . ASP   B 113 ? 1.1084 0.8673 0.5593 0.3734  -0.1227 0.0330  122 ASP   B CB  
1144 C  CG  . ASP   B 113 ? 1.1995 0.9598 0.6150 0.4016  -0.1302 0.0338  122 ASP   B CG  
1145 O  OD1 . ASP   B 113 ? 1.2084 0.9938 0.6307 0.3970  -0.1225 0.0363  122 ASP   B OD1 
1146 O  OD2 . ASP   B 113 ? 1.2637 1.0005 0.6438 0.4301  -0.1446 0.0311  122 ASP   B OD2 
1147 N  N   . ILE   B 114 ? 0.9957 0.8155 0.5427 0.3202  -0.0873 0.0383  123 ILE   B N   
1148 C  CA  . ILE   B 114 ? 0.9749 0.8019 0.5531 0.3028  -0.0785 0.0382  123 ILE   B CA  
1149 C  C   . ILE   B 114 ? 0.9476 0.7877 0.5243 0.3262  -0.0773 0.0412  123 ILE   B C   
1150 O  O   . ILE   B 114 ? 0.9328 0.7994 0.5043 0.3465  -0.0722 0.0471  123 ILE   B O   
1151 C  CB  . ILE   B 114 ? 0.9632 0.8253 0.5787 0.2798  -0.0604 0.0416  123 ILE   B CB  
1152 C  CG1 . ILE   B 114 ? 0.9909 0.8501 0.6037 0.2647  -0.0602 0.0397  123 ILE   B CG1 
1153 C  CG2 . ILE   B 114 ? 0.9652 0.8287 0.6094 0.2607  -0.0524 0.0406  123 ILE   B CG2 
1154 C  CD1 . ILE   B 114 ? 0.9904 0.8832 0.6373 0.2444  -0.0450 0.0409  123 ILE   B CD1 
1155 N  N   . GLY   B 115 ? 0.9298 0.7556 0.5132 0.3238  -0.0802 0.0379  124 GLY   B N   
1156 C  CA  . GLY   B 115 ? 0.9232 0.7617 0.5046 0.3469  -0.0775 0.0413  124 GLY   B CA  
1157 C  C   . GLY   B 115 ? 0.8959 0.7777 0.5083 0.3415  -0.0555 0.0513  124 GLY   B C   
1158 O  O   . GLY   B 115 ? 0.8815 0.7782 0.5213 0.3155  -0.0446 0.0525  124 GLY   B O   
1159 N  N   . ALA   B 116 ? 0.8853 0.7868 0.4927 0.3665  -0.0490 0.0589  125 ALA   B N   
1160 C  CA  . ALA   B 116 ? 0.8698 0.8110 0.5077 0.3615  -0.0274 0.0703  125 ALA   B CA  
1161 C  C   . ALA   B 116 ? 0.8791 0.8264 0.5128 0.3842  -0.0209 0.0771  125 ALA   B C   
1162 O  O   . ALA   B 116 ? 0.8986 0.8325 0.5004 0.4141  -0.0320 0.0756  125 ALA   B O   
1163 C  CB  . ALA   B 116 ? 0.8575 0.8311 0.4987 0.3678  -0.0205 0.0773  125 ALA   B CB  
1164 N  N   . VAL   B 117 ? 0.8628 0.8277 0.5259 0.3718  -0.0035 0.0844  126 VAL   B N   
1165 C  CA  A VAL   B 117 ? 0.8722 0.8427 0.5304 0.3940  0.0051  0.0927  126 VAL   B CA  
1166 C  CA  B VAL   B 117 ? 0.8735 0.8435 0.5333 0.3921  0.0054  0.0924  126 VAL   B CA  
1167 C  C   . VAL   B 117 ? 0.8581 0.8683 0.5395 0.3959  0.0284  0.1099  126 VAL   B C   
1168 O  O   . VAL   B 117 ? 0.8330 0.8611 0.5486 0.3686  0.0413  0.1138  126 VAL   B O   
1169 C  CB  A VAL   B 117 ? 0.8858 0.8347 0.5494 0.3864  0.0030  0.0865  126 VAL   B CB  
1170 C  CB  B VAL   B 117 ? 0.8848 0.8363 0.5590 0.3745  0.0056  0.0860  126 VAL   B CB  
1171 C  CG1 A VAL   B 117 ? 0.9130 0.8256 0.5488 0.3958  -0.0215 0.0713  126 VAL   B CG1 
1172 C  CG1 B VAL   B 117 ? 0.8857 0.8461 0.5639 0.3896  0.0199  0.0963  126 VAL   B CG1 
1173 C  CG2 A VAL   B 117 ? 0.8771 0.8299 0.5756 0.3497  0.0124  0.0844  126 VAL   B CG2 
1174 C  CG2 B VAL   B 117 ? 0.9107 0.8258 0.5633 0.3766  -0.0175 0.0702  126 VAL   B CG2 
1175 N  N   . ALA   B 118 ? 0.8613 0.8860 0.5234 0.4296  0.0332  0.1205  127 ALA   B N   
1176 C  CA  . ALA   B 118 ? 0.8580 0.9231 0.5413 0.4345  0.0560  0.1392  127 ALA   B CA  
1177 C  C   . ALA   B 118 ? 0.8746 0.9422 0.5657 0.4420  0.0730  0.1514  127 ALA   B C   
1178 O  O   . ALA   B 118 ? 0.8922 0.9699 0.5645 0.4743  0.0806  0.1632  127 ALA   B O   
1179 C  CB  . ALA   B 118 ? 0.8673 0.9529 0.5267 0.4671  0.0539  0.1459  127 ALA   B CB  
1180 N  N   . LEU   B 119 ? 0.8661 0.9222 0.5817 0.4143  0.0787  0.1483  128 LEU   B N   
1181 C  CA  . LEU   B 119 ? 0.8733 0.9278 0.5960 0.4194  0.0950  0.1595  128 LEU   B CA  
1182 C  C   . LEU   B 119 ? 0.8756 0.9483 0.6426 0.3861  0.1141  0.1683  128 LEU   B C   
1183 O  O   . LEU   B 119 ? 0.8712 0.9397 0.6585 0.3555  0.1081  0.1574  128 LEU   B O   
1184 C  CB  . LEU   B 119 ? 0.8897 0.9075 0.5944 0.4227  0.0812  0.1456  128 LEU   B CB  
1185 C  CG  . LEU   B 119 ? 0.9148 0.9110 0.5767 0.4557  0.0602  0.1354  128 LEU   B CG  
1186 C  CD1 . LEU   B 119 ? 0.9299 0.8932 0.5831 0.4513  0.0441  0.1189  128 LEU   B CD1 
1187 C  CD2 . LEU   B 119 ? 0.9266 0.9345 0.5635 0.4966  0.0699  0.1502  128 LEU   B CD2 
1188 N  N   . ASP   B 120 ? 0.8803 0.9714 0.6609 0.3931  0.1369  0.1882  129 ASP   B N   
1189 C  CA  . ASP   B 120 ? 0.8736 0.9825 0.6965 0.3647  0.1568  0.1998  129 ASP   B CA  
1190 C  C   . ASP   B 120 ? 0.8650 0.9489 0.6966 0.3512  0.1640  0.1996  129 ASP   B C   
1191 O  O   . ASP   B 120 ? 0.8875 0.9623 0.7033 0.3730  0.1744  0.2106  129 ASP   B O   
1192 C  CB  . ASP   B 120 ? 0.9183 1.0611 0.7510 0.3816  0.1796  0.2248  129 ASP   B CB  
1193 C  CG  . ASP   B 120 ? 1.0057 1.1879 0.8778 0.3600  0.1889  0.2323  129 ASP   B CG  
1194 O  OD1 . ASP   B 120 ? 1.0221 1.2039 0.9130 0.3319  0.1771  0.2173  129 ASP   B OD1 
1195 O  OD2 . ASP   B 120 ? 1.0321 1.2471 0.9170 0.3720  0.2080  0.2534  129 ASP   B OD2 
1196 N  N   . TYR   B 121 ? 0.8377 0.9118 0.6937 0.3173  0.1602  0.1884  130 TYR   B N   
1197 C  CA  . TYR   B 121 ? 0.8255 0.8757 0.6897 0.3047  0.1671  0.1877  130 TYR   B CA  
1198 C  C   . TYR   B 121 ? 0.7925 0.8484 0.6963 0.2676  0.1746  0.1870  130 TYR   B C   
1199 O  O   . TYR   B 121 ? 0.7828 0.8552 0.7034 0.2497  0.1671  0.1794  130 TYR   B O   
1200 C  CB  . TYR   B 121 ? 0.8478 0.8675 0.6881 0.3085  0.1477  0.1680  130 TYR   B CB  
1201 C  CG  . TYR   B 121 ? 0.8792 0.8848 0.6837 0.3442  0.1435  0.1696  130 TYR   B CG  
1202 C  CD1 . TYR   B 121 ? 0.9029 0.8941 0.6998 0.3570  0.1552  0.1782  130 TYR   B CD1 
1203 C  CD2 . TYR   B 121 ? 0.9019 0.9071 0.6780 0.3671  0.1270  0.1623  130 TYR   B CD2 
1204 C  CE1 . TYR   B 121 ? 0.9376 0.9170 0.6999 0.3926  0.1504  0.1789  130 TYR   B CE1 
1205 C  CE2 . TYR   B 121 ? 0.9360 0.9283 0.6782 0.4021  0.1215  0.1627  130 TYR   B CE2 
1206 C  CZ  . TYR   B 121 ? 0.9656 0.9459 0.7011 0.4150  0.1328  0.1705  130 TYR   B CZ  
1207 O  OH  . TYR   B 121 ? 1.0221 0.9897 0.7222 0.4519  0.1259  0.1695  130 TYR   B OH  
1208 N  N   . PRO   B 122 ? 0.7757 0.8154 0.6926 0.2562  0.1873  0.1930  131 PRO   B N   
1209 C  CA  . PRO   B 122 ? 0.7524 0.7927 0.7046 0.2214  0.1912  0.1895  131 PRO   B CA  
1210 C  C   . PRO   B 122 ? 0.7310 0.7622 0.6840 0.2023  0.1714  0.1661  131 PRO   B C   
1211 O  O   . PRO   B 122 ? 0.7359 0.7514 0.6632 0.2133  0.1573  0.1535  131 PRO   B O   
1212 C  CB  . PRO   B 122 ? 0.7765 0.7909 0.7300 0.2197  0.2048  0.1975  131 PRO   B CB  
1213 C  CG  . PRO   B 122 ? 0.7956 0.8079 0.7226 0.2539  0.2154  0.2135  131 PRO   B CG  
1214 C  CD  . PRO   B 122 ? 0.7848 0.8028 0.6828 0.2760  0.1977  0.2024  131 PRO   B CD  
1215 N  N   . ALA   B 123 ? 0.6994 0.7409 0.6822 0.1741  0.1703  0.1605  132 ALA   B N   
1216 C  CA  . ALA   B 123 ? 0.6865 0.7221 0.6710 0.1562  0.1536  0.1401  132 ALA   B CA  
1217 C  C   . ALA   B 123 ? 0.6690 0.6732 0.6387 0.1534  0.1468  0.1273  132 ALA   B C   
1218 O  O   . ALA   B 123 ? 0.6663 0.6642 0.6240 0.1500  0.1321  0.1120  132 ALA   B O   
1219 C  CB  . ALA   B 123 ? 0.6780 0.7288 0.6973 0.1291  0.1551  0.1375  132 ALA   B CB  
1220 N  N   . GLY   B 124 ? 0.6481 0.6338 0.6172 0.1570  0.1581  0.1347  133 GLY   B N   
1221 C  CA  . GLY   B 124 ? 0.6385 0.5973 0.5934 0.1580  0.1532  0.1241  133 GLY   B CA  
1222 C  C   . GLY   B 124 ? 0.6220 0.5733 0.5471 0.1815  0.1438  0.1191  133 GLY   B C   
1223 O  O   . GLY   B 124 ? 0.6301 0.5634 0.5446 0.1841  0.1389  0.1100  133 GLY   B O   
1224 N  N   . THR   B 125 ? 0.5948 0.5600 0.5063 0.1995  0.1402  0.1244  134 THR   B N   
1225 C  CA  . THR   B 125 ? 0.6043 0.5617 0.4877 0.2212  0.1274  0.1175  134 THR   B CA  
1226 C  C   . THR   B 125 ? 0.5949 0.5538 0.4747 0.2099  0.1092  0.1010  134 THR   B C   
1227 O  O   . THR   B 125 ? 0.6009 0.5517 0.4609 0.2230  0.0963  0.0934  134 THR   B O   
1228 C  CB  . THR   B 125 ? 0.6309 0.6001 0.4979 0.2485  0.1313  0.1307  134 THR   B CB  
1229 O  OG1 . THR   B 125 ? 0.6572 0.6292 0.5311 0.2560  0.1512  0.1491  134 THR   B OG1 
1230 C  CG2 . THR   B 125 ? 0.6415 0.5986 0.4773 0.2750  0.1180  0.1239  134 THR   B CG2 
1231 N  N   . SER   B 126 ? 0.5751 0.5443 0.4732 0.1871  0.1080  0.0966  135 SER   B N   
1232 C  CA  . SER   B 126 ? 0.5715 0.5418 0.4653 0.1768  0.0935  0.0837  135 SER   B CA  
1233 C  C   . SER   B 126 ? 0.5739 0.5263 0.4590 0.1735  0.0844  0.0713  135 SER   B C   
1234 O  O   . SER   B 126 ? 0.5676 0.5112 0.4612 0.1660  0.0901  0.0689  135 SER   B O   
1235 C  CB  . SER   B 126 ? 0.5650 0.5464 0.4805 0.1536  0.0957  0.0803  135 SER   B CB  
1236 O  OG  . SER   B 126 ? 0.5736 0.5772 0.4993 0.1554  0.1008  0.0898  135 SER   B OG  
1237 N  N   . GLY   B 127 ? 0.5745 0.5218 0.4435 0.1790  0.0705  0.0639  136 GLY   B N   
1238 C  CA  . GLY   B 127 ? 0.5963 0.5301 0.4597 0.1760  0.0614  0.0531  136 GLY   B CA  
1239 C  C   . GLY   B 127 ? 0.6171 0.5411 0.4645 0.1974  0.0545  0.0523  136 GLY   B C   
1240 O  O   . GLY   B 127 ? 0.6273 0.5425 0.4719 0.1959  0.0450  0.0429  136 GLY   B O   
1241 N  N   . SER   B 128 ? 0.6101 0.5367 0.4475 0.2183  0.0594  0.0620  137 SER   B N   
1242 C  CA  . SER   B 128 ? 0.6195 0.5365 0.4378 0.2430  0.0516  0.0606  137 SER   B CA  
1243 C  C   . SER   B 128 ? 0.6352 0.5444 0.4382 0.2476  0.0326  0.0516  137 SER   B C   
1244 O  O   . SER   B 128 ? 0.6298 0.5433 0.4282 0.2443  0.0291  0.0533  137 SER   B O   
1245 C  CB  . SER   B 128 ? 0.6315 0.5545 0.4388 0.2664  0.0614  0.0745  137 SER   B CB  
1246 O  OG  . SER   B 128 ? 0.6451 0.5681 0.4625 0.2663  0.0776  0.0828  137 SER   B OG  
1247 N  N   . PRO   B 129 ? 0.6490 0.5463 0.4452 0.2542  0.0194  0.0414  138 PRO   B N   
1248 C  CA  . PRO   B 129 ? 0.6634 0.5493 0.4472 0.2556  0.0002  0.0323  138 PRO   B CA  
1249 C  C   . PRO   B 129 ? 0.7050 0.5839 0.4620 0.2835  -0.0099 0.0342  138 PRO   B C   
1250 O  O   . PRO   B 129 ? 0.7136 0.5932 0.4583 0.3080  -0.0067 0.0389  138 PRO   B O   
1251 C  CB  . PRO   B 129 ? 0.6759 0.5545 0.4675 0.2514  -0.0098 0.0206  138 PRO   B CB  
1252 C  CG  . PRO   B 129 ? 0.6754 0.5584 0.4688 0.2655  0.0001  0.0239  138 PRO   B CG  
1253 C  CD  . PRO   B 129 ? 0.6477 0.5413 0.4488 0.2595  0.0208  0.0370  138 PRO   B CD  
1254 N  N   . ILE   B 130 ? 0.7232 0.5925 0.4682 0.2815  -0.0231 0.0300  139 ILE   B N   
1255 C  CA  . ILE   B 130 ? 0.7518 0.6098 0.4678 0.3078  -0.0369 0.0289  139 ILE   B CA  
1256 C  C   . ILE   B 130 ? 0.7825 0.6183 0.4928 0.3063  -0.0594 0.0141  139 ILE   B C   
1257 O  O   . ILE   B 130 ? 0.7736 0.6035 0.4983 0.2810  -0.0639 0.0085  139 ILE   B O   
1258 C  CB  . ILE   B 130 ? 0.7630 0.6250 0.4698 0.3057  -0.0358 0.0347  139 ILE   B CB  
1259 C  CG1 . ILE   B 130 ? 0.7691 0.6571 0.4875 0.3056  -0.0140 0.0489  139 ILE   B CG1 
1260 C  CG2 . ILE   B 130 ? 0.7828 0.6286 0.4561 0.3330  -0.0531 0.0314  139 ILE   B CG2 
1261 C  CD1 . ILE   B 130 ? 0.7857 0.6849 0.5095 0.2915  -0.0096 0.0527  139 ILE   B CD1 
1262 N  N   . LEU   B 131 ? 0.8119 0.6360 0.5029 0.3332  -0.0732 0.0079  140 LEU   B N   
1263 C  CA  . LEU   B 131 ? 0.8501 0.6544 0.5389 0.3334  -0.0964 -0.0077 140 LEU   B CA  
1264 C  C   . LEU   B 131 ? 0.8880 0.6684 0.5458 0.3546  -0.1187 -0.0147 140 LEU   B C   
1265 O  O   . LEU   B 131 ? 0.9112 0.6923 0.5426 0.3834  -0.1174 -0.0087 140 LEU   B O   
1266 C  CB  . LEU   B 131 ? 0.8721 0.6806 0.5639 0.3496  -0.0985 -0.0133 140 LEU   B CB  
1267 C  CG  . LEU   B 131 ? 0.8923 0.7218 0.6009 0.3461  -0.0753 -0.0039 140 LEU   B CG  
1268 C  CD1 . LEU   B 131 ? 0.9173 0.7466 0.6211 0.3681  -0.0804 -0.0103 140 LEU   B CD1 
1269 C  CD2 . LEU   B 131 ? 0.8931 0.7327 0.6329 0.3104  -0.0646 -0.0033 140 LEU   B CD2 
1270 N  N   . ASP   B 132 ? 0.8981 0.6567 0.5585 0.3425  -0.1399 -0.0277 141 ASP   B N   
1271 C  CA  . ASP   B 132 ? 0.9454 0.6753 0.5753 0.3640  -0.1654 -0.0376 141 ASP   B CA  
1272 C  C   . ASP   B 132 ? 0.9935 0.7176 0.6171 0.3875  -0.1819 -0.0503 141 ASP   B C   
1273 O  O   . ASP   B 132 ? 0.9895 0.7329 0.6326 0.3854  -0.1717 -0.0500 141 ASP   B O   
1274 C  CB  . ASP   B 132 ? 0.9524 0.6569 0.5863 0.3395  -0.1810 -0.0444 141 ASP   B CB  
1275 C  CG  . ASP   B 132 ? 0.9516 0.6553 0.6201 0.3090  -0.1869 -0.0530 141 ASP   B CG  
1276 O  OD1 . ASP   B 132 ? 0.9320 0.6503 0.6180 0.3116  -0.1867 -0.0587 141 ASP   B OD1 
1277 O  OD2 . ASP   B 132 ? 0.9744 0.6635 0.6519 0.2837  -0.1914 -0.0535 141 ASP   B OD2 
1278 N  N   . LYS   B 133 ? 1.0367 0.7332 0.6317 0.4110  -0.2085 -0.0625 142 LYS   B N   
1279 C  CA  . LYS   B 133 ? 1.0782 0.7668 0.6624 0.4373  -0.2279 -0.0768 142 LYS   B CA  
1280 C  C   . LYS   B 133 ? 1.0799 0.7720 0.6998 0.4138  -0.2383 -0.0899 142 LYS   B C   
1281 O  O   . LYS   B 133 ? 1.0838 0.7812 0.7031 0.4331  -0.2474 -0.0997 142 LYS   B O   
1282 C  CB  . LYS   B 133 ? 1.1549 0.8100 0.6987 0.4674  -0.2564 -0.0884 142 LYS   B CB  
1283 C  CG  . LYS   B 133 ? 1.2543 0.9098 0.7608 0.4959  -0.2463 -0.0754 142 LYS   B CG  
1284 C  CD  . LYS   B 133 ? 1.3610 0.9793 0.8259 0.5225  -0.2752 -0.0870 142 LYS   B CD  
1285 C  CE  . LYS   B 133 ? 1.4314 1.0545 0.8617 0.5492  -0.2635 -0.0732 142 LYS   B CE  
1286 N  NZ  . LYS   B 133 ? 1.4974 1.0820 0.8857 0.5735  -0.2914 -0.0844 142 LYS   B NZ  
1287 N  N   . CYS   B 134 ? 1.0705 0.7625 0.7216 0.3737  -0.2358 -0.0896 143 CYS   B N   
1288 C  CA  . CYS   B 134 ? 1.0569 0.7593 0.7471 0.3490  -0.2417 -0.0997 143 CYS   B CA  
1289 C  C   . CYS   B 134 ? 1.0158 0.7532 0.7335 0.3357  -0.2143 -0.0898 143 CYS   B C   
1290 O  O   . CYS   B 134 ? 1.0049 0.7561 0.7558 0.3158  -0.2159 -0.0965 143 CYS   B O   
1291 C  CB  . CYS   B 134 ? 1.0889 0.7740 0.7997 0.3138  -0.2525 -0.1037 143 CYS   B CB  
1292 S  SG  . CYS   B 134 ? 1.2213 0.8595 0.9061 0.3260  -0.2911 -0.1203 143 CYS   B SG  
1293 N  N   . GLY   B 135 ? 0.9921 0.7438 0.6970 0.3466  -0.1901 -0.0743 144 GLY   B N   
1294 C  CA  . GLY   B 135 ? 0.9571 0.7368 0.6845 0.3348  -0.1644 -0.0645 144 GLY   B CA  
1295 C  C   . GLY   B 135 ? 0.9224 0.7119 0.6761 0.2971  -0.1484 -0.0563 144 GLY   B C   
1296 O  O   . GLY   B 135 ? 0.9096 0.7203 0.6842 0.2843  -0.1296 -0.0505 144 GLY   B O   
1297 N  N   . ARG   B 136 ? 0.8989 0.6712 0.6492 0.2808  -0.1560 -0.0558 145 ARG   B N   
1298 C  CA  . ARG   B 136 ? 0.8677 0.6472 0.6389 0.2475  -0.1416 -0.0479 145 ARG   B CA  
1299 C  C   . ARG   B 136 ? 0.8256 0.6150 0.5854 0.2493  -0.1199 -0.0331 145 ARG   B C   
1300 O  O   . ARG   B 136 ? 0.8324 0.6142 0.5646 0.2719  -0.1214 -0.0288 145 ARG   B O   
1301 C  CB  . ARG   B 136 ? 0.9104 0.6650 0.6809 0.2302  -0.1582 -0.0526 145 ARG   B CB  
1302 C  CG  . ARG   B 136 ? 0.9586 0.7072 0.7511 0.2196  -0.1782 -0.0667 145 ARG   B CG  
1303 C  CD  . ARG   B 136 ? 1.0319 0.7513 0.8225 0.2024  -0.1943 -0.0697 145 ARG   B CD  
1304 N  NE  . ARG   B 136 ? 1.1276 0.8158 0.8798 0.2274  -0.2128 -0.0740 145 ARG   B NE  
1305 C  CZ  . ARG   B 136 ? 1.1912 0.8474 0.9267 0.2206  -0.2245 -0.0736 145 ARG   B CZ  
1306 N  NH1 . ARG   B 136 ? 1.1856 0.8364 0.9395 0.1884  -0.2181 -0.0674 145 ARG   B NH1 
1307 N  NH2 . ARG   B 136 ? 1.2231 0.8516 0.9208 0.2476  -0.2417 -0.0784 145 ARG   B NH2 
1308 N  N   . VAL   B 137 ? 0.7740 0.5819 0.5556 0.2268  -0.1001 -0.0257 146 VAL   B N   
1309 C  CA  . VAL   B 137 ? 0.7499 0.5691 0.5258 0.2257  -0.0807 -0.0133 146 VAL   B CA  
1310 C  C   . VAL   B 137 ? 0.7580 0.5642 0.5211 0.2163  -0.0834 -0.0092 146 VAL   B C   
1311 O  O   . VAL   B 137 ? 0.7594 0.5610 0.5344 0.1929  -0.0837 -0.0099 146 VAL   B O   
1312 C  CB  . VAL   B 137 ? 0.7285 0.5699 0.5296 0.2084  -0.0606 -0.0087 146 VAL   B CB  
1313 C  CG1 . VAL   B 137 ? 0.7256 0.5774 0.5230 0.2056  -0.0432 0.0025  146 VAL   B CG1 
1314 C  CG2 . VAL   B 137 ? 0.7197 0.5715 0.5282 0.2222  -0.0577 -0.0121 146 VAL   B CG2 
1315 N  N   . ILE   B 138 ? 0.7591 0.5587 0.4960 0.2369  -0.0861 -0.0048 147 ILE   B N   
1316 C  CA  . ILE   B 138 ? 0.7576 0.5446 0.4779 0.2327  -0.0895 -0.0012 147 ILE   B CA  
1317 C  C   . ILE   B 138 ? 0.7264 0.5337 0.4525 0.2238  -0.0702 0.0091  147 ILE   B C   
1318 O  O   . ILE   B 138 ? 0.7260 0.5262 0.4394 0.2200  -0.0716 0.0121  147 ILE   B O   
1319 C  CB  . ILE   B 138 ? 0.7894 0.5567 0.4756 0.2614  -0.1060 -0.0037 147 ILE   B CB  
1320 C  CG1 . ILE   B 138 ? 0.8041 0.5888 0.4798 0.2890  -0.0975 0.0022  147 ILE   B CG1 
1321 C  CG2 . ILE   B 138 ? 0.8064 0.5469 0.4864 0.2655  -0.1298 -0.0163 147 ILE   B CG2 
1322 C  CD1 . ILE   B 138 ? 0.8547 0.6271 0.4946 0.3192  -0.1084 0.0032  147 ILE   B CD1 
1323 N  N   . GLY   B 139 ? 0.7027 0.5333 0.4478 0.2198  -0.0533 0.0136  148 GLY   B N   
1324 C  CA  . GLY   B 139 ? 0.6785 0.5282 0.4333 0.2091  -0.0366 0.0214  148 GLY   B CA  
1325 C  C   . GLY   B 139 ? 0.6610 0.5315 0.4299 0.2141  -0.0208 0.0272  148 GLY   B C   
1326 O  O   . GLY   B 139 ? 0.6593 0.5289 0.4265 0.2290  -0.0220 0.0263  148 GLY   B O   
1327 N  N   . LEU   B 140 ? 0.6426 0.5302 0.4247 0.2023  -0.0066 0.0329  149 LEU   B N   
1328 C  CA  . LEU   B 140 ? 0.6309 0.5352 0.4280 0.2044  0.0089  0.0394  149 LEU   B CA  
1329 C  C   . LEU   B 140 ? 0.6418 0.5619 0.4351 0.2150  0.0164  0.0490  149 LEU   B C   
1330 O  O   . LEU   B 140 ? 0.6400 0.5642 0.4269 0.2123  0.0130  0.0496  149 LEU   B O   
1331 C  CB  . LEU   B 140 ? 0.6074 0.5192 0.4273 0.1810  0.0194  0.0374  149 LEU   B CB  
1332 C  CG  . LEU   B 140 ? 0.6189 0.5218 0.4469 0.1681  0.0151  0.0290  149 LEU   B CG  
1333 C  CD1 . LEU   B 140 ? 0.6061 0.5181 0.4535 0.1492  0.0269  0.0278  149 LEU   B CD1 
1334 C  CD2 . LEU   B 140 ? 0.6324 0.5286 0.4581 0.1823  0.0098  0.0256  149 LEU   B CD2 
1335 N  N   . TYR   B 141 ? 0.6455 0.5758 0.4440 0.2270  0.0276  0.0572  150 TYR   B N   
1336 C  CA  . TYR   B 141 ? 0.6580 0.6076 0.4578 0.2376  0.0376  0.0688  150 TYR   B CA  
1337 C  C   . TYR   B 141 ? 0.6501 0.6163 0.4778 0.2172  0.0524  0.0733  150 TYR   B C   
1338 O  O   . TYR   B 141 ? 0.6560 0.6168 0.4975 0.2061  0.0591  0.0716  150 TYR   B O   
1339 C  CB  . TYR   B 141 ? 0.6746 0.6233 0.4633 0.2633  0.0424  0.0765  150 TYR   B CB  
1340 C  CG  . TYR   B 141 ? 0.6791 0.6500 0.4749 0.2738  0.0585  0.0920  150 TYR   B CG  
1341 C  CD1 . TYR   B 141 ? 0.6815 0.6605 0.4990 0.2647  0.0759  0.1007  150 TYR   B CD1 
1342 C  CD2 . TYR   B 141 ? 0.6988 0.6823 0.4794 0.2936  0.0566  0.0985  150 TYR   B CD2 
1343 C  CE1 . TYR   B 141 ? 0.6934 0.6931 0.5205 0.2726  0.0921  0.1168  150 TYR   B CE1 
1344 C  CE2 . TYR   B 141 ? 0.6995 0.7071 0.4886 0.3043  0.0730  0.1145  150 TYR   B CE2 
1345 C  CZ  . TYR   B 141 ? 0.7128 0.7290 0.5270 0.2922  0.0913  0.1242  150 TYR   B CZ  
1346 O  OH  . TYR   B 141 ? 0.7440 0.7845 0.5702 0.3005  0.1090  0.1419  150 TYR   B OH  
1347 N  N   . GLY   B 142 ? 0.6375 0.6238 0.4735 0.2139  0.0570  0.0787  151 GLY   B N   
1348 C  CA  . GLY   B 142 ? 0.6350 0.6370 0.4998 0.1943  0.0693  0.0821  151 GLY   B CA  
1349 C  C   . GLY   B 142 ? 0.6417 0.6612 0.5170 0.1817  0.0668  0.0793  151 GLY   B C   
1350 O  O   . GLY   B 142 ? 0.6452 0.6795 0.5462 0.1664  0.0756  0.0815  151 GLY   B O   
1351 N  N   . ASN   B 143 ? 0.6357 0.6519 0.4912 0.1877  0.0539  0.0734  152 ASN   B N   
1352 C  CA  . ASN   B 143 ? 0.6380 0.6712 0.5000 0.1790  0.0505  0.0701  152 ASN   B CA  
1353 C  C   . ASN   B 143 ? 0.6608 0.7047 0.5035 0.2005  0.0444  0.0744  152 ASN   B C   
1354 O  O   . ASN   B 143 ? 0.6644 0.6886 0.4783 0.2136  0.0328  0.0706  152 ASN   B O   
1355 C  CB  . ASN   B 143 ? 0.6499 0.6668 0.5049 0.1637  0.0412  0.0579  152 ASN   B CB  
1356 C  CG  . ASN   B 143 ? 0.6783 0.7118 0.5400 0.1546  0.0378  0.0530  152 ASN   B CG  
1357 O  OD1 . ASN   B 143 ? 0.6656 0.7262 0.5469 0.1531  0.0430  0.0570  152 ASN   B OD1 
1358 N  ND2 . ASN   B 143 ? 0.6835 0.7023 0.5290 0.1492  0.0286  0.0446  152 ASN   B ND2 
1359 N  N   . GLY   B 144 ? 0.6744 0.7495 0.5336 0.2042  0.0519  0.0822  153 GLY   B N   
1360 C  CA  . GLY   B 144 ? 0.7061 0.7970 0.5482 0.2271  0.0476  0.0873  153 GLY   B CA  
1361 C  C   . GLY   B 144 ? 0.7175 0.8496 0.5858 0.2248  0.0554  0.0937  153 GLY   B C   
1362 O  O   . GLY   B 144 ? 0.7008 0.8459 0.5947 0.2035  0.0568  0.0885  153 GLY   B O   
1363 N  N   . VAL   B 145 ? 0.7373 0.8919 0.6003 0.2479  0.0604  0.1050  154 VAL   B N   
1364 C  CA  . VAL   B 145 ? 0.7472 0.9463 0.6360 0.2480  0.0673  0.1118  154 VAL   B CA  
1365 C  C   . VAL   B 145 ? 0.7684 0.9947 0.6732 0.2612  0.0849  0.1304  154 VAL   B C   
1366 O  O   . VAL   B 145 ? 0.7729 0.9819 0.6589 0.2778  0.0896  0.1377  154 VAL   B O   
1367 C  CB  . VAL   B 145 ? 0.7675 0.9732 0.6291 0.2658  0.0527  0.1053  154 VAL   B CB  
1368 C  CG1 . VAL   B 145 ? 0.7771 0.9828 0.6065 0.3007  0.0512  0.1134  154 VAL   B CG1 
1369 C  CG2 . VAL   B 145 ? 0.7607 1.0082 0.6504 0.2570  0.0531  0.1036  154 VAL   B CG2 
1370 N  N   . VAL   B 146 ? 0.7764 1.0464 0.7174 0.2535  0.0947  0.1382  155 VAL   B N   
1371 C  CA  . VAL   B 146 ? 0.8009 1.1027 0.7619 0.2644  0.1138  0.1582  155 VAL   B CA  
1372 C  C   . VAL   B 146 ? 0.8294 1.1654 0.7773 0.2916  0.1108  0.1630  155 VAL   B C   
1373 O  O   . VAL   B 146 ? 0.8210 1.1795 0.7785 0.2860  0.1015  0.1544  155 VAL   B O   
1374 C  CB  . VAL   B 146 ? 0.7914 1.1198 0.8071 0.2348  0.1282  0.1651  155 VAL   B CB  
1375 C  CG1 . VAL   B 146 ? 0.7911 1.1456 0.8260 0.2450  0.1508  0.1888  155 VAL   B CG1 
1376 C  CG2 . VAL   B 146 ? 0.8081 1.1001 0.8334 0.2072  0.1266  0.1556  155 VAL   B CG2 
1377 N  N   . ILE   B 147 ? 0.8669 1.2054 0.7888 0.3238  0.1169  0.1754  156 ILE   B N   
1378 C  CA  . ILE   B 147 ? 0.9002 1.2695 0.8039 0.3543  0.1134  0.1797  156 ILE   B CA  
1379 C  C   . ILE   B 147 ? 0.9029 1.3308 0.8441 0.3600  0.1350  0.2007  156 ILE   B C   
1380 O  O   . ILE   B 147 ? 0.8959 1.3347 0.8755 0.3392  0.1526  0.2124  156 ILE   B O   
1381 C  CB  . ILE   B 147 ? 0.9456 1.2798 0.7912 0.3899  0.1021  0.1769  156 ILE   B CB  
1382 C  CG1 . ILE   B 147 ? 0.9739 1.2953 0.8104 0.4046  0.1162  0.1909  156 ILE   B CG1 
1383 C  CG2 . ILE   B 147 ? 0.9788 1.2618 0.7938 0.3811  0.0802  0.1563  156 ILE   B CG2 
1384 C  CD1 . ILE   B 147 ? 1.0220 1.3176 0.8031 0.4449  0.1053  0.1892  156 ILE   B CD1 
1385 N  N   . LYS   B 148 ? 0.9107 1.3768 0.8425 0.3870  0.1339  0.2057  157 LYS   B N   
1386 C  CA  . LYS   B 148 ? 0.9032 1.4320 0.8718 0.3944  0.1543  0.2262  157 LYS   B CA  
1387 C  C   . LYS   B 148 ? 0.9161 1.4512 0.9038 0.3943  0.1801  0.2493  157 LYS   B C   
1388 O  O   . LYS   B 148 ? 0.8933 1.4675 0.9342 0.3730  0.1986  0.2634  157 LYS   B O   
1389 C  CB  . LYS   B 148 ? 0.9319 1.4900 0.8693 0.4361  0.1494  0.2296  157 LYS   B CB  
1390 C  CG  . LYS   B 148 ? 1.0128 1.5586 0.9214 0.4426  0.1237  0.2080  157 LYS   B CG  
1391 C  CD  . LYS   B 148 ? 1.0825 1.6710 0.9731 0.4801  0.1210  0.2125  157 LYS   B CD  
1392 C  CE  . LYS   B 148 ? 1.0972 1.7595 1.0457 0.4678  0.1334  0.2215  157 LYS   B CE  
1393 N  NZ  . LYS   B 148 ? 1.1245 1.8295 1.0542 0.5050  0.1286  0.2234  157 LYS   B NZ  
1394 N  N   . ASN   B 149 ? 0.9470 1.4426 0.8919 0.4178  0.1810  0.2530  158 ASN   B N   
1395 C  CA  . ASN   B 149 ? 0.9533 1.4502 0.9066 0.4242  0.2050  0.2751  158 ASN   B CA  
1396 C  C   . ASN   B 149 ? 0.9470 1.4153 0.9297 0.3870  0.2133  0.2754  158 ASN   B C   
1397 O  O   . ASN   B 149 ? 0.9571 1.4150 0.9390 0.3932  0.2314  0.2920  158 ASN   B O   
1398 C  CB  . ASN   B 149 ? 1.0114 1.4796 0.9051 0.4685  0.2022  0.2788  158 ASN   B CB  
1399 C  CG  . ASN   B 149 ? 1.1000 1.5240 0.9393 0.4864  0.1728  0.2554  158 ASN   B CG  
1400 O  OD1 . ASN   B 149 ? 1.1143 1.5484 0.9424 0.4925  0.1568  0.2433  158 ASN   B OD1 
1401 N  ND2 . ASN   B 149 ? 1.1471 1.5207 0.9511 0.4964  0.1652  0.2490  158 ASN   B ND2 
1402 N  N   . GLY   B 150 ? 0.9242 1.3794 0.9294 0.3516  0.2002  0.2574  159 GLY   B N   
1403 C  CA  . GLY   B 150 ? 0.9062 1.3342 0.9385 0.3163  0.2054  0.2548  159 GLY   B CA  
1404 C  C   . GLY   B 150 ? 0.9142 1.2819 0.9084 0.3185  0.1943  0.2424  159 GLY   B C   
1405 O  O   . GLY   B 150 ? 0.9162 1.2578 0.9274 0.2897  0.1934  0.2349  159 GLY   B O   
1406 N  N   . SER   B 151 ? 0.9114 1.2573 0.8543 0.3534  0.1849  0.2394  160 SER   B N   
1407 C  CA  A SER   B 151 ? 0.9293 1.2215 0.8352 0.3592  0.1725  0.2269  160 SER   B CA  
1408 C  CA  B SER   B 151 ? 0.9270 1.2191 0.8342 0.3581  0.1729  0.2270  160 SER   B CA  
1409 C  C   . SER   B 151 ? 0.9200 1.1838 0.8223 0.3351  0.1505  0.2023  160 SER   B C   
1410 O  O   . SER   B 151 ? 0.9086 1.1919 0.8242 0.3233  0.1416  0.1937  160 SER   B O   
1411 C  CB  A SER   B 151 ? 0.9680 1.2481 0.8223 0.4027  0.1646  0.2278  160 SER   B CB  
1412 C  CB  B SER   B 151 ? 0.9609 1.2393 0.8169 0.4016  0.1666  0.2291  160 SER   B CB  
1413 O  OG  A SER   B 151 ? 1.0265 1.2570 0.8467 0.4084  0.1494  0.2136  160 SER   B OG  
1414 O  OG  B SER   B 151 ? 0.9823 1.2802 0.8191 0.4220  0.1546  0.2241  160 SER   B OG  
1415 N  N   . TYR   B 152 ? 0.9020 1.1214 0.7860 0.3293  0.1422  0.1915  161 TYR   B N   
1416 C  CA  . TYR   B 152 ? 0.8784 1.0702 0.7573 0.3082  0.1235  0.1703  161 TYR   B CA  
1417 C  C   . TYR   B 152 ? 0.8528 1.0134 0.6849 0.3303  0.1033  0.1577  161 TYR   B C   
1418 O  O   . TYR   B 152 ? 0.8682 1.0113 0.6732 0.3545  0.1027  0.1612  161 TYR   B O   
1419 C  CB  . TYR   B 152 ? 0.8863 1.0527 0.7826 0.2827  0.1284  0.1665  161 TYR   B CB  
1420 C  CG  . TYR   B 152 ? 0.9036 1.0541 0.8088 0.2546  0.1151  0.1481  161 TYR   B CG  
1421 C  CD1 . TYR   B 152 ? 0.8956 1.0693 0.8335 0.2307  0.1164  0.1450  161 TYR   B CD1 
1422 C  CD2 . TYR   B 152 ? 0.9370 1.0504 0.8202 0.2518  0.1023  0.1344  161 TYR   B CD2 
1423 C  CE1 . TYR   B 152 ? 0.9127 1.0714 0.8558 0.2078  0.1049  0.1286  161 TYR   B CE1 
1424 C  CE2 . TYR   B 152 ? 0.9502 1.0506 0.8410 0.2275  0.0925  0.1195  161 TYR   B CE2 
1425 C  CZ  . TYR   B 152 ? 0.9455 1.0676 0.8640 0.2068  0.0939  0.1167  161 TYR   B CZ  
1426 O  OH  . TYR   B 152 ? 0.9644 1.0737 0.8874 0.1856  0.0845  0.1021  161 TYR   B OH  
1427 N  N   . VAL   B 153 ? 0.8097 0.9619 0.6319 0.3222  0.0861  0.1428  162 VAL   B N   
1428 C  CA  . VAL   B 153 ? 0.7900 0.9079 0.5712 0.3376  0.0660  0.1301  162 VAL   B CA  
1429 C  C   . VAL   B 153 ? 0.7415 0.8328 0.5277 0.3093  0.0550  0.1145  162 VAL   B C   
1430 O  O   . VAL   B 153 ? 0.7197 0.8216 0.5185 0.2924  0.0514  0.1085  162 VAL   B O   
1431 C  CB  . VAL   B 153 ? 0.8026 0.9311 0.5565 0.3630  0.0551  0.1290  162 VAL   B CB  
1432 C  CG1 . VAL   B 153 ? 0.8318 0.9181 0.5457 0.3729  0.0327  0.1144  162 VAL   B CG1 
1433 C  CG2 . VAL   B 153 ? 0.8075 0.9604 0.5514 0.3957  0.0661  0.1447  162 VAL   B CG2 
1434 N  N   . SER   B 154 ? 0.7181 0.7776 0.4950 0.3054  0.0505  0.1083  163 SER   B N   
1435 C  CA  . SER   B 154 ? 0.6981 0.7346 0.4808 0.2798  0.0424  0.0953  163 SER   B CA  
1436 C  C   . SER   B 154 ? 0.7046 0.7121 0.4556 0.2866  0.0225  0.0837  163 SER   B C   
1437 O  O   . SER   B 154 ? 0.7249 0.7164 0.4483 0.3101  0.0134  0.0831  163 SER   B O   
1438 C  CB  . SER   B 154 ? 0.6954 0.7157 0.4879 0.2716  0.0488  0.0951  163 SER   B CB  
1439 O  OG  . SER   B 154 ? 0.7056 0.7026 0.4989 0.2521  0.0400  0.0827  163 SER   B OG  
1440 N  N   . ALA   B 155 ? 0.6920 0.6890 0.4464 0.2657  0.0156  0.0744  164 ALA   B N   
1441 C  CA  . ALA   B 155 ? 0.7008 0.6662 0.4287 0.2670  -0.0016 0.0645  164 ALA   B CA  
1442 C  C   . ALA   B 155 ? 0.7122 0.6519 0.4387 0.2627  -0.0056 0.0594  164 ALA   B C   
1443 O  O   . ALA   B 155 ? 0.7090 0.6558 0.4570 0.2534  0.0054  0.0618  164 ALA   B O   
1444 C  CB  . ALA   B 155 ? 0.6991 0.6627 0.4343 0.2442  -0.0039 0.0581  164 ALA   B CB  
1445 N  N   . ILE   B 156 ? 0.7201 0.6300 0.4221 0.2696  -0.0219 0.0520  165 ILE   B N   
1446 C  CA  . ILE   B 156 ? 0.7269 0.6146 0.4316 0.2620  -0.0280 0.0452  165 ILE   B CA  
1447 C  C   . ILE   B 156 ? 0.7133 0.5939 0.4302 0.2336  -0.0280 0.0401  165 ILE   B C   
1448 O  O   . ILE   B 156 ? 0.7167 0.5787 0.4160 0.2313  -0.0389 0.0363  165 ILE   B O   
1449 C  CB  . ILE   B 156 ? 0.7602 0.6187 0.4354 0.2813  -0.0473 0.0389  165 ILE   B CB  
1450 C  CG1 . ILE   B 156 ? 0.7916 0.6580 0.4477 0.3147  -0.0478 0.0443  165 ILE   B CG1 
1451 C  CG2 . ILE   B 156 ? 0.7621 0.6023 0.4467 0.2702  -0.0541 0.0307  165 ILE   B CG2 
1452 C  CD1 . ILE   B 156 ? 0.8314 0.6685 0.4554 0.3382  -0.0684 0.0368  165 ILE   B CD1 
1453 N  N   . THR   B 157 ? 0.6867 0.5827 0.4311 0.2139  -0.0146 0.0410  166 THR   B N   
1454 C  CA  . THR   B 157 ? 0.6824 0.5748 0.4364 0.1901  -0.0131 0.0369  166 THR   B CA  
1455 C  C   . THR   B 157 ? 0.6783 0.5515 0.4366 0.1777  -0.0185 0.0308  166 THR   B C   
1456 O  O   . THR   B 157 ? 0.6606 0.5383 0.4349 0.1742  -0.0132 0.0295  166 THR   B O   
1457 C  CB  . THR   B 157 ? 0.6847 0.6007 0.4639 0.1757  0.0018  0.0391  166 THR   B CB  
1458 O  OG1 . THR   B 157 ? 0.6919 0.6292 0.4723 0.1845  0.0064  0.0447  166 THR   B OG1 
1459 C  CG2 . THR   B 157 ? 0.6853 0.5978 0.4708 0.1547  0.0032  0.0344  166 THR   B CG2 
1460 N  N   . GLN   B 158 ? 0.6846 0.5374 0.4298 0.1705  -0.0281 0.0276  167 GLN   B N   
1461 C  CA  . GLN   B 158 ? 0.6962 0.5334 0.4494 0.1567  -0.0328 0.0229  167 GLN   B CA  
1462 C  C   . GLN   B 158 ? 0.7108 0.5460 0.4693 0.1354  -0.0274 0.0234  167 GLN   B C   
1463 O  O   . GLN   B 158 ? 0.6991 0.5315 0.4429 0.1357  -0.0276 0.0259  167 GLN   B O   
1464 C  CB  . GLN   B 158 ? 0.7157 0.5254 0.4486 0.1680  -0.0509 0.0194  167 GLN   B CB  
1465 C  CG  . GLN   B 158 ? 0.7314 0.5250 0.4752 0.1541  -0.0588 0.0140  167 GLN   B CG  
1466 C  CD  . GLN   B 158 ? 0.7198 0.5293 0.4884 0.1509  -0.0535 0.0105  167 GLN   B CD  
1467 O  OE1 . GLN   B 158 ? 0.7160 0.5454 0.5040 0.1394  -0.0389 0.0123  167 GLN   B OE1 
1468 N  NE2 . GLN   B 158 ? 0.6754 0.4751 0.4426 0.1618  -0.0661 0.0043  167 GLN   B NE2 
1469 N  N   . GLY   B 159 ? 0.7254 0.5636 0.5036 0.1193  -0.0222 0.0212  168 GLY   B N   
1470 C  CA  . GLY   B 159 ? 0.7697 0.6066 0.5520 0.1012  -0.0160 0.0227  168 GLY   B CA  
1471 C  C   . GLY   B 159 ? 0.8448 0.6564 0.6178 0.0937  -0.0256 0.0235  168 GLY   B C   
1472 O  O   . GLY   B 159 ? 0.8570 0.6489 0.6159 0.1037  -0.0394 0.0220  168 GLY   B O   
1473 N  N   . LYS   B 160 ? 0.8904 0.7013 0.6706 0.0766  -0.0184 0.0263  169 LYS   B N   
1474 C  CA  . LYS   B 160 ? 0.9427 0.7300 0.7182 0.0657  -0.0250 0.0293  169 LYS   B CA  
1475 C  C   . LYS   B 160 ? 0.9623 0.7618 0.7674 0.0491  -0.0187 0.0287  169 LYS   B C   
1476 O  O   . LYS   B 160 ? 0.9520 0.7742 0.7713 0.0431  -0.0051 0.0292  169 LYS   B O   
1477 C  CB  . LYS   B 160 ? 0.9946 0.7697 0.7491 0.0613  -0.0201 0.0362  169 LYS   B CB  
1478 C  CG  . LYS   B 160 ? 1.0843 0.8289 0.8293 0.0510  -0.0266 0.0415  169 LYS   B CG  
1479 C  CD  . LYS   B 160 ? 1.1671 0.8984 0.8869 0.0497  -0.0205 0.0493  169 LYS   B CD  
1480 C  CE  . LYS   B 160 ? 1.2410 0.9347 0.9452 0.0423  -0.0282 0.0559  169 LYS   B CE  
1481 N  NZ  . LYS   B 160 ? 1.2923 0.9702 0.9663 0.0451  -0.0225 0.0639  169 LYS   B NZ  
1482 N  N   . ARG   B 161 ? 0.9879 0.7736 0.8029 0.0424  -0.0294 0.0269  170 ARG   B N   
1483 C  CA  . ARG   B 161 ? 1.0051 0.8064 0.8515 0.0265  -0.0242 0.0263  170 ARG   B CA  
1484 C  C   . ARG   B 161 ? 1.0413 0.8314 0.8890 0.0077  -0.0179 0.0358  170 ARG   B C   
1485 O  O   . ARG   B 161 ? 1.0565 0.8179 0.8946 0.0025  -0.0287 0.0386  170 ARG   B O   
1486 C  CB  . ARG   B 161 ? 1.0179 0.8155 0.8798 0.0294  -0.0399 0.0178  170 ARG   B CB  
1487 C  CG  . ARG   B 161 ? 1.0305 0.8516 0.9284 0.0156  -0.0351 0.0154  170 ARG   B CG  
1488 C  CD  . ARG   B 161 ? 1.0685 0.8833 0.9819 0.0168  -0.0538 0.0062  170 ARG   B CD  
1489 N  NE  . ARG   B 161 ? 1.0883 0.9291 1.0390 0.0024  -0.0493 0.0041  170 ARG   B NE  
1490 C  CZ  . ARG   B 161 ? 1.1079 0.9725 1.0771 0.0110  -0.0510 -0.0048 170 ARG   B CZ  
1491 N  NH1 . ARG   B 161 ? 1.1062 0.9692 1.0594 0.0334  -0.0567 -0.0115 170 ARG   B NH1 
1492 N  NH2 . ARG   B 161 ? 1.0956 0.9863 1.0991 -0.0018 -0.0467 -0.0064 170 ARG   B NH2 
1493 N  N   . GLU   B 162 ? 1.0521 0.8629 0.9088 -0.0011 -0.0001 0.0413  171 GLU   B N   
1494 C  CA  . GLU   B 162 ? 1.0826 0.8873 0.9400 -0.0173 0.0101  0.0525  171 GLU   B CA  
1495 C  C   . GLU   B 162 ? 1.0855 0.8929 0.9741 -0.0355 0.0076  0.0546  171 GLU   B C   
1496 O  O   . GLU   B 162 ? 1.1057 0.8854 0.9917 -0.0428 -0.0047 0.0567  171 GLU   B O   
1497 C  CB  . GLU   B 162 ? 1.1198 0.9494 0.9776 -0.0177 0.0295  0.0563  171 GLU   B CB  
1498 C  CG  . GLU   B 162 ? 1.2197 1.0453 1.0479 -0.0030 0.0316  0.0549  171 GLU   B CG  
1499 C  CD  . GLU   B 162 ? 1.3601 1.1552 1.1562 -0.0002 0.0272  0.0619  171 GLU   B CD  
1500 O  OE1 . GLU   B 162 ? 1.3962 1.1851 1.1827 -0.0077 0.0378  0.0719  171 GLU   B OE1 
1501 O  OE2 . GLU   B 162 ? 1.4022 1.1795 1.1807 0.0112  0.0136  0.0578  171 GLU   B OE2 
1502 S  S   . DMS   C .   ? 1.3145 1.2222 1.2316 0.0366  0.0576  -0.0610 201 DMS   B S   
1503 O  O   . DMS   C .   ? 1.3136 1.2306 1.2195 0.0428  0.0629  -0.0527 201 DMS   B O   
1504 C  C1  . DMS   C .   ? 1.3212 1.2077 1.2394 0.0400  0.0633  -0.0641 201 DMS   B C1  
1505 C  C2  . DMS   C .   ? 1.3044 1.2148 1.2452 0.0295  0.0601  -0.0498 201 DMS   B C2  
1506 N  N1  . A1B86 D .   ? 1.0071 1.0843 0.9753 0.1321  0.0940  0.0887  202 A1B86 B N1  
1507 C  C4  . A1B86 D .   ? 0.9924 1.0650 0.9851 0.0955  0.0851  0.0673  202 A1B86 B C4  
1508 C  C5  . A1B86 D .   ? 1.0015 1.0783 0.9730 0.1166  0.0837  0.0746  202 A1B86 B C5  
1509 C  C6  . A1B86 D .   ? 1.0000 1.0920 0.9911 0.1310  0.1084  0.1022  202 A1B86 B C6  
1510 C  C7  . A1B86 D .   ? 1.0089 1.1001 0.9858 0.1542  0.1176  0.1169  202 A1B86 B C7  
1511 C  C8  . A1B86 D .   ? 1.0192 1.0852 0.9668 0.1703  0.1135  0.1149  202 A1B86 B C8  
1512 C  C10 . A1B86 D .   ? 1.0212 1.1133 0.9684 0.2025  0.1354  0.1448  202 A1B86 B C10 
1513 C  C13 . A1B86 D .   ? 1.0505 1.3045 1.1090 0.1999  0.1843  0.2035  202 A1B86 B C13 
1514 C  C15 . A1B86 D .   ? 1.0963 1.3435 1.1067 0.2555  0.2036  0.2311  202 A1B86 B C15 
1515 C  C17 . A1B86 D .   ? 1.0755 1.3811 1.1131 0.2779  0.2412  0.2736  202 A1B86 B C17 
1516 C  C20 . A1B86 D .   ? 1.0052 1.1240 1.0003 0.1601  0.1307  0.1331  202 A1B86 B C20 
1517 C  C21 . A1B86 D .   ? 1.0065 1.0843 0.9558 0.1249  0.0712  0.0678  202 A1B86 B C21 
1518 C  C22 . A1B86 D .   ? 1.0051 1.0812 0.9530 0.1128  0.0617  0.0550  202 A1B86 B C22 
1519 O  O1  . A1B86 D .   ? 1.0339 1.2346 1.0713 0.1714  0.1499  0.1614  202 A1B86 B O1  
1520 C  C12 . A1B86 D .   ? 1.0415 1.2275 1.0649 0.1862  0.1604  0.1729  202 A1B86 B C12 
1521 O  O2  . A1B86 D .   ? 1.0560 1.2634 1.0854 0.2023  0.1775  0.1938  202 A1B86 B O2  
1522 C  C14 . A1B86 D .   ? 1.0662 1.3378 1.1197 0.2250  0.2036  0.2274  202 A1B86 B C14 
1523 C  C19 . A1B86 D .   ? 1.0484 1.3622 1.1403 0.2194  0.2217  0.2465  202 A1B86 B C19 
1524 C  C18 . A1B86 D .   ? 1.0497 1.3814 1.1349 0.2450  0.2413  0.2703  202 A1B86 B C18 
1525 C  C16 . A1B86 D .   ? 1.0983 1.3614 1.0995 0.2826  0.2213  0.2531  202 A1B86 B C16 
1526 N  N2  . A1B86 D .   ? 1.0337 1.1816 1.0338 0.1902  0.1575  0.1673  202 A1B86 B N2  
1527 C  C11 . A1B86 D .   ? 1.0193 1.1389 0.9997 0.1841  0.1408  0.1481  202 A1B86 B C11 
1528 C  C9  . A1B86 D .   ? 1.0173 1.0836 0.9509 0.1940  0.1214  0.1279  202 A1B86 B C9  
1529 CL CL  . A1B86 D .   ? 1.0171 1.0522 0.9168 0.2140  0.1143  0.1230  202 A1B86 B CL  
1530 O  O   . A1B86 D .   ? 0.9863 1.0926 1.0082 0.1130  0.1134  0.1030  202 A1B86 B O   
1531 C  C3  . A1B86 D .   ? 0.9894 1.0613 0.9805 0.0844  0.0743  0.0532  202 A1B86 B C3  
1532 C  C2  . A1B86 D .   ? 0.9968 1.0710 0.9651 0.0933  0.0632  0.0474  202 A1B86 B C2  
1533 C  C1  . A1B86 D .   ? 0.9976 1.0702 0.9606 0.0837  0.0525  0.0332  202 A1B86 B C1  
1534 N  N   . A1B86 D .   ? 1.0113 1.0648 0.9415 0.0930  0.0451  0.0297  202 A1B86 B N   
1535 C  C   . A1B86 D .   ? 0.9984 1.0611 0.9772 0.0659  0.0536  0.0240  202 A1B86 B C   
# 
