data_7HP3
# 
_entry.id   7HP3 
# 
_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   7HP3         pdb_00007hp3 10.2210/pdb7hp3/pdb 
WWPDB D_1001407753 ?            ?                   
# 
_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       2025-05-28 
_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             ? 
# 
loop_
_database_PDB_caveat.id 
_database_PDB_caveat.text 
1 
;Residues LYS B 15 and GLY B 22 that are next to each other in the sample sequence are not properly linked: distance between C (C conformer) and N (C conformer) is 2.58.
;
2 
;Residues LYS B 15 and GLY B 22 that are next to each other in the sample sequence are not properly linked: distance between C (D conformer) and N (D conformer) is 2.58.
;
# 
_pdbx_database_status.entry_id                        7HP3 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                                  5067.486  1  ? ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                           18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                            78.133    3  ? ?    ? ? 
4 non-polymer syn 'N-[(8S)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrazin-3-yl]quinoline-5-carboxamide' 293.323   1  ? ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                                   96.063    1  ? ?    ? ? 
6 water       nat water                                                                           18.015    97 ? ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                            DMS   
4 'N-[(8S)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrazin-3-yl]quinoline-5-carboxamide' A1BHB 
5 'SULFATE ION'                                                                   SO4   
6 water                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BHB non-polymer         . 'N-[(8S)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrazin-3-yl]quinoline-5-carboxamide' ? 'C16 H15 N5 O'   
293.323 
ALA   'L-peptide linking' y ALANINE                                                                         ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                        ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                      ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                 ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                        ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                            ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                           ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                   ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                         ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                          ? 'C3 H7 N O3'     
105.093 
SO4   non-polymer         . 'SULFATE ION'                                                                   ? 'O4 S -2'        
96.063  
THR   'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                      ? 'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                        ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  15  LYS LYS B . n 
B 2 7   GLY 7   22  16  GLY GLY B . n 
B 2 8   GLU 8   23  17  GLU GLU B . n 
B 2 9   THR 9   24  18  THR THR B . n 
B 2 10  THR 10  25  19  THR THR B . n 
B 2 11  ASP 11  26  20  ASP ASP B . n 
B 2 12  GLY 12  27  21  GLY GLY B . n 
B 2 13  VAL 13  28  22  VAL VAL B . n 
B 2 14  TYR 14  29  23  TYR TYR B . n 
B 2 15  ARG 15  30  24  ARG ARG B . n 
B 2 16  VAL 16  31  25  VAL VAL B . n 
B 2 17  MET 17  32  26  MET MET B . n 
B 2 18  THR 18  33  27  THR THR B . n 
B 2 19  ARG 19  34  28  ARG ARG B . n 
B 2 20  ARG 20  35  29  ARG ARG B . n 
B 2 21  LEU 21  36  30  LEU LEU B . n 
B 2 22  LEU 22  37  31  LEU LEU B . n 
B 2 23  GLY 23  38  32  GLY GLY B . n 
B 2 24  SER 24  39  33  SER SER B . n 
B 2 25  THR 25  40  34  THR THR B . n 
B 2 26  GLN 26  41  35  GLN GLN B . n 
B 2 27  VAL 27  42  36  VAL VAL B . n 
B 2 28  GLY 28  43  37  GLY GLY B . n 
B 2 29  VAL 29  44  38  VAL VAL B . n 
B 2 30  GLY 30  45  39  GLY GLY B . n 
B 2 31  VAL 31  46  40  VAL VAL B . n 
B 2 32  MET 32  47  41  MET MET B . n 
B 2 33  GLN 33  48  42  GLN GLN B . n 
B 2 34  GLU 34  49  43  GLU GLU B . n 
B 2 35  GLY 35  50  44  GLY GLY B . n 
B 2 36  VAL 36  51  45  VAL VAL B . n 
B 2 37  PHE 37  52  46  PHE PHE B . n 
B 2 38  HIS 38  53  47  HIS HIS B . n 
B 2 39  THR 39  54  48  THR THR B . n 
B 2 40  MET 40  55  49  MET MET B . n 
B 2 41  TRP 41  56  50  TRP TRP B . n 
B 2 42  HIS 42  57  51  HIS HIS B . n 
B 2 43  VAL 43  58  52  VAL VAL B . n 
B 2 44  THR 44  59  53  THR THR B . n 
B 2 45  LYS 45  60  54  LYS LYS B . n 
B 2 46  GLY 46  61  55  GLY GLY B . n 
B 2 47  ALA 47  62  56  ALA ALA B . n 
B 2 48  ALA 48  63  57  ALA ALA B . n 
B 2 49  LEU 49  64  58  LEU LEU B . n 
B 2 50  ARG 50  65  59  ARG ARG B . n 
B 2 51  SER 51  66  60  SER SER B . n 
B 2 52  GLY 52  67  61  GLY GLY B . n 
B 2 53  GLU 53  68  62  GLU GLU B . n 
B 2 54  GLY 54  69  63  GLY GLY B . n 
B 2 55  ARG 55  70  64  ARG ARG B . n 
B 2 56  LEU 56  71  65  LEU LEU B . n 
B 2 57  ASP 57  72  66  ASP ASP B . n 
B 2 58  PRO 58  73  67  PRO PRO B . n 
B 2 59  TYR 59  74  68  TYR TYR B . n 
B 2 60  TRP 60  75  69  TRP TRP B . n 
B 2 61  GLY 61  76  70  GLY GLY B . n 
B 2 62  ASP 62  77  71  ASP ASP B . n 
B 2 63  VAL 63  78  72  VAL VAL B . n 
B 2 64  LYS 64  79  73  LYS LYS B . n 
B 2 65  GLN 65  80  74  GLN GLN B . n 
B 2 66  ASP 66  81  75  ASP ASP B . n 
B 2 67  LEU 67  82  76  LEU LEU B . n 
B 2 68  VAL 68  83  77  VAL VAL B . n 
B 2 69  SER 69  84  78  SER SER B . n 
B 2 70  TYR 70  85  79  TYR TYR B . n 
B 2 71  CYS 71  86  80  CYS CYS B . n 
B 2 72  GLY 72  87  81  GLY GLY B . n 
B 2 73  PRO 73  88  82  PRO PRO B . n 
B 2 74  TRP 74  89  83  TRP TRP B . n 
B 2 75  LYS 75  90  84  LYS LYS B . n 
B 2 76  LEU 76  91  85  LEU LEU B . n 
B 2 77  ASP 77  92  86  ASP ASP B . n 
B 2 78  ALA 78  93  87  ALA ALA B . n 
B 2 79  ALA 79  94  88  ALA ALA B . n 
B 2 80  TRP 80  95  89  TRP TRP B . n 
B 2 81  ASP 81  96  90  ASP ASP B . n 
B 2 82  GLY 82  97  91  GLY GLY B . n 
B 2 83  LEU 83  98  92  LEU LEU B . n 
B 2 84  SER 84  99  93  SER SER B . n 
B 2 85  GLU 85  100 94  GLU GLU B . n 
B 2 86  VAL 86  101 95  VAL VAL B . n 
B 2 87  GLN 87  102 96  GLN GLN B . n 
B 2 88  LEU 88  103 97  LEU LEU B . n 
B 2 89  LEU 89  104 98  LEU LEU B . n 
B 2 90  ALA 90  105 99  ALA ALA B . n 
B 2 91  VAL 91  106 100 VAL VAL B . n 
B 2 92  PRO 92  107 101 PRO PRO B . n 
B 2 93  PRO 93  108 102 PRO PRO B . n 
B 2 94  GLY 94  109 103 GLY GLY B . n 
B 2 95  GLU 95  110 104 GLU GLU B . n 
B 2 96  ARG 96  111 105 ARG ARG B . n 
B 2 97  ALA 97  112 106 ALA ALA B . n 
B 2 98  LYS 98  113 107 LYS LYS B . n 
B 2 99  ASN 99  114 108 ASN ASN B . n 
B 2 100 ILE 100 115 109 ILE ILE B . n 
B 2 101 GLN 101 116 110 GLN GLN B . n 
B 2 102 THR 102 117 111 THR THR B . n 
B 2 103 LEU 103 118 112 LEU LEU B . n 
B 2 104 PRO 104 119 113 PRO PRO B . n 
B 2 105 GLY 105 120 114 GLY GLY B . n 
B 2 106 ILE 106 121 115 ILE ILE B . n 
B 2 107 PHE 107 122 116 PHE PHE B . n 
B 2 108 LYS 108 123 117 LYS LYS B . n 
B 2 109 THR 109 124 118 THR THR B . n 
B 2 110 LYS 110 125 119 LYS LYS B . n 
B 2 111 ASP 111 126 120 ASP ASP B . n 
B 2 112 GLY 112 127 121 GLY GLY B . n 
B 2 113 ASP 113 128 122 ASP ASP B . n 
B 2 114 ILE 114 129 123 ILE ILE B . n 
B 2 115 GLY 115 130 124 GLY GLY B . n 
B 2 116 ALA 116 131 125 ALA ALA B . n 
B 2 117 VAL 117 132 126 VAL VAL B . n 
B 2 118 ALA 118 133 127 ALA ALA B . n 
B 2 119 LEU 119 134 128 LEU LEU B . n 
B 2 120 ASP 120 135 129 ASP ASP B . n 
B 2 121 TYR 121 136 130 TYR TYR B . n 
B 2 122 PRO 122 137 131 PRO PRO B . n 
B 2 123 ALA 123 138 132 ALA ALA B . n 
B 2 124 GLY 124 139 133 GLY GLY B . n 
B 2 125 THR 125 140 134 THR THR B . n 
B 2 126 SER 126 141 135 SER SER B . n 
B 2 127 GLY 127 142 136 GLY GLY B . n 
B 2 128 SER 128 143 137 SER SER B . n 
B 2 129 PRO 129 144 138 PRO PRO B . n 
B 2 130 ILE 130 145 139 ILE ILE B . n 
B 2 131 LEU 131 146 140 LEU LEU B . n 
B 2 132 ASP 132 147 141 ASP ASP B . n 
B 2 133 LYS 133 148 142 LYS LYS B . n 
B 2 134 CYS 134 149 143 CYS CYS B . n 
B 2 135 GLY 135 150 144 GLY GLY B . n 
B 2 136 ARG 136 151 145 ARG ARG B . n 
B 2 137 VAL 137 152 146 VAL VAL B . n 
B 2 138 ILE 138 153 147 ILE ILE B . n 
B 2 139 GLY 139 154 148 GLY GLY B . n 
B 2 140 LEU 140 155 149 LEU LEU B . n 
B 2 141 TYR 141 156 150 TYR TYR B . n 
B 2 142 GLY 142 157 151 GLY GLY B . n 
B 2 143 ASN 143 158 152 ASN ASN B . n 
B 2 144 GLY 144 159 153 GLY GLY B . n 
B 2 145 VAL 145 160 154 VAL VAL B . n 
B 2 146 VAL 146 161 155 VAL VAL B . n 
B 2 147 ILE 147 162 156 ILE ILE B . n 
B 2 148 LYS 148 163 157 LYS LYS B . n 
B 2 149 ASN 149 164 158 ASN ASN B . n 
B 2 150 GLY 150 165 159 GLY GLY B . n 
B 2 151 SER 151 166 160 SER SER B . n 
B 2 152 TYR 152 167 161 TYR TYR B . n 
B 2 153 VAL 153 168 162 VAL VAL B . n 
B 2 154 SER 154 169 163 SER SER B . n 
B 2 155 ALA 155 170 164 ALA ALA B . n 
B 2 156 ILE 156 171 165 ILE ILE B . n 
B 2 157 THR 157 172 166 THR THR B . n 
B 2 158 GLN 158 173 167 GLN GLN B . n 
B 2 159 GLY 159 174 168 GLY GLY B . n 
B 2 160 LYS 160 175 169 LYS LYS B . n 
B 2 161 ARG 161 176 170 ARG ARG B . n 
B 2 162 GLU 162 177 171 GLU GLU B . n 
B 2 163 GLU 163 178 ?   ?   ?   B . n 
B 2 164 GLU 164 179 ?   ?   ?   B . n 
B 2 165 THR 165 180 ?   ?   ?   B . n 
B 2 166 PRO 166 181 ?   ?   ?   B . n 
B 2 167 VAL 167 182 ?   ?   ?   B . n 
B 2 168 GLU 168 183 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BHB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BHB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BHB 1  204 301 A1BHB LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 6 HOH   1  101 48  HOH   HOH A . 
H 6 HOH   2  102 34  HOH   HOH A . 
H 6 HOH   3  103 105 HOH   HOH A . 
H 6 HOH   4  104 119 HOH   HOH A . 
H 6 HOH   5  105 98  HOH   HOH A . 
H 6 HOH   6  106 130 HOH   HOH A . 
H 6 HOH   7  107 65  HOH   HOH A . 
H 6 HOH   8  108 54  HOH   HOH A . 
H 6 HOH   9  109 118 HOH   HOH A . 
H 6 HOH   10 110 16  HOH   HOH A . 
H 6 HOH   11 111 121 HOH   HOH A . 
H 6 HOH   12 112 40  HOH   HOH A . 
H 6 HOH   13 113 120 HOH   HOH A . 
H 6 HOH   14 114 70  HOH   HOH A . 
H 6 HOH   15 115 49  HOH   HOH A . 
H 6 HOH   16 116 110 HOH   HOH A . 
H 6 HOH   17 117 50  HOH   HOH A . 
H 6 HOH   18 118 29  HOH   HOH A . 
H 6 HOH   19 119 28  HOH   HOH A . 
H 6 HOH   20 120 77  HOH   HOH A . 
H 6 HOH   21 121 27  HOH   HOH A . 
H 6 HOH   22 122 83  HOH   HOH A . 
I 6 HOH   1  301 51  HOH   HOH B . 
I 6 HOH   2  302 11  HOH   HOH B . 
I 6 HOH   3  303 58  HOH   HOH B . 
I 6 HOH   4  304 90  HOH   HOH B . 
I 6 HOH   5  305 92  HOH   HOH B . 
I 6 HOH   6  306 46  HOH   HOH B . 
I 6 HOH   7  307 1   HOH   HOH B . 
I 6 HOH   8  308 32  HOH   HOH B . 
I 6 HOH   9  309 14  HOH   HOH B . 
I 6 HOH   10 310 4   HOH   HOH B . 
I 6 HOH   11 311 62  HOH   HOH B . 
I 6 HOH   12 312 5   HOH   HOH B . 
I 6 HOH   13 313 20  HOH   HOH B . 
I 6 HOH   14 314 24  HOH   HOH B . 
I 6 HOH   15 315 107 HOH   HOH B . 
I 6 HOH   16 316 131 HOH   HOH B . 
I 6 HOH   17 317 89  HOH   HOH B . 
I 6 HOH   18 318 117 HOH   HOH B . 
I 6 HOH   19 319 135 HOH   HOH B . 
I 6 HOH   20 320 31  HOH   HOH B . 
I 6 HOH   21 321 134 HOH   HOH B . 
I 6 HOH   22 322 42  HOH   HOH B . 
I 6 HOH   23 323 100 HOH   HOH B . 
I 6 HOH   24 324 108 HOH   HOH B . 
I 6 HOH   25 325 9   HOH   HOH B . 
I 6 HOH   26 326 36  HOH   HOH B . 
I 6 HOH   27 327 115 HOH   HOH B . 
I 6 HOH   28 328 126 HOH   HOH B . 
I 6 HOH   29 329 30  HOH   HOH B . 
I 6 HOH   30 330 81  HOH   HOH B . 
I 6 HOH   31 331 2   HOH   HOH B . 
I 6 HOH   32 332 68  HOH   HOH B . 
I 6 HOH   33 333 56  HOH   HOH B . 
I 6 HOH   34 334 116 HOH   HOH B . 
I 6 HOH   35 335 57  HOH   HOH B . 
I 6 HOH   36 336 60  HOH   HOH B . 
I 6 HOH   37 337 10  HOH   HOH B . 
I 6 HOH   38 338 133 HOH   HOH B . 
I 6 HOH   39 339 63  HOH   HOH B . 
I 6 HOH   40 340 35  HOH   HOH B . 
I 6 HOH   41 341 23  HOH   HOH B . 
I 6 HOH   42 342 17  HOH   HOH B . 
I 6 HOH   43 343 79  HOH   HOH B . 
I 6 HOH   44 344 66  HOH   HOH B . 
I 6 HOH   45 345 39  HOH   HOH B . 
I 6 HOH   46 346 112 HOH   HOH B . 
I 6 HOH   47 347 102 HOH   HOH B . 
I 6 HOH   48 348 67  HOH   HOH B . 
I 6 HOH   49 349 82  HOH   HOH B . 
I 6 HOH   50 350 13  HOH   HOH B . 
I 6 HOH   51 351 103 HOH   HOH B . 
I 6 HOH   52 352 73  HOH   HOH B . 
I 6 HOH   53 353 72  HOH   HOH B . 
I 6 HOH   54 354 21  HOH   HOH B . 
I 6 HOH   55 355 122 HOH   HOH B . 
I 6 HOH   56 356 43  HOH   HOH B . 
I 6 HOH   57 357 18  HOH   HOH B . 
I 6 HOH   58 358 3   HOH   HOH B . 
I 6 HOH   59 359 106 HOH   HOH B . 
I 6 HOH   60 360 125 HOH   HOH B . 
I 6 HOH   61 361 12  HOH   HOH B . 
I 6 HOH   62 362 94  HOH   HOH B . 
I 6 HOH   63 363 64  HOH   HOH B . 
I 6 HOH   64 364 26  HOH   HOH B . 
I 6 HOH   65 365 129 HOH   HOH B . 
I 6 HOH   66 366 87  HOH   HOH B . 
I 6 HOH   67 367 69  HOH   HOH B . 
I 6 HOH   68 368 45  HOH   HOH B . 
I 6 HOH   69 369 44  HOH   HOH B . 
I 6 HOH   70 370 61  HOH   HOH B . 
I 6 HOH   71 371 75  HOH   HOH B . 
I 6 HOH   72 372 80  HOH   HOH B . 
I 6 HOH   73 373 59  HOH   HOH B . 
I 6 HOH   74 374 109 HOH   HOH B . 
I 6 HOH   75 375 85  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HP3 
_cell.length_a           42.400 
_cell.length_b           42.400 
_cell.length_c           216.420 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HP3 
_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          7HP3 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.09 
_exptl_crystal.density_percent_sol   41.04 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-09-29 
_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                     7HP3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.40 
_reflns.d_resolution_high            1.84 
_reflns.number_obs                   18277 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.130 
_reflns.pdbx_netI_over_sigmaI        12.2 
_reflns.pdbx_redundancy              22.0 
_reflns.pdbx_Rrim_I_all              0.133 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     401433 
_reflns.pdbx_chi_squared             0.98 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.84 
_reflns_shell.d_res_low                   1.89 
_reflns_shell.number_measured_all         24075 
_reflns_shell.number_unique_obs           1304 
_reflns_shell.Rmerge_I_obs                8.109 
_reflns_shell.pdbx_chi_squared            0.86 
_reflns_shell.pdbx_redundancy             18.5 
_reflns_shell.percent_possible_obs        99.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             8.328 
_reflns_shell.pdbx_Rpim_I_all             1.822 
_reflns_shell.pdbx_CC_half                0.266 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HP3 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     16431 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             42.44 
_refine.ls_d_res_high                            1.84 
_refine.ls_percent_reflns_obs                    94.76 
_refine.ls_R_factor_obs                          0.24227 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.24026 
_refine.ls_R_factor_R_free                       0.27988 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_number_reflns_R_free                  847 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.B_iso_mean                               64.931 
_refine.aniso_B[1][1]                            -0.23 
_refine.aniso_B[2][2]                            -0.23 
_refine.aniso_B[3][3]                            0.46 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.263 
_refine.pdbx_overall_ESU_R_Free                  0.201 
_refine.overall_SU_ML                            0.309 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             25.004 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               1621 
_refine_hist.d_res_high                       1.84 
_refine_hist.d_res_low                        42.44 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.012  0.014  ? 2761 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.004  0.015  ? 1998 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.624  1.642  ? 3105 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.286  1.601  ? 4633 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.371  5.000  ? 304  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.689 23.271 ? 107  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.277 15.000 ? 330  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.412 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.070  0.200  ? 269  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2758 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 534  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.264  1.847  ? 1410 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.297  1.572  ? 1336 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.397  2.236  ? 1462 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.397  2.243  ? 1463 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.342  1.885  ? 1351 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.341  1.814  ? 1338 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.444  2.491  ? 1632 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       12.731 16.885 ? 2605 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         12.741 16.458 ? 2589 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.840 
_refine_ls_shell.d_res_low                        1.888 
_refine_ls_shell.number_reflns_R_work             725 
_refine_ls_shell.R_factor_R_work                  0.639 
_refine_ls_shell.percent_reflns_obs               59.08 
_refine_ls_shell.R_factor_R_free                  0.694 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             46 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HP3 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014790-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HP3 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HP3 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HP3 B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 183 
# 
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 7HP3 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HP3 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HP3 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HP3 LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                113 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 56  LYS B 60  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 137 SER B 141 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             149 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             149 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.451 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        149 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       149 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8  ? 
AA2 ? 10 ? 
# 
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 
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? parallel      
AA2 9 10 ? 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 69  LEU B 71  
AA1 2  LEU B 49  ? SER B 51  ? LEU B 64  SER B 66  
AA1 3  MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4  GLY B 12  ? THR B 18  ? GLY B 27  THR B 33  
AA1 5  THR B 25  ? GLN B 33  ? THR B 40  GLN B 48  
AA1 6  VAL B 36  ? MET B 40  ? VAL B 51  MET B 55  
AA1 7  LEU B 67  ? TYR B 70  ? LEU B 82  TYR B 85  
AA1 8  PRO B 58  ? ASP B 62  ? PRO B 73  ASP B 77  
AA2 1  GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2  LYS B 98  ? THR B 102 ? LYS B 113 THR B 117 
AA2 3  VAL B 86  ? ALA B 90  ? VAL B 101 ALA B 105 
AA2 4  PRO B 129 ? LEU B 131 ? PRO B 144 LEU B 146 
AA2 5  VAL B 137 ? VAL B 146 ? VAL B 152 VAL B 161 
AA2 6  TYR B 152 ? THR B 157 ? TYR B 167 THR B 172 
AA2 7  GLY B 112 ? VAL B 117 ? GLY B 127 VAL B 132 
AA2 8  GLY B 105 ? THR B 109 ? GLY B 120 THR B 124 
AA2 9  ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA2 10 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
# 
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 71  N LEU B 49  ? N LEU B 64  
AA1 2 3  O ARG B 50  ? O ARG B 65  N ILE A 10  ? N ILE A 53  
AA1 3 4  N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 30  
AA1 4 5  N VAL B 16  ? N VAL B 31  O GLY B 28  ? O GLY B 43  
AA1 5 6  N VAL B 31  ? N VAL B 46  O HIS B 38  ? O HIS B 53  
AA1 6 7  N THR B 39  ? N THR B 54  O VAL B 68  ? O VAL B 83  
AA1 7 8  O SER B 69  ? O SER B 84  N TRP B 60  ? N TRP B 75  
AA2 1 2  N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 116 
AA2 2 3  O THR B 102 ? O THR B 117 N VAL B 86  ? N VAL B 101 
AA2 3 4  N LEU B 89  ? N LEU B 104 O PRO B 129 ? O PRO B 144 
AA2 4 5  N ILE B 130 ? N ILE B 145 O GLY B 139 ? O GLY B 154 
AA2 5 6  N LEU B 140 ? N LEU B 155 O THR B 157 ? O THR B 172 
AA2 6 7  O SER B 154 ? O SER B 169 N VAL B 117 ? N VAL B 132 
AA2 7 8  O ILE B 114 ? O ILE B 129 N PHE B 107 ? N PHE B 122 
AA2 8 9  O LYS B 108 ? O LYS B 123 N LEU A 31  ? N LEU A 74  
AA2 9 10 N ALA A 34  ? N ALA A 77  O SER A 42  ? O SER A 85  
# 
_pdbx_entry_details.entry_id                   7HP3 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 B GLU 23 ? B O B HOH 301 ? ? 2.08 
2 1 OE1 B GLU 23 ? A O B HOH 301 ? ? 2.08 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             100 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             100 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.381 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.152 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               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 ASN A 70  ? C -67.49  -177.85 
2 1 ASN A 70  ? D -67.49  -177.85 
3 1 GLU B 23  ? C -29.20  108.23  
4 1 GLU B 23  ? D -29.16  108.66  
5 1 ASP B 26  ? ? -48.24  154.49  
6 1 LEU B 36  ? ? -107.81 -165.29 
7 1 CYS B 86  ? ? 83.79   -6.96   
8 1 LEU B 98  ? ? -127.12 -52.43  
9 1 VAL B 106 ? ? -119.93 79.30   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             GLU 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              100 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   11.06 
# 
loop_
_pdbx_validate_polymer_linkage.id 
_pdbx_validate_polymer_linkage.PDB_model_num 
_pdbx_validate_polymer_linkage.auth_atom_id_1 
_pdbx_validate_polymer_linkage.auth_asym_id_1 
_pdbx_validate_polymer_linkage.auth_comp_id_1 
_pdbx_validate_polymer_linkage.auth_seq_id_1 
_pdbx_validate_polymer_linkage.PDB_ins_code_1 
_pdbx_validate_polymer_linkage.label_alt_id_1 
_pdbx_validate_polymer_linkage.auth_atom_id_2 
_pdbx_validate_polymer_linkage.auth_asym_id_2 
_pdbx_validate_polymer_linkage.auth_comp_id_2 
_pdbx_validate_polymer_linkage.auth_seq_id_2 
_pdbx_validate_polymer_linkage.PDB_ins_code_2 
_pdbx_validate_polymer_linkage.label_alt_id_2 
_pdbx_validate_polymer_linkage.dist 
1 1 C B LYS 15 ? C N B GLY 22 ? C 2.58 
2 1 C B LYS 15 ? D N B GLY 22 ? D 2.58 
# 
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 345 ? I HOH . 
2 1 B HOH 360 ? I HOH . 
3 1 B HOH 365 ? I HOH . 
4 1 B HOH 368 ? I HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.8204 -1.7821 -19.5422 0.5449 0.5486 0.1018 0.1722 0.1482 0.1092  2.7176 4.4983 2.0762 -1.3045 
0.4829 1.3368  0.4540 0.1657 0.3481 -0.5647 -0.3262 -0.3788 -0.0055 0.1797 -0.1278 
'X-RAY DIFFRACTION' 2 ? refined -19.2016 0.8754  -15.7180 0.8154 0.8110 0.2205 0.1923 0.0747 -0.0428 0.5154 0.3207 1.4571 -0.3146 
0.5701 -0.2835 0.2990 0.1752 0.0450 -0.1641 -0.3302 0.1078  0.2679  0.1921 0.0312  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 15 ? ? B 302 ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B GLU 178 ? B GLU 163 
14 1 Y 1 B GLU 179 ? B GLU 164 
15 1 Y 1 B THR 180 ? B THR 165 
16 1 Y 1 B PRO 181 ? B PRO 166 
17 1 Y 1 B VAL 182 ? B VAL 167 
18 1 Y 1 B GLU 183 ? 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 
A1BHB N1   N N N 1   
A1BHB N3   N Y N 2   
A1BHB C4   C Y N 3   
A1BHB C5   C N N 4   
A1BHB C6   C N N 5   
A1BHB C7   C N N 6   
A1BHB C8   C Y N 7   
A1BHB C10  C Y N 8   
A1BHB C13  C Y N 9   
A1BHB C15  C Y N 10  
A1BHB O1   O N N 11  
A1BHB C1   C N N 12  
A1BHB C2   C Y N 13  
A1BHB C3   C Y N 14  
A1BHB N2   N Y N 15  
A1BHB N4   N N N 16  
A1BHB C9   C Y N 17  
A1BHB C11  C Y N 18  
A1BHB C12  C Y N 19  
A1BHB N5   N Y N 20  
A1BHB C14  C Y N 21  
A1BHB C16  C Y N 22  
A1BHB H1   H N N 23  
A1BHB H3   H N N 24  
A1BHB H4   H N N 25  
A1BHB H6   H N N 26  
A1BHB H7   H N N 27  
A1BHB H8   H N N 28  
A1BHB H9   H N N 29  
A1BHB H11  H N N 30  
A1BHB H13  H N N 31  
A1BHB H15  H N N 32  
A1BHB H2   H N N 33  
A1BHB H5   H N N 34  
A1BHB H10  H N N 35  
A1BHB H12  H N N 36  
A1BHB H14  H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
DMS   S    S N N 125 
DMS   O    O N N 126 
DMS   C1   C N N 127 
DMS   C2   C N N 128 
DMS   H11  H N N 129 
DMS   H12  H N N 130 
DMS   H13  H N N 131 
DMS   H21  H N N 132 
DMS   H22  H N N 133 
DMS   H23  H N N 134 
GLN   N    N N N 135 
GLN   CA   C N S 136 
GLN   C    C N N 137 
GLN   O    O N N 138 
GLN   CB   C N N 139 
GLN   CG   C N N 140 
GLN   CD   C N N 141 
GLN   OE1  O N N 142 
GLN   NE2  N N N 143 
GLN   OXT  O N N 144 
GLN   H    H N N 145 
GLN   H2   H N N 146 
GLN   HA   H N N 147 
GLN   HB2  H N N 148 
GLN   HB3  H N N 149 
GLN   HG2  H N N 150 
GLN   HG3  H N N 151 
GLN   HE21 H N N 152 
GLN   HE22 H N N 153 
GLN   HXT  H N N 154 
GLU   N    N N N 155 
GLU   CA   C N S 156 
GLU   C    C N N 157 
GLU   O    O N N 158 
GLU   CB   C N N 159 
GLU   CG   C N N 160 
GLU   CD   C N N 161 
GLU   OE1  O N N 162 
GLU   OE2  O N N 163 
GLU   OXT  O N N 164 
GLU   H    H N N 165 
GLU   H2   H N N 166 
GLU   HA   H N N 167 
GLU   HB2  H N N 168 
GLU   HB3  H N N 169 
GLU   HG2  H N N 170 
GLU   HG3  H N N 171 
GLU   HE2  H N N 172 
GLU   HXT  H N N 173 
GLY   N    N N N 174 
GLY   CA   C N N 175 
GLY   C    C N N 176 
GLY   O    O N N 177 
GLY   OXT  O N N 178 
GLY   H    H N N 179 
GLY   H2   H N N 180 
GLY   HA2  H N N 181 
GLY   HA3  H N N 182 
GLY   HXT  H N N 183 
HIS   N    N N N 184 
HIS   CA   C N S 185 
HIS   C    C N N 186 
HIS   O    O N N 187 
HIS   CB   C N N 188 
HIS   CG   C Y N 189 
HIS   ND1  N Y N 190 
HIS   CD2  C Y N 191 
HIS   CE1  C Y N 192 
HIS   NE2  N Y N 193 
HIS   OXT  O N N 194 
HIS   H    H N N 195 
HIS   H2   H N N 196 
HIS   HA   H N N 197 
HIS   HB2  H N N 198 
HIS   HB3  H N N 199 
HIS   HD1  H N N 200 
HIS   HD2  H N N 201 
HIS   HE1  H N N 202 
HIS   HE2  H N N 203 
HIS   HXT  H N N 204 
HOH   O    O N N 205 
HOH   H1   H N N 206 
HOH   H2   H N N 207 
ILE   N    N N N 208 
ILE   CA   C N S 209 
ILE   C    C N N 210 
ILE   O    O N N 211 
ILE   CB   C N S 212 
ILE   CG1  C N N 213 
ILE   CG2  C N N 214 
ILE   CD1  C N N 215 
ILE   OXT  O N N 216 
ILE   H    H N N 217 
ILE   H2   H N N 218 
ILE   HA   H N N 219 
ILE   HB   H N N 220 
ILE   HG12 H N N 221 
ILE   HG13 H N N 222 
ILE   HG21 H N N 223 
ILE   HG22 H N N 224 
ILE   HG23 H N N 225 
ILE   HD11 H N N 226 
ILE   HD12 H N N 227 
ILE   HD13 H N N 228 
ILE   HXT  H N N 229 
LEU   N    N N N 230 
LEU   CA   C N S 231 
LEU   C    C N N 232 
LEU   O    O N N 233 
LEU   CB   C N N 234 
LEU   CG   C N N 235 
LEU   CD1  C N N 236 
LEU   CD2  C N N 237 
LEU   OXT  O N N 238 
LEU   H    H N N 239 
LEU   H2   H N N 240 
LEU   HA   H N N 241 
LEU   HB2  H N N 242 
LEU   HB3  H N N 243 
LEU   HG   H N N 244 
LEU   HD11 H N N 245 
LEU   HD12 H N N 246 
LEU   HD13 H N N 247 
LEU   HD21 H N N 248 
LEU   HD22 H N N 249 
LEU   HD23 H N N 250 
LEU   HXT  H N N 251 
LYS   N    N N N 252 
LYS   CA   C N S 253 
LYS   C    C N N 254 
LYS   O    O N N 255 
LYS   CB   C N N 256 
LYS   CG   C N N 257 
LYS   CD   C N N 258 
LYS   CE   C N N 259 
LYS   NZ   N N N 260 
LYS   OXT  O N N 261 
LYS   H    H N N 262 
LYS   H2   H N N 263 
LYS   HA   H N N 264 
LYS   HB2  H N N 265 
LYS   HB3  H N N 266 
LYS   HG2  H N N 267 
LYS   HG3  H N N 268 
LYS   HD2  H N N 269 
LYS   HD3  H N N 270 
LYS   HE2  H N N 271 
LYS   HE3  H N N 272 
LYS   HZ1  H N N 273 
LYS   HZ2  H N N 274 
LYS   HZ3  H N N 275 
LYS   HXT  H N N 276 
MET   N    N N N 277 
MET   CA   C N S 278 
MET   C    C N N 279 
MET   O    O N N 280 
MET   CB   C N N 281 
MET   CG   C N N 282 
MET   SD   S N N 283 
MET   CE   C N N 284 
MET   OXT  O N N 285 
MET   H    H N N 286 
MET   H2   H N N 287 
MET   HA   H N N 288 
MET   HB2  H N N 289 
MET   HB3  H N N 290 
MET   HG2  H N N 291 
MET   HG3  H N N 292 
MET   HE1  H N N 293 
MET   HE2  H N N 294 
MET   HE3  H N N 295 
MET   HXT  H N N 296 
PHE   N    N N N 297 
PHE   CA   C N S 298 
PHE   C    C N N 299 
PHE   O    O N N 300 
PHE   CB   C N N 301 
PHE   CG   C Y N 302 
PHE   CD1  C Y N 303 
PHE   CD2  C Y N 304 
PHE   CE1  C Y N 305 
PHE   CE2  C Y N 306 
PHE   CZ   C Y N 307 
PHE   OXT  O N N 308 
PHE   H    H N N 309 
PHE   H2   H N N 310 
PHE   HA   H N N 311 
PHE   HB2  H N N 312 
PHE   HB3  H N N 313 
PHE   HD1  H N N 314 
PHE   HD2  H N N 315 
PHE   HE1  H N N 316 
PHE   HE2  H N N 317 
PHE   HZ   H N N 318 
PHE   HXT  H N N 319 
PRO   N    N N N 320 
PRO   CA   C N S 321 
PRO   C    C N N 322 
PRO   O    O N N 323 
PRO   CB   C N N 324 
PRO   CG   C N N 325 
PRO   CD   C N N 326 
PRO   OXT  O N N 327 
PRO   H    H N N 328 
PRO   HA   H N N 329 
PRO   HB2  H N N 330 
PRO   HB3  H N N 331 
PRO   HG2  H N N 332 
PRO   HG3  H N N 333 
PRO   HD2  H N N 334 
PRO   HD3  H N N 335 
PRO   HXT  H N N 336 
SER   N    N N N 337 
SER   CA   C N S 338 
SER   C    C N N 339 
SER   O    O N N 340 
SER   CB   C N N 341 
SER   OG   O N N 342 
SER   OXT  O N N 343 
SER   H    H N N 344 
SER   H2   H N N 345 
SER   HA   H N N 346 
SER   HB2  H N N 347 
SER   HB3  H N N 348 
SER   HG   H N N 349 
SER   HXT  H N N 350 
SO4   S    S N N 351 
SO4   O1   O N N 352 
SO4   O2   O N N 353 
SO4   O3   O N N 354 
SO4   O4   O N N 355 
THR   N    N N N 356 
THR   CA   C N S 357 
THR   C    C N N 358 
THR   O    O N N 359 
THR   CB   C N R 360 
THR   OG1  O N N 361 
THR   CG2  C N N 362 
THR   OXT  O N N 363 
THR   H    H N N 364 
THR   H2   H N N 365 
THR   HA   H N N 366 
THR   HB   H N N 367 
THR   HG1  H N N 368 
THR   HG21 H N N 369 
THR   HG22 H N N 370 
THR   HG23 H N N 371 
THR   HXT  H N N 372 
TRP   N    N N N 373 
TRP   CA   C N S 374 
TRP   C    C N N 375 
TRP   O    O N N 376 
TRP   CB   C N N 377 
TRP   CG   C Y N 378 
TRP   CD1  C Y N 379 
TRP   CD2  C Y N 380 
TRP   NE1  N Y N 381 
TRP   CE2  C Y N 382 
TRP   CE3  C Y N 383 
TRP   CZ2  C Y N 384 
TRP   CZ3  C Y N 385 
TRP   CH2  C Y N 386 
TRP   OXT  O N N 387 
TRP   H    H N N 388 
TRP   H2   H N N 389 
TRP   HA   H N N 390 
TRP   HB2  H N N 391 
TRP   HB3  H N N 392 
TRP   HD1  H N N 393 
TRP   HE1  H N N 394 
TRP   HE3  H N N 395 
TRP   HZ2  H N N 396 
TRP   HZ3  H N N 397 
TRP   HH2  H N N 398 
TRP   HXT  H N N 399 
TYR   N    N N N 400 
TYR   CA   C N S 401 
TYR   C    C N N 402 
TYR   O    O N N 403 
TYR   CB   C N N 404 
TYR   CG   C Y N 405 
TYR   CD1  C Y N 406 
TYR   CD2  C Y N 407 
TYR   CE1  C Y N 408 
TYR   CE2  C Y N 409 
TYR   CZ   C Y N 410 
TYR   OH   O N N 411 
TYR   OXT  O N N 412 
TYR   H    H N N 413 
TYR   H2   H N N 414 
TYR   HA   H N N 415 
TYR   HB2  H N N 416 
TYR   HB3  H N N 417 
TYR   HD1  H N N 418 
TYR   HD2  H N N 419 
TYR   HE1  H N N 420 
TYR   HE2  H N N 421 
TYR   HH   H N N 422 
TYR   HXT  H N N 423 
VAL   N    N N N 424 
VAL   CA   C N S 425 
VAL   C    C N N 426 
VAL   O    O N N 427 
VAL   CB   C N N 428 
VAL   CG1  C N N 429 
VAL   CG2  C N N 430 
VAL   OXT  O N N 431 
VAL   H    H N N 432 
VAL   H2   H N N 433 
VAL   HA   H N N 434 
VAL   HB   H N N 435 
VAL   HG11 H N N 436 
VAL   HG12 H N N 437 
VAL   HG13 H N N 438 
VAL   HG21 H N N 439 
VAL   HG22 H N N 440 
VAL   HG23 H N N 441 
VAL   HXT  H N N 442 
# 
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 
A1BHB O1  C1   doub N N 1   
A1BHB C1  N1   sing N N 2   
A1BHB N1  C2   sing N N 3   
A1BHB C2  C3   sing Y N 4   
A1BHB C3  N2   doub Y N 5   
A1BHB N2  N3   sing Y N 6   
A1BHB N3  C4   sing Y N 7   
A1BHB C4  C5   sing N N 8   
A1BHB C5  N4   sing N N 9   
A1BHB N4  C6   sing N N 10  
A1BHB C6  C7   sing N N 11  
A1BHB C1  C8   sing N N 12  
A1BHB C8  C9   doub Y N 13  
A1BHB C9  C10  sing Y N 14  
A1BHB C10 C11  doub Y N 15  
A1BHB C11 C12  sing Y N 16  
A1BHB C12 N5   doub Y N 17  
A1BHB N5  C13  sing Y N 18  
A1BHB C13 C14  doub Y N 19  
A1BHB C14 C15  sing Y N 20  
A1BHB C15 C16  doub Y N 21  
A1BHB C2  C4   doub Y N 22  
A1BHB C8  C16  sing Y N 23  
A1BHB N3  C7   sing N N 24  
A1BHB C12 C16  sing Y N 25  
A1BHB N1  H1   sing N N 26  
A1BHB C5  H3   sing N N 27  
A1BHB C5  H4   sing N N 28  
A1BHB C6  H6   sing N N 29  
A1BHB C6  H7   sing N N 30  
A1BHB C7  H8   sing N N 31  
A1BHB C7  H9   sing N N 32  
A1BHB C10 H11  sing N N 33  
A1BHB C13 H13  sing N N 34  
A1BHB C15 H15  sing N N 35  
A1BHB C3  H2   sing N N 36  
A1BHB N4  H5   sing N N 37  
A1BHB C9  H10  sing N N 38  
A1BHB C11 H12  sing N N 39  
A1BHB C14 H14  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
SO4   S   O1   doub N N 339 
SO4   S   O2   doub N N 340 
SO4   S   O3   sing N N 341 
SO4   S   O4   sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002322 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HP3 
_atom_sites.fract_transf_matrix[1][1]   0.023585 
_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]   0.023585 
_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]   0.004621 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -20.736 19.087  -7.570  1.00 81.38  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.046 18.379  -7.544  1.00 79.53  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.309 17.749  -8.930  1.00 75.94  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.447 18.467  -9.956  1.00 76.76  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.153 19.296  -7.023  1.00 83.17  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.515 18.633  -6.870  1.00 86.03  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.950 18.391  -5.706  1.00 87.50  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.166 18.405  -7.913  1.00 88.98  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.392 16.426  -8.931  1.00 67.96  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.378 15.570  -10.126 1.00 63.73  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.798 15.354  -10.632 1.00 60.32  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.732 15.347  -9.817  1.00 58.17  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.748 14.230  -9.785  1.00 61.39  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.426 14.406  -9.205  1.00 62.56  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.621 12.838  -9.179  1.00 63.44  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.934 13.425  -9.002  1.00 63.00  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.955 15.244  -11.956 1.00 57.58  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.285 15.011  -12.574 1.00 56.77  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.079 14.035  -13.701 1.00 54.17  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.934 13.869  -14.171 1.00 50.95  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.961 16.307  -13.023 1.00 60.61  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.145 17.100  -14.006 1.00 64.68  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.143 17.943  -13.560 1.00 65.93  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.355 16.995  -15.389 1.00 66.47  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.369 18.668  -14.458 1.00 69.60  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.610 17.741  -16.292 1.00 67.29  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.596 18.563  -15.823 1.00 69.23  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.799 19.282  -16.667 1.00 70.68  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.169 13.375  -14.071 1.00 54.00  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.146 12.391  -15.179 1.00 52.38  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.947 12.892  -16.406 1.00 53.64  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.987 13.562  -16.232 1.00 54.62  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.630 11.024  -14.696 1.00 51.89  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.022 11.068  -14.093 1.00 53.60  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.609 10.392  -13.763 1.00 51.80  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.629 9.697   -14.082 1.00 54.70  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.512 12.457  -17.600 1.00 54.03  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.128 12.774  -18.941 1.00 56.15  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.181 11.488  -19.775 1.00 53.17  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.151 10.804  -19.875 1.00 50.55  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.272 13.762  -19.737 1.00 58.82  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.347 15.211  -19.320 1.00 61.39  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.361 16.099  -20.079 1.00 64.61  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.491 15.562  -20.820 1.00 66.97  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.423 17.328  -19.908 1.00 68.40  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.332 11.102  -20.314 1.00 54.89  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.418 9.840   -21.112 1.00 55.22  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.525 9.987   -22.343 1.00 55.95  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.422 11.117  -22.875 1.00 58.93  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.871 9.554   -21.470 1.00 58.28  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.115 8.150   -22.003 1.00 60.83  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.611 7.871   -22.221 1.00 64.72  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.780 6.430   -22.332 1.00 66.20  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.560 5.744   -23.455 1.00 67.70  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.225 6.392   -24.553 1.00 71.84  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.621 4.421   -23.480 1.00 65.38  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.880 8.904   -22.764 1.00 55.67  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.891 8.863   -23.880 1.00 57.30  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.161 7.725   -24.865 1.00 58.15  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.379 7.648   -25.836 1.00 60.58  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.466 8.724   -23.379 1.00 56.16  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.152 6.858   -24.640 1.00 57.09  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.439 5.780   -25.597 1.00 56.87  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.148 4.616   -24.982 1.00 58.58  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.263 4.579   -23.662 1.00 54.99  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.514 3.668   -25.855 1.00 58.98  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.096 2.355   -25.497 1.00 60.84  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -27.955 1.378   -25.331 1.00 62.58  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.860 1.641   -25.870 1.00 64.72  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.064 1.786   -26.529 1.00 62.49  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.287 2.642   -26.700 1.00 65.97  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.314 3.729   -26.082 1.00 65.67  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.192 2.243   -27.481 1.00 70.65  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.196 0.319   -24.553 1.00 61.59  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.195 -0.754  -24.420 1.00 60.41  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.649 -1.869  -25.349 1.00 62.29  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.605 -2.612  -25.029 1.00 62.37  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.055 -1.145  -22.961 1.00 60.24  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.559 0.064   -22.167 1.00 59.76  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.166 -2.364  -22.817 1.00 60.09  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.686 -0.119  -20.679 1.00 59.59  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.988 -1.942  -26.509 0.25 63.70  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.969 -1.986  -26.491 0.25 62.95  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.988 -1.942  -26.509 0.25 63.70  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.969 -1.986  -26.491 0.25 62.95  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.302 -2.851  -27.638 0.25 64.79  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.333 -2.887  -27.610 0.25 63.63  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.302 -2.851  -27.638 0.25 64.79  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.333 -2.887  -27.610 0.25 63.63  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.987 -3.344  -28.240 0.25 65.00  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.042 -3.331  -28.298 0.25 64.65  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.987 -3.344  -28.240 0.25 65.00  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.042 -3.331  -28.298 0.25 64.65  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.046 -2.525  -28.365 0.25 65.04  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.172 -2.462  -28.538 0.25 65.13  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.046 -2.525  -28.365 0.25 65.04  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.172 -2.462  -28.538 0.25 65.13  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.168 -2.150  -28.696 0.25 67.58  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.320 -2.188  -28.559 0.25 65.72  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.168 -2.150  -28.696 0.25 67.58  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.320 -2.188  -28.559 0.25 65.72  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.362 -1.192  -29.387 0.25 68.47  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.572 -2.021  -27.893 0.25 64.45  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.362 -1.192  -29.387 0.25 68.47  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.572 -2.021  -27.893 0.25 64.45  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.391 -1.481  -28.103 0.25 67.23  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.562 -2.947  -29.844 0.25 67.47  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.391 -1.481  -28.103 0.25 67.23  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.562 -2.947  -29.844 0.25 67.47  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.928 -4.632  -28.582 1.00 64.72  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.859 -5.181  -29.442 1.00 67.97  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.089 -4.620  -30.857 1.00 74.56  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.257 -4.540  -31.259 1.00 76.65  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.943 -6.698  -29.419 1.00 67.07  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.861 -7.330  -30.218 1.00 67.01  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.858 -7.586  -31.566 1.00 72.79  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.619 -7.818  -29.697 1.00 67.27  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.672 -8.171  -31.913 1.00 71.61  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.902 -8.340  -30.788 1.00 69.06  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -22.022 -7.807  -28.424 1.00 62.64  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.630 -8.878  -30.635 1.00 69.36  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.776 -8.360  -28.282 1.00 64.11  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.089 -8.886  -29.373 1.00 66.35  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -24.039 -4.146  -31.530 1.00 79.59  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -24.122 -3.525  -32.871 1.00 88.89  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.310 -4.379  -33.833 1.00 90.04  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -22.084 -4.478  -33.618 1.00 87.45  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -23.620 -2.085  -32.838 1.00 93.92  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -24.530 -1.163  -32.031 1.00 97.35  ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -25.912 -0.861  -32.612 1.00 105.34 ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -25.997 -0.274  -33.743 1.00 111.25 ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -26.915 -1.196  -31.928 1.00 104.65 ? 62  GLU   A OE2 1 
ATOM   133  N N   . LYS   A 1 20  ? -23.991 -5.017  -34.795 1.00 95.91  ? 63  LYS   A N   1 
ATOM   134  C CA  . LYS   A 1 20  ? -23.352 -5.889  -35.823 1.00 97.69  ? 63  LYS   A CA  1 
ATOM   135  C C   . LYS   A 1 20  ? -22.391 -5.018  -36.621 1.00 95.31  ? 63  LYS   A C   1 
ATOM   136  O O   . LYS   A 1 20  ? -22.785 -3.875  -36.950 1.00 98.87  ? 63  LYS   A O   1 
ATOM   137  C CB  . LYS   A 1 20  ? -24.396 -6.522  -36.742 1.00 103.37 ? 63  LYS   A CB  1 
ATOM   138  C CG  . LYS   A 1 20  ? -25.068 -7.776  -36.202 1.00 106.91 ? 63  LYS   A CG  1 
ATOM   139  C CD  . LYS   A 1 20  ? -26.350 -8.116  -36.953 1.00 111.47 ? 63  LYS   A CD  1 
ATOM   140  C CE  . LYS   A 1 20  ? -27.161 -9.233  -36.330 1.00 113.09 ? 63  LYS   A CE  1 
ATOM   141  N NZ  . LYS   A 1 20  ? -28.603 -8.895  -36.303 1.00 114.93 ? 63  LYS   A NZ  1 
ATOM   142  N N   . ASP   A 1 21  ? -21.186 -5.515  -36.895 1.00 94.46  ? 64  ASP   A N   1 
ATOM   143  C CA  . ASP   A 1 21  ? -20.168 -4.749  -37.661 1.00 100.39 ? 64  ASP   A CA  1 
ATOM   144  C C   . ASP   A 1 21  ? -19.853 -3.451  -36.891 1.00 95.87  ? 64  ASP   A C   1 
ATOM   145  O O   . ASP   A 1 21  ? -20.009 -2.369  -37.464 1.00 94.25  ? 64  ASP   A O   1 
ATOM   146  C CB  . ASP   A 1 21  ? -20.626 -4.467  -39.110 1.00 111.32 ? 64  ASP   A CB  1 
ATOM   147  C CG  . ASP   A 1 21  ? -20.880 -5.690  -39.993 1.00 118.58 ? 64  ASP   A CG  1 
ATOM   148  O OD1 . ASP   A 1 21  ? -19.885 -6.377  -40.374 1.00 122.88 ? 64  ASP   A OD1 1 
ATOM   149  O OD2 . ASP   A 1 21  ? -22.071 -5.937  -40.320 1.00 122.24 ? 64  ASP   A OD2 1 
ATOM   150  N N   . ALA   A 1 22  ? -19.450 -3.550  -35.608 1.00 91.67  ? 65  ALA   A N   1 
ATOM   151  C CA  . ALA   A 1 22  ? -18.638 -2.502  -34.940 1.00 85.62  ? 65  ALA   A CA  1 
ATOM   152  C C   . ALA   A 1 22  ? -17.148 -2.778  -35.294 1.00 84.90  ? 65  ALA   A C   1 
ATOM   153  O O   . ALA   A 1 22  ? -16.813 -3.976  -35.793 1.00 85.73  ? 65  ALA   A O   1 
ATOM   154  C CB  . ALA   A 1 22  ? -18.861 -2.508  -33.458 1.00 84.53  ? 65  ALA   A CB  1 
ATOM   155  N N   . GLU   A 1 23  ? -16.348 -1.665  -35.234 1.00 85.49  ? 66  GLU   A N   1 
ATOM   156  C CA  . GLU   A 1 23  ? -14.854 -1.663  -35.231 1.00 84.98  ? 66  GLU   A CA  1 
ATOM   157  C C   . GLU   A 1 23  ? -14.392 -2.824  -34.342 1.00 80.79  ? 66  GLU   A C   1 
ATOM   158  O O   . GLU   A 1 23  ? -14.834 -2.903  -33.162 1.00 69.49  ? 66  GLU   A O   1 
ATOM   159  C CB  . GLU   A 1 23  ? -14.387 -0.328  -34.640 1.00 88.39  ? 66  GLU   A CB  1 
ATOM   160  C CG  . GLU   A 1 23  ? -12.926 0.054   -34.832 1.00 92.15  ? 66  GLU   A CG  1 
ATOM   161  C CD  . GLU   A 1 23  ? -12.814 1.571   -34.671 1.00 97.24  ? 66  GLU   A CD  1 
ATOM   162  O OE1 . GLU   A 1 23  ? -12.657 2.284   -35.695 1.00 107.69 ? 66  GLU   A OE1 1 
ATOM   163  O OE2 . GLU   A 1 23  ? -12.995 2.060   -33.546 1.00 97.82  ? 66  GLU   A OE2 1 
ATOM   164  N N   . VAL   A 1 24  ? -13.606 -3.744  -34.886 1.00 79.60  ? 67  VAL   A N   1 
ATOM   165  C CA  . VAL   A 1 24  ? -13.089 -4.906  -34.116 1.00 79.38  ? 67  VAL   A CA  1 
ATOM   166  C C   . VAL   A 1 24  ? -11.608 -4.586  -33.923 1.00 80.41  ? 67  VAL   A C   1 
ATOM   167  O O   . VAL   A 1 24  ? -10.941 -4.396  -34.894 1.00 81.77  ? 67  VAL   A O   1 
ATOM   168  C CB  . VAL   A 1 24  ? -13.399 -6.209  -34.878 1.00 79.50  ? 67  VAL   A CB  1 
ATOM   169  C CG1 . VAL   A 1 24  ? -12.980 -7.424  -34.101 1.00 74.57  ? 67  VAL   A CG1 1 
ATOM   170  C CG2 . VAL   A 1 24  ? -14.885 -6.296  -35.240 1.00 79.13  ? 67  VAL   A CG2 1 
ATOM   171  N N   A THR   A 1 25  ? -11.143 -4.453  -32.672 0.23 77.48  ? 68  THR   A N   1 
ATOM   172  N N   B THR   A 1 25  ? -11.143 -4.453  -32.671 0.25 77.48  ? 68  THR   A N   1 
ATOM   173  N N   C THR   A 1 25  ? -11.143 -4.504  -32.671 0.25 77.39  ? 68  THR   A N   1 
ATOM   174  N N   D THR   A 1 25  ? -11.143 -4.504  -32.671 0.25 77.39  ? 68  THR   A N   1 
ATOM   175  C CA  A THR   A 1 25  ? -9.766  -3.968  -32.363 0.23 78.16  ? 68  THR   A CA  1 
ATOM   176  C CA  B THR   A 1 25  ? -9.766  -3.967  -32.363 0.25 78.16  ? 68  THR   A CA  1 
ATOM   177  C CA  C THR   A 1 25  ? -9.734  -4.153  -32.346 0.25 77.89  ? 68  THR   A CA  1 
ATOM   178  C CA  D THR   A 1 25  ? -9.734  -4.153  -32.346 0.25 77.89  ? 68  THR   A CA  1 
ATOM   179  C C   A THR   A 1 25  ? -9.324  -4.399  -30.961 0.23 75.06  ? 68  THR   A C   1 
ATOM   180  C C   B THR   A 1 25  ? -9.324  -4.399  -30.960 0.25 75.06  ? 68  THR   A C   1 
ATOM   181  C C   C THR   A 1 25  ? -9.412  -4.570  -30.911 0.25 74.43  ? 68  THR   A C   1 
ATOM   182  C C   D THR   A 1 25  ? -9.412  -4.570  -30.911 0.25 74.43  ? 68  THR   A C   1 
ATOM   183  O O   A THR   A 1 25  ? -10.126 -5.035  -30.246 0.23 72.13  ? 68  THR   A O   1 
ATOM   184  O O   B THR   A 1 25  ? -10.125 -5.035  -30.246 0.25 72.13  ? 68  THR   A O   1 
ATOM   185  O O   C THR   A 1 25  ? -10.301 -5.131  -30.243 0.25 71.53  ? 68  THR   A O   1 
ATOM   186  O O   D THR   A 1 25  ? -10.301 -5.131  -30.243 0.25 71.53  ? 68  THR   A O   1 
ATOM   187  C CB  A THR   A 1 25  ? -9.678  -2.444  -32.536 0.23 79.60  ? 68  THR   A CB  1 
ATOM   188  C CB  B THR   A 1 25  ? -9.679  -2.444  -32.536 0.25 79.61  ? 68  THR   A CB  1 
ATOM   189  C CB  C THR   A 1 25  ? -9.478  -2.656  -32.568 0.25 79.71  ? 68  THR   A CB  1 
ATOM   190  C CB  D THR   A 1 25  ? -9.478  -2.656  -32.568 0.25 79.71  ? 68  THR   A CB  1 
ATOM   191  O OG1 A THR   A 1 25  ? -8.315  -2.032  -32.440 0.23 81.65  ? 68  THR   A OG1 1 
ATOM   192  O OG1 B THR   A 1 25  ? -8.316  -2.031  -32.440 0.25 81.65  ? 68  THR   A OG1 1 
ATOM   193  O OG1 C THR   A 1 25  ? -8.065  -2.455  -32.616 0.25 81.88  ? 68  THR   A OG1 1 
ATOM   194  O OG1 D THR   A 1 25  ? -8.065  -2.455  -32.616 0.25 81.88  ? 68  THR   A OG1 1 
ATOM   195  C CG2 A THR   A 1 25  ? -10.500 -1.687  -31.520 0.23 76.30  ? 68  THR   A CG2 1 
ATOM   196  C CG2 B THR   A 1 25  ? -10.501 -1.687  -31.520 0.25 76.30  ? 68  THR   A CG2 1 
ATOM   197  C CG2 C THR   A 1 25  ? -10.105 -1.787  -31.501 0.25 76.54  ? 68  THR   A CG2 1 
ATOM   198  C CG2 D THR   A 1 25  ? -10.105 -1.787  -31.501 0.25 76.54  ? 68  THR   A CG2 1 
ATOM   199  N N   A GLY   A 1 26  ? -8.080  -4.063  -30.603 0.23 75.51  ? 69  GLY   A N   1 
ATOM   200  N N   B GLY   A 1 26  ? -8.080  -4.062  -30.603 0.25 75.49  ? 69  GLY   A N   1 
ATOM   201  N N   C GLY   A 1 26  ? -8.174  -4.323  -30.477 0.25 74.40  ? 69  GLY   A N   1 
ATOM   202  N N   D GLY   A 1 26  ? -8.174  -4.323  -30.477 0.25 74.40  ? 69  GLY   A N   1 
ATOM   203  C CA  A GLY   A 1 26  ? -7.417  -4.484  -29.355 0.23 74.52  ? 69  GLY   A CA  1 
ATOM   204  C CA  B GLY   A 1 26  ? -7.416  -4.484  -29.356 0.25 74.52  ? 69  GLY   A CA  1 
ATOM   205  C CA  C GLY   A 1 26  ? -7.685  -4.692  -29.137 0.25 72.87  ? 69  GLY   A CA  1 
ATOM   206  C CA  D GLY   A 1 26  ? -7.685  -4.692  -29.137 0.25 72.87  ? 69  GLY   A CA  1 
ATOM   207  C C   A GLY   A 1 26  ? -6.985  -5.939  -29.406 0.23 74.39  ? 69  GLY   A C   1 
ATOM   208  C C   B GLY   A 1 26  ? -6.985  -5.938  -29.407 0.25 74.38  ? 69  GLY   A C   1 
ATOM   209  C C   C GLY   A 1 26  ? -7.177  -6.123  -29.083 0.25 72.31  ? 69  GLY   A C   1 
ATOM   210  C C   D GLY   A 1 26  ? -7.177  -6.123  -29.083 0.25 72.31  ? 69  GLY   A C   1 
ATOM   211  O O   A GLY   A 1 26  ? -7.564  -6.705  -30.201 0.23 75.59  ? 69  GLY   A O   1 
ATOM   212  O O   B GLY   A 1 26  ? -7.564  -6.705  -30.200 0.25 75.59  ? 69  GLY   A O   1 
ATOM   213  O O   C GLY   A 1 26  ? -7.916  -7.049  -29.499 0.25 72.08  ? 69  GLY   A O   1 
ATOM   214  O O   D GLY   A 1 26  ? -7.916  -7.049  -29.499 0.25 72.08  ? 69  GLY   A O   1 
ATOM   215  N N   A ASN   A 1 27  ? -6.011  -6.304  -28.570 0.23 74.76  ? 70  ASN   A N   1 
ATOM   216  N N   B ASN   A 1 27  ? -6.010  -6.304  -28.571 0.25 74.76  ? 70  ASN   A N   1 
ATOM   217  N N   C ASN   A 1 27  ? -5.959  -6.288  -28.560 0.25 73.17  ? 70  ASN   A N   1 
ATOM   218  N N   D ASN   A 1 27  ? -5.959  -6.288  -28.560 0.25 73.17  ? 70  ASN   A N   1 
ATOM   219  C CA  A ASN   A 1 27  ? -5.494  -7.694  -28.420 0.23 75.90  ? 70  ASN   A CA  1 
ATOM   220  C CA  B ASN   A 1 27  ? -5.493  -7.694  -28.420 0.25 75.91  ? 70  ASN   A CA  1 
ATOM   221  C CA  C ASN   A 1 27  ? -5.321  -7.600  -28.268 0.25 73.97  ? 70  ASN   A CA  1 
ATOM   222  C CA  D ASN   A 1 27  ? -5.321  -7.600  -28.268 0.25 73.97  ? 70  ASN   A CA  1 
ATOM   223  C C   A ASN   A 1 27  ? -6.070  -8.299  -27.127 0.23 71.35  ? 70  ASN   A C   1 
ATOM   224  C C   B ASN   A 1 27  ? -6.069  -8.299  -27.127 0.25 71.34  ? 70  ASN   A C   1 
ATOM   225  C C   C ASN   A 1 27  ? -6.071  -8.302  -27.128 0.25 70.22  ? 70  ASN   A C   1 
ATOM   226  C C   D ASN   A 1 27  ? -6.071  -8.302  -27.128 0.25 70.22  ? 70  ASN   A C   1 
ATOM   227  O O   A ASN   A 1 27  ? -6.989  -7.677  -26.565 0.23 69.18  ? 70  ASN   A O   1 
ATOM   228  O O   B ASN   A 1 27  ? -6.990  -7.677  -26.566 0.25 69.18  ? 70  ASN   A O   1 
ATOM   229  O O   C ASN   A 1 27  ? -7.099  -7.755  -26.687 0.25 68.08  ? 70  ASN   A O   1 
ATOM   230  O O   D ASN   A 1 27  ? -7.099  -7.755  -26.687 0.25 68.08  ? 70  ASN   A O   1 
ATOM   231  C CB  A ASN   A 1 27  ? -3.964  -7.720  -28.539 0.23 80.10  ? 70  ASN   A CB  1 
ATOM   232  C CB  B ASN   A 1 27  ? -3.963  -7.720  -28.539 0.25 80.12  ? 70  ASN   A CB  1 
ATOM   233  C CB  C ASN   A 1 27  ? -3.836  -7.421  -27.949 0.25 76.55  ? 70  ASN   A CB  1 
ATOM   234  C CB  D ASN   A 1 27  ? -3.836  -7.421  -27.949 0.25 76.55  ? 70  ASN   A CB  1 
ATOM   235  C CG  A ASN   A 1 27  ? -3.274  -6.685  -27.675 0.23 81.12  ? 70  ASN   A CG  1 
ATOM   236  C CG  B ASN   A 1 27  ? -3.274  -6.685  -27.675 0.25 81.14  ? 70  ASN   A CG  1 
ATOM   237  C CG  C ASN   A 1 27  ? -3.588  -6.470  -26.800 0.25 75.00  ? 70  ASN   A CG  1 
ATOM   238  C CG  D ASN   A 1 27  ? -3.588  -6.470  -26.800 0.25 75.00  ? 70  ASN   A CG  1 
ATOM   239  O OD1 A ASN   A 1 27  ? -3.535  -5.491  -27.809 0.23 83.26  ? 70  ASN   A OD1 1 
ATOM   240  O OD1 B ASN   A 1 27  ? -3.535  -5.491  -27.810 0.25 83.31  ? 70  ASN   A OD1 1 
ATOM   241  O OD1 C ASN   A 1 27  ? -4.138  -5.372  -26.763 0.25 75.32  ? 70  ASN   A OD1 1 
ATOM   242  O OD1 D ASN   A 1 27  ? -4.138  -5.372  -26.763 0.25 75.32  ? 70  ASN   A OD1 1 
ATOM   243  N ND2 A ASN   A 1 27  ? -2.381  -7.124  -26.802 0.23 81.04  ? 70  ASN   A ND2 1 
ATOM   244  N ND2 B ASN   A 1 27  ? -2.381  -7.125  -26.802 0.25 81.06  ? 70  ASN   A ND2 1 
ATOM   245  N ND2 C ASN   A 1 27  ? -2.740  -6.873  -25.870 0.25 75.84  ? 70  ASN   A ND2 1 
ATOM   246  N ND2 D ASN   A 1 27  ? -2.740  -6.873  -25.870 0.25 75.84  ? 70  ASN   A ND2 1 
ATOM   247  N N   . SER   A 1 28  ? -5.587  -9.484  -26.716 1.00 70.36  ? 71  SER   A N   1 
ATOM   248  C CA  . SER   A 1 28  ? -6.157  -10.335 -25.622 1.00 69.70  ? 71  SER   A CA  1 
ATOM   249  C C   . SER   A 1 28  ? -5.025  -10.892 -24.764 1.00 70.45  ? 71  SER   A C   1 
ATOM   250  O O   . SER   A 1 28  ? -4.740  -12.089 -24.834 1.00 75.98  ? 71  SER   A O   1 
ATOM   251  C CB  . SER   A 1 28  ? -6.977  -11.529 -26.104 1.00 69.45  ? 71  SER   A CB  1 
ATOM   252  O OG  . SER   A 1 28  ? -7.887  -11.174 -27.139 1.00 76.13  ? 71  SER   A OG  1 
ATOM   253  N N   . PRO   A 1 29  ? -4.346  -10.055 -23.949 1.00 68.49  ? 72  PRO   A N   1 
ATOM   254  C CA  . PRO   A 1 29  ? -3.170  -10.493 -23.188 1.00 70.61  ? 72  PRO   A CA  1 
ATOM   255  C C   . PRO   A 1 29  ? -3.546  -11.243 -21.895 1.00 67.46  ? 72  PRO   A C   1 
ATOM   256  O O   . PRO   A 1 29  ? -4.603  -10.937 -21.314 1.00 62.14  ? 72  PRO   A O   1 
ATOM   257  C CB  . PRO   A 1 29  ? -2.457  -9.157  -22.902 1.00 71.63  ? 72  PRO   A CB  1 
ATOM   258  C CG  . PRO   A 1 29  ? -3.623  -8.176  -22.715 1.00 71.15  ? 72  PRO   A CG  1 
ATOM   259  C CD  . PRO   A 1 29  ? -4.690  -8.642  -23.700 1.00 68.79  ? 72  PRO   A CD  1 
ATOM   260  N N   . ARG   A 1 30  ? -2.713  -12.200 -21.492 1.00 70.33  ? 73  ARG   A N   1 
ATOM   261  C CA  . ARG   A 1 30  ? -2.795  -12.883 -20.169 1.00 73.02  ? 73  ARG   A CA  1 
ATOM   262  C C   . ARG   A 1 30  ? -1.758  -12.244 -19.240 1.00 70.56  ? 73  ARG   A C   1 
ATOM   263  O O   . ARG   A 1 30  ? -0.569  -12.474 -19.451 1.00 70.51  ? 73  ARG   A O   1 
ATOM   264  C CB  . ARG   A 1 30  ? -2.564  -14.397 -20.290 1.00 81.64  ? 73  ARG   A CB  1 
ATOM   265  C CG  . ARG   A 1 30  ? -3.601  -15.122 -21.147 1.00 88.85  ? 73  ARG   A CG  1 
ATOM   266  C CD  . ARG   A 1 30  ? -3.347  -16.620 -21.369 1.00 94.97  ? 73  ARG   A CD  1 
ATOM   267  N NE  . ARG   A 1 30  ? -4.129  -17.180 -22.489 1.00 102.21 ? 73  ARG   A NE  1 
ATOM   268  C CZ  . ARG   A 1 30  ? -5.385  -17.648 -22.411 1.00 102.15 ? 73  ARG   A CZ  1 
ATOM   269  N NH1 . ARG   A 1 30  ? -6.039  -17.643 -21.256 1.00 105.29 ? 73  ARG   A NH1 1 
ATOM   270  N NH2 . ARG   A 1 30  ? -5.987  -18.122 -23.490 1.00 91.72  ? 73  ARG   A NH2 1 
ATOM   271  N N   . LEU   A 1 31  ? -2.218  -11.471 -18.247 1.00 68.11  ? 74  LEU   A N   1 
ATOM   272  C CA  . LEU   A 1 31  ? -1.374  -10.708 -17.288 1.00 67.00  ? 74  LEU   A CA  1 
ATOM   273  C C   . LEU   A 1 31  ? -1.559  -11.266 -15.855 1.00 65.59  ? 74  LEU   A C   1 
ATOM   274  O O   . LEU   A 1 31  ? -2.730  -11.421 -15.423 1.00 61.40  ? 74  LEU   A O   1 
ATOM   275  C CB  . LEU   A 1 31  ? -1.798  -9.236  -17.358 1.00 66.19  ? 74  LEU   A CB  1 
ATOM   276  C CG  . LEU   A 1 31  ? -1.619  -8.511  -18.695 1.00 69.04  ? 74  LEU   A CG  1 
ATOM   277  C CD1 . LEU   A 1 31  ? -2.136  -7.080  -18.575 1.00 68.15  ? 74  LEU   A CD1 1 
ATOM   278  C CD2 . LEU   A 1 31  ? -0.157  -8.531  -19.169 1.00 71.77  ? 74  LEU   A CD2 1 
ATOM   279  N N   . ASP   A 1 32  ? -0.460  -11.462 -15.117 1.00 66.44  ? 75  ASP   A N   1 
ATOM   280  C CA  . ASP   A 1 32  ? -0.450  -11.688 -13.645 1.00 67.31  ? 75  ASP   A CA  1 
ATOM   281  C C   . ASP   A 1 32  ? -0.593  -10.368 -12.890 1.00 64.60  ? 75  ASP   A C   1 
ATOM   282  O O   . ASP   A 1 32  ? 0.360   -9.548  -12.934 1.00 67.73  ? 75  ASP   A O   1 
ATOM   283  C CB  . ASP   A 1 32  ? 0.861   -12.334 -13.208 1.00 73.06  ? 75  ASP   A CB  1 
ATOM   284  C CG  . ASP   A 1 32  ? 1.031   -13.748 -13.740 1.00 75.59  ? 75  ASP   A CG  1 
ATOM   285  O OD1 . ASP   A 1 32  ? 0.021   -14.492 -13.767 1.00 76.12  ? 75  ASP   A OD1 1 
ATOM   286  O OD2 . ASP   A 1 32  ? 2.167   -14.092 -14.111 1.00 78.83  ? 75  ASP   A OD2 1 
ATOM   287  N N   . VAL   A 1 33  ? -1.706  -10.194 -12.168 1.00 61.39  ? 76  VAL   A N   1 
ATOM   288  C CA  . VAL   A 1 33  ? -2.044  -8.919  -11.467 1.00 60.42  ? 76  VAL   A CA  1 
ATOM   289  C C   . VAL   A 1 33  ? -2.331  -9.200  -9.974  1.00 60.93  ? 76  VAL   A C   1 
ATOM   290  O O   . VAL   A 1 33  ? -2.637  -10.376 -9.584  1.00 59.15  ? 76  VAL   A O   1 
ATOM   291  C CB  . VAL   A 1 33  ? -3.201  -8.157  -12.160 1.00 58.31  ? 76  VAL   A CB  1 
ATOM   292  C CG1 . VAL   A 1 33  ? -2.925  -7.886  -13.634 1.00 58.24  ? 76  VAL   A CG1 1 
ATOM   293  C CG2 . VAL   A 1 33  ? -4.544  -8.855  -12.014 1.00 56.58  ? 76  VAL   A CG2 1 
ATOM   294  N N   . ALA   A 1 34  ? -2.178  -8.158  -9.153  1.00 61.29  ? 77  ALA   A N   1 
ATOM   295  C CA  . ALA   A 1 34  ? -2.534  -8.146  -7.715  1.00 61.38  ? 77  ALA   A CA  1 
ATOM   296  C C   . ALA   A 1 34  ? -3.558  -7.032  -7.537  1.00 59.60  ? 77  ALA   A C   1 
ATOM   297  O O   . ALA   A 1 34  ? -3.465  -6.049  -8.289  1.00 58.36  ? 77  ALA   A O   1 
ATOM   298  C CB  . ALA   A 1 34  ? -1.318  -7.963  -6.824  1.00 63.25  ? 77  ALA   A CB  1 
ATOM   299  N N   . LEU   A 1 35  ? -4.507  -7.221  -6.612  1.00 57.60  ? 78  LEU   A N   1 
ATOM   300  C CA  . LEU   A 1 35  ? -5.530  -6.211  -6.284  1.00 56.23  ? 78  LEU   A CA  1 
ATOM   301  C C   . LEU   A 1 35  ? -5.396  -5.845  -4.805  1.00 58.35  ? 78  LEU   A C   1 
ATOM   302  O O   . LEU   A 1 35  ? -5.521  -6.764  -3.905  1.00 59.13  ? 78  LEU   A O   1 
ATOM   303  C CB  . LEU   A 1 35  ? -6.910  -6.763  -6.626  1.00 54.52  ? 78  LEU   A CB  1 
ATOM   304  C CG  . LEU   A 1 35  ? -8.084  -5.839  -6.314  1.00 53.08  ? 78  LEU   A CG  1 
ATOM   305  C CD1 . LEU   A 1 35  ? -8.123  -4.601  -7.166  1.00 51.99  ? 78  LEU   A CD1 1 
ATOM   306  C CD2 . LEU   A 1 35  ? -9.379  -6.594  -6.491  1.00 54.04  ? 78  LEU   A CD2 1 
ATOM   307  N N   . ASP   A 1 36  ? -5.113  -4.562  -4.574  1.00 57.85  ? 79  ASP   A N   1 
ATOM   308  C CA  . ASP   A 1 36  ? -4.773  -4.025  -3.242  1.00 58.31  ? 79  ASP   A CA  1 
ATOM   309  C C   . ASP   A 1 36  ? -6.081  -3.561  -2.601  1.00 58.21  ? 79  ASP   A C   1 
ATOM   310  O O   . ASP   A 1 36  ? -7.157  -3.499  -3.297  1.00 55.02  ? 79  ASP   A O   1 
ATOM   311  C CB  . ASP   A 1 36  ? -3.663  -2.969  -3.334  1.00 59.45  ? 79  ASP   A CB  1 
ATOM   312  C CG  . ASP   A 1 36  ? -4.082  -1.548  -3.701  1.00 58.11  ? 79  ASP   A CG  1 
ATOM   313  O OD1 . ASP   A 1 36  ? -5.289  -1.306  -3.970  1.00 54.72  ? 79  ASP   A OD1 1 
ATOM   314  O OD2 . ASP   A 1 36  ? -3.177  -0.679  -3.716  1.00 60.76  ? 79  ASP   A OD2 1 
ATOM   315  N N   . GLU   A 1 37  ? -5.986  -3.195  -1.324  1.00 60.57  ? 80  GLU   A N   1 
ATOM   316  C CA  . GLU   A 1 37  ? -7.164  -2.874  -0.497  1.00 60.82  ? 80  GLU   A CA  1 
ATOM   317  C C   . GLU   A 1 37  ? -7.828  -1.569  -0.982  1.00 58.32  ? 80  GLU   A C   1 
ATOM   318  O O   . GLU   A 1 37  ? -9.023  -1.368  -0.692  1.00 57.02  ? 80  GLU   A O   1 
ATOM   319  C CB  . GLU   A 1 37  ? -6.737  -2.866  0.970   1.00 63.83  ? 80  GLU   A CB  1 
ATOM   320  C CG  . GLU   A 1 37  ? -7.906  -2.936  1.929   1.00 66.20  ? 80  GLU   A CG  1 
ATOM   321  C CD  . GLU   A 1 37  ? -7.528  -2.666  3.398   1.00 69.98  ? 80  GLU   A CD  1 
ATOM   322  O OE1 . GLU   A 1 37  ? -7.193  -1.486  3.744   1.00 69.63  ? 80  GLU   A OE1 1 
ATOM   323  O OE2 . GLU   A 1 37  ? -7.506  -3.637  4.190   1.00 71.85  ? 80  GLU   A OE2 1 
ATOM   324  N N   A SER   A 1 38  ? -7.093  -0.712  -1.704  0.23 58.10  ? 81  SER   A N   1 
ATOM   325  N N   B SER   A 1 38  ? -7.093  -0.712  -1.704  0.25 58.09  ? 81  SER   A N   1 
ATOM   326  N N   C SER   A 1 38  ? -7.071  -0.719  -1.687  0.25 58.26  ? 81  SER   A N   1 
ATOM   327  N N   D SER   A 1 38  ? -7.071  -0.719  -1.687  0.27 58.26  ? 81  SER   A N   1 
ATOM   328  C CA  A SER   A 1 38  ? -7.639  0.546   -2.280  0.23 57.59  ? 81  SER   A CA  1 
ATOM   329  C CA  B SER   A 1 38  ? -7.639  0.546   -2.280  0.25 57.59  ? 81  SER   A CA  1 
ATOM   330  C CA  C SER   A 1 38  ? -7.565  0.573   -2.227  0.25 57.98  ? 81  SER   A CA  1 
ATOM   331  C CA  D SER   A 1 38  ? -7.565  0.572   -2.226  0.27 57.97  ? 81  SER   A CA  1 
ATOM   332  C C   A SER   A 1 38  ? -8.251  0.288   -3.669  0.23 55.61  ? 81  SER   A C   1 
ATOM   333  C C   B SER   A 1 38  ? -8.251  0.287   -3.669  0.25 55.61  ? 81  SER   A C   1 
ATOM   334  C C   C SER   A 1 38  ? -8.162  0.382   -3.630  0.25 56.08  ? 81  SER   A C   1 
ATOM   335  C C   D SER   A 1 38  ? -8.162  0.381   -3.630  0.27 56.08  ? 81  SER   A C   1 
ATOM   336  O O   A SER   A 1 38  ? -8.658  1.266   -4.319  0.23 55.63  ? 81  SER   A O   1 
ATOM   337  O O   B SER   A 1 38  ? -8.657  1.265   -4.319  0.25 55.64  ? 81  SER   A O   1 
ATOM   338  O O   C SER   A 1 38  ? -8.449  1.401   -4.280  0.25 56.41  ? 81  SER   A O   1 
ATOM   339  O O   D SER   A 1 38  ? -8.448  1.401   -4.280  0.27 56.42  ? 81  SER   A O   1 
ATOM   340  C CB  A SER   A 1 38  ? -6.591  1.620   -2.348  0.23 59.64  ? 81  SER   A CB  1 
ATOM   341  C CB  B SER   A 1 38  ? -6.592  1.620   -2.348  0.25 59.65  ? 81  SER   A CB  1 
ATOM   342  C CB  C SER   A 1 38  ? -6.469  1.596   -2.246  0.25 60.23  ? 81  SER   A CB  1 
ATOM   343  C CB  D SER   A 1 38  ? -6.469  1.596   -2.245  0.27 60.23  ? 81  SER   A CB  1 
ATOM   344  O OG  A SER   A 1 38  ? -5.565  1.394   -1.399  0.23 62.93  ? 81  SER   A OG  1 
ATOM   345  O OG  B SER   A 1 38  ? -5.564  1.393   -1.400  0.25 62.94  ? 81  SER   A OG  1 
ATOM   346  O OG  C SER   A 1 38  ? -5.772  1.621   -1.012  0.25 63.79  ? 81  SER   A OG  1 
ATOM   347  O OG  D SER   A 1 38  ? -5.772  1.621   -1.012  0.27 63.81  ? 81  SER   A OG  1 
ATOM   348  N N   A GLY   A 1 39  ? -8.318  -0.971  -4.116  0.23 54.40  ? 82  GLY   A N   1 
ATOM   349  N N   B GLY   A 1 39  ? -8.318  -0.972  -4.116  0.25 54.40  ? 82  GLY   A N   1 
ATOM   350  N N   C GLY   A 1 39  ? -8.342  -0.865  -4.083  0.25 54.69  ? 82  GLY   A N   1 
ATOM   351  N N   D GLY   A 1 39  ? -8.342  -0.865  -4.083  0.27 54.69  ? 82  GLY   A N   1 
ATOM   352  C CA  A GLY   A 1 39  ? -8.959  -1.349  -5.392  0.23 52.46  ? 82  GLY   A CA  1 
ATOM   353  C CA  B GLY   A 1 39  ? -8.959  -1.349  -5.392  0.25 52.47  ? 82  GLY   A CA  1 
ATOM   354  C CA  C GLY   A 1 39  ? -8.984  -1.183  -5.374  0.25 52.71  ? 82  GLY   A CA  1 
ATOM   355  C CA  D GLY   A 1 39  ? -8.984  -1.183  -5.374  0.27 52.71  ? 82  GLY   A CA  1 
ATOM   356  C C   A GLY   A 1 39  ? -8.076  -1.076  -6.611  0.23 52.34  ? 82  GLY   A C   1 
ATOM   357  C C   B GLY   A 1 39  ? -8.076  -1.076  -6.611  0.25 52.34  ? 82  GLY   A C   1 
ATOM   358  C C   C GLY   A 1 39  ? -8.103  -0.827  -6.570  0.25 52.63  ? 82  GLY   A C   1 
ATOM   359  C C   D GLY   A 1 39  ? -8.103  -0.826  -6.570  0.27 52.63  ? 82  GLY   A C   1 
ATOM   360  O O   A GLY   A 1 39  ? -8.622  -1.096  -7.718  0.23 50.84  ? 82  GLY   A O   1 
ATOM   361  O O   B GLY   A 1 39  ? -8.622  -1.095  -7.717  0.25 50.84  ? 82  GLY   A O   1 
ATOM   362  O O   C GLY   A 1 39  ? -8.667  -0.467  -7.606  0.25 51.10  ? 82  GLY   A O   1 
ATOM   363  O O   D GLY   A 1 39  ? -8.667  -0.466  -7.606  0.27 51.10  ? 82  GLY   A O   1 
ATOM   364  N N   A ASP   A 1 40  ? -6.772  -0.845  -6.415  0.23 54.21  ? 83  ASP   A N   1 
ATOM   365  N N   B ASP   A 1 40  ? -6.771  -0.844  -6.416  0.25 54.21  ? 83  ASP   A N   1 
ATOM   366  N N   C ASP   A 1 40  ? -6.778  -0.923  -6.426  0.25 54.46  ? 83  ASP   A N   1 
ATOM   367  N N   D ASP   A 1 40  ? -6.778  -0.923  -6.426  0.27 54.45  ? 83  ASP   A N   1 
ATOM   368  C CA  A ASP   A 1 40  ? -5.775  -0.592  -7.492  0.23 55.46  ? 83  ASP   A CA  1 
ATOM   369  C CA  B ASP   A 1 40  ? -5.775  -0.591  -7.492  0.25 55.47  ? 83  ASP   A CA  1 
ATOM   370  C CA  C ASP   A 1 40  ? -5.787  -0.601  -7.487  0.25 55.81  ? 83  ASP   A CA  1 
ATOM   371  C CA  D ASP   A 1 40  ? -5.787  -0.601  -7.486  0.27 55.82  ? 83  ASP   A CA  1 
ATOM   372  C C   A ASP   A 1 40  ? -5.121  -1.916  -7.899  0.23 55.38  ? 83  ASP   A C   1 
ATOM   373  C C   B ASP   A 1 40  ? -5.121  -1.916  -7.899  0.25 55.39  ? 83  ASP   A C   1 
ATOM   374  C C   C ASP   A 1 40  ? -5.080  -1.892  -7.911  0.25 55.66  ? 83  ASP   A C   1 
ATOM   375  C C   D ASP   A 1 40  ? -5.080  -1.893  -7.911  0.27 55.66  ? 83  ASP   A C   1 
ATOM   376  O O   A ASP   A 1 40  ? -4.520  -2.578  -7.017  0.23 57.02  ? 83  ASP   A O   1 
ATOM   377  O O   B ASP   A 1 40  ? -4.520  -2.578  -7.017  0.25 57.03  ? 83  ASP   A O   1 
ATOM   378  O O   C ASP   A 1 40  ? -4.409  -2.513  -7.049  0.25 57.40  ? 83  ASP   A O   1 
ATOM   379  O O   D ASP   A 1 40  ? -4.408  -2.513  -7.049  0.27 57.41  ? 83  ASP   A O   1 
ATOM   380  C CB  A ASP   A 1 40  ? -4.718  0.427   -7.054  0.23 58.05  ? 83  ASP   A CB  1 
ATOM   381  C CB  B ASP   A 1 40  ? -4.717  0.427   -7.054  0.25 58.05  ? 83  ASP   A CB  1 
ATOM   382  C CB  C ASP   A 1 40  ? -4.813  0.485   -7.020  0.25 58.52  ? 83  ASP   A CB  1 
ATOM   383  C CB  D ASP   A 1 40  ? -4.812  0.485   -7.019  0.27 58.52  ? 83  ASP   A CB  1 
ATOM   384  C CG  A ASP   A 1 40  ? -5.262  1.837   -6.915  0.23 58.88  ? 83  ASP   A CG  1 
ATOM   385  C CG  B ASP   A 1 40  ? -5.261  1.837   -6.915  0.25 58.89  ? 83  ASP   A CG  1 
ATOM   386  C CG  C ASP   A 1 40  ? -5.485  1.833   -6.816  0.25 59.42  ? 83  ASP   A CG  1 
ATOM   387  C CG  D ASP   A 1 40  ? -5.485  1.832   -6.816  0.27 59.43  ? 83  ASP   A CG  1 
ATOM   388  O OD1 A ASP   A 1 40  ? -6.168  2.199   -7.701  0.23 58.40  ? 83  ASP   A OD1 1 
ATOM   389  O OD1 B ASP   A 1 40  ? -6.168  2.199   -7.702  0.25 58.42  ? 83  ASP   A OD1 1 
ATOM   390  O OD1 C ASP   A 1 40  ? -6.581  2.035   -7.387  0.25 58.98  ? 83  ASP   A OD1 1 
ATOM   391  O OD1 D ASP   A 1 40  ? -6.581  2.034   -7.387  0.27 59.01  ? 83  ASP   A OD1 1 
ATOM   392  O OD2 A ASP   A 1 40  ? -4.783  2.562   -6.019  0.23 61.67  ? 83  ASP   A OD2 1 
ATOM   393  O OD2 B ASP   A 1 40  ? -4.783  2.562   -6.020  0.25 61.68  ? 83  ASP   A OD2 1 
ATOM   394  O OD2 C ASP   A 1 40  ? -4.921  2.666   -6.077  0.25 62.36  ? 83  ASP   A OD2 1 
ATOM   395  O OD2 D ASP   A 1 40  ? -4.922  2.666   -6.077  0.27 62.38  ? 83  ASP   A OD2 1 
ATOM   396  N N   . PHE   A 1 41  ? -5.242  -2.282  -9.183  1.00 53.62  ? 84  PHE   A N   1 
ATOM   397  C CA  . PHE   A 1 41  ? -4.551  -3.458  -9.771  1.00 53.56  ? 84  PHE   A CA  1 
ATOM   398  C C   . PHE   A 1 41  ? -3.113  -3.068  -9.973  1.00 57.77  ? 84  PHE   A C   1 
ATOM   399  O O   . PHE   A 1 41  ? -2.847  -1.861  -10.138 1.00 60.67  ? 84  PHE   A O   1 
ATOM   400  C CB  . PHE   A 1 41  ? -5.143  -3.915  -11.097 1.00 51.01  ? 84  PHE   A CB  1 
ATOM   401  C CG  . PHE   A 1 41  ? -6.457  -4.645  -10.988 1.00 48.14  ? 84  PHE   A CG  1 
ATOM   402  C CD1 . PHE   A 1 41  ? -6.499  -5.966  -10.599 1.00 48.38  ? 84  PHE   A CD1 1 
ATOM   403  C CD2 . PHE   A 1 41  ? -7.648  -4.021  -11.307 1.00 47.85  ? 84  PHE   A CD2 1 
ATOM   404  C CE1 . PHE   A 1 41  ? -7.710  -6.645  -10.505 1.00 47.44  ? 84  PHE   A CE1 1 
ATOM   405  C CE2 . PHE   A 1 41  ? -8.851  -4.703  -11.232 1.00 46.40  ? 84  PHE   A CE2 1 
ATOM   406  C CZ  . PHE   A 1 41  ? -8.881  -6.021  -10.838 1.00 45.40  ? 84  PHE   A CZ  1 
ATOM   407  N N   . SER   A 1 42  ? -2.214  -4.040  -9.908  1.00 60.98  ? 85  SER   A N   1 
ATOM   408  C CA  . SER   A 1 42  ? -0.795  -3.816  -10.223 1.00 65.59  ? 85  SER   A CA  1 
ATOM   409  C C   . SER   A 1 42  ? -0.229  -5.076  -10.884 1.00 68.21  ? 85  SER   A C   1 
ATOM   410  O O   . SER   A 1 42  ? -0.811  -6.170  -10.691 1.00 66.07  ? 85  SER   A O   1 
ATOM   411  C CB  . SER   A 1 42  ? -0.074  -3.422  -8.981  1.00 69.09  ? 85  SER   A CB  1 
ATOM   412  O OG  . SER   A 1 42  ? -0.162  -4.454  -7.996  1.00 70.77  ? 85  SER   A OG  1 
ATOM   413  N N   . LEU   A 1 43  ? 0.839   -4.924  -11.666 1.00 72.91  ? 86  LEU   A N   1 
ATOM   414  C CA  . LEU   A 1 43  ? 1.540   -6.074  -12.289 1.00 76.67  ? 86  LEU   A CA  1 
ATOM   415  C C   . LEU   A 1 43  ? 2.485   -6.714  -11.272 1.00 77.42  ? 86  LEU   A C   1 
ATOM   416  O O   . LEU   A 1 43  ? 3.486   -6.101  -10.911 1.00 76.88  ? 86  LEU   A O   1 
ATOM   417  C CB  . LEU   A 1 43  ? 2.302   -5.601  -13.529 1.00 80.33  ? 86  LEU   A CB  1 
ATOM   418  C CG  . LEU   A 1 43  ? 1.392   -5.092  -14.638 1.00 80.98  ? 86  LEU   A CG  1 
ATOM   419  C CD1 . LEU   A 1 43  ? 2.152   -4.167  -15.572 1.00 85.20  ? 86  LEU   A CD1 1 
ATOM   420  C CD2 . LEU   A 1 43  ? 0.781   -6.262  -15.396 1.00 81.26  ? 86  LEU   A CD2 1 
ATOM   421  N N   . VAL   A 1 44  ? 2.147   -7.929  -10.870 1.00 79.29  ? 87  VAL   A N   1 
ATOM   422  C CA  . VAL   A 1 44  ? 3.107   -8.968  -10.417 1.00 86.28  ? 87  VAL   A CA  1 
ATOM   423  C C   . VAL   A 1 44  ? 4.010   -9.259  -11.614 1.00 93.95  ? 87  VAL   A C   1 
ATOM   424  O O   . VAL   A 1 44  ? 3.484   -9.275  -12.753 1.00 101.81 ? 87  VAL   A O   1 
ATOM   425  C CB  . VAL   A 1 44  ? 2.350   -10.231 -9.972  1.00 83.97  ? 87  VAL   A CB  1 
ATOM   426  C CG1 . VAL   A 1 44  ? 3.302   -11.338 -9.527  1.00 85.70  ? 87  VAL   A CG1 1 
ATOM   427  C CG2 . VAL   A 1 44  ? 1.319   -9.906  -8.902  1.00 81.40  ? 87  VAL   A CG2 1 
ATOM   428  N N   . GLU   A 1 45  ? 5.297   -9.487  -11.400 1.00 103.20 ? 88  GLU   A N   1 
ATOM   429  C CA  . GLU   A 1 45  ? 6.249   -9.662  -12.529 1.00 111.62 ? 88  GLU   A CA  1 
ATOM   430  C C   . GLU   A 1 45  ? 7.332   -10.682 -12.156 1.00 116.42 ? 88  GLU   A C   1 
ATOM   431  O O   . GLU   A 1 45  ? 7.381   -11.739 -12.804 1.00 117.17 ? 88  GLU   A O   1 
ATOM   432  C CB  . GLU   A 1 45  ? 6.786   -8.282  -12.914 1.00 116.75 ? 88  GLU   A CB  1 
ATOM   433  C CG  . GLU   A 1 45  ? 5.930   -7.558  -13.949 1.00 115.18 ? 88  GLU   A CG  1 
ATOM   434  C CD  . GLU   A 1 45  ? 6.317   -7.835  -15.390 1.00 114.47 ? 88  GLU   A CD  1 
ATOM   435  O OE1 . GLU   A 1 45  ? 6.807   -8.952  -15.660 1.00 115.60 ? 88  GLU   A OE1 1 
ATOM   436  O OE2 . GLU   A 1 45  ? 6.146   -6.927  -16.232 1.00 114.23 ? 88  GLU   A OE2 1 
ATOM   437  N N   C LYS   B 2 6   ? -38.511 12.331  -11.410 0.50 129.61 ? 15  LYS   B N   1 
ATOM   438  N N   D LYS   B 2 6   ? -38.511 12.331  -11.410 0.50 129.61 ? 15  LYS   B N   1 
ATOM   439  C CA  C LYS   B 2 6   ? -38.171 13.774  -11.266 0.50 129.77 ? 15  LYS   B CA  1 
ATOM   440  C CA  D LYS   B 2 6   ? -38.171 13.774  -11.266 0.50 129.77 ? 15  LYS   B CA  1 
ATOM   441  C C   C LYS   B 2 6   ? -36.861 14.063  -12.006 0.50 130.68 ? 15  LYS   B C   1 
ATOM   442  C C   D LYS   B 2 6   ? -36.861 14.063  -12.006 0.50 130.68 ? 15  LYS   B C   1 
ATOM   443  O O   C LYS   B 2 6   ? -36.542 15.234  -12.278 0.50 131.78 ? 15  LYS   B O   1 
ATOM   444  O O   D LYS   B 2 6   ? -36.542 15.234  -12.278 0.50 131.78 ? 15  LYS   B O   1 
ATOM   445  C CB  C LYS   B 2 6   ? -38.058 14.147  -9.786  0.50 129.08 ? 15  LYS   B CB  1 
ATOM   446  C CB  D LYS   B 2 6   ? -38.058 14.147  -9.786  0.50 129.08 ? 15  LYS   B CB  1 
ATOM   447  C CG  C LYS   B 2 6   ? -39.382 14.186  -9.040  0.50 129.50 ? 15  LYS   B CG  1 
ATOM   448  C CG  D LYS   B 2 6   ? -39.382 14.186  -9.040  0.50 129.50 ? 15  LYS   B CG  1 
ATOM   449  C CD  C LYS   B 2 6   ? -39.274 14.741  -7.645  0.50 129.66 ? 15  LYS   B CD  1 
ATOM   450  C CD  D LYS   B 2 6   ? -39.274 14.741  -7.645  0.50 129.66 ? 15  LYS   B CD  1 
ATOM   451  C CE  C LYS   B 2 6   ? -40.624 14.888  -6.975  0.50 130.93 ? 15  LYS   B CE  1 
ATOM   452  C CE  D LYS   B 2 6   ? -40.624 14.888  -6.975  0.50 130.93 ? 15  LYS   B CE  1 
ATOM   453  N NZ  C LYS   B 2 6   ? -40.496 15.394  -5.589  0.50 131.34 ? 15  LYS   B NZ  1 
ATOM   454  N NZ  D LYS   B 2 6   ? -40.496 15.394  -5.589  0.50 131.34 ? 15  LYS   B NZ  1 
ATOM   455  N N   A GLY   B 2 7   ? -37.451 12.219  -12.124 0.25 80.82  ? 22  GLY   B N   1 
ATOM   456  N N   B GLY   B 2 7   ? -37.452 12.219  -12.124 0.25 80.81  ? 22  GLY   B N   1 
ATOM   457  N N   C GLY   B 2 7   ? -36.038 11.640  -11.693 0.25 81.20  ? 22  GLY   B N   1 
ATOM   458  N N   D GLY   B 2 7   ? -36.038 11.640  -11.693 0.25 81.20  ? 22  GLY   B N   1 
ATOM   459  C CA  A GLY   B 2 7   ? -36.100 12.092  -12.744 0.25 80.51  ? 22  GLY   B CA  1 
ATOM   460  C CA  B GLY   B 2 7   ? -36.100 12.093  -12.743 0.25 80.50  ? 22  GLY   B CA  1 
ATOM   461  C CA  C GLY   B 2 7   ? -35.023 11.879  -12.764 0.25 80.89  ? 22  GLY   B CA  1 
ATOM   462  C CA  D GLY   B 2 7   ? -35.022 11.878  -12.764 0.25 80.88  ? 22  GLY   B CA  1 
ATOM   463  C C   A GLY   B 2 7   ? -36.087 11.087  -13.885 0.25 80.45  ? 22  GLY   B C   1 
ATOM   464  C C   B GLY   B 2 7   ? -36.086 11.088  -13.885 0.25 80.44  ? 22  GLY   B C   1 
ATOM   465  C C   C GLY   B 2 7   ? -35.028 10.775  -13.810 0.25 80.81  ? 22  GLY   B C   1 
ATOM   466  C C   D GLY   B 2 7   ? -35.028 10.774  -13.810 0.25 80.80  ? 22  GLY   B C   1 
ATOM   467  O O   A GLY   B 2 7   ? -37.016 10.254  -13.954 0.25 81.15  ? 22  GLY   B O   1 
ATOM   468  O O   B GLY   B 2 7   ? -37.015 10.255  -13.955 0.25 81.14  ? 22  GLY   B O   1 
ATOM   469  O O   C GLY   B 2 7   ? -35.223 9.599   -13.434 0.25 81.31  ? 22  GLY   B O   1 
ATOM   470  O O   D GLY   B 2 7   ? -35.224 9.598   -13.433 0.25 81.31  ? 22  GLY   B O   1 
ATOM   471  N N   A GLU   B 2 8   ? -35.062 11.162  -14.742 0.25 79.60  ? 23  GLU   B N   1 
ATOM   472  N N   B GLU   B 2 8   ? -35.061 11.165  -14.741 0.25 79.56  ? 23  GLU   B N   1 
ATOM   473  N N   C GLU   B 2 8   ? -34.816 11.125  -15.084 0.25 79.99  ? 23  GLU   B N   1 
ATOM   474  N N   D GLU   B 2 8   ? -34.816 11.124  -15.084 0.25 79.96  ? 23  GLU   B N   1 
ATOM   475  C CA  A GLU   B 2 8   ? -34.830 10.250  -15.895 0.25 78.81  ? 23  GLU   B CA  1 
ATOM   476  C CA  B GLU   B 2 8   ? -34.827 10.256  -15.895 0.25 78.74  ? 23  GLU   B CA  1 
ATOM   477  C CA  C GLU   B 2 8   ? -34.819 10.145  -16.201 0.25 79.33  ? 23  GLU   B CA  1 
ATOM   478  C CA  D GLU   B 2 8   ? -34.820 10.143  -16.201 0.25 79.28  ? 23  GLU   B CA  1 
ATOM   479  C C   A GLU   B 2 8   ? -34.426 8.862   -15.377 0.25 77.29  ? 23  GLU   B C   1 
ATOM   480  C C   B GLU   B 2 8   ? -34.428 8.868   -15.379 0.25 77.15  ? 23  GLU   B C   1 
ATOM   481  C C   C GLU   B 2 8   ? -34.364 8.788   -15.651 0.25 77.64  ? 23  GLU   B C   1 
ATOM   482  C C   D GLU   B 2 8   ? -34.367 8.785   -15.652 0.25 77.53  ? 23  GLU   B C   1 
ATOM   483  O O   A GLU   B 2 8   ? -33.309 8.735   -14.840 0.25 76.23  ? 23  GLU   B O   1 
ATOM   484  O O   B GLU   B 2 8   ? -33.314 8.728   -14.837 0.25 76.14  ? 23  GLU   B O   1 
ATOM   485  O O   C GLU   B 2 8   ? -33.170 8.636   -15.323 0.25 76.76  ? 23  GLU   B O   1 
ATOM   486  O O   D GLU   B 2 8   ? -33.173 8.633   -15.322 0.25 76.69  ? 23  GLU   B O   1 
ATOM   487  C CB  A GLU   B 2 8   ? -33.747 10.830  -16.809 0.25 79.19  ? 23  GLU   B CB  1 
ATOM   488  C CB  B GLU   B 2 8   ? -33.744 10.832  -16.810 0.25 79.15  ? 23  GLU   B CB  1 
ATOM   489  C CB  C GLU   B 2 8   ? -33.932 10.594  -17.365 0.25 79.59  ? 23  GLU   B CB  1 
ATOM   490  C CB  D GLU   B 2 8   ? -33.932 10.593  -17.364 0.25 79.56  ? 23  GLU   B CB  1 
ATOM   491  C CG  A GLU   B 2 8   ? -33.702 10.180  -18.182 0.25 79.82  ? 23  GLU   B CG  1 
ATOM   492  C CG  B GLU   B 2 8   ? -33.702 10.181  -18.182 0.25 79.79  ? 23  GLU   B CG  1 
ATOM   493  C CG  C GLU   B 2 8   ? -34.103 9.731   -18.605 0.25 80.20  ? 23  GLU   B CG  1 
ATOM   494  C CG  D GLU   B 2 8   ? -34.103 9.730   -18.606 0.25 80.19  ? 23  GLU   B CG  1 
ATOM   495  C CD  A GLU   B 2 8   ? -32.730 10.817  -19.163 0.25 80.43  ? 23  GLU   B CD  1 
ATOM   496  C CD  B GLU   B 2 8   ? -32.729 10.817  -19.163 0.25 80.42  ? 23  GLU   B CD  1 
ATOM   497  C CD  C GLU   B 2 8   ? -33.438 10.259  -19.868 0.25 80.95  ? 23  GLU   B CD  1 
ATOM   498  C CD  D GLU   B 2 8   ? -33.438 10.259  -19.868 0.25 80.94  ? 23  GLU   B CD  1 
ATOM   499  O OE1 A GLU   B 2 8   ? -31.821 11.543  -18.715 0.25 80.25  ? 23  GLU   B OE1 1 
ATOM   500  O OE1 B GLU   B 2 8   ? -31.821 11.543  -18.716 0.25 80.24  ? 23  GLU   B OE1 1 
ATOM   501  O OE1 C GLU   B 2 8   ? -32.438 11.004  -19.741 0.25 80.23  ? 23  GLU   B OE1 1 
ATOM   502  O OE1 D GLU   B 2 8   ? -32.438 11.004  -19.741 0.25 80.23  ? 23  GLU   B OE1 1 
ATOM   503  O OE2 A GLU   B 2 8   ? -32.897 10.606  -20.377 0.25 81.80  ? 23  GLU   B OE2 1 
ATOM   504  O OE2 B GLU   B 2 8   ? -32.897 10.606  -20.377 0.25 81.79  ? 23  GLU   B OE2 1 
ATOM   505  O OE2 C GLU   B 2 8   ? -33.936 9.942   -20.983 0.25 82.35  ? 23  GLU   B OE2 1 
ATOM   506  O OE2 D GLU   B 2 8   ? -33.936 9.943   -20.983 0.25 82.34  ? 23  GLU   B OE2 1 
ATOM   507  N N   A THR   B 2 9   ? -35.293 7.857   -15.538 0.25 76.42  ? 24  THR   B N   1 
ATOM   508  N N   B THR   B 2 9   ? -35.309 7.884   -15.571 0.25 75.96  ? 24  THR   B N   1 
ATOM   509  N N   C THR   B 2 9   ? -35.300 7.848   -15.542 0.25 76.57  ? 24  THR   B N   1 
ATOM   510  N N   D THR   B 2 9   ? -35.304 7.843   -15.552 0.25 76.24  ? 24  THR   B N   1 
ATOM   511  C CA  A THR   B 2 9   ? -35.072 6.481   -15.020 0.25 75.28  ? 24  THR   B CA  1 
ATOM   512  C CA  B THR   B 2 9   ? -35.190 6.507   -15.027 0.25 74.69  ? 24  THR   B CA  1 
ATOM   513  C CA  C THR   B 2 9   ? -35.070 6.478   -15.018 0.25 75.34  ? 24  THR   B CA  1 
ATOM   514  C CA  D THR   B 2 9   ? -35.082 6.478   -15.015 0.25 74.82  ? 24  THR   B CA  1 
ATOM   515  C C   A THR   B 2 9   ? -34.898 5.480   -16.162 0.25 73.69  ? 24  THR   B C   1 
ATOM   516  C C   B THR   B 2 9   ? -34.988 5.488   -16.153 0.25 73.35  ? 24  THR   B C   1 
ATOM   517  C C   C THR   B 2 9   ? -34.896 5.479   -16.162 0.25 73.72  ? 24  THR   B C   1 
ATOM   518  C C   D THR   B 2 9   ? -34.998 5.467   -16.160 0.25 73.46  ? 24  THR   B C   1 
ATOM   519  O O   A THR   B 2 9   ? -34.660 4.297   -15.851 0.25 73.90  ? 24  THR   B O   1 
ATOM   520  O O   B THR   B 2 9   ? -34.816 4.300   -15.822 0.25 73.60  ? 24  THR   B O   1 
ATOM   521  O O   C THR   B 2 9   ? -34.659 4.295   -15.852 0.25 73.92  ? 24  THR   B O   1 
ATOM   522  O O   D THR   B 2 9   ? -34.936 4.262   -15.852 0.25 73.75  ? 24  THR   B O   1 
ATOM   523  C CB  A THR   B 2 9   ? -36.240 6.009   -14.148 0.25 76.07  ? 24  THR   B CB  1 
ATOM   524  C CB  B THR   B 2 9   ? -36.436 6.149   -14.210 0.25 75.18  ? 24  THR   B CB  1 
ATOM   525  C CB  C THR   B 2 9   ? -36.238 6.007   -14.147 0.25 76.11  ? 24  THR   B CB  1 
ATOM   526  C CB  D THR   B 2 9   ? -36.202 6.083   -14.045 0.25 75.24  ? 24  THR   B CB  1 
ATOM   527  O OG1 A THR   B 2 9   ? -36.726 7.152   -13.445 0.25 76.96  ? 24  THR   B OG1 1 
ATOM   528  O OG1 B THR   B 2 9   ? -37.577 6.531   -14.979 0.25 75.48  ? 24  THR   B OG1 1 
ATOM   529  O OG1 C THR   B 2 9   ? -36.726 7.151   -13.445 0.25 76.98  ? 24  THR   B OG1 1 
ATOM   530  O OG1 D THR   B 2 9   ? -37.421 6.618   -14.562 0.25 75.46  ? 24  THR   B OG1 1 
ATOM   531  C CG2 A THR   B 2 9   ? -35.839 4.892   -13.207 0.25 76.34  ? 24  THR   B CG2 1 
ATOM   532  C CG2 B THR   B 2 9   ? -36.471 6.833   -12.861 0.25 75.75  ? 24  THR   B CG2 1 
ATOM   533  C CG2 C THR   B 2 9   ? -35.839 4.891   -13.205 0.25 76.37  ? 24  THR   B CG2 1 
ATOM   534  C CG2 D THR   B 2 9   ? -35.968 6.588   -12.638 0.25 75.54  ? 24  THR   B CG2 1 
ATOM   535  N N   . THR   B 2 10  ? -35.007 5.930   -17.416 1.00 72.30  ? 25  THR   B N   1 
ATOM   536  C CA  . THR   B 2 10  ? -34.969 5.035   -18.600 1.00 68.80  ? 25  THR   B CA  1 
ATOM   537  C C   . THR   B 2 10  ? -33.671 4.218   -18.584 1.00 64.35  ? 25  THR   B C   1 
ATOM   538  O O   . THR   B 2 10  ? -32.595 4.822   -18.387 1.00 64.85  ? 25  THR   B O   1 
ATOM   539  C CB  . THR   B 2 10  ? -35.081 5.793   -19.943 1.00 68.83  ? 25  THR   B CB  1 
ATOM   540  O OG1 . THR   B 2 10  ? -36.075 6.821   -19.952 1.00 69.80  ? 25  THR   B OG1 1 
ATOM   541  C CG2 . THR   B 2 10  ? -35.415 4.836   -21.059 1.00 68.22  ? 25  THR   B CG2 1 
ATOM   542  N N   . ASP   B 2 11  ? -33.760 2.911   -18.817 1.00 61.66  ? 26  ASP   B N   1 
ATOM   543  C CA  . ASP   B 2 11  ? -32.571 2.056   -19.020 1.00 61.68  ? 26  ASP   B CA  1 
ATOM   544  C C   . ASP   B 2 11  ? -31.626 2.721   -20.040 1.00 61.56  ? 26  ASP   B C   1 
ATOM   545  O O   . ASP   B 2 11  ? -32.120 3.501   -20.963 1.00 62.31  ? 26  ASP   B O   1 
ATOM   546  C CB  . ASP   B 2 11  ? -32.930 0.643   -19.498 1.00 62.93  ? 26  ASP   B CB  1 
ATOM   547  C CG  . ASP   B 2 11  ? -33.424 -0.392  -18.478 1.00 64.31  ? 26  ASP   B CG  1 
ATOM   548  O OD1 . ASP   B 2 11  ? -33.756 -0.028  -17.332 1.00 60.81  ? 26  ASP   B OD1 1 
ATOM   549  O OD2 . ASP   B 2 11  ? -33.497 -1.596  -18.900 1.00 67.15  ? 26  ASP   B OD2 1 
ATOM   550  N N   . GLY   B 2 12  ? -30.333 2.394   -19.953 1.00 58.80  ? 27  GLY   B N   1 
ATOM   551  C CA  . GLY   B 2 12  ? -29.345 2.765   -20.978 1.00 57.95  ? 27  GLY   B CA  1 
ATOM   552  C C   . GLY   B 2 12  ? -28.072 3.235   -20.336 1.00 56.73  ? 27  GLY   B C   1 
ATOM   553  O O   . GLY   B 2 12  ? -27.956 3.122   -19.111 1.00 56.00  ? 27  GLY   B O   1 
ATOM   554  N N   . VAL   B 2 13  ? -27.130 3.710   -21.143 1.00 55.67  ? 28  VAL   B N   1 
ATOM   555  C CA  . VAL   B 2 13  ? -25.836 4.261   -20.666 1.00 54.20  ? 28  VAL   B CA  1 
ATOM   556  C C   . VAL   B 2 13  ? -25.958 5.780   -20.495 1.00 54.61  ? 28  VAL   B C   1 
ATOM   557  O O   . VAL   B 2 13  ? -26.737 6.460   -21.282 1.00 54.91  ? 28  VAL   B O   1 
ATOM   558  C CB  . VAL   B 2 13  ? -24.717 3.809   -21.591 1.00 54.56  ? 28  VAL   B CB  1 
ATOM   559  C CG1 . VAL   B 2 13  ? -24.870 4.346   -23.075 1.00 55.75  ? 28  VAL   B CG1 1 
ATOM   560  C CG2 . VAL   B 2 13  ? -23.363 4.146   -21.013 1.00 53.85  ? 28  VAL   B CG2 1 
ATOM   561  N N   . TYR   B 2 14  ? -25.236 6.330   -19.519 1.00 53.14  ? 29  TYR   B N   1 
ATOM   562  C CA  . TYR   B 2 14  ? -25.330 7.753   -19.122 1.00 53.71  ? 29  TYR   B CA  1 
ATOM   563  C C   . TYR   B 2 14  ? -23.942 8.301   -18.812 1.00 54.56  ? 29  TYR   B C   1 
ATOM   564  O O   . TYR   B 2 14  ? -23.034 7.560   -18.319 1.00 55.03  ? 29  TYR   B O   1 
ATOM   565  C CB  . TYR   B 2 14  ? -26.169 7.976   -17.876 1.00 53.43  ? 29  TYR   B CB  1 
ATOM   566  C CG  . TYR   B 2 14  ? -27.644 7.749   -18.005 1.00 52.97  ? 29  TYR   B CG  1 
ATOM   567  C CD1 . TYR   B 2 14  ? -28.160 6.494   -18.301 1.00 53.39  ? 29  TYR   B CD1 1 
ATOM   568  C CD2 . TYR   B 2 14  ? -28.504 8.806   -17.781 1.00 53.17  ? 29  TYR   B CD2 1 
ATOM   569  C CE1 . TYR   B 2 14  ? -29.527 6.295   -18.356 1.00 54.25  ? 29  TYR   B CE1 1 
ATOM   570  C CE2 . TYR   B 2 14  ? -29.868 8.641   -17.891 1.00 54.23  ? 29  TYR   B CE2 1 
ATOM   571  C CZ  . TYR   B 2 14  ? -30.377 7.377   -18.171 1.00 54.88  ? 29  TYR   B CZ  1 
ATOM   572  O OH  . TYR   B 2 14  ? -31.735 7.241   -18.218 1.00 57.98  ? 29  TYR   B OH  1 
ATOM   573  N N   . ARG   B 2 15  ? -23.783 9.591   -19.086 1.00 55.47  ? 30  ARG   B N   1 
ATOM   574  C CA  . ARG   B 2 15  ? -22.545 10.326  -18.733 1.00 56.11  ? 30  ARG   B CA  1 
ATOM   575  C C   . ARG   B 2 15  ? -22.698 10.794  -17.292 1.00 54.44  ? 30  ARG   B C   1 
ATOM   576  O O   . ARG   B 2 15  ? -23.765 11.285  -16.982 1.00 53.43  ? 30  ARG   B O   1 
ATOM   577  C CB  . ARG   B 2 15  ? -22.336 11.554  -19.625 1.00 56.93  ? 30  ARG   B CB  1 
ATOM   578  C CG  . ARG   B 2 15  ? -22.194 11.250  -21.104 1.00 58.12  ? 30  ARG   B CG  1 
ATOM   579  C CD  . ARG   B 2 15  ? -22.037 12.513  -21.938 1.00 59.39  ? 30  ARG   B CD  1 
ATOM   580  N NE  . ARG   B 2 15  ? -22.222 12.219  -23.357 1.00 59.14  ? 30  ARG   B NE  1 
ATOM   581  C CZ  . ARG   B 2 15  ? -21.253 11.868  -24.196 1.00 59.90  ? 30  ARG   B CZ  1 
ATOM   582  N NH1 . ARG   B 2 15  ? -20.003 11.822  -23.775 1.00 60.19  ? 30  ARG   B NH1 1 
ATOM   583  N NH2 . ARG   B 2 15  ? -21.537 11.571  -25.462 1.00 60.69  ? 30  ARG   B NH2 1 
ATOM   584  N N   . VAL   B 2 16  ? -21.624 10.710  -16.514 1.00 54.76  ? 31  VAL   B N   1 
ATOM   585  C CA  . VAL   B 2 16  ? -21.493 11.377  -15.198 1.00 55.20  ? 31  VAL   B CA  1 
ATOM   586  C C   . VAL   B 2 16  ? -20.647 12.625  -15.352 1.00 55.51  ? 31  VAL   B C   1 
ATOM   587  O O   . VAL   B 2 16  ? -19.471 12.499  -15.643 1.00 55.62  ? 31  VAL   B O   1 
ATOM   588  C CB  . VAL   B 2 16  ? -20.846 10.429  -14.162 1.00 55.34  ? 31  VAL   B CB  1 
ATOM   589  C CG1 . VAL   B 2 16  ? -20.808 11.099  -12.813 1.00 54.69  ? 31  VAL   B CG1 1 
ATOM   590  C CG2 . VAL   B 2 16  ? -21.563 9.091   -14.116 1.00 55.15  ? 31  VAL   B CG2 1 
ATOM   591  N N   . MET   B 2 17  ? -21.229 13.764  -15.029 1.00 57.71  ? 32  MET   B N   1 
ATOM   592  C CA  . MET   B 2 17  ? -20.626 15.092  -15.264 1.00 60.06  ? 32  MET   B CA  1 
ATOM   593  C C   . MET   B 2 17  ? -20.395 15.769  -13.920 1.00 60.77  ? 32  MET   B C   1 
ATOM   594  O O   . MET   B 2 17  ? -21.190 15.507  -12.978 1.00 60.71  ? 32  MET   B O   1 
ATOM   595  C CB  . MET   B 2 17  ? -21.572 15.987  -16.073 1.00 60.94  ? 32  MET   B CB  1 
ATOM   596  C CG  . MET   B 2 17  ? -22.070 15.402  -17.411 1.00 61.01  ? 32  MET   B CG  1 
ATOM   597  S SD  . MET   B 2 17  ? -20.747 15.000  -18.593 1.00 61.87  ? 32  MET   B SD  1 
ATOM   598  C CE  . MET   B 2 17  ? -20.040 16.624  -18.913 1.00 63.30  ? 32  MET   B CE  1 
ATOM   599  N N   . THR   B 2 18  ? -19.408 16.663  -13.868 1.00 62.70  ? 33  THR   B N   1 
ATOM   600  C CA  . THR   B 2 18  ? -19.267 17.664  -12.787 1.00 65.49  ? 33  THR   B CA  1 
ATOM   601  C C   . THR   B 2 18  ? -19.169 19.100  -13.346 1.00 68.56  ? 33  THR   B C   1 
ATOM   602  O O   . THR   B 2 18  ? -18.499 19.295  -14.369 1.00 66.37  ? 33  THR   B O   1 
ATOM   603  C CB  . THR   B 2 18  ? -18.086 17.287  -11.880 1.00 64.91  ? 33  THR   B CB  1 
ATOM   604  O OG1 . THR   B 2 18  ? -18.143 18.230  -10.813 1.00 64.60  ? 33  THR   B OG1 1 
ATOM   605  C CG2 . THR   B 2 18  ? -16.743 17.318  -12.584 1.00 64.78  ? 33  THR   B CG2 1 
ATOM   606  N N   . ARG   B 2 19  ? -19.756 20.063  -12.608 1.00 73.84  ? 34  ARG   B N   1 
ATOM   607  C CA  . ARG   B 2 19  ? -19.571 21.539  -12.743 1.00 78.77  ? 34  ARG   B CA  1 
ATOM   608  C C   . ARG   B 2 19  ? -18.537 22.084  -11.733 1.00 79.48  ? 34  ARG   B C   1 
ATOM   609  O O   . ARG   B 2 19  ? -18.343 23.307  -11.685 1.00 77.51  ? 34  ARG   B O   1 
ATOM   610  C CB  . ARG   B 2 19  ? -20.931 22.216  -12.552 1.00 82.22  ? 34  ARG   B CB  1 
ATOM   611  C CG  . ARG   B 2 19  ? -21.945 21.832  -13.625 1.00 87.66  ? 34  ARG   B CG  1 
ATOM   612  C CD  . ARG   B 2 19  ? -22.328 22.950  -14.601 1.00 89.57  ? 34  ARG   B CD  1 
ATOM   613  N NE  . ARG   B 2 19  ? -23.369 22.572  -15.560 1.00 91.04  ? 34  ARG   B NE  1 
ATOM   614  C CZ  . ARG   B 2 19  ? -24.645 22.311  -15.256 1.00 94.34  ? 34  ARG   B CZ  1 
ATOM   615  N NH1 . ARG   B 2 19  ? -25.074 22.367  -14.000 1.00 98.13  ? 34  ARG   B NH1 1 
ATOM   616  N NH2 . ARG   B 2 19  ? -25.496 21.984  -16.213 1.00 93.13  ? 34  ARG   B NH2 1 
ATOM   617  N N   . ARG   B 2 20  ? -17.861 21.223  -10.975 1.00 83.21  ? 35  ARG   B N   1 
ATOM   618  C CA  . ARG   B 2 20  ? -16.996 21.641  -9.835  1.00 88.33  ? 35  ARG   B CA  1 
ATOM   619  C C   . ARG   B 2 20  ? -15.647 22.103  -10.400 1.00 86.46  ? 35  ARG   B C   1 
ATOM   620  O O   . ARG   B 2 20  ? -14.884 22.777  -9.692  1.00 87.42  ? 35  ARG   B O   1 
ATOM   621  C CB  . ARG   B 2 20  ? -16.875 20.491  -8.830  1.00 92.00  ? 35  ARG   B CB  1 
ATOM   622  C CG  . ARG   B 2 20  ? -16.737 20.907  -7.371  1.00 99.20  ? 35  ARG   B CG  1 
ATOM   623  C CD  . ARG   B 2 20  ? -16.463 19.671  -6.518  1.00 107.13 ? 35  ARG   B CD  1 
ATOM   624  N NE  . ARG   B 2 20  ? -15.687 18.679  -7.282  1.00 111.74 ? 35  ARG   B NE  1 
ATOM   625  C CZ  . ARG   B 2 20  ? -14.353 18.637  -7.395  1.00 113.26 ? 35  ARG   B CZ  1 
ATOM   626  N NH1 . ARG   B 2 20  ? -13.586 19.510  -6.759  1.00 117.28 ? 35  ARG   B NH1 1 
ATOM   627  N NH2 . ARG   B 2 20  ? -13.786 17.706  -8.144  1.00 111.78 ? 35  ARG   B NH2 1 
ATOM   628  N N   . LEU   B 2 21  ? -15.359 21.761  -11.650 1.00 83.94  ? 36  LEU   B N   1 
ATOM   629  C CA  . LEU   B 2 21  ? -14.113 22.187  -12.336 1.00 82.18  ? 36  LEU   B CA  1 
ATOM   630  C C   . LEU   B 2 21  ? -14.445 23.250  -13.396 1.00 78.83  ? 36  LEU   B C   1 
ATOM   631  O O   . LEU   B 2 21  ? -15.558 23.866  -13.333 1.00 75.10  ? 36  LEU   B O   1 
ATOM   632  C CB  . LEU   B 2 21  ? -13.438 20.937  -12.905 1.00 83.28  ? 36  LEU   B CB  1 
ATOM   633  C CG  . LEU   B 2 21  ? -12.412 20.278  -11.987 1.00 85.75  ? 36  LEU   B CG  1 
ATOM   634  C CD1 . LEU   B 2 21  ? -12.938 20.130  -10.563 1.00 85.85  ? 36  LEU   B CD1 1 
ATOM   635  C CD2 . LEU   B 2 21  ? -11.989 18.929  -12.548 1.00 87.25  ? 36  LEU   B CD2 1 
ATOM   636  N N   . LEU   B 2 22  ? -13.492 23.510  -14.297 1.00 78.84  ? 37  LEU   B N   1 
ATOM   637  C CA  . LEU   B 2 22  ? -13.703 24.407  -15.461 1.00 78.65  ? 37  LEU   B CA  1 
ATOM   638  C C   . LEU   B 2 22  ? -14.855 23.848  -16.293 1.00 77.99  ? 37  LEU   B C   1 
ATOM   639  O O   . LEU   B 2 22  ? -14.903 22.608  -16.444 1.00 76.51  ? 37  LEU   B O   1 
ATOM   640  C CB  . LEU   B 2 22  ? -12.433 24.492  -16.298 1.00 78.01  ? 37  LEU   B CB  1 
ATOM   641  C CG  . LEU   B 2 22  ? -12.487 25.582  -17.357 1.00 78.41  ? 37  LEU   B CG  1 
ATOM   642  C CD1 . LEU   B 2 22  ? -12.270 26.950  -16.735 1.00 77.73  ? 37  LEU   B CD1 1 
ATOM   643  C CD2 . LEU   B 2 22  ? -11.487 25.303  -18.487 1.00 80.00  ? 37  LEU   B CD2 1 
ATOM   644  N N   . GLY   B 2 23  ? -15.760 24.716  -16.770 1.00 77.96  ? 38  GLY   B N   1 
ATOM   645  C CA  . GLY   B 2 23  ? -16.954 24.303  -17.535 1.00 77.03  ? 38  GLY   B CA  1 
ATOM   646  C C   . GLY   B 2 23  ? -17.601 23.052  -16.949 1.00 75.80  ? 38  GLY   B C   1 
ATOM   647  O O   . GLY   B 2 23  ? -17.566 22.879  -15.717 1.00 76.33  ? 38  GLY   B O   1 
ATOM   648  N N   . SER   B 2 24  ? -18.196 22.219  -17.805 1.00 74.53  ? 39  SER   B N   1 
ATOM   649  C CA  . SER   B 2 24  ? -18.759 20.886  -17.464 1.00 71.85  ? 39  SER   B CA  1 
ATOM   650  C C   . SER   B 2 24  ? -17.760 19.803  -17.856 1.00 69.93  ? 39  SER   B C   1 
ATOM   651  O O   . SER   B 2 24  ? -17.429 19.764  -19.026 1.00 68.31  ? 39  SER   B O   1 
ATOM   652  C CB  . SER   B 2 24  ? -20.050 20.694  -18.172 1.00 72.10  ? 39  SER   B CB  1 
ATOM   653  O OG  . SER   B 2 24  ? -20.972 21.674  -17.713 1.00 72.22  ? 39  SER   B OG  1 
ATOM   654  N N   . THR   B 2 25  ? -17.292 18.991  -16.907 1.00 67.34  ? 40  THR   B N   1 
ATOM   655  C CA  . THR   B 2 25  ? -16.239 17.969  -17.124 1.00 66.95  ? 40  THR   B CA  1 
ATOM   656  C C   . THR   B 2 25  ? -16.845 16.575  -16.962 1.00 65.97  ? 40  THR   B C   1 
ATOM   657  O O   . THR   B 2 25  ? -17.526 16.368  -15.954 1.00 65.39  ? 40  THR   B O   1 
ATOM   658  C CB  . THR   B 2 25  ? -15.062 18.160  -16.159 1.00 67.27  ? 40  THR   B CB  1 
ATOM   659  O OG1 . THR   B 2 25  ? -14.513 19.460  -16.395 1.00 67.48  ? 40  THR   B OG1 1 
ATOM   660  C CG2 . THR   B 2 25  ? -13.980 17.113  -16.336 1.00 66.91  ? 40  THR   B CG2 1 
ATOM   661  N N   . GLN   B 2 26  ? -16.594 15.656  -17.899 1.00 64.10  ? 41  GLN   B N   1 
ATOM   662  C CA  . GLN   B 2 26  ? -17.075 14.256  -17.749 1.00 63.13  ? 41  GLN   B CA  1 
ATOM   663  C C   . GLN   B 2 26  ? -16.077 13.503  -16.849 1.00 62.75  ? 41  GLN   B C   1 
ATOM   664  O O   . GLN   B 2 26  ? -14.877 13.412  -17.218 1.00 63.36  ? 41  GLN   B O   1 
ATOM   665  C CB  . GLN   B 2 26  ? -17.285 13.567  -19.104 1.00 61.74  ? 41  GLN   B CB  1 
ATOM   666  C CG  . GLN   B 2 26  ? -17.803 12.137  -19.001 1.00 61.25  ? 41  GLN   B CG  1 
ATOM   667  C CD  . GLN   B 2 26  ? -18.170 11.485  -20.316 1.00 61.13  ? 41  GLN   B CD  1 
ATOM   668  O OE1 . GLN   B 2 26  ? -18.845 12.074  -21.166 1.00 63.14  ? 41  GLN   B OE1 1 
ATOM   669  N NE2 . GLN   B 2 26  ? -17.724 10.254  -20.507 1.00 60.38  ? 41  GLN   B NE2 1 
ATOM   670  N N   . VAL   B 2 27  ? -16.551 12.979  -15.721 1.00 61.51  ? 42  VAL   B N   1 
ATOM   671  C CA  . VAL   B 2 27  ? -15.688 12.266  -14.721 1.00 60.64  ? 42  VAL   B CA  1 
ATOM   672  C C   . VAL   B 2 27  ? -15.847 10.756  -14.937 1.00 58.44  ? 42  VAL   B C   1 
ATOM   673  O O   . VAL   B 2 27  ? -14.930 9.989   -14.560 1.00 58.37  ? 42  VAL   B O   1 
ATOM   674  C CB  . VAL   B 2 27  ? -16.035 12.674  -13.283 1.00 62.07  ? 42  VAL   B CB  1 
ATOM   675  C CG1 . VAL   B 2 27  ? -15.605 14.101  -12.960 1.00 63.84  ? 42  VAL   B CG1 1 
ATOM   676  C CG2 . VAL   B 2 27  ? -17.509 12.491  -12.985 1.00 61.21  ? 42  VAL   B CG2 1 
ATOM   677  N N   . GLY   B 2 28  ? -16.968 10.353  -15.545 1.00 56.37  ? 43  GLY   B N   1 
ATOM   678  C CA  . GLY   B 2 28  ? -17.205 8.950   -15.919 1.00 54.96  ? 43  GLY   B CA  1 
ATOM   679  C C   . GLY   B 2 28  ? -18.563 8.735   -16.566 1.00 54.52  ? 43  GLY   B C   1 
ATOM   680  O O   . GLY   B 2 28  ? -19.145 9.717   -17.126 1.00 55.22  ? 43  GLY   B O   1 
ATOM   681  N N   . VAL   B 2 29  ? -19.001 7.466   -16.526 1.00 53.85  ? 44  VAL   B N   1 
ATOM   682  C CA  . VAL   B 2 29  ? -20.114 6.804   -17.292 1.00 53.49  ? 44  VAL   B CA  1 
ATOM   683  C C   . VAL   B 2 29  ? -20.794 5.809   -16.333 1.00 52.82  ? 44  VAL   B C   1 
ATOM   684  O O   . VAL   B 2 29  ? -20.067 5.326   -15.393 1.00 52.82  ? 44  VAL   B O   1 
ATOM   685  C CB  . VAL   B 2 29  ? -19.577 6.056   -18.532 1.00 54.34  ? 44  VAL   B CB  1 
ATOM   686  C CG1 . VAL   B 2 29  ? -20.693 5.378   -19.341 1.00 54.62  ? 44  VAL   B CG1 1 
ATOM   687  C CG2 . VAL   B 2 29  ? -18.738 6.950   -19.448 1.00 54.48  ? 44  VAL   B CG2 1 
ATOM   688  N N   . GLY   B 2 30  ? -22.088 5.496   -16.533 1.00 51.72  ? 45  GLY   B N   1 
ATOM   689  C CA  . GLY   B 2 30  ? -22.718 4.374   -15.823 1.00 50.80  ? 45  GLY   B CA  1 
ATOM   690  C C   . GLY   B 2 30  ? -23.895 3.797   -16.559 1.00 50.94  ? 45  GLY   B C   1 
ATOM   691  O O   . GLY   B 2 30  ? -24.243 4.318   -17.678 1.00 50.91  ? 45  GLY   B O   1 
ATOM   692  N N   . VAL   B 2 31  ? -24.523 2.796   -15.939 1.00 49.64  ? 46  VAL   B N   1 
ATOM   693  C CA  . VAL   B 2 31  ? -25.632 1.995   -16.514 1.00 50.02  ? 46  VAL   B CA  1 
ATOM   694  C C   . VAL   B 2 31  ? -26.866 2.173   -15.664 1.00 51.06  ? 46  VAL   B C   1 
ATOM   695  O O   . VAL   B 2 31  ? -26.760 1.931   -14.447 1.00 49.52  ? 46  VAL   B O   1 
ATOM   696  C CB  . VAL   B 2 31  ? -25.287 0.511   -16.623 1.00 50.66  ? 46  VAL   B CB  1 
ATOM   697  C CG1 . VAL   B 2 31  ? -26.475 -0.290  -17.149 1.00 51.68  ? 46  VAL   B CG1 1 
ATOM   698  C CG2 . VAL   B 2 31  ? -24.066 0.292   -17.487 1.00 51.22  ? 46  VAL   B CG2 1 
ATOM   699  N N   . MET   B 2 32  ? -27.983 2.551   -16.279 1.00 51.47  ? 47  MET   B N   1 
ATOM   700  C CA  . MET   B 2 32  ? -29.309 2.562   -15.635 1.00 52.75  ? 47  MET   B CA  1 
ATOM   701  C C   . MET   B 2 32  ? -30.041 1.257   -15.994 1.00 54.20  ? 47  MET   B C   1 
ATOM   702  O O   . MET   B 2 32  ? -30.276 1.001   -17.174 1.00 53.04  ? 47  MET   B O   1 
ATOM   703  C CB  . MET   B 2 32  ? -30.100 3.800   -16.068 1.00 53.89  ? 47  MET   B CB  1 
ATOM   704  C CG  . MET   B 2 32  ? -31.366 4.033   -15.266 1.00 55.15  ? 47  MET   B CG  1 
ATOM   705  S SD  . MET   B 2 32  ? -31.007 4.500   -13.538 1.00 56.25  ? 47  MET   B SD  1 
ATOM   706  C CE  . MET   B 2 32  ? -30.677 6.246   -13.744 1.00 56.49  ? 47  MET   B CE  1 
ATOM   707  N N   . GLN   B 2 33  ? -30.391 0.431   -15.006 1.00 54.48  ? 48  GLN   B N   1 
ATOM   708  C CA  . GLN   B 2 33  ? -31.048 -0.865  -15.271 1.00 55.72  ? 48  GLN   B CA  1 
ATOM   709  C C   . GLN   B 2 33  ? -31.986 -1.177  -14.116 1.00 57.08  ? 48  GLN   B C   1 
ATOM   710  O O   . GLN   B 2 33  ? -31.559 -1.150  -12.921 1.00 56.99  ? 48  GLN   B O   1 
ATOM   711  C CB  . GLN   B 2 33  ? -30.038 -1.978  -15.538 1.00 56.18  ? 48  GLN   B CB  1 
ATOM   712  C CG  . GLN   B 2 33  ? -30.770 -3.282  -15.784 1.00 57.86  ? 48  GLN   B CG  1 
ATOM   713  C CD  . GLN   B 2 33  ? -29.973 -4.381  -16.438 1.00 59.59  ? 48  GLN   B CD  1 
ATOM   714  O OE1 . GLN   B 2 33  ? -30.136 -5.548  -16.094 1.00 62.34  ? 48  GLN   B OE1 1 
ATOM   715  N NE2 . GLN   B 2 33  ? -29.077 -4.036  -17.344 1.00 58.83  ? 48  GLN   B NE2 1 
ATOM   716  N N   . GLU   B 2 34  ? -33.245 -1.424  -14.438 1.00 58.18  ? 49  GLU   B N   1 
ATOM   717  C CA  . GLU   B 2 34  ? -34.307 -1.705  -13.433 1.00 57.97  ? 49  GLU   B CA  1 
ATOM   718  C C   . GLU   B 2 34  ? -34.289 -0.637  -12.327 1.00 56.87  ? 49  GLU   B C   1 
ATOM   719  O O   . GLU   B 2 34  ? -34.596 -0.980  -11.239 1.00 56.88  ? 49  GLU   B O   1 
ATOM   720  C CB  . GLU   B 2 34  ? -34.120 -3.109  -12.838 1.00 59.43  ? 49  GLU   B CB  1 
ATOM   721  C CG  . GLU   B 2 34  ? -33.875 -4.202  -13.870 1.00 60.21  ? 49  GLU   B CG  1 
ATOM   722  C CD  . GLU   B 2 34  ? -33.189 -5.500  -13.438 1.00 61.65  ? 49  GLU   B CD  1 
ATOM   723  O OE1 . GLU   B 2 34  ? -33.536 -5.995  -12.376 1.00 62.19  ? 49  GLU   B OE1 1 
ATOM   724  O OE2 . GLU   B 2 34  ? -32.314 -6.064  -14.216 1.00 63.33  ? 49  GLU   B OE2 1 
ATOM   725  N N   . GLY   B 2 35  ? -34.060 0.646   -12.616 1.00 55.37  ? 50  GLY   B N   1 
ATOM   726  C CA  . GLY   B 2 35  ? -34.291 1.744   -11.663 1.00 54.40  ? 50  GLY   B CA  1 
ATOM   727  C C   . GLY   B 2 35  ? -33.046 2.006   -10.825 1.00 52.89  ? 50  GLY   B C   1 
ATOM   728  O O   . GLY   B 2 35  ? -33.075 2.932   -10.044 1.00 51.95  ? 50  GLY   B O   1 
ATOM   729  N N   . VAL   B 2 36  ? -31.964 1.273   -11.081 1.00 51.62  ? 51  VAL   B N   1 
ATOM   730  C CA  . VAL   B 2 36  ? -30.683 1.377   -10.346 1.00 50.97  ? 51  VAL   B CA  1 
ATOM   731  C C   . VAL   B 2 36  ? -29.605 1.910   -11.279 1.00 49.66  ? 51  VAL   B C   1 
ATOM   732  O O   . VAL   B 2 36  ? -29.492 1.426   -12.428 1.00 50.60  ? 51  VAL   B O   1 
ATOM   733  C CB  . VAL   B 2 36  ? -30.293 0.043   -9.649  1.00 51.45  ? 51  VAL   B CB  1 
ATOM   734  C CG1 . VAL   B 2 36  ? -28.899 0.113   -9.008  1.00 51.23  ? 51  VAL   B CG1 1 
ATOM   735  C CG2 . VAL   B 2 36  ? -31.304 -0.309  -8.543  1.00 52.05  ? 51  VAL   B CG2 1 
ATOM   736  N N   . PHE   B 2 37  ? -28.840 2.869   -10.803 1.00 48.47  ? 52  PHE   B N   1 
ATOM   737  C CA  . PHE   B 2 37  ? -27.678 3.439   -11.506 1.00 48.13  ? 52  PHE   B CA  1 
ATOM   738  C C   . PHE   B 2 37  ? -26.416 2.748   -10.990 1.00 47.93  ? 52  PHE   B C   1 
ATOM   739  O O   . PHE   B 2 37  ? -26.175 2.813   -9.784  1.00 47.67  ? 52  PHE   B O   1 
ATOM   740  C CB  . PHE   B 2 37  ? -27.610 4.959   -11.325 1.00 47.90  ? 52  PHE   B CB  1 
ATOM   741  C CG  . PHE   B 2 37  ? -26.625 5.560   -12.291 1.00 48.05  ? 52  PHE   B CG  1 
ATOM   742  C CD1 . PHE   B 2 37  ? -26.846 5.450   -13.648 1.00 48.88  ? 52  PHE   B CD1 1 
ATOM   743  C CD2 . PHE   B 2 37  ? -25.462 6.158   -11.853 1.00 47.91  ? 52  PHE   B CD2 1 
ATOM   744  C CE1 . PHE   B 2 37  ? -25.902 5.914   -14.565 1.00 48.91  ? 52  PHE   B CE1 1 
ATOM   745  C CE2 . PHE   B 2 37  ? -24.522 6.637   -12.752 1.00 48.14  ? 52  PHE   B CE2 1 
ATOM   746  C CZ  . PHE   B 2 37  ? -24.757 6.543   -14.111 1.00 48.50  ? 52  PHE   B CZ  1 
ATOM   747  N N   . HIS   B 2 38  ? -25.658 2.120   -11.877 1.00 48.08  ? 53  HIS   B N   1 
ATOM   748  C CA  . HIS   B 2 38  ? -24.393 1.382   -11.615 1.00 48.02  ? 53  HIS   B CA  1 
ATOM   749  C C   . HIS   B 2 38  ? -23.203 2.169   -12.187 1.00 48.02  ? 53  HIS   B C   1 
ATOM   750  O O   . HIS   B 2 38  ? -23.210 2.493   -13.396 1.00 48.12  ? 53  HIS   B O   1 
ATOM   751  C CB  . HIS   B 2 38  ? -24.452 0.015   -12.275 1.00 48.46  ? 53  HIS   B CB  1 
ATOM   752  C CG  . HIS   B 2 38  ? -25.682 -0.757  -11.982 1.00 49.00  ? 53  HIS   B CG  1 
ATOM   753  N ND1 . HIS   B 2 38  ? -26.899 -0.425  -12.532 1.00 49.85  ? 53  HIS   B ND1 1 
ATOM   754  C CD2 . HIS   B 2 38  ? -25.891 -1.838  -11.169 1.00 49.68  ? 53  HIS   B CD2 1 
ATOM   755  C CE1 . HIS   B 2 38  ? -27.811 -1.289  -12.128 1.00 50.20  ? 53  HIS   B CE1 1 
ATOM   756  N NE2 . HIS   B 2 38  ? -27.227 -2.149  -11.252 1.00 50.22  ? 53  HIS   B NE2 1 
ATOM   757  N N   . THR   B 2 39  ? -22.217 2.520   -11.361 1.00 47.79  ? 54  THR   B N   1 
ATOM   758  C CA  . THR   B 2 39  ? -20.975 3.106   -11.908 1.00 48.48  ? 54  THR   B CA  1 
ATOM   759  C C   . THR   B 2 39  ? -19.795 2.541   -11.124 1.00 48.63  ? 54  THR   B C   1 
ATOM   760  O O   . THR   B 2 39  ? -20.045 1.673   -10.219 1.00 48.05  ? 54  THR   B O   1 
ATOM   761  C CB  . THR   B 2 39  ? -21.086 4.637   -11.985 1.00 48.38  ? 54  THR   B CB  1 
ATOM   762  O OG1 . THR   B 2 39  ? -19.958 5.193   -12.716 1.00 48.52  ? 54  THR   B OG1 1 
ATOM   763  C CG2 . THR   B 2 39  ? -21.196 5.257   -10.624 1.00 47.34  ? 54  THR   B CG2 1 
ATOM   764  N N   . MET   B 2 40  ? -18.589 3.039   -11.402 1.00 49.71  ? 55  MET   B N   1 
ATOM   765  C CA  . MET   B 2 40  ? -17.385 2.679   -10.623 1.00 50.99  ? 55  MET   B CA  1 
ATOM   766  C C   . MET   B 2 40  ? -17.231 3.649   -9.444  1.00 51.09  ? 55  MET   B C   1 
ATOM   767  O O   . MET   B 2 40  ? -17.578 4.857   -9.573  1.00 50.76  ? 55  MET   B O   1 
ATOM   768  C CB  . MET   B 2 40  ? -16.182 2.643   -11.548 1.00 53.84  ? 55  MET   B CB  1 
ATOM   769  C CG  . MET   B 2 40  ? -16.514 1.816   -12.845 1.00 54.30  ? 55  MET   B CG  1 
ATOM   770  S SD  . MET   B 2 40  ? -15.195 0.717   -13.105 1.00 61.02  ? 55  MET   B SD  1 
ATOM   771  C CE  . MET   B 2 40  ? -15.652 -0.755  -12.203 1.00 59.90  ? 55  MET   B CE  1 
ATOM   772  N N   A TRP   B 2 41  ? -16.742 3.136   -8.309  0.23 51.14  ? 56  TRP   B N   1 
ATOM   773  N N   B TRP   B 2 41  ? -16.752 3.145   -8.302  0.25 50.22  ? 56  TRP   B N   1 
ATOM   774  N N   C TRP   B 2 41  ? -16.740 3.135   -8.309  0.25 51.14  ? 56  TRP   B N   1 
ATOM   775  N N   D TRP   B 2 41  ? -16.751 3.145   -8.303  0.27 50.22  ? 56  TRP   B N   1 
ATOM   776  C CA  A TRP   B 2 41  ? -16.607 3.909   -7.050  0.23 51.09  ? 56  TRP   B CA  1 
ATOM   777  C CA  B TRP   B 2 41  ? -16.650 3.945   -7.058  0.25 49.61  ? 56  TRP   B CA  1 
ATOM   778  C CA  C TRP   B 2 41  ? -16.609 3.906   -7.049  0.25 51.09  ? 56  TRP   B CA  1 
ATOM   779  C CA  D TRP   B 2 41  ? -16.653 3.942   -7.058  0.27 49.62  ? 56  TRP   B CA  1 
ATOM   780  C C   A TRP   B 2 41  ? -15.732 5.147   -7.300  0.23 51.13  ? 56  TRP   B C   1 
ATOM   781  C C   B TRP   B 2 41  ? -15.738 5.160   -7.302  0.25 50.12  ? 56  TRP   B C   1 
ATOM   782  C C   C TRP   B 2 41  ? -15.740 5.147   -7.296  0.25 51.14  ? 56  TRP   B C   1 
ATOM   783  C C   D TRP   B 2 41  ? -15.746 5.161   -7.297  0.27 50.13  ? 56  TRP   B C   1 
ATOM   784  O O   A TRP   B 2 41  ? -16.092 6.236   -6.814  0.23 50.92  ? 56  TRP   B O   1 
ATOM   785  O O   B TRP   B 2 41  ? -16.075 6.257   -6.817  0.25 49.96  ? 56  TRP   B O   1 
ATOM   786  O O   C TRP   B 2 41  ? -16.102 6.234   -6.811  0.25 50.94  ? 56  TRP   B O   1 
ATOM   787  O O   D TRP   B 2 41  ? -16.085 6.254   -6.813  0.27 49.98  ? 56  TRP   B O   1 
ATOM   788  C CB  A TRP   B 2 41  ? -16.064 3.048   -5.894  0.23 51.27  ? 56  TRP   B CB  1 
ATOM   789  C CB  B TRP   B 2 41  ? -16.188 3.098   -5.858  0.25 48.82  ? 56  TRP   B CB  1 
ATOM   790  C CB  C TRP   B 2 41  ? -16.062 3.046   -5.894  0.25 51.27  ? 56  TRP   B CB  1 
ATOM   791  C CB  D TRP   B 2 41  ? -16.189 3.097   -5.857  0.27 48.82  ? 56  TRP   B CB  1 
ATOM   792  C CG  A TRP   B 2 41  ? -16.152 3.770   -4.585  0.23 51.21  ? 56  TRP   B CG  1 
ATOM   793  C CG  B TRP   B 2 41  ? -16.107 3.923   -4.612  0.25 47.88  ? 56  TRP   B CG  1 
ATOM   794  C CG  C TRP   B 2 41  ? -16.151 3.768   -4.585  0.25 51.21  ? 56  TRP   B CG  1 
ATOM   795  C CG  D TRP   B 2 41  ? -16.108 3.922   -4.611  0.27 47.87  ? 56  TRP   B CG  1 
ATOM   796  C CD1 A TRP   B 2 41  ? -17.186 3.730   -3.697  0.23 51.07  ? 56  TRP   B CD1 1 
ATOM   797  C CD1 B TRP   B 2 41  ? -15.065 4.718   -4.233  0.25 47.72  ? 56  TRP   B CD1 1 
ATOM   798  C CD1 C TRP   B 2 41  ? -17.186 3.730   -3.698  0.25 51.06  ? 56  TRP   B CD1 1 
ATOM   799  C CD1 D TRP   B 2 41  ? -15.066 4.716   -4.231  0.27 47.71  ? 56  TRP   B CD1 1 
ATOM   800  C CD2 A TRP   B 2 41  ? -15.198 4.707   -4.050  0.23 51.57  ? 56  TRP   B CD2 1 
ATOM   801  C CD2 B TRP   B 2 41  ? -17.129 4.106   -3.619  0.25 47.28  ? 56  TRP   B CD2 1 
ATOM   802  C CD2 C TRP   B 2 41  ? -15.196 4.706   -4.051  0.25 51.57  ? 56  TRP   B CD2 1 
ATOM   803  C CD2 D TRP   B 2 41  ? -17.131 4.106   -3.618  0.27 47.27  ? 56  TRP   B CD2 1 
ATOM   804  N NE1 A TRP   B 2 41  ? -16.936 4.570   -2.645  0.23 51.07  ? 56  TRP   B NE1 1 
ATOM   805  N NE1 B TRP   B 2 41  ? -15.360 5.381   -3.078  0.25 46.79  ? 56  TRP   B NE1 1 
ATOM   806  N NE1 C TRP   B 2 41  ? -16.936 4.572   -2.647  0.25 51.07  ? 56  TRP   B NE1 1 
ATOM   807  N NE1 D TRP   B 2 41  ? -15.362 5.380   -3.078  0.27 46.78  ? 56  TRP   B NE1 1 
ATOM   808  C CE2 A TRP   B 2 41  ? -15.726 5.184   -2.835  0.23 51.29  ? 56  TRP   B CE2 1 
ATOM   809  C CE2 B TRP   B 2 41  ? -16.619 5.024   -2.672  0.25 46.87  ? 56  TRP   B CE2 1 
ATOM   810  C CE2 C TRP   B 2 41  ? -15.725 5.184   -2.836  0.25 51.29  ? 56  TRP   B CE2 1 
ATOM   811  C CE2 D TRP   B 2 41  ? -16.621 5.024   -2.671  0.27 46.86  ? 56  TRP   B CE2 1 
ATOM   812  C CE3 A TRP   B 2 41  ? -13.956 5.192   -4.482  0.23 52.22  ? 56  TRP   B CE3 1 
ATOM   813  C CE3 B TRP   B 2 41  ? -18.421 3.601   -3.438  0.25 47.11  ? 56  TRP   B CE3 1 
ATOM   814  C CE3 C TRP   B 2 41  ? -13.953 5.190   -4.481  0.25 52.22  ? 56  TRP   B CE3 1 
ATOM   815  C CE3 D TRP   B 2 41  ? -18.424 3.602   -3.437  0.27 47.10  ? 56  TRP   B CE3 1 
ATOM   816  C CZ2 A TRP   B 2 41  ? -15.043 6.102   -2.037  0.23 51.83  ? 56  TRP   B CZ2 1 
ATOM   817  C CZ2 B TRP   B 2 41  ? -17.346 5.416   -1.547  0.25 46.81  ? 56  TRP   B CZ2 1 
ATOM   818  C CZ2 C TRP   B 2 41  ? -15.044 6.103   -2.038  0.25 51.83  ? 56  TRP   B CZ2 1 
ATOM   819  C CZ2 D TRP   B 2 41  ? -17.348 5.417   -1.547  0.27 46.78  ? 56  TRP   B CZ2 1 
ATOM   820  C CZ3 A TRP   B 2 41  ? -13.285 6.105   -3.696  0.23 52.22  ? 56  TRP   B CZ3 1 
ATOM   821  C CZ3 B TRP   B 2 41  ? -19.134 3.985   -2.316  0.25 47.05  ? 56  TRP   B CZ3 1 
ATOM   822  C CZ3 C TRP   B 2 41  ? -13.283 6.103   -3.695  0.25 52.21  ? 56  TRP   B CZ3 1 
ATOM   823  C CZ3 D TRP   B 2 41  ? -19.137 3.987   -2.315  0.27 47.02  ? 56  TRP   B CZ3 1 
ATOM   824  C CH2 A TRP   B 2 41  ? -13.822 6.551   -2.492  0.23 52.07  ? 56  TRP   B CH2 1 
ATOM   825  C CH2 B TRP   B 2 41  ? -18.603 4.880   -1.385  0.25 46.76  ? 56  TRP   B CH2 1 
ATOM   826  C CH2 C TRP   B 2 41  ? -13.822 6.550   -2.493  0.25 52.08  ? 56  TRP   B CH2 1 
ATOM   827  C CH2 D TRP   B 2 41  ? -18.606 4.881   -1.383  0.27 46.72  ? 56  TRP   B CH2 1 
ATOM   828  N N   A HIS   B 2 42  ? -14.621 5.000   -8.027  0.23 51.33  ? 57  HIS   B N   1 
ATOM   829  N N   B HIS   B 2 42  ? -14.625 4.999   -8.025  0.25 50.95  ? 57  HIS   B N   1 
ATOM   830  N N   C HIS   B 2 42  ? -14.632 5.023   -8.011  0.25 51.36  ? 57  HIS   B N   1 
ATOM   831  N N   D HIS   B 2 42  ? -14.636 5.022   -8.010  0.27 50.98  ? 57  HIS   B N   1 
ATOM   832  C CA  A HIS   B 2 42  ? -13.611 6.089   -8.180  0.23 51.94  ? 57  HIS   B CA  1 
ATOM   833  C CA  B HIS   B 2 42  ? -13.612 6.086   -8.181  0.25 51.76  ? 57  HIS   B CA  1 
ATOM   834  C CA  C HIS   B 2 42  ? -13.643 6.132   -8.124  0.25 51.93  ? 57  HIS   B CA  1 
ATOM   835  C CA  D HIS   B 2 42  ? -13.644 6.129   -8.124  0.27 51.75  ? 57  HIS   B CA  1 
ATOM   836  C C   A HIS   B 2 42  ? -14.151 7.256   -9.042  0.23 52.38  ? 57  HIS   B C   1 
ATOM   837  C C   B HIS   B 2 42  ? -14.151 7.254   -9.042  0.25 52.31  ? 57  HIS   B C   1 
ATOM   838  C C   C HIS   B 2 42  ? -14.228 7.310   -8.934  0.25 52.35  ? 57  HIS   B C   1 
ATOM   839  C C   D HIS   B 2 42  ? -14.228 7.309   -8.934  0.27 52.28  ? 57  HIS   B C   1 
ATOM   840  O O   A HIS   B 2 42  ? -13.434 8.301   -9.146  0.23 53.05  ? 57  HIS   B O   1 
ATOM   841  O O   B HIS   B 2 42  ? -13.432 8.300   -9.146  0.25 53.02  ? 57  HIS   B O   1 
ATOM   842  O O   C HIS   B 2 42  ? -13.658 8.438   -8.839  0.25 52.94  ? 57  HIS   B O   1 
ATOM   843  O O   D HIS   B 2 42  ? -13.658 8.437   -8.838  0.27 52.91  ? 57  HIS   B O   1 
ATOM   844  C CB  A HIS   B 2 42  ? -12.296 5.544   -8.741  0.23 52.40  ? 57  HIS   B CB  1 
ATOM   845  C CB  B HIS   B 2 42  ? -12.297 5.542   -8.741  0.25 52.31  ? 57  HIS   B CB  1 
ATOM   846  C CB  C HIS   B 2 42  ? -12.315 5.615   -8.677  0.25 52.35  ? 57  HIS   B CB  1 
ATOM   847  C CB  D HIS   B 2 42  ? -12.315 5.613   -8.677  0.27 52.27  ? 57  HIS   B CB  1 
ATOM   848  C CG  A HIS   B 2 42  ? -12.340 5.290   -10.206 0.23 52.87  ? 57  HIS   B CG  1 
ATOM   849  C CG  B HIS   B 2 42  ? -12.340 5.289   -10.206 0.25 52.82  ? 57  HIS   B CG  1 
ATOM   850  C CG  C HIS   B 2 42  ? -12.325 5.394   -10.148 0.25 52.81  ? 57  HIS   B CG  1 
ATOM   851  C CG  D HIS   B 2 42  ? -12.326 5.393   -10.148 0.27 52.76  ? 57  HIS   B CG  1 
ATOM   852  N ND1 A HIS   B 2 42  ? -12.384 4.015   -10.731 0.23 53.07  ? 57  HIS   B ND1 1 
ATOM   853  N ND1 B HIS   B 2 42  ? -12.384 4.014   -10.731 0.25 53.05  ? 57  HIS   B ND1 1 
ATOM   854  N ND1 C HIS   B 2 42  ? -12.220 4.134   -10.704 0.25 53.06  ? 57  HIS   B ND1 1 
ATOM   855  N ND1 D HIS   B 2 42  ? -12.220 4.133   -10.704 0.27 53.03  ? 57  HIS   B ND1 1 
ATOM   856  C CD2 A HIS   B 2 42  ? -12.337 6.142   -11.258 0.23 53.16  ? 57  HIS   B CD2 1 
ATOM   857  C CD2 B HIS   B 2 42  ? -12.337 6.141   -11.258 0.25 53.14  ? 57  HIS   B CD2 1 
ATOM   858  C CD2 C HIS   B 2 42  ? -12.410 6.265   -11.179 0.25 53.10  ? 57  HIS   B CD2 1 
ATOM   859  C CD2 D HIS   B 2 42  ? -12.410 6.265   -11.179 0.27 53.08  ? 57  HIS   B CD2 1 
ATOM   860  C CE1 A HIS   B 2 42  ? -12.404 4.093   -12.048 0.23 53.45  ? 57  HIS   B CE1 1 
ATOM   861  C CE1 B HIS   B 2 42  ? -12.403 4.093   -12.048 0.25 53.43  ? 57  HIS   B CE1 1 
ATOM   862  C CE1 C HIS   B 2 42  ? -12.241 4.242   -12.019 0.25 53.40  ? 57  HIS   B CE1 1 
ATOM   863  C CE1 D HIS   B 2 42  ? -12.240 4.242   -12.020 0.27 53.39  ? 57  HIS   B CE1 1 
ATOM   864  N NE2 A HIS   B 2 42  ? -12.386 5.383   -12.389 0.23 53.48  ? 57  HIS   B NE2 1 
ATOM   865  N NE2 B HIS   B 2 42  ? -12.385 5.383   -12.389 0.25 53.46  ? 57  HIS   B NE2 1 
ATOM   866  N NE2 C HIS   B 2 42  ? -12.367 5.535   -12.329 0.25 53.38  ? 57  HIS   B NE2 1 
ATOM   867  N NE2 D HIS   B 2 42  ? -12.367 5.534   -12.328 0.27 53.36  ? 57  HIS   B NE2 1 
ATOM   868  N N   . VAL   B 2 43  ? -15.319 7.073   -9.684  1.00 52.13  ? 58  VAL   B N   1 
ATOM   869  C CA  . VAL   B 2 43  ? -16.003 8.136   -10.476 1.00 52.41  ? 58  VAL   B CA  1 
ATOM   870  C C   . VAL   B 2 43  ? -16.713 9.117   -9.534  1.00 52.32  ? 58  VAL   B C   1 
ATOM   871  O O   . VAL   B 2 43  ? -16.542 10.329  -9.770  1.00 53.28  ? 58  VAL   B O   1 
ATOM   872  C CB  . VAL   B 2 43  ? -16.979 7.484   -11.471 1.00 52.72  ? 58  VAL   B CB  1 
ATOM   873  C CG1 . VAL   B 2 43  ? -17.905 8.483   -12.164 1.00 53.40  ? 58  VAL   B CG1 1 
ATOM   874  C CG2 . VAL   B 2 43  ? -16.242 6.667   -12.522 1.00 53.41  ? 58  VAL   B CG2 1 
ATOM   875  N N   . THR   B 2 44  ? -17.534 8.632   -8.588  1.00 51.13  ? 59  THR   B N   1 
ATOM   876  C CA  . THR   B 2 44  ? -18.398 9.471   -7.701  1.00 51.00  ? 59  THR   B CA  1 
ATOM   877  C C   . THR   B 2 44  ? -17.772 9.650   -6.308  1.00 51.55  ? 59  THR   B C   1 
ATOM   878  O O   . THR   B 2 44  ? -18.128 10.669  -5.593  1.00 51.36  ? 59  THR   B O   1 
ATOM   879  C CB  . THR   B 2 44  ? -19.834 8.928   -7.620  1.00 50.34  ? 59  THR   B CB  1 
ATOM   880  O OG1 . THR   B 2 44  ? -19.861 7.651   -6.969  1.00 48.92  ? 59  THR   B OG1 1 
ATOM   881  C CG2 . THR   B 2 44  ? -20.432 8.763   -9.012  1.00 51.01  ? 59  THR   B CG2 1 
ATOM   882  N N   . LYS   B 2 45  ? -16.885 8.727   -5.940  1.00 52.42  ? 60  LYS   B N   1 
ATOM   883  C CA  . LYS   B 2 45  ? -16.442 8.484   -4.541  1.00 54.33  ? 60  LYS   B CA  1 
ATOM   884  C C   . LYS   B 2 45  ? -17.649 8.347   -3.598  1.00 53.67  ? 60  LYS   B C   1 
ATOM   885  O O   . LYS   B 2 45  ? -17.512 8.757   -2.403  1.00 53.68  ? 60  LYS   B O   1 
ATOM   886  C CB  . LYS   B 2 45  ? -15.606 9.652   -4.014  1.00 56.36  ? 60  LYS   B CB  1 
ATOM   887  C CG  . LYS   B 2 45  ? -14.724 10.334  -5.028  1.00 58.82  ? 60  LYS   B CG  1 
ATOM   888  C CD  . LYS   B 2 45  ? -13.374 9.744   -5.118  1.00 60.68  ? 60  LYS   B CD  1 
ATOM   889  C CE  . LYS   B 2 45  ? -12.437 10.731  -5.784  1.00 62.71  ? 60  LYS   B CE  1 
ATOM   890  N NZ  . LYS   B 2 45  ? -11.827 10.124  -6.989  1.00 64.11  ? 60  LYS   B NZ  1 
ATOM   891  N N   . GLY   B 2 46  ? -18.784 7.826   -4.065  1.00 52.60  ? 61  GLY   B N   1 
ATOM   892  C CA  . GLY   B 2 46  ? -19.957 7.611   -3.202  1.00 53.11  ? 61  GLY   B CA  1 
ATOM   893  C C   . GLY   B 2 46  ? -20.807 8.860   -3.028  1.00 54.28  ? 61  GLY   B C   1 
ATOM   894  O O   . GLY   B 2 46  ? -21.827 8.758   -2.377  1.00 53.63  ? 61  GLY   B O   1 
ATOM   895  N N   . ALA   B 2 47  ? -20.482 9.997   -3.655  1.00 56.29  ? 62  ALA   B N   1 
ATOM   896  C CA  . ALA   B 2 47  ? -21.347 11.215  -3.629  1.00 56.72  ? 62  ALA   B CA  1 
ATOM   897  C C   . ALA   B 2 47  ? -22.705 10.946  -4.304  1.00 56.32  ? 62  ALA   B C   1 
ATOM   898  O O   . ALA   B 2 47  ? -22.797 10.088  -5.188  1.00 56.32  ? 62  ALA   B O   1 
ATOM   899  C CB  . ALA   B 2 47  ? -20.659 12.379  -4.324  1.00 57.29  ? 62  ALA   B CB  1 
ATOM   900  N N   . ALA   B 2 48  ? -23.701 11.730  -3.922  1.00 56.55  ? 63  ALA   B N   1 
ATOM   901  C CA  . ALA   B 2 48  ? -25.048 11.805  -4.518  1.00 57.30  ? 63  ALA   B CA  1 
ATOM   902  C C   . ALA   B 2 48  ? -24.955 12.408  -5.921  1.00 57.86  ? 63  ALA   B C   1 
ATOM   903  O O   . ALA   B 2 48  ? -23.948 13.070  -6.225  1.00 58.98  ? 63  ALA   B O   1 
ATOM   904  C CB  . ALA   B 2 48  ? -25.955 12.631  -3.630  1.00 57.87  ? 63  ALA   B CB  1 
ATOM   905  N N   . LEU   B 2 49  ? -25.976 12.141  -6.737  1.00 58.57  ? 64  LEU   B N   1 
ATOM   906  C CA  . LEU   B 2 49  ? -26.077 12.547  -8.159  1.00 59.92  ? 64  LEU   B CA  1 
ATOM   907  C C   . LEU   B 2 49  ? -27.422 13.219  -8.406  1.00 62.13  ? 64  LEU   B C   1 
ATOM   908  O O   . LEU   B 2 49  ? -28.426 12.866  -7.747  1.00 63.54  ? 64  LEU   B O   1 
ATOM   909  C CB  . LEU   B 2 49  ? -25.940 11.332  -9.084  1.00 58.91  ? 64  LEU   B CB  1 
ATOM   910  C CG  . LEU   B 2 49  ? -24.663 10.508  -8.930  1.00 58.63  ? 64  LEU   B CG  1 
ATOM   911  C CD1 . LEU   B 2 49  ? -24.753 9.235   -9.749  1.00 57.80  ? 64  LEU   B CD1 1 
ATOM   912  C CD2 . LEU   B 2 49  ? -23.417 11.299  -9.289  1.00 59.75  ? 64  LEU   B CD2 1 
ATOM   913  N N   . ARG   B 2 50  ? -27.410 14.191  -9.299  1.00 64.87  ? 65  ARG   B N   1 
ATOM   914  C CA  . ARG   B 2 50  ? -28.619 14.856  -9.797  1.00 67.88  ? 65  ARG   B CA  1 
ATOM   915  C C   . ARG   B 2 50  ? -29.007 14.191  -11.130 1.00 69.27  ? 65  ARG   B C   1 
ATOM   916  O O   . ARG   B 2 50  ? -28.093 13.814  -11.914 1.00 66.48  ? 65  ARG   B O   1 
ATOM   917  C CB  . ARG   B 2 50  ? -28.246 16.334  -9.878  1.00 73.19  ? 65  ARG   B CB  1 
ATOM   918  C CG  . ARG   B 2 50  ? -29.370 17.241  -10.349 1.00 78.49  ? 65  ARG   B CG  1 
ATOM   919  C CD  . ARG   B 2 50  ? -29.090 18.703  -10.055 1.00 81.07  ? 65  ARG   B CD  1 
ATOM   920  N NE  . ARG   B 2 50  ? -27.755 19.148  -10.473 1.00 82.50  ? 65  ARG   B NE  1 
ATOM   921  C CZ  . ARG   B 2 50  ? -27.388 19.483  -11.712 1.00 83.62  ? 65  ARG   B CZ  1 
ATOM   922  N NH1 . ARG   B 2 50  ? -28.218 19.339  -12.737 1.00 82.91  ? 65  ARG   B NH1 1 
ATOM   923  N NH2 . ARG   B 2 50  ? -26.157 19.923  -11.923 1.00 85.68  ? 65  ARG   B NH2 1 
ATOM   924  N N   . SER   B 2 51  ? -30.302 13.992  -11.362 1.00 70.80  ? 66  SER   B N   1 
ATOM   925  C CA  . SER   B 2 51  ? -30.872 13.696  -12.700 1.00 75.39  ? 66  SER   B CA  1 
ATOM   926  C C   . SER   B 2 51  ? -32.039 14.656  -12.982 1.00 78.62  ? 66  SER   B C   1 
ATOM   927  O O   . SER   B 2 51  ? -33.181 14.345  -12.597 1.00 79.24  ? 66  SER   B O   1 
ATOM   928  C CB  . SER   B 2 51  ? -31.302 12.267  -12.783 1.00 74.69  ? 66  SER   B CB  1 
ATOM   929  O OG  . SER   B 2 51  ? -32.071 12.072  -13.933 1.00 73.68  ? 66  SER   B OG  1 
ATOM   930  N N   . GLY   B 2 52  ? -31.763 15.791  -13.626 1.00 81.90  ? 67  GLY   B N   1 
ATOM   931  C CA  . GLY   B 2 52  ? -32.712 16.918  -13.698 1.00 83.57  ? 67  GLY   B CA  1 
ATOM   932  C C   . GLY   B 2 52  ? -32.963 17.469  -12.311 1.00 85.44  ? 67  GLY   B C   1 
ATOM   933  O O   . GLY   B 2 52  ? -31.987 17.812  -11.642 1.00 88.64  ? 67  GLY   B O   1 
ATOM   934  N N   . GLU   B 2 53  ? -34.212 17.512  -11.858 1.00 87.68  ? 68  GLU   B N   1 
ATOM   935  C CA  . GLU   B 2 53  ? -34.530 17.953  -10.474 1.00 89.97  ? 68  GLU   B CA  1 
ATOM   936  C C   . GLU   B 2 53  ? -34.471 16.758  -9.516  1.00 87.15  ? 68  GLU   B C   1 
ATOM   937  O O   . GLU   B 2 53  ? -34.482 17.006  -8.317  1.00 88.91  ? 68  GLU   B O   1 
ATOM   938  C CB  . GLU   B 2 53  ? -35.869 18.689  -10.420 1.00 93.86  ? 68  GLU   B CB  1 
ATOM   939  C CG  . GLU   B 2 53  ? -35.728 20.172  -10.730 1.00 98.82  ? 68  GLU   B CG  1 
ATOM   940  C CD  . GLU   B 2 53  ? -34.879 20.975  -9.750  1.00 102.97 ? 68  GLU   B CD  1 
ATOM   941  O OE1 . GLU   B 2 53  ? -35.063 20.805  -8.518  1.00 105.61 ? 68  GLU   B OE1 1 
ATOM   942  O OE2 . GLU   B 2 53  ? -34.030 21.774  -10.217 1.00 103.15 ? 68  GLU   B OE2 1 
ATOM   943  N N   . GLY   B 2 54  ? -34.354 15.530  -10.031 1.00 85.08  ? 69  GLY   B N   1 
ATOM   944  C CA  . GLY   B 2 54  ? -34.266 14.295  -9.231  1.00 82.35  ? 69  GLY   B CA  1 
ATOM   945  C C   . GLY   B 2 54  ? -32.957 14.201  -8.461  1.00 78.75  ? 69  GLY   B C   1 
ATOM   946  O O   . GLY   B 2 54  ? -31.957 14.836  -8.898  1.00 76.30  ? 69  GLY   B O   1 
ATOM   947  N N   . ARG   B 2 55  ? -32.968 13.461  -7.345  1.00 74.20  ? 70  ARG   B N   1 
ATOM   948  C CA  . ARG   B 2 55  ? -31.746 13.092  -6.572  1.00 71.95  ? 70  ARG   B CA  1 
ATOM   949  C C   . ARG   B 2 55  ? -31.526 11.566  -6.608  1.00 68.73  ? 70  ARG   B C   1 
ATOM   950  O O   . ARG   B 2 55  ? -32.497 10.792  -6.511  1.00 68.58  ? 70  ARG   B O   1 
ATOM   951  C CB  . ARG   B 2 55  ? -31.828 13.618  -5.140  1.00 74.92  ? 70  ARG   B CB  1 
ATOM   952  C CG  . ARG   B 2 55  ? -30.479 13.686  -4.440  1.00 76.82  ? 70  ARG   B CG  1 
ATOM   953  C CD  . ARG   B 2 55  ? -30.610 14.132  -2.988  1.00 79.70  ? 70  ARG   B CD  1 
ATOM   954  N NE  . ARG   B 2 55  ? -29.386 13.881  -2.235  1.00 81.21  ? 70  ARG   B NE  1 
ATOM   955  C CZ  . ARG   B 2 55  ? -28.680 14.785  -1.549  1.00 85.24  ? 70  ARG   B CZ  1 
ATOM   956  N NH1 . ARG   B 2 55  ? -29.079 16.045  -1.465  1.00 87.17  ? 70  ARG   B NH1 1 
ATOM   957  N NH2 . ARG   B 2 55  ? -27.581 14.410  -0.910  1.00 86.31  ? 70  ARG   B NH2 1 
ATOM   958  N N   . LEU   B 2 56  ? -30.286 11.127  -6.837  1.00 63.35  ? 71  LEU   B N   1 
ATOM   959  C CA  . LEU   B 2 56  ? -29.944 9.688   -6.776  1.00 61.21  ? 71  LEU   B CA  1 
ATOM   960  C C   . LEU   B 2 56  ? -29.047 9.507   -5.547  1.00 58.58  ? 71  LEU   B C   1 
ATOM   961  O O   . LEU   B 2 56  ? -27.982 10.159  -5.513  1.00 57.60  ? 71  LEU   B O   1 
ATOM   962  C CB  . LEU   B 2 56  ? -29.217 9.219   -8.055  1.00 60.05  ? 71  LEU   B CB  1 
ATOM   963  C CG  . LEU   B 2 56  ? -29.941 9.255   -9.410  1.00 61.78  ? 71  LEU   B CG  1 
ATOM   964  C CD1 . LEU   B 2 56  ? -29.277 8.262   -10.352 1.00 60.73  ? 71  LEU   B CD1 1 
ATOM   965  C CD2 . LEU   B 2 56  ? -31.426 8.923   -9.323  1.00 62.70  ? 71  LEU   B CD2 1 
ATOM   966  N N   . ASP   B 2 57  ? -29.451 8.671   -4.583  1.00 57.40  ? 72  ASP   B N   1 
ATOM   967  C CA  . ASP   B 2 57  ? -28.622 8.401   -3.374  1.00 56.55  ? 72  ASP   B CA  1 
ATOM   968  C C   . ASP   B 2 57  ? -27.867 7.081   -3.511  1.00 54.00  ? 72  ASP   B C   1 
ATOM   969  O O   . ASP   B 2 57  ? -28.424 6.066   -3.969  1.00 53.58  ? 72  ASP   B O   1 
ATOM   970  C CB  . ASP   B 2 57  ? -29.489 8.425   -2.126  1.00 59.03  ? 72  ASP   B CB  1 
ATOM   971  C CG  . ASP   B 2 57  ? -30.045 9.825   -1.869  1.00 61.80  ? 72  ASP   B CG  1 
ATOM   972  O OD1 . ASP   B 2 57  ? -29.293 10.817  -2.076  1.00 63.52  ? 72  ASP   B OD1 1 
ATOM   973  O OD2 . ASP   B 2 57  ? -31.226 9.919   -1.553  1.00 63.93  ? 72  ASP   B OD2 1 
ATOM   974  N N   . PRO   B 2 58  ? -26.578 7.041   -3.093  1.00 51.68  ? 73  PRO   B N   1 
ATOM   975  C CA  . PRO   B 2 58  ? -25.816 5.789   -3.069  1.00 50.86  ? 73  PRO   B CA  1 
ATOM   976  C C   . PRO   B 2 58  ? -26.575 4.761   -2.196  1.00 49.90  ? 73  PRO   B C   1 
ATOM   977  O O   . PRO   B 2 58  ? -27.343 5.142   -1.322  1.00 50.22  ? 73  PRO   B O   1 
ATOM   978  C CB  . PRO   B 2 58  ? -24.465 6.190   -2.454  1.00 50.66  ? 73  PRO   B CB  1 
ATOM   979  C CG  . PRO   B 2 58  ? -24.811 7.418   -1.615  1.00 50.91  ? 73  PRO   B CG  1 
ATOM   980  C CD  . PRO   B 2 58  ? -25.826 8.151   -2.471  1.00 51.67  ? 73  PRO   B CD  1 
ATOM   981  N N   . TYR   B 2 59  ? -26.466 3.481   -2.536  1.00 48.93  ? 74  TYR   B N   1 
ATOM   982  C CA  . TYR   B 2 59  ? -27.230 2.396   -1.894  1.00 49.06  ? 74  TYR   B CA  1 
ATOM   983  C C   . TYR   B 2 59  ? -26.260 1.318   -1.436  1.00 48.14  ? 74  TYR   B C   1 
ATOM   984  O O   . TYR   B 2 59  ? -26.494 0.732   -0.404  1.00 48.47  ? 74  TYR   B O   1 
ATOM   985  C CB  . TYR   B 2 59  ? -28.270 1.811   -2.846  1.00 49.31  ? 74  TYR   B CB  1 
ATOM   986  C CG  . TYR   B 2 59  ? -29.150 0.759   -2.211  1.00 49.30  ? 74  TYR   B CG  1 
ATOM   987  C CD1 . TYR   B 2 59  ? -28.704 -0.544  -2.111  1.00 49.72  ? 74  TYR   B CD1 1 
ATOM   988  C CD2 . TYR   B 2 59  ? -30.470 1.054   -1.763  1.00 50.20  ? 74  TYR   B CD2 1 
ATOM   989  C CE1 . TYR   B 2 59  ? -29.530 -1.537  -1.574  1.00 50.59  ? 74  TYR   B CE1 1 
ATOM   990  C CE2 . TYR   B 2 59  ? -31.309 0.070   -1.207  1.00 51.52  ? 74  TYR   B CE2 1 
ATOM   991  C CZ  . TYR   B 2 59  ? -30.843 -1.242  -1.121  1.00 51.38  ? 74  TYR   B CZ  1 
ATOM   992  O OH  . TYR   B 2 59  ? -31.583 -2.295  -0.622  1.00 52.20  ? 74  TYR   B OH  1 
ATOM   993  N N   . TRP   B 2 60  ? -25.310 1.003   -2.284  1.00 46.92  ? 75  TRP   B N   1 
ATOM   994  C CA  . TRP   B 2 60  ? -24.285 -0.034  -2.051  1.00 46.88  ? 75  TRP   B CA  1 
ATOM   995  C C   . TRP   B 2 60  ? -22.978 0.407   -2.704  1.00 46.63  ? 75  TRP   B C   1 
ATOM   996  O O   . TRP   B 2 60  ? -22.997 0.891   -3.917  1.00 47.02  ? 75  TRP   B O   1 
ATOM   997  C CB  . TRP   B 2 60  ? -24.727 -1.379  -2.615  1.00 47.32  ? 75  TRP   B CB  1 
ATOM   998  C CG  . TRP   B 2 60  ? -23.618 -2.381  -2.572  1.00 47.35  ? 75  TRP   B CG  1 
ATOM   999  C CD1 . TRP   B 2 60  ? -23.240 -3.090  -1.455  1.00 47.36  ? 75  TRP   B CD1 1 
ATOM   1000 C CD2 . TRP   B 2 60  ? -22.653 -2.675  -3.600  1.00 47.39  ? 75  TRP   B CD2 1 
ATOM   1001 N NE1 . TRP   B 2 60  ? -22.145 -3.862  -1.757  1.00 47.43  ? 75  TRP   B NE1 1 
ATOM   1002 C CE2 . TRP   B 2 60  ? -21.752 -3.618  -3.053  1.00 47.47  ? 75  TRP   B CE2 1 
ATOM   1003 C CE3 . TRP   B 2 60  ? -22.474 -2.291  -4.945  1.00 47.45  ? 75  TRP   B CE3 1 
ATOM   1004 C CZ2 . TRP   B 2 60  ? -20.697 -4.164  -3.792  1.00 47.62  ? 75  TRP   B CZ2 1 
ATOM   1005 C CZ3 . TRP   B 2 60  ? -21.420 -2.802  -5.668  1.00 47.60  ? 75  TRP   B CZ3 1 
ATOM   1006 C CH2 . TRP   B 2 60  ? -20.561 -3.754  -5.112  1.00 47.71  ? 75  TRP   B CH2 1 
ATOM   1007 N N   . GLY   B 2 61  ? -21.864 0.110   -2.050  1.00 46.46  ? 76  GLY   B N   1 
ATOM   1008 C CA  . GLY   B 2 61  ? -20.566 0.276   -2.720  1.00 46.67  ? 76  GLY   B CA  1 
ATOM   1009 C C   . GLY   B 2 61  ? -19.434 -0.363  -1.986  1.00 46.92  ? 76  GLY   B C   1 
ATOM   1010 O O   . GLY   B 2 61  ? -19.616 -0.688  -0.777  1.00 47.94  ? 76  GLY   B O   1 
ATOM   1011 N N   . ASP   B 2 62  ? -18.313 -0.475  -2.678  1.00 47.89  ? 77  ASP   B N   1 
ATOM   1012 C CA  . ASP   B 2 62  ? -17.108 -1.207  -2.220  1.00 49.31  ? 77  ASP   B CA  1 
ATOM   1013 C C   . ASP   B 2 62  ? -15.922 -0.615  -2.965  1.00 48.84  ? 77  ASP   B C   1 
ATOM   1014 O O   . ASP   B 2 62  ? -15.819 -0.871  -4.178  1.00 49.53  ? 77  ASP   B O   1 
ATOM   1015 C CB  . ASP   B 2 62  ? -17.279 -2.703  -2.471  1.00 51.28  ? 77  ASP   B CB  1 
ATOM   1016 C CG  . ASP   B 2 62  ? -16.262 -3.564  -1.777  1.00 53.64  ? 77  ASP   B CG  1 
ATOM   1017 O OD1 . ASP   B 2 62  ? -15.147 -3.688  -2.241  1.00 56.54  ? 77  ASP   B OD1 1 
ATOM   1018 O OD2 . ASP   B 2 62  ? -16.619 -4.096  -0.755  1.00 58.26  ? 77  ASP   B OD2 1 
ATOM   1019 N N   . VAL   B 2 63  ? -15.021 0.060   -2.251  1.00 48.71  ? 78  VAL   B N   1 
ATOM   1020 C CA  . VAL   B 2 63  ? -13.779 0.668   -2.819  1.00 48.54  ? 78  VAL   B CA  1 
ATOM   1021 C C   . VAL   B 2 63  ? -12.908 -0.443  -3.398  1.00 49.42  ? 78  VAL   B C   1 
ATOM   1022 O O   . VAL   B 2 63  ? -12.251 -0.219  -4.423  1.00 50.75  ? 78  VAL   B O   1 
ATOM   1023 C CB  . VAL   B 2 63  ? -12.994 1.492   -1.777  1.00 48.17  ? 78  VAL   B CB  1 
ATOM   1024 C CG1 . VAL   B 2 63  ? -11.575 1.724   -2.235  1.00 49.12  ? 78  VAL   B CG1 1 
ATOM   1025 C CG2 . VAL   B 2 63  ? -13.668 2.822   -1.514  1.00 48.05  ? 78  VAL   B CG2 1 
ATOM   1026 N N   . LYS   B 2 64  ? -12.979 -1.661  -2.897  1.00 50.14  ? 79  LYS   B N   1 
ATOM   1027 C CA  . LYS   B 2 64  ? -12.019 -2.671  -3.426  1.00 51.15  ? 79  LYS   B CA  1 
ATOM   1028 C C   . LYS   B 2 64  ? -12.525 -3.257  -4.756  1.00 50.99  ? 79  LYS   B C   1 
ATOM   1029 O O   . LYS   B 2 64  ? -11.721 -3.432  -5.691  1.00 50.70  ? 79  LYS   B O   1 
ATOM   1030 C CB  . LYS   B 2 64  ? -11.716 -3.767  -2.402  1.00 52.04  ? 79  LYS   B CB  1 
ATOM   1031 C CG  . LYS   B 2 64  ? -10.726 -4.769  -2.991  1.00 53.57  ? 79  LYS   B CG  1 
ATOM   1032 C CD  . LYS   B 2 64  ? -10.128 -5.697  -1.939  1.00 54.50  ? 79  LYS   B CD  1 
ATOM   1033 C CE  . LYS   B 2 64  ? -9.227  -6.732  -2.574  1.00 56.15  ? 79  LYS   B CE  1 
ATOM   1034 N NZ  . LYS   B 2 64  ? -9.004  -7.842  -1.624  1.00 57.62  ? 79  LYS   B NZ  1 
ATOM   1035 N N   . GLN   B 2 65  ? -13.801 -3.606  -4.845  1.00 50.57  ? 80  GLN   B N   1 
ATOM   1036 C CA  . GLN   B 2 65  ? -14.396 -4.011  -6.143  1.00 50.26  ? 80  GLN   B CA  1 
ATOM   1037 C C   . GLN   B 2 65  ? -14.426 -2.800  -7.091  1.00 49.31  ? 80  GLN   B C   1 
ATOM   1038 O O   . GLN   B 2 65  ? -14.480 -3.019  -8.284  1.00 49.58  ? 80  GLN   B O   1 
ATOM   1039 C CB  . GLN   B 2 65  ? -15.825 -4.512  -5.986  1.00 51.60  ? 80  GLN   B CB  1 
ATOM   1040 C CG  . GLN   B 2 65  ? -15.965 -5.716  -5.053  1.00 53.14  ? 80  GLN   B CG  1 
ATOM   1041 C CD  . GLN   B 2 65  ? -17.408 -6.169  -4.937  1.00 54.54  ? 80  GLN   B CD  1 
ATOM   1042 O OE1 . GLN   B 2 65  ? -18.149 -6.332  -5.933  1.00 56.86  ? 80  GLN   B OE1 1 
ATOM   1043 N NE2 . GLN   B 2 65  ? -17.819 -6.434  -3.711  1.00 54.63  ? 80  GLN   B NE2 1 
ATOM   1044 N N   A ASP   B 2 66  ? -14.401 -1.586  -6.523  0.23 48.54  ? 81  ASP   B N   1 
ATOM   1045 N N   B ASP   B 2 66  ? -14.401 -1.586  -6.523  0.25 48.54  ? 81  ASP   B N   1 
ATOM   1046 N N   C ASP   B 2 66  ? -14.396 -1.581  -6.535  0.25 48.55  ? 81  ASP   B N   1 
ATOM   1047 N N   D ASP   B 2 66  ? -14.396 -1.581  -6.535  0.27 48.55  ? 81  ASP   B N   1 
ATOM   1048 C CA  A ASP   B 2 66  ? -14.441 -0.262  -7.198  0.23 48.35  ? 81  ASP   B CA  1 
ATOM   1049 C CA  B ASP   B 2 66  ? -14.441 -0.262  -7.197  0.25 48.35  ? 81  ASP   B CA  1 
ATOM   1050 C CA  C ASP   B 2 66  ? -14.437 -0.272  -7.239  0.25 48.39  ? 81  ASP   B CA  1 
ATOM   1051 C CA  D ASP   B 2 66  ? -14.437 -0.272  -7.238  0.27 48.39  ? 81  ASP   B CA  1 
ATOM   1052 C C   A ASP   B 2 66  ? -15.783 -0.112  -7.920  0.23 48.12  ? 81  ASP   B C   1 
ATOM   1053 C C   B ASP   B 2 66  ? -15.783 -0.112  -7.919  0.25 48.12  ? 81  ASP   B C   1 
ATOM   1054 C C   C ASP   B 2 66  ? -15.791 -0.123  -7.937  0.25 48.14  ? 81  ASP   B C   1 
ATOM   1055 C C   D ASP   B 2 66  ? -15.791 -0.122  -7.937  0.27 48.14  ? 81  ASP   B C   1 
ATOM   1056 O O   A ASP   B 2 66  ? -15.771 0.390   -9.075  0.23 48.37  ? 81  ASP   B O   1 
ATOM   1057 O O   B ASP   B 2 66  ? -15.770 0.390   -9.075  0.25 48.37  ? 81  ASP   B O   1 
ATOM   1058 O O   C ASP   B 2 66  ? -15.796 0.370   -9.096  0.25 48.35  ? 81  ASP   B O   1 
ATOM   1059 O O   D ASP   B 2 66  ? -15.796 0.371   -9.096  0.27 48.36  ? 81  ASP   B O   1 
ATOM   1060 C CB  A ASP   B 2 66  ? -13.268 -0.061  -8.172  0.23 48.87  ? 81  ASP   B CB  1 
ATOM   1061 C CB  B ASP   B 2 66  ? -13.268 -0.061  -8.172  0.25 48.87  ? 81  ASP   B CB  1 
ATOM   1062 C CB  C ASP   B 2 66  ? -13.288 -0.108  -8.248  0.25 48.90  ? 81  ASP   B CB  1 
ATOM   1063 C CB  D ASP   B 2 66  ? -13.288 -0.107  -8.248  0.27 48.90  ? 81  ASP   B CB  1 
ATOM   1064 C CG  A ASP   B 2 66  ? -13.179 1.340   -8.767  0.23 48.82  ? 81  ASP   B CG  1 
ATOM   1065 C CG  B ASP   B 2 66  ? -13.180 1.341   -8.766  0.25 48.82  ? 81  ASP   B CG  1 
ATOM   1066 C CG  C ASP   B 2 66  ? -13.166 1.293   -8.836  0.25 48.87  ? 81  ASP   B CG  1 
ATOM   1067 C CG  D ASP   B 2 66  ? -13.166 1.294   -8.836  0.27 48.87  ? 81  ASP   B CG  1 
ATOM   1068 O OD1 A ASP   B 2 66  ? -13.645 2.299   -8.109  0.23 48.60  ? 81  ASP   B OD1 1 
ATOM   1069 O OD1 B ASP   B 2 66  ? -13.646 2.299   -8.108  0.25 48.60  ? 81  ASP   B OD1 1 
ATOM   1070 O OD1 C ASP   B 2 66  ? -13.607 2.257   -8.176  0.25 48.64  ? 81  ASP   B OD1 1 
ATOM   1071 O OD1 D ASP   B 2 66  ? -13.608 2.257   -8.175  0.27 48.64  ? 81  ASP   B OD1 1 
ATOM   1072 O OD2 A ASP   B 2 66  ? -12.662 1.458   -9.906  0.23 49.67  ? 81  ASP   B OD2 1 
ATOM   1073 O OD2 B ASP   B 2 66  ? -12.664 1.459   -9.906  0.25 49.67  ? 81  ASP   B OD2 1 
ATOM   1074 O OD2 C ASP   B 2 66  ? -12.641 1.406   -9.975  0.25 49.72  ? 81  ASP   B OD2 1 
ATOM   1075 O OD2 D ASP   B 2 66  ? -12.642 1.407   -9.975  0.27 49.73  ? 81  ASP   B OD2 1 
ATOM   1076 N N   . LEU   B 2 67  ? -16.884 -0.499  -7.254  1.00 47.27  ? 82  LEU   B N   1 
ATOM   1077 C CA  . LEU   B 2 67  ? -18.272 -0.395  -7.807  1.00 47.31  ? 82  LEU   B CA  1 
ATOM   1078 C C   . LEU   B 2 67  ? -19.147 0.364   -6.831  1.00 46.96  ? 82  LEU   B C   1 
ATOM   1079 O O   . LEU   B 2 67  ? -18.865 0.317   -5.577  1.00 46.73  ? 82  LEU   B O   1 
ATOM   1080 C CB  . LEU   B 2 67  ? -18.841 -1.787  -8.022  1.00 47.67  ? 82  LEU   B CB  1 
ATOM   1081 C CG  . LEU   B 2 67  ? -18.156 -2.592  -9.100  1.00 48.15  ? 82  LEU   B CG  1 
ATOM   1082 C CD1 . LEU   B 2 67  ? -18.732 -3.995  -9.186  1.00 48.59  ? 82  LEU   B CD1 1 
ATOM   1083 C CD2 . LEU   B 2 67  ? -18.328 -1.853  -10.486 1.00 48.30  ? 82  LEU   B CD2 1 
ATOM   1084 N N   . VAL   B 2 68  ? -20.238 0.940   -7.333  1.00 46.97  ? 83  VAL   B N   1 
ATOM   1085 C CA  . VAL   B 2 68  ? -21.308 1.563   -6.503  1.00 46.77  ? 83  VAL   B CA  1 
ATOM   1086 C C   . VAL   B 2 68  ? -22.641 1.511   -7.269  1.00 47.01  ? 83  VAL   B C   1 
ATOM   1087 O O   . VAL   B 2 68  ? -22.667 1.592   -8.528  1.00 47.22  ? 83  VAL   B O   1 
ATOM   1088 C CB  . VAL   B 2 68  ? -20.898 3.003   -6.151  1.00 46.51  ? 83  VAL   B CB  1 
ATOM   1089 C CG1 . VAL   B 2 68  ? -20.567 3.816   -7.411  1.00 46.63  ? 83  VAL   B CG1 1 
ATOM   1090 C CG2 . VAL   B 2 68  ? -21.943 3.723   -5.328  1.00 46.39  ? 83  VAL   B CG2 1 
ATOM   1091 N N   . SER   B 2 69  ? -23.735 1.412   -6.545  1.00 47.04  ? 84  SER   B N   1 
ATOM   1092 C CA  . SER   B 2 69  ? -25.106 1.379   -7.085  1.00 47.33  ? 84  SER   B CA  1 
ATOM   1093 C C   . SER   B 2 69  ? -25.892 2.473   -6.382  1.00 47.20  ? 84  SER   B C   1 
ATOM   1094 O O   . SER   B 2 69  ? -25.614 2.765   -5.156  1.00 46.97  ? 84  SER   B O   1 
ATOM   1095 C CB  . SER   B 2 69  ? -25.707 -0.016  -6.924  1.00 47.70  ? 84  SER   B CB  1 
ATOM   1096 O OG  . SER   B 2 69  ? -26.106 -0.227  -5.554  1.00 47.65  ? 84  SER   B OG  1 
ATOM   1097 N N   . TYR   B 2 70  ? -26.848 3.061   -7.094  1.00 47.39  ? 85  TYR   B N   1 
ATOM   1098 C CA  . TYR   B 2 70  ? -27.689 4.205   -6.665  1.00 47.40  ? 85  TYR   B CA  1 
ATOM   1099 C C   . TYR   B 2 70  ? -29.142 3.755   -6.801  1.00 47.83  ? 85  TYR   B C   1 
ATOM   1100 O O   . TYR   B 2 70  ? -29.476 3.099   -7.838  1.00 48.11  ? 85  TYR   B O   1 
ATOM   1101 C CB  . TYR   B 2 70  ? -27.415 5.453   -7.517  1.00 47.32  ? 85  TYR   B CB  1 
ATOM   1102 C CG  . TYR   B 2 70  ? -26.098 6.111   -7.226  1.00 47.01  ? 85  TYR   B CG  1 
ATOM   1103 C CD1 . TYR   B 2 70  ? -24.925 5.597   -7.723  1.00 46.91  ? 85  TYR   B CD1 1 
ATOM   1104 C CD2 . TYR   B 2 70  ? -26.023 7.210   -6.364  1.00 46.89  ? 85  TYR   B CD2 1 
ATOM   1105 C CE1 . TYR   B 2 70  ? -23.698 6.161   -7.402  1.00 46.70  ? 85  TYR   B CE1 1 
ATOM   1106 C CE2 . TYR   B 2 70  ? -24.809 7.814   -6.059  1.00 46.68  ? 85  TYR   B CE2 1 
ATOM   1107 C CZ  . TYR   B 2 70  ? -23.638 7.269   -6.562  1.00 46.59  ? 85  TYR   B CZ  1 
ATOM   1108 O OH  . TYR   B 2 70  ? -22.405 7.820   -6.292  1.00 46.59  ? 85  TYR   B OH  1 
ATOM   1109 N N   . CYS   B 2 71  ? -29.927 3.984   -5.724  1.00 49.73  ? 86  CYS   B N   1 
ATOM   1110 C CA  . CYS   B 2 71  ? -31.404 3.862   -5.645  1.00 51.89  ? 86  CYS   B CA  1 
ATOM   1111 C C   . CYS   B 2 71  ? -31.727 2.380   -5.376  1.00 53.05  ? 86  CYS   B C   1 
ATOM   1112 O O   . CYS   B 2 71  ? -32.865 2.099   -5.045  1.00 54.91  ? 86  CYS   B O   1 
ATOM   1113 C CB  . CYS   B 2 71  ? -32.147 4.322   -6.897  1.00 53.78  ? 86  CYS   B CB  1 
ATOM   1114 S SG  . CYS   B 2 71  ? -31.675 6.016   -7.353  1.00 56.46  ? 86  CYS   B SG  1 
ATOM   1115 N N   . GLY   B 2 72  ? -30.740 1.470   -5.401  1.00 53.20  ? 87  GLY   B N   1 
ATOM   1116 C CA  . GLY   B 2 72  ? -31.101 0.081   -5.140  1.00 53.56  ? 87  GLY   B CA  1 
ATOM   1117 C C   . GLY   B 2 72  ? -29.880 -0.792  -5.240  1.00 53.05  ? 87  GLY   B C   1 
ATOM   1118 O O   . GLY   B 2 72  ? -28.784 -0.297  -5.504  1.00 53.12  ? 87  GLY   B O   1 
ATOM   1119 N N   . PRO   B 2 73  ? -30.085 -2.100  -4.981  1.00 52.74  ? 88  PRO   B N   1 
ATOM   1120 C CA  . PRO   B 2 73  ? -29.005 -3.117  -4.998  1.00 52.50  ? 88  PRO   B CA  1 
ATOM   1121 C C   . PRO   B 2 73  ? -28.503 -3.280  -6.437  1.00 51.50  ? 88  PRO   B C   1 
ATOM   1122 O O   . PRO   B 2 73  ? -29.346 -3.137  -7.363  1.00 53.23  ? 88  PRO   B O   1 
ATOM   1123 C CB  . PRO   B 2 73  ? -29.658 -4.384  -4.388  1.00 52.61  ? 88  PRO   B CB  1 
ATOM   1124 C CG  . PRO   B 2 73  ? -31.121 -4.244  -4.707  1.00 53.00  ? 88  PRO   B CG  1 
ATOM   1125 C CD  . PRO   B 2 73  ? -31.384 -2.748  -4.608  1.00 52.86  ? 88  PRO   B CD  1 
ATOM   1126 N N   . TRP   B 2 74  ? -27.204 -3.596  -6.573  1.00 50.99  ? 89  TRP   B N   1 
ATOM   1127 C CA  . TRP   B 2 74  ? -26.539 -4.000  -7.830  1.00 51.84  ? 89  TRP   B CA  1 
ATOM   1128 C C   . TRP   B 2 74  ? -27.415 -5.009  -8.598  1.00 53.05  ? 89  TRP   B C   1 
ATOM   1129 O O   . TRP   B 2 74  ? -27.715 -6.065  -8.017  1.00 53.14  ? 89  TRP   B O   1 
ATOM   1130 C CB  . TRP   B 2 74  ? -25.141 -4.552  -7.548  1.00 51.19  ? 89  TRP   B CB  1 
ATOM   1131 C CG  . TRP   B 2 74  ? -24.352 -4.741  -8.811  1.00 50.26  ? 89  TRP   B CG  1 
ATOM   1132 C CD1 . TRP   B 2 74  ? -24.299 -5.876  -9.565  1.00 50.40  ? 89  TRP   B CD1 1 
ATOM   1133 C CD2 . TRP   B 2 74  ? -23.525 -3.768  -9.487  1.00 49.74  ? 89  TRP   B CD2 1 
ATOM   1134 N NE1 . TRP   B 2 74  ? -23.455 -5.688  -10.625 1.00 49.98  ? 89  TRP   B NE1 1 
ATOM   1135 C CE2 . TRP   B 2 74  ? -22.980 -4.406  -10.621 1.00 49.36  ? 89  TRP   B CE2 1 
ATOM   1136 C CE3 . TRP   B 2 74  ? -23.184 -2.424  -9.251  1.00 49.30  ? 89  TRP   B CE3 1 
ATOM   1137 C CZ2 . TRP   B 2 74  ? -22.143 -3.759  -11.547 1.00 49.84  ? 89  TRP   B CZ2 1 
ATOM   1138 C CZ3 . TRP   B 2 74  ? -22.359 -1.781  -10.160 1.00 48.72  ? 89  TRP   B CZ3 1 
ATOM   1139 C CH2 . TRP   B 2 74  ? -21.844 -2.445  -11.288 1.00 49.25  ? 89  TRP   B CH2 1 
ATOM   1140 N N   . LYS   B 2 75  ? -27.797 -4.700  -9.854  1.00 53.69  ? 90  LYS   B N   1 
ATOM   1141 C CA  . LYS   B 2 75  ? -28.759 -5.530  -10.654 1.00 55.12  ? 90  LYS   B CA  1 
ATOM   1142 C C   . LYS   B 2 75  ? -28.077 -6.376  -11.739 1.00 55.82  ? 90  LYS   B C   1 
ATOM   1143 O O   . LYS   B 2 75  ? -28.712 -7.325  -12.199 1.00 57.00  ? 90  LYS   B O   1 
ATOM   1144 C CB  . LYS   B 2 75  ? -29.777 -4.633  -11.343 1.00 55.51  ? 90  LYS   B CB  1 
ATOM   1145 C CG  . LYS   B 2 75  ? -30.641 -3.827  -10.402 1.00 55.55  ? 90  LYS   B CG  1 
ATOM   1146 C CD  . LYS   B 2 75  ? -31.666 -4.699  -9.724  1.00 57.06  ? 90  LYS   B CD  1 
ATOM   1147 C CE  . LYS   B 2 75  ? -32.254 -4.028  -8.507  1.00 58.30  ? 90  LYS   B CE  1 
ATOM   1148 N NZ  . LYS   B 2 75  ? -33.655 -3.662  -8.790  1.00 59.94  ? 90  LYS   B NZ  1 
ATOM   1149 N N   . LEU   B 2 76  ? -26.829 -6.093  -12.106 1.00 56.58  ? 91  LEU   B N   1 
ATOM   1150 C CA  . LEU   B 2 76  ? -26.168 -6.667  -13.313 1.00 58.30  ? 91  LEU   B CA  1 
ATOM   1151 C C   . LEU   B 2 76  ? -25.429 -7.941  -12.927 1.00 59.73  ? 91  LEU   B C   1 
ATOM   1152 O O   . LEU   B 2 76  ? -24.521 -7.876  -12.078 1.00 58.90  ? 91  LEU   B O   1 
ATOM   1153 C CB  . LEU   B 2 76  ? -25.193 -5.633  -13.876 1.00 58.00  ? 91  LEU   B CB  1 
ATOM   1154 C CG  . LEU   B 2 76  ? -25.774 -4.222  -14.044 1.00 58.02  ? 91  LEU   B CG  1 
ATOM   1155 C CD1 . LEU   B 2 76  ? -24.753 -3.289  -14.685 1.00 57.85  ? 91  LEU   B CD1 1 
ATOM   1156 C CD2 . LEU   B 2 76  ? -27.043 -4.226  -14.887 1.00 58.79  ? 91  LEU   B CD2 1 
ATOM   1157 N N   . ASP   B 2 77  ? -25.793 -9.061  -13.537 1.00 62.46  ? 92  ASP   B N   1 
ATOM   1158 C CA  . ASP   B 2 77  ? -25.300 -10.390 -13.088 1.00 65.40  ? 92  ASP   B CA  1 
ATOM   1159 C C   . ASP   B 2 77  ? -24.777 -11.201 -14.278 1.00 64.53  ? 92  ASP   B C   1 
ATOM   1160 O O   . ASP   B 2 77  ? -24.161 -12.230 -14.054 1.00 64.87  ? 92  ASP   B O   1 
ATOM   1161 C CB  . ASP   B 2 77  ? -26.390 -11.135 -12.305 1.00 68.74  ? 92  ASP   B CB  1 
ATOM   1162 C CG  . ASP   B 2 77  ? -27.706 -11.261 -13.069 1.00 73.10  ? 92  ASP   B CG  1 
ATOM   1163 O OD1 . ASP   B 2 77  ? -27.828 -10.646 -14.192 1.00 74.23  ? 92  ASP   B OD1 1 
ATOM   1164 O OD2 . ASP   B 2 77  ? -28.615 -11.964 -12.546 1.00 76.26  ? 92  ASP   B OD2 1 
ATOM   1165 N N   . ALA   B 2 78  ? -24.941 -10.747 -15.512 1.00 63.02  ? 93  ALA   B N   1 
ATOM   1166 C CA  . ALA   B 2 78  ? -24.395 -11.493 -16.657 1.00 62.48  ? 93  ALA   B CA  1 
ATOM   1167 C C   . ALA   B 2 78  ? -22.863 -11.568 -16.493 1.00 61.40  ? 93  ALA   B C   1 
ATOM   1168 O O   . ALA   B 2 78  ? -22.253 -10.568 -15.930 1.00 59.12  ? 93  ALA   B O   1 
ATOM   1169 C CB  . ALA   B 2 78  ? -24.846 -10.842 -17.943 1.00 62.07  ? 93  ALA   B CB  1 
ATOM   1170 N N   . ALA   B 2 79  ? -22.269 -12.667 -17.020 1.00 62.31  ? 94  ALA   B N   1 
ATOM   1171 C CA  . ALA   B 2 79  ? -20.819 -12.959 -16.972 1.00 62.92  ? 94  ALA   B CA  1 
ATOM   1172 C C   . ALA   B 2 79  ? -20.246 -13.257 -18.367 1.00 63.50  ? 94  ALA   B C   1 
ATOM   1173 O O   . ALA   B 2 79  ? -20.891 -14.003 -19.121 1.00 63.82  ? 94  ALA   B O   1 
ATOM   1174 C CB  . ALA   B 2 79  ? -20.608 -14.142 -16.041 1.00 63.37  ? 94  ALA   B CB  1 
ATOM   1175 N N   . TRP   B 2 80  ? -19.024 -12.791 -18.655 1.00 63.92  ? 95  TRP   B N   1 
ATOM   1176 C CA  . TRP   B 2 80  ? -18.207 -13.272 -19.802 1.00 66.64  ? 95  TRP   B CA  1 
ATOM   1177 C C   . TRP   B 2 80  ? -18.117 -14.797 -19.765 1.00 69.26  ? 95  TRP   B C   1 
ATOM   1178 O O   . TRP   B 2 80  ? -17.847 -15.342 -18.694 1.00 69.44  ? 95  TRP   B O   1 
ATOM   1179 C CB  . TRP   B 2 80  ? -16.799 -12.664 -19.817 1.00 66.29  ? 95  TRP   B CB  1 
ATOM   1180 C CG  . TRP   B 2 80  ? -15.980 -13.068 -21.013 1.00 65.70  ? 95  TRP   B CG  1 
ATOM   1181 C CD1 . TRP   B 2 80  ? -16.404 -13.191 -22.303 1.00 66.92  ? 95  TRP   B CD1 1 
ATOM   1182 C CD2 . TRP   B 2 80  ? -14.578 -13.405 -21.026 1.00 66.15  ? 95  TRP   B CD2 1 
ATOM   1183 N NE1 . TRP   B 2 80  ? -15.370 -13.579 -23.120 1.00 67.00  ? 95  TRP   B NE1 1 
ATOM   1184 C CE2 . TRP   B 2 80  ? -14.241 -13.744 -22.362 1.00 67.15  ? 95  TRP   B CE2 1 
ATOM   1185 C CE3 . TRP   B 2 80  ? -13.584 -13.508 -20.037 1.00 65.58  ? 95  TRP   B CE3 1 
ATOM   1186 C CZ2 . TRP   B 2 80  ? -12.955 -14.132 -22.737 1.00 67.47  ? 95  TRP   B CZ2 1 
ATOM   1187 C CZ3 . TRP   B 2 80  ? -12.315 -13.901 -20.414 1.00 66.51  ? 95  TRP   B CZ3 1 
ATOM   1188 C CH2 . TRP   B 2 80  ? -12.005 -14.199 -21.755 1.00 67.36  ? 95  TRP   B CH2 1 
ATOM   1189 N N   . ASP   B 2 81  ? -18.347 -15.458 -20.893 1.00 72.71  ? 96  ASP   B N   1 
ATOM   1190 C CA  . ASP   B 2 81  ? -18.396 -16.948 -20.951 1.00 75.71  ? 96  ASP   B CA  1 
ATOM   1191 C C   . ASP   B 2 81  ? -16.958 -17.553 -21.020 1.00 76.46  ? 96  ASP   B C   1 
ATOM   1192 O O   . ASP   B 2 81  ? -16.862 -18.808 -20.856 1.00 78.67  ? 96  ASP   B O   1 
ATOM   1193 C CB  . ASP   B 2 81  ? -19.256 -17.442 -22.124 1.00 76.69  ? 96  ASP   B CB  1 
ATOM   1194 C CG  . ASP   B 2 81  ? -18.734 -17.064 -23.492 1.00 77.62  ? 96  ASP   B CG  1 
ATOM   1195 O OD1 . ASP   B 2 81  ? -17.652 -16.442 -23.561 1.00 78.24  ? 96  ASP   B OD1 1 
ATOM   1196 O OD2 . ASP   B 2 81  ? -19.435 -17.360 -24.480 1.00 79.57  ? 96  ASP   B OD2 1 
ATOM   1197 N N   . GLY   B 2 82  ? -15.938 -16.685 -21.246 1.00 75.46  ? 97  GLY   B N   1 
ATOM   1198 C CA  . GLY   B 2 82  ? -14.495 -17.007 -21.278 1.00 76.39  ? 97  GLY   B CA  1 
ATOM   1199 C C   . GLY   B 2 82  ? -13.973 -17.332 -22.678 1.00 79.42  ? 97  GLY   B C   1 
ATOM   1200 O O   . GLY   B 2 82  ? -12.770 -17.637 -22.786 1.00 78.37  ? 97  GLY   B O   1 
ATOM   1201 N N   . LEU   B 2 83  ? -14.841 -17.262 -23.699 1.00 81.34  ? 98  LEU   B N   1 
ATOM   1202 C CA  . LEU   B 2 83  ? -14.592 -17.707 -25.088 1.00 84.42  ? 98  LEU   B CA  1 
ATOM   1203 C C   . LEU   B 2 83  ? -14.896 -16.608 -26.116 1.00 83.49  ? 98  LEU   B C   1 
ATOM   1204 O O   . LEU   B 2 83  ? -14.069 -16.418 -27.046 1.00 84.76  ? 98  LEU   B O   1 
ATOM   1205 C CB  . LEU   B 2 83  ? -15.482 -18.919 -25.367 1.00 88.70  ? 98  LEU   B CB  1 
ATOM   1206 C CG  . LEU   B 2 83  ? -14.961 -20.250 -24.834 1.00 92.35  ? 98  LEU   B CG  1 
ATOM   1207 C CD1 . LEU   B 2 83  ? -16.027 -21.325 -24.949 1.00 94.80  ? 98  LEU   B CD1 1 
ATOM   1208 C CD2 . LEU   B 2 83  ? -13.710 -20.671 -25.585 1.00 94.10  ? 98  LEU   B CD2 1 
ATOM   1209 N N   . SER   B 2 84  ? -16.086 -16.010 -26.075 1.00 80.91  ? 99  SER   B N   1 
ATOM   1210 C CA  . SER   B 2 84  ? -16.607 -15.158 -27.184 1.00 78.09  ? 99  SER   B CA  1 
ATOM   1211 C C   . SER   B 2 84  ? -16.062 -13.724 -27.078 1.00 75.41  ? 99  SER   B C   1 
ATOM   1212 O O   . SER   B 2 84  ? -15.733 -13.264 -25.962 1.00 74.14  ? 99  SER   B O   1 
ATOM   1213 C CB  . SER   B 2 84  ? -18.109 -15.175 -27.221 1.00 78.14  ? 99  SER   B CB  1 
ATOM   1214 O OG  . SER   B 2 84  ? -18.646 -15.768 -26.034 1.00 80.15  ? 99  SER   B OG  1 
ATOM   1215 N N   . GLU   B 2 85  ? -15.943 -13.044 -28.211 1.00 74.52  ? 100 GLU   B N   1 
ATOM   1216 C CA  . GLU   B 2 85  ? -15.737 -11.570 -28.322 1.00 72.86  ? 100 GLU   B CA  1 
ATOM   1217 C C   . GLU   B 2 85  ? -16.987 -10.836 -27.644 1.00 69.30  ? 100 GLU   B C   1 
ATOM   1218 O O   . GLU   B 2 85  ? -18.140 -11.476 -27.235 1.00 69.97  ? 100 GLU   B O   1 
ATOM   1219 C CB  . GLU   B 2 85  ? -15.592 -11.094 -29.786 1.00 74.91  ? 100 GLU   B CB  1 
ATOM   1220 C CG  . GLU   B 2 85  ? -14.359 -11.640 -30.531 1.00 76.94  ? 100 GLU   B CG  1 
ATOM   1221 C CD  . GLU   B 2 85  ? -13.803 -10.826 -31.716 1.00 78.17  ? 100 GLU   B CD  1 
ATOM   1222 O OE1 . GLU   B 2 85  ? -14.520 -9.967  -32.277 1.00 76.69  ? 100 GLU   B OE1 1 
ATOM   1223 O OE2 . GLU   B 2 85  ? -12.617 -11.048 -32.071 1.00 80.18  ? 100 GLU   B OE2 1 
ATOM   1224 N N   . VAL   B 2 86  ? -16.624 -9.656  -27.102 1.00 66.96  ? 101 VAL   B N   1 
ATOM   1225 C CA  . VAL   B 2 86  ? -17.530 -8.695  -26.375 1.00 64.61  ? 101 VAL   B CA  1 
ATOM   1226 C C   . VAL   B 2 86  ? -17.447 -7.310  -27.019 1.00 63.10  ? 101 VAL   B C   1 
ATOM   1227 O O   . VAL   B 2 86  ? -16.555 -7.098  -27.881 1.00 64.97  ? 101 VAL   B O   1 
ATOM   1228 C CB  . VAL   B 2 86  ? -17.149 -8.611  -24.880 1.00 63.37  ? 101 VAL   B CB  1 
ATOM   1229 C CG1 . VAL   B 2 86  ? -17.110 -10.009 -24.311 1.00 63.45  ? 101 VAL   B CG1 1 
ATOM   1230 C CG2 . VAL   B 2 86  ? -15.822 -7.883  -24.706 1.00 63.28  ? 101 VAL   B CG2 1 
ATOM   1231 N N   . GLN   B 2 87  ? -18.348 -6.398  -26.571 1.00 61.00  ? 102 GLN   B N   1 
ATOM   1232 C CA  . GLN   B 2 87  ? -18.361 -4.988  -27.017 1.00 60.37  ? 102 GLN   B CA  1 
ATOM   1233 C C   . GLN   B 2 87  ? -18.244 -4.059  -25.817 1.00 58.87  ? 102 GLN   B C   1 
ATOM   1234 O O   . GLN   B 2 87  ? -19.083 -4.126  -24.913 1.00 57.80  ? 102 GLN   B O   1 
ATOM   1235 C CB  . GLN   B 2 87  ? -19.593 -4.704  -27.892 1.00 60.94  ? 102 GLN   B CB  1 
ATOM   1236 C CG  . GLN   B 2 87  ? -19.558 -5.496  -29.191 1.00 61.87  ? 102 GLN   B CG  1 
ATOM   1237 C CD  . GLN   B 2 87  ? -20.536 -5.025  -30.262 1.00 62.44  ? 102 GLN   B CD  1 
ATOM   1238 O OE1 . GLN   B 2 87  ? -21.434 -4.203  -30.037 1.00 61.75  ? 102 GLN   B OE1 1 
ATOM   1239 N NE2 . GLN   B 2 87  ? -20.381 -5.600  -31.444 1.00 62.83  ? 102 GLN   B NE2 1 
ATOM   1240 N N   . LEU   B 2 88  ? -17.183 -3.274  -25.813 1.00 57.98  ? 103 LEU   B N   1 
ATOM   1241 C CA  . LEU   B 2 88  ? -17.118 -2.073  -24.981 1.00 57.15  ? 103 LEU   B CA  1 
ATOM   1242 C C   . LEU   B 2 88  ? -18.046 -1.025  -25.599 1.00 57.54  ? 103 LEU   B C   1 
ATOM   1243 O O   . LEU   B 2 88  ? -17.750 -0.570  -26.706 1.00 58.27  ? 103 LEU   B O   1 
ATOM   1244 C CB  . LEU   B 2 88  ? -15.676 -1.575  -24.876 1.00 57.23  ? 103 LEU   B CB  1 
ATOM   1245 C CG  . LEU   B 2 88  ? -15.561 -0.247  -24.135 1.00 56.62  ? 103 LEU   B CG  1 
ATOM   1246 C CD1 . LEU   B 2 88  ? -16.078 -0.374  -22.707 1.00 56.41  ? 103 LEU   B CD1 1 
ATOM   1247 C CD2 . LEU   B 2 88  ? -14.141 0.251   -24.143 1.00 57.20  ? 103 LEU   B CD2 1 
ATOM   1248 N N   . LEU   B 2 89  ? -19.156 -0.690  -24.930 1.00 56.78  ? 104 LEU   B N   1 
ATOM   1249 C CA  . LEU   B 2 89  ? -19.925 0.509   -25.310 1.00 56.87  ? 104 LEU   B CA  1 
ATOM   1250 C C   . LEU   B 2 89  ? -19.238 1.716   -24.659 1.00 56.56  ? 104 LEU   B C   1 
ATOM   1251 O O   . LEU   B 2 89  ? -19.724 2.220   -23.621 1.00 56.22  ? 104 LEU   B O   1 
ATOM   1252 C CB  . LEU   B 2 89  ? -21.388 0.247   -24.958 1.00 57.46  ? 104 LEU   B CB  1 
ATOM   1253 C CG  . LEU   B 2 89  ? -22.385 1.405   -25.033 1.00 58.58  ? 104 LEU   B CG  1 
ATOM   1254 C CD1 . LEU   B 2 89  ? -22.028 2.428   -26.097 1.00 59.20  ? 104 LEU   B CD1 1 
ATOM   1255 C CD2 . LEU   B 2 89  ? -23.794 0.877   -25.289 1.00 59.61  ? 104 LEU   B CD2 1 
ATOM   1256 N N   . ALA   B 2 90  ? -18.143 2.187   -25.294 1.00 56.55  ? 105 ALA   B N   1 
ATOM   1257 C CA  . ALA   B 2 90  ? -17.335 3.350   -24.831 1.00 55.93  ? 105 ALA   B CA  1 
ATOM   1258 C C   . ALA   B 2 90  ? -18.117 4.654   -25.003 1.00 55.74  ? 105 ALA   B C   1 
ATOM   1259 O O   . ALA   B 2 90  ? -18.657 4.839   -26.094 1.00 56.62  ? 105 ALA   B O   1 
ATOM   1260 C CB  . ALA   B 2 90  ? -16.014 3.430   -25.547 1.00 56.10  ? 105 ALA   B CB  1 
ATOM   1261 N N   . VAL   B 2 91  ? -18.190 5.489   -23.951 1.00 54.55  ? 106 VAL   B N   1 
ATOM   1262 C CA  . VAL   B 2 91  ? -18.773 6.856   -23.947 1.00 53.85  ? 106 VAL   B CA  1 
ATOM   1263 C C   . VAL   B 2 91  ? -17.675 7.844   -23.545 1.00 54.54  ? 106 VAL   B C   1 
ATOM   1264 O O   . VAL   B 2 91  ? -17.612 8.325   -22.416 1.00 54.45  ? 106 VAL   B O   1 
ATOM   1265 C CB  . VAL   B 2 91  ? -20.012 6.890   -23.053 1.00 52.56  ? 106 VAL   B CB  1 
ATOM   1266 C CG1 . VAL   B 2 91  ? -20.682 8.247   -22.978 1.00 52.63  ? 106 VAL   B CG1 1 
ATOM   1267 C CG2 . VAL   B 2 91  ? -21.017 5.823   -23.429 1.00 52.52  ? 106 VAL   B CG2 1 
ATOM   1268 N N   . PRO   B 2 92  ? -16.773 8.222   -24.484 1.00 56.19  ? 107 PRO   B N   1 
ATOM   1269 C CA  . PRO   B 2 92  ? -15.633 9.080   -24.176 1.00 56.46  ? 107 PRO   B CA  1 
ATOM   1270 C C   . PRO   B 2 92  ? -16.131 10.511  -23.997 1.00 56.56  ? 107 PRO   B C   1 
ATOM   1271 O O   . PRO   B 2 92  ? -17.207 10.881  -24.530 1.00 57.65  ? 107 PRO   B O   1 
ATOM   1272 C CB  . PRO   B 2 92  ? -14.663 8.890   -25.364 1.00 58.10  ? 107 PRO   B CB  1 
ATOM   1273 C CG  . PRO   B 2 92  ? -15.350 7.906   -26.346 1.00 58.11  ? 107 PRO   B CG  1 
ATOM   1274 C CD  . PRO   B 2 92  ? -16.808 7.848   -25.898 1.00 57.40  ? 107 PRO   B CD  1 
ATOM   1275 N N   . PRO   B 2 93  ? -15.352 11.390  -23.319 1.00 57.28  ? 108 PRO   B N   1 
ATOM   1276 C CA  . PRO   B 2 93  ? -15.821 12.732  -22.990 1.00 58.20  ? 108 PRO   B CA  1 
ATOM   1277 C C   . PRO   B 2 93  ? -15.998 13.603  -24.257 1.00 59.68  ? 108 PRO   B C   1 
ATOM   1278 O O   . PRO   B 2 93  ? -15.166 13.623  -25.020 1.00 60.21  ? 108 PRO   B O   1 
ATOM   1279 C CB  . PRO   B 2 93  ? -14.733 13.258  -22.044 1.00 57.79  ? 108 PRO   B CB  1 
ATOM   1280 C CG  . PRO   B 2 93  ? -14.085 12.003  -21.521 1.00 57.82  ? 108 PRO   B CG  1 
ATOM   1281 C CD  . PRO   B 2 93  ? -14.011 11.147  -22.766 1.00 58.16  ? 108 PRO   B CD  1 
ATOM   1282 N N   . GLY   B 2 94  ? -17.125 14.289  -24.400 1.00 61.17  ? 109 GLY   B N   1 
ATOM   1283 C CA  . GLY   B 2 94  ? -17.490 15.096  -25.578 1.00 63.23  ? 109 GLY   B CA  1 
ATOM   1284 C C   . GLY   B 2 94  ? -17.679 14.313  -26.879 1.00 64.63  ? 109 GLY   B C   1 
ATOM   1285 O O   . GLY   B 2 94  ? -17.733 14.953  -27.924 1.00 64.25  ? 109 GLY   B O   1 
ATOM   1286 N N   . GLU   B 2 95  ? -17.745 12.985  -26.861 1.00 65.72  ? 110 GLU   B N   1 
ATOM   1287 C CA  . GLU   B 2 95  ? -17.836 12.177  -28.105 1.00 66.83  ? 110 GLU   B CA  1 
ATOM   1288 C C   . GLU   B 2 95  ? -19.039 11.246  -27.966 1.00 67.02  ? 110 GLU   B C   1 
ATOM   1289 O O   . GLU   B 2 95  ? -19.507 11.041  -26.824 1.00 65.74  ? 110 GLU   B O   1 
ATOM   1290 C CB  . GLU   B 2 95  ? -16.526 11.435  -28.370 1.00 68.59  ? 110 GLU   B CB  1 
ATOM   1291 C CG  . GLU   B 2 95  ? -15.298 12.355  -28.364 1.00 70.97  ? 110 GLU   B CG  1 
ATOM   1292 C CD  . GLU   B 2 95  ? -13.904 11.669  -28.727 1.00 73.42  ? 110 GLU   B CD  1 
ATOM   1293 O OE1 . GLU   B 2 95  ? -13.864 10.440  -28.641 1.00 76.12  ? 110 GLU   B OE1 1 
ATOM   1294 O OE2 . GLU   B 2 95  ? -12.880 12.374  -28.999 1.00 74.80  ? 110 GLU   B OE2 1 
ATOM   1295 N N   . ARG   B 2 96  ? -19.579 10.783  -29.085 1.00 67.12  ? 111 ARG   B N   1 
ATOM   1296 C CA  . ARG   B 2 96  ? -20.792 9.936   -29.141 1.00 67.96  ? 111 ARG   B CA  1 
ATOM   1297 C C   . ARG   B 2 96  ? -20.460 8.549   -28.583 1.00 66.53  ? 111 ARG   B C   1 
ATOM   1298 O O   . ARG   B 2 96  ? -19.306 8.104   -28.770 1.00 65.73  ? 111 ARG   B O   1 
ATOM   1299 C CB  . ARG   B 2 96  ? -21.256 9.826   -30.594 1.00 71.14  ? 111 ARG   B CB  1 
ATOM   1300 C CG  . ARG   B 2 96  ? -22.635 9.207   -30.766 1.00 74.18  ? 111 ARG   B CG  1 
ATOM   1301 C CD  . ARG   B 2 96  ? -23.433 9.866   -31.886 1.00 77.28  ? 111 ARG   B CD  1 
ATOM   1302 N NE  . ARG   B 2 96  ? -22.779 9.756   -33.172 1.00 80.69  ? 111 ARG   B NE  1 
ATOM   1303 C CZ  . ARG   B 2 96  ? -22.165 10.746  -33.840 1.00 85.35  ? 111 ARG   B CZ  1 
ATOM   1304 N NH1 . ARG   B 2 96  ? -22.095 11.981  -33.350 1.00 83.87  ? 111 ARG   B NH1 1 
ATOM   1305 N NH2 . ARG   B 2 96  ? -21.641 10.482  -35.033 1.00 84.81  ? 111 ARG   B NH2 1 
ATOM   1306 N N   . ALA   B 2 97  ? -21.447 7.890   -27.955 1.00 65.22  ? 112 ALA   B N   1 
ATOM   1307 C CA  . ALA   B 2 97  ? -21.375 6.461   -27.568 1.00 64.97  ? 112 ALA   B CA  1 
ATOM   1308 C C   . ALA   B 2 97  ? -20.929 5.634   -28.778 1.00 66.99  ? 112 ALA   B C   1 
ATOM   1309 O O   . ALA   B 2 97  ? -21.427 5.889   -29.899 1.00 64.87  ? 112 ALA   B O   1 
ATOM   1310 C CB  . ALA   B 2 97  ? -22.723 6.023   -27.073 1.00 65.02  ? 112 ALA   B CB  1 
ATOM   1311 N N   . LYS   B 2 98  ? -20.031 4.668   -28.592 1.00 68.45  ? 113 LYS   B N   1 
ATOM   1312 C CA  . LYS   B 2 98  ? -19.446 3.924   -29.749 1.00 70.11  ? 113 LYS   B CA  1 
ATOM   1313 C C   . LYS   B 2 98  ? -19.101 2.485   -29.329 1.00 68.92  ? 113 LYS   B C   1 
ATOM   1314 O O   . LYS   B 2 98  ? -18.321 2.348   -28.330 1.00 68.61  ? 113 LYS   B O   1 
ATOM   1315 C CB  . LYS   B 2 98  ? -18.195 4.695   -30.175 1.00 73.61  ? 113 LYS   B CB  1 
ATOM   1316 C CG  . LYS   B 2 98  ? -17.475 4.238   -31.449 1.00 78.83  ? 113 LYS   B CG  1 
ATOM   1317 C CD  . LYS   B 2 98  ? -16.020 4.737   -31.497 1.00 82.07  ? 113 LYS   B CD  1 
ATOM   1318 C CE  . LYS   B 2 98  ? -15.481 5.088   -30.110 1.00 82.64  ? 113 LYS   B CE  1 
ATOM   1319 N NZ  . LYS   B 2 98  ? -14.175 5.787   -30.147 1.00 84.27  ? 113 LYS   B NZ  1 
ATOM   1320 N N   . ASN   B 2 99  ? -19.694 1.476   -29.986 1.00 66.04  ? 114 ASN   B N   1 
ATOM   1321 C CA  . ASN   B 2 99  ? -19.426 0.038   -29.726 1.00 66.18  ? 114 ASN   B CA  1 
ATOM   1322 C C   . ASN   B 2 99  ? -18.047 -0.302  -30.280 1.00 66.46  ? 114 ASN   B C   1 
ATOM   1323 O O   . ASN   B 2 99  ? -17.769 0.088   -31.419 1.00 67.70  ? 114 ASN   B O   1 
ATOM   1324 C CB  . ASN   B 2 99  ? -20.478 -0.927  -30.294 1.00 66.55  ? 114 ASN   B CB  1 
ATOM   1325 C CG  . ASN   B 2 99  ? -21.839 -0.811  -29.626 1.00 67.40  ? 114 ASN   B CG  1 
ATOM   1326 O OD1 . ASN   B 2 99  ? -22.496 0.237   -29.687 1.00 67.99  ? 114 ASN   B OD1 1 
ATOM   1327 N ND2 . ASN   B 2 99  ? -22.295 -1.870  -28.971 1.00 68.10  ? 114 ASN   B ND2 1 
ATOM   1328 N N   . ILE   B 2 100 ? -17.240 -1.070  -29.555 1.00 64.42  ? 115 ILE   B N   1 
ATOM   1329 C CA  . ILE   B 2 100 ? -15.933 -1.591  -30.031 1.00 64.68  ? 115 ILE   B CA  1 
ATOM   1330 C C   . ILE   B 2 100 ? -15.876 -3.056  -29.644 1.00 65.40  ? 115 ILE   B C   1 
ATOM   1331 O O   . ILE   B 2 100 ? -15.926 -3.362  -28.390 1.00 66.13  ? 115 ILE   B O   1 
ATOM   1332 C CB  . ILE   B 2 100 ? -14.743 -0.858  -29.401 1.00 64.57  ? 115 ILE   B CB  1 
ATOM   1333 C CG1 . ILE   B 2 100 ? -14.833 0.664   -29.443 1.00 64.50  ? 115 ILE   B CG1 1 
ATOM   1334 C CG2 . ILE   B 2 100 ? -13.458 -1.382  -29.971 1.00 65.60  ? 115 ILE   B CG2 1 
ATOM   1335 C CD1 . ILE   B 2 100 ? -14.687 1.264   -30.839 1.00 65.16  ? 115 ILE   B CD1 1 
ATOM   1336 N N   . GLN   B 2 101 ? -15.647 -3.921  -30.606 1.00 66.29  ? 116 GLN   B N   1 
ATOM   1337 C CA  . GLN   B 2 101 ? -15.695 -5.375  -30.415 1.00 67.72  ? 116 GLN   B CA  1 
ATOM   1338 C C   . GLN   B 2 101 ? -14.267 -5.836  -30.184 1.00 69.13  ? 116 GLN   B C   1 
ATOM   1339 O O   . GLN   B 2 101 ? -13.405 -5.469  -30.998 1.00 71.79  ? 116 GLN   B O   1 
ATOM   1340 C CB  . GLN   B 2 101 ? -16.334 -6.055  -31.613 1.00 69.10  ? 116 GLN   B CB  1 
ATOM   1341 C CG  . GLN   B 2 101 ? -16.423 -7.569  -31.497 1.00 70.03  ? 116 GLN   B CG  1 
ATOM   1342 C CD  . GLN   B 2 101 ? -17.557 -8.118  -32.453 1.00 71.28  ? 116 GLN   B CD  1 
ATOM   1343 O OE1 . GLN   B 2 101 ? -18.666 -7.475  -32.598 1.00 70.60  ? 116 GLN   B OE1 1 
ATOM   1344 N NE2 . GLN   B 2 101 ? -17.277 -9.329  -32.952 1.00 73.00  ? 116 GLN   B NE2 1 
ATOM   1345 N N   . THR   B 2 102 ? -14.046 -6.662  -29.149 1.00 68.53  ? 117 THR   B N   1 
ATOM   1346 C CA  . THR   B 2 102 ? -12.701 -7.176  -28.801 1.00 68.89  ? 117 THR   B CA  1 
ATOM   1347 C C   . THR   B 2 102 ? -12.858 -8.586  -28.243 1.00 69.22  ? 117 THR   B C   1 
ATOM   1348 O O   . THR   B 2 102 ? -14.005 -8.936  -27.886 1.00 70.03  ? 117 THR   B O   1 
ATOM   1349 C CB  . THR   B 2 102 ? -11.991 -6.152  -27.908 1.00 67.84  ? 117 THR   B CB  1 
ATOM   1350 O OG1 . THR   B 2 102 ? -10.625 -6.561  -27.848 1.00 68.76  ? 117 THR   B OG1 1 
ATOM   1351 C CG2 . THR   B 2 102 ? -12.618 -6.006  -26.539 1.00 67.18  ? 117 THR   B CG2 1 
ATOM   1352 N N   . LEU   B 2 103 ? -11.781 -9.387  -28.292 1.00 69.87  ? 118 LEU   B N   1 
ATOM   1353 C CA  . LEU   B 2 103 ? -11.676 -10.640 -27.506 1.00 69.39  ? 118 LEU   B CA  1 
ATOM   1354 C C   . LEU   B 2 103 ? -10.901 -10.308 -26.228 1.00 68.40  ? 118 LEU   B C   1 
ATOM   1355 O O   . LEU   B 2 103 ? -9.731  -9.875  -26.236 1.00 67.32  ? 118 LEU   B O   1 
ATOM   1356 C CB  . LEU   B 2 103 ? -11.000 -11.788 -28.268 1.00 70.98  ? 118 LEU   B CB  1 
ATOM   1357 C CG  . LEU   B 2 103 ? -10.969 -13.080 -27.433 1.00 71.59  ? 118 LEU   B CG  1 
ATOM   1358 C CD1 . LEU   B 2 103 ? -12.275 -13.842 -27.571 1.00 71.60  ? 118 LEU   B CD1 1 
ATOM   1359 C CD2 . LEU   B 2 103 ? -9.795  -13.983 -27.785 1.00 73.63  ? 118 LEU   B CD2 1 
ATOM   1360 N N   . PRO   B 2 104 ? -11.553 -10.440 -25.049 1.00 67.18  ? 119 PRO   B N   1 
ATOM   1361 C CA  . PRO   B 2 104 ? -10.878 -10.110 -23.810 1.00 66.87  ? 119 PRO   B CA  1 
ATOM   1362 C C   . PRO   B 2 104 ? -9.709  -11.110 -23.575 1.00 68.59  ? 119 PRO   B C   1 
ATOM   1363 O O   . PRO   B 2 104 ? -9.802  -12.310 -23.994 1.00 71.12  ? 119 PRO   B O   1 
ATOM   1364 C CB  . PRO   B 2 104 ? -11.939 -10.298 -22.718 1.00 65.44  ? 119 PRO   B CB  1 
ATOM   1365 C CG  . PRO   B 2 104 ? -13.260 -10.330 -23.451 1.00 65.18  ? 119 PRO   B CG  1 
ATOM   1366 C CD  . PRO   B 2 104 ? -12.950 -10.850 -24.853 1.00 66.60  ? 119 PRO   B CD  1 
ATOM   1367 N N   . GLY   B 2 105 ? -8.626  -10.505 -23.026 1.00 69.01  ? 120 GLY   B N   1 
ATOM   1368 C CA  . GLY   B 2 105 ? -7.558  -11.228 -22.321 1.00 70.49  ? 120 GLY   B CA  1 
ATOM   1369 C C   . GLY   B 2 105 ? -7.979  -11.627 -20.906 1.00 69.96  ? 120 GLY   B C   1 
ATOM   1370 O O   . GLY   B 2 105 ? -9.196  -11.590 -20.585 1.00 67.99  ? 120 GLY   B O   1 
ATOM   1371 N N   . ILE   B 2 106 ? -6.993  -12.001 -20.086 1.00 71.68  ? 121 ILE   B N   1 
ATOM   1372 C CA  . ILE   B 2 106 ? -7.181  -12.539 -18.704 1.00 71.66  ? 121 ILE   B CA  1 
ATOM   1373 C C   . ILE   B 2 106 ? -6.268  -11.778 -17.739 1.00 70.71  ? 121 ILE   B C   1 
ATOM   1374 O O   . ILE   B 2 106 ? -5.052  -11.647 -17.963 1.00 71.03  ? 121 ILE   B O   1 
ATOM   1375 C CB  . ILE   B 2 106 ? -6.874  -14.046 -18.670 1.00 75.25  ? 121 ILE   B CB  1 
ATOM   1376 C CG1 . ILE   B 2 106 ? -7.655  -14.852 -19.715 1.00 78.88  ? 121 ILE   B CG1 1 
ATOM   1377 C CG2 . ILE   B 2 106 ? -7.108  -14.605 -17.309 1.00 76.70  ? 121 ILE   B CG2 1 
ATOM   1378 C CD1 . ILE   B 2 106 ? -9.072  -15.177 -19.305 1.00 78.24  ? 121 ILE   B CD1 1 
ATOM   1379 N N   . PHE   B 2 107 ? -6.846  -11.336 -16.632 1.00 69.11  ? 122 PHE   B N   1 
ATOM   1380 C CA  . PHE   B 2 107 ? -6.114  -11.012 -15.396 1.00 68.01  ? 122 PHE   B CA  1 
ATOM   1381 C C   . PHE   B 2 107 ? -6.092  -12.271 -14.527 1.00 70.52  ? 122 PHE   B C   1 
ATOM   1382 O O   . PHE   B 2 107 ? -7.173  -12.706 -14.100 1.00 71.94  ? 122 PHE   B O   1 
ATOM   1383 C CB  . PHE   B 2 107 ? -6.858  -9.913  -14.654 1.00 65.40  ? 122 PHE   B CB  1 
ATOM   1384 C CG  . PHE   B 2 107 ? -6.593  -8.491  -15.036 1.00 64.78  ? 122 PHE   B CG  1 
ATOM   1385 C CD1 . PHE   B 2 107 ? -5.810  -8.148  -16.128 1.00 65.71  ? 122 PHE   B CD1 1 
ATOM   1386 C CD2 . PHE   B 2 107 ? -7.202  -7.480  -14.313 1.00 63.88  ? 122 PHE   B CD2 1 
ATOM   1387 C CE1 . PHE   B 2 107 ? -5.631  -6.823  -16.483 1.00 65.32  ? 122 PHE   B CE1 1 
ATOM   1388 C CE2 . PHE   B 2 107 ? -7.030  -6.155  -14.687 1.00 63.86  ? 122 PHE   B CE2 1 
ATOM   1389 C CZ  . PHE   B 2 107 ? -6.246  -5.829  -15.762 1.00 64.13  ? 122 PHE   B CZ  1 
ATOM   1390 N N   . LYS   B 2 108 ? -4.903  -12.804 -14.240 1.00 72.47  ? 123 LYS   B N   1 
ATOM   1391 C CA  . LYS   B 2 108 ? -4.673  -13.928 -13.297 1.00 72.67  ? 123 LYS   B CA  1 
ATOM   1392 C C   . LYS   B 2 108 ? -4.361  -13.294 -11.938 1.00 71.45  ? 123 LYS   B C   1 
ATOM   1393 O O   . LYS   B 2 108 ? -3.391  -12.502 -11.892 1.00 68.98  ? 123 LYS   B O   1 
ATOM   1394 C CB  . LYS   B 2 108 ? -3.517  -14.823 -13.759 1.00 76.40  ? 123 LYS   B CB  1 
ATOM   1395 C CG  . LYS   B 2 108 ? -3.849  -15.844 -14.843 1.00 80.29  ? 123 LYS   B CG  1 
ATOM   1396 C CD  . LYS   B 2 108 ? -2.682  -16.154 -15.789 1.00 84.30  ? 123 LYS   B CD  1 
ATOM   1397 C CE  . LYS   B 2 108 ? -2.652  -17.593 -16.294 1.00 89.33  ? 123 LYS   B CE  1 
ATOM   1398 N NZ  . LYS   B 2 108 ? -2.173  -17.727 -17.706 1.00 93.93  ? 123 LYS   B NZ  1 
ATOM   1399 N N   . THR   B 2 109 ? -5.220  -13.557 -10.943 1.00 70.36  ? 124 THR   B N   1 
ATOM   1400 C CA  . THR   B 2 109 ? -5.029  -13.175 -9.517  1.00 72.00  ? 124 THR   B CA  1 
ATOM   1401 C C   . THR   B 2 109 ? -5.009  -14.438 -8.645  1.00 72.92  ? 124 THR   B C   1 
ATOM   1402 O O   . THR   B 2 109 ? -5.466  -15.532 -9.096  1.00 71.73  ? 124 THR   B O   1 
ATOM   1403 C CB  . THR   B 2 109 ? -6.067  -12.155 -9.016  1.00 71.06  ? 124 THR   B CB  1 
ATOM   1404 O OG1 . THR   B 2 109 ? -7.233  -12.807 -8.510  1.00 70.67  ? 124 THR   B OG1 1 
ATOM   1405 C CG2 . THR   B 2 109 ? -6.444  -11.154 -10.091 1.00 71.31  ? 124 THR   B CG2 1 
ATOM   1406 N N   . LYS   B 2 110 ? -4.507  -14.265 -7.425  1.00 74.38  ? 125 LYS   B N   1 
ATOM   1407 C CA  . LYS   B 2 110 ? -4.420  -15.323 -6.391  1.00 76.90  ? 125 LYS   B CA  1 
ATOM   1408 C C   . LYS   B 2 110 ? -5.847  -15.750 -6.000  1.00 78.07  ? 125 LYS   B C   1 
ATOM   1409 O O   . LYS   B 2 110 ? -6.008  -16.932 -5.558  1.00 81.39  ? 125 LYS   B O   1 
ATOM   1410 C CB  . LYS   B 2 110 ? -3.617  -14.783 -5.204  1.00 76.60  ? 125 LYS   B CB  1 
ATOM   1411 C CG  . LYS   B 2 110 ? -4.350  -13.731 -4.390  1.00 76.26  ? 125 LYS   B CG  1 
ATOM   1412 C CD  . LYS   B 2 110 ? -3.534  -13.123 -3.269  1.00 77.65  ? 125 LYS   B CD  1 
ATOM   1413 C CE  . LYS   B 2 110 ? -4.338  -12.870 -2.008  1.00 77.50  ? 125 LYS   B CE  1 
ATOM   1414 N NZ  . LYS   B 2 110 ? -5.523  -12.018 -2.250  1.00 77.90  ? 125 LYS   B NZ  1 
ATOM   1415 N N   . ASP   B 2 111 ? -6.835  -14.850 -6.161  1.00 75.59  ? 126 ASP   B N   1 
ATOM   1416 C CA  . ASP   B 2 111 ? -8.280  -15.139 -5.938  1.00 75.09  ? 126 ASP   B CA  1 
ATOM   1417 C C   . ASP   B 2 111 ? -8.944  -15.564 -7.253  1.00 76.49  ? 126 ASP   B C   1 
ATOM   1418 O O   . ASP   B 2 111 ? -10.174 -15.722 -7.268  1.00 77.93  ? 126 ASP   B O   1 
ATOM   1419 C CB  . ASP   B 2 111 ? -9.034  -13.926 -5.397  1.00 74.11  ? 126 ASP   B CB  1 
ATOM   1420 C CG  . ASP   B 2 111 ? -8.690  -13.589 -3.968  1.00 73.65  ? 126 ASP   B CG  1 
ATOM   1421 O OD1 . ASP   B 2 111 ? -7.691  -14.128 -3.462  1.00 72.30  ? 126 ASP   B OD1 1 
ATOM   1422 O OD2 . ASP   B 2 111 ? -9.457  -12.828 -3.370  1.00 76.43  ? 126 ASP   B OD2 1 
ATOM   1423 N N   . GLY   B 2 112 ? -8.178  -15.717 -8.328  1.00 75.83  ? 127 GLY   B N   1 
ATOM   1424 C CA  . GLY   B 2 112 ? -8.685  -16.338 -9.555  1.00 76.09  ? 127 GLY   B CA  1 
ATOM   1425 C C   . GLY   B 2 112 ? -8.667  -15.379 -10.729 1.00 75.58  ? 127 GLY   B C   1 
ATOM   1426 O O   . GLY   B 2 112 ? -8.246  -14.211 -10.545 1.00 73.85  ? 127 GLY   B O   1 
ATOM   1427 N N   . ASP   B 2 113 ? -9.163  -15.879 -11.862 1.00 76.16  ? 128 ASP   B N   1 
ATOM   1428 C CA  . ASP   B 2 113 ? -9.041  -15.286 -13.222 1.00 76.65  ? 128 ASP   B CA  1 
ATOM   1429 C C   . ASP   B 2 113 ? -10.212 -14.323 -13.482 1.00 74.77  ? 128 ASP   B C   1 
ATOM   1430 O O   . ASP   B 2 113 ? -11.371 -14.692 -13.158 1.00 73.65  ? 128 ASP   B O   1 
ATOM   1431 C CB  . ASP   B 2 113 ? -8.998  -16.389 -14.285 1.00 78.73  ? 128 ASP   B CB  1 
ATOM   1432 C CG  . ASP   B 2 113 ? -7.654  -17.085 -14.446 1.00 81.78  ? 128 ASP   B CG  1 
ATOM   1433 O OD1 . ASP   B 2 113 ? -6.741  -16.801 -13.599 1.00 85.48  ? 128 ASP   B OD1 1 
ATOM   1434 O OD2 . ASP   B 2 113 ? -7.535  -17.919 -15.416 1.00 85.64  ? 128 ASP   B OD2 1 
ATOM   1435 N N   . ILE   B 2 114 ? -9.913  -13.167 -14.117 1.00 73.42  ? 129 ILE   B N   1 
ATOM   1436 C CA  . ILE   B 2 114 ? -10.900 -12.111 -14.506 1.00 70.62  ? 129 ILE   B CA  1 
ATOM   1437 C C   . ILE   B 2 114 ? -10.677 -11.793 -15.984 1.00 68.09  ? 129 ILE   B C   1 
ATOM   1438 O O   . ILE   B 2 114 ? -9.520  -11.576 -16.324 1.00 66.99  ? 129 ILE   B O   1 
ATOM   1439 C CB  . ILE   B 2 114 ? -10.714 -10.801 -13.714 1.00 68.55  ? 129 ILE   B CB  1 
ATOM   1440 C CG1 . ILE   B 2 114 ? -9.948  -11.028 -12.417 1.00 71.30  ? 129 ILE   B CG1 1 
ATOM   1441 C CG2 . ILE   B 2 114 ? -12.037 -10.112 -13.517 1.00 68.29  ? 129 ILE   B CG2 1 
ATOM   1442 C CD1 . ILE   B 2 114 ? -9.920  -9.824  -11.447 1.00 71.02  ? 129 ILE   B CD1 1 
ATOM   1443 N N   . GLY   B 2 115 ? -11.759 -11.632 -16.753 1.00 66.56  ? 130 GLY   B N   1 
ATOM   1444 C CA  . GLY   B 2 115 ? -11.732 -11.036 -18.111 1.00 66.57  ? 130 GLY   B CA  1 
ATOM   1445 C C   . GLY   B 2 115 ? -11.079 -9.660  -18.117 1.00 65.05  ? 130 GLY   B C   1 
ATOM   1446 O O   . GLY   B 2 115 ? -11.132 -8.921  -17.090 1.00 64.02  ? 130 GLY   B O   1 
ATOM   1447 N N   . ALA   B 2 116 ? -10.358 -9.346  -19.187 1.00 64.98  ? 131 ALA   B N   1 
ATOM   1448 C CA  . ALA   B 2 116 ? -9.667  -8.044  -19.305 1.00 64.53  ? 131 ALA   B CA  1 
ATOM   1449 C C   . ALA   B 2 116 ? -9.769  -7.562  -20.752 1.00 64.59  ? 131 ALA   B C   1 
ATOM   1450 O O   . ALA   B 2 116 ? -9.521  -8.371  -21.684 1.00 65.81  ? 131 ALA   B O   1 
ATOM   1451 C CB  . ALA   B 2 116 ? -8.235  -8.163  -18.823 1.00 65.04  ? 131 ALA   B CB  1 
ATOM   1452 N N   A VAL   B 2 117 ? -10.116 -6.287  -20.951 0.23 63.98  ? 132 VAL   B N   1 
ATOM   1453 N N   B VAL   B 2 117 ? -10.105 -6.282  -20.932 0.25 64.09  ? 132 VAL   B N   1 
ATOM   1454 N N   C VAL   B 2 117 ? -10.116 -6.287  -20.951 0.25 63.97  ? 132 VAL   B N   1 
ATOM   1455 N N   D VAL   B 2 117 ? -10.106 -6.282  -20.932 0.27 64.08  ? 132 VAL   B N   1 
ATOM   1456 C CA  A VAL   B 2 117 ? -10.251 -5.674  -22.311 0.23 65.00  ? 132 VAL   B CA  1 
ATOM   1457 C CA  B VAL   B 2 117 ? -10.255 -5.625  -22.267 0.25 65.17  ? 132 VAL   B CA  1 
ATOM   1458 C CA  C VAL   B 2 117 ? -10.251 -5.675  -22.311 0.25 64.99  ? 132 VAL   B CA  1 
ATOM   1459 C CA  D VAL   B 2 117 ? -10.255 -5.625  -22.267 0.27 65.17  ? 132 VAL   B CA  1 
ATOM   1460 C C   A VAL   B 2 117 ? -9.092  -4.693  -22.533 0.23 65.25  ? 132 VAL   B C   1 
ATOM   1461 C C   B VAL   B 2 117 ? -9.050  -4.704  -22.498 0.25 65.40  ? 132 VAL   B C   1 
ATOM   1462 C C   C VAL   B 2 117 ? -9.093  -4.693  -22.534 0.25 65.25  ? 132 VAL   B C   1 
ATOM   1463 C C   D VAL   B 2 117 ? -9.050  -4.704  -22.498 0.27 65.40  ? 132 VAL   B C   1 
ATOM   1464 O O   A VAL   B 2 117 ? -8.934  -3.770  -21.714 0.23 64.32  ? 132 VAL   B O   1 
ATOM   1465 O O   B VAL   B 2 117 ? -8.819  -3.825  -21.646 0.25 64.49  ? 132 VAL   B O   1 
ATOM   1466 O O   C VAL   B 2 117 ? -8.934  -3.770  -21.715 0.25 64.32  ? 132 VAL   B O   1 
ATOM   1467 O O   D VAL   B 2 117 ? -8.819  -3.825  -21.646 0.27 64.49  ? 132 VAL   B O   1 
ATOM   1468 C CB  A VAL   B 2 117 ? -11.629 -5.013  -22.511 0.23 64.43  ? 132 VAL   B CB  1 
ATOM   1469 C CB  B VAL   B 2 117 ? -11.597 -4.872  -22.357 0.25 64.69  ? 132 VAL   B CB  1 
ATOM   1470 C CB  C VAL   B 2 117 ? -11.629 -5.015  -22.512 0.25 64.43  ? 132 VAL   B CB  1 
ATOM   1471 C CB  D VAL   B 2 117 ? -11.597 -4.873  -22.357 0.27 64.69  ? 132 VAL   B CB  1 
ATOM   1472 C CG1 A VAL   B 2 117 ? -12.753 -6.005  -22.255 0.23 64.56  ? 132 VAL   B CG1 1 
ATOM   1473 C CG1 B VAL   B 2 117 ? -11.498 -3.590  -23.167 0.25 64.80  ? 132 VAL   B CG1 1 
ATOM   1474 C CG1 C VAL   B 2 117 ? -12.753 -6.007  -22.254 0.25 64.56  ? 132 VAL   B CG1 1 
ATOM   1475 C CG1 D VAL   B 2 117 ? -11.498 -3.590  -23.166 0.27 64.80  ? 132 VAL   B CG1 1 
ATOM   1476 C CG2 A VAL   B 2 117 ? -11.821 -3.762  -21.666 0.23 63.12  ? 132 VAL   B CG2 1 
ATOM   1477 C CG2 B VAL   B 2 117 ? -12.692 -5.766  -22.919 0.25 64.98  ? 132 VAL   B CG2 1 
ATOM   1478 C CG2 C VAL   B 2 117 ? -11.821 -3.763  -21.667 0.25 63.11  ? 132 VAL   B CG2 1 
ATOM   1479 C CG2 D VAL   B 2 117 ? -12.692 -5.767  -22.920 0.27 64.98  ? 132 VAL   B CG2 1 
ATOM   1480 N N   . ALA   B 2 118 ? -8.298  -4.919  -23.587 1.00 66.17  ? 133 ALA   B N   1 
ATOM   1481 C CA  . ALA   B 2 118 ? -7.133  -4.076  -23.941 1.00 67.44  ? 133 ALA   B CA  1 
ATOM   1482 C C   . ALA   B 2 118 ? -7.608  -3.006  -24.930 1.00 69.05  ? 133 ALA   B C   1 
ATOM   1483 O O   . ALA   B 2 118 ? -7.583  -3.271  -26.131 1.00 68.35  ? 133 ALA   B O   1 
ATOM   1484 C CB  . ALA   B 2 118 ? -6.011  -4.917  -24.528 1.00 69.34  ? 133 ALA   B CB  1 
ATOM   1485 N N   . LEU   B 2 119 ? -8.175  -1.921  -24.405 1.00 68.21  ? 134 LEU   B N   1 
ATOM   1486 C CA  . LEU   B 2 119 ? -8.712  -0.774  -25.166 1.00 67.26  ? 134 LEU   B CA  1 
ATOM   1487 C C   . LEU   B 2 119 ? -8.423  0.475   -24.344 1.00 67.80  ? 134 LEU   B C   1 
ATOM   1488 O O   . LEU   B 2 119 ? -8.797  0.502   -23.143 1.00 68.69  ? 134 LEU   B O   1 
ATOM   1489 C CB  . LEU   B 2 119 ? -10.215 -0.972  -25.349 1.00 67.20  ? 134 LEU   B CB  1 
ATOM   1490 C CG  . LEU   B 2 119 ? -10.653 -2.111  -26.272 1.00 67.74  ? 134 LEU   B CG  1 
ATOM   1491 C CD1 . LEU   B 2 119 ? -12.168 -2.235  -26.267 1.00 66.59  ? 134 LEU   B CD1 1 
ATOM   1492 C CD2 . LEU   B 2 119 ? -10.139 -1.911  -27.700 1.00 69.77  ? 134 LEU   B CD2 1 
ATOM   1493 N N   . ASP   B 2 120 ? -7.699  1.422   -24.908 1.00 68.39  ? 135 ASP   B N   1 
ATOM   1494 C CA  . ASP   B 2 120 ? -7.215  2.645   -24.231 1.00 69.50  ? 135 ASP   B CA  1 
ATOM   1495 C C   . ASP   B 2 120 ? -8.241  3.737   -24.481 1.00 67.85  ? 135 ASP   B C   1 
ATOM   1496 O O   . ASP   B 2 120 ? -8.592  3.936   -25.614 1.00 69.14  ? 135 ASP   B O   1 
ATOM   1497 C CB  . ASP   B 2 120 ? -5.845  3.024   -24.809 1.00 73.88  ? 135 ASP   B CB  1 
ATOM   1498 C CG  . ASP   B 2 120 ? -4.868  3.482   -23.737 1.00 76.89  ? 135 ASP   B CG  1 
ATOM   1499 O OD1 . ASP   B 2 120 ? -5.272  4.389   -22.958 1.00 75.56  ? 135 ASP   B OD1 1 
ATOM   1500 O OD2 . ASP   B 2 120 ? -3.727  2.901   -23.683 1.00 80.77  ? 135 ASP   B OD2 1 
ATOM   1501 N N   A TYR   B 2 121 ? -8.725  4.400   -23.429 0.23 66.58  ? 136 TYR   B N   1 
ATOM   1502 N N   B TYR   B 2 121 ? -8.726  4.400   -23.429 0.25 66.57  ? 136 TYR   B N   1 
ATOM   1503 N N   C TYR   B 2 121 ? -8.698  4.415   -23.430 0.25 66.63  ? 136 TYR   B N   1 
ATOM   1504 N N   D TYR   B 2 121 ? -8.698  4.415   -23.431 0.27 66.63  ? 136 TYR   B N   1 
ATOM   1505 C CA  A TYR   B 2 121 ? -9.611  5.594   -23.502 0.23 66.21  ? 136 TYR   B CA  1 
ATOM   1506 C CA  B TYR   B 2 121 ? -9.611  5.594   -23.502 0.25 66.21  ? 136 TYR   B CA  1 
ATOM   1507 C CA  C TYR   B 2 121 ? -9.630  5.567   -23.513 0.25 66.28  ? 136 TYR   B CA  1 
ATOM   1508 C CA  D TYR   B 2 121 ? -9.630  5.567   -23.514 0.27 66.28  ? 136 TYR   B CA  1 
ATOM   1509 C C   A TYR   B 2 121 ? -9.298  6.526   -22.336 0.23 65.76  ? 136 TYR   B C   1 
ATOM   1510 C C   B TYR   B 2 121 ? -9.298  6.526   -22.336 0.25 65.76  ? 136 TYR   B C   1 
ATOM   1511 C C   C TYR   B 2 121 ? -9.343  6.526   -22.363 0.25 65.80  ? 136 TYR   B C   1 
ATOM   1512 C C   D TYR   B 2 121 ? -9.343  6.526   -22.363 0.27 65.80  ? 136 TYR   B C   1 
ATOM   1513 O O   A TYR   B 2 121 ? -8.679  6.104   -21.358 0.23 65.97  ? 136 TYR   B O   1 
ATOM   1514 O O   B TYR   B 2 121 ? -8.679  6.103   -21.358 0.25 65.97  ? 136 TYR   B O   1 
ATOM   1515 O O   C TYR   B 2 121 ? -8.717  6.136   -21.376 0.25 66.02  ? 136 TYR   B O   1 
ATOM   1516 O O   D TYR   B 2 121 ? -8.717  6.135   -21.376 0.27 66.02  ? 136 TYR   B O   1 
ATOM   1517 C CB  A TYR   B 2 121 ? -11.089 5.195   -23.509 0.23 65.82  ? 136 TYR   B CB  1 
ATOM   1518 C CB  B TYR   B 2 121 ? -11.089 5.195   -23.509 0.25 65.81  ? 136 TYR   B CB  1 
ATOM   1519 C CB  C TYR   B 2 121 ? -11.086 5.095   -23.504 0.25 65.96  ? 136 TYR   B CB  1 
ATOM   1520 C CB  D TYR   B 2 121 ? -11.086 5.095   -23.504 0.27 65.95  ? 136 TYR   B CB  1 
ATOM   1521 C CG  A TYR   B 2 121 ? -11.565 4.617   -24.814 0.23 67.03  ? 136 TYR   B CG  1 
ATOM   1522 C CG  B TYR   B 2 121 ? -11.565 4.617   -24.814 0.25 67.03  ? 136 TYR   B CG  1 
ATOM   1523 C CG  C TYR   B 2 121 ? -11.591 4.574   -24.824 0.25 67.20  ? 136 TYR   B CG  1 
ATOM   1524 C CG  D TYR   B 2 121 ? -11.591 4.574   -24.824 0.27 67.20  ? 136 TYR   B CG  1 
ATOM   1525 C CD1 A TYR   B 2 121 ? -11.867 5.437   -25.892 0.23 67.69  ? 136 TYR   B CD1 1 
ATOM   1526 C CD1 B TYR   B 2 121 ? -11.867 5.437   -25.892 0.25 67.69  ? 136 TYR   B CD1 1 
ATOM   1527 C CD1 C TYR   B 2 121 ? -11.830 5.434   -25.885 0.25 67.90  ? 136 TYR   B CD1 1 
ATOM   1528 C CD1 D TYR   B 2 121 ? -11.831 5.434   -25.885 0.27 67.90  ? 136 TYR   B CD1 1 
ATOM   1529 C CD2 A TYR   B 2 121 ? -11.679 3.247   -24.990 0.23 67.57  ? 136 TYR   B CD2 1 
ATOM   1530 C CD2 B TYR   B 2 121 ? -11.678 3.248   -24.990 0.25 67.57  ? 136 TYR   B CD2 1 
ATOM   1531 C CD2 C TYR   B 2 121 ? -11.820 3.222   -25.023 0.25 67.73  ? 136 TYR   B CD2 1 
ATOM   1532 C CD2 D TYR   B 2 121 ? -11.820 3.222   -25.023 0.27 67.74  ? 136 TYR   B CD2 1 
ATOM   1533 C CE1 A TYR   B 2 121 ? -12.285 4.911   -27.104 0.23 68.34  ? 136 TYR   B CE1 1 
ATOM   1534 C CE1 B TYR   B 2 121 ? -12.285 4.910   -27.104 0.25 68.34  ? 136 TYR   B CE1 1 
ATOM   1535 C CE1 C TYR   B 2 121 ? -12.286 4.965   -27.107 0.25 68.57  ? 136 TYR   B CE1 1 
ATOM   1536 C CE1 D TYR   B 2 121 ? -12.286 4.965   -27.107 0.27 68.57  ? 136 TYR   B CE1 1 
ATOM   1537 C CE2 A TYR   B 2 121 ? -12.098 2.705   -26.195 0.23 68.43  ? 136 TYR   B CE2 1 
ATOM   1538 C CE2 B TYR   B 2 121 ? -12.097 2.705   -26.195 0.25 68.44  ? 136 TYR   B CE2 1 
ATOM   1539 C CE2 C TYR   B 2 121 ? -12.278 2.736   -26.238 0.25 68.62  ? 136 TYR   B CE2 1 
ATOM   1540 C CE2 D TYR   B 2 121 ? -12.278 2.736   -26.238 0.27 68.62  ? 136 TYR   B CE2 1 
ATOM   1541 C CZ  A TYR   B 2 121 ? -12.397 3.539   -27.258 0.23 68.73  ? 136 TYR   B CZ  1 
ATOM   1542 C CZ  B TYR   B 2 121 ? -12.397 3.539   -27.258 0.25 68.73  ? 136 TYR   B CZ  1 
ATOM   1543 C CZ  C TYR   B 2 121 ? -12.508 3.611   -27.287 0.25 68.94  ? 136 TYR   B CZ  1 
ATOM   1544 C CZ  D TYR   B 2 121 ? -12.508 3.610   -27.287 0.27 68.94  ? 136 TYR   B CZ  1 
ATOM   1545 O OH  A TYR   B 2 121 ? -12.808 3.005   -28.447 0.23 69.80  ? 136 TYR   B OH  1 
ATOM   1546 O OH  B TYR   B 2 121 ? -12.807 3.004   -28.447 0.25 69.81  ? 136 TYR   B OH  1 
ATOM   1547 O OH  C TYR   B 2 121 ? -12.956 3.137   -28.488 0.25 70.09  ? 136 TYR   B OH  1 
ATOM   1548 O OH  D TYR   B 2 121 ? -12.956 3.136   -28.488 0.27 70.10  ? 136 TYR   B OH  1 
ATOM   1549 N N   A PRO   B 2 122 ? -9.718  7.812   -22.393 0.23 65.52  ? 137 PRO   B N   1 
ATOM   1550 N N   B PRO   B 2 122 ? -9.718  7.812   -22.393 0.25 65.51  ? 137 PRO   B N   1 
ATOM   1551 N N   C PRO   B 2 122 ? -9.796  7.797   -22.446 0.25 65.57  ? 137 PRO   B N   1 
ATOM   1552 N N   D PRO   B 2 122 ? -9.796  7.797   -22.446 0.27 65.56  ? 137 PRO   B N   1 
ATOM   1553 C CA  A PRO   B 2 122 ? -9.496  8.737   -21.287 0.23 65.26  ? 137 PRO   B CA  1 
ATOM   1554 C CA  B PRO   B 2 122 ? -9.496  8.736   -21.287 0.25 65.27  ? 137 PRO   B CA  1 
ATOM   1555 C CA  C PRO   B 2 122 ? -9.587  8.756   -21.368 0.25 65.28  ? 137 PRO   B CA  1 
ATOM   1556 C CA  D PRO   B 2 122 ? -9.587  8.756   -21.368 0.27 65.28  ? 137 PRO   B CA  1 
ATOM   1557 C C   A PRO   B 2 122 ? -10.187 8.226   -20.014 0.23 63.84  ? 137 PRO   B C   1 
ATOM   1558 C C   B PRO   B 2 122 ? -10.187 8.226   -20.014 0.25 63.84  ? 137 PRO   B C   1 
ATOM   1559 C C   C PRO   B 2 122 ? -10.264 8.248   -20.086 0.25 63.86  ? 137 PRO   B C   1 
ATOM   1560 C C   D PRO   B 2 122 ? -10.263 8.248   -20.086 0.27 63.86  ? 137 PRO   B C   1 
ATOM   1561 O O   A PRO   B 2 122 ? -11.214 7.566   -20.125 0.23 63.46  ? 137 PRO   B O   1 
ATOM   1562 O O   B PRO   B 2 122 ? -11.214 7.566   -20.126 0.25 63.47  ? 137 PRO   B O   1 
ATOM   1563 O O   C PRO   B 2 122 ? -11.313 7.628   -20.193 0.25 63.44  ? 137 PRO   B O   1 
ATOM   1564 O O   D PRO   B 2 122 ? -11.313 7.628   -20.194 0.27 63.44  ? 137 PRO   B O   1 
ATOM   1565 C CB  A PRO   B 2 122 ? -10.113 10.071  -21.738 0.23 65.72  ? 137 PRO   B CB  1 
ATOM   1566 C CB  B PRO   B 2 122 ? -10.112 10.071  -21.737 0.25 65.72  ? 137 PRO   B CB  1 
ATOM   1567 C CB  C PRO   B 2 122 ? -10.241 10.054  -21.872 0.25 65.78  ? 137 PRO   B CB  1 
ATOM   1568 C CB  D PRO   B 2 122 ? -10.240 10.054  -21.872 0.27 65.78  ? 137 PRO   B CB  1 
ATOM   1569 C CG  A PRO   B 2 122 ? -10.317 9.937   -23.235 0.23 66.38  ? 137 PRO   B CG  1 
ATOM   1570 C CG  B PRO   B 2 122 ? -10.317 9.937   -23.235 0.25 66.38  ? 137 PRO   B CG  1 
ATOM   1571 C CG  C PRO   B 2 122 ? -10.363 9.873   -23.370 0.25 66.49  ? 137 PRO   B CG  1 
ATOM   1572 C CG  D PRO   B 2 122 ? -10.363 9.873   -23.370 0.27 66.49  ? 137 PRO   B CG  1 
ATOM   1573 C CD  A PRO   B 2 122 ? -10.428 8.450   -23.512 0.23 66.54  ? 137 PRO   B CD  1 
ATOM   1574 C CD  B PRO   B 2 122 ? -10.429 8.450   -23.512 0.25 66.54  ? 137 PRO   B CD  1 
ATOM   1575 C CD  C PRO   B 2 122 ? -10.544 8.382   -23.570 0.25 66.58  ? 137 PRO   B CD  1 
ATOM   1576 C CD  D PRO   B 2 122 ? -10.544 8.382   -23.570 0.27 66.59  ? 137 PRO   B CD  1 
ATOM   1577 N N   A ALA   B 2 123 ? -9.613  8.558   -18.854 0.23 62.81  ? 138 ALA   B N   1 
ATOM   1578 N N   B ALA   B 2 123 ? -9.613  8.558   -18.854 0.25 62.81  ? 138 ALA   B N   1 
ATOM   1579 N N   C ALA   B 2 123 ? -9.655  8.521   -18.927 0.25 62.81  ? 138 ALA   B N   1 
ATOM   1580 N N   D ALA   B 2 123 ? -9.655  8.520   -18.927 0.27 62.81  ? 138 ALA   B N   1 
ATOM   1581 C CA  A ALA   B 2 123 ? -10.110 8.201   -17.504 0.23 61.26  ? 138 ALA   B CA  1 
ATOM   1582 C CA  B ALA   B 2 123 ? -10.110 8.201   -17.504 0.25 61.26  ? 138 ALA   B CA  1 
ATOM   1583 C CA  C ALA   B 2 123 ? -10.146 8.117   -17.586 0.25 61.25  ? 138 ALA   B CA  1 
ATOM   1584 C CA  D ALA   B 2 123 ? -10.146 8.117   -17.586 0.27 61.25  ? 138 ALA   B CA  1 
ATOM   1585 C C   A ALA   B 2 123 ? -11.607 8.517   -17.376 0.23 60.07  ? 138 ALA   B C   1 
ATOM   1586 C C   B ALA   B 2 123 ? -11.607 8.517   -17.376 0.25 60.07  ? 138 ALA   B C   1 
ATOM   1587 C C   C ALA   B 2 123 ? -11.628 8.480   -17.418 0.25 60.08  ? 138 ALA   B C   1 
ATOM   1588 C C   D ALA   B 2 123 ? -11.628 8.479   -17.418 0.27 60.08  ? 138 ALA   B C   1 
ATOM   1589 O O   A ALA   B 2 123 ? -12.321 7.760   -16.650 0.23 58.34  ? 138 ALA   B O   1 
ATOM   1590 O O   B ALA   B 2 123 ? -12.322 7.760   -16.650 0.25 58.33  ? 138 ALA   B O   1 
ATOM   1591 O O   C ALA   B 2 123 ? -12.346 7.736   -16.682 0.25 58.41  ? 138 ALA   B O   1 
ATOM   1592 O O   D ALA   B 2 123 ? -12.347 7.736   -16.682 0.27 58.40  ? 138 ALA   B O   1 
ATOM   1593 C CB  A ALA   B 2 123 ? -9.294  8.931   -16.469 0.23 61.33  ? 138 ALA   B CB  1 
ATOM   1594 C CB  B ALA   B 2 123 ? -9.294  8.931   -16.469 0.25 61.33  ? 138 ALA   B CB  1 
ATOM   1595 C CB  C ALA   B 2 123 ? -9.309  8.769   -16.519 0.25 61.29  ? 138 ALA   B CB  1 
ATOM   1596 C CB  D ALA   B 2 123 ? -9.308  8.769   -16.520 0.27 61.29  ? 138 ALA   B CB  1 
ATOM   1597 N N   . GLY   B 2 124 ? -12.071 9.562   -18.094 1.00 59.47  ? 139 GLY   B N   1 
ATOM   1598 C CA  . GLY   B 2 124 ? -13.470 10.012  -18.048 1.00 57.64  ? 139 GLY   B CA  1 
ATOM   1599 C C   . GLY   B 2 124 ? -14.416 9.036   -18.714 1.00 54.73  ? 139 GLY   B C   1 
ATOM   1600 O O   . GLY   B 2 124 ? -15.666 9.221   -18.558 1.00 53.65  ? 139 GLY   B O   1 
ATOM   1601 N N   . THR   B 2 125 ? -13.859 8.012   -19.358 1.00 54.29  ? 140 THR   B N   1 
ATOM   1602 C CA  . THR   B 2 125 ? -14.633 6.878   -19.927 1.00 54.94  ? 140 THR   B CA  1 
ATOM   1603 C C   . THR   B 2 125 ? -14.952 5.793   -18.866 1.00 54.46  ? 140 THR   B C   1 
ATOM   1604 O O   . THR   B 2 125 ? -15.754 4.859   -19.226 1.00 54.29  ? 140 THR   B O   1 
ATOM   1605 C CB  . THR   B 2 125 ? -13.921 6.281   -21.152 1.00 56.74  ? 140 THR   B CB  1 
ATOM   1606 O OG1 . THR   B 2 125 ? -13.594 7.338   -22.066 1.00 57.76  ? 140 THR   B OG1 1 
ATOM   1607 C CG2 . THR   B 2 125 ? -14.749 5.308   -21.972 1.00 56.60  ? 140 THR   B CG2 1 
ATOM   1608 N N   A SER   B 2 126 ? -14.371 5.895   -17.651 0.23 54.02  ? 141 SER   B N   1 
ATOM   1609 N N   B SER   B 2 126 ? -14.371 5.895   -17.651 0.25 54.02  ? 141 SER   B N   1 
ATOM   1610 N N   C SER   B 2 126 ? -14.362 5.884   -17.660 0.25 54.04  ? 141 SER   B N   1 
ATOM   1611 N N   D SER   B 2 126 ? -14.362 5.884   -17.660 0.27 54.04  ? 141 SER   B N   1 
ATOM   1612 C CA  A SER   B 2 126 ? -14.541 4.921   -16.529 0.23 53.33  ? 141 SER   B CA  1 
ATOM   1613 C CA  B SER   B 2 126 ? -14.541 4.921   -16.529 0.25 53.33  ? 141 SER   B CA  1 
ATOM   1614 C CA  C SER   B 2 126 ? -14.541 4.886   -16.564 0.25 53.37  ? 141 SER   B CA  1 
ATOM   1615 C CA  D SER   B 2 126 ? -14.541 4.886   -16.564 0.27 53.37  ? 141 SER   B CA  1 
ATOM   1616 C C   A SER   B 2 126 ? -16.070 4.757   -16.269 0.23 52.49  ? 141 SER   B C   1 
ATOM   1617 C C   B SER   B 2 126 ? -16.070 4.758   -16.270 0.25 52.49  ? 141 SER   B C   1 
ATOM   1618 C C   C SER   B 2 126 ? -16.067 4.754   -16.291 0.25 52.50  ? 141 SER   B C   1 
ATOM   1619 C C   D SER   B 2 126 ? -16.068 4.754   -16.292 0.27 52.50  ? 141 SER   B C   1 
ATOM   1620 O O   A SER   B 2 126 ? -16.815 5.841   -16.182 0.23 52.76  ? 141 SER   B O   1 
ATOM   1621 O O   B SER   B 2 126 ? -16.815 5.841   -16.185 0.25 52.77  ? 141 SER   B O   1 
ATOM   1622 O O   C SER   B 2 126 ? -16.801 5.847   -16.233 0.25 52.77  ? 141 SER   B O   1 
ATOM   1623 O O   D SER   B 2 126 ? -16.801 5.847   -16.234 0.27 52.77  ? 141 SER   B O   1 
ATOM   1624 C CB  A SER   B 2 126 ? -13.803 5.352   -15.253 0.23 53.14  ? 141 SER   B CB  1 
ATOM   1625 C CB  B SER   B 2 126 ? -13.803 5.353   -15.252 0.25 53.14  ? 141 SER   B CB  1 
ATOM   1626 C CB  C SER   B 2 126 ? -13.780 5.259   -15.298 0.25 53.20  ? 141 SER   B CB  1 
ATOM   1627 C CB  D SER   B 2 126 ? -13.780 5.258   -15.298 0.27 53.20  ? 141 SER   B CB  1 
ATOM   1628 O OG  A SER   B 2 126 ? -12.395 5.133   -15.363 0.23 53.57  ? 141 SER   B OG  1 
ATOM   1629 O OG  B SER   B 2 126 ? -12.395 5.133   -15.362 0.25 53.57  ? 141 SER   B OG  1 
ATOM   1630 O OG  C SER   B 2 126 ? -12.387 5.015   -15.446 0.25 53.69  ? 141 SER   B OG  1 
ATOM   1631 O OG  D SER   B 2 126 ? -12.387 5.014   -15.446 0.27 53.69  ? 141 SER   B OG  1 
ATOM   1632 N N   . GLY   B 2 127 ? -16.499 3.439   -16.282 1.00 52.36  ? 142 GLY   B N   1 
ATOM   1633 C CA  . GLY   B 2 127 ? -17.924 3.138   -16.008 1.00 52.28  ? 142 GLY   B CA  1 
ATOM   1634 C C   . GLY   B 2 127 ? -18.634 2.616   -17.235 1.00 53.10  ? 142 GLY   B C   1 
ATOM   1635 O O   . GLY   B 2 127 ? -19.783 2.140   -17.107 1.00 53.32  ? 142 GLY   B O   1 
ATOM   1636 N N   . SER   B 2 128 ? -18.012 2.807   -18.414 1.00 53.47  ? 143 SER   B N   1 
ATOM   1637 C CA  . SER   B 2 128 ? -18.574 2.342   -19.699 1.00 53.99  ? 143 SER   B CA  1 
ATOM   1638 C C   . SER   B 2 128 ? -18.790 0.791   -19.649 1.00 53.96  ? 143 SER   B C   1 
ATOM   1639 O O   . SER   B 2 128 ? -17.936 0.055   -19.208 1.00 54.80  ? 143 SER   B O   1 
ATOM   1640 C CB  . SER   B 2 128 ? -17.681 2.712   -20.881 1.00 54.63  ? 143 SER   B CB  1 
ATOM   1641 O OG  . SER   B 2 128 ? -17.778 4.113   -21.187 1.00 54.47  ? 143 SER   B OG  1 
ATOM   1642 N N   . PRO   B 2 129 ? -19.973 0.323   -20.069 1.00 53.37  ? 144 PRO   B N   1 
ATOM   1643 C CA  . PRO   B 2 129 ? -20.370 -1.086  -19.986 1.00 53.65  ? 144 PRO   B CA  1 
ATOM   1644 C C   . PRO   B 2 129 ? -19.765 -1.971  -21.064 1.00 55.66  ? 144 PRO   B C   1 
ATOM   1645 O O   . PRO   B 2 129 ? -19.573 -1.515  -22.206 1.00 57.24  ? 144 PRO   B O   1 
ATOM   1646 C CB  . PRO   B 2 129 ? -21.888 -1.115  -20.192 1.00 53.44  ? 144 PRO   B CB  1 
ATOM   1647 C CG  . PRO   B 2 129 ? -22.175 0.129   -20.989 1.00 53.13  ? 144 PRO   B CG  1 
ATOM   1648 C CD  . PRO   B 2 129 ? -21.143 1.133   -20.503 1.00 53.04  ? 144 PRO   B CD  1 
ATOM   1649 N N   . ILE   B 2 130 ? -19.591 -3.234  -20.691 1.00 55.48  ? 145 ILE   B N   1 
ATOM   1650 C CA  . ILE   B 2 130 ? -19.090 -4.308  -21.563 1.00 56.81  ? 145 ILE   B CA  1 
ATOM   1651 C C   . ILE   B 2 130 ? -20.259 -5.257  -21.709 1.00 58.25  ? 145 ILE   B C   1 
ATOM   1652 O O   . ILE   B 2 130 ? -20.958 -5.434  -20.694 1.00 56.18  ? 145 ILE   B O   1 
ATOM   1653 C CB  . ILE   B 2 130 ? -17.842 -4.940  -20.970 1.00 56.71  ? 145 ILE   B CB  1 
ATOM   1654 C CG1 . ILE   B 2 130 ? -16.732 -3.908  -20.789 1.00 56.71  ? 145 ILE   B CG1 1 
ATOM   1655 C CG2 . ILE   B 2 130 ? -17.382 -6.108  -21.805 1.00 58.06  ? 145 ILE   B CG2 1 
ATOM   1656 C CD1 . ILE   B 2 130 ? -15.736 -4.276  -19.697 1.00 57.29  ? 145 ILE   B CD1 1 
ATOM   1657 N N   . LEU   B 2 131 ? -20.563 -5.630  -22.967 1.00 60.07  ? 146 LEU   B N   1 
ATOM   1658 C CA  . LEU   B 2 131 ? -21.781 -6.380  -23.367 1.00 62.41  ? 146 LEU   B CA  1 
ATOM   1659 C C   . LEU   B 2 131 ? -21.421 -7.733  -23.991 1.00 63.66  ? 146 LEU   B C   1 
ATOM   1660 O O   . LEU   B 2 131 ? -20.375 -7.800  -24.671 1.00 64.38  ? 146 LEU   B O   1 
ATOM   1661 C CB  . LEU   B 2 131 ? -22.518 -5.582  -24.439 1.00 65.06  ? 146 LEU   B CB  1 
ATOM   1662 C CG  . LEU   B 2 131 ? -22.586 -4.082  -24.227 1.00 65.59  ? 146 LEU   B CG  1 
ATOM   1663 C CD1 . LEU   B 2 131 ? -23.433 -3.465  -25.333 1.00 67.26  ? 146 LEU   B CD1 1 
ATOM   1664 C CD2 . LEU   B 2 131 ? -23.144 -3.783  -22.847 1.00 66.11  ? 146 LEU   B CD2 1 
ATOM   1665 N N   . ASP   B 2 132 ? -22.315 -8.728  -23.754 1.00 64.49  ? 147 ASP   B N   1 
ATOM   1666 C CA  . ASP   B 2 132 ? -22.316 -10.017 -24.494 1.00 67.04  ? 147 ASP   B CA  1 
ATOM   1667 C C   . ASP   B 2 132 ? -23.146 -9.831  -25.791 1.00 69.41  ? 147 ASP   B C   1 
ATOM   1668 O O   . ASP   B 2 132 ? -23.715 -8.717  -26.013 1.00 68.37  ? 147 ASP   B O   1 
ATOM   1669 C CB  . ASP   B 2 132 ? -22.774 -11.201 -23.626 1.00 66.88  ? 147 ASP   B CB  1 
ATOM   1670 C CG  . ASP   B 2 132 ? -24.213 -11.173 -23.131 1.00 66.94  ? 147 ASP   B CG  1 
ATOM   1671 O OD1 . ASP   B 2 132 ? -25.066 -10.498 -23.743 1.00 66.66  ? 147 ASP   B OD1 1 
ATOM   1672 O OD2 . ASP   B 2 132 ? -24.454 -11.788 -22.058 1.00 69.24  ? 147 ASP   B OD2 1 
ATOM   1673 N N   . LYS   B 2 133 ? -23.244 -10.880 -26.599 1.00 72.52  ? 148 LYS   B N   1 
ATOM   1674 C CA  . LYS   B 2 133 ? -23.896 -10.827 -27.939 1.00 76.43  ? 148 LYS   B CA  1 
ATOM   1675 C C   . LYS   B 2 133 ? -25.405 -10.674 -27.727 1.00 75.63  ? 148 LYS   B C   1 
ATOM   1676 O O   . LYS   B 2 133 ? -26.079 -10.204 -28.654 1.00 75.34  ? 148 LYS   B O   1 
ATOM   1677 C CB  . LYS   B 2 133 ? -23.519 -12.042 -28.803 1.00 80.42  ? 148 LYS   B CB  1 
ATOM   1678 C CG  . LYS   B 2 133 ? -22.108 -12.009 -29.395 1.00 83.93  ? 148 LYS   B CG  1 
ATOM   1679 C CD  . LYS   B 2 133 ? -21.385 -13.379 -29.499 1.00 87.57  ? 148 LYS   B CD  1 
ATOM   1680 C CE  . LYS   B 2 133 ? -19.894 -13.254 -29.791 1.00 89.23  ? 148 LYS   B CE  1 
ATOM   1681 N NZ  . LYS   B 2 133 ? -19.263 -14.524 -30.247 1.00 91.34  ? 148 LYS   B NZ  1 
ATOM   1682 N N   . CYS   B 2 134 ? -25.907 -10.976 -26.525 1.00 73.92  ? 149 CYS   B N   1 
ATOM   1683 C CA  . CYS   B 2 134 ? -27.350 -10.818 -26.216 1.00 73.53  ? 149 CYS   B CA  1 
ATOM   1684 C C   . CYS   B 2 134 ? -27.618 -9.390  -25.718 1.00 70.49  ? 149 CYS   B C   1 
ATOM   1685 O O   . CYS   B 2 134 ? -28.757 -9.090  -25.421 1.00 70.36  ? 149 CYS   B O   1 
ATOM   1686 C CB  . CYS   B 2 134 ? -27.829 -11.877 -25.231 1.00 75.54  ? 149 CYS   B CB  1 
ATOM   1687 S SG  . CYS   B 2 134 ? -28.039 -13.512 -25.984 1.00 79.03  ? 149 CYS   B SG  1 
ATOM   1688 N N   . GLY   B 2 135 ? -26.616 -8.515  -25.681 1.00 68.36  ? 150 GLY   B N   1 
ATOM   1689 C CA  . GLY   B 2 135 ? -26.783 -7.134  -25.175 1.00 66.26  ? 150 GLY   B CA  1 
ATOM   1690 C C   . GLY   B 2 135 ? -26.772 -7.019  -23.639 1.00 64.45  ? 150 GLY   B C   1 
ATOM   1691 O O   . GLY   B 2 135 ? -27.011 -5.923  -23.171 1.00 63.09  ? 150 GLY   B O   1 
ATOM   1692 N N   . ARG   B 2 136 ? -26.497 -8.101  -22.899 1.00 64.48  ? 151 ARG   B N   1 
ATOM   1693 C CA  . ARG   B 2 136 ? -26.447 -8.139  -21.405 1.00 64.26  ? 151 ARG   B CA  1 
ATOM   1694 C C   . ARG   B 2 136 ? -25.128 -7.540  -20.908 1.00 61.43  ? 151 ARG   B C   1 
ATOM   1695 O O   . ARG   B 2 136 ? -24.067 -7.853  -21.504 1.00 60.92  ? 151 ARG   B O   1 
ATOM   1696 C CB  . ARG   B 2 136 ? -26.661 -9.576  -20.927 1.00 66.35  ? 151 ARG   B CB  1 
ATOM   1697 C CG  . ARG   B 2 136 ? -28.124 -9.989  -20.956 1.00 68.35  ? 151 ARG   B CG  1 
ATOM   1698 C CD  . ARG   B 2 136 ? -28.286 -11.416 -20.542 1.00 71.43  ? 151 ARG   B CD  1 
ATOM   1699 N NE  . ARG   B 2 136 ? -27.442 -12.238 -21.393 1.00 75.30  ? 151 ARG   B NE  1 
ATOM   1700 C CZ  . ARG   B 2 136 ? -26.831 -13.358 -21.029 1.00 77.58  ? 151 ARG   B CZ  1 
ATOM   1701 N NH1 . ARG   B 2 136 ? -26.938 -13.844 -19.794 1.00 80.93  ? 151 ARG   B NH1 1 
ATOM   1702 N NH2 . ARG   B 2 136 ? -26.096 -13.986 -21.917 1.00 79.76  ? 151 ARG   B NH2 1 
ATOM   1703 N N   . VAL   B 2 137 ? -25.183 -6.688  -19.886 1.00 59.72  ? 152 VAL   B N   1 
ATOM   1704 C CA  . VAL   B 2 137 ? -23.963 -6.030  -19.329 1.00 57.76  ? 152 VAL   B CA  1 
ATOM   1705 C C   . VAL   B 2 137 ? -23.230 -7.059  -18.470 1.00 58.03  ? 152 VAL   B C   1 
ATOM   1706 O O   . VAL   B 2 137 ? -23.757 -7.477  -17.391 1.00 58.10  ? 152 VAL   B O   1 
ATOM   1707 C CB  . VAL   B 2 137 ? -24.248 -4.753  -18.541 1.00 56.79  ? 152 VAL   B CB  1 
ATOM   1708 C CG1 . VAL   B 2 137 ? -22.950 -4.068  -18.156 1.00 56.93  ? 152 VAL   B CG1 1 
ATOM   1709 C CG2 . VAL   B 2 137 ? -25.160 -3.774  -19.234 1.00 56.43  ? 152 VAL   B CG2 1 
ATOM   1710 N N   . ILE   B 2 138 ? -22.029 -7.409  -18.884 1.00 57.51  ? 153 ILE   B N   1 
ATOM   1711 C CA  . ILE   B 2 138 ? -21.215 -8.433  -18.186 1.00 58.16  ? 153 ILE   B CA  1 
ATOM   1712 C C   . ILE   B 2 138 ? -20.178 -7.760  -17.285 1.00 56.65  ? 153 ILE   B C   1 
ATOM   1713 O O   . ILE   B 2 138 ? -19.432 -8.528  -16.559 1.00 58.27  ? 153 ILE   B O   1 
ATOM   1714 C CB  . ILE   B 2 138 ? -20.519 -9.378  -19.185 1.00 58.91  ? 153 ILE   B CB  1 
ATOM   1715 C CG1 . ILE   B 2 138 ? -19.661 -8.600  -20.179 1.00 59.24  ? 153 ILE   B CG1 1 
ATOM   1716 C CG2 . ILE   B 2 138 ? -21.528 -10.295 -19.830 1.00 59.32  ? 153 ILE   B CG2 1 
ATOM   1717 C CD1 . ILE   B 2 138 ? -18.703 -9.479  -20.962 1.00 61.36  ? 153 ILE   B CD1 1 
ATOM   1718 N N   . GLY   B 2 139 ? -20.065 -6.430  -17.343 1.00 55.88  ? 154 GLY   B N   1 
ATOM   1719 C CA  . GLY   B 2 139 ? -19.181 -5.683  -16.416 1.00 55.27  ? 154 GLY   B CA  1 
ATOM   1720 C C   . GLY   B 2 139 ? -18.951 -4.253  -16.851 1.00 54.90  ? 154 GLY   B C   1 
ATOM   1721 O O   . GLY   B 2 139 ? -19.422 -3.882  -17.969 1.00 54.01  ? 154 GLY   B O   1 
ATOM   1722 N N   . LEU   B 2 140 ? -18.176 -3.502  -16.072 1.00 53.84  ? 155 LEU   B N   1 
ATOM   1723 C CA  . LEU   B 2 140 ? -17.837 -2.101  -16.386 1.00 54.16  ? 155 LEU   B CA  1 
ATOM   1724 C C   . LEU   B 2 140 ? -16.332 -1.956  -16.591 1.00 54.96  ? 155 LEU   B C   1 
ATOM   1725 O O   . LEU   B 2 140 ? -15.514 -2.682  -15.921 1.00 54.25  ? 155 LEU   B O   1 
ATOM   1726 C CB  . LEU   B 2 140 ? -18.292 -1.150  -15.280 1.00 53.07  ? 155 LEU   B CB  1 
ATOM   1727 C CG  . LEU   B 2 140 ? -19.743 -1.196  -14.817 1.00 52.82  ? 155 LEU   B CG  1 
ATOM   1728 C CD1 . LEU   B 2 140 ? -19.947 -0.059  -13.829 1.00 53.00  ? 155 LEU   B CD1 1 
ATOM   1729 C CD2 . LEU   B 2 140 ? -20.764 -1.090  -15.942 1.00 54.04  ? 155 LEU   B CD2 1 
ATOM   1730 N N   A TYR   B 2 141 ? -15.983 -1.068  -17.532 0.23 54.90  ? 156 TYR   B N   1 
ATOM   1731 N N   B TYR   B 2 141 ? -15.983 -1.068  -17.533 0.25 54.90  ? 156 TYR   B N   1 
ATOM   1732 N N   C TYR   B 2 141 ? -15.961 -1.016  -17.466 0.25 55.13  ? 156 TYR   B N   1 
ATOM   1733 N N   D TYR   B 2 141 ? -15.961 -1.016  -17.466 0.27 55.13  ? 156 TYR   B N   1 
ATOM   1734 C CA  A TYR   B 2 141 ? -14.616 -0.619  -17.907 0.23 55.41  ? 156 TYR   B CA  1 
ATOM   1735 C CA  B TYR   B 2 141 ? -14.617 -0.620  -17.908 0.25 55.41  ? 156 TYR   B CA  1 
ATOM   1736 C CA  C TYR   B 2 141 ? -14.571 -0.649  -17.844 0.25 55.76  ? 156 TYR   B CA  1 
ATOM   1737 C CA  D TYR   B 2 141 ? -14.571 -0.650  -17.843 0.27 55.76  ? 156 TYR   B CA  1 
ATOM   1738 C C   A TYR   B 2 141 ? -14.146 0.453   -16.924 0.23 55.31  ? 156 TYR   B C   1 
ATOM   1739 C C   B TYR   B 2 141 ? -14.146 0.452   -16.925 0.25 55.31  ? 156 TYR   B C   1 
ATOM   1740 C C   C TYR   B 2 141 ? -14.113 0.524   -16.978 0.25 55.67  ? 156 TYR   B C   1 
ATOM   1741 C C   D TYR   B 2 141 ? -14.112 0.523   -16.978 0.27 55.67  ? 156 TYR   B C   1 
ATOM   1742 O O   A TYR   B 2 141 ? -15.029 1.217   -16.414 0.23 55.46  ? 156 TYR   B O   1 
ATOM   1743 O O   B TYR   B 2 141 ? -15.029 1.217   -16.415 0.25 55.47  ? 156 TYR   B O   1 
ATOM   1744 O O   C TYR   B 2 141 ? -14.969 1.413   -16.701 0.25 55.86  ? 156 TYR   B O   1 
ATOM   1745 O O   D TYR   B 2 141 ? -14.968 1.413   -16.702 0.27 55.87  ? 156 TYR   B O   1 
ATOM   1746 C CB  A TYR   B 2 141 ? -14.664 -0.033  -19.328 0.23 56.20  ? 156 TYR   B CB  1 
ATOM   1747 C CB  B TYR   B 2 141 ? -14.665 -0.032  -19.328 0.25 56.20  ? 156 TYR   B CB  1 
ATOM   1748 C CB  C TYR   B 2 141 ? -14.567 -0.263  -19.328 0.25 56.83  ? 156 TYR   B CB  1 
ATOM   1749 C CB  D TYR   B 2 141 ? -14.566 -0.263  -19.328 0.27 56.84  ? 156 TYR   B CB  1 
ATOM   1750 C CG  A TYR   B 2 141 ? -13.374 0.522   -19.891 0.23 56.50  ? 156 TYR   B CG  1 
ATOM   1751 C CG  B TYR   B 2 141 ? -13.375 0.523   -19.891 0.25 56.50  ? 156 TYR   B CG  1 
ATOM   1752 C CG  C TYR   B 2 141 ? -13.325 0.403   -19.874 0.25 57.14  ? 156 TYR   B CG  1 
ATOM   1753 C CG  D TYR   B 2 141 ? -13.324 0.402   -19.874 0.27 57.14  ? 156 TYR   B CG  1 
ATOM   1754 C CD1 A TYR   B 2 141 ? -13.104 1.882   -19.856 0.23 56.30  ? 156 TYR   B CD1 1 
ATOM   1755 C CD1 B TYR   B 2 141 ? -13.104 1.883   -19.856 0.25 56.30  ? 156 TYR   B CD1 1 
ATOM   1756 C CD1 C TYR   B 2 141 ? -13.130 1.772   -19.764 0.25 56.94  ? 156 TYR   B CD1 1 
ATOM   1757 C CD1 D TYR   B 2 141 ? -13.130 1.771   -19.765 0.27 56.94  ? 156 TYR   B CD1 1 
ATOM   1758 C CD2 A TYR   B 2 141 ? -12.444 -0.303  -20.506 0.23 57.15  ? 156 TYR   B CD2 1 
ATOM   1759 C CD2 B TYR   B 2 141 ? -12.444 -0.302  -20.507 0.25 57.15  ? 156 TYR   B CD2 1 
ATOM   1760 C CD2 C TYR   B 2 141 ? -12.373 -0.328  -20.562 0.25 57.86  ? 156 TYR   B CD2 1 
ATOM   1761 C CD2 D TYR   B 2 141 ? -12.371 -0.330  -20.561 0.27 57.86  ? 156 TYR   B CD2 1 
ATOM   1762 C CE1 A TYR   B 2 141 ? -11.930 2.403   -20.382 0.23 56.87  ? 156 TYR   B CE1 1 
ATOM   1763 C CE1 B TYR   B 2 141 ? -11.930 2.403   -20.382 0.25 56.87  ? 156 TYR   B CE1 1 
ATOM   1764 C CE1 C TYR   B 2 141 ? -11.998 2.387   -20.279 0.25 57.47  ? 156 TYR   B CE1 1 
ATOM   1765 C CE1 D TYR   B 2 141 ? -11.998 2.386   -20.280 0.27 57.47  ? 156 TYR   B CE1 1 
ATOM   1766 C CE2 A TYR   B 2 141 ? -11.270 0.203   -21.050 0.23 57.84  ? 156 TYR   B CE2 1 
ATOM   1767 C CE2 B TYR   B 2 141 ? -11.271 0.203   -21.051 0.25 57.83  ? 156 TYR   B CE2 1 
ATOM   1768 C CE2 C TYR   B 2 141 ? -11.242 0.271   -21.098 0.25 58.53  ? 156 TYR   B CE2 1 
ATOM   1769 C CE2 D TYR   B 2 141 ? -11.241 0.270   -21.098 0.27 58.53  ? 156 TYR   B CE2 1 
ATOM   1770 C CZ  A TYR   B 2 141 ? -11.011 1.563   -20.999 0.23 57.72  ? 156 TYR   B CZ  1 
ATOM   1771 C CZ  B TYR   B 2 141 ? -11.012 1.563   -21.000 0.25 57.72  ? 156 TYR   B CZ  1 
ATOM   1772 C CZ  C TYR   B 2 141 ? -11.052 1.636   -20.965 0.25 58.38  ? 156 TYR   B CZ  1 
ATOM   1773 C CZ  D TYR   B 2 141 ? -11.052 1.636   -20.966 0.27 58.38  ? 156 TYR   B CZ  1 
ATOM   1774 O OH  A TYR   B 2 141 ? -9.857  2.061   -21.552 0.23 58.18  ? 156 TYR   B OH  1 
ATOM   1775 O OH  B TYR   B 2 141 ? -9.857  2.061   -21.553 0.25 58.18  ? 156 TYR   B OH  1 
ATOM   1776 O OH  C TYR   B 2 141 ? -9.937  2.216   -21.518 0.25 58.89  ? 156 TYR   B OH  1 
ATOM   1777 O OH  D TYR   B 2 141 ? -9.937  2.216   -21.520 0.27 58.89  ? 156 TYR   B OH  1 
ATOM   1778 N N   A GLY   B 2 142 ? -12.828 0.520   -16.655 0.23 56.11  ? 157 GLY   B N   1 
ATOM   1779 N N   B GLY   B 2 142 ? -12.828 0.519   -16.655 0.25 56.10  ? 157 GLY   B N   1 
ATOM   1780 N N   C GLY   B 2 142 ? -12.832 0.552   -16.572 0.25 56.39  ? 157 GLY   B N   1 
ATOM   1781 N N   D GLY   B 2 142 ? -12.832 0.551   -16.572 0.27 56.39  ? 157 GLY   B N   1 
ATOM   1782 C CA  A GLY   B 2 142 ? -12.233 1.674   -15.946 0.23 56.38  ? 157 GLY   B CA  1 
ATOM   1783 C CA  B GLY   B 2 142 ? -12.232 1.673   -15.946 0.25 56.38  ? 157 GLY   B CA  1 
ATOM   1784 C CA  C GLY   B 2 142 ? -12.292 1.690   -15.798 0.25 56.62  ? 157 GLY   B CA  1 
ATOM   1785 C CA  D GLY   B 2 142 ? -12.291 1.690   -15.798 0.27 56.62  ? 157 GLY   B CA  1 
ATOM   1786 C C   A GLY   B 2 142 ? -11.397 1.331   -14.716 0.23 56.74  ? 157 GLY   B C   1 
ATOM   1787 C C   B GLY   B 2 142 ? -11.397 1.330   -14.716 0.25 56.74  ? 157 GLY   B C   1 
ATOM   1788 C C   C GLY   B 2 142 ? -11.327 1.308   -14.683 0.25 57.06  ? 157 GLY   B C   1 
ATOM   1789 C C   D GLY   B 2 142 ? -11.327 1.308   -14.683 0.27 57.06  ? 157 GLY   B C   1 
ATOM   1790 O O   A GLY   B 2 142 ? -10.882 2.295   -14.095 0.23 56.87  ? 157 GLY   B O   1 
ATOM   1791 O O   B GLY   B 2 142 ? -10.883 2.295   -14.094 0.25 56.87  ? 157 GLY   B O   1 
ATOM   1792 O O   C GLY   B 2 142 ? -10.646 2.230   -14.172 0.25 57.37  ? 157 GLY   B O   1 
ATOM   1793 O O   D GLY   B 2 142 ? -10.647 2.230   -14.171 0.27 57.37  ? 157 GLY   B O   1 
ATOM   1794 N N   A ASN   B 2 143 ? -11.264 0.048   -14.341 0.23 57.16  ? 158 ASN   B N   1 
ATOM   1795 N N   B ASN   B 2 143 ? -11.264 0.048   -14.341 0.25 57.16  ? 158 ASN   B N   1 
ATOM   1796 N N   C ASN   B 2 143 ? -11.275 0.032   -14.280 0.25 57.39  ? 158 ASN   B N   1 
ATOM   1797 N N   D ASN   B 2 143 ? -11.275 0.032   -14.279 0.27 57.39  ? 158 ASN   B N   1 
ATOM   1798 C CA  A ASN   B 2 143 ? -10.327 -0.385  -13.263 0.23 57.30  ? 158 ASN   B CA  1 
ATOM   1799 C CA  B ASN   B 2 143 ? -10.327 -0.385  -13.262 0.25 57.29  ? 158 ASN   B CA  1 
ATOM   1800 C CA  C ASN   B 2 143 ? -10.333 -0.442  -13.227 0.25 57.49  ? 158 ASN   B CA  1 
ATOM   1801 C CA  D ASN   B 2 143 ? -10.333 -0.442  -13.227 0.27 57.49  ? 158 ASN   B CA  1 
ATOM   1802 C C   A ASN   B 2 143 ? -9.356  -1.435  -13.821 0.23 58.21  ? 158 ASN   B C   1 
ATOM   1803 C C   B ASN   B 2 143 ? -9.356  -1.435  -13.820 0.25 58.20  ? 158 ASN   B C   1 
ATOM   1804 C C   C ASN   B 2 143 ? -9.351  -1.448  -13.838 0.25 58.33  ? 158 ASN   B C   1 
ATOM   1805 C C   D ASN   B 2 143 ? -9.351  -1.448  -13.838 0.27 58.33  ? 158 ASN   B C   1 
ATOM   1806 O O   A ASN   B 2 143 ? -9.808  -2.606  -14.091 0.23 59.01  ? 158 ASN   B O   1 
ATOM   1807 O O   B ASN   B 2 143 ? -9.808  -2.606  -14.090 0.25 59.02  ? 158 ASN   B O   1 
ATOM   1808 O O   C ASN   B 2 143 ? -9.792  -2.602  -14.178 0.25 59.17  ? 158 ASN   B O   1 
ATOM   1809 O O   D ASN   B 2 143 ? -9.792  -2.603  -14.176 0.27 59.17  ? 158 ASN   B O   1 
ATOM   1810 C CB  A ASN   B 2 143 ? -11.046 -0.938  -12.024 0.23 56.90  ? 158 ASN   B CB  1 
ATOM   1811 C CB  B ASN   B 2 143 ? -11.045 -0.938  -12.023 0.25 56.90  ? 158 ASN   B CB  1 
ATOM   1812 C CB  C ASN   B 2 143 ? -11.059 -1.067  -12.029 0.25 57.15  ? 158 ASN   B CB  1 
ATOM   1813 C CB  D ASN   B 2 143 ? -11.058 -1.067  -12.029 0.27 57.15  ? 158 ASN   B CB  1 
ATOM   1814 C CG  A ASN   B 2 143 ? -10.159 -0.987  -10.789 0.23 56.92  ? 158 ASN   B CG  1 
ATOM   1815 C CG  B ASN   B 2 143 ? -10.159 -0.986  -10.788 0.25 56.92  ? 158 ASN   B CG  1 
ATOM   1816 C CG  C ASN   B 2 143 ? -10.176 -1.193  -10.799 0.25 57.24  ? 158 ASN   B CG  1 
ATOM   1817 C CG  D ASN   B 2 143 ? -10.176 -1.193  -10.798 0.27 57.24  ? 158 ASN   B CG  1 
ATOM   1818 O OD1 A ASN   B 2 143 ? -9.167  -0.258  -10.682 0.23 57.17  ? 158 ASN   B OD1 1 
ATOM   1819 O OD1 B ASN   B 2 143 ? -9.166  -0.258  -10.681 0.25 57.17  ? 158 ASN   B OD1 1 
ATOM   1820 O OD1 C ASN   B 2 143 ? -9.156  -0.509  -10.670 0.25 57.51  ? 158 ASN   B OD1 1 
ATOM   1821 O OD1 D ASN   B 2 143 ? -9.156  -0.509  -10.669 0.27 57.51  ? 158 ASN   B OD1 1 
ATOM   1822 N ND2 A ASN   B 2 143 ? -10.508 -1.847  -9.841  0.23 56.54  ? 158 ASN   B ND2 1 
ATOM   1823 N ND2 B ASN   B 2 143 ? -10.508 -1.847  -9.840  0.25 56.54  ? 158 ASN   B ND2 1 
ATOM   1824 N ND2 C ASN   B 2 143 ? -10.557 -2.073  -9.882  0.25 56.88  ? 158 ASN   B ND2 1 
ATOM   1825 N ND2 D ASN   B 2 143 ? -10.557 -2.073  -9.882  0.27 56.88  ? 158 ASN   B ND2 1 
ATOM   1826 N N   . GLY   B 2 144 ? -8.068  -1.033  -13.935 1.00 58.66  ? 159 GLY   B N   1 
ATOM   1827 C CA  . GLY   B 2 144 ? -7.062  -1.910  -14.542 1.00 61.03  ? 159 GLY   B CA  1 
ATOM   1828 C C   . GLY   B 2 144 ? -5.659  -1.375  -14.356 1.00 63.51  ? 159 GLY   B C   1 
ATOM   1829 O O   . GLY   B 2 144 ? -5.395  -0.794  -13.297 1.00 61.98  ? 159 GLY   B O   1 
ATOM   1830 N N   . VAL   B 2 145 ? -4.800  -1.570  -15.358 1.00 65.78  ? 160 VAL   B N   1 
ATOM   1831 C CA  . VAL   B 2 145 ? -3.336  -1.441  -15.178 1.00 68.31  ? 160 VAL   B CA  1 
ATOM   1832 C C   . VAL   B 2 145 ? -2.683  -0.893  -16.457 1.00 72.48  ? 160 VAL   B C   1 
ATOM   1833 O O   . VAL   B 2 145 ? -3.210  -1.154  -17.571 1.00 73.99  ? 160 VAL   B O   1 
ATOM   1834 C CB  . VAL   B 2 145 ? -2.803  -2.818  -14.769 1.00 69.13  ? 160 VAL   B CB  1 
ATOM   1835 C CG1 . VAL   B 2 145 ? -2.614  -3.784  -15.934 1.00 68.74  ? 160 VAL   B CG1 1 
ATOM   1836 C CG2 . VAL   B 2 145 ? -1.539  -2.662  -13.969 1.00 70.84  ? 160 VAL   B CG2 1 
ATOM   1837 N N   . VAL   B 2 146 ? -1.557  -0.194  -16.298 1.00 75.42  ? 161 VAL   B N   1 
ATOM   1838 C CA  . VAL   B 2 146 ? -0.661  0.225   -17.406 1.00 80.53  ? 161 VAL   B CA  1 
ATOM   1839 C C   . VAL   B 2 146 ? 0.389   -0.867  -17.605 1.00 84.06  ? 161 VAL   B C   1 
ATOM   1840 O O   . VAL   B 2 146 ? 1.003   -1.264  -16.648 1.00 84.23  ? 161 VAL   B O   1 
ATOM   1841 C CB  . VAL   B 2 146 ? -0.067  1.621   -17.153 1.00 80.48  ? 161 VAL   B CB  1 
ATOM   1842 C CG1 . VAL   B 2 146 ? 0.632   2.151   -18.400 1.00 83.76  ? 161 VAL   B CG1 1 
ATOM   1843 C CG2 . VAL   B 2 146 ? -1.158  2.602   -16.753 1.00 79.55  ? 161 VAL   B CG2 1 
ATOM   1844 N N   A ILE   B 2 147 ? 0.585   -1.318  -18.851 0.23 86.35  ? 162 ILE   B N   1 
ATOM   1845 N N   B ILE   B 2 147 ? 0.585   -1.317  -18.851 0.25 86.34  ? 162 ILE   B N   1 
ATOM   1846 N N   C ILE   B 2 147 ? 0.560   -1.323  -18.851 0.25 86.25  ? 162 ILE   B N   1 
ATOM   1847 N N   D ILE   B 2 147 ? 0.560   -1.323  -18.851 0.27 86.24  ? 162 ILE   B N   1 
ATOM   1848 C CA  A ILE   B 2 147 ? 1.444   -2.492  -19.199 0.23 88.83  ? 162 ILE   B CA  1 
ATOM   1849 C CA  B ILE   B 2 147 ? 1.445   -2.491  -19.200 0.25 88.82  ? 162 ILE   B CA  1 
ATOM   1850 C CA  C ILE   B 2 147 ? 1.486   -2.433  -19.229 0.25 88.71  ? 162 ILE   B CA  1 
ATOM   1851 C CA  D ILE   B 2 147 ? 1.486   -2.433  -19.229 0.27 88.70  ? 162 ILE   B CA  1 
ATOM   1852 C C   A ILE   B 2 147 ? 2.773   -1.999  -19.786 0.23 91.94  ? 162 ILE   B C   1 
ATOM   1853 C C   B ILE   B 2 147 ? 2.773   -1.999  -19.786 0.25 91.94  ? 162 ILE   B C   1 
ATOM   1854 C C   C ILE   B 2 147 ? 2.801   -1.824  -19.725 0.25 91.58  ? 162 ILE   B C   1 
ATOM   1855 C C   D ILE   B 2 147 ? 2.802   -1.824  -19.725 0.27 91.58  ? 162 ILE   B C   1 
ATOM   1856 O O   A ILE   B 2 147 ? 2.889   -0.784  -20.043 0.23 91.21  ? 162 ILE   B O   1 
ATOM   1857 O O   B ILE   B 2 147 ? 2.890   -0.785  -20.044 0.25 91.19  ? 162 ILE   B O   1 
ATOM   1858 O O   C ILE   B 2 147 ? 2.863   -0.587  -19.863 0.25 90.77  ? 162 ILE   B O   1 
ATOM   1859 O O   D ILE   B 2 147 ? 2.863   -0.587  -19.864 0.27 90.76  ? 162 ILE   B O   1 
ATOM   1860 C CB  A ILE   B 2 147 ? 0.705   -3.452  -20.155 0.23 89.62  ? 162 ILE   B CB  1 
ATOM   1861 C CB  B ILE   B 2 147 ? 0.705   -3.452  -20.154 0.25 89.62  ? 162 ILE   B CB  1 
ATOM   1862 C CB  C ILE   B 2 147 ? 0.834   -3.371  -20.268 0.25 89.75  ? 162 ILE   B CB  1 
ATOM   1863 C CB  D ILE   B 2 147 ? 0.835   -3.371  -20.267 0.27 89.74  ? 162 ILE   B CB  1 
ATOM   1864 C CG1 A ILE   B 2 147 ? 0.359   -2.799  -21.499 0.23 89.93  ? 162 ILE   B CG1 1 
ATOM   1865 C CG1 B ILE   B 2 147 ? 0.360   -2.801  -21.500 0.25 89.91  ? 162 ILE   B CG1 1 
ATOM   1866 C CG1 C ILE   B 2 147 ? 0.398   -2.633  -21.540 0.25 89.80  ? 162 ILE   B CG1 1 
ATOM   1867 C CG1 D ILE   B 2 147 ? 0.399   -2.635  -21.541 0.27 89.78  ? 162 ILE   B CG1 1 
ATOM   1868 C CG2 A ILE   B 2 147 ? -0.526  -4.025  -19.468 0.23 88.23  ? 162 ILE   B CG2 1 
ATOM   1869 C CG2 B ILE   B 2 147 ? -0.526  -4.023  -19.468 0.25 88.21  ? 162 ILE   B CG2 1 
ATOM   1870 C CG2 C ILE   B 2 147 ? -0.315  -4.134  -19.627 0.25 88.54  ? 162 ILE   B CG2 1 
ATOM   1871 C CG2 D ILE   B 2 147 ? -0.316  -4.133  -19.627 0.27 88.53  ? 162 ILE   B CG2 1 
ATOM   1872 C CD1 A ILE   B 2 147 ? -0.392  -3.701  -22.448 0.23 90.17  ? 162 ILE   B CD1 1 
ATOM   1873 C CD1 B ILE   B 2 147 ? -0.392  -3.706  -22.445 0.25 90.14  ? 162 ILE   B CD1 1 
ATOM   1874 C CD1 C ILE   B 2 147 ? -0.374  -3.482  -22.517 0.25 89.96  ? 162 ILE   B CD1 1 
ATOM   1875 C CD1 D ILE   B 2 147 ? -0.374  -3.491  -22.513 0.27 89.94  ? 162 ILE   B CD1 1 
ATOM   1876 N N   A LYS   B 2 148 ? 3.731   -2.915  -19.980 0.23 95.41  ? 163 LYS   B N   1 
ATOM   1877 N N   B LYS   B 2 148 ? 3.731   -2.915  -19.979 0.25 95.40  ? 163 LYS   B N   1 
ATOM   1878 N N   C LYS   B 2 148 ? 3.805   -2.668  -19.985 0.25 94.90  ? 163 LYS   B N   1 
ATOM   1879 N N   D LYS   B 2 148 ? 3.805   -2.668  -19.985 0.27 94.90  ? 163 LYS   B N   1 
ATOM   1880 C CA  A LYS   B 2 148 ? 5.072   -2.638  -20.571 0.23 99.03  ? 163 LYS   B CA  1 
ATOM   1881 C CA  B LYS   B 2 148 ? 5.072   -2.639  -20.571 0.25 99.03  ? 163 LYS   B CA  1 
ATOM   1882 C CA  C LYS   B 2 148 ? 5.177   -2.252  -20.393 0.25 98.15  ? 163 LYS   B CA  1 
ATOM   1883 C CA  D LYS   B 2 148 ? 5.178   -2.252  -20.393 0.27 98.16  ? 163 LYS   B CA  1 
ATOM   1884 C C   A LYS   B 2 148 ? 4.970   -1.474  -21.563 0.23 99.88  ? 163 LYS   B C   1 
ATOM   1885 C C   B LYS   B 2 148 ? 4.971   -1.474  -21.563 0.25 99.89  ? 163 LYS   B C   1 
ATOM   1886 C C   C LYS   B 2 148 ? 5.089   -1.301  -21.592 0.25 99.33  ? 163 LYS   B C   1 
ATOM   1887 C C   D LYS   B 2 148 ? 5.089   -1.301  -21.592 0.27 99.34  ? 163 LYS   B C   1 
ATOM   1888 O O   A LYS   B 2 148 ? 5.638   -0.444  -21.343 0.23 101.34 ? 163 LYS   B O   1 
ATOM   1889 O O   B LYS   B 2 148 ? 5.638   -0.445  -21.341 0.25 101.37 ? 163 LYS   B O   1 
ATOM   1890 O O   C LYS   B 2 148 ? 5.918   -0.376  -21.685 0.25 101.37 ? 163 LYS   B O   1 
ATOM   1891 O O   D LYS   B 2 148 ? 5.919   -0.376  -21.685 0.27 101.40 ? 163 LYS   B O   1 
ATOM   1892 C CB  A LYS   B 2 148 ? 5.613   -3.865  -21.311 0.23 101.35 ? 163 LYS   B CB  1 
ATOM   1893 C CB  B LYS   B 2 148 ? 5.613   -3.866  -21.311 0.25 101.35 ? 163 LYS   B CB  1 
ATOM   1894 C CB  C LYS   B 2 148 ? 6.044   -3.461  -20.762 0.25 100.10 ? 163 LYS   B CB  1 
ATOM   1895 C CB  D LYS   B 2 148 ? 6.044   -3.461  -20.762 0.27 100.10 ? 163 LYS   B CB  1 
ATOM   1896 C CG  A LYS   B 2 148 ? 5.993   -5.055  -20.440 0.23 102.49 ? 163 LYS   B CG  1 
ATOM   1897 C CG  B LYS   B 2 148 ? 5.993   -5.055  -20.440 0.25 102.49 ? 163 LYS   B CG  1 
ATOM   1898 C CG  C LYS   B 2 148 ? 5.797   -4.728  -19.951 0.25 100.49 ? 163 LYS   B CG  1 
ATOM   1899 C CG  D LYS   B 2 148 ? 5.797   -4.728  -19.951 0.27 100.49 ? 163 LYS   B CG  1 
ATOM   1900 C CD  A LYS   B 2 148 ? 6.469   -6.258  -21.236 0.23 104.95 ? 163 LYS   B CD  1 
ATOM   1901 C CD  B LYS   B 2 148 ? 6.469   -6.258  -21.237 0.25 104.96 ? 163 LYS   B CD  1 
ATOM   1902 C CD  C LYS   B 2 148 ? 7.055   -5.432  -19.484 0.25 102.31 ? 163 LYS   B CD  1 
ATOM   1903 C CD  D LYS   B 2 148 ? 7.054   -5.432  -19.484 0.27 102.32 ? 163 LYS   B CD  1 
ATOM   1904 C CE  A LYS   B 2 148 ? 7.735   -6.009  -22.033 0.23 107.59 ? 163 LYS   B CE  1 
ATOM   1905 C CE  B LYS   B 2 148 ? 7.735   -6.009  -22.034 0.25 107.60 ? 163 LYS   B CE  1 
ATOM   1906 C CE  C LYS   B 2 148 ? 8.128   -5.570  -20.544 0.25 104.78 ? 163 LYS   B CE  1 
ATOM   1907 C CE  D LYS   B 2 148 ? 8.128   -5.570  -20.543 0.27 104.78 ? 163 LYS   B CE  1 
ATOM   1908 N NZ  A LYS   B 2 148 ? 8.938   -5.996  -21.166 0.23 108.84 ? 163 LYS   B NZ  1 
ATOM   1909 N NZ  B LYS   B 2 148 ? 8.938   -5.996  -21.167 0.25 108.87 ? 163 LYS   B NZ  1 
ATOM   1910 N NZ  C LYS   B 2 148 ? 9.356   -6.182  -19.986 0.25 105.80 ? 163 LYS   B NZ  1 
ATOM   1911 N NZ  D LYS   B 2 148 ? 9.356   -6.181  -19.985 0.27 105.80 ? 163 LYS   B NZ  1 
ATOM   1912 N N   A ASN   B 2 149 ? 4.144   -1.652  -22.601 0.23 99.62  ? 164 ASN   B N   1 
ATOM   1913 N N   B ASN   B 2 149 ? 4.145   -1.652  -22.601 0.25 99.64  ? 164 ASN   B N   1 
ATOM   1914 N N   C ASN   B 2 149 ? 4.102   -1.531  -22.462 0.25 98.82  ? 164 ASN   B N   1 
ATOM   1915 N N   D ASN   B 2 149 ? 4.103   -1.531  -22.461 0.27 98.84  ? 164 ASN   B N   1 
ATOM   1916 C CA  A ASN   B 2 149 ? 3.905   -0.702  -23.723 0.23 99.01  ? 164 ASN   B CA  1 
ATOM   1917 C CA  B ASN   B 2 149 ? 3.907   -0.702  -23.722 0.25 99.01  ? 164 ASN   B CA  1 
ATOM   1918 C CA  C ASN   B 2 149 ? 3.837   -0.769  -23.710 0.25 98.09  ? 164 ASN   B CA  1 
ATOM   1919 C CA  D ASN   B 2 149 ? 3.838   -0.769  -23.710 0.27 98.09  ? 164 ASN   B CA  1 
ATOM   1920 C C   A ASN   B 2 149 ? 3.790   0.737   -23.206 0.23 96.70  ? 164 ASN   B C   1 
ATOM   1921 C C   B ASN   B 2 149 ? 3.791   0.738   -23.205 0.25 96.71  ? 164 ASN   B C   1 
ATOM   1922 C C   C ASN   B 2 149 ? 3.492   0.692   -23.386 0.25 96.10  ? 164 ASN   B C   1 
ATOM   1923 C C   D ASN   B 2 149 ? 3.493   0.692   -23.386 0.27 96.10  ? 164 ASN   B C   1 
ATOM   1924 O O   A ASN   B 2 149 ? 4.499   1.615   -23.738 0.23 99.69  ? 164 ASN   B O   1 
ATOM   1925 O O   B ASN   B 2 149 ? 4.500   1.615   -23.737 0.25 99.74  ? 164 ASN   B O   1 
ATOM   1926 O O   C ASN   B 2 149 ? 3.681   1.549   -24.280 0.25 98.28  ? 164 ASN   B O   1 
ATOM   1927 O O   D ASN   B 2 149 ? 3.680   1.549   -24.281 0.27 98.31  ? 164 ASN   B O   1 
ATOM   1928 C CB  A ASN   B 2 149 ? 2.633   -1.060  -24.499 0.23 99.46  ? 164 ASN   B CB  1 
ATOM   1929 C CB  B ASN   B 2 149 ? 2.635   -1.059  -24.499 0.25 99.47  ? 164 ASN   B CB  1 
ATOM   1930 C CB  C ASN   B 2 149 ? 2.714   -1.427  -24.520 0.25 98.38  ? 164 ASN   B CB  1 
ATOM   1931 C CB  D ASN   B 2 149 ? 2.716   -1.427  -24.520 0.27 98.38  ? 164 ASN   B CB  1 
ATOM   1932 C CG  A ASN   B 2 149 ? 2.529   -2.529  -24.854 0.23 100.44 ? 164 ASN   B CG  1 
ATOM   1933 C CG  B ASN   B 2 149 ? 2.530   -2.529  -24.853 0.25 100.45 ? 164 ASN   B CG  1 
ATOM   1934 C CG  C ASN   B 2 149 ? 2.885   -2.926  -24.666 0.25 99.15  ? 164 ASN   B CG  1 
ATOM   1935 C CG  D ASN   B 2 149 ? 2.886   -2.926  -24.665 0.27 99.15  ? 164 ASN   B CG  1 
ATOM   1936 O OD1 A ASN   B 2 149 ? 3.535   -3.187  -25.118 0.23 102.44 ? 164 ASN   B OD1 1 
ATOM   1937 O OD1 B ASN   B 2 149 ? 3.535   -3.188  -25.117 0.25 102.46 ? 164 ASN   B OD1 1 
ATOM   1938 O OD1 C ASN   B 2 149 ? 3.478   -3.575  -23.803 0.25 98.86  ? 164 ASN   B OD1 1 
ATOM   1939 O OD1 D ASN   B 2 149 ? 3.478   -3.575  -23.802 0.27 98.85  ? 164 ASN   B OD1 1 
ATOM   1940 N ND2 A ASN   B 2 149 ? 1.313   -3.050  -24.870 0.23 99.39  ? 164 ASN   B ND2 1 
ATOM   1941 N ND2 B ASN   B 2 149 ? 1.313   -3.049  -24.868 0.25 99.39  ? 164 ASN   B ND2 1 
ATOM   1942 N ND2 C ASN   B 2 149 ? 2.367   -3.488  -25.747 0.25 99.42  ? 164 ASN   B ND2 1 
ATOM   1943 N ND2 D ASN   B 2 149 ? 2.368   -3.488  -25.747 0.27 99.42  ? 164 ASN   B ND2 1 
ATOM   1944 N N   . GLY   B 2 150 ? 2.955   0.952   -22.188 1.00 93.34  ? 165 GLY   B N   1 
ATOM   1945 C CA  . GLY   B 2 150 ? 2.453   2.282   -21.795 1.00 87.45  ? 165 GLY   B CA  1 
ATOM   1946 C C   . GLY   B 2 150 ? 0.935   2.328   -21.961 1.00 82.42  ? 165 GLY   B C   1 
ATOM   1947 O O   . GLY   B 2 150 ? 0.273   3.310   -21.459 1.00 79.97  ? 165 GLY   B O   1 
ATOM   1948 N N   A SER   B 2 151 ? 0.375   1.309   -22.633 0.23 81.22  ? 166 SER   B N   1 
ATOM   1949 N N   B SER   B 2 151 ? 0.383   1.302   -22.627 0.25 81.76  ? 166 SER   B N   1 
ATOM   1950 N N   C SER   B 2 151 ? 0.377   1.308   -22.635 0.25 81.23  ? 166 SER   B N   1 
ATOM   1951 N N   D SER   B 2 151 ? 0.385   1.301   -22.628 0.27 81.77  ? 166 SER   B N   1 
ATOM   1952 C CA  A SER   B 2 151 ? -1.076  1.180   -22.938 0.23 79.41  ? 166 SER   B CA  1 
ATOM   1953 C CA  B SER   B 2 151 ? -1.063  1.145   -22.939 0.25 80.28  ? 166 SER   B CA  1 
ATOM   1954 C CA  C SER   B 2 151 ? -1.072  1.181   -22.941 0.25 79.44  ? 166 SER   B CA  1 
ATOM   1955 C CA  D SER   B 2 151 ? -1.059  1.146   -22.942 0.27 80.31  ? 166 SER   B CA  1 
ATOM   1956 C C   A SER   B 2 151 ? -1.843  0.706   -21.694 0.23 77.59  ? 166 SER   B C   1 
ATOM   1957 C C   B SER   B 2 151 ? -1.840  0.704   -21.688 0.25 78.13  ? 166 SER   B C   1 
ATOM   1958 C C   C SER   B 2 151 ? -1.832  0.698   -21.701 0.25 77.67  ? 166 SER   B C   1 
ATOM   1959 C C   D SER   B 2 151 ? -1.829  0.697   -21.695 0.27 78.21  ? 166 SER   B C   1 
ATOM   1960 O O   A SER   B 2 151 ? -1.197  0.321   -20.684 0.23 77.25  ? 166 SER   B O   1 
ATOM   1961 O O   B SER   B 2 151 ? -1.200  0.345   -20.665 0.25 77.70  ? 166 SER   B O   1 
ATOM   1962 O O   C SER   B 2 151 ? -1.193  0.329   -20.682 0.25 77.29  ? 166 SER   B O   1 
ATOM   1963 O O   D SER   B 2 151 ? -1.197  0.351   -20.663 0.27 77.74  ? 166 SER   B O   1 
ATOM   1964 C CB  A SER   B 2 151 ? -1.320  0.266   -24.114 0.23 79.95  ? 166 SER   B CB  1 
ATOM   1965 C CB  B SER   B 2 151 ? -1.267  0.184   -24.083 0.25 81.35  ? 166 SER   B CB  1 
ATOM   1966 C CB  C SER   B 2 151 ? -1.319  0.267   -24.117 0.25 79.96  ? 166 SER   B CB  1 
ATOM   1967 C CB  D SER   B 2 151 ? -1.265  0.187   -24.086 0.27 81.37  ? 166 SER   B CB  1 
ATOM   1968 O OG  A SER   B 2 151 ? -2.696  0.271   -24.479 0.23 78.62  ? 166 SER   B OG  1 
ATOM   1969 O OG  B SER   B 2 151 ? -0.611  -1.047  -23.828 0.25 82.49  ? 166 SER   B OG  1 
ATOM   1970 O OG  C SER   B 2 151 ? -2.696  0.271   -24.478 0.25 78.60  ? 166 SER   B OG  1 
ATOM   1971 O OG  D SER   B 2 151 ? -0.609  -1.042  -23.833 0.27 82.53  ? 166 SER   B OG  1 
ATOM   1972 N N   A TYR   B 2 152 ? -3.177  0.750   -21.765 0.23 75.47  ? 167 TYR   B N   1 
ATOM   1973 N N   B TYR   B 2 152 ? -3.174  0.749   -21.764 0.25 75.65  ? 167 TYR   B N   1 
ATOM   1974 N N   C TYR   B 2 152 ? -3.149  0.647   -21.815 0.25 75.68  ? 167 TYR   B N   1 
ATOM   1975 N N   D TYR   B 2 152 ? -3.147  0.647   -21.814 0.27 75.87  ? 167 TYR   B N   1 
ATOM   1976 C CA  A TYR   B 2 152 ? -4.106  0.463   -20.642 0.23 73.81  ? 167 TYR   B CA  1 
ATOM   1977 C CA  B TYR   B 2 152 ? -4.105  0.463   -20.643 0.25 73.91  ? 167 TYR   B CA  1 
ATOM   1978 C CA  C TYR   B 2 152 ? -4.051  0.416   -20.670 0.25 74.08  ? 167 TYR   B CA  1 
ATOM   1979 C CA  D TYR   B 2 152 ? -4.051  0.417   -20.670 0.27 74.18  ? 167 TYR   B CA  1 
ATOM   1980 C C   A TYR   B 2 152 ? -4.862  -0.847  -20.901 0.23 72.42  ? 167 TYR   B C   1 
ATOM   1981 C C   B TYR   B 2 152 ? -4.862  -0.847  -20.901 0.25 72.46  ? 167 TYR   B C   1 
ATOM   1982 C C   C TYR   B 2 152 ? -4.884  -0.846  -20.901 0.25 72.53  ? 167 TYR   B C   1 
ATOM   1983 C C   D TYR   B 2 152 ? -4.884  -0.846  -20.901 0.27 72.57  ? 167 TYR   B C   1 
ATOM   1984 O O   A TYR   B 2 152 ? -5.316  -1.063  -22.022 0.23 71.12  ? 167 TYR   B O   1 
ATOM   1985 O O   B TYR   B 2 152 ? -5.315  -1.064  -22.022 0.25 71.12  ? 167 TYR   B O   1 
ATOM   1986 O O   C TYR   B 2 152 ? -5.413  -1.026  -21.998 0.25 71.11  ? 167 TYR   B O   1 
ATOM   1987 O O   D TYR   B 2 152 ? -5.412  -1.026  -21.997 0.27 71.11  ? 167 TYR   B O   1 
ATOM   1988 C CB  A TYR   B 2 152 ? -5.071  1.635   -20.455 0.23 73.24  ? 167 TYR   B CB  1 
ATOM   1989 C CB  B TYR   B 2 152 ? -5.071  1.635   -20.456 0.25 73.29  ? 167 TYR   B CB  1 
ATOM   1990 C CB  C TYR   B 2 152 ? -4.902  1.665   -20.456 0.25 73.68  ? 167 TYR   B CB  1 
ATOM   1991 C CB  D TYR   B 2 152 ? -4.903  1.665   -20.456 0.27 73.73  ? 167 TYR   B CB  1 
ATOM   1992 C CG  A TYR   B 2 152 ? -6.005  1.497   -19.280 0.23 72.45  ? 167 TYR   B CG  1 
ATOM   1993 C CG  B TYR   B 2 152 ? -6.005  1.497   -19.281 0.25 72.48  ? 167 TYR   B CG  1 
ATOM   1994 C CG  C TYR   B 2 152 ? -5.832  1.555   -19.280 0.25 72.99  ? 167 TYR   B CG  1 
ATOM   1995 C CG  D TYR   B 2 152 ? -5.832  1.555   -19.281 0.27 73.02  ? 167 TYR   B CG  1 
ATOM   1996 C CD1 A TYR   B 2 152 ? -5.543  1.612   -17.977 0.23 72.24  ? 167 TYR   B CD1 1 
ATOM   1997 C CD1 B TYR   B 2 152 ? -5.543  1.612   -17.978 0.25 72.25  ? 167 TYR   B CD1 1 
ATOM   1998 C CD1 C TYR   B 2 152 ? -5.388  1.789   -17.990 0.25 72.82  ? 167 TYR   B CD1 1 
ATOM   1999 C CD1 D TYR   B 2 152 ? -5.388  1.789   -17.990 0.27 72.83  ? 167 TYR   B CD1 1 
ATOM   2000 C CD2 A TYR   B 2 152 ? -7.356  1.255   -19.472 0.23 71.96  ? 167 TYR   B CD2 1 
ATOM   2001 C CD2 B TYR   B 2 152 ? -7.356  1.255   -19.473 0.25 71.98  ? 167 TYR   B CD2 1 
ATOM   2002 C CD2 C TYR   B 2 152 ? -7.153  1.185   -19.463 0.25 72.69  ? 167 TYR   B CD2 1 
ATOM   2003 C CD2 D TYR   B 2 152 ? -7.153  1.185   -19.464 0.27 72.71  ? 167 TYR   B CD2 1 
ATOM   2004 C CE1 A TYR   B 2 152 ? -6.398  1.485   -16.893 0.23 71.31  ? 167 TYR   B CE1 1 
ATOM   2005 C CE1 B TYR   B 2 152 ? -6.398  1.485   -16.894 0.25 71.32  ? 167 TYR   B CE1 1 
ATOM   2006 C CE1 C TYR   B 2 152 ? -6.241  1.672   -16.904 0.25 71.94  ? 167 TYR   B CE1 1 
ATOM   2007 C CE1 D TYR   B 2 152 ? -6.240  1.672   -16.904 0.27 71.95  ? 167 TYR   B CE1 1 
ATOM   2008 C CE2 A TYR   B 2 152 ? -8.224  1.124   -18.402 0.23 71.52  ? 167 TYR   B CE2 1 
ATOM   2009 C CE2 B TYR   B 2 152 ? -8.224  1.124   -18.403 0.25 71.53  ? 167 TYR   B CE2 1 
ATOM   2010 C CE2 C TYR   B 2 152 ? -8.018  1.065   -18.392 0.25 72.24  ? 167 TYR   B CE2 1 
ATOM   2011 C CE2 D TYR   B 2 152 ? -8.018  1.065   -18.392 0.27 72.25  ? 167 TYR   B CE2 1 
ATOM   2012 C CZ  A TYR   B 2 152 ? -7.744  1.238   -17.107 0.23 70.96  ? 167 TYR   B CZ  1 
ATOM   2013 C CZ  B TYR   B 2 152 ? -7.744  1.237   -17.108 0.25 70.97  ? 167 TYR   B CZ  1 
ATOM   2014 C CZ  C TYR   B 2 152 ? -7.560  1.306   -17.107 0.25 71.64  ? 167 TYR   B CZ  1 
ATOM   2015 C CZ  D TYR   B 2 152 ? -7.560  1.306   -17.107 0.27 71.65  ? 167 TYR   B CZ  1 
ATOM   2016 O OH  A TYR   B 2 152 ? -8.604  1.114   -16.055 0.23 70.79  ? 167 TYR   B OH  1 
ATOM   2017 O OH  B TYR   B 2 152 ? -8.604  1.114   -16.056 0.25 70.81  ? 167 TYR   B OH  1 
ATOM   2018 O OH  C TYR   B 2 152 ? -8.419  1.192   -16.054 0.25 71.57  ? 167 TYR   B OH  1 
ATOM   2019 O OH  D TYR   B 2 152 ? -8.419  1.192   -16.054 0.27 71.58  ? 167 TYR   B OH  1 
ATOM   2020 N N   . VAL   B 2 153 ? -5.001  -1.681  -19.863 1.00 70.73  ? 168 VAL   B N   1 
ATOM   2021 C CA  . VAL   B 2 153 ? -5.852  -2.907  -19.887 1.00 69.14  ? 168 VAL   B CA  1 
ATOM   2022 C C   . VAL   B 2 153 ? -6.832  -2.839  -18.680 1.00 65.88  ? 168 VAL   B C   1 
ATOM   2023 O O   . VAL   B 2 153 ? -6.358  -2.756  -17.569 1.00 63.62  ? 168 VAL   B O   1 
ATOM   2024 C CB  . VAL   B 2 153 ? -4.940  -4.153  -19.884 1.00 70.06  ? 168 VAL   B CB  1 
ATOM   2025 C CG1 . VAL   B 2 153 ? -5.729  -5.443  -20.030 1.00 69.89  ? 168 VAL   B CG1 1 
ATOM   2026 C CG2 . VAL   B 2 153 ? -3.882  -4.079  -20.984 1.00 73.12  ? 168 VAL   B CG2 1 
ATOM   2027 N N   . SER   B 2 154 ? -8.152  -2.843  -18.921 1.00 63.66  ? 169 SER   B N   1 
ATOM   2028 C CA  . SER   B 2 154 ? -9.225  -2.777  -17.888 1.00 61.13  ? 169 SER   B CA  1 
ATOM   2029 C C   . SER   B 2 154 ? -9.711  -4.203  -17.530 1.00 60.60  ? 169 SER   B C   1 
ATOM   2030 O O   . SER   B 2 154 ? -10.055 -4.992  -18.467 1.00 60.76  ? 169 SER   B O   1 
ATOM   2031 C CB  . SER   B 2 154 ? -10.407 -1.934  -18.361 1.00 60.15  ? 169 SER   B CB  1 
ATOM   2032 O OG  . SER   B 2 154 ? -11.531 -2.004  -17.458 1.00 59.18  ? 169 SER   B OG  1 
ATOM   2033 N N   . ALA   B 2 155 ? -9.901  -4.467  -16.227 1.00 59.38  ? 170 ALA   B N   1 
ATOM   2034 C CA  . ALA   B 2 155 ? -10.716 -5.602  -15.731 1.00 58.70  ? 170 ALA   B CA  1 
ATOM   2035 C C   . ALA   B 2 155 ? -12.194 -5.300  -16.412 1.00 58.99  ? 170 ALA   B C   1 
ATOM   2036 O O   . ALA   B 2 155 ? -12.719 -4.127  -16.473 1.00 60.23  ? 170 ALA   B O   1 
ATOM   2037 C CB  . ALA   B 2 155 ? -10.717 -5.714  -14.179 1.00 58.66  ? 170 ALA   B CB  1 
ATOM   2038 N N   . ILE   B 2 156 ? -12.746 -6.476  -16.740 1.00 58.89  ? 171 ILE   B N   1 
ATOM   2039 C CA  . ILE   B 2 156 ? -14.262 -6.635  -16.825 1.00 57.86  ? 171 ILE   B CA  1 
ATOM   2040 C C   . ILE   B 2 156 ? -14.757 -6.774  -15.366 1.00 56.70  ? 171 ILE   B C   1 
ATOM   2041 O O   . ILE   B 2 156 ? -14.836 -7.930  -14.901 1.00 55.94  ? 171 ILE   B O   1 
ATOM   2042 C CB  . ILE   B 2 156 ? -14.697 -7.820  -17.723 1.00 58.44  ? 171 ILE   B CB  1 
ATOM   2043 C CG1 . ILE   B 2 156 ? -13.961 -7.824  -19.066 1.00 59.46  ? 171 ILE   B CG1 1 
ATOM   2044 C CG2 . ILE   B 2 156 ? -16.210 -7.788  -17.890 1.00 57.88  ? 171 ILE   B CG2 1 
ATOM   2045 C CD1 . ILE   B 2 156 ? -14.123 -9.099  -19.876 1.00 60.72  ? 171 ILE   B CD1 1 
ATOM   2046 N N   . THR   B 2 157 ? -14.982 -5.633  -14.690 1.00 55.95  ? 172 THR   B N   1 
ATOM   2047 C CA  . THR   B 2 157 ? -15.502 -5.559  -13.282 1.00 55.24  ? 172 THR   B CA  1 
ATOM   2048 C C   . THR   B 2 157 ? -17.055 -5.728  -13.260 1.00 55.08  ? 172 THR   B C   1 
ATOM   2049 O O   . THR   B 2 157 ? -17.821 -4.815  -13.726 1.00 55.33  ? 172 THR   B O   1 
ATOM   2050 C CB  . THR   B 2 157 ? -15.119 -4.229  -12.624 1.00 54.81  ? 172 THR   B CB  1 
ATOM   2051 O OG1 . THR   B 2 157 ? -13.624 -4.003  -12.801 1.00 55.96  ? 172 THR   B OG1 1 
ATOM   2052 C CG2 . THR   B 2 157 ? -15.497 -4.202  -11.157 1.00 54.03  ? 172 THR   B CG2 1 
ATOM   2053 N N   . GLN   B 2 158 ? -17.493 -6.829  -12.571 1.00 54.40  ? 173 GLN   B N   1 
ATOM   2054 C CA  . GLN   B 2 158 ? -18.924 -7.184  -12.366 1.00 54.70  ? 173 GLN   B CA  1 
ATOM   2055 C C   . GLN   B 2 158 ? -19.240 -7.289  -10.858 1.00 55.18  ? 173 GLN   B C   1 
ATOM   2056 O O   . GLN   B 2 158 ? -18.473 -7.891  -10.143 1.00 54.48  ? 173 GLN   B O   1 
ATOM   2057 C CB  . GLN   B 2 158 ? -19.218 -8.504  -13.077 1.00 55.39  ? 173 GLN   B CB  1 
ATOM   2058 C CG  . GLN   B 2 158 ? -20.708 -8.846  -13.159 1.00 56.08  ? 173 GLN   B CG  1 
ATOM   2059 C CD  . GLN   B 2 158 ? -21.610 -7.741  -13.701 1.00 55.37  ? 173 GLN   B CD  1 
ATOM   2060 O OE1 . GLN   B 2 158 ? -21.733 -6.646  -13.124 1.00 54.87  ? 173 GLN   B OE1 1 
ATOM   2061 N NE2 . GLN   B 2 158 ? -22.323 -8.046  -14.765 1.00 54.79  ? 173 GLN   B NE2 1 
ATOM   2062 N N   . GLY   B 2 159 ? -20.365 -6.759  -10.412 1.00 56.35  ? 174 GLY   B N   1 
ATOM   2063 C CA  . GLY   B 2 159 ? -20.856 -6.919  -9.020  1.00 57.90  ? 174 GLY   B CA  1 
ATOM   2064 C C   . GLY   B 2 159 ? -21.636 -8.214  -8.847  1.00 61.26  ? 174 GLY   B C   1 
ATOM   2065 O O   . GLY   B 2 159 ? -21.729 -9.031  -9.749  1.00 62.67  ? 174 GLY   B O   1 
ATOM   2066 N N   . LYS   B 2 160 ? -22.208 -8.396  -7.680  1.00 67.26  ? 175 LYS   B N   1 
ATOM   2067 C CA  . LYS   B 2 160 ? -23.040 -9.556  -7.287  1.00 72.61  ? 175 LYS   B CA  1 
ATOM   2068 C C   . LYS   B 2 160 ? -24.493 -9.050  -7.247  1.00 74.00  ? 175 LYS   B C   1 
ATOM   2069 O O   . LYS   B 2 160 ? -24.722 -7.942  -6.757  1.00 72.29  ? 175 LYS   B O   1 
ATOM   2070 C CB  . LYS   B 2 160 ? -22.487 -10.070 -5.948  1.00 77.15  ? 175 LYS   B CB  1 
ATOM   2071 C CG  . LYS   B 2 160 ? -23.163 -11.309 -5.383  1.00 82.16  ? 175 LYS   B CG  1 
ATOM   2072 C CD  . LYS   B 2 160 ? -22.225 -12.257 -4.643  1.00 84.62  ? 175 LYS   B CD  1 
ATOM   2073 C CE  . LYS   B 2 160 ? -22.901 -13.563 -4.271  1.00 87.71  ? 175 LYS   B CE  1 
ATOM   2074 N NZ  . LYS   B 2 160 ? -23.424 -13.526 -2.884  1.00 91.67  ? 175 LYS   B NZ  1 
ATOM   2075 N N   . ARG   B 2 161 ? -25.443 -9.803  -7.789  1.00 76.42  ? 176 ARG   B N   1 
ATOM   2076 C CA  . ARG   B 2 161 ? -26.896 -9.558  -7.570  1.00 80.06  ? 176 ARG   B CA  1 
ATOM   2077 C C   . ARG   B 2 161 ? -27.320 -10.430 -6.378  1.00 83.11  ? 176 ARG   B C   1 
ATOM   2078 O O   . ARG   B 2 161 ? -26.826 -11.573 -6.313  1.00 83.25  ? 176 ARG   B O   1 
ATOM   2079 C CB  . ARG   B 2 161 ? -27.650 -9.844  -8.880  1.00 81.36  ? 176 ARG   B CB  1 
ATOM   2080 C CG  . ARG   B 2 161 ? -29.097 -9.376  -8.912  1.00 80.85  ? 176 ARG   B CG  1 
ATOM   2081 C CD  . ARG   B 2 161 ? -29.845 -9.887  -10.136 1.00 82.72  ? 176 ARG   B CD  1 
ATOM   2082 N NE  . ARG   B 2 161 ? -31.258 -9.520  -10.070 1.00 84.26  ? 176 ARG   B NE  1 
ATOM   2083 C CZ  . ARG   B 2 161 ? -31.899 -8.663  -10.874 1.00 84.46  ? 176 ARG   B CZ  1 
ATOM   2084 N NH1 . ARG   B 2 161 ? -31.280 -8.043  -11.870 1.00 80.26  ? 176 ARG   B NH1 1 
ATOM   2085 N NH2 . ARG   B 2 161 ? -33.185 -8.431  -10.656 1.00 85.57  ? 176 ARG   B NH2 1 
ATOM   2086 N N   . GLU   B 2 162 ? -28.175 -9.920  -5.479  1.00 86.19  ? 177 GLU   B N   1 
ATOM   2087 C CA  . GLU   B 2 162 ? -28.633 -10.634 -4.245  1.00 91.37  ? 177 GLU   B CA  1 
ATOM   2088 C C   . GLU   B 2 162 ? -30.112 -11.031 -4.376  1.00 91.46  ? 177 GLU   B C   1 
ATOM   2089 O O   . GLU   B 2 162 ? -30.416 -12.219 -4.677  1.00 93.16  ? 177 GLU   B O   1 
ATOM   2090 C CB  . GLU   B 2 162 ? -28.420 -9.760  -3.004  1.00 94.60  ? 177 GLU   B CB  1 
ATOM   2091 C CG  . GLU   B 2 162 ? -26.950 -9.463  -2.680  1.00 97.42  ? 177 GLU   B CG  1 
ATOM   2092 C CD  . GLU   B 2 162 ? -26.267 -10.344 -1.630  1.00 100.88 ? 177 GLU   B CD  1 
ATOM   2093 O OE1 . GLU   B 2 162 ? -26.751 -10.361 -0.459  1.00 96.73  ? 177 GLU   B OE1 1 
ATOM   2094 O OE2 . GLU   B 2 162 ? -25.236 -11.009 -1.979  1.00 99.66  ? 177 GLU   B OE2 1 
HETATM 2095 S S   A DMS   C 3 .   ? -7.938  5.658   -17.642 0.23 88.78  ? 201 DMS   B S   1 
HETATM 2096 S S   B DMS   C 3 .   ? -7.938  5.659   -17.642 0.25 88.77  ? 201 DMS   B S   1 
HETATM 2097 O O   A DMS   C 3 .   ? -6.568  5.077   -17.888 0.23 90.52  ? 201 DMS   B O   1 
HETATM 2098 O O   B DMS   C 3 .   ? -6.568  5.078   -17.889 0.25 90.53  ? 201 DMS   B O   1 
HETATM 2099 C C1  A DMS   C 3 .   ? -8.389  5.234   -15.969 0.23 88.46  ? 201 DMS   B C1  1 
HETATM 2100 C C1  B DMS   C 3 .   ? -8.389  5.234   -15.969 0.25 88.46  ? 201 DMS   B C1  1 
HETATM 2101 C C2  A DMS   C 3 .   ? -9.081  4.586   -18.472 0.23 88.43  ? 201 DMS   B C2  1 
HETATM 2102 C C2  B DMS   C 3 .   ? -9.082  4.586   -18.472 0.25 88.41  ? 201 DMS   B C2  1 
HETATM 2103 S S   A DMS   D 3 .   ? -18.608 12.249  -0.624  0.23 207.00 ? 202 DMS   B S   1 
HETATM 2104 S S   B DMS   D 3 .   ? -18.608 12.249  -0.625  0.25 207.10 ? 202 DMS   B S   1 
HETATM 2105 O O   A DMS   D 3 .   ? -19.449 11.093  -1.086  0.23 204.29 ? 202 DMS   B O   1 
HETATM 2106 O O   B DMS   D 3 .   ? -19.449 11.093  -1.086  0.25 204.38 ? 202 DMS   B O   1 
HETATM 2107 C C1  A DMS   D 3 .   ? -19.438 13.717  -1.176  0.23 205.41 ? 202 DMS   B C1  1 
HETATM 2108 C C1  B DMS   D 3 .   ? -19.438 13.717  -1.177  0.25 205.46 ? 202 DMS   B C1  1 
HETATM 2109 C C2  A DMS   D 3 .   ? -17.220 12.316  -1.727  0.23 205.70 ? 202 DMS   B C2  1 
HETATM 2110 C C2  B DMS   D 3 .   ? -17.220 12.317  -1.727  0.25 205.74 ? 202 DMS   B C2  1 
HETATM 2111 S S   A DMS   E 3 .   ? -6.766  3.291   -13.568 0.23 121.43 ? 203 DMS   B S   1 
HETATM 2112 S S   B DMS   E 3 .   ? -6.766  3.292   -13.568 0.25 121.43 ? 203 DMS   B S   1 
HETATM 2113 O O   A DMS   E 3 .   ? -6.221  1.933   -13.241 0.23 119.73 ? 203 DMS   B O   1 
HETATM 2114 O O   B DMS   E 3 .   ? -6.221  1.933   -13.241 0.25 119.70 ? 203 DMS   B O   1 
HETATM 2115 C C1  A DMS   E 3 .   ? -7.944  3.677   -12.295 0.23 121.38 ? 203 DMS   B C1  1 
HETATM 2116 C C1  B DMS   E 3 .   ? -7.944  3.677   -12.295 0.25 121.41 ? 203 DMS   B C1  1 
HETATM 2117 C C2  A DMS   E 3 .   ? -5.504  4.440   -13.094 0.23 121.50 ? 203 DMS   B C2  1 
HETATM 2118 C C2  B DMS   E 3 .   ? -5.504  4.441   -13.094 0.25 121.49 ? 203 DMS   B C2  1 
HETATM 2119 N N1  C A1BHB F 4 .   ? -8.357  4.781   -12.606 0.26 58.43  ? 204 A1BHB B N1  1 
HETATM 2120 N N1  D A1BHB F 4 .   ? -8.358  4.781   -12.606 0.27 58.43  ? 204 A1BHB B N1  1 
HETATM 2121 N N3  C A1BHB F 4 .   ? -9.040  4.469   -9.123  0.26 55.10  ? 204 A1BHB B N3  1 
HETATM 2122 N N3  D A1BHB F 4 .   ? -9.039  4.469   -9.122  0.27 55.10  ? 204 A1BHB B N3  1 
HETATM 2123 C C4  C A1BHB F 4 .   ? -8.817  3.894   -10.323 0.26 55.23  ? 204 A1BHB B C4  1 
HETATM 2124 C C4  D A1BHB F 4 .   ? -8.817  3.894   -10.322 0.27 55.23  ? 204 A1BHB B C4  1 
HETATM 2125 C C5  C A1BHB F 4 .   ? -8.822  2.404   -10.462 0.26 55.11  ? 204 A1BHB B C5  1 
HETATM 2126 C C5  D A1BHB F 4 .   ? -8.822  2.405   -10.462 0.27 55.11  ? 204 A1BHB B C5  1 
HETATM 2127 C C6  C A1BHB F 4 .   ? -9.637  2.346   -8.149  0.26 53.75  ? 204 A1BHB B C6  1 
HETATM 2128 C C6  D A1BHB F 4 .   ? -9.637  2.346   -8.149  0.27 53.75  ? 204 A1BHB B C6  1 
HETATM 2129 C C7  C A1BHB F 4 .   ? -9.315  3.794   -7.861  0.26 53.79  ? 204 A1BHB B C7  1 
HETATM 2130 C C7  D A1BHB F 4 .   ? -9.314  3.795   -7.861  0.27 53.78  ? 204 A1BHB B C7  1 
HETATM 2131 C C8  C A1BHB F 4 .   ? -7.552  5.617   -14.761 0.26 61.52  ? 204 A1BHB B C8  1 
HETATM 2132 C C8  D A1BHB F 4 .   ? -7.552  5.616   -14.760 0.27 61.53  ? 204 A1BHB B C8  1 
HETATM 2133 C C10 C A1BHB F 4 .   ? -5.524  5.845   -16.060 0.26 63.42  ? 204 A1BHB B C10 1 
HETATM 2134 C C10 D A1BHB F 4 .   ? -5.524  5.845   -16.060 0.27 63.42  ? 204 A1BHB B C10 1 
HETATM 2135 C C13 C A1BHB F 4 .   ? -9.300  4.049   -18.214 0.26 61.90  ? 204 A1BHB B C13 1 
HETATM 2136 C C13 D A1BHB F 4 .   ? -9.300  4.049   -18.214 0.27 61.90  ? 204 A1BHB B C13 1 
HETATM 2137 C C15 C A1BHB F 4 .   ? -9.566  4.652   -15.909 0.26 60.80  ? 204 A1BHB B C15 1 
HETATM 2138 C C15 D A1BHB F 4 .   ? -9.567  4.651   -15.908 0.27 60.79  ? 204 A1BHB B C15 1 
HETATM 2139 O O1  C A1BHB F 4 .   ? -8.695  6.948   -13.185 0.26 61.52  ? 204 A1BHB B O1  1 
HETATM 2140 O O1  D A1BHB F 4 .   ? -8.695  6.948   -13.184 0.27 61.54  ? 204 A1BHB B O1  1 
HETATM 2141 C C1  C A1BHB F 4 .   ? -8.250  5.832   -13.454 0.26 60.32  ? 204 A1BHB B C1  1 
HETATM 2142 C C1  D A1BHB F 4 .   ? -8.250  5.832   -13.454 0.27 60.32  ? 204 A1BHB B C1  1 
HETATM 2143 C C2  C A1BHB F 4 .   ? -8.616  4.908   -11.235 0.26 56.75  ? 204 A1BHB B C2  1 
HETATM 2144 C C2  D A1BHB F 4 .   ? -8.616  4.908   -11.235 0.27 56.75  ? 204 A1BHB B C2  1 
HETATM 2145 C C3  C A1BHB F 4 .   ? -8.724  6.103   -10.527 0.26 56.27  ? 204 A1BHB B C3  1 
HETATM 2146 C C3  D A1BHB F 4 .   ? -8.724  6.104   -10.527 0.27 56.28  ? 204 A1BHB B C3  1 
HETATM 2147 N N2  C A1BHB F 4 .   ? -8.987  5.841   -9.253  0.26 55.43  ? 204 A1BHB B N2  1 
HETATM 2148 N N2  D A1BHB F 4 .   ? -8.987  5.842   -9.252  0.27 55.43  ? 204 A1BHB B N2  1 
HETATM 2149 N N4  C A1BHB F 4 .   ? -8.693  1.792   -9.141  0.26 54.43  ? 204 A1BHB B N4  1 
HETATM 2150 N N4  D A1BHB F 4 .   ? -8.692  1.793   -9.141  0.27 54.42  ? 204 A1BHB B N4  1 
HETATM 2151 C C9  C A1BHB F 4 .   ? -6.239  5.998   -14.859 0.26 62.66  ? 204 A1BHB B C9  1 
HETATM 2152 C C9  D A1BHB F 4 .   ? -6.240  5.998   -14.858 0.27 62.66  ? 204 A1BHB B C9  1 
HETATM 2153 C C11 C A1BHB F 4 .   ? -6.131  5.335   -17.170 0.26 63.82  ? 204 A1BHB B C11 1 
HETATM 2154 C C11 D A1BHB F 4 .   ? -6.132  5.336   -17.169 0.27 63.83  ? 204 A1BHB B C11 1 
HETATM 2155 C C12 C A1BHB F 4 .   ? -7.486  4.938   -17.124 0.26 62.73  ? 204 A1BHB B C12 1 
HETATM 2156 C C12 D A1BHB F 4 .   ? -7.486  4.938   -17.123 0.27 62.74  ? 204 A1BHB B C12 1 
HETATM 2157 N N5  C A1BHB F 4 .   ? -8.034  4.412   -18.268 0.26 62.58  ? 204 A1BHB B N5  1 
HETATM 2158 N N5  D A1BHB F 4 .   ? -8.034  4.413   -18.268 0.27 62.58  ? 204 A1BHB B N5  1 
HETATM 2159 C C14 C A1BHB F 4 .   ? -10.102 4.143   -17.060 0.26 61.27  ? 204 A1BHB B C14 1 
HETATM 2160 C C14 D A1BHB F 4 .   ? -10.102 4.143   -17.059 0.27 61.27  ? 204 A1BHB B C14 1 
HETATM 2161 C C16 C A1BHB F 4 .   ? -8.214  5.068   -15.903 0.26 61.77  ? 204 A1BHB B C16 1 
HETATM 2162 C C16 D A1BHB F 4 .   ? -8.214  5.067   -15.902 0.27 61.77  ? 204 A1BHB B C16 1 
HETATM 2163 S S   C SO4   G 5 .   ? -18.723 11.694  -0.437  0.50 137.10 ? 205 SO4   B S   1 
HETATM 2164 S S   D SO4   G 5 .   ? -18.723 11.694  -0.437  0.50 137.10 ? 205 SO4   B S   1 
HETATM 2165 O O1  C SO4   G 5 .   ? -19.568 12.687  0.175   0.50 138.39 ? 205 SO4   B O1  1 
HETATM 2166 O O1  D SO4   G 5 .   ? -19.568 12.687  0.175   0.50 138.39 ? 205 SO4   B O1  1 
HETATM 2167 O O2  C SO4   G 5 .   ? -17.715 11.276  0.497   0.50 139.83 ? 205 SO4   B O2  1 
HETATM 2168 O O2  D SO4   G 5 .   ? -17.715 11.276  0.497   0.50 139.83 ? 205 SO4   B O2  1 
HETATM 2169 O O3  C SO4   G 5 .   ? -19.515 10.552  -0.807  0.50 136.14 ? 205 SO4   B O3  1 
HETATM 2170 O O3  D SO4   G 5 .   ? -19.515 10.552  -0.807  0.50 136.14 ? 205 SO4   B O3  1 
HETATM 2171 O O4  C SO4   G 5 .   ? -18.089 12.254  -1.607  0.50 139.06 ? 205 SO4   B O4  1 
HETATM 2172 O O4  D SO4   G 5 .   ? -18.089 12.254  -1.607  0.50 139.06 ? 205 SO4   B O4  1 
HETATM 2173 O O   A HOH   H 6 .   ? -8.061  0.745   3.297   0.50 65.52  ? 101 HOH   A O   1 
HETATM 2174 O O   B HOH   H 6 .   ? -8.061  0.745   3.297   0.50 65.52  ? 101 HOH   A O   1 
HETATM 2175 O O   . HOH   H 6 .   ? -2.414  -3.904  -6.529  1.00 59.13  ? 102 HOH   A O   1 
HETATM 2176 O O   A HOH   H 6 .   ? -28.113 -5.851  -28.053 0.50 62.05  ? 103 HOH   A O   1 
HETATM 2177 O O   B HOH   H 6 .   ? -28.113 -5.851  -28.053 0.50 62.05  ? 103 HOH   A O   1 
HETATM 2178 O O   . HOH   H 6 .   ? -3.848  -0.372  -0.586  1.00 60.82  ? 104 HOH   A O   1 
HETATM 2179 O O   A HOH   H 6 .   ? -23.661 19.167  -19.420 0.50 67.13  ? 105 HOH   A O   1 
HETATM 2180 O O   B HOH   H 6 .   ? -23.661 19.167  -19.420 0.50 67.13  ? 105 HOH   A O   1 
HETATM 2181 O O   C HOH   H 6 .   ? 9.202   -9.647  -14.882 0.50 83.37  ? 106 HOH   A O   1 
HETATM 2182 O O   D HOH   H 6 .   ? 9.202   -9.647  -14.882 0.50 83.37  ? 106 HOH   A O   1 
HETATM 2183 O O   . HOH   H 6 .   ? -23.985 9.267   -27.474 1.00 48.98  ? 107 HOH   A O   1 
HETATM 2184 O O   A HOH   H 6 .   ? 7.786   -5.084  -17.358 0.50 90.73  ? 108 HOH   A O   1 
HETATM 2185 O O   B HOH   H 6 .   ? 7.786   -5.084  -17.358 0.50 90.73  ? 108 HOH   A O   1 
HETATM 2186 O O   . HOH   H 6 .   ? -4.724  -14.765 -25.347 1.00 54.33  ? 109 HOH   A O   1 
HETATM 2187 O O   A HOH   H 6 .   ? -29.043 15.696  -14.897 0.50 74.23  ? 110 HOH   A O   1 
HETATM 2188 O O   B HOH   H 6 .   ? -29.043 15.696  -14.897 0.50 74.23  ? 110 HOH   A O   1 
HETATM 2189 O O   A HOH   H 6 .   ? -0.620  -12.587 -23.323 0.50 89.44  ? 111 HOH   A O   1 
HETATM 2190 O O   B HOH   H 6 .   ? -0.620  -12.587 -23.323 0.50 89.44  ? 111 HOH   A O   1 
HETATM 2191 O O   A HOH   H 6 .   ? -5.387  2.164   -10.398 0.23 57.93  ? 112 HOH   A O   1 
HETATM 2192 O O   B HOH   H 6 .   ? -5.388  2.162   -10.398 0.25 57.93  ? 112 HOH   A O   1 
HETATM 2193 O O   A HOH   H 6 .   ? -22.692 -9.383  -34.527 0.50 74.69  ? 113 HOH   A O   1 
HETATM 2194 O O   B HOH   H 6 .   ? -22.692 -9.383  -34.527 0.50 74.69  ? 113 HOH   A O   1 
HETATM 2195 O O   A HOH   H 6 .   ? -26.381 -3.467  -35.357 0.50 77.69  ? 114 HOH   A O   1 
HETATM 2196 O O   B HOH   H 6 .   ? -26.381 -3.467  -35.357 0.50 77.69  ? 114 HOH   A O   1 
HETATM 2197 O O   A HOH   H 6 .   ? -8.110  -1.678  6.542   0.50 69.32  ? 115 HOH   A O   1 
HETATM 2198 O O   B HOH   H 6 .   ? -8.110  -1.678  6.542   0.50 69.32  ? 115 HOH   A O   1 
HETATM 2199 O O   . HOH   H 6 .   ? -3.472  -3.787  0.105   1.00 69.67  ? 116 HOH   A O   1 
HETATM 2200 O O   . HOH   H 6 .   ? -30.813 0.310   -23.116 1.00 58.63  ? 117 HOH   A O   1 
HETATM 2201 O O   . HOH   H 6 .   ? -4.861  -10.057 -5.652  1.00 61.21  ? 118 HOH   A O   1 
HETATM 2202 O O   A HOH   H 6 .   ? -3.125  -11.585 -6.800  0.50 64.22  ? 119 HOH   A O   1 
HETATM 2203 O O   B HOH   H 6 .   ? -3.125  -11.585 -6.800  0.50 64.22  ? 119 HOH   A O   1 
HETATM 2204 O O   A HOH   H 6 .   ? -9.189  2.196   -8.442  0.23 49.30  ? 120 HOH   A O   1 
HETATM 2205 O O   B HOH   H 6 .   ? -9.189  2.197   -8.442  0.25 49.27  ? 120 HOH   A O   1 
HETATM 2206 O O   A HOH   H 6 .   ? -2.825  -8.790  -3.462  0.50 71.13  ? 121 HOH   A O   1 
HETATM 2207 O O   B HOH   H 6 .   ? -2.825  -8.790  -3.462  0.50 71.13  ? 121 HOH   A O   1 
HETATM 2208 O O   A HOH   H 6 .   ? -11.361 3.911   -5.008  0.23 21.08  ? 122 HOH   A O   1 
HETATM 2209 O O   B HOH   H 6 .   ? -11.621 5.330   -4.770  0.25 28.07  ? 122 HOH   A O   1 
HETATM 2210 O O   . HOH   I 6 .   ? -30.431 12.725  -19.715 1.00 70.52  ? 301 HOH   B O   1 
HETATM 2211 O O   . HOH   I 6 .   ? -33.620 1.605   -15.586 1.00 63.61  ? 302 HOH   B O   1 
HETATM 2212 O O   . HOH   I 6 .   ? -17.303 12.958  -5.650  1.00 66.31  ? 303 HOH   B O   1 
HETATM 2213 O O   A HOH   I 6 .   ? -19.685 -12.171 -25.452 0.50 69.01  ? 304 HOH   B O   1 
HETATM 2214 O O   B HOH   I 6 .   ? -19.685 -12.171 -25.452 0.50 69.01  ? 304 HOH   B O   1 
HETATM 2215 O O   A HOH   I 6 .   ? -15.902 -10.136 -15.291 0.50 71.56  ? 305 HOH   B O   1 
HETATM 2216 O O   B HOH   I 6 .   ? -15.902 -10.136 -15.291 0.50 71.56  ? 305 HOH   B O   1 
HETATM 2217 O O   A HOH   I 6 .   ? -16.491 20.828  -14.145 0.50 64.60  ? 306 HOH   B O   1 
HETATM 2218 O O   B HOH   I 6 .   ? -16.491 20.828  -14.145 0.50 64.60  ? 306 HOH   B O   1 
HETATM 2219 O O   . HOH   I 6 .   ? -13.055 -2.281  -14.750 1.00 49.64  ? 307 HOH   B O   1 
HETATM 2220 O O   . HOH   I 6 .   ? -12.538 -3.693  -9.987  1.00 53.27  ? 308 HOH   B O   1 
HETATM 2221 O O   A HOH   I 6 .   ? -6.612  -0.303  -10.942 0.23 52.93  ? 309 HOH   B O   1 
HETATM 2222 O O   B HOH   I 6 .   ? -6.613  -0.303  -10.942 0.25 52.93  ? 309 HOH   B O   1 
HETATM 2223 O O   C HOH   I 6 .   ? -6.605  -0.297  -10.940 0.25 53.00  ? 309 HOH   B O   1 
HETATM 2224 O O   D HOH   I 6 .   ? -6.609  -0.297  -10.943 0.27 52.99  ? 309 HOH   B O   1 
HETATM 2225 O O   . HOH   I 6 .   ? -18.228 -10.799 -16.473 1.00 48.60  ? 310 HOH   B O   1 
HETATM 2226 O O   . HOH   I 6 .   ? -14.282 -5.987  -1.473  1.00 64.45  ? 311 HOH   B O   1 
HETATM 2227 O O   . HOH   I 6 .   ? -26.216 -7.836  -16.676 1.00 51.13  ? 312 HOH   B O   1 
HETATM 2228 O O   . HOH   I 6 .   ? -7.149  -8.900  -3.121  1.00 48.77  ? 313 HOH   B O   1 
HETATM 2229 O O   . HOH   I 6 .   ? -16.838 -7.253  -7.999  1.00 71.68  ? 314 HOH   B O   1 
HETATM 2230 O O   A HOH   I 6 .   ? -8.706  -10.843 -7.593  0.50 77.65  ? 315 HOH   B O   1 
HETATM 2231 O O   B HOH   I 6 .   ? -8.706  -10.843 -7.593  0.50 77.65  ? 315 HOH   B O   1 
HETATM 2232 O O   C HOH   I 6 .   ? -7.383  1.898   -13.738 0.26 47.67  ? 316 HOH   B O   1 
HETATM 2233 O O   D HOH   I 6 .   ? -7.385  1.897   -13.739 0.27 47.64  ? 316 HOH   B O   1 
HETATM 2234 O O   A HOH   I 6 .   ? -28.589 -4.002  -22.261 0.50 68.00  ? 317 HOH   B O   1 
HETATM 2235 O O   B HOH   I 6 .   ? -28.589 -4.002  -22.261 0.50 68.00  ? 317 HOH   B O   1 
HETATM 2236 O O   A HOH   I 6 .   ? -9.446  -7.028  -25.500 0.23 57.90  ? 318 HOH   B O   1 
HETATM 2237 O O   B HOH   I 6 .   ? -9.440  -7.030  -25.509 0.25 58.03  ? 318 HOH   B O   1 
HETATM 2238 O O   C HOH   I 6 .   ? -24.185 -6.462  -4.598  0.50 59.43  ? 319 HOH   B O   1 
HETATM 2239 O O   D HOH   I 6 .   ? -24.185 -6.462  -4.598  0.50 59.43  ? 319 HOH   B O   1 
HETATM 2240 O O   A HOH   I 6 .   ? -12.136 2.148   -5.663  0.23 29.11  ? 320 HOH   B O   1 
HETATM 2241 O O   B HOH   I 6 .   ? -12.133 2.155   -5.659  0.25 29.02  ? 320 HOH   B O   1 
HETATM 2242 O O   C HOH   I 6 .   ? -22.226 15.125  -6.243  0.50 58.08  ? 321 HOH   B O   1 
HETATM 2243 O O   D HOH   I 6 .   ? -22.226 15.125  -6.243  0.50 58.08  ? 321 HOH   B O   1 
HETATM 2244 O O   A HOH   I 6 .   ? -19.873 -7.930  -2.851  0.50 74.24  ? 322 HOH   B O   1 
HETATM 2245 O O   B HOH   I 6 .   ? -19.873 -7.930  -2.851  0.50 74.24  ? 322 HOH   B O   1 
HETATM 2246 O O   A HOH   I 6 .   ? -35.780 6.230   -11.097 0.50 85.51  ? 323 HOH   B O   1 
HETATM 2247 O O   B HOH   I 6 .   ? -35.780 6.230   -11.097 0.50 85.51  ? 323 HOH   B O   1 
HETATM 2248 O O   A HOH   I 6 .   ? -21.650 -12.372 -13.078 0.50 60.90  ? 324 HOH   B O   1 
HETATM 2249 O O   B HOH   I 6 .   ? -21.650 -12.372 -13.078 0.50 60.90  ? 324 HOH   B O   1 
HETATM 2250 O O   . HOH   I 6 .   ? -15.011 -4.480  1.400   1.00 47.06  ? 325 HOH   B O   1 
HETATM 2251 O O   . HOH   I 6 .   ? -30.640 12.619  -16.517 1.00 67.42  ? 326 HOH   B O   1 
HETATM 2252 O O   A HOH   I 6 .   ? -15.501 9.230   -0.633  0.50 70.52  ? 327 HOH   B O   1 
HETATM 2253 O O   B HOH   I 6 .   ? -15.501 9.230   -0.633  0.50 70.52  ? 327 HOH   B O   1 
HETATM 2254 O O   C HOH   I 6 .   ? -20.513 14.233  -33.378 0.50 69.69  ? 328 HOH   B O   1 
HETATM 2255 O O   D HOH   I 6 .   ? -20.513 14.233  -33.378 0.50 69.69  ? 328 HOH   B O   1 
HETATM 2256 O O   . HOH   I 6 .   ? -11.147 11.951  -19.129 1.00 55.58  ? 329 HOH   B O   1 
HETATM 2257 O O   A HOH   I 6 .   ? -35.407 -5.119  -10.354 0.50 67.73  ? 330 HOH   B O   1 
HETATM 2258 O O   B HOH   I 6 .   ? -35.407 -5.119  -10.354 0.50 67.73  ? 330 HOH   B O   1 
HETATM 2259 O O   . HOH   I 6 .   ? -27.881 -6.232  -18.555 1.00 61.87  ? 331 HOH   B O   1 
HETATM 2260 O O   A HOH   I 6 .   ? -21.568 -13.718 -21.804 0.50 67.03  ? 332 HOH   B O   1 
HETATM 2261 O O   B HOH   I 6 .   ? -21.568 -13.718 -21.804 0.50 67.03  ? 332 HOH   B O   1 
HETATM 2262 O O   A HOH   I 6 .   ? -16.189 -14.697 -16.554 0.50 75.49  ? 333 HOH   B O   1 
HETATM 2263 O O   B HOH   I 6 .   ? -16.189 -14.697 -16.554 0.50 75.49  ? 333 HOH   B O   1 
HETATM 2264 O O   . HOH   I 6 .   ? -14.480 -12.236 -16.619 1.00 53.69  ? 334 HOH   B O   1 
HETATM 2265 O O   A HOH   I 6 .   ? -16.178 26.285  -12.066 0.50 78.57  ? 335 HOH   B O   1 
HETATM 2266 O O   B HOH   I 6 .   ? -16.178 26.285  -12.066 0.50 78.57  ? 335 HOH   B O   1 
HETATM 2267 O O   A HOH   I 6 .   ? -21.366 5.689   -32.695 0.50 79.74  ? 336 HOH   B O   1 
HETATM 2268 O O   B HOH   I 6 .   ? -21.366 5.689   -32.695 0.50 79.74  ? 336 HOH   B O   1 
HETATM 2269 O O   . HOH   I 6 .   ? -18.606 14.991  -22.124 1.00 49.57  ? 337 HOH   B O   1 
HETATM 2270 O O   C HOH   I 6 .   ? -7.299  10.034  -19.215 0.26 48.85  ? 338 HOH   B O   1 
HETATM 2271 O O   D HOH   I 6 .   ? -7.299  10.033  -19.215 0.27 48.85  ? 338 HOH   B O   1 
HETATM 2272 O O   A HOH   I 6 .   ? -27.542 -7.075  -5.388  0.50 81.59  ? 339 HOH   B O   1 
HETATM 2273 O O   B HOH   I 6 .   ? -27.542 -7.075  -5.388  0.50 81.59  ? 339 HOH   B O   1 
HETATM 2274 O O   . HOH   I 6 .   ? -16.456 -14.215 -30.869 1.00 71.40  ? 340 HOH   B O   1 
HETATM 2275 O O   . HOH   I 6 .   ? -31.911 7.149   -4.780  1.00 72.94  ? 341 HOH   B O   1 
HETATM 2276 O O   A HOH   I 6 .   ? -0.373  0.224   -13.669 0.50 72.61  ? 342 HOH   B O   1 
HETATM 2277 O O   B HOH   I 6 .   ? -0.373  0.224   -13.669 0.50 72.61  ? 342 HOH   B O   1 
HETATM 2278 O O   A HOH   I 6 .   ? -23.987 -8.529  -2.943  0.50 100.06 ? 343 HOH   B O   1 
HETATM 2279 O O   B HOH   I 6 .   ? -23.987 -8.529  -2.943  0.50 100.06 ? 343 HOH   B O   1 
HETATM 2280 O O   A HOH   I 6 .   ? -24.370 11.715  -26.241 0.50 79.64  ? 344 HOH   B O   1 
HETATM 2281 O O   B HOH   I 6 .   ? -24.370 11.715  -26.241 0.50 79.64  ? 344 HOH   B O   1 
HETATM 2282 O O   A HOH   I 6 .   ? -21.200 7.125   0.000   0.23 61.85  ? 345 HOH   B O   1 
HETATM 2283 O O   B HOH   I 6 .   ? -21.200 7.128   0.000   0.25 61.80  ? 345 HOH   B O   1 
HETATM 2284 O O   A HOH   I 6 .   ? -29.865 -7.510  -5.810  0.50 75.47  ? 346 HOH   B O   1 
HETATM 2285 O O   B HOH   I 6 .   ? -29.865 -7.510  -5.810  0.50 75.47  ? 346 HOH   B O   1 
HETATM 2286 O O   A HOH   I 6 .   ? -30.541 4.536   -2.512  0.25 44.22  ? 347 HOH   B O   1 
HETATM 2287 O O   B HOH   I 6 .   ? -30.541 4.536   -2.512  0.25 44.22  ? 347 HOH   B O   1 
HETATM 2288 O O   A HOH   I 6 .   ? -24.240 -14.921 -17.318 0.50 72.65  ? 348 HOH   B O   1 
HETATM 2289 O O   B HOH   I 6 .   ? -24.240 -14.921 -17.318 0.50 72.65  ? 348 HOH   B O   1 
HETATM 2290 O O   A HOH   I 6 .   ? -11.133 -4.898  -8.292  0.23 58.56  ? 349 HOH   B O   1 
HETATM 2291 O O   B HOH   I 6 .   ? -11.133 -4.899  -8.292  0.25 58.59  ? 349 HOH   B O   1 
HETATM 2292 O O   A HOH   I 6 .   ? -29.560 -1.368  -18.945 0.50 64.49  ? 350 HOH   B O   1 
HETATM 2293 O O   B HOH   I 6 .   ? -29.560 -1.368  -18.945 0.50 64.49  ? 350 HOH   B O   1 
HETATM 2294 O O   . HOH   I 6 .   ? -20.485 2.840   -32.593 1.00 57.87  ? 351 HOH   B O   1 
HETATM 2295 O O   A HOH   I 6 .   ? -11.008 7.665   -13.880 0.23 37.28  ? 352 HOH   B O   1 
HETATM 2296 O O   B HOH   I 6 .   ? -11.007 7.666   -13.881 0.25 37.23  ? 352 HOH   B O   1 
HETATM 2297 O O   A HOH   I 6 .   ? -17.129 14.611  -30.917 0.50 68.33  ? 353 HOH   B O   1 
HETATM 2298 O O   B HOH   I 6 .   ? -17.129 14.611  -30.917 0.50 68.33  ? 353 HOH   B O   1 
HETATM 2299 O O   . HOH   I 6 .   ? -14.741 16.523  -20.233 1.00 67.05  ? 354 HOH   B O   1 
HETATM 2300 O O   A HOH   I 6 .   ? -20.384 24.629  -16.929 0.50 74.98  ? 355 HOH   B O   1 
HETATM 2301 O O   B HOH   I 6 .   ? -20.384 24.629  -16.929 0.50 74.98  ? 355 HOH   B O   1 
HETATM 2302 O O   A HOH   I 6 .   ? -19.137 25.252  -14.407 0.50 61.81  ? 356 HOH   B O   1 
HETATM 2303 O O   B HOH   I 6 .   ? -19.137 25.252  -14.407 0.50 61.81  ? 356 HOH   B O   1 
HETATM 2304 O O   A HOH   I 6 .   ? -19.669 -13.433 -22.926 0.50 53.48  ? 357 HOH   B O   1 
HETATM 2305 O O   B HOH   I 6 .   ? -19.669 -13.433 -22.926 0.50 53.48  ? 357 HOH   B O   1 
HETATM 2306 O O   . HOH   I 6 .   ? -25.820 -4.740  -3.973  1.00 52.20  ? 358 HOH   B O   1 
HETATM 2307 O O   A HOH   I 6 .   ? -18.636 18.892  -21.860 0.50 69.93  ? 359 HOH   B O   1 
HETATM 2308 O O   B HOH   I 6 .   ? -18.636 18.892  -21.860 0.50 69.93  ? 359 HOH   B O   1 
HETATM 2309 O O   C HOH   I 6 .   ? -18.026 18.026  -27.052 0.50 88.94  ? 360 HOH   B O   1 
HETATM 2310 O O   D HOH   I 6 .   ? -18.026 18.026  -27.052 0.50 88.94  ? 360 HOH   B O   1 
HETATM 2311 O O   A HOH   I 6 .   ? -6.962  -6.010  0.075   0.50 74.82  ? 361 HOH   B O   1 
HETATM 2312 O O   B HOH   I 6 .   ? -6.962  -6.010  0.075   0.50 74.82  ? 361 HOH   B O   1 
HETATM 2313 O O   A HOH   I 6 .   ? -10.474 22.093  -14.620 0.50 88.82  ? 362 HOH   B O   1 
HETATM 2314 O O   B HOH   I 6 .   ? -10.474 22.093  -14.620 0.50 88.82  ? 362 HOH   B O   1 
HETATM 2315 O O   A HOH   I 6 .   ? -19.505 -5.859  -0.863  0.50 57.16  ? 363 HOH   B O   1 
HETATM 2316 O O   B HOH   I 6 .   ? -19.505 -5.859  -0.863  0.50 57.16  ? 363 HOH   B O   1 
HETATM 2317 O O   A HOH   I 6 .   ? -17.051 16.661  -21.894 0.50 58.94  ? 364 HOH   B O   1 
HETATM 2318 O O   B HOH   I 6 .   ? -17.051 16.661  -21.894 0.50 58.94  ? 364 HOH   B O   1 
HETATM 2319 O O   C HOH   I 6 .   ? -3.748  3.748   -27.053 0.26 87.94  ? 365 HOH   B O   1 
HETATM 2320 O O   D HOH   I 6 .   ? -3.748  3.749   -27.052 0.27 87.81  ? 365 HOH   B O   1 
HETATM 2321 O O   . HOH   I 6 .   ? -1.786  -14.614 -9.636  1.00 72.50  ? 366 HOH   B O   1 
HETATM 2322 O O   A HOH   I 6 .   ? -7.045  -10.824 -5.215  0.50 67.95  ? 367 HOH   B O   1 
HETATM 2323 O O   B HOH   I 6 .   ? -7.045  -10.824 -5.215  0.50 67.95  ? 367 HOH   B O   1 
HETATM 2324 O O   A HOH   I 6 .   ? -30.308 -12.092 -27.052 0.25 101.06 ? 368 HOH   B O   1 
HETATM 2325 O O   B HOH   I 6 .   ? -30.308 -12.092 -27.052 0.25 101.06 ? 368 HOH   B O   1 
HETATM 2326 O O   A HOH   I 6 .   ? -22.453 3.201   0.234   0.23 29.49  ? 369 HOH   B O   1 
HETATM 2327 O O   B HOH   I 6 .   ? -21.736 4.786   -1.060  0.25 54.32  ? 369 HOH   B O   1 
HETATM 2328 O O   . HOH   I 6 .   ? -29.417 -5.543  -0.986  1.00 55.27  ? 370 HOH   B O   1 
HETATM 2329 O O   A HOH   I 6 .   ? -11.850 12.570  -14.777 0.23 54.21  ? 371 HOH   B O   1 
HETATM 2330 O O   B HOH   I 6 .   ? -11.850 12.571  -14.777 0.25 54.17  ? 371 HOH   B O   1 
HETATM 2331 O O   A HOH   I 6 .   ? -32.231 -6.790  -6.734  0.50 72.07  ? 372 HOH   B O   1 
HETATM 2332 O O   B HOH   I 6 .   ? -32.231 -6.790  -6.734  0.50 72.07  ? 372 HOH   B O   1 
HETATM 2333 O O   A HOH   I 6 .   ? -19.399 -12.014 -13.197 0.50 63.93  ? 373 HOH   B O   1 
HETATM 2334 O O   B HOH   I 6 .   ? -19.399 -12.014 -13.197 0.50 63.93  ? 373 HOH   B O   1 
HETATM 2335 O O   A HOH   I 6 .   ? -11.131 -6.990  1.925   0.50 65.18  ? 374 HOH   B O   1 
HETATM 2336 O O   B HOH   I 6 .   ? -11.131 -6.990  1.925   0.50 65.18  ? 374 HOH   B O   1 
HETATM 2337 O O   A HOH   I 6 .   ? -8.993  5.813   -8.688  0.23 63.94  ? 375 HOH   B O   1 
HETATM 2338 O O   B HOH   I 6 .   ? -8.994  5.814   -8.688  0.25 63.93  ? 375 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 1.0233 1.0513 1.0173 0.0956  0.1041  -0.1417 50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.0023 1.0512 0.9681 0.1038  0.1043  -0.1468 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.9695 1.0026 0.9130 0.1106  0.1101  -0.1176 50  ASP   A C   
4    O O   . ASP   A 7   ? 0.9892 0.9887 0.9385 0.1208  0.1101  -0.1041 50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.0412 1.0951 1.0235 0.1144  0.0972  -0.1746 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.0742 1.1556 1.0389 0.1213  0.0989  -0.1847 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.0842 1.1967 1.0437 0.1180  0.1006  -0.2083 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.1174 1.1883 1.0748 0.1310  0.0987  -0.1703 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.8710 0.9250 0.7859 0.1062  0.1139  -0.1089 51  MET   A N   
10   C CA  . MET   A 8   ? 0.8298 0.8722 0.7194 0.1107  0.1185  -0.0823 51  MET   A CA  
11   C C   . MET   A 8   ? 0.7887 0.8353 0.6677 0.1240  0.1132  -0.0866 51  MET   A C   
12   O O   . MET   A 8   ? 0.7501 0.8228 0.6372 0.1241  0.1102  -0.1098 51  MET   A O   
13   C CB  . MET   A 8   ? 0.8005 0.8632 0.6685 0.0994  0.1226  -0.0740 51  MET   A CB  
14   C CG  . MET   A 8   ? 0.8103 0.8737 0.6931 0.0881  0.1241  -0.0745 51  MET   A CG  
15   S SD  . MET   A 8   ? 0.8255 0.9033 0.6816 0.0798  0.1271  -0.0592 51  MET   A SD  
16   C CE  . MET   A 8   ? 0.8117 0.8810 0.7008 0.0709  0.1286  -0.0566 51  MET   A CE  
17   N N   . TYR   A 9   ? 0.7680 0.7888 0.6307 0.1361  0.1121  -0.0663 52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.7599 0.7827 0.6143 0.1514  0.1027  -0.0712 52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.7422 0.7516 0.5641 0.1571  0.1033  -0.0476 52  TYR   A C   
20   O O   . TYR   A 9   ? 0.7126 0.7032 0.5200 0.1527  0.1124  -0.0261 52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.8117 0.8091 0.6821 0.1687  0.0931  -0.0786 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.8826 0.8313 0.7433 0.1759  0.0965  -0.0543 52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.8962 0.8309 0.7777 0.1650  0.1047  -0.0523 52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.9269 0.8419 0.7566 0.1936  0.0923  -0.0332 52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.9597 0.8485 0.8359 0.1690  0.1123  -0.0282 52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.9583 0.8246 0.7738 0.2002  0.0996  -0.0084 52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.9786 0.8323 0.8193 0.1862  0.1117  -0.0047 52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.0158 0.8220 0.8474 0.1891  0.1236  0.0210  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.7385 0.7603 0.5528 0.1662  0.0938  -0.0543 53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.7329 0.7422 0.5152 0.1747  0.0902  -0.0363 53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.7630 0.7423 0.5328 0.2004  0.0751  -0.0330 53  ILE   A C   
32   O O   . ILE   A 10  ? 0.7657 0.7509 0.5586 0.2105  0.0634  -0.0526 53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.7153 0.7598 0.4964 0.1641  0.0894  -0.0451 53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.7171 0.7920 0.5273 0.1650  0.0823  -0.0720 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.7098 0.7710 0.4872 0.1430  0.1025  -0.0403 53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.7240 0.8227 0.5314 0.1589  0.0799  -0.0760 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.7904 0.7402 0.5221 0.2121  0.0742  -0.0106 54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.8388 0.7519 0.5424 0.2403  0.0583  -0.0030 54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.8127 0.7249 0.4826 0.2479  0.0516  0.0053  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.7866 0.6971 0.4368 0.2376  0.0662  0.0220  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.8984 0.7603 0.5760 0.2502  0.0681  0.0221  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.9276 0.7730 0.6317 0.2511  0.0689  0.0164  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.9940 0.7866 0.6743 0.2562  0.0838  0.0451  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.0416 0.8160 0.6870 0.2562  0.0981  0.0695  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.0436 0.8129 0.7422 0.2593  0.0832  0.0431  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.8340 0.7499 0.5014 0.2652  0.0291  -0.0085 55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.8487 0.7631 0.4860 0.2734  0.0196  -0.0039 55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.8935 0.7588 0.4734 0.2906  0.0256  0.0246  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.9500 0.7769 0.5120 0.3059  0.0261  0.0361  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.8782 0.8049 0.5311 0.2903  -0.0088 -0.0277 55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.9124 0.8483 0.5505 0.2935  -0.0209 -0.0311 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.9449 0.9001 0.6138 0.3071  -0.0500 -0.0598 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.9565 0.9309 0.6278 0.2995  -0.0564 -0.0662 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.9995 0.9465 0.6260 0.3180  -0.0704 -0.0576 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 1.0855 0.9853 0.6585 0.3458  -0.0781 -0.0419 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.9634 0.9265 0.5943 0.3089  -0.0751 -0.0634 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.8997 0.7642 0.4511 0.2882  0.0316  0.0362  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.9529 0.7757 0.4483 0.3022  0.0436  0.0637  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.9801 0.7936 0.4357 0.3207  0.0273  0.0628  56  ALA   A C   
60   O O   . ALA   A 13  ? 1.0396 0.8184 0.4436 0.3349  0.0380  0.0844  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.9341 0.7645 0.4352 0.2797  0.0735  0.0805  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.9493 0.7919 0.4279 0.3201  0.0047  0.0391  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.9616 0.7938 0.4055 0.3387  -0.0143 0.0351  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.9559 0.8293 0.4402 0.3239  -0.0283 0.0119  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.8799 0.7927 0.4168 0.2949  -0.0168 0.0022  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.9729 0.8363 0.4317 0.3416  -0.0499 0.0043  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.9751 0.8699 0.4664 0.3292  -0.0640 -0.0155 58  ASP   A CA  
68   C C   . ASP   A 15  ? 1.0026 0.8993 0.4757 0.3146  -0.0452 -0.0007 58  ASP   A C   
69   O O   . ASP   A 15  ? 1.0538 0.9234 0.4818 0.3234  -0.0280 0.0217  58  ASP   A O   
70   C CB  . ASP   A 15  ? 1.0046 0.8870 0.4824 0.3562  -0.1005 -0.0346 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 1.0402 0.9240 0.5424 0.3729  -0.1247 -0.0540 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 1.0273 0.9172 0.5506 0.3648  -0.1111 -0.0500 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 1.1023 0.9795 0.6025 0.3959  -0.1591 -0.0743 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.9673 0.8951 0.4775 0.2920  -0.0464 -0.0125 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.9577 0.8856 0.4516 0.2806  -0.0340 -0.0011 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.9917 0.9073 0.4675 0.2982  -0.0603 -0.0136 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.9727 0.9088 0.4880 0.2888  -0.0777 -0.0342 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.9296 0.8917 0.4674 0.2460  -0.0177 -0.0027 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.9170 0.8868 0.4667 0.2338  0.0047  0.0075  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.9329 0.8936 0.4565 0.2362  -0.0110 0.0060  59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.8898 0.8931 0.4812 0.2034  0.0173  0.0015  59  ILE   A CD1 
82   N N   A THR   A 17  ? 1.0405 0.9218 0.4577 0.3242  -0.0624 -0.0021 60  THR   A N   
83   N N   B THR   A 17  ? 1.0306 0.9125 0.4483 0.3235  -0.0621 -0.0021 60  THR   A N   
84   N N   C THR   A 17  ? 1.0405 0.9218 0.4577 0.3242  -0.0624 -0.0021 60  THR   A N   
85   N N   D THR   A 17  ? 1.0306 0.9125 0.4483 0.3235  -0.0621 -0.0021 60  THR   A N   
86   C CA  A THR   A 17  ? 1.0723 0.9325 0.4566 0.3497  -0.0892 -0.0137 60  THR   A CA  
87   C CA  B THR   A 17  ? 1.0566 0.9180 0.4430 0.3489  -0.0898 -0.0146 60  THR   A CA  
88   C CA  C THR   A 17  ? 1.0723 0.9325 0.4566 0.3497  -0.0892 -0.0137 60  THR   A CA  
89   C CA  D THR   A 17  ? 1.0566 0.9180 0.4430 0.3489  -0.0898 -0.0146 60  THR   A CA  
90   C C   A THR   A 17  ? 1.1000 0.9375 0.4318 0.3598  -0.0730 0.0046  60  THR   A C   
91   C C   B THR   A 17  ? 1.0965 0.9328 0.4269 0.3615  -0.0747 0.0038  60  THR   A C   
92   C C   C THR   A 17  ? 1.1000 0.9375 0.4318 0.3598  -0.0730 0.0046  60  THR   A C   
93   C C   D THR   A 17  ? 1.0965 0.9328 0.4269 0.3615  -0.0747 0.0038  60  THR   A C   
94   O O   A THR   A 17  ? 1.1145 0.9383 0.4182 0.3626  -0.0466 0.0269  60  THR   A O   
95   O O   B THR   A 17  ? 1.1188 0.9384 0.4171 0.3676  -0.0503 0.0256  60  THR   A O   
96   O O   C THR   A 17  ? 1.1145 0.9383 0.4182 0.3626  -0.0466 0.0269  60  THR   A O   
97   O O   D THR   A 17  ? 1.1188 0.9384 0.4171 0.3676  -0.0503 0.0256  60  THR   A O   
98   C CB  A THR   A 17  ? 1.1253 0.9603 0.4819 0.3832  -0.1155 -0.0239 60  THR   A CB  
99   C CB  B THR   A 17  ? 1.0964 0.9369 0.4634 0.3799  -0.1174 -0.0270 60  THR   A CB  
100  C CB  C THR   A 17  ? 1.1253 0.9603 0.4819 0.3832  -0.1155 -0.0239 60  THR   A CB  
101  C CB  D THR   A 17  ? 1.0964 0.9369 0.4634 0.3799  -0.1174 -0.0270 60  THR   A CB  
102  O OG1 A THR   A 17  ? 1.1674 0.9682 0.4657 0.4026  -0.0978 -0.0001 60  THR   A OG1 
103  O OG1 B THR   A 17  ? 1.0492 0.9198 0.4795 0.3673  -0.1337 -0.0496 60  THR   A OG1 
104  O OG1 C THR   A 17  ? 1.1674 0.9682 0.4657 0.4026  -0.0978 -0.0001 60  THR   A OG1 
105  O OG1 D THR   A 17  ? 1.0492 0.9198 0.4795 0.3673  -0.1337 -0.0496 60  THR   A OG1 
106  C CG2 A THR   A 17  ? 1.0945 0.9535 0.5064 0.3752  -0.1291 -0.0420 60  THR   A CG2 
107  C CG2 B THR   A 17  ? 1.1434 0.9555 0.4645 0.4124  -0.1468 -0.0388 60  THR   A CG2 
108  C CG2 C THR   A 17  ? 1.0945 0.9535 0.5064 0.3752  -0.1291 -0.0420 60  THR   A CG2 
109  C CG2 D THR   A 17  ? 1.1434 0.9555 0.4645 0.4124  -0.1468 -0.0388 60  THR   A CG2 
110  N N   . TRP   A 18  ? 1.1003 0.9347 0.4238 0.3643  -0.0876 -0.0054 61  TRP   A N   
111  C CA  . TRP   A 18  ? 1.1687 0.9777 0.4360 0.3833  -0.0791 0.0059  61  TRP   A CA  
112  C C   . TRP   A 18  ? 1.2866 1.0570 0.4893 0.4235  -0.0924 0.0064  61  TRP   A C   
113  O O   . TRP   A 18  ? 1.3133 1.0783 0.5208 0.4384  -0.1245 -0.0132 61  TRP   A O   
114  C CB  . TRP   A 18  ? 1.1513 0.9658 0.4312 0.3792  -0.0971 -0.0096 61  TRP   A CB  
115  C CG  . TRP   A 18  ? 1.1753 0.9675 0.4032 0.3983  -0.0887 -0.0012 61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 1.2795 1.0392 0.4469 0.4350  -0.1045 -0.0074 61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 1.1739 0.9757 0.4062 0.3830  -0.0631 0.0130  61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 1.2787 1.0287 0.4133 0.4427  -0.0865 0.0027  61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 1.2235 1.0000 0.4003 0.4112  -0.0622 0.0146  61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 1.0920 0.9206 0.3674 0.3504  -0.0413 0.0239  61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 1.2280 1.0085 0.3987 0.4067  -0.0401 0.0255  61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 1.1127 0.9431 0.3800 0.3471  -0.0232 0.0345  61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 1.1646 0.9727 0.3835 0.3745  -0.0221 0.0349  61  TRP   A CH2 
124  N N   . GLU   A 19  ? 1.3775 1.1222 0.5243 0.4396  -0.0673 0.0287  62  GLU   A N   
125  C CA  . GLU   A 19  ? 1.5345 1.2356 0.6074 0.4786  -0.0734 0.0351  62  GLU   A CA  
126  C C   . GLU   A 19  ? 1.5765 1.2544 0.5899 0.5020  -0.0687 0.0380  62  GLU   A C   
127  O O   . GLU   A 19  ? 1.5428 1.2269 0.5529 0.4906  -0.0340 0.0561  62  GLU   A O   
128  C CB  . GLU   A 19  ? 1.6083 1.2952 0.6650 0.4771  -0.0424 0.0614  62  GLU   A CB  
129  C CG  . GLU   A 19  ? 1.6286 1.3331 0.7371 0.4608  -0.0514 0.0553  62  GLU   A CG  
130  C CD  . GLU   A 19  ? 1.7384 1.4271 0.8367 0.4859  -0.0916 0.0354  62  GLU   A CD  
131  O OE1 . GLU   A 19  ? 1.8512 1.4951 0.8805 0.5210  -0.0988 0.0436  62  GLU   A OE1 
132  O OE2 . GLU   A 19  ? 1.6988 1.4191 0.8583 0.4710  -0.1155 0.0114  62  GLU   A OE2 
133  N N   . LYS   A 20  ? 1.6714 1.3266 0.6458 0.5330  -0.1043 0.0175  63  LYS   A N   
134  C CA  . LYS   A 20  ? 1.7236 1.3534 0.6347 0.5612  -0.1055 0.0150  63  LYS   A CA  
135  C C   . LYS   A 20  ? 1.7289 1.3252 0.5673 0.5818  -0.0690 0.0441  63  LYS   A C   
136  O O   . LYS   A 20  ? 1.7910 1.3638 0.6015 0.5940  -0.0675 0.0557  63  LYS   A O   
137  C CB  . LYS   A 20  ? 1.8133 1.4209 0.6932 0.5941  -0.1549 -0.0145 63  LYS   A CB  
138  C CG  . LYS   A 20  ? 1.8279 1.4631 0.7710 0.5775  -0.1876 -0.0445 63  LYS   A CG  
139  C CD  . LYS   A 20  ? 1.8945 1.5135 0.8273 0.6056  -0.2408 -0.0769 63  LYS   A CD  
140  C CE  . LYS   A 20  ? 1.8796 1.5278 0.8895 0.5841  -0.2722 -0.1069 63  LYS   A CE  
141  N NZ  . LYS   A 20  ? 1.8862 1.5431 0.9373 0.5876  -0.3104 -0.1313 63  LYS   A NZ  
142  N N   . ASP   A 21  ? 1.7277 1.3216 0.5397 0.5847  -0.0392 0.0558  64  ASP   A N   
143  C CA  . ASP   A 21  ? 1.8347 1.3985 0.5809 0.6020  0.0027  0.0849  64  ASP   A CA  
144  C C   . ASP   A 21  ? 1.7607 1.3361 0.5456 0.5743  0.0352  0.1100  64  ASP   A C   
145  O O   . ASP   A 21  ? 1.7670 1.3081 0.5057 0.5906  0.0450  0.1271  64  ASP   A O   
146  C CB  . ASP   A 21  ? 2.0244 1.5341 0.6711 0.6502  -0.0137 0.0841  64  ASP   A CB  
147  C CG  . ASP   A 21  ? 2.1378 1.6307 0.7368 0.6828  -0.0464 0.0579  64  ASP   A CG  
148  O OD1 . ASP   A 21  ? 2.2019 1.6936 0.7731 0.6911  -0.0234 0.0611  64  ASP   A OD1 
149  O OD2 . ASP   A 21  ? 2.1906 1.6718 0.7819 0.7013  -0.0957 0.0325  64  ASP   A OD2 
150  N N   . ALA   A 22  ? 1.6657 1.2852 0.5318 0.5342  0.0493  0.1113  65  ALA   A N   
151  C CA  . ALA   A 22  ? 1.5737 1.2058 0.4736 0.5084  0.0905  0.1364  65  ALA   A CA  
152  C C   . ALA   A 22  ? 1.5705 1.2032 0.4518 0.5102  0.1326  0.1526  65  ALA   A C   
153  O O   . ALA   A 22  ? 1.5893 1.2224 0.4457 0.5264  0.1250  0.1397  65  ALA   A O   
154  C CB  . ALA   A 22  ? 1.5156 1.1923 0.5036 0.4691  0.0844  0.1281  65  ALA   A CB  
155  N N   . GLU   A 23  ? 1.5788 1.2054 0.4640 0.4996  0.1745  0.1792  66  GLU   A N   
156  C CA  . GLU   A 23  ? 1.5637 1.2032 0.4617 0.4897  0.2214  0.1959  66  GLU   A CA  
157  C C   . GLU   A 23  ? 1.4753 1.1602 0.4340 0.4693  0.2121  0.1779  66  GLU   A C   
158  O O   . GLU   A 23  ? 1.3007 1.0162 0.3232 0.4420  0.1921  0.1668  66  GLU   A O   
159  C CB  . GLU   A 23  ? 1.5915 1.2359 0.5307 0.4645  0.2535  0.2177  66  GLU   A CB  
160  C CG  . GLU   A 23  ? 1.6344 1.2831 0.5836 0.4566  0.3068  0.2390  66  GLU   A CG  
161  C CD  . GLU   A 23  ? 1.6999 1.3311 0.6634 0.4427  0.3329  0.2624  66  GLU   A CD  
162  O OE1 . GLU   A 23  ? 1.8684 1.4545 0.7688 0.4626  0.3590  0.2851  66  GLU   A OE1 
163  O OE2 . GLU   A 23  ? 1.6759 1.3333 0.7075 0.4140  0.3242  0.2575  66  GLU   A OE2 
164  N N   . VAL   A 24  ? 1.4669 1.1540 0.4032 0.4841  0.2236  0.1738  67  VAL   A N   
165  C CA  . VAL   A 24  ? 1.4340 1.1591 0.4229 0.4685  0.2141  0.1572  67  VAL   A CA  
166  C C   . VAL   A 24  ? 1.4291 1.1750 0.4511 0.4556  0.2605  0.1724  67  VAL   A C   
167  O O   . VAL   A 24  ? 1.4673 1.1945 0.4449 0.4754  0.2921  0.1847  67  VAL   A O   
168  C CB  . VAL   A 24  ? 1.4555 1.1664 0.3984 0.4968  0.1870  0.1370  67  VAL   A CB  
169  C CG1 . VAL   A 24  ? 1.3656 1.1086 0.3590 0.4823  0.1729  0.1201  67  VAL   A CG1 
170  C CG2 . VAL   A 24  ? 1.4704 1.1566 0.3793 0.5122  0.1435  0.1228  67  VAL   A CG2 
171  N N   A THR   A 25  ? 1.3535 1.1371 0.4530 0.4229  0.2645  0.1715  68  THR   A N   
172  N N   B THR   A 25  ? 1.3536 1.1371 0.4531 0.4229  0.2645  0.1715  68  THR   A N   
173  N N   C THR   A 25  ? 1.3523 1.1363 0.4517 0.4232  0.2636  0.1707  68  THR   A N   
174  N N   D THR   A 25  ? 1.3523 1.1363 0.4517 0.4232  0.2636  0.1707  68  THR   A N   
175  C CA  A THR   A 25  ? 1.3388 1.1461 0.4845 0.4070  0.3065  0.1842  68  THR   A CA  
176  C CA  B THR   A 25  ? 1.3388 1.1461 0.4845 0.4070  0.3065  0.1842  68  THR   A CA  
177  C CA  C THR   A 25  ? 1.3344 1.1440 0.4810 0.4079  0.3039  0.1817  68  THR   A CA  
178  C CA  D THR   A 25  ? 1.3344 1.1440 0.4810 0.4079  0.3039  0.1817  68  THR   A CA  
179  C C   A THR   A 25  ? 1.2586 1.1092 0.4840 0.3781  0.2941  0.1722  68  THR   A C   
180  C C   B THR   A 25  ? 1.2586 1.1091 0.4840 0.3781  0.2941  0.1722  68  THR   A C   
181  C C   C THR   A 25  ? 1.2505 1.1019 0.4755 0.3786  0.2884  0.1694  68  THR   A C   
182  C C   D THR   A 25  ? 1.2505 1.1019 0.4755 0.3786  0.2884  0.1694  68  THR   A C   
183  O O   A THR   A 25  ? 1.2146 1.0728 0.4531 0.3699  0.2562  0.1572  68  THR   A O   
184  O O   B THR   A 25  ? 1.2145 1.0727 0.4530 0.3699  0.2562  0.1572  68  THR   A O   
185  O O   C THR   A 25  ? 1.2089 1.0652 0.4435 0.3709  0.2505  0.1552  68  THR   A O   
186  O O   D THR   A 25  ? 1.2089 1.0652 0.4435 0.3709  0.2505  0.1552  68  THR   A O   
187  C CB  A THR   A 25  ? 1.3630 1.1537 0.5078 0.3989  0.3373  0.2074  68  THR   A CB  
188  C CB  B THR   A 25  ? 1.3630 1.1537 0.5078 0.3989  0.3373  0.2074  68  THR   A CB  
189  C CB  C THR   A 25  ? 1.3621 1.1571 0.5090 0.4003  0.3395  0.2056  68  THR   A CB  
190  C CB  D THR   A 25  ? 1.3621 1.1571 0.5090 0.4003  0.3395  0.2056  68  THR   A CB  
191  O OG1 A THR   A 25  ? 1.3678 1.1788 0.5554 0.3865  0.3806  0.2189  68  THR   A OG1 
192  O OG1 B THR   A 25  ? 1.3679 1.1789 0.5555 0.3865  0.3806  0.2189  68  THR   A OG1 
193  O OG1 C THR   A 25  ? 1.3711 1.1862 0.5537 0.3927  0.3825  0.2151  68  THR   A OG1 
194  O OG1 D THR   A 25  ? 1.3711 1.1862 0.5537 0.3927  0.3825  0.2151  68  THR   A OG1 
195  C CG2 A THR   A 25  ? 1.3059 1.1035 0.4897 0.3750  0.3161  0.2060  68  THR   A CG2 
196  C CG2 B THR   A 25  ? 1.3058 1.1034 0.4895 0.3750  0.3161  0.2060  68  THR   A CG2 
197  C CG2 C THR   A 25  ? 1.3033 1.1080 0.4966 0.3734  0.3246  0.2067  68  THR   A CG2 
198  C CG2 D THR   A 25  ? 1.3033 1.1080 0.4966 0.3734  0.3246  0.2067  68  THR   A CG2 
199  N N   A GLY   A 26  ? 1.2387 1.1152 0.5149 0.3641  0.3256  0.1787  69  GLY   A N   
200  N N   B GLY   A 26  ? 1.2385 1.1150 0.5147 0.3641  0.3256  0.1787  69  GLY   A N   
201  N N   C GLY   A 26  ? 1.2231 1.1024 0.5011 0.3640  0.3171  0.1743  69  GLY   A N   
202  N N   D GLY   A 26  ? 1.2231 1.1024 0.5011 0.3640  0.3171  0.1743  69  GLY   A N   
203  C CA  A GLY   A 26  ? 1.1883 1.1052 0.5377 0.3411  0.3162  0.1669  69  GLY   A CA  
204  C CA  B GLY   A 26  ? 1.1883 1.1052 0.5377 0.3411  0.3162  0.1669  69  GLY   A CA  
205  C CA  C GLY   A 26  ? 1.1670 1.0847 0.5168 0.3393  0.3036  0.1626  69  GLY   A CA  
206  C CA  D GLY   A 26  ? 1.1670 1.0847 0.5168 0.3393  0.3036  0.1626  69  GLY   A CA  
207  C C   A GLY   A 26  ? 1.1830 1.1121 0.5311 0.3540  0.3005  0.1504  69  GLY   A C   
208  C C   B GLY   A 26  ? 1.1829 1.1119 0.5310 0.3540  0.3005  0.1504  69  GLY   A C   
209  C C   C GLY   A 26  ? 1.1533 1.0856 0.5084 0.3497  0.2885  0.1463  69  GLY   A C   
210  C C   D GLY   A 26  ? 1.1533 1.0856 0.5084 0.3497  0.2885  0.1463  69  GLY   A C   
211  O O   A GLY   A 26  ? 1.2249 1.1305 0.5166 0.3773  0.2847  0.1439  69  GLY   A O   
212  O O   B GLY   A 26  ? 1.2249 1.1305 0.5166 0.3773  0.2847  0.1439  69  GLY   A O   
213  O O   C GLY   A 26  ? 1.1712 1.0850 0.4824 0.3665  0.2617  0.1360  69  GLY   A O   
214  O O   D GLY   A 26  ? 1.1712 1.0850 0.4824 0.3665  0.2617  0.1360  69  GLY   A O   
215  N N   A ASN   A 27  ? 1.1560 1.1193 0.5653 0.3405  0.3019  0.1422  70  ASN   A N   
216  N N   B ASN   A 27  ? 1.1560 1.1192 0.5652 0.3405  0.3019  0.1422  70  ASN   A N   
217  N N   C ASN   A 27  ? 1.1347 1.0990 0.5461 0.3401  0.3031  0.1423  70  ASN   A N   
218  N N   D ASN   A 27  ? 1.1347 1.0990 0.5461 0.3401  0.3031  0.1423  70  ASN   A N   
219  C CA  A ASN   A 27  ? 1.1626 1.1395 0.5815 0.3508  0.2842  0.1253  70  ASN   A CA  
220  C CA  B ASN   A 27  ? 1.1628 1.1396 0.5816 0.3508  0.2842  0.1253  70  ASN   A CA  
221  C CA  C ASN   A 27  ? 1.1322 1.1149 0.5632 0.3472  0.2869  0.1255  70  ASN   A CA  
222  C CA  D ASN   A 27  ? 1.1322 1.1149 0.5632 0.3472  0.2869  0.1255  70  ASN   A CA  
223  C C   A ASN   A 27  ? 1.0938 1.0792 0.5377 0.3332  0.2426  0.1138  70  ASN   A C   
224  C C   B ASN   A 27  ? 1.0937 1.0791 0.5376 0.3332  0.2426  0.1138  70  ASN   A C   
225  C C   C ASN   A 27  ? 1.0796 1.0650 0.5234 0.3333  0.2425  0.1138  70  ASN   A C   
226  C C   D ASN   A 27  ? 1.0796 1.0650 0.5234 0.3333  0.2425  0.1138  70  ASN   A C   
227  O O   A ASN   A 27  ? 1.0689 1.0473 0.5121 0.3172  0.2298  0.1183  70  ASN   A O   
228  O O   B ASN   A 27  ? 1.0689 1.0473 0.5121 0.3172  0.2299  0.1183  70  ASN   A O   
229  O O   C ASN   A 27  ? 1.0589 1.0336 0.4943 0.3199  0.2282  0.1180  70  ASN   A O   
230  O O   D ASN   A 27  ? 1.0589 1.0336 0.4943 0.3199  0.2282  0.1180  70  ASN   A O   
231  C CB  A ASN   A 27  ? 1.1906 1.1968 0.6557 0.3532  0.3158  0.1236  70  ASN   A CB  
232  C CB  B ASN   A 27  ? 1.1909 1.1971 0.6559 0.3532  0.3158  0.1236  70  ASN   A CB  
233  C CB  C ASN   A 27  ? 1.1316 1.1498 0.6272 0.3398  0.3135  0.1237  70  ASN   A CB  
234  C CB  D ASN   A 27  ? 1.1316 1.1498 0.6272 0.3398  0.3135  0.1237  70  ASN   A CB  
235  C CG  A ASN   A 27  ? 1.1707 1.2052 0.7061 0.3271  0.3332  0.1291  70  ASN   A CG  
236  C CG  B ASN   A 27  ? 1.1710 1.2055 0.7064 0.3271  0.3332  0.1291  70  ASN   A CG  
237  C CG  C ASN   A 27  ? 1.0834 1.1244 0.6417 0.3107  0.3149  0.1268  70  ASN   A CG  
238  C CG  D ASN   A 27  ? 1.0834 1.1244 0.6417 0.3107  0.3149  0.1268  70  ASN   A CG  
239  O OD1 A ASN   A 27  ? 1.2014 1.2263 0.7356 0.3165  0.3533  0.1440  70  ASN   A OD1 
240  O OD1 B ASN   A 27  ? 1.2020 1.2269 0.7362 0.3165  0.3533  0.1440  70  ASN   A OD1 
241  O OD1 C ASN   A 27  ? 1.0932 1.1223 0.6460 0.2988  0.3243  0.1392  70  ASN   A OD1 
242  O OD1 D ASN   A 27  ? 1.0932 1.1223 0.6460 0.2988  0.3243  0.1392  70  ASN   A OD1 
243  N ND2 A ASN   A 27  ? 1.1382 1.2057 0.7352 0.3181  0.3240  0.1161  70  ASN   A ND2 
244  N ND2 B ASN   A 27  ? 1.1384 1.2059 0.7353 0.3181  0.3240  0.1161  70  ASN   A ND2 
245  N ND2 C ASN   A 27  ? 1.0638 1.1363 0.6815 0.3010  0.3040  0.1142  70  ASN   A ND2 
246  N ND2 D ASN   A 27  ? 1.0638 1.1363 0.6815 0.3010  0.3040  0.1142  70  ASN   A ND2 
247  N N   . SER   A 28  ? 1.0719 1.0686 0.5328 0.3378  0.2230  0.0998  71  SER   A N   
248  C CA  . SER   A 28  ? 1.0606 1.0562 0.5311 0.3258  0.1828  0.0898  71  SER   A CA  
249  C C   . SER   A 28  ? 1.0446 1.0664 0.5659 0.3207  0.1761  0.0806  71  SER   A C   
250  O O   . SER   A 28  ? 1.1182 1.1354 0.6330 0.3344  0.1584  0.0696  71  SER   A O   
251  C CB  . SER   A 28  ? 1.0819 1.0505 0.5063 0.3418  0.1550  0.0806  71  SER   A CB  
252  O OG  . SER   A 28  ? 1.1918 1.1353 0.5654 0.3548  0.1593  0.0850  71  SER   A OG  
253  N N   . PRO   A 29  ? 0.9934 1.0417 0.5670 0.3028  0.1874  0.0832  72  PRO   A N   
254  C CA  . PRO   A 29  ? 0.9938 1.0691 0.6198 0.3009  0.1804  0.0723  72  PRO   A CA  
255  C C   . PRO   A 29  ? 0.9550 1.0245 0.5837 0.2899  0.1404  0.0656  72  PRO   A C   
256  O O   . PRO   A 29  ? 0.8988 0.9544 0.5078 0.2744  0.1270  0.0714  72  PRO   A O   
257  C CB  . PRO   A 29  ? 0.9803 1.0825 0.6588 0.2855  0.2078  0.0774  72  PRO   A CB  
258  C CG  . PRO   A 29  ? 0.9880 1.0732 0.6422 0.2694  0.2084  0.0894  72  PRO   A CG  
259  C CD  . PRO   A 29  ? 0.9915 1.0438 0.5784 0.2846  0.2042  0.0945  72  PRO   A CD  
260  N N   . ARG   A 30  ? 0.9811 1.0595 0.6315 0.2991  0.1233  0.0539  73  ARG   A N   
261  C CA  . ARG   A 30  ? 1.0152 1.0879 0.6713 0.2902  0.0870  0.0485  73  ARG   A CA  
262  C C   . ARG   A 30  ? 0.9537 1.0584 0.6688 0.2805  0.0876  0.0422  73  ARG   A C   
263  O O   . ARG   A 30  ? 0.9318 1.0595 0.6875 0.2931  0.0938  0.0316  73  ARG   A O   
264  C CB  . ARG   A 30  ? 1.1357 1.1914 0.7747 0.3088  0.0625  0.0393  73  ARG   A CB  
265  C CG  . ARG   A 30  ? 1.2563 1.2787 0.8407 0.3186  0.0563  0.0419  73  ARG   A CG  
266  C CD  . ARG   A 30  ? 1.3454 1.3482 0.9147 0.3383  0.0326  0.0313  73  ARG   A CD  
267  N NE  . ARG   A 30  ? 1.4608 1.4373 0.9852 0.3525  0.0323  0.0297  73  ARG   A NE  
268  C CZ  . ARG   A 30  ? 1.4825 1.4277 0.9708 0.3449  0.0127  0.0332  73  ARG   A CZ  
269  N NH1 . ARG   A 30  ? 1.5255 1.4608 1.0140 0.3223  -0.0046 0.0406  73  ARG   A NH1 
270  N NH2 . ARG   A 30  ? 1.3692 1.2934 0.8223 0.3604  0.0109  0.0281  73  ARG   A NH2 
271  N N   . LEU   A 31  ? 0.9200 1.0266 0.6410 0.2598  0.0804  0.0465  74  LEU   A N   
272  C CA  . LEU   A 31  ? 0.8783 1.0134 0.6537 0.2490  0.0779  0.0388  74  LEU   A CA  
273  C C   . LEU   A 31  ? 0.8689 0.9918 0.6313 0.2427  0.0397  0.0345  74  LEU   A C   
274  O O   . LEU   A 31  ? 0.8402 0.9367 0.5559 0.2323  0.0283  0.0436  74  LEU   A O   
275  C CB  . LEU   A 31  ? 0.8612 1.0048 0.6489 0.2315  0.1023  0.0470  74  LEU   A CB  
276  C CG  . LEU   A 31  ? 0.8919 1.0427 0.6884 0.2361  0.1425  0.0547  74  LEU   A CG  
277  C CD1 . LEU   A 31  ? 0.8774 1.0295 0.6825 0.2178  0.1603  0.0635  74  LEU   A CD1 
278  C CD2 . LEU   A 31  ? 0.8972 1.0788 0.7507 0.2470  0.1616  0.0452  74  LEU   A CD2 
279  N N   . ASP   A 32  ? 0.8596 1.0014 0.6631 0.2483  0.0218  0.0208  75  ASP   A N   
280  C CA  . ASP   A 32  ? 0.8764 1.0094 0.6716 0.2427  -0.0127 0.0157  75  ASP   A CA  
281  C C   . ASP   A 32  ? 0.8296 0.9782 0.6466 0.2240  -0.0075 0.0141  75  ASP   A C   
282  O O   . ASP   A 32  ? 0.8370 1.0192 0.7170 0.2227  0.0036  0.0028  75  ASP   A O   
283  C CB  . ASP   A 32  ? 0.9310 1.0794 0.7653 0.2595  -0.0364 -0.0011 75  ASP   A CB  
284  C CG  . ASP   A 32  ? 0.9774 1.1061 0.7883 0.2799  -0.0491 -0.0019 75  ASP   A CG  
285  O OD1 . ASP   A 32  ? 1.0169 1.1079 0.7675 0.2783  -0.0583 0.0104  75  ASP   A OD1 
286  O OD2 . ASP   A 32  ? 0.9955 1.1473 0.8523 0.2970  -0.0499 -0.0162 75  ASP   A OD2 
287  N N   . VAL   A 33  ? 0.8119 0.9377 0.5827 0.2102  -0.0162 0.0231  76  VAL   A N   
288  C CA  . VAL   A 33  ? 0.7919 0.9285 0.5753 0.1927  -0.0107 0.0213  76  VAL   A CA  
289  C C   . VAL   A 33  ? 0.8154 0.9348 0.5648 0.1886  -0.0423 0.0182  76  VAL   A C   
290  O O   . VAL   A 33  ? 0.8183 0.9086 0.5205 0.1954  -0.0632 0.0241  76  VAL   A O   
291  C CB  . VAL   A 33  ? 0.7747 0.9038 0.5371 0.1800  0.0170  0.0346  76  VAL   A CB  
292  C CG1 . VAL   A 33  ? 0.7628 0.9026 0.5472 0.1866  0.0480  0.0395  76  VAL   A CG1 
293  C CG2 . VAL   A 33  ? 0.7852 0.8814 0.4831 0.1755  0.0094  0.0467  76  VAL   A CG2 
294  N N   . ALA   A 34  ? 0.8073 0.9419 0.5795 0.1789  -0.0461 0.0086  77  ALA   A N   
295  C CA  . ALA   A 34  ? 0.8258 0.9448 0.5614 0.1743  -0.0715 0.0048  77  ALA   A CA  
296  C C   . ALA   A 34  ? 0.8066 0.9264 0.5312 0.1564  -0.0531 0.0090  77  ALA   A C   
297  O O   . ALA   A 34  ? 0.7697 0.9102 0.5372 0.1499  -0.0287 0.0076  77  ALA   A O   
298  C CB  . ALA   A 34  ? 0.8309 0.9675 0.6046 0.1835  -0.0991 -0.0157 77  ALA   A CB  
299  N N   . LEU   A 35  ? 0.8082 0.9042 0.4761 0.1494  -0.0627 0.0147  78  LEU   A N   
300  C CA  . LEU   A 35  ? 0.7948 0.8916 0.4499 0.1339  -0.0478 0.0161  78  LEU   A CA  
301  C C   . LEU   A 35  ? 0.8286 0.9225 0.4657 0.1331  -0.0701 0.0034  78  LEU   A C   
302  O O   . LEU   A 35  ? 0.8651 0.9332 0.4483 0.1387  -0.0913 0.0073  78  LEU   A O   
303  C CB  . LEU   A 35  ? 0.7975 0.8708 0.4028 0.1262  -0.0340 0.0335  78  LEU   A CB  
304  C CG  . LEU   A 35  ? 0.7837 0.8579 0.3751 0.1114  -0.0184 0.0344  78  LEU   A CG  
305  C CD1 . LEU   A 35  ? 0.7473 0.8430 0.3848 0.1065  0.0034  0.0308  78  LEU   A CD1 
306  C CD2 . LEU   A 35  ? 0.8187 0.8702 0.3641 0.1046  -0.0097 0.0491  78  LEU   A CD2 
307  N N   . ASP   A 36  ? 0.8006 0.9173 0.4798 0.1275  -0.0662 -0.0113 79  ASP   A N   
308  C CA  . ASP   A 36  ? 0.8073 0.9265 0.4815 0.1294  -0.0897 -0.0296 79  ASP   A CA  
309  C C   . ASP   A 36  ? 0.8266 0.9323 0.4525 0.1180  -0.0793 -0.0256 79  ASP   A C   
310  O O   . ASP   A 36  ? 0.7923 0.8930 0.4051 0.1078  -0.0532 -0.0110 79  ASP   A O   
311  C CB  . ASP   A 36  ? 0.7848 0.9360 0.5378 0.1304  -0.0939 -0.0507 79  ASP   A CB  
312  C CG  . ASP   A 36  ? 0.7498 0.9166 0.5415 0.1164  -0.0701 -0.0552 79  ASP   A CG  
313  O OD1 . ASP   A 36  ? 0.7215 0.8769 0.4807 0.1068  -0.0492 -0.0424 79  ASP   A OD1 
314  O OD2 . ASP   A 36  ? 0.7532 0.9435 0.6118 0.1154  -0.0734 -0.0726 79  ASP   A OD2 
315  N N   . GLU   A 37  ? 0.8657 0.9671 0.4684 0.1210  -0.0995 -0.0404 80  GLU   A N   
316  C CA  . GLU   A 37  ? 0.8916 0.9789 0.4402 0.1129  -0.0917 -0.0388 80  GLU   A CA  
317  C C   . GLU   A 37  ? 0.8412 0.9473 0.4272 0.1001  -0.0667 -0.0440 80  GLU   A C   
318  O O   . GLU   A 37  ? 0.8396 0.9374 0.3892 0.0916  -0.0511 -0.0389 80  GLU   A O   
319  C CB  . GLU   A 37  ? 0.9463 1.0222 0.4565 0.1235  -0.1221 -0.0549 80  GLU   A CB  
320  C CG  . GLU   A 37  ? 1.0087 1.0624 0.4442 0.1184  -0.1143 -0.0492 80  GLU   A CG  
321  C CD  . GLU   A 37  ? 1.0739 1.1169 0.4681 0.1304  -0.1425 -0.0684 80  GLU   A CD  
322  O OE1 . GLU   A 37  ? 1.0501 1.1135 0.4817 0.1316  -0.1508 -0.0930 80  GLU   A OE1 
323  O OE2 . GLU   A 37  ? 1.1312 1.1431 0.4557 0.1399  -0.1584 -0.0595 80  GLU   A OE2 
324  N N   A SER   A 38  ? 0.8066 0.9363 0.4644 0.0988  -0.0618 -0.0536 81  SER   A N   
325  N N   B SER   A 38  ? 0.8064 0.9361 0.4643 0.0988  -0.0618 -0.0536 81  SER   A N   
326  N N   C SER   A 38  ? 0.8087 0.9384 0.4665 0.0990  -0.0624 -0.0538 81  SER   A N   
327  N N   D SER   A 38  ? 0.8086 0.9383 0.4664 0.0990  -0.0624 -0.0538 81  SER   A N   
328  C CA  A SER   A 38  ? 0.7831 0.9260 0.4791 0.0879  -0.0384 -0.0566 81  SER   A CA  
329  C CA  B SER   A 38  ? 0.7830 0.9259 0.4791 0.0879  -0.0384 -0.0566 81  SER   A CA  
330  C CA  C SER   A 38  ? 0.7870 0.9307 0.4850 0.0883  -0.0401 -0.0580 81  SER   A CA  
331  C CA  D SER   A 38  ? 0.7870 0.9306 0.4849 0.0883  -0.0401 -0.0580 81  SER   A CA  
332  C C   A SER   A 38  ? 0.7568 0.8971 0.4590 0.0826  -0.0109 -0.0352 81  SER   A C   
333  C C   B SER   A 38  ? 0.7568 0.8971 0.4590 0.0826  -0.0109 -0.0351 81  SER   A C   
334  C C   C SER   A 38  ? 0.7606 0.9025 0.4675 0.0827  -0.0120 -0.0371 81  SER   A C   
335  C C   D SER   A 38  ? 0.7607 0.9026 0.4676 0.0827  -0.0120 -0.0371 81  SER   A C   
336  O O   A SER   A 38  ? 0.7444 0.8919 0.4772 0.0758  0.0082  -0.0347 81  SER   A O   
337  O O   B SER   A 38  ? 0.7445 0.8920 0.4773 0.0758  0.0082  -0.0347 81  SER   A O   
338  O O   C SER   A 38  ? 0.7501 0.9004 0.4925 0.0761  0.0063  -0.0377 81  SER   A O   
339  O O   D SER   A 38  ? 0.7503 0.9006 0.4927 0.0761  0.0063  -0.0377 81  SER   A O   
340  C CB  A SER   A 38  ? 0.7779 0.9422 0.5460 0.0878  -0.0449 -0.0758 81  SER   A CB  
341  C CB  B SER   A 38  ? 0.7779 0.9422 0.5460 0.0878  -0.0449 -0.0758 81  SER   A CB  
342  C CB  C SER   A 38  ? 0.7848 0.9497 0.5539 0.0889  -0.0484 -0.0778 81  SER   A CB  
343  C CB  D SER   A 38  ? 0.7848 0.9497 0.5539 0.0889  -0.0484 -0.0778 81  SER   A CB  
344  O OG  A SER   A 38  ? 0.8161 0.9848 0.5899 0.0980  -0.0770 -0.0943 81  SER   A OG  
345  O OG  B SER   A 38  ? 0.8162 0.9849 0.5900 0.0980  -0.0770 -0.0943 81  SER   A OG  
346  O OG  C SER   A 38  ? 0.8314 0.9979 0.5944 0.0975  -0.0804 -0.0994 81  SER   A OG  
347  O OG  D SER   A 38  ? 0.8316 0.9981 0.5946 0.0975  -0.0803 -0.0994 81  SER   A OG  
348  N N   A GLY   A 39  ? 0.7554 0.8832 0.4281 0.0872  -0.0108 -0.0188 82  GLY   A N   
349  N N   B GLY   A 39  ? 0.7554 0.8832 0.4281 0.0872  -0.0108 -0.0188 82  GLY   A N   
350  N N   C GLY   A 39  ? 0.7583 0.8870 0.4327 0.0866  -0.0104 -0.0199 82  GLY   A N   
351  N N   D GLY   A 39  ? 0.7583 0.8869 0.4327 0.0866  -0.0104 -0.0199 82  GLY   A N   
352  C CA  A GLY   A 39  ? 0.7337 0.8558 0.4037 0.0848  0.0110  -0.0003 82  GLY   A CA  
353  C CA  B GLY   A 39  ? 0.7337 0.8559 0.4037 0.0848  0.0110  -0.0003 82  GLY   A CA  
354  C CA  C GLY   A 39  ? 0.7351 0.8588 0.4087 0.0840  0.0121  -0.0017 82  GLY   A CA  
355  C CA  D GLY   A 39  ? 0.7351 0.8588 0.4087 0.0840  0.0121  -0.0017 82  GLY   A CA  
356  C C   A GLY   A 39  ? 0.7101 0.8452 0.4332 0.0888  0.0226  0.0026  82  GLY   A C   
357  C C   B GLY   A 39  ? 0.7100 0.8452 0.4331 0.0888  0.0226  0.0026  82  GLY   A C   
358  C C   C GLY   A 39  ? 0.7113 0.8485 0.4398 0.0874  0.0240  0.0007  82  GLY   A C   
359  C C   D GLY   A 39  ? 0.7113 0.8485 0.4398 0.0874  0.0240  0.0007  82  GLY   A C   
360  O O   A GLY   A 39  ? 0.6931 0.8235 0.4151 0.0880  0.0421  0.0157  82  GLY   A O   
361  O O   B GLY   A 39  ? 0.6931 0.8234 0.4150 0.0880  0.0421  0.0157  82  GLY   A O   
362  O O   C GLY   A 39  ? 0.6902 0.8254 0.4260 0.0847  0.0454  0.0111  82  GLY   A O   
363  O O   D GLY   A 39  ? 0.6901 0.8253 0.4259 0.0847  0.0454  0.0110  82  GLY   A O   
364  N N   A ASP   A 40  ? 0.7138 0.8645 0.4813 0.0936  0.0112  -0.0096 83  ASP   A N   
365  N N   B ASP   A 40  ? 0.7137 0.8645 0.4812 0.0936  0.0112  -0.0096 83  ASP   A N   
366  N N   C ASP   A 40  ? 0.7179 0.8679 0.4832 0.0940  0.0109  -0.0089 83  ASP   A N   
367  N N   D ASP   A 40  ? 0.7179 0.8679 0.4831 0.0940  0.0109  -0.0089 83  ASP   A N   
368  C CA  A ASP   A 40  ? 0.7055 0.8718 0.5299 0.0968  0.0250  -0.0080 83  ASP   A CA  
369  C CA  B ASP   A 40  ? 0.7056 0.8718 0.5300 0.0968  0.0250  -0.0080 83  ASP   A CA  
370  C CA  C ASP   A 40  ? 0.7103 0.8763 0.5339 0.0968  0.0249  -0.0079 83  ASP   A CA  
371  C CA  D ASP   A 40  ? 0.7104 0.8763 0.5340 0.0968  0.0249  -0.0079 83  ASP   A CA  
372  C C   A ASP   A 40  ? 0.7083 0.8720 0.5239 0.1088  0.0169  -0.0017 83  ASP   A C   
373  C C   B ASP   A 40  ? 0.7083 0.8721 0.5240 0.1088  0.0169  -0.0017 83  ASP   A C   
374  C C   C ASP   A 40  ? 0.7107 0.8752 0.5286 0.1088  0.0171  -0.0020 83  ASP   A C   
375  C C   D ASP   A 40  ? 0.7107 0.8753 0.5287 0.1088  0.0171  -0.0020 83  ASP   A C   
376  O O   A ASP   A 40  ? 0.7320 0.8954 0.5390 0.1162  -0.0097 -0.0113 83  ASP   A O   
377  O O   B ASP   A 40  ? 0.7320 0.8955 0.5390 0.1162  -0.0097 -0.0113 83  ASP   A O   
378  O O   C ASP   A 40  ? 0.7338 0.8997 0.5474 0.1163  -0.0094 -0.0124 83  ASP   A O   
379  O O   D ASP   A 40  ? 0.7339 0.8998 0.5475 0.1163  -0.0094 -0.0124 83  ASP   A O   
380  C CB  A ASP   A 40  ? 0.7094 0.8975 0.5986 0.0939  0.0185  -0.0275 83  ASP   A CB  
381  C CB  B ASP   A 40  ? 0.7094 0.8975 0.5986 0.0939  0.0185  -0.0275 83  ASP   A CB  
382  C CB  C ASP   A 40  ? 0.7165 0.9036 0.6031 0.0931  0.0189  -0.0274 83  ASP   A CB  
383  C CB  D ASP   A 40  ? 0.7165 0.9036 0.6031 0.0932  0.0189  -0.0274 83  ASP   A CB  
384  C CG  A ASP   A 40  ? 0.7130 0.9026 0.6216 0.0825  0.0302  -0.0334 83  ASP   A CG  
385  C CG  B ASP   A 40  ? 0.7131 0.9026 0.6217 0.0825  0.0302  -0.0334 83  ASP   A CG  
386  C CG  C ASP   A 40  ? 0.7242 0.9108 0.6227 0.0820  0.0296  -0.0328 83  ASP   A CG  
387  C CG  D ASP   A 40  ? 0.7243 0.9109 0.6228 0.0820  0.0296  -0.0328 83  ASP   A CG  
388  O OD1 A ASP   A 40  ? 0.7157 0.8943 0.6087 0.0780  0.0529  -0.0191 83  ASP   A OD1 
389  O OD1 B ASP   A 40  ? 0.7159 0.8945 0.6089 0.0780  0.0529  -0.0190 83  ASP   A OD1 
390  O OD1 C ASP   A 40  ? 0.7326 0.9059 0.6025 0.0778  0.0480  -0.0191 83  ASP   A OD1 
391  O OD1 D ASP   A 40  ? 0.7329 0.9062 0.6027 0.0778  0.0480  -0.0191 83  ASP   A OD1 
392  O OD2 A ASP   A 40  ? 0.7345 0.9349 0.6736 0.0797  0.0143  -0.0537 83  ASP   A OD2 
393  O OD2 B ASP   A 40  ? 0.7347 0.9351 0.6738 0.0797  0.0143  -0.0537 83  ASP   A OD2 
394  O OD2 C ASP   A 40  ? 0.7443 0.9433 0.6818 0.0786  0.0172  -0.0525 83  ASP   A OD2 
395  O OD2 D ASP   A 40  ? 0.7445 0.9435 0.6819 0.0786  0.0172  -0.0525 83  ASP   A OD2 
396  N N   . PHE   A 41  ? 0.6875 0.8472 0.5024 0.1126  0.0376  0.0129  84  PHE   A N   
397  C CA  . PHE   A 41  ? 0.6873 0.8463 0.5011 0.1257  0.0336  0.0174  84  PHE   A CA  
398  C C   . PHE   A 41  ? 0.7087 0.8947 0.5915 0.1298  0.0360  0.0052  84  PHE   A C   
399  O O   . PHE   A 41  ? 0.7250 0.9258 0.6541 0.1209  0.0519  0.0003  84  PHE   A O   
400  C CB  . PHE   A 41  ? 0.6674 0.8134 0.4570 0.1302  0.0547  0.0342  84  PHE   A CB  
401  C CG  . PHE   A 41  ? 0.6602 0.7807 0.3878 0.1284  0.0487  0.0445  84  PHE   A CG  
402  C CD1 . PHE   A 41  ? 0.6802 0.7850 0.3727 0.1351  0.0288  0.0467  84  PHE   A CD1 
403  C CD2 . PHE   A 41  ? 0.6659 0.7776 0.3743 0.1201  0.0631  0.0516  84  PHE   A CD2 
404  C CE1 . PHE   A 41  ? 0.6930 0.7741 0.3352 0.1310  0.0255  0.0562  84  PHE   A CE1 
405  C CE2 . PHE   A 41  ? 0.6698 0.7619 0.3310 0.1175  0.0584  0.0589  84  PHE   A CE2 
406  C CZ  . PHE   A 41  ? 0.6728 0.7498 0.3024 0.1219  0.0408  0.0616  84  PHE   A CZ  
407  N N   . SER   A 42  ? 0.7438 0.9359 0.6370 0.1427  0.0199  -0.0007 85  SER   A N   
408  C CA  . SER   A 42  ? 0.7679 0.9899 0.7343 0.1483  0.0241  -0.0136 85  SER   A CA  
409  C C   . SER   A 42  ? 0.8027 1.0244 0.7644 0.1651  0.0217  -0.0108 85  SER   A C   
410  O O   . SER   A 42  ? 0.8039 1.0002 0.7062 0.1725  0.0049  -0.0031 85  SER   A O   
411  C CB  . SER   A 42  ? 0.7951 1.0329 0.7969 0.1473  -0.0044 -0.0356 85  SER   A CB  
412  O OG  . SER   A 42  ? 0.8383 1.0587 0.7917 0.1577  -0.0403 -0.0398 85  SER   A OG  
413  N N   . LEU   A 43  ? 0.8330 1.0809 0.8561 0.1705  0.0401  -0.0166 86  LEU   A N   
414  C CA  . LEU   A 43  ? 0.8771 1.1299 0.9059 0.1887  0.0382  -0.0183 86  LEU   A CA  
415  C C   . LEU   A 43  ? 0.8739 1.1388 0.9287 0.2004  -0.0007 -0.0387 86  LEU   A C   
416  O O   . LEU   A 43  ? 0.8327 1.1289 0.9592 0.1987  -0.0052 -0.0572 86  LEU   A O   
417  C CB  . LEU   A 43  ? 0.8965 1.1742 0.9813 0.1901  0.0776  -0.0169 86  LEU   A CB  
418  C CG  . LEU   A 43  ? 0.9230 1.1823 0.9713 0.1837  0.1142  0.0046  86  LEU   A CG  
419  C CD1 . LEU   A 43  ? 0.9485 1.2310 1.0575 0.1788  0.1556  0.0066  86  LEU   A CD1 
420  C CD2 . LEU   A 43  ? 0.9567 1.1905 0.9402 0.1984  0.1140  0.0165  86  LEU   A CD2 
421  N N   . VAL   A 44  ? 0.9255 1.1637 0.9233 0.2123  -0.0282 -0.0351 87  VAL   A N   
422  C CA  . VAL   A 44  ? 1.0073 1.2502 1.0206 0.2321  -0.0609 -0.0500 87  VAL   A CA  
423  C C   . VAL   A 44  ? 1.0781 1.3473 1.1439 0.2440  -0.0370 -0.0549 87  VAL   A C   
424  O O   . VAL   A 44  ? 1.1878 1.4489 1.2314 0.2422  -0.0040 -0.0393 87  VAL   A O   
425  C CB  . VAL   A 44  ? 1.0201 1.2193 0.9508 0.2407  -0.0875 -0.0384 87  VAL   A CB  
426  C CG1 . VAL   A 44  ? 1.0394 1.2367 0.9800 0.2632  -0.1232 -0.0523 87  VAL   A CG1 
427  C CG2 . VAL   A 44  ? 1.0156 1.1880 0.8890 0.2269  -0.1016 -0.0303 87  VAL   A CG2 
428  N N   . GLU   A 45  ? 1.1635 1.4627 1.2949 0.2572  -0.0525 -0.0767 88  GLU   A N   
429  C CA  . GLU   A 45  ? 1.2391 1.5703 1.4314 0.2682  -0.0248 -0.0841 88  GLU   A CA  
430  C C   . GLU   A 45  ? 1.2840 1.6287 1.5105 0.2921  -0.0587 -0.1056 88  GLU   A C   
431  O O   . GLU   A 45  ? 1.3057 1.6385 1.5075 0.3094  -0.0581 -0.1024 88  GLU   A O   
432  C CB  . GLU   A 45  ? 1.2653 1.6345 1.5360 0.2517  0.0106  -0.0897 88  GLU   A CB  
433  C CG  . GLU   A 45  ? 1.2597 1.6161 1.5002 0.2370  0.0573  -0.0658 88  GLU   A CG  
434  C CD  . GLU   A 45  ? 1.2423 1.6102 1.4969 0.2469  0.0981  -0.0592 88  GLU   A CD  
435  O OE1 . GLU   A 45  ? 1.2562 1.6270 1.5090 0.2678  0.0865  -0.0674 88  GLU   A OE1 
436  O OE2 . GLU   A 45  ? 1.2341 1.6062 1.4997 0.2350  0.1413  -0.0462 88  GLU   A OE2 
437  N N   C LYS   B 6   ? 1.7502 1.8506 1.3238 0.1320  0.0807  -0.1389 15  LYS   B N   
438  N N   D LYS   B 6   ? 1.7502 1.8506 1.3238 0.1320  0.0807  -0.1389 15  LYS   B N   
439  C CA  C LYS   B 6   ? 1.7551 1.8489 1.3266 0.1392  0.0840  -0.1388 15  LYS   B CA  
440  C CA  D LYS   B 6   ? 1.7551 1.8489 1.3266 0.1392  0.0840  -0.1388 15  LYS   B CA  
441  C C   C LYS   B 6   ? 1.7755 1.8510 1.3385 0.1436  0.0843  -0.1317 15  LYS   B C   
442  C C   D LYS   B 6   ? 1.7755 1.8510 1.3385 0.1436  0.0843  -0.1317 15  LYS   B C   
443  O O   C LYS   B 6   ? 1.7933 1.8605 1.3530 0.1506  0.0854  -0.1303 15  LYS   B O   
444  O O   D LYS   B 6   ? 1.7933 1.8605 1.3530 0.1506  0.0854  -0.1303 15  LYS   B O   
445  C CB  C LYS   B 6   ? 1.7440 1.8420 1.3182 0.1322  0.0883  -0.1402 15  LYS   B CB  
446  C CB  D LYS   B 6   ? 1.7440 1.8420 1.3182 0.1322  0.0883  -0.1402 15  LYS   B CB  
447  C CG  C LYS   B 6   ? 1.7399 1.8583 1.3223 0.1305  0.0887  -0.1471 15  LYS   B CG  
448  C CG  D LYS   B 6   ? 1.7399 1.8583 1.3223 0.1305  0.0887  -0.1471 15  LYS   B CG  
449  C CD  C LYS   B 6   ? 1.7403 1.8622 1.3238 0.1265  0.0929  -0.1489 15  LYS   B CD  
450  C CD  D LYS   B 6   ? 1.7403 1.8622 1.3238 0.1265  0.0929  -0.1489 15  LYS   B CD  
451  C CE  C LYS   B 6   ? 1.7463 1.8909 1.3374 0.1271  0.0936  -0.1557 15  LYS   B CE  
452  C CE  D LYS   B 6   ? 1.7463 1.8909 1.3374 0.1271  0.0936  -0.1557 15  LYS   B CE  
453  N NZ  C LYS   B 6   ? 1.7504 1.8984 1.3414 0.1240  0.0977  -0.1576 15  LYS   B NZ  
454  N NZ  D LYS   B 6   ? 1.7504 1.8984 1.3414 0.1240  0.0977  -0.1576 15  LYS   B NZ  
455  N N   A GLY   B 7   ? 1.1398 1.2250 0.7057 0.1353  0.0802  -0.1333 22  GLY   B N   
456  N N   B GLY   B 7   ? 1.1397 1.2249 0.7056 0.1353  0.0802  -0.1333 22  GLY   B N   
457  N N   C GLY   B 7   ? 1.1507 1.2240 0.7104 0.1286  0.0823  -0.1265 22  GLY   B N   
458  N N   D GLY   B 7   ? 1.1506 1.2239 0.7104 0.1286  0.0823  -0.1265 22  GLY   B N   
459  C CA  A GLY   B 7   ? 1.1441 1.2134 0.7012 0.1381  0.0805  -0.1261 22  GLY   B CA  
460  C CA  B GLY   B 7   ? 1.1440 1.2132 0.7011 0.1381  0.0805  -0.1261 22  GLY   B CA  
461  C CA  C GLY   B 7   ? 1.1539 1.2137 0.7055 0.1367  0.0818  -0.1205 22  GLY   B CA  
462  C CA  D GLY   B 7   ? 1.1538 1.2136 0.7054 0.1367  0.0818  -0.1205 22  GLY   B CA  
463  C C   A GLY   B 7   ? 1.1465 1.2117 0.6985 0.1417  0.0755  -0.1248 22  GLY   B C   
464  C C   B GLY   B 7   ? 1.1463 1.2115 0.6983 0.1417  0.0755  -0.1248 22  GLY   B C   
465  C C   C GLY   B 7   ? 1.1558 1.2123 0.7023 0.1399  0.0769  -0.1195 22  GLY   B C   
466  C C   D GLY   B 7   ? 1.1557 1.2122 0.7021 0.1399  0.0768  -0.1195 22  GLY   B C   
467  O O   A GLY   B 7   ? 1.1515 1.2248 0.7068 0.1382  0.0714  -0.1291 22  GLY   B O   
468  O O   B GLY   B 7   ? 1.1514 1.2247 0.7067 0.1382  0.0714  -0.1291 22  GLY   B O   
469  O O   C GLY   B 7   ? 1.1615 1.2201 0.7077 0.1322  0.0744  -0.1207 22  GLY   B O   
470  O O   D GLY   B 7   ? 1.1614 1.2200 0.7076 0.1321  0.0744  -0.1207 22  GLY   B O   
471  N N   A GLU   B 8   ? 1.1423 1.1958 0.6861 0.1485  0.0754  -0.1188 23  GLU   B N   
472  N N   B GLU   B 8   ? 1.1419 1.1954 0.6857 0.1485  0.0754  -0.1188 23  GLU   B N   
473  N N   C GLU   B 8   ? 1.1491 1.1995 0.6903 0.1510  0.0750  -0.1172 23  GLU   B N   
474  N N   D GLU   B 8   ? 1.1487 1.1992 0.6900 0.1510  0.0750  -0.1172 23  GLU   B N   
475  C CA  A GLU   B 8   ? 1.1370 1.1843 0.6731 0.1542  0.0707  -0.1169 23  GLU   B CA  
476  C CA  B GLU   B 8   ? 1.1361 1.1834 0.6722 0.1542  0.0707  -0.1169 23  GLU   B CA  
477  C CA  C GLU   B 8   ? 1.1445 1.1906 0.6790 0.1563  0.0696  -0.1167 23  GLU   B CA  
478  C CA  D GLU   B 8   ? 1.1438 1.1899 0.6783 0.1563  0.0696  -0.1167 23  GLU   B CA  
479  C C   A GLU   B 8   ? 1.1202 1.1642 0.6523 0.1454  0.0687  -0.1157 23  GLU   B C   
480  C C   B GLU   B 8   ? 1.1183 1.1624 0.6505 0.1455  0.0687  -0.1157 23  GLU   B C   
481  C C   C GLU   B 8   ? 1.1257 1.1681 0.6560 0.1475  0.0679  -0.1153 23  GLU   B C   
482  C C   D GLU   B 8   ? 1.1242 1.1667 0.6546 0.1475  0.0679  -0.1153 23  GLU   B C   
483  O O   A GLU   B 8   ? 1.1099 1.1482 0.6382 0.1418  0.0720  -0.1104 23  GLU   B O   
484  O O   B GLU   B 8   ? 1.1088 1.1471 0.6370 0.1418  0.0720  -0.1104 23  GLU   B O   
485  O O   C GLU   B 8   ? 1.1185 1.1542 0.6437 0.1457  0.0708  -0.1094 23  GLU   B O   
486  O O   D GLU   B 8   ? 1.1176 1.1533 0.6428 0.1457  0.0708  -0.1094 23  GLU   B O   
487  C CB  A GLU   B 8   ? 1.1474 1.1854 0.6759 0.1640  0.0723  -0.1099 23  GLU   B CB  
488  C CB  B GLU   B 8   ? 1.1469 1.1849 0.6755 0.1640  0.0723  -0.1099 23  GLU   B CB  
489  C CB  C GLU   B 8   ? 1.1534 1.1907 0.6798 0.1678  0.0699  -0.1106 23  GLU   B CB  
490  C CB  D GLU   B 8   ? 1.1530 1.1903 0.6794 0.1678  0.0699  -0.1106 23  GLU   B CB  
491  C CG  A GLU   B 8   ? 1.1596 1.1928 0.6800 0.1737  0.0673  -0.1090 23  GLU   B CG  
492  C CG  B GLU   B 8   ? 1.1594 1.1926 0.6798 0.1737  0.0673  -0.1090 23  GLU   B CG  
493  C CG  C GLU   B 8   ? 1.1650 1.1984 0.6839 0.1758  0.0640  -0.1113 23  GLU   B CG  
494  C CG  D GLU   B 8   ? 1.1648 1.1982 0.6837 0.1758  0.0640  -0.1113 23  GLU   B CG  
495  C CD  A GLU   B 8   ? 1.1718 1.1989 0.6852 0.1844  0.0691  -0.1017 23  GLU   B CD  
496  C CD  B GLU   B 8   ? 1.1717 1.1987 0.6850 0.1844  0.0691  -0.1016 23  GLU   B CD  
497  C CD  C GLU   B 8   ? 1.1788 1.2065 0.6901 0.1889  0.0642  -0.1059 23  GLU   B CD  
498  C CD  D GLU   B 8   ? 1.1787 1.2063 0.6900 0.1889  0.0642  -0.1059 23  GLU   B CD  
499  O OE1 A GLU   B 8   ? 1.1701 1.1951 0.6837 0.1822  0.0740  -0.0956 23  GLU   B OE1 
500  O OE1 B GLU   B 8   ? 1.1700 1.1950 0.6836 0.1822  0.0740  -0.0956 23  GLU   B OE1 
501  O OE1 C GLU   B 8   ? 1.1712 1.1961 0.6811 0.1900  0.0690  -0.0990 23  GLU   B OE1 
502  O OE1 D GLU   B 8   ? 1.1711 1.1960 0.6811 0.1900  0.0690  -0.0990 23  GLU   B OE1 
503  O OE2 A GLU   B 8   ? 1.1918 1.2166 0.6994 0.1946  0.0653  -0.1017 23  GLU   B OE2 
504  O OE2 B GLU   B 8   ? 1.1917 1.2166 0.6993 0.1946  0.0653  -0.1017 23  GLU   B OE2 
505  O OE2 C GLU   B 8   ? 1.1984 1.2249 0.7054 0.1977  0.0592  -0.1083 23  GLU   B OE2 
506  O OE2 D GLU   B 8   ? 1.1984 1.2249 0.7053 0.1977  0.0592  -0.1083 23  GLU   B OE2 
507  N N   A THR   B 9   ? 1.1080 1.1551 0.6405 0.1420  0.0629  -0.1202 24  THR   B N   
508  N N   B THR   B 9   ? 1.1021 1.1493 0.6347 0.1423  0.0629  -0.1202 24  THR   B N   
509  N N   C THR   B 9   ? 1.1099 1.1570 0.6424 0.1419  0.0629  -0.1202 24  THR   B N   
510  N N   D THR   B 9   ? 1.1057 1.1528 0.6382 0.1420  0.0628  -0.1202 24  THR   B N   
511  C CA  A THR   B 9   ? 1.0966 1.1391 0.6245 0.1327  0.0597  -0.1196 24  THR   B CA  
512  C CA  B THR   B 9   ? 1.0886 1.1320 0.6172 0.1327  0.0595  -0.1201 24  THR   B CA  
513  C CA  C THR   B 9   ? 1.0974 1.1398 0.6252 0.1327  0.0597  -0.1195 24  THR   B CA  
514  C CA  D THR   B 9   ? 1.0907 1.1333 0.6187 0.1327  0.0596  -0.1196 24  THR   B CA  
515  C C   A THR   B 9   ? 1.0840 1.1155 0.6003 0.1394  0.0525  -0.1190 24  THR   B C   
516  C C   B THR   B 9   ? 1.0791 1.1114 0.5961 0.1391  0.0523  -0.1194 24  THR   B C   
517  C C   C THR   B 9   ? 1.0843 1.1158 0.6006 0.1394  0.0525  -0.1190 24  THR   B C   
518  C C   D THR   B 9   ? 1.0806 1.1128 0.5975 0.1391  0.0522  -0.1194 24  THR   B C   
519  O O   A THR   B 9   ? 1.0912 1.1155 0.6010 0.1332  0.0485  -0.1184 24  THR   B O   
520  O O   B THR   B 9   ? 1.0866 1.1121 0.5975 0.1324  0.0482  -0.1191 24  THR   B O   
521  O O   C THR   B 9   ? 1.0914 1.1157 0.6012 0.1332  0.0485  -0.1184 24  THR   B O   
522  O O   D THR   B 9   ? 1.0883 1.1143 0.5996 0.1322  0.0476  -0.1196 24  THR   B O   
523  C CB  A THR   B 9   ? 1.0999 1.1539 0.6366 0.1209  0.0576  -0.1246 24  THR   B CB  
524  C CB  B THR   B 9   ? 1.0873 1.1434 0.6255 0.1216  0.0576  -0.1255 24  THR   B CB  
525  C CB  C THR   B 9   ? 1.1003 1.1543 0.6370 0.1209  0.0576  -0.1246 24  THR   B CB  
526  C CB  D THR   B 9   ? 1.0889 1.1434 0.6261 0.1205  0.0583  -0.1245 24  THR   B CB  
527  O OG1 A THR   B 9   ? 1.1034 1.1699 0.6507 0.1195  0.0633  -0.1269 24  THR   B OG1 
528  O OG1 B THR   B 9   ? 1.0866 1.1513 0.6300 0.1273  0.0542  -0.1302 24  THR   B OG1 
529  O OG1 C THR   B 9   ? 1.1037 1.1702 0.6510 0.1195  0.0633  -0.1269 24  THR   B OG1 
530  O OG1 D THR   B 9   ? 1.0856 1.1513 0.6302 0.1247  0.0562  -0.1296 24  THR   B OG1 
531  C CG2 A THR   B 9   ? 1.1059 1.1554 0.6391 0.1090  0.0566  -0.1227 24  THR   B CG2 
532  C CG2 B THR   B 9   ? 1.0884 1.1542 0.6354 0.1138  0.0643  -0.1258 24  THR   B CG2 
533  C CG2 C THR   B 9   ? 1.1062 1.1558 0.6394 0.1090  0.0566  -0.1227 24  THR   B CG2 
534  C CG2 D THR   B 9   ? 1.0882 1.1494 0.6322 0.1118  0.0651  -0.1237 24  THR   B CG2 
535  N N   . THR   B 10  ? 1.0681 1.0976 0.5811 0.1520  0.0505  -0.1192 25  THR   B N   
536  C CA  . THR   B 10  ? 1.0310 1.0504 0.5324 0.1601  0.0429  -0.1197 25  THR   B CA  
537  C C   . THR   B 10  ? 0.9832 0.9899 0.4716 0.1619  0.0426  -0.1144 25  THR   B C   
538  O O   . THR   B 10  ? 0.9900 0.9963 0.4774 0.1649  0.0491  -0.1086 25  THR   B O   
539  C CB  . THR   B 10  ? 1.0323 1.0516 0.5312 0.1749  0.0422  -0.1195 25  THR   B CB  
540  O OG1 . THR   B 10  ? 1.0369 1.0679 0.5472 0.1756  0.0441  -0.1234 25  THR   B OG1 
541  C CG2 . THR   B 10  ? 1.0307 1.0418 0.5193 0.1819  0.0331  -0.1222 25  THR   B CG2 
542  N N   . ASP   B 11  ? 0.9559 0.9524 0.4343 0.1605  0.0347  -0.1161 26  ASP   B N   
543  C CA  . ASP   B 11  ? 0.9658 0.9488 0.4288 0.1656  0.0329  -0.1118 26  ASP   B CA  
544  C C   . ASP   B 11  ? 0.9667 0.9488 0.4232 0.1814  0.0365  -0.1067 26  ASP   B C   
545  O O   . ASP   B 11  ? 0.9735 0.9606 0.4334 0.1901  0.0365  -0.1079 26  ASP   B O   
546  C CB  . ASP   B 11  ? 0.9906 0.9598 0.4406 0.1660  0.0217  -0.1154 26  ASP   B CB  
547  C CG  . ASP   B 11  ? 1.0094 0.9742 0.4598 0.1502  0.0168  -0.1179 26  ASP   B CG  
548  O OD1 . ASP   B 11  ? 0.9571 0.9328 0.4203 0.1376  0.0220  -0.1180 26  ASP   B OD1 
549  O OD2 . ASP   B 11  ? 1.0552 1.0045 0.4915 0.1514  0.0069  -0.1198 26  ASP   B OD2 
550  N N   . GLY   B 12  ? 0.9368 0.9134 0.3837 0.1857  0.0390  -0.1008 27  GLY   B N   
551  C CA  . GLY   B 12  ? 0.9291 0.9053 0.3672 0.2011  0.0413  -0.0949 27  GLY   B CA  
552  C C   . GLY   B 12  ? 0.9115 0.8929 0.3511 0.1995  0.0495  -0.0870 27  GLY   B C   
553  O O   . GLY   B 12  ? 0.8997 0.8825 0.3453 0.1870  0.0524  -0.0869 27  GLY   B O   
554  N N   . VAL   B 13  ? 0.8987 0.8836 0.3328 0.2117  0.0528  -0.0800 28  VAL   B N   
555  C CA  . VAL   B 13  ? 0.8770 0.8691 0.3129 0.2108  0.0605  -0.0710 28  VAL   B CA  
556  C C   . VAL   B 13  ? 0.8744 0.8762 0.3241 0.2067  0.0670  -0.0679 28  VAL   B C   
557  O O   . VAL   B 13  ? 0.8764 0.8799 0.3298 0.2120  0.0658  -0.0704 28  VAL   B O   
558  C CB  . VAL   B 13  ? 0.8866 0.8785 0.3079 0.2258  0.0599  -0.0646 28  VAL   B CB  
559  C CG1 . VAL   B 13  ? 0.9020 0.8970 0.3192 0.2408  0.0588  -0.0628 28  VAL   B CG1 
560  C CG2 . VAL   B 13  ? 0.8744 0.8747 0.2968 0.2238  0.0669  -0.0551 28  VAL   B CG2 
561  N N   . TYR   B 14  ? 0.8518 0.8589 0.3083 0.1979  0.0732  -0.0627 29  TYR   B N   
562  C CA  . TYR   B 14  ? 0.8529 0.8662 0.3216 0.1919  0.0785  -0.0601 29  TYR   B CA  
563  C C   . TYR   B 14  ? 0.8615 0.8809 0.3304 0.1904  0.0842  -0.0495 29  TYR   B C   
564  O O   . TYR   B 14  ? 0.8689 0.8890 0.3326 0.1886  0.0852  -0.0459 29  TYR   B O   
565  C CB  . TYR   B 14  ? 0.8458 0.8588 0.3253 0.1780  0.0794  -0.0668 29  TYR   B CB  
566  C CG  . TYR   B 14  ? 0.8394 0.8506 0.3227 0.1767  0.0747  -0.0765 29  TYR   B CG  
567  C CD1 . TYR   B 14  ? 0.8489 0.8545 0.3252 0.1783  0.0684  -0.0818 29  TYR   B CD1 
568  C CD2 . TYR   B 14  ? 0.8371 0.8522 0.3306 0.1735  0.0764  -0.0802 29  TYR   B CD2 
569  C CE1 . TYR   B 14  ? 0.8581 0.8639 0.3392 0.1754  0.0639  -0.0902 29  TYR   B CE1 
570  C CE2 . TYR   B 14  ? 0.8487 0.8651 0.3466 0.1725  0.0724  -0.0887 29  TYR   B CE2 
571  C CZ  . TYR   B 14  ? 0.8600 0.8728 0.3524 0.1728  0.0662  -0.0934 29  TYR   B CZ  
572  O OH  . TYR   B 14  ? 0.8963 0.9124 0.3943 0.1703  0.0621  -0.1012 29  TYR   B OH  
573  N N   . ARG   B 15  ? 0.8697 0.8934 0.3445 0.1910  0.0875  -0.0444 30  ARG   B N   
574  C CA  . ARG   B 15  ? 0.8749 0.9049 0.3520 0.1871  0.0926  -0.0336 30  ARG   B CA  
575  C C   . ARG   B 15  ? 0.8513 0.8795 0.3376 0.1724  0.0949  -0.0363 30  ARG   B C   
576  O O   . ARG   B 15  ? 0.8377 0.8620 0.3303 0.1683  0.0939  -0.0437 30  ARG   B O   
577  C CB  . ARG   B 15  ? 0.8836 0.9172 0.3623 0.1927  0.0941  -0.0264 30  ARG   B CB  
578  C CG  . ARG   B 15  ? 0.9006 0.9373 0.3703 0.2081  0.0922  -0.0231 30  ARG   B CG  
579  C CD  . ARG   B 15  ? 0.9149 0.9549 0.3865 0.2125  0.0938  -0.0156 30  ARG   B CD  
580  N NE  . ARG   B 15  ? 0.9140 0.9557 0.3772 0.2277  0.0913  -0.0149 30  ARG   B NE  
581  C CZ  . ARG   B 15  ? 0.9235 0.9740 0.3783 0.2381  0.0924  -0.0060 30  ARG   B CZ  
582  N NH1 . ARG   B 15  ? 0.9242 0.9839 0.3787 0.2345  0.0962  0.0036  30  ARG   B NH1 
583  N NH2 . ARG   B 15  ? 0.9361 0.9873 0.3826 0.2526  0.0897  -0.0068 30  ARG   B NH2 
584  N N   . VAL   B 16  ? 0.8539 0.8860 0.3405 0.1658  0.0980  -0.0300 31  VAL   B N   
585  C CA  . VAL   B 16  ? 0.8571 0.8882 0.3518 0.1524  0.1007  -0.0300 31  VAL   B CA  
586  C C   . VAL   B 16  ? 0.8589 0.8937 0.3565 0.1504  0.1033  -0.0196 31  VAL   B C   
587  O O   . VAL   B 16  ? 0.8589 0.9013 0.3529 0.1527  0.1051  -0.0097 31  VAL   B O   
588  C CB  . VAL   B 16  ? 0.8591 0.8916 0.3519 0.1454  0.1019  -0.0297 31  VAL   B CB  
589  C CG1 . VAL   B 16  ? 0.8487 0.8798 0.3493 0.1322  0.1042  -0.0308 31  VAL   B CG1 
590  C CG2 . VAL   B 16  ? 0.8599 0.8877 0.3478 0.1475  0.0984  -0.0384 31  VAL   B CG2 
591  N N   . MET   B 17  ? 0.8865 0.9159 0.3901 0.1453  0.1031  -0.0221 32  MET   B N   
592  C CA  . MET   B 17  ? 0.9157 0.9448 0.4212 0.1431  0.1040  -0.0129 32  MET   B CA  
593  C C   . MET   B 17  ? 0.9245 0.9492 0.4352 0.1300  0.1049  -0.0131 32  MET   B C   
594  O O   . MET   B 17  ? 0.9242 0.9444 0.4380 0.1249  0.1045  -0.0232 32  MET   B O   
595  C CB  . MET   B 17  ? 0.9287 0.9517 0.4349 0.1493  0.1017  -0.0162 32  MET   B CB  
596  C CG  . MET   B 17  ? 0.9304 0.9560 0.4315 0.1628  0.1000  -0.0183 32  MET   B CG  
597  S SD  . MET   B 17  ? 0.9399 0.9769 0.4337 0.1723  0.1016  -0.0047 32  MET   B SD  
598  C CE  . MET   B 17  ? 0.9572 0.9943 0.4533 0.1685  0.1025  0.0079  32  MET   B CE  
599  N N   . THR   B 18  ? 0.9484 0.9742 0.4598 0.1249  0.1056  -0.0024 33  THR   B N   
600  C CA  . THR   B 18  ? 0.9850 1.0030 0.5001 0.1133  0.1049  -0.0021 33  THR   B CA  
601  C C   . THR   B 18  ? 1.0266 1.0373 0.5410 0.1130  0.1025  0.0045  33  THR   B C   
602  O O   . THR   B 18  ? 0.9974 1.0146 0.5095 0.1176  0.1028  0.0151  33  THR   B O   
603  C CB  . THR   B 18  ? 0.9751 0.9997 0.4913 0.1041  0.1070  0.0043  33  THR   B CB  
604  O OG1 . THR   B 18  ? 0.9735 0.9884 0.4925 0.0936  0.1055  0.0024  33  THR   B OG1 
605  C CG2 . THR   B 18  ? 0.9701 1.0065 0.4844 0.1055  0.1083  0.0192  33  THR   B CG2 
606  N N   . ARG   B 19  ? 1.0973 1.0950 0.6130 0.1073  0.1001  -0.0011 34  ARG   B N   
607  C CA  . ARG   B 19  ? 1.1643 1.1504 0.6781 0.1036  0.0965  0.0048  34  ARG   B CA  
608  C C   . ARG   B 19  ? 1.1741 1.1570 0.6887 0.0902  0.0955  0.0120  34  ARG   B C   
609  O O   . ARG   B 19  ? 1.1540 1.1247 0.6662 0.0852  0.0915  0.0168  34  ARG   B O   
610  C CB  . ARG   B 19  ? 1.2129 1.1853 0.7257 0.1074  0.0936  -0.0071 34  ARG   B CB  
611  C CG  . ARG   B 19  ? 1.2810 1.2565 0.7930 0.1202  0.0938  -0.0133 34  ARG   B CG  
612  C CD  . ARG   B 19  ? 1.3098 1.2755 0.8177 0.1267  0.0903  -0.0105 34  ARG   B CD  
613  N NE  . ARG   B 19  ? 1.3276 1.2965 0.8350 0.1391  0.0902  -0.0175 34  ARG   B NE  
614  C CZ  . ARG   B 19  ? 1.3691 1.3369 0.8784 0.1436  0.0897  -0.0309 34  ARG   B CZ  
615  N NH1 . ARG   B 19  ? 1.4174 1.3816 0.9292 0.1374  0.0897  -0.0392 34  ARG   B NH1 
616  N NH2 . ARG   B 19  ? 1.3527 1.3243 0.8615 0.1544  0.0892  -0.0359 34  ARG   B NH2 
617  N N   . ARG   B 20  ? 1.2173 1.2098 0.7345 0.0845  0.0984  0.0132  35  ARG   B N   
618  C CA  . ARG   B 20  ? 1.2827 1.2722 0.8010 0.0714  0.0973  0.0179  35  ARG   B CA  
619  C C   . ARG   B 20  ? 1.2565 1.2536 0.7747 0.0665  0.0967  0.0350  35  ARG   B C   
620  O O   . ARG   B 20  ? 1.2701 1.2628 0.7887 0.0550  0.0941  0.0414  35  ARG   B O   
621  C CB  . ARG   B 20  ? 1.3256 1.3231 0.8466 0.0681  0.1007  0.0120  35  ARG   B CB  
622  C CG  . ARG   B 20  ? 1.4194 1.4083 0.9411 0.0570  0.0991  0.0082  35  ARG   B CG  
623  C CD  . ARG   B 20  ? 1.5158 1.5149 1.0397 0.0541  0.1029  0.0047  35  ARG   B CD  
624  N NE  . ARG   B 20  ? 1.5687 1.5839 1.0927 0.0589  0.1061  0.0126  35  ARG   B NE  
625  C CZ  . ARG   B 20  ? 1.5842 1.6102 1.1088 0.0545  0.1069  0.0254  35  ARG   B CZ  
626  N NH1 . ARG   B 20  ? 1.6360 1.6584 1.1617 0.0435  0.1045  0.0324  35  ARG   B NH1 
627  N NH2 . ARG   B 20  ? 1.5609 1.6018 1.0843 0.0616  0.1098  0.0312  35  ARG   B NH2 
628  N N   . LEU   B 21  ? 1.2209 1.2299 0.7384 0.0749  0.0986  0.0424  36  LEU   B N   
629  C CA  . LEU   B 21  ? 1.1950 1.2149 0.7126 0.0714  0.0984  0.0598  36  LEU   B CA  
630  C C   . LEU   B 21  ? 1.1565 1.1677 0.6709 0.0753  0.0951  0.0650  36  LEU   B C   
631  O O   . LEU   B 21  ? 1.1160 1.1093 0.6279 0.0781  0.0919  0.0548  36  LEU   B O   
632  C CB  . LEU   B 21  ? 1.2014 1.2433 0.7194 0.0789  0.1034  0.0652  36  LEU   B CB  
633  C CG  . LEU   B 21  ? 1.2278 1.2818 0.7485 0.0712  0.1057  0.0694  36  LEU   B CG  
634  C CD1 . LEU   B 21  ? 1.2326 1.2744 0.7548 0.0638  0.1049  0.0571  36  LEU   B CD1 
635  C CD2 . LEU   B 21  ? 1.2411 1.3138 0.7600 0.0818  0.1101  0.0713  36  LEU   B CD2 
636  N N   . LEU   B 22  ? 1.1524 1.1762 0.6666 0.0752  0.0955  0.0807  37  LEU   B N   
637  C CA  . LEU   B 22  ? 1.1529 1.1715 0.6637 0.0797  0.0928  0.0876  37  LEU   B CA  
638  C C   . LEU   B 22  ? 1.1459 1.1630 0.6541 0.0955  0.0947  0.0765  37  LEU   B C   
639  O O   . LEU   B 22  ? 1.1225 1.1528 0.6315 0.1036  0.0989  0.0719  37  LEU   B O   
640  C CB  . LEU   B 22  ? 1.1378 1.1764 0.6495 0.0781  0.0944  0.1067  37  LEU   B CB  
641  C CG  . LEU   B 22  ? 1.1463 1.1786 0.6543 0.0793  0.0909  0.1164  37  LEU   B CG  
642  C CD1 . LEU   B 22  ? 1.1445 1.1574 0.6512 0.0643  0.0841  0.1218  37  LEU   B CD1 
643  C CD2 . LEU   B 22  ? 1.1576 1.2155 0.6663 0.0840  0.0944  0.1332  37  LEU   B CD2 
644  N N   . GLY   B 23  ? 1.1523 1.1530 0.6568 0.0996  0.0910  0.0721  38  GLY   B N   
645  C CA  . GLY   B 23  ? 1.1421 1.1402 0.6444 0.1141  0.0918  0.0610  38  GLY   B CA  
646  C C   . GLY   B 23  ? 1.1243 1.1268 0.6290 0.1187  0.0949  0.0469  38  GLY   B C   
647  O O   . GLY   B 23  ? 1.1313 1.1300 0.6388 0.1101  0.0950  0.0412  38  GLY   B O   
648  N N   . SER   B 24  ? 1.1063 1.1160 0.6095 0.1316  0.0969  0.0414  39  SER   B N   
649  C CA  . SER   B 24  ? 1.0700 1.0852 0.5745 0.1368  0.0993  0.0296  39  SER   B CA  
650  C C   . SER   B 24  ? 1.0401 1.0734 0.5434 0.1406  0.1029  0.0373  39  SER   B C   
651  O O   . SER   B 24  ? 1.0179 1.0598 0.5177 0.1494  0.1035  0.0451  39  SER   B O   
652  C CB  . SER   B 24  ? 1.0754 1.0857 0.5781 0.1482  0.0980  0.0189  39  SER   B CB  
653  O OG  . SER   B 24  ? 1.0820 1.0766 0.5854 0.1454  0.0948  0.0112  39  SER   B OG  
654  N N   . THR   B 25  ? 1.0048 1.0436 0.5102 0.1347  0.1049  0.0354  40  THR   B N   
655  C CA  . THR   B 25  ? 0.9948 1.0506 0.4981 0.1381  0.1080  0.0429  40  THR   B CA  
656  C C   . THR   B 25  ? 0.9832 1.0394 0.4839 0.1449  0.1086  0.0312  40  THR   B C   
657  O O   . THR   B 25  ? 0.9779 1.0252 0.4815 0.1386  0.1079  0.0206  40  THR   B O   
658  C CB  . THR   B 25  ? 0.9956 1.0577 0.5023 0.1256  0.1093  0.0517  40  THR   B CB  
659  O OG1 . THR   B 25  ? 0.9981 1.0590 0.5065 0.1187  0.1077  0.0634  40  THR   B OG1 
660  C CG2 . THR   B 25  ? 0.9857 1.0664 0.4899 0.1299  0.1125  0.0592  40  THR   B CG2 
661  N N   . GLN   B 26  ? 0.9582 1.0243 0.4530 0.1571  0.1095  0.0334  41  GLN   B N   
662  C CA  . GLN   B 26  ? 0.9477 1.0125 0.4382 0.1630  0.1090  0.0231  41  GLN   B CA  
663  C C   . GLN   B 26  ? 0.9406 1.0130 0.4305 0.1574  0.1111  0.0266  41  GLN   B C   
664  O O   . GLN   B 26  ? 0.9444 1.0310 0.4317 0.1603  0.1133  0.0385  41  GLN   B O   
665  C CB  . GLN   B 26  ? 0.9315 1.0005 0.4138 0.1792  0.1078  0.0226  41  GLN   B CB  
666  C CG  . GLN   B 26  ? 0.9287 0.9935 0.4049 0.1851  0.1057  0.0121  41  GLN   B CG  
667  C CD  . GLN   B 26  ? 0.9301 0.9954 0.3971 0.2011  0.1032  0.0098  41  GLN   B CD  
668  O OE1 . GLN   B 26  ? 0.9564 1.0186 0.4237 0.2068  0.1017  0.0084  41  GLN   B OE1 
669  N NE2 . GLN   B 26  ? 0.9225 0.9911 0.3802 0.2092  0.1023  0.0092  41  GLN   B NE2 
670  N N   . VAL   B 27  ? 0.9267 0.9914 0.4188 0.1498  0.1106  0.0170  42  VAL   B N   
671  C CA  . VAL   B 27  ? 0.9141 0.9842 0.4057 0.1435  0.1124  0.0192  42  VAL   B CA  
672  C C   . VAL   B 27  ? 0.8892 0.9589 0.3722 0.1527  0.1111  0.0131  42  VAL   B C   
673  O O   . VAL   B 27  ? 0.8874 0.9642 0.3661 0.1532  0.1124  0.0172  42  VAL   B O   
674  C CB  . VAL   B 27  ? 0.9326 0.9942 0.4312 0.1290  0.1126  0.0134  42  VAL   B CB  
675  C CG1 . VAL   B 27  ? 0.9532 1.0143 0.4581 0.1195  0.1130  0.0208  42  VAL   B CG1 
676  C CG2 . VAL   B 27  ? 0.9253 0.9746 0.4257 0.1283  0.1103  -0.0005 42  VAL   B CG2 
677  N N   . GLY   B 28  ? 0.8670 0.9281 0.3467 0.1599  0.1081  0.0039  43  GLY   B N   
678  C CA  . GLY   B 28  ? 0.8535 0.9114 0.3232 0.1693  0.1052  -0.0019 43  GLY   B CA  
679  C C   . GLY   B 28  ? 0.8519 0.8998 0.3199 0.1749  0.1012  -0.0121 43  GLY   B C   
680  O O   . GLY   B 28  ? 0.8594 0.9062 0.3324 0.1761  0.1011  -0.0122 43  GLY   B O   
681  N N   . VAL   B 29  ? 0.8483 0.8890 0.3087 0.1785  0.0974  -0.0196 44  VAL   B N   
682  C CA  . VAL   B 29  ? 0.8487 0.8803 0.3033 0.1863  0.0919  -0.0287 44  VAL   B CA  
683  C C   . VAL   B 29  ? 0.8437 0.8656 0.2974 0.1779  0.0887  -0.0380 44  VAL   B C   
684  O O   . VAL   B 29  ? 0.8439 0.8666 0.2961 0.1717  0.0904  -0.0357 44  VAL   B O   
685  C CB  . VAL   B 29  ? 0.8635 0.8969 0.3042 0.2030  0.0893  -0.0252 44  VAL   B CB  
686  C CG1 . VAL   B 29  ? 0.8728 0.8957 0.3066 0.2109  0.0827  -0.0345 44  VAL   B CG1 
687  C CG2 . VAL   B 29  ? 0.8610 0.9071 0.3019 0.2113  0.0931  -0.0141 44  VAL   B CG2 
688  N N   . GLY   B 30  ? 0.8322 0.8461 0.2866 0.1773  0.0840  -0.0475 45  GLY   B N   
689  C CA  . GLY   B 30  ? 0.8246 0.8294 0.2760 0.1706  0.0797  -0.0552 45  GLY   B CA  
690  C C   . GLY   B 30  ? 0.8304 0.8273 0.2776 0.1751  0.0728  -0.0633 45  GLY   B C   
691  O O   . GLY   B 30  ? 0.8295 0.8282 0.2764 0.1847  0.0718  -0.0632 45  GLY   B O   
692  N N   . VAL   B 31  ? 0.8176 0.8062 0.2622 0.1677  0.0682  -0.0697 46  VAL   B N   
693  C CA  . VAL   B 31  ? 0.8271 0.8067 0.2665 0.1698  0.0600  -0.0773 46  VAL   B CA  
694  C C   . VAL   B 31  ? 0.8355 0.8173 0.2873 0.1559  0.0595  -0.0838 46  VAL   B C   
695  O O   . VAL   B 31  ? 0.8144 0.7968 0.2701 0.1442  0.0616  -0.0840 46  VAL   B O   
696  C CB  . VAL   B 31  ? 0.8453 0.8115 0.2680 0.1736  0.0530  -0.0786 46  VAL   B CB  
697  C CG1 . VAL   B 31  ? 0.8634 0.8191 0.2809 0.1737  0.0435  -0.0863 46  VAL   B CG1 
698  C CG2 . VAL   B 31  ? 0.8570 0.8227 0.2662 0.1893  0.0534  -0.0723 46  VAL   B CG2 
699  N N   . MET   B 32  ? 0.8380 0.8221 0.2953 0.1577  0.0567  -0.0888 47  MET   B N   
700  C CA  . MET   B 32  ? 0.8495 0.8374 0.3174 0.1461  0.0548  -0.0955 47  MET   B CA  
701  C C   . MET   B 32  ? 0.8742 0.8519 0.3333 0.1449  0.0449  -0.1006 47  MET   B C   
702  O O   . MET   B 32  ? 0.8639 0.8361 0.3153 0.1554  0.0394  -0.1023 47  MET   B O   
703  C CB  . MET   B 32  ? 0.8568 0.8546 0.3360 0.1490  0.0575  -0.0978 47  MET   B CB  
704  C CG  . MET   B 32  ? 0.8657 0.8720 0.3576 0.1376  0.0574  -0.1038 47  MET   B CG  
705  S SD  . MET   B 32  ? 0.8741 0.8876 0.3755 0.1240  0.0651  -0.1021 47  MET   B SD  
706  C CE  . MET   B 32  ? 0.8724 0.8925 0.3812 0.1304  0.0721  -0.0991 47  MET   B CE  
707  N N   . GLN   B 33  ? 0.8785 0.8531 0.3381 0.1321  0.0422  -0.1028 48  GLN   B N   
708  C CA  . GLN   B 33  ? 0.9013 0.8640 0.3515 0.1290  0.0317  -0.1069 48  GLN   B CA  
709  C C   . GLN   B 33  ? 0.9133 0.8819 0.3733 0.1115  0.0308  -0.1098 48  GLN   B C   
710  O O   . GLN   B 33  ? 0.9096 0.8818 0.3739 0.1022  0.0361  -0.1074 48  GLN   B O   
711  C CB  . GLN   B 33  ? 0.9193 0.8649 0.3502 0.1355  0.0268  -0.1042 48  GLN   B CB  
712  C CG  . GLN   B 33  ? 0.9492 0.8799 0.3693 0.1314  0.0147  -0.1086 48  GLN   B CG  
713  C CD  . GLN   B 33  ? 0.9853 0.8958 0.3830 0.1423  0.0071  -0.1077 48  GLN   B CD  
714  O OE1 . GLN   B 33  ? 1.0287 0.9241 0.4155 0.1357  -0.0011 -0.1094 48  GLN   B OE1 
715  N NE2 . GLN   B 33  ? 0.9785 0.8885 0.3681 0.1591  0.0097  -0.1048 48  GLN   B NE2 
716  N N   . GLU   B 34  ? 0.9248 0.8964 0.3893 0.1071  0.0244  -0.1146 49  GLU   B N   
717  C CA  . GLU   B 34  ? 0.9154 0.8964 0.3907 0.0903  0.0230  -0.1171 49  GLU   B CA  
718  C C   . GLU   B 34  ? 0.8906 0.8890 0.3811 0.0840  0.0339  -0.1159 49  GLU   B C   
719  O O   . GLU   B 34  ? 0.8873 0.8909 0.3828 0.0710  0.0348  -0.1158 49  GLU   B O   
720  C CB  . GLU   B 34  ? 0.9426 0.9090 0.4065 0.0803  0.0161  -0.1159 49  GLU   B CB  
721  C CG  . GLU   B 34  ? 0.9662 0.9107 0.4109 0.0883  0.0050  -0.1167 49  GLU   B CG  
722  C CD  . GLU   B 34  ? 0.9968 0.9209 0.4245 0.0843  -0.0011 -0.1146 49  GLU   B CD  
723  O OE1 . GLU   B 34  ? 1.0020 0.9275 0.4334 0.0690  -0.0019 -0.1138 49  GLU   B OE1 
724  O OE2 . GLU   B 34  ? 1.0303 0.9363 0.4396 0.0974  -0.0057 -0.1137 49  GLU   B OE2 
725  N N   . GLY   B 35  ? 0.8662 0.8735 0.3639 0.0927  0.0411  -0.1155 50  GLY   B N   
726  C CA  . GLY   B 35  ? 0.8438 0.8672 0.3557 0.0875  0.0498  -0.1158 50  GLY   B CA  
727  C C   . GLY   B 35  ? 0.8265 0.8466 0.3362 0.0860  0.0567  -0.1110 50  GLY   B C   
728  O O   . GLY   B 35  ? 0.8080 0.8384 0.3272 0.0827  0.0635  -0.1111 50  GLY   B O   
729  N N   . VAL   B 36  ? 0.8196 0.8254 0.3161 0.0900  0.0547  -0.1072 51  VAL   B N   
730  C CA  . VAL   B 36  ? 0.8137 0.8160 0.3066 0.0890  0.0604  -0.1020 51  VAL   B CA  
731  C C   . VAL   B 36  ? 0.8008 0.7987 0.2873 0.1028  0.0629  -0.0976 51  VAL   B C   
732  O O   . VAL   B 36  ? 0.8188 0.8083 0.2953 0.1129  0.0575  -0.0975 51  VAL   B O   
733  C CB  . VAL   B 36  ? 0.8265 0.8184 0.3099 0.0809  0.0566  -0.1006 51  VAL   B CB  
734  C CG1 . VAL   B 36  ? 0.8264 0.8150 0.3051 0.0815  0.0621  -0.0951 51  VAL   B CG1 
735  C CG2 . VAL   B 36  ? 0.8286 0.8283 0.3205 0.0654  0.0558  -0.1036 51  VAL   B CG2 
736  N N   . PHE   B 37  ? 0.7822 0.7856 0.2737 0.1031  0.0703  -0.0937 52  PHE   B N   
737  C CA  . PHE   B 37  ? 0.7801 0.7818 0.2666 0.1140  0.0735  -0.0876 52  PHE   B CA  
738  C C   . PHE   B 37  ? 0.7824 0.7785 0.2599 0.1129  0.0747  -0.0823 52  PHE   B C   
739  O O   . PHE   B 37  ? 0.7767 0.7758 0.2588 0.1029  0.0784  -0.0815 52  PHE   B O   
740  C CB  . PHE   B 37  ? 0.7707 0.7813 0.2678 0.1144  0.0799  -0.0859 52  PHE   B CB  
741  C CG  . PHE   B 37  ? 0.7745 0.7843 0.2668 0.1257  0.0819  -0.0793 52  PHE   B CG  
742  C CD1 . PHE   B 37  ? 0.7878 0.7949 0.2744 0.1374  0.0781  -0.0796 52  PHE   B CD1 
743  C CD2 . PHE   B 37  ? 0.7716 0.7840 0.2646 0.1245  0.0871  -0.0724 52  PHE   B CD2 
744  C CE1 . PHE   B 37  ? 0.7896 0.7974 0.2711 0.1481  0.0799  -0.0727 52  PHE   B CE1 
745  C CE2 . PHE   B 37  ? 0.7756 0.7892 0.2642 0.1342  0.0887  -0.0651 52  PHE   B CE2 
746  C CZ  . PHE   B 37  ? 0.7826 0.7945 0.2656 0.1462  0.0854  -0.0651 52  PHE   B CZ  
747  N N   . HIS   B 38  ? 0.7910 0.7800 0.2558 0.1236  0.0716  -0.0789 53  HIS   B N   
748  C CA  . HIS   B 38  ? 0.7956 0.7794 0.2493 0.1262  0.0719  -0.0736 53  HIS   B CA  
749  C C   . HIS   B 38  ? 0.7936 0.7844 0.2462 0.1359  0.0770  -0.0657 53  HIS   B C   
750  O O   . HIS   B 38  ? 0.7956 0.7875 0.2451 0.1474  0.0758  -0.0644 53  HIS   B O   
751  C CB  . HIS   B 38  ? 0.8110 0.7814 0.2489 0.1329  0.0636  -0.0759 53  HIS   B CB  
752  C CG  . HIS   B 38  ? 0.8201 0.7833 0.2582 0.1241  0.0571  -0.0829 53  HIS   B CG  
753  N ND1 . HIS   B 38  ? 0.8276 0.7936 0.2726 0.1235  0.0542  -0.0880 53  HIS   B ND1 
754  C CD2 . HIS   B 38  ? 0.8336 0.7878 0.2662 0.1145  0.0527  -0.0850 53  HIS   B CD2 
755  C CE1 . HIS   B 38  ? 0.8344 0.7943 0.2784 0.1141  0.0480  -0.0927 53  HIS   B CE1 
756  N NE2 . HIS   B 38  ? 0.8397 0.7920 0.2763 0.1077  0.0471  -0.0908 53  HIS   B NE2 
757  N N   . THR   B 39  ? 0.7879 0.7843 0.2433 0.1312  0.0825  -0.0601 54  THR   B N   
758  C CA  . THR   B 39  ? 0.7948 0.7989 0.2480 0.1398  0.0865  -0.0512 54  THR   B CA  
759  C C   . THR   B 39  ? 0.7983 0.8035 0.2458 0.1374  0.0885  -0.0461 54  THR   B C   
760  O O   . THR   B 39  ? 0.7943 0.7923 0.2389 0.1296  0.0863  -0.0503 54  THR   B O   
761  C CB  . THR   B 39  ? 0.7865 0.7994 0.2523 0.1373  0.0914  -0.0486 54  THR   B CB  
762  O OG1 . THR   B 39  ? 0.7864 0.8072 0.2497 0.1460  0.0944  -0.0390 54  THR   B OG1 
763  C CG2 . THR   B 39  ? 0.7688 0.7845 0.2453 0.1234  0.0953  -0.0497 54  THR   B CG2 
764  N N   . MET   B 40  ? 0.8089 0.8239 0.2556 0.1430  0.0926  -0.0372 55  MET   B N   
765  C CA  . MET   B 40  ? 0.8249 0.8444 0.2680 0.1405  0.0953  -0.0313 55  MET   B CA  
766  C C   . MET   B 40  ? 0.8197 0.8454 0.2760 0.1265  0.1004  -0.0294 55  MET   B C   
767  O O   . MET   B 40  ? 0.8106 0.8406 0.2773 0.1231  0.1029  -0.0286 55  MET   B O   
768  C CB  . MET   B 40  ? 0.8605 0.8894 0.2955 0.1541  0.0965  -0.0223 55  MET   B CB  
769  C CG  . MET   B 40  ? 0.8734 0.8949 0.2948 0.1696  0.0908  -0.0253 55  MET   B CG  
770  S SD  . MET   B 40  ? 0.9634 0.9874 0.3675 0.1828  0.0894  -0.0197 55  MET   B SD  
771  C CE  . MET   B 40  ? 0.9593 0.9640 0.3526 0.1774  0.0832  -0.0284 55  MET   B CE  
772  N N   A TRP   B 41  ? 0.8211 0.8459 0.2760 0.1189  0.1015  -0.0291 56  TRP   B N   
773  N N   B TRP   B 41  ? 0.8094 0.8342 0.2644 0.1188  0.1015  -0.0291 56  TRP   B N   
774  N N   C TRP   B 41  ? 0.8211 0.8460 0.2760 0.1189  0.1015  -0.0291 56  TRP   B N   
775  N N   D TRP   B 41  ? 0.8094 0.8343 0.2645 0.1188  0.1015  -0.0291 56  TRP   B N   
776  C CA  A TRP   B 41  ? 0.8154 0.8444 0.2811 0.1053  0.1056  -0.0283 56  TRP   B CA  
777  C CA  B TRP   B 41  ? 0.7966 0.8256 0.2627 0.1052  0.1056  -0.0285 56  TRP   B CA  
778  C CA  C TRP   B 41  ? 0.8155 0.8445 0.2812 0.1053  0.1056  -0.0283 56  TRP   B CA  
779  C CA  D TRP   B 41  ? 0.7967 0.8256 0.2628 0.1052  0.1056  -0.0285 56  TRP   B CA  
780  C C   A TRP   B 41  ? 0.8098 0.8504 0.2823 0.1056  0.1097  -0.0193 56  TRP   B C   
781  C C   B TRP   B 41  ? 0.7969 0.8376 0.2696 0.1056  0.1097  -0.0193 56  TRP   B C   
782  C C   C TRP   B 41  ? 0.8099 0.8505 0.2825 0.1056  0.1097  -0.0193 56  TRP   B C   
783  C C   D TRP   B 41  ? 0.7971 0.8377 0.2698 0.1055  0.1097  -0.0193 56  TRP   B C   
784  O O   A TRP   B 41  ? 0.8034 0.8449 0.2862 0.0971  0.1117  -0.0202 56  TRP   B O   
785  O O   B TRP   B 41  ? 0.7911 0.8328 0.2741 0.0971  0.1117  -0.0200 56  TRP   B O   
786  O O   C TRP   B 41  ? 0.8036 0.8451 0.2865 0.0971  0.1117  -0.0203 56  TRP   B O   
787  O O   D TRP   B 41  ? 0.7914 0.8330 0.2744 0.0970  0.1117  -0.0201 56  TRP   B O   
788  C CB  A TRP   B 41  ? 0.8200 0.8468 0.2811 0.0990  0.1058  -0.0283 56  TRP   B CB  
789  C CB  B TRP   B 41  ? 0.7888 0.8151 0.2508 0.0982  0.1058  -0.0291 56  TRP   B CB  
790  C CB  C TRP   B 41  ? 0.8200 0.8468 0.2811 0.0990  0.1058  -0.0283 56  TRP   B CB  
791  C CB  D TRP   B 41  ? 0.7888 0.8151 0.2508 0.0982  0.1058  -0.0291 56  TRP   B CB  
792  C CG  A TRP   B 41  ? 0.8150 0.8442 0.2865 0.0851  0.1093  -0.0294 56  TRP   B CG  
793  C CG  B TRP   B 41  ? 0.7721 0.8023 0.2446 0.0850  0.1096  -0.0288 56  TRP   B CG  
794  C CG  C TRP   B 41  ? 0.8150 0.8442 0.2865 0.0851  0.1093  -0.0294 56  TRP   B CG  
795  C CG  D TRP   B 41  ? 0.7720 0.8022 0.2445 0.0850  0.1096  -0.0288 56  TRP   B CG  
796  C CD1 A TRP   B 41  ? 0.8133 0.8369 0.2900 0.0752  0.1088  -0.0371 56  TRP   B CD1 
797  C CD1 B TRP   B 41  ? 0.7654 0.8050 0.2427 0.0817  0.1133  -0.0212 56  TRP   B CD1 
798  C CD1 C TRP   B 41  ? 0.8133 0.8369 0.2899 0.0752  0.1088  -0.0371 56  TRP   B CD1 
799  C CD1 D TRP   B 41  ? 0.7652 0.8048 0.2425 0.0817  0.1133  -0.0212 56  TRP   B CD1 
800  C CD2 A TRP   B 41  ? 0.8143 0.8528 0.2923 0.0799  0.1133  -0.0224 56  TRP   B CD2 
801  C CD2 B TRP   B 41  ? 0.7637 0.7893 0.2433 0.0739  0.1099  -0.0363 56  TRP   B CD2 
802  C CD2 C TRP   B 41  ? 0.8142 0.8527 0.2922 0.0799  0.1133  -0.0224 56  TRP   B CD2 
803  C CD2 D TRP   B 41  ? 0.7636 0.7891 0.2431 0.0739  0.1099  -0.0364 56  TRP   B CD2 
804  N NE1 A TRP   B 41  ? 0.8091 0.8372 0.2941 0.0653  0.1124  -0.0360 56  TRP   B NE1 
805  N NE1 B TRP   B 41  ? 0.7510 0.7899 0.2367 0.0696  0.1153  -0.0240 56  TRP   B NE1 
806  N NE1 C TRP   B 41  ? 0.8091 0.8372 0.2941 0.0654  0.1124  -0.0360 56  TRP   B NE1 
807  N NE1 D TRP   B 41  ? 0.7509 0.7898 0.2366 0.0696  0.1153  -0.0240 56  TRP   B NE1 
808  C CE2 A TRP   B 41  ? 0.8090 0.8450 0.2948 0.0676  0.1148  -0.0272 56  TRP   B CE2 
809  C CE2 B TRP   B 41  ? 0.7542 0.7852 0.2414 0.0652  0.1136  -0.0333 56  TRP   B CE2 
810  C CE2 C TRP   B 41  ? 0.8090 0.8450 0.2948 0.0676  0.1148  -0.0272 56  TRP   B CE2 
811  C CE2 D TRP   B 41  ? 0.7540 0.7850 0.2412 0.0651  0.1136  -0.0334 56  TRP   B CE2 
812  C CE3 A TRP   B 41  ? 0.8189 0.8683 0.2968 0.0843  0.1154  -0.0123 56  TRP   B CE3 
813  C CE3 B TRP   B 41  ? 0.7638 0.7822 0.2439 0.0704  0.1071  -0.0449 56  TRP   B CE3 
814  C CE3 C TRP   B 41  ? 0.8189 0.8683 0.2967 0.0843  0.1154  -0.0123 56  TRP   B CE3 
815  C CE3 D TRP   B 41  ? 0.7636 0.7820 0.2437 0.0703  0.1071  -0.0449 56  TRP   B CE3 
816  C CZ2 A TRP   B 41  ? 0.8117 0.8533 0.3040 0.0597  0.1177  -0.0227 56  TRP   B CZ2 
817  C CZ2 B TRP   B 41  ? 0.7517 0.7807 0.2459 0.0545  0.1148  -0.0392 56  TRP   B CZ2 
818  C CZ2 C TRP   B 41  ? 0.8118 0.8534 0.3041 0.0597  0.1177  -0.0227 56  TRP   B CZ2 
819  C CZ2 D TRP   B 41  ? 0.7514 0.7805 0.2456 0.0544  0.1148  -0.0392 56  TRP   B CZ2 
820  C CZ3 A TRP   B 41  ? 0.8142 0.8701 0.2995 0.0752  0.1183  -0.0072 56  TRP   B CZ3 
821  C CZ3 B TRP   B 41  ? 0.7602 0.7790 0.2483 0.0592  0.1088  -0.0500 56  TRP   B CZ3 
822  C CZ3 C TRP   B 41  ? 0.8141 0.8701 0.2995 0.0752  0.1183  -0.0072 56  TRP   B CZ3 
823  C CZ3 D TRP   B 41  ? 0.7599 0.7787 0.2480 0.0592  0.1088  -0.0500 56  TRP   B CZ3 
824  C CH2 A TRP   B 41  ? 0.8118 0.8627 0.3038 0.0632  0.1191  -0.0127 56  TRP   B CH2 
825  C CH2 B TRP   B 41  ? 0.7527 0.7766 0.2473 0.0520  0.1127  -0.0474 56  TRP   B CH2 
826  C CH2 C TRP   B 41  ? 0.8119 0.8628 0.3039 0.0632  0.1191  -0.0127 56  TRP   B CH2 
827  C CH2 D TRP   B 41  ? 0.7522 0.7760 0.2468 0.0520  0.1127  -0.0474 56  TRP   B CH2 
828  N N   A HIS   B 42  ? 0.8113 0.8608 0.2778 0.1151  0.1105  -0.0106 57  HIS   B N   
829  N N   B HIS   B 42  ? 0.8066 0.8560 0.2731 0.1151  0.1105  -0.0106 57  HIS   B N   
830  N N   C HIS   B 42  ? 0.8117 0.8611 0.2784 0.1148  0.1105  -0.0106 57  HIS   B N   
831  N N   D HIS   B 42  ? 0.8069 0.8564 0.2737 0.1148  0.1105  -0.0107 57  HIS   B N   
832  C CA  A HIS   B 42  ? 0.8126 0.8753 0.2853 0.1138  0.1141  0.0000  57  HIS   B CA  
833  C CA  B HIS   B 42  ? 0.8104 0.8731 0.2831 0.1138  0.1141  0.0000  57  HIS   B CA  
834  C CA  C HIS   B 42  ? 0.8124 0.8748 0.2856 0.1130  0.1142  -0.0002 57  HIS   B CA  
835  C CA  D HIS   B 42  ? 0.8102 0.8726 0.2834 0.1130  0.1142  -0.0002 57  HIS   B CA  
836  C C   A HIS   B 42  ? 0.8158 0.8792 0.2951 0.1156  0.1143  0.0011  57  HIS   B C   
837  C C   B HIS   B 42  ? 0.8149 0.8783 0.2942 0.1156  0.1143  0.0011  57  HIS   B C   
838  C C   C HIS   B 42  ? 0.8154 0.8780 0.2955 0.1143  0.1143  0.0004  57  HIS   B C   
839  C C   D HIS   B 42  ? 0.8145 0.8771 0.2946 0.1143  0.1143  0.0004  57  HIS   B C   
840  O O   A HIS   B 42  ? 0.8193 0.8918 0.3044 0.1124  0.1166  0.0101  57  HIS   B O   
841  O O   B HIS   B 42  ? 0.8189 0.8913 0.3040 0.1125  0.1166  0.0101  57  HIS   B O   
842  O O   C HIS   B 42  ? 0.8181 0.8878 0.3054 0.1089  0.1166  0.0079  57  HIS   B O   
843  O O   D HIS   B 42  ? 0.8177 0.8874 0.3049 0.1089  0.1166  0.0079  57  HIS   B O   
844  C CB  A HIS   B 42  ? 0.8172 0.8921 0.2815 0.1241  0.1150  0.0095  57  HIS   B CB  
845  C CB  B HIS   B 42  ? 0.8161 0.8910 0.2804 0.1241  0.1150  0.0094  57  HIS   B CB  
846  C CB  C HIS   B 42  ? 0.8164 0.8912 0.2815 0.1231  0.1151  0.0094  57  HIS   B CB  
847  C CB  D HIS   B 42  ? 0.8153 0.8901 0.2804 0.1231  0.1151  0.0094  57  HIS   B CB  
848  C CG  A HIS   B 42  ? 0.8248 0.9023 0.2815 0.1394  0.1133  0.0115  57  HIS   B CG  
849  C CG  B HIS   B 42  ? 0.8242 0.9017 0.2809 0.1394  0.1133  0.0114  57  HIS   B CG  
850  C CG  C HIS   B 42  ? 0.8235 0.9015 0.2814 0.1383  0.1136  0.0118  57  HIS   B CG  
851  C CG  D HIS   B 42  ? 0.8229 0.9009 0.2808 0.1383  0.1136  0.0118  57  HIS   B CG  
852  N ND1 A HIS   B 42  ? 0.8338 0.9058 0.2768 0.1515  0.1099  0.0078  57  HIS   B ND1 
853  N ND1 B HIS   B 42  ? 0.8335 0.9055 0.2765 0.1515  0.1099  0.0078  57  HIS   B ND1 
854  N ND1 C HIS   B 42  ? 0.8325 0.9069 0.2764 0.1510  0.1105  0.0094  57  HIS   B ND1 
855  N ND1 D HIS   B 42  ? 0.8322 0.9066 0.2761 0.1510  0.1105  0.0094  57  HIS   B ND1 
856  C CD2 A HIS   B 42  ? 0.8252 0.9095 0.2851 0.1450  0.1142  0.0167  57  HIS   B CD2 
857  C CD2 B HIS   B 42  ? 0.8249 0.9092 0.2848 0.1450  0.1142  0.0167  57  HIS   B CD2 
858  C CD2 C HIS   B 42  ? 0.8242 0.9079 0.2855 0.1434  0.1143  0.0164  57  HIS   B CD2 
859  C CD2 D HIS   B 42  ? 0.8239 0.9076 0.2852 0.1434  0.1143  0.0164  57  HIS   B CD2 
860  C CE1 A HIS   B 42  ? 0.8389 0.9148 0.2770 0.1644  0.1088  0.0105  57  HIS   B CE1 
861  C CE1 B HIS   B 42  ? 0.8387 0.9146 0.2768 0.1644  0.1088  0.0105  57  HIS   B CE1 
862  C CE1 C HIS   B 42  ? 0.8370 0.9156 0.2764 0.1637  0.1096  0.0122  57  HIS   B CE1 
863  C CE1 D HIS   B 42  ? 0.8368 0.9154 0.2762 0.1637  0.1096  0.0123  57  HIS   B CE1 
864  N NE2 A HIS   B 42  ? 0.8331 0.9170 0.2817 0.1605  0.1117  0.0161  57  HIS   B NE2 
865  N NE2 B HIS   B 42  ? 0.8328 0.9168 0.2815 0.1605  0.1117  0.0161  57  HIS   B NE2 
866  N NE2 C HIS   B 42  ? 0.8310 0.9157 0.2812 0.1590  0.1121  0.0167  57  HIS   B NE2 
867  N NE2 D HIS   B 42  ? 0.8308 0.9155 0.2810 0.1590  0.1121  0.0167  57  HIS   B NE2 
868  N N   . VAL   B 43  ? 0.8160 0.8705 0.2938 0.1206  0.1115  -0.0067 58  VAL   B N   
869  C CA  . VAL   B 43  ? 0.8181 0.8715 0.3016 0.1228  0.1112  -0.0072 58  VAL   B CA  
870  C C   . VAL   B 43  ? 0.8154 0.8631 0.3091 0.1104  0.1120  -0.0121 58  VAL   B C   
871  O O   . VAL   B 43  ? 0.8251 0.8751 0.3242 0.1083  0.1130  -0.0071 58  VAL   B O   
872  C CB  . VAL   B 43  ? 0.8264 0.8728 0.3038 0.1331  0.1075  -0.0142 58  VAL   B CB  
873  C CG1 . VAL   B 43  ? 0.8340 0.8776 0.3172 0.1349  0.1067  -0.0170 58  VAL   B CG1 
874  C CG2 . VAL   B 43  ? 0.8372 0.8887 0.3031 0.1473  0.1062  -0.0090 58  VAL   B CG2 
875  N N   . THR   B 44  ? 0.8022 0.8427 0.2976 0.1034  0.1111  -0.0215 59  THR   B N   
876  C CA  . THR   B 44  ? 0.7994 0.8349 0.3033 0.0936  0.1116  -0.0279 59  THR   B CA  
877  C C   . THR   B 44  ? 0.8049 0.8416 0.3119 0.0822  0.1138  -0.0262 59  THR   B C   
878  O O   . THR   B 44  ? 0.8014 0.8350 0.3149 0.0747  0.1144  -0.0287 59  THR   B O   
879  C CB  . THR   B 44  ? 0.7928 0.8222 0.2974 0.0937  0.1092  -0.0391 59  THR   B CB  
880  O OG1 . THR   B 44  ? 0.7770 0.8043 0.2770 0.0905  0.1082  -0.0426 59  THR   B OG1 
881  C CG2 . THR   B 44  ? 0.8029 0.8309 0.3041 0.1049  0.1064  -0.0408 59  THR   B CG2 
882  N N   . LYS   B 45  ? 0.8164 0.8568 0.3183 0.0818  0.1146  -0.0224 60  LYS   B N   
883  C CA  . LYS   B 45  ? 0.8401 0.8808 0.3432 0.0716  0.1161  -0.0229 60  LYS   B CA  
884  C C   . LYS   B 45  ? 0.8328 0.8668 0.3395 0.0644  0.1156  -0.0335 60  LYS   B C   
885  O O   . LYS   B 45  ? 0.8316 0.8654 0.3423 0.0548  0.1172  -0.0346 60  LYS   B O   
886  C CB  . LYS   B 45  ? 0.8627 0.9073 0.3712 0.0644  0.1180  -0.0160 60  LYS   B CB  
887  C CG  . LYS   B 45  ? 0.8915 0.9433 0.4000 0.0696  0.1183  -0.0054 60  LYS   B CG  
888  C CD  . LYS   B 45  ? 0.9128 0.9754 0.4170 0.0721  0.1196  0.0039  60  LYS   B CD  
889  C CE  . LYS   B 45  ? 0.9344 1.0065 0.4415 0.0728  0.1202  0.0158  60  LYS   B CE  
890  N NZ  . LYS   B 45  ? 0.9507 1.0333 0.4515 0.0853  0.1207  0.0228  60  LYS   B NZ  
891  N N   . GLY   B 46  ? 0.8210 0.8509 0.3266 0.0683  0.1134  -0.0407 61  GLY   B N   
892  C CA  . GLY   B 46  ? 0.8272 0.8540 0.3366 0.0614  0.1129  -0.0499 61  GLY   B CA  
893  C C   . GLY   B 46  ? 0.8394 0.8660 0.3567 0.0591  0.1136  -0.0544 61  GLY   B C   
894  O O   . GLY   B 46  ? 0.8301 0.8567 0.3509 0.0545  0.1134  -0.0619 61  GLY   B O   
895  N N   . ALA   B 47  ? 0.8642 0.8906 0.3837 0.0628  0.1139  -0.0501 62  ALA   B N   
896  C CA  . ALA   B 47  ? 0.8687 0.8926 0.3937 0.0626  0.1135  -0.0548 62  ALA   B CA  
897  C C   . ALA   B 47  ? 0.8631 0.8872 0.3895 0.0683  0.1115  -0.0623 62  ALA   B C   
898  O O   . ALA   B 47  ? 0.8642 0.8889 0.3868 0.0743  0.1098  -0.0618 62  ALA   B O   
899  C CB  . ALA   B 47  ? 0.8765 0.8985 0.4017 0.0658  0.1132  -0.0475 62  ALA   B CB  
900  N N   . ALA   B 48  ? 0.8646 0.8882 0.3958 0.0671  0.1114  -0.0690 63  ALA   B N   
901  C CA  . ALA   B 48  ? 0.8725 0.8980 0.4066 0.0725  0.1095  -0.0761 63  ALA   B CA  
902  C C   . ALA   B 48  ? 0.8811 0.9037 0.4134 0.0822  0.1078  -0.0725 63  ALA   B C   
903  O O   . ALA   B 48  ? 0.8971 0.9163 0.4273 0.0832  0.1084  -0.0648 63  ALA   B O   
904  C CB  . ALA   B 48  ? 0.8776 0.9046 0.4165 0.0695  0.1102  -0.0833 63  ALA   B CB  
905  N N   . LEU   B 49  ? 0.8892 0.9138 0.4224 0.0886  0.1056  -0.0775 64  LEU   B N   
906  C CA  . LEU   B 49  ? 0.9077 0.9301 0.4388 0.0988  0.1037  -0.0751 64  LEU   B CA  
907  C C   . LEU   B 49  ? 0.9338 0.9577 0.4692 0.1031  0.1021  -0.0828 64  LEU   B C   
908  O O   . LEU   B 49  ? 0.9482 0.9778 0.4878 0.0995  0.1019  -0.0904 64  LEU   B O   
909  C CB  . LEU   B 49  ? 0.8962 0.9197 0.4222 0.1042  0.1015  -0.0734 64  LEU   B CB  
910  C CG  . LEU   B 49  ? 0.8948 0.9177 0.4150 0.1022  0.1026  -0.0664 64  LEU   B CG  
911  C CD1 . LEU   B 49  ? 0.8868 0.9088 0.4003 0.1082  0.0994  -0.0670 64  LEU   B CD1 
912  C CD2 . LEU   B 49  ? 0.9098 0.9321 0.4280 0.1044  0.1046  -0.0566 64  LEU   B CD2 
913  N N   . ARG   B 50  ? 0.9702 0.9900 0.5043 0.1106  0.1011  -0.0804 65  ARG   B N   
914  C CA  . ARG   B 50  ? 1.0072 1.0279 0.5439 0.1173  0.0991  -0.0869 65  ARG   B CA  
915  C C   . ARG   B 50  ? 1.0248 1.0477 0.5594 0.1258  0.0965  -0.0872 65  ARG   B C   
916  O O   . ARG   B 50  ? 0.9920 1.0124 0.5214 0.1294  0.0963  -0.0799 65  ARG   B O   
917  C CB  . ARG   B 50  ? 1.0778 1.0901 0.6130 0.1196  0.0991  -0.0835 65  ARG   B CB  
918  C CG  . ARG   B 50  ? 1.1450 1.1560 0.6813 0.1275  0.0969  -0.0896 65  ARG   B CG  
919  C CD  . ARG   B 50  ? 1.1822 1.1823 0.7157 0.1277  0.0962  -0.0877 65  ARG   B CD  
920  N NE  . ARG   B 50  ? 1.2045 1.1966 0.7336 0.1259  0.0962  -0.0765 65  ARG   B NE  
921  C CZ  . ARG   B 50  ? 1.2208 1.2096 0.7465 0.1325  0.0948  -0.0699 65  ARG   B CZ  
922  N NH1 . ARG   B 50  ? 1.2108 1.2026 0.7364 0.1421  0.0933  -0.0735 65  ARG   B NH1 
923  N NH2 . ARG   B 50  ? 1.2498 1.2334 0.7722 0.1292  0.0950  -0.0590 65  ARG   B NH2 
924  N N   . SER   B 51  ? 1.0411 1.0697 0.5792 0.1291  0.0943  -0.0951 66  SER   B N   
925  C CA  . SER   B 51  ? 1.0995 1.1292 0.6357 0.1386  0.0910  -0.0965 66  SER   B CA  
926  C C   . SER   B 51  ? 1.1382 1.1705 0.6782 0.1448  0.0896  -0.1028 66  SER   B C   
927  O O   . SER   B 51  ? 1.1413 1.1826 0.6867 0.1430  0.0885  -0.1105 66  SER   B O   
928  C CB  . SER   B 51  ? 1.0891 1.1235 0.6250 0.1361  0.0884  -0.0997 66  SER   B CB  
929  O OG  . SER   B 51  ? 1.0762 1.1121 0.6111 0.1446  0.0845  -0.1028 66  SER   B OG  
930  N N   . GLY   B 52  ? 1.1830 1.2084 0.7201 0.1518  0.0895  -0.0993 67  GLY   B N   
931  C CA  . GLY   B 52  ? 1.2035 1.2287 0.7427 0.1577  0.0883  -0.1049 67  GLY   B CA  
932  C C   . GLY   B 52  ? 1.2259 1.2521 0.7683 0.1512  0.0903  -0.1092 67  GLY   B C   
933  O O   . GLY   B 52  ? 1.2695 1.2886 0.8096 0.1451  0.0923  -0.1042 67  GLY   B O   
934  N N   . GLU   B 53  ? 1.2492 1.2853 0.7967 0.1523  0.0897  -0.1181 68  GLU   B N   
935  C CA  . GLU   B 53  ? 1.2762 1.3156 0.8265 0.1470  0.0917  -0.1229 68  GLU   B CA  
936  C C   . GLU   B 53  ? 1.2358 1.2848 0.7905 0.1361  0.0938  -0.1238 68  GLU   B C   
937  O O   . GLU   B 53  ? 1.2569 1.3081 0.8130 0.1306  0.0959  -0.1262 68  GLU   B O   
938  C CB  . GLU   B 53  ? 1.3221 1.3690 0.8749 0.1549  0.0903  -0.1315 68  GLU   B CB  
939  C CG  . GLU   B 53  ? 1.3918 1.4246 0.9381 0.1633  0.0886  -0.1309 68  GLU   B CG  
940  C CD  . GLU   B 53  ? 1.4504 1.4702 0.9917 0.1582  0.0897  -0.1283 68  GLU   B CD  
941  O OE1 . GLU   B 53  ? 1.4809 1.5071 1.0248 0.1523  0.0917  -0.1323 68  GLU   B OE1 
942  O OE2 . GLU   B 53  ? 1.4604 1.4639 0.9950 0.1599  0.0881  -0.1218 68  GLU   B OE2 
943  N N   . GLY   B 54  ? 1.2081 1.2610 0.7635 0.1334  0.0928  -0.1216 69  GLY   B N   
944  C CA  . GLY   B 54  ? 1.1702 1.2300 0.7283 0.1229  0.0938  -0.1217 69  GLY   B CA  
945  C C   . GLY   B 54  ? 1.1286 1.1801 0.6832 0.1154  0.0967  -0.1156 69  GLY   B C   
946  O O   . GLY   B 54  ? 1.1031 1.1433 0.6526 0.1184  0.0971  -0.1094 69  GLY   B O   
947  N N   . ARG   B 55  ? 1.0682 1.1258 0.6253 0.1056  0.0984  -0.1169 70  ARG   B N   
948  C CA  . ARG   B 55  ? 1.0429 1.0942 0.5967 0.0975  0.1009  -0.1113 70  ARG   B CA  
949  C C   . ARG   B 55  ? 1.0020 1.0552 0.5543 0.0918  0.0996  -0.1093 70  ARG   B C   
950  O O   . ARG   B 55  ? 0.9958 1.0580 0.5517 0.0888  0.0978  -0.1138 70  ARG   B O   
951  C CB  . ARG   B 55  ? 1.0785 1.1330 0.6348 0.0914  0.1038  -0.1143 70  ARG   B CB  
952  C CG  . ARG   B 55  ? 1.1068 1.1527 0.6592 0.0851  0.1060  -0.1082 70  ARG   B CG  
953  C CD  . ARG   B 55  ? 1.1417 1.1905 0.6957 0.0791  0.1085  -0.1118 70  ARG   B CD  
954  N NE  . ARG   B 55  ? 1.1639 1.2068 0.7148 0.0715  0.1103  -0.1063 70  ARG   B NE  
955  C CZ  . ARG   B 55  ? 1.2184 1.2536 0.7666 0.0693  0.1112  -0.1044 70  ARG   B CZ  
956  N NH1 . ARG   B 55  ? 1.2448 1.2753 0.7920 0.0743  0.1101  -0.1079 70  ARG   B NH1 
957  N NH2 . ARG   B 55  ? 1.2339 1.2655 0.7797 0.0619  0.1127  -0.0991 70  ARG   B NH2 
958  N N   . LEU   B 56  ? 0.9386 0.9834 0.4849 0.0908  0.1000  -0.1023 71  LEU   B N   
959  C CA  . LEU   B 56  ? 0.9131 0.9569 0.4555 0.0859  0.0984  -0.1003 71  LEU   B CA  
960  C C   . LEU   B 56  ? 0.8808 0.9229 0.4220 0.0771  0.1017  -0.0971 71  LEU   B C   
961  O O   . LEU   B 56  ? 0.8711 0.9076 0.4097 0.0783  0.1039  -0.0916 71  LEU   B O   
962  C CB  . LEU   B 56  ? 0.9035 0.9397 0.4383 0.0937  0.0959  -0.0950 71  LEU   B CB  
963  C CG  . LEU   B 56  ? 0.9257 0.9620 0.4597 0.1034  0.0921  -0.0973 71  LEU   B CG  
964  C CD1 . LEU   B 56  ? 0.9177 0.9472 0.4424 0.1088  0.0889  -0.0932 71  LEU   B CD1 
965  C CD2 . LEU   B 56  ? 0.9325 0.9772 0.4724 0.1011  0.0893  -0.1051 71  LEU   B CD2 
966  N N   . ASP   B 57  ? 0.8636 0.9108 0.4066 0.0682  0.1019  -0.0998 72  ASP   B N   
967  C CA  . ASP   B 57  ? 0.8539 0.8996 0.3952 0.0596  0.1048  -0.0970 72  ASP   B CA  
968  C C   . ASP   B 57  ? 0.8261 0.8656 0.3598 0.0573  0.1029  -0.0927 72  ASP   B C   
969  O O   . ASP   B 57  ? 0.8218 0.8607 0.3530 0.0571  0.0988  -0.0945 72  ASP   B O   
970  C CB  . ASP   B 57  ? 0.8800 0.9354 0.4274 0.0516  0.1067  -0.1023 72  ASP   B CB  
971  C CG  . ASP   B 57  ? 0.9117 0.9717 0.4644 0.0554  0.1088  -0.1065 72  ASP   B CG  
972  O OD1 . ASP   B 57  ? 0.9368 0.9892 0.4874 0.0597  0.1099  -0.1035 72  ASP   B OD1 
973  O OD2 . ASP   B 57  ? 0.9332 1.0041 0.4916 0.0546  0.1087  -0.1123 72  ASP   B OD2 
974  N N   . PRO   B 58  ? 0.7999 0.8344 0.3290 0.0554  0.1051  -0.0869 73  PRO   B N   
975  C CA  . PRO   B 58  ? 0.7941 0.8230 0.3150 0.0537  0.1033  -0.0830 73  PRO   B CA  
976  C C   . PRO   B 58  ? 0.7812 0.8123 0.3025 0.0442  0.1017  -0.0870 73  PRO   B C   
977  O O   . PRO   B 58  ? 0.7801 0.8192 0.3086 0.0378  0.1038  -0.0911 73  PRO   B O   
978  C CB  . PRO   B 58  ? 0.7929 0.8201 0.3117 0.0517  0.1070  -0.0770 73  PRO   B CB  
979  C CG  . PRO   B 58  ? 0.7918 0.8238 0.3186 0.0474  0.1103  -0.0798 73  PRO   B CG  
980  C CD  . PRO   B 58  ? 0.7991 0.8334 0.3306 0.0539  0.1089  -0.0840 73  PRO   B CD  
981  N N   . TYR   B 59  ? 0.7739 0.7981 0.2870 0.0440  0.0974  -0.0859 74  TYR   B N   
982  C CA  . TYR   B 59  ? 0.7758 0.8003 0.2879 0.0347  0.0943  -0.0889 74  TYR   B CA  
983  C C   . TYR   B 59  ? 0.7708 0.7858 0.2723 0.0316  0.0929  -0.0848 74  TYR   B C   
984  O O   . TYR   B 59  ? 0.7746 0.7908 0.2762 0.0217  0.0929  -0.0854 74  TYR   B O   
985  C CB  . TYR   B 59  ? 0.7798 0.8028 0.2908 0.0371  0.0881  -0.0923 74  TYR   B CB  
986  C CG  . TYR   B 59  ? 0.7793 0.8036 0.2903 0.0261  0.0842  -0.0946 74  TYR   B CG  
987  C CD1 . TYR   B 59  ? 0.7926 0.8044 0.2920 0.0227  0.0794  -0.0922 74  TYR   B CD1 
988  C CD2 . TYR   B 59  ? 0.7823 0.8207 0.3043 0.0192  0.0848  -0.0990 74  TYR   B CD2 
989  C CE1 . TYR   B 59  ? 0.8040 0.8156 0.3025 0.0115  0.0748  -0.0935 74  TYR   B CE1 
990  C CE2 . TYR   B 59  ? 0.7978 0.8394 0.3202 0.0079  0.0809  -0.1000 74  TYR   B CE2 
991  C CZ  . TYR   B 59  ? 0.8048 0.8321 0.3154 0.0034  0.0755  -0.0970 74  TYR   B CZ  
992  O OH  . TYR   B 59  ? 0.8155 0.8429 0.3247 -0.0085 0.0705  -0.0970 74  TYR   B OH  
993  N N   . TRP   B 60  ? 0.7615 0.7676 0.2535 0.0407  0.0910  -0.0808 75  TRP   B N   
994  C CA  . TRP   B 60  ? 0.7684 0.7646 0.2480 0.0411  0.0890  -0.0767 75  TRP   B CA  
995  C C   . TRP   B 60  ? 0.7671 0.7624 0.2420 0.0518  0.0913  -0.0711 75  TRP   B C   
996  O O   . TRP   B 60  ? 0.7718 0.7678 0.2467 0.0621  0.0904  -0.0705 75  TRP   B O   
997  C CB  . TRP   B 60  ? 0.7816 0.7658 0.2502 0.0421  0.0809  -0.0785 75  TRP   B CB  
998  C CG  . TRP   B 60  ? 0.7910 0.7633 0.2446 0.0459  0.0782  -0.0745 75  TRP   B CG  
999  C CD1 . TRP   B 60  ? 0.7941 0.7622 0.2429 0.0375  0.0783  -0.0730 75  TRP   B CD1 
1000 C CD2 . TRP   B 60  ? 0.7980 0.7629 0.2397 0.0597  0.0759  -0.0710 75  TRP   B CD2 
1001 N NE1 . TRP   B 60  ? 0.8036 0.7609 0.2375 0.0456  0.0756  -0.0693 75  TRP   B NE1 
1002 C CE2 . TRP   B 60  ? 0.8059 0.7620 0.2353 0.0595  0.0743  -0.0680 75  TRP   B CE2 
1003 C CE3 . TRP   B 60  ? 0.7995 0.7647 0.2387 0.0729  0.0748  -0.0701 75  TRP   B CE3 
1004 C CZ2 . TRP   B 60  ? 0.8153 0.7639 0.2301 0.0725  0.0717  -0.0644 75  TRP   B CZ2 
1005 C CZ3 . TRP   B 60  ? 0.8080 0.7668 0.2335 0.0854  0.0727  -0.0661 75  TRP   B CZ3 
1006 C CH2 . TRP   B 60  ? 0.8162 0.7668 0.2294 0.0856  0.0709  -0.0635 75  TRP   B CH2 
1007 N N   . GLY   B 61  ? 0.7672 0.7610 0.2368 0.0506  0.0935  -0.0666 76  GLY   B N   
1008 C CA  . GLY   B 61  ? 0.7720 0.7660 0.2352 0.0611  0.0948  -0.0602 76  GLY   B CA  
1009 C C   . GLY   B 61  ? 0.7785 0.7702 0.2337 0.0597  0.0957  -0.0558 76  GLY   B C   
1010 O O   . GLY   B 61  ? 0.7912 0.7821 0.2481 0.0490  0.0966  -0.0575 76  GLY   B O   
1011 N N   . ASP   B 62  ? 0.7931 0.7857 0.2406 0.0705  0.0958  -0.0500 77  ASP   B N   
1012 C CA  . ASP   B 62  ? 0.8152 0.8060 0.2524 0.0728  0.0959  -0.0452 77  ASP   B CA  
1013 C C   . ASP   B 62  ? 0.8061 0.8070 0.2425 0.0833  0.0989  -0.0376 77  ASP   B C   
1014 O O   . ASP   B 62  ? 0.8179 0.8169 0.2469 0.0957  0.0960  -0.0365 77  ASP   B O   
1015 C CB  . ASP   B 62  ? 0.8506 0.8262 0.2717 0.0772  0.0888  -0.0479 77  ASP   B CB  
1016 C CG  . ASP   B 62  ? 0.8856 0.8571 0.2954 0.0779  0.0882  -0.0445 77  ASP   B CG  
1017 O OD1 . ASP   B 62  ? 0.9234 0.8988 0.3256 0.0887  0.0888  -0.0391 77  ASP   B OD1 
1018 O OD2 . ASP   B 62  ? 0.9464 0.9117 0.3552 0.0675  0.0871  -0.0471 77  ASP   B OD2 
1019 N N   . VAL   B 63  ? 0.7989 0.8102 0.2415 0.0787  0.1039  -0.0322 78  VAL   B N   
1020 C CA  . VAL   B 63  ? 0.7923 0.8164 0.2355 0.0865  0.1070  -0.0233 78  VAL   B CA  
1021 C C   . VAL   B 63  ? 0.8093 0.8317 0.2366 0.0995  0.1041  -0.0197 78  VAL   B C   
1022 O O   . VAL   B 63  ? 0.8242 0.8552 0.2485 0.1110  0.1047  -0.0139 78  VAL   B O   
1023 C CB  . VAL   B 63  ? 0.7812 0.8157 0.2334 0.0770  0.1119  -0.0183 78  VAL   B CB  
1024 C CG1 . VAL   B 63  ? 0.7894 0.8374 0.2392 0.0846  0.1140  -0.0082 78  VAL   B CG1 
1025 C CG2 . VAL   B 63  ? 0.7740 0.8112 0.2404 0.0681  0.1144  -0.0204 78  VAL   B CG2 
1026 N N   . LYS   B 64  ? 0.8261 0.8368 0.2420 0.0992  0.1003  -0.0233 79  LYS   B N   
1027 C CA  . LYS   B 64  ? 0.8450 0.8540 0.2441 0.1133  0.0974  -0.0196 79  LYS   B CA  
1028 C C   . LYS   B 64  ? 0.8500 0.8493 0.2379 0.1265  0.0917  -0.0228 79  LYS   B C   
1029 O O   . LYS   B 64  ? 0.8472 0.8528 0.2262 0.1415  0.0912  -0.0178 79  LYS   B O   
1030 C CB  . LYS   B 64  ? 0.8632 0.8623 0.2517 0.1096  0.0949  -0.0213 79  LYS   B CB  
1031 C CG  . LYS   B 64  ? 0.8895 0.8865 0.2592 0.1260  0.0914  -0.0177 79  LYS   B CG  
1032 C CD  . LYS   B 64  ? 0.9069 0.8974 0.2663 0.1235  0.0900  -0.0175 79  LYS   B CD  
1033 C CE  . LYS   B 64  ? 0.9359 0.9226 0.2746 0.1416  0.0857  -0.0149 79  LYS   B CE  
1034 N NZ  . LYS   B 64  ? 0.9637 0.9362 0.2891 0.1391  0.0819  -0.0171 79  LYS   B NZ  
1035 N N   . GLN   B 65  ? 0.8497 0.8345 0.2372 0.1216  0.0872  -0.0306 80  GLN   B N   
1036 C CA  . GLN   B 65  ? 0.8518 0.8275 0.2304 0.1330  0.0815  -0.0341 80  GLN   B CA  
1037 C C   . GLN   B 65  ? 0.8314 0.8211 0.2210 0.1380  0.0856  -0.0307 80  GLN   B C   
1038 O O   . GLN   B 65  ? 0.8384 0.8257 0.2197 0.1511  0.0823  -0.0308 80  GLN   B O   
1039 C CB  . GLN   B 65  ? 0.8741 0.8337 0.2526 0.1244  0.0758  -0.0427 80  GLN   B CB  
1040 C CG  . GLN   B 65  ? 0.9025 0.8463 0.2700 0.1175  0.0709  -0.0460 80  GLN   B CG  
1041 C CD  . GLN   B 65  ? 0.9244 0.8547 0.2930 0.1077  0.0650  -0.0533 80  GLN   B CD  
1042 O OE1 . GLN   B 65  ? 0.9573 0.8806 0.3224 0.1132  0.0598  -0.0570 80  GLN   B OE1 
1043 N NE2 . GLN   B 65  ? 0.9253 0.8522 0.2981 0.0929  0.0654  -0.0553 80  GLN   B NE2 
1044 N N   A ASP   B 66  ? 0.8117 0.8141 0.2184 0.1275  0.0920  -0.0280 81  ASP   B N   
1045 N N   B ASP   B 66  ? 0.8117 0.8141 0.2184 0.1275  0.0920  -0.0280 81  ASP   B N   
1046 N N   C ASP   B 66  ? 0.8117 0.8142 0.2184 0.1277  0.0920  -0.0279 81  ASP   B N   
1047 N N   D ASP   B 66  ? 0.8117 0.8142 0.2184 0.1277  0.0920  -0.0279 81  ASP   B N   
1048 C CA  A ASP   B 66  ? 0.8010 0.8160 0.2200 0.1289  0.0962  -0.0243 81  ASP   B CA  
1049 C CA  B ASP   B 66  ? 0.8010 0.8160 0.2200 0.1289  0.0962  -0.0243 81  ASP   B CA  
1050 C CA  C ASP   B 66  ? 0.8016 0.8165 0.2202 0.1294  0.0961  -0.0242 81  ASP   B CA  
1051 C CA  D ASP   B 66  ? 0.8016 0.8165 0.2202 0.1294  0.0961  -0.0242 81  ASP   B CA  
1052 C C   A ASP   B 66  ? 0.7999 0.8067 0.2217 0.1296  0.0928  -0.0313 81  ASP   B C   
1053 C C   B ASP   B 66  ? 0.8000 0.8067 0.2217 0.1296  0.0928  -0.0313 81  ASP   B C   
1054 C C   C ASP   B 66  ? 0.8003 0.8068 0.2218 0.1297  0.0927  -0.0313 81  ASP   B C   
1055 C C   D ASP   B 66  ? 0.8003 0.8069 0.2218 0.1297  0.0927  -0.0313 81  ASP   B C   
1056 O O   A ASP   B 66  ? 0.8013 0.8132 0.2232 0.1394  0.0929  -0.0288 81  ASP   B O   
1057 O O   B ASP   B 66  ? 0.8013 0.8132 0.2232 0.1394  0.0929  -0.0288 81  ASP   B O   
1058 O O   C ASP   B 66  ? 0.8013 0.8128 0.2230 0.1396  0.0927  -0.0290 81  ASP   B O   
1059 O O   D ASP   B 66  ? 0.8013 0.8128 0.2230 0.1396  0.0927  -0.0290 81  ASP   B O   
1060 C CB  A ASP   B 66  ? 0.8050 0.8330 0.2186 0.1431  0.0981  -0.0153 81  ASP   B CB  
1061 C CB  B ASP   B 66  ? 0.8050 0.8330 0.2186 0.1431  0.0981  -0.0153 81  ASP   B CB  
1062 C CB  C ASP   B 66  ? 0.8058 0.8334 0.2186 0.1440  0.0978  -0.0154 81  ASP   B CB  
1063 C CB  D ASP   B 66  ? 0.8058 0.8334 0.2186 0.1440  0.0978  -0.0154 81  ASP   B CB  
1064 C CG  A ASP   B 66  ? 0.7957 0.8372 0.2218 0.1428  0.1025  -0.0097 81  ASP   B CG  
1065 C CG  B ASP   B 66  ? 0.7957 0.8371 0.2218 0.1428  0.1025  -0.0097 81  ASP   B CG  
1066 C CG  C ASP   B 66  ? 0.7967 0.8380 0.2219 0.1438  0.1023  -0.0097 81  ASP   B CG  
1067 C CG  D ASP   B 66  ? 0.7967 0.8380 0.2219 0.1438  0.1023  -0.0097 81  ASP   B CG  
1068 O OD1 A ASP   B 66  ? 0.7879 0.8309 0.2277 0.1301  0.1053  -0.0111 81  ASP   B OD1 
1069 O OD1 B ASP   B 66  ? 0.7879 0.8308 0.2277 0.1301  0.1053  -0.0111 81  ASP   B OD1 
1070 O OD1 C ASP   B 66  ? 0.7886 0.8317 0.2276 0.1311  0.1052  -0.0108 81  ASP   B OD1 
1071 O OD1 D ASP   B 66  ? 0.7886 0.8317 0.2276 0.1311  0.1052  -0.0108 81  ASP   B OD1 
1072 O OD2 A ASP   B 66  ? 0.8054 0.8551 0.2265 0.1559  0.1026  -0.0041 81  ASP   B OD2 
1073 O OD2 B ASP   B 66  ? 0.8054 0.8551 0.2265 0.1559  0.1026  -0.0041 81  ASP   B OD2 
1074 O OD2 C ASP   B 66  ? 0.8064 0.8561 0.2266 0.1569  0.1024  -0.0041 81  ASP   B OD2 
1075 O OD2 D ASP   B 66  ? 0.8064 0.8561 0.2266 0.1569  0.1024  -0.0041 81  ASP   B OD2 
1076 N N   . LEU   B 67  ? 0.7919 0.7879 0.2161 0.1193  0.0899  -0.0392 82  LEU   B N   
1077 C CA  . LEU   B 67  ? 0.7933 0.7828 0.2214 0.1181  0.0863  -0.0463 82  LEU   B CA  
1078 C C   . LEU   B 67  ? 0.7826 0.7756 0.2258 0.1033  0.0895  -0.0503 82  LEU   B C   
1079 O O   . LEU   B 67  ? 0.7780 0.7726 0.2247 0.0930  0.0923  -0.0498 82  LEU   B O   
1080 C CB  . LEU   B 67  ? 0.8079 0.7811 0.2222 0.1206  0.0783  -0.0519 82  LEU   B CB  
1081 C CG  . LEU   B 67  ? 0.8218 0.7888 0.2187 0.1373  0.0737  -0.0496 82  LEU   B CG  
1082 C CD1 . LEU   B 67  ? 0.8390 0.7863 0.2207 0.1383  0.0644  -0.0555 82  LEU   B CD1 
1083 C CD2 . LEU   B 67  ? 0.8207 0.7942 0.2200 0.1488  0.0741  -0.0483 82  LEU   B CD2 
1084 N N   . VAL   B 68  ? 0.7800 0.7736 0.2309 0.1027  0.0886  -0.0549 83  VAL   B N   
1085 C CA  . VAL   B 68  ? 0.7721 0.7689 0.2360 0.0904  0.0905  -0.0602 83  VAL   B CA  
1086 C C   . VAL   B 68  ? 0.7754 0.7691 0.2415 0.0925  0.0861  -0.0666 83  VAL   B C   
1087 O O   . VAL   B 68  ? 0.7800 0.7722 0.2417 0.1038  0.0837  -0.0659 83  VAL   B O   
1088 C CB  . VAL   B 68  ? 0.7614 0.7687 0.2368 0.0874  0.0969  -0.0565 83  VAL   B CB  
1089 C CG1 . VAL   B 68  ? 0.7614 0.7730 0.2373 0.0984  0.0977  -0.0522 83  VAL   B CG1 
1090 C CG2 . VAL   B 68  ? 0.7548 0.7656 0.2421 0.0772  0.0989  -0.0622 83  VAL   B CG2 
1091 N N   . SER   B 69  ? 0.7733 0.7676 0.2463 0.0821  0.0852  -0.0724 84  SER   B N   
1092 C CA  . SER   B 69  ? 0.7757 0.7698 0.2527 0.0817  0.0811  -0.0786 84  SER   B CA  
1093 C C   . SER   B 69  ? 0.7655 0.7706 0.2572 0.0741  0.0857  -0.0818 84  SER   B C   
1094 O O   . SER   B 69  ? 0.7594 0.7690 0.2561 0.0653  0.0901  -0.0810 84  SER   B O   
1095 C CB  . SER   B 69  ? 0.7862 0.7707 0.2552 0.0766  0.0741  -0.0821 84  SER   B CB  
1096 O OG  . SER   B 69  ? 0.7825 0.7706 0.2573 0.0627  0.0759  -0.0838 84  SER   B OG  
1097 N N   . TYR   B 70  ? 0.7645 0.7738 0.2622 0.0780  0.0845  -0.0856 85  TYR   B N   
1098 C CA  . TYR   B 70  ? 0.7568 0.7766 0.2673 0.0742  0.0881  -0.0893 85  TYR   B CA  
1099 C C   . TYR   B 70  ? 0.7596 0.7833 0.2742 0.0706  0.0837  -0.0957 85  TYR   B C   
1100 O O   . TYR   B 70  ? 0.7670 0.7850 0.2756 0.0763  0.0778  -0.0968 85  TYR   B O   
1101 C CB  . TYR   B 70  ? 0.7543 0.7760 0.2676 0.0839  0.0906  -0.0872 85  TYR   B CB  
1102 C CG  . TYR   B 70  ? 0.7510 0.7719 0.2630 0.0849  0.0952  -0.0805 85  TYR   B CG  
1103 C CD1 . TYR   B 70  ? 0.7544 0.7705 0.2573 0.0905  0.0947  -0.0741 85  TYR   B CD1 
1104 C CD2 . TYR   B 70  ? 0.7455 0.7709 0.2650 0.0797  0.0997  -0.0805 85  TYR   B CD2 
1105 C CE1 . TYR   B 70  ? 0.7514 0.7691 0.2538 0.0902  0.0988  -0.0672 85  TYR   B CE1 
1106 C CE2 . TYR   B 70  ? 0.7435 0.7681 0.2620 0.0792  0.1031  -0.0739 85  TYR   B CE2 
1107 C CZ  . TYR   B 70  ? 0.7459 0.7676 0.2564 0.0838  0.1028  -0.0669 85  TYR   B CZ  
1108 O OH  . TYR   B 70  ? 0.7457 0.7687 0.2556 0.0828  0.1059  -0.0595 85  TYR   B OH  
1109 N N   . CYS   B 71  ? 0.7774 0.8108 0.3010 0.0609  0.0860  -0.0992 86  CYS   B N   
1110 C CA  . CYS   B 71  ? 0.7988 0.8423 0.3301 0.0563  0.0834  -0.1050 86  CYS   B CA  
1111 C C   . CYS   B 71  ? 0.8168 0.8558 0.3427 0.0475  0.0777  -0.1051 86  CYS   B C   
1112 O O   . CYS   B 71  ? 0.8350 0.8837 0.3673 0.0402  0.0755  -0.1085 86  CYS   B O   
1113 C CB  . CYS   B 71  ? 0.8213 0.8670 0.3548 0.0657  0.0803  -0.1079 86  CYS   B CB  
1114 S SG  . CYS   B 71  ? 0.8536 0.9008 0.3908 0.0765  0.0857  -0.1068 86  CYS   B SG  
1115 N N   . GLY   B 72  ? 0.8271 0.8525 0.3414 0.0476  0.0754  -0.1011 87  GLY   B N   
1116 C CA  . GLY   B 72  ? 0.8362 0.8549 0.3439 0.0390  0.0689  -0.1013 87  GLY   B CA  
1117 C C   . GLY   B 72  ? 0.8400 0.8422 0.3332 0.0421  0.0666  -0.0971 87  GLY   B C   
1118 O O   . GLY   B 72  ? 0.8433 0.8421 0.3327 0.0506  0.0705  -0.0937 87  GLY   B O   
1119 N N   . PRO   B 73  ? 0.8424 0.8346 0.3269 0.0346  0.0599  -0.0969 88  PRO   B N   
1120 C CA  . PRO   B 73  ? 0.8506 0.8253 0.3189 0.0373  0.0563  -0.0934 88  PRO   B CA  
1121 C C   . PRO   B 73  ? 0.8454 0.8087 0.3024 0.0526  0.0519  -0.0930 88  PRO   B C   
1122 O O   . PRO   B 73  ? 0.8660 0.8308 0.3255 0.0566  0.0477  -0.0963 88  PRO   B O   
1123 C CB  . PRO   B 73  ? 0.8562 0.8235 0.3191 0.0243  0.0492  -0.0940 88  PRO   B CB  
1124 C CG  . PRO   B 73  ? 0.8543 0.8319 0.3274 0.0188  0.0457  -0.0980 88  PRO   B CG  
1125 C CD  . PRO   B 73  ? 0.8407 0.8378 0.3298 0.0223  0.0547  -0.0997 88  PRO   B CD  
1126 N N   . TRP   B 74  ? 0.8462 0.7999 0.2913 0.0607  0.0526  -0.0890 89  TRP   B N   
1127 C CA  . TRP   B 74  ? 0.8658 0.8074 0.2963 0.0760  0.0478  -0.0877 89  TRP   B CA  
1128 C C   . TRP   B 74  ? 0.8889 0.8168 0.3096 0.0765  0.0366  -0.0918 89  TRP   B C   
1129 O O   . TRP   B 74  ? 0.8961 0.8131 0.3096 0.0669  0.0304  -0.0926 89  TRP   B O   
1130 C CB  . TRP   B 74  ? 0.8648 0.7978 0.2821 0.0815  0.0487  -0.0830 89  TRP   B CB  
1131 C CG  . TRP   B 74  ? 0.8600 0.7856 0.2639 0.0992  0.0459  -0.0811 89  TRP   B CG  
1132 C CD1 . TRP   B 74  ? 0.8740 0.7815 0.2593 0.1073  0.0362  -0.0827 89  TRP   B CD1 
1133 C CD2 . TRP   B 74  ? 0.8488 0.7851 0.2559 0.1113  0.0522  -0.0769 89  TRP   B CD2 
1134 N NE1 . TRP   B 74  ? 0.8715 0.7791 0.2481 0.1246  0.0368  -0.0800 89  TRP   B NE1 
1135 C CE2 . TRP   B 74  ? 0.8532 0.7789 0.2433 0.1269  0.0466  -0.0760 89  TRP   B CE2 
1136 C CE3 . TRP   B 74  ? 0.8328 0.7857 0.2545 0.1103  0.0615  -0.0736 89  TRP   B CE3 
1137 C CZ2 . TRP   B 74  ? 0.8571 0.7910 0.2455 0.1415  0.0506  -0.0715 89  TRP   B CZ2 
1138 C CZ3 . TRP   B 74  ? 0.8240 0.7833 0.2439 0.1235  0.0648  -0.0689 89  TRP   B CZ3 
1139 C CH2 . TRP   B 74  ? 0.8386 0.7898 0.2426 0.1388  0.0598  -0.0675 89  TRP   B CH2 
1140 N N   . LYS   B 75  ? 0.8974 0.8252 0.3173 0.0870  0.0335  -0.0940 90  LYS   B N   
1141 C CA  . LYS   B 75  ? 0.9221 0.8380 0.3342 0.0872  0.0223  -0.0984 90  LYS   B CA  
1142 C C   . LYS   B 75  ? 0.9445 0.8412 0.3350 0.1023  0.0144  -0.0982 90  LYS   B C   
1143 O O   . LYS   B 75  ? 0.9681 0.8496 0.3479 0.1011  0.0033  -0.1015 90  LYS   B O   
1144 C CB  . LYS   B 75  ? 0.9181 0.8472 0.3436 0.0890  0.0234  -0.1018 90  LYS   B CB  
1145 C CG  . LYS   B 75  ? 0.9055 0.8538 0.3511 0.0759  0.0298  -0.1031 90  LYS   B CG  
1146 C CD  . LYS   B 75  ? 0.9247 0.8714 0.3720 0.0601  0.0233  -0.1053 90  LYS   B CD  
1147 C CE  . LYS   B 75  ? 0.9279 0.8942 0.3929 0.0470  0.0308  -0.1054 90  LYS   B CE  
1148 N NZ  . LYS   B 75  ? 0.9399 0.9202 0.4173 0.0425  0.0286  -0.1093 90  LYS   B NZ  
1149 N N   . LEU   B 76  ? 0.9564 0.8533 0.3398 0.1159  0.0191  -0.0942 91  LEU   B N   
1150 C CA  . LEU   B 76  ? 0.9893 0.8724 0.3531 0.1341  0.0129  -0.0939 91  LEU   B CA  
1151 C C   . LEU   B 76  ? 1.0205 0.8844 0.3643 0.1356  0.0067  -0.0928 91  LEU   B C   
1152 O O   . LEU   B 76  ? 1.0084 0.8767 0.3527 0.1335  0.0130  -0.0886 91  LEU   B O   
1153 C CB  . LEU   B 76  ? 0.9796 0.8767 0.3473 0.1477  0.0221  -0.0891 91  LEU   B CB  
1154 C CG  . LEU   B 76  ? 0.9667 0.8830 0.3548 0.1451  0.0296  -0.0892 91  LEU   B CG  
1155 C CD1 . LEU   B 76  ? 0.9601 0.8880 0.3496 0.1585  0.0372  -0.0835 91  LEU   B CD1 
1156 C CD2 . LEU   B 76  ? 0.9764 0.8902 0.3669 0.1457  0.0230  -0.0950 91  LEU   B CD2 
1157 N N   . ASP   B 77  ? 1.0683 0.9105 0.3940 0.1396  -0.0058 -0.0966 92  ASP   B N   
1158 C CA  . ASP   B 77  ? 1.1201 0.9398 0.4250 0.1390  -0.0140 -0.0964 92  ASP   B CA  
1159 C C   . ASP   B 77  ? 1.1242 0.9239 0.4035 0.1588  -0.0236 -0.0982 92  ASP   B C   
1160 O O   . ASP   B 77  ? 1.1415 0.9222 0.4008 0.1630  -0.0301 -0.0978 92  ASP   B O   
1161 C CB  . ASP   B 77  ? 1.1654 0.9744 0.4720 0.1192  -0.0217 -0.0993 92  ASP   B CB  
1162 C CG  . ASP   B 77  ? 1.2212 1.0258 0.5304 0.1153  -0.0306 -0.1043 92  ASP   B CG  
1163 O OD1 . ASP   B 77  ? 1.2324 1.0438 0.5439 0.1280  -0.0296 -0.1059 92  ASP   B OD1 
1164 O OD2 . ASP   B 77  ? 1.2642 1.0597 0.5733 0.0992  -0.0385 -0.1060 92  ASP   B OD2 
1165 N N   . ALA   B 78  ? 1.1039 0.9078 0.3825 0.1722  -0.0245 -0.0998 93  ALA   B N   
1166 C CA  . ALA   B 78  ? 1.1116 0.8976 0.3647 0.1929  -0.0334 -0.1014 93  ALA   B CA  
1167 C C   . ALA   B 78  ? 1.1002 0.8899 0.3426 0.2066  -0.0274 -0.0960 93  ALA   B C   
1168 O O   . ALA   B 78  ? 1.0575 0.8711 0.3175 0.2035  -0.0139 -0.0904 93  ALA   B O   
1169 C CB  . ALA   B 78  ? 1.1025 0.8962 0.3595 0.2041  -0.0337 -0.1035 93  ALA   B CB  
1170 N N   . ALA   B 79  ? 1.1285 0.8960 0.3429 0.2220  -0.0373 -0.0977 94  ALA   B N   
1171 C CA  . ALA   B 79  ? 1.1408 0.9094 0.3402 0.2379  -0.0339 -0.0931 94  ALA   B CA  
1172 C C   . ALA   B 79  ? 1.1574 0.9197 0.3354 0.2642  -0.0391 -0.0940 94  ALA   B C   
1173 O O   . ALA   B 79  ? 1.1747 0.9142 0.3359 0.2698  -0.0521 -0.1002 94  ALA   B O   
1174 C CB  . ALA   B 79  ? 1.1595 0.9053 0.3428 0.2310  -0.0416 -0.0943 94  ALA   B CB  
1175 N N   . TRP   B 80  ? 1.1569 0.9380 0.3335 0.2801  -0.0302 -0.0878 95  TRP   B N   
1176 C CA  . TRP   B 80  ? 1.2014 0.9771 0.3532 0.3074  -0.0349 -0.0876 95  TRP   B CA  
1177 C C   . TRP   B 80  ? 1.2566 0.9976 0.3771 0.3148  -0.0498 -0.0931 95  TRP   B C   
1178 O O   . TRP   B 80  ? 1.2631 0.9950 0.3803 0.3049  -0.0508 -0.0924 95  TRP   B O   
1179 C CB  . TRP   B 80  ? 1.1868 0.9896 0.3420 0.3204  -0.0227 -0.0787 95  TRP   B CB  
1180 C CG  . TRP   B 80  ? 1.1875 0.9896 0.3190 0.3491  -0.0264 -0.0778 95  TRP   B CG  
1181 C CD1 . TRP   B 80  ? 1.2097 1.0038 0.3292 0.3641  -0.0334 -0.0819 95  TRP   B CD1 
1182 C CD2 . TRP   B 80  ? 1.1952 1.0065 0.3116 0.3673  -0.0233 -0.0723 95  TRP   B CD2 
1183 N NE1 . TRP   B 80  ? 1.2169 1.0143 0.3143 0.3908  -0.0347 -0.0794 95  TRP   B NE1 
1184 C CE2 . TRP   B 80  ? 1.2161 1.0243 0.3110 0.3935  -0.0288 -0.0735 95  TRP   B CE2 
1185 C CE3 . TRP   B 80  ? 1.1841 1.0056 0.3020 0.3647  -0.0170 -0.0667 95  TRP   B CE3 
1186 C CZ2 . TRP   B 80  ? 1.2235 1.0407 0.2992 0.4172  -0.0275 -0.0690 95  TRP   B CZ2 
1187 C CZ3 . TRP   B 80  ? 1.1991 1.0293 0.2984 0.3877  -0.0160 -0.0622 95  TRP   B CZ3 
1188 C CH2 . TRP   B 80  ? 1.2172 1.0461 0.2958 0.4139  -0.0210 -0.0632 95  TRP   B CH2 
1189 N N   . ASP   B 81  ? 1.3146 1.0357 0.4121 0.3316  -0.0617 -0.0985 96  ASP   B N   
1190 C CA  . ASP   B 81  ? 1.3764 1.0590 0.4412 0.3388  -0.0786 -0.1048 96  ASP   B CA  
1191 C C   . ASP   B 81  ? 1.3945 1.0754 0.4351 0.3618  -0.0785 -0.1018 96  ASP   B C   
1192 O O   . ASP   B 81  ? 1.4429 1.0909 0.4553 0.3671  -0.0920 -0.1064 96  ASP   B O   
1193 C CB  . ASP   B 81  ? 1.4020 1.0616 0.4502 0.3476  -0.0927 -0.1124 96  ASP   B CB  
1194 C CG  . ASP   B 81  ? 1.4127 1.0848 0.4517 0.3740  -0.0906 -0.1116 96  ASP   B CG  
1195 O OD1 . ASP   B 81  ? 1.4094 1.1089 0.4542 0.3861  -0.0781 -0.1044 96  ASP   B OD1 
1196 O OD2 . ASP   B 81  ? 1.4469 1.1025 0.4738 0.3815  -0.1013 -0.1177 96  ASP   B OD2 
1197 N N   . GLY   B 82  ? 1.3671 1.0818 0.4183 0.3739  -0.0645 -0.0941 97  GLY   B N   
1198 C CA  . GLY   B 82  ? 1.3814 1.1052 0.4157 0.3951  -0.0610 -0.0892 97  GLY   B CA  
1199 C C   . GLY   B 82  ? 1.4288 1.1506 0.4382 0.4262  -0.0664 -0.0906 97  GLY   B C   
1200 O O   . GLY   B 82  ? 1.4177 1.1485 0.4113 0.4463  -0.0640 -0.0866 97  GLY   B O   
1201 N N   . LEU   B 83  ? 1.4575 1.1692 0.4635 0.4304  -0.0733 -0.0960 98  LEU   B N   
1202 C CA  . LEU   B 83  ? 1.5086 1.2113 0.4877 0.4594  -0.0816 -0.0994 98  LEU   B CA  
1203 C C   . LEU   B 83  ? 1.4826 1.2108 0.4787 0.4644  -0.0738 -0.0967 98  LEU   B C   
1204 O O   . LEU   B 83  ? 1.4965 1.2421 0.4819 0.4894  -0.0701 -0.0927 98  LEU   B O   
1205 C CB  . LEU   B 83  ? 1.5870 1.2435 0.5394 0.4598  -0.1017 -0.1104 98  LEU   B CB  
1206 C CG  . LEU   B 83  ? 1.6541 1.2792 0.5755 0.4675  -0.1134 -0.1140 98  LEU   B CG  
1207 C CD1 . LEU   B 83  ? 1.7077 1.2862 0.6079 0.4604  -0.1336 -0.1241 98  LEU   B CD1 
1208 C CD2 . LEU   B 83  ? 1.6840 1.3140 0.5774 0.5020  -0.1143 -0.1124 98  LEU   B CD2 
1209 N N   . SER   B 84  ? 1.4428 1.1706 0.4608 0.4439  -0.0733 -0.0993 99  SER   B N   
1210 C CA  . SER   B 84  ? 1.3985 1.1413 0.4273 0.4496  -0.0701 -0.0991 99  SER   B CA  
1211 C C   . SER   B 84  ? 1.3403 1.1260 0.3988 0.4452  -0.0513 -0.0884 99  SER   B C   
1212 O O   . SER   B 84  ? 1.3127 1.1135 0.3907 0.4284  -0.0416 -0.0829 99  SER   B O   
1213 C CB  . SER   B 84  ? 1.4024 1.1262 0.4402 0.4311  -0.0785 -0.1067 99  SER   B CB  
1214 O OG  . SER   B 84  ? 1.4335 1.1371 0.4744 0.4085  -0.0841 -0.1101 99  SER   B OG  
1215 N N   . GLU   B 85  ? 1.3221 1.1264 0.3829 0.4601  -0.0469 -0.0854 100 GLU   B N   
1216 C CA  . GLU   B 85  ? 1.2790 1.1205 0.3688 0.4540  -0.0311 -0.0760 100 GLU   B CA  
1217 C C   . GLU   B 85  ? 1.2246 1.0650 0.3432 0.4245  -0.0285 -0.0787 100 GLU   B C   
1218 O O   . GLU   B 85  ? 1.2433 1.0553 0.3598 0.4094  -0.0394 -0.0882 100 GLU   B O   
1219 C CB  . GLU   B 85  ? 1.3022 1.1580 0.3858 0.4755  -0.0296 -0.0735 100 GLU   B CB  
1220 C CG  . GLU   B 85  ? 1.3339 1.1976 0.3916 0.5058  -0.0305 -0.0696 100 GLU   B CG  
1221 C CD  . GLU   B 85  ? 1.3389 1.2326 0.3984 0.5249  -0.0224 -0.0615 100 GLU   B CD  
1222 O OE1 . GLU   B 85  ? 1.3123 1.2141 0.3874 0.5190  -0.0193 -0.0611 100 GLU   B OE1 
1223 O OE2 . GLU   B 85  ? 1.3636 1.2740 0.4086 0.5462  -0.0189 -0.0550 100 GLU   B OE2 
1224 N N   . VAL   B 86  ? 1.1762 1.0460 0.3217 0.4124  -0.0140 -0.0699 101 VAL   B N   
1225 C CA  . VAL   B 86  ? 1.1339 1.0113 0.3094 0.3864  -0.0078 -0.0700 101 VAL   B CA  
1226 C C   . VAL   B 86  ? 1.0993 1.0047 0.2935 0.3884  0.0028  -0.0627 101 VAL   B C   
1227 O O   . VAL   B 86  ? 1.1203 1.0420 0.3059 0.4081  0.0067  -0.0561 101 VAL   B O   
1228 C CB  . VAL   B 86  ? 1.1120 0.9947 0.3009 0.3677  -0.0014 -0.0665 101 VAL   B CB  
1229 C CG1 . VAL   B 86  ? 1.1292 0.9843 0.2971 0.3678  -0.0121 -0.0727 101 VAL   B CG1 
1230 C CG2 . VAL   B 86  ? 1.0981 1.0108 0.2953 0.3733  0.0111  -0.0548 101 VAL   B CG2 
1231 N N   . GLN   B 87  ? 1.0626 0.9736 0.2814 0.3684  0.0074  -0.0636 102 GLN   B N   
1232 C CA  . GLN   B 87  ? 1.0399 0.9753 0.2785 0.3667  0.0174  -0.0568 102 GLN   B CA  
1233 C C   . GLN   B 87  ? 1.0077 0.9580 0.2711 0.3455  0.0277  -0.0515 102 GLN   B C   
1234 O O   . GLN   B 87  ? 0.9941 0.9337 0.2680 0.3270  0.0257  -0.0573 102 GLN   B O   
1235 C CB  . GLN   B 87  ? 1.0489 0.9762 0.2901 0.3674  0.0120  -0.0635 102 GLN   B CB  
1236 C CG  . GLN   B 87  ? 1.0732 0.9884 0.2891 0.3908  0.0026  -0.0675 102 GLN   B CG  
1237 C CD  . GLN   B 87  ? 1.0801 0.9936 0.2987 0.3955  -0.0008 -0.0716 102 GLN   B CD  
1238 O OE1 . GLN   B 87  ? 1.0631 0.9811 0.3017 0.3806  0.0020  -0.0732 102 GLN   B OE1 
1239 N NE2 . GLN   B 87  ? 1.0948 1.0008 0.2914 0.4175  -0.0080 -0.0740 102 GLN   B NE2 
1240 N N   . LEU   B 88  ? 0.9858 0.9602 0.2568 0.3490  0.0378  -0.0405 103 LEU   B N   
1241 C CA  . LEU   B 88  ? 0.9616 0.9524 0.2573 0.3309  0.0477  -0.0345 103 LEU   B CA  
1242 C C   . LEU   B 88  ? 0.9607 0.9556 0.2699 0.3271  0.0494  -0.0357 103 LEU   B C   
1243 O O   . LEU   B 88  ? 0.9674 0.9735 0.2730 0.3412  0.0512  -0.0306 103 LEU   B O   
1244 C CB  . LEU   B 88  ? 0.9536 0.9687 0.2519 0.3361  0.0568  -0.0217 103 LEU   B CB  
1245 C CG  . LEU   B 88  ? 0.9325 0.9638 0.2550 0.3183  0.0662  -0.0148 103 LEU   B CG  
1246 C CD1 . LEU   B 88  ? 0.9299 0.9501 0.2631 0.2976  0.0660  -0.0205 103 LEU   B CD1 
1247 C CD2 . LEU   B 88  ? 0.9306 0.9870 0.2556 0.3233  0.0743  -0.0012 103 LEU   B CD2 
1248 N N   . LEU   B 89  ? 0.9491 0.9356 0.2727 0.3096  0.0484  -0.0423 104 LEU   B N   
1249 C CA  . LEU   B 89  ? 0.9426 0.9363 0.2819 0.3041  0.0518  -0.0421 104 LEU   B CA  
1250 C C   . LEU   B 89  ? 0.9267 0.9391 0.2832 0.2938  0.0622  -0.0323 104 LEU   B C   
1251 O O   . LEU   B 89  ? 0.9177 0.9289 0.2892 0.2762  0.0649  -0.0346 104 LEU   B O   
1252 C CB  . LEU   B 89  ? 0.9535 0.9312 0.2983 0.2924  0.0454  -0.0534 104 LEU   B CB  
1253 C CG  . LEU   B 89  ? 0.9601 0.9430 0.3225 0.2835  0.0482  -0.0554 104 LEU   B CG  
1254 C CD1 . LEU   B 89  ? 0.9626 0.9593 0.3273 0.2947  0.0529  -0.0481 104 LEU   B CD1 
1255 C CD2 . LEU   B 89  ? 0.9786 0.9467 0.3393 0.2809  0.0392  -0.0666 104 LEU   B CD2 
1256 N N   . ALA   B 90  ? 0.9218 0.9514 0.2755 0.3048  0.0676  -0.0213 105 ALA   B N   
1257 C CA  . ALA   B 90  ? 0.9027 0.9511 0.2709 0.2962  0.0768  -0.0100 105 ALA   B CA  
1258 C C   . ALA   B 90  ? 0.8945 0.9452 0.2780 0.2878  0.0795  -0.0098 105 ALA   B C   
1259 O O   . ALA   B 90  ? 0.9076 0.9566 0.2870 0.2982  0.0768  -0.0117 105 ALA   B O   
1260 C CB  . ALA   B 90  ? 0.9013 0.9685 0.2615 0.3105  0.0809  0.0020  105 ALA   B CB  
1261 N N   . VAL   B 91  ? 0.8733 0.9266 0.2727 0.2705  0.0840  -0.0082 106 VAL   B N   
1262 C CA  . VAL   B 91  ? 0.8588 0.9144 0.2726 0.2617  0.0870  -0.0068 106 VAL   B CA  
1263 C C   . VAL   B 91  ? 0.8597 0.9304 0.2821 0.2547  0.0939  0.0060  106 VAL   B C   
1264 O O   . VAL   B 91  ? 0.8552 0.9253 0.2882 0.2396  0.0966  0.0063  106 VAL   B O   
1265 C CB  . VAL   B 91  ? 0.8439 0.8862 0.2668 0.2480  0.0844  -0.0182 106 VAL   B CB  
1266 C CG1 . VAL   B 91  ? 0.8402 0.8831 0.2764 0.2400  0.0868  -0.0182 106 VAL   B CG1 
1267 C CG2 . VAL   B 91  ? 0.8508 0.8794 0.2650 0.2537  0.0769  -0.0297 106 VAL   B CG2 
1268 N N   . PRO   B 92  ? 0.8770 0.9628 0.2951 0.2653  0.0968  0.0175  107 PRO   B N   
1269 C CA  . PRO   B 92  ? 0.8726 0.9746 0.2980 0.2587  0.1027  0.0313  107 PRO   B CA  
1270 C C   . PRO   B 92  ? 0.8704 0.9696 0.3088 0.2470  0.1044  0.0334  107 PRO   B C   
1271 O O   . PRO   B 92  ? 0.8872 0.9764 0.3267 0.2496  0.1016  0.0266  107 PRO   B O   
1272 C CB  . PRO   B 92  ? 0.8909 1.0104 0.3060 0.2757  0.1044  0.0423  107 PRO   B CB  
1273 C CG  . PRO   B 92  ? 0.8990 1.0088 0.2998 0.2928  0.0988  0.0329  107 PRO   B CG  
1274 C CD  . PRO   B 92  ? 0.8955 0.9841 0.3013 0.2842  0.0943  0.0184  107 PRO   B CD  
1275 N N   . PRO   B 93  ? 0.8737 0.9813 0.3213 0.2347  0.1084  0.0432  108 PRO   B N   
1276 C CA  . PRO   B 93  ? 0.8839 0.9851 0.3423 0.2226  0.1089  0.0443  108 PRO   B CA  
1277 C C   . PRO   B 93  ? 0.9018 1.0065 0.3590 0.2307  0.1087  0.0506  108 PRO   B C   
1278 O O   . PRO   B 93  ? 0.9053 1.0245 0.3580 0.2386  0.1107  0.0614  108 PRO   B O   
1279 C CB  . PRO   B 93  ? 0.8733 0.9837 0.3388 0.2092  0.1123  0.0545  108 PRO   B CB  
1280 C CG  . PRO   B 93  ? 0.8734 0.9898 0.3334 0.2119  0.1131  0.0531  108 PRO   B CG  
1281 C CD  . PRO   B 93  ? 0.8798 1.0023 0.3274 0.2312  0.1119  0.0533  108 PRO   B CD  
1282 N N   . GLY   B 94  ? 0.9239 1.0152 0.3849 0.2285  0.1063  0.0433  109 GLY   B N   
1283 C CA  . GLY   B 94  ? 0.9507 1.0420 0.4098 0.2365  0.1054  0.0473  109 GLY   B CA  
1284 C C   . GLY   B 94  ? 0.9705 1.0664 0.4187 0.2552  0.1038  0.0455  109 GLY   B C   
1285 O O   . GLY   B 94  ? 0.9653 1.0649 0.4111 0.2628  0.1037  0.0515  109 GLY   B O   
1286 N N   . GLU   B 95  ? 0.9870 1.0822 0.4278 0.2629  0.1020  0.0381  110 GLU   B N   
1287 C CA  . GLU   B 95  ? 1.0041 1.1027 0.4323 0.2818  0.0997  0.0365  110 GLU   B CA  
1288 C C   . GLU   B 95  ? 1.0132 1.0955 0.4376 0.2845  0.0941  0.0199  110 GLU   B C   
1289 O O   . GLU   B 95  ? 0.9981 1.0708 0.4289 0.2720  0.0932  0.0119  110 GLU   B O   
1290 C CB  . GLU   B 95  ? 1.0237 1.1390 0.4432 0.2908  0.1022  0.0460  110 GLU   B CB  
1291 C CG  . GLU   B 95  ? 1.0457 1.1798 0.4708 0.2854  0.1077  0.0634  110 GLU   B CG  
1292 C CD  . GLU   B 95  ? 1.0723 1.2284 0.4888 0.2961  0.1108  0.0748  110 GLU   B CD  
1293 O OE1 . GLU   B 95  ? 1.1107 1.2638 0.5175 0.3049  0.1086  0.0675  110 GLU   B OE1 
1294 O OE2 . GLU   B 95  ? 1.0821 1.2579 0.5020 0.2945  0.1151  0.0907  110 GLU   B OE2 
1295 N N   . ARG   B 96  ? 1.0187 1.0979 0.4335 0.2994  0.0902  0.0152  111 ARG   B N   
1296 C CA  . ARG   B 96  ? 1.0358 1.0997 0.4463 0.3025  0.0838  0.0001  111 ARG   B CA  
1297 C C   . ARG   B 96  ? 1.0219 1.0817 0.4241 0.3035  0.0812  -0.0047 111 ARG   B C   
1298 O O   . ARG   B 96  ? 1.0109 1.0812 0.4051 0.3110  0.0835  0.0034  111 ARG   B O   
1299 C CB  . ARG   B 96  ? 1.0796 1.1428 0.4803 0.3196  0.0801  -0.0015 111 ARG   B CB  
1300 C CG  . ARG   B 96  ? 1.1242 1.1721 0.5223 0.3217  0.0729  -0.0164 111 ARG   B CG  
1301 C CD  . ARG   B 96  ? 1.1640 1.2105 0.5614 0.3307  0.0707  -0.0181 111 ARG   B CD  
1302 N NE  . ARG   B 96  ? 1.2085 1.2638 0.5936 0.3484  0.0709  -0.0105 111 ARG   B NE  
1303 C CZ  . ARG   B 96  ? 1.2630 1.3305 0.6493 0.3531  0.0757  0.0015  111 ARG   B CZ  
1304 N NH1 . ARG   B 96  ? 1.2390 1.3095 0.6380 0.3408  0.0803  0.0077  111 ARG   B NH1 
1305 N NH2 . ARG   B 96  ? 1.2574 1.3336 0.6312 0.3706  0.0754  0.0073  111 ARG   B NH2 
1306 N N   . ALA   B 97  ? 1.0096 1.0551 0.4132 0.2967  0.0764  -0.0173 112 ALA   B N   
1307 C CA  . ALA   B 97  ? 1.0128 1.0497 0.4061 0.2986  0.0717  -0.0239 112 ALA   B CA  
1308 C C   . ALA   B 97  ? 1.0441 1.0820 0.4191 0.3189  0.0679  -0.0224 112 ALA   B C   
1309 O O   . ALA   B 97  ? 1.0188 1.0562 0.3895 0.3299  0.0654  -0.0237 112 ALA   B O   
1310 C CB  . ALA   B 97  ? 1.0170 1.0392 0.4142 0.2900  0.0659  -0.0371 112 ALA   B CB  
1311 N N   . LYS   B 98  ? 1.0661 1.1051 0.4296 0.3249  0.0672  -0.0201 113 LYS   B N   
1312 C CA  . LYS   B 98  ? 1.0926 1.1343 0.4368 0.3464  0.0640  -0.0177 113 LYS   B CA  
1313 C C   . LYS   B 98  ? 1.0862 1.1169 0.4155 0.3508  0.0586  -0.0229 113 LYS   B C   
1314 O O   . LYS   B 98  ? 1.0792 1.1153 0.4122 0.3423  0.0627  -0.0185 113 LYS   B O   
1315 C CB  . LYS   B 98  ? 1.1286 1.1933 0.4746 0.3529  0.0721  -0.0026 113 LYS   B CB  
1316 C CG  . LYS   B 98  ? 1.1974 1.2718 0.5258 0.3761  0.0710  0.0028  113 LYS   B CG  
1317 C CD  . LYS   B 98  ? 1.2294 1.3292 0.5596 0.3796  0.0792  0.0188  113 LYS   B CD  
1318 C CE  . LYS   B 98  ? 1.2301 1.3353 0.5743 0.3606  0.0845  0.0233  113 LYS   B CE  
1319 N NZ  . LYS   B 98  ? 1.2405 1.3716 0.5898 0.3607  0.0924  0.0397  113 LYS   B NZ  
1320 N N   . ASN   B 99  ? 1.0605 1.0750 0.3737 0.3622  0.0493  -0.0322 114 ASN   B N   
1321 C CA  . ASN   B 99  ? 1.0731 1.0731 0.3683 0.3683  0.0422  -0.0379 114 ASN   B CA  
1322 C C   . ASN   B 99  ? 1.0771 1.0905 0.3573 0.3869  0.0449  -0.0289 114 ASN   B C   
1323 O O   . ASN   B 99  ? 1.0909 1.1158 0.3656 0.4022  0.0466  -0.0236 114 ASN   B O   
1324 C CB  . ASN   B 99  ? 1.0902 1.0670 0.3713 0.3747  0.0301  -0.0503 114 ASN   B CB  
1325 C CG  . ASN   B 99  ? 1.1006 1.0647 0.3953 0.3558  0.0264  -0.0595 114 ASN   B CG  
1326 O OD1 . ASN   B 99  ? 1.1001 1.0718 0.4113 0.3477  0.0304  -0.0591 114 ASN   B OD1 
1327 N ND2 . ASN   B 99  ? 1.1181 1.0633 0.4059 0.3484  0.0185  -0.0676 114 ASN   B ND2 
1328 N N   . ILE   B 100 ? 1.0543 1.0665 0.3267 0.3869  0.0449  -0.0274 115 ILE   B N   
1329 C CA  . ILE   B 100 ? 1.0592 1.0836 0.3147 0.4064  0.0464  -0.0200 115 ILE   B CA  
1330 C C   . ILE   B 100 ? 1.0822 1.0849 0.3178 0.4118  0.0373  -0.0284 115 ILE   B C   
1331 O O   . ILE   B 100 ? 1.0920 1.0864 0.3342 0.3954  0.0374  -0.0311 115 ILE   B O   
1332 C CB  . ILE   B 100 ? 1.0448 1.0952 0.3131 0.3999  0.0574  -0.0067 115 ILE   B CB  
1333 C CG1 . ILE   B 100 ? 1.0306 1.0988 0.3211 0.3883  0.0660  0.0016  115 ILE   B CG1 
1334 C CG2 . ILE   B 100 ? 1.0584 1.1243 0.3095 0.4211  0.0589  0.0010  115 ILE   B CG2 
1335 C CD1 . ILE   B 100 ? 1.0355 1.1182 0.3222 0.4041  0.0680  0.0082  115 ILE   B CD1 
1336 N N   . GLN   B 101 ? 1.1040 1.0990 0.3154 0.4342  0.0302  -0.0313 116 GLN   B N   
1337 C CA  . GLN   B 101 ? 1.1384 1.1078 0.3266 0.4418  0.0192  -0.0405 116 GLN   B CA  
1338 C C   . GLN   B 101 ? 1.1558 1.1386 0.3320 0.4545  0.0229  -0.0329 116 GLN   B C   
1339 O O   . GLN   B 101 ? 1.1833 1.1893 0.3549 0.4716  0.0284  -0.0238 116 GLN   B O   
1340 C CB  . GLN   B 101 ? 1.1694 1.1197 0.3364 0.4595  0.0078  -0.0491 116 GLN   B CB  
1341 C CG  . GLN   B 101 ? 1.2000 1.1202 0.3405 0.4680  -0.0053 -0.0588 116 GLN   B CG  
1342 C CD  . GLN   B 101 ? 1.2293 1.1238 0.3550 0.4758  -0.0186 -0.0701 116 GLN   B CD  
1343 O OE1 . GLN   B 101 ? 1.2158 1.1084 0.3580 0.4627  -0.0188 -0.0737 116 GLN   B OE1 
1344 N NE2 . GLN   B 101 ? 1.2682 1.1422 0.3632 0.4953  -0.0299 -0.0758 116 GLN   B NE2 
1345 N N   . THR   B 102 ? 1.1549 1.1237 0.3251 0.4472  0.0195  -0.0365 117 THR   B N   
1346 C CA  . THR   B 102 ? 1.1594 1.1400 0.3178 0.4586  0.0225  -0.0299 117 THR   B CA  
1347 C C   . THR   B 102 ? 1.1812 1.1303 0.3183 0.4603  0.0111  -0.0398 117 THR   B C   
1348 O O   . THR   B 102 ? 1.1996 1.1225 0.3385 0.4461  0.0032  -0.0497 117 THR   B O   
1349 C CB  . THR   B 102 ? 1.1286 1.1373 0.3118 0.4426  0.0357  -0.0186 117 THR   B CB  
1350 O OG1 . THR   B 102 ? 1.1384 1.1641 0.3097 0.4575  0.0391  -0.0108 117 THR   B OG1 
1351 C CG2 . THR   B 102 ? 1.1183 1.1150 0.3192 0.4153  0.0365  -0.0228 117 THR   B CG2 
1352 N N   . LEU   B 103 ? 1.1958 1.1473 0.3117 0.4788  0.0093  -0.0373 118 LEU   B N   
1353 C CA  . LEU   B 103 ? 1.2048 1.1296 0.3021 0.4785  0.0003  -0.0442 118 LEU   B CA  
1354 C C   . LEU   B 103 ? 1.1809 1.1233 0.2944 0.4637  0.0099  -0.0366 118 LEU   B C   
1355 O O   . LEU   B 103 ? 1.1558 1.1286 0.2733 0.4721  0.0194  -0.0258 118 LEU   B O   
1356 C CB  . LEU   B 103 ? 1.2405 1.1539 0.3024 0.5086  -0.0086 -0.0472 118 LEU   B CB  
1357 C CG  . LEU   B 103 ? 1.2654 1.1473 0.3071 0.5070  -0.0191 -0.0549 118 LEU   B CG  
1358 C CD1 . LEU   B 103 ? 1.2833 1.1242 0.3128 0.5002  -0.0340 -0.0679 118 LEU   B CD1 
1359 C CD2 . LEU   B 103 ? 1.3010 1.1838 0.3126 0.5355  -0.0228 -0.0533 118 LEU   B CD2 
1360 N N   . PRO   B 104 ? 1.1673 1.0928 0.2922 0.4397  0.0082  -0.0415 119 PRO   B N   
1361 C CA  . PRO   B 104 ? 1.1531 1.0941 0.2934 0.4250  0.0169  -0.0349 119 PRO   B CA  
1362 C C   . PRO   B 104 ? 1.1831 1.1229 0.3000 0.4423  0.0142  -0.0330 119 PRO   B C   
1363 O O   . PRO   B 104 ? 1.2338 1.1467 0.3216 0.4585  0.0020  -0.0409 119 PRO   B O   
1364 C CB  . PRO   B 104 ? 1.1392 1.0568 0.2903 0.3992  0.0129  -0.0426 119 PRO   B CB  
1365 C CG  . PRO   B 104 ? 1.1428 1.0410 0.2927 0.3968  0.0049  -0.0512 119 PRO   B CG  
1366 C CD  . PRO   B 104 ? 1.1705 1.0645 0.2953 0.4252  -0.0016 -0.0527 119 PRO   B CD  
1367 N N   . GLY   B 105 ? 1.1736 1.1444 0.3039 0.4397  0.0255  -0.0220 120 GLY   B N   
1368 C CA  . GLY   B 105 ? 1.1956 1.1694 0.3130 0.4470  0.0256  -0.0191 120 GLY   B CA  
1369 C C   . GLY   B 105 ? 1.1938 1.1470 0.3172 0.4247  0.0230  -0.0242 120 GLY   B C   
1370 O O   . GLY   B 105 ? 1.1733 1.1047 0.3052 0.4066  0.0186  -0.0318 120 GLY   B O   
1371 N N   . ILE   B 106 ? 1.2144 1.1757 0.3332 0.4264  0.0258  -0.0199 121 ILE   B N   
1372 C CA  . ILE   B 106 ? 1.2200 1.1624 0.3401 0.4087  0.0231  -0.0240 121 ILE   B CA  
1373 C C   . ILE   B 106 ? 1.1909 1.1638 0.3318 0.3970  0.0352  -0.0138 121 ILE   B C   
1374 O O   . ILE   B 106 ? 1.1871 1.1871 0.3246 0.4118  0.0409  -0.0049 121 ILE   B O   
1375 C CB  . ILE   B 106 ? 1.2863 1.2004 0.3724 0.4256  0.0112  -0.0306 121 ILE   B CB  
1376 C CG1 . ILE   B 106 ? 1.3507 1.2338 0.4125 0.4399  -0.0020 -0.0404 121 ILE   B CG1 
1377 C CG2 . ILE   B 106 ? 1.3113 1.2050 0.3979 0.4074  0.0080  -0.0345 121 ILE   B CG2 
1378 C CD1 . ILE   B 106 ? 1.3527 1.2022 0.4176 0.4193  -0.0107 -0.0501 121 ILE   B CD1 
1379 N N   . PHE   B 107 ? 1.1654 1.1337 0.3267 0.3709  0.0384  -0.0152 122 PHE   B N   
1380 C CA  . PHE   B 107 ? 1.1415 1.1261 0.3164 0.3578  0.0460  -0.0089 122 PHE   B CA  
1381 C C   . PHE   B 107 ? 1.1888 1.1459 0.3446 0.3571  0.0379  -0.0154 122 PHE   B C   
1382 O O   . PHE   B 107 ? 1.2169 1.1452 0.3712 0.3435  0.0310  -0.0240 122 PHE   B O   
1383 C CB  . PHE   B 107 ? 1.0964 1.0870 0.3012 0.3305  0.0527  -0.0082 122 PHE   B CB  
1384 C CG  . PHE   B 107 ? 1.0703 1.0924 0.2984 0.3257  0.0630  0.0009  122 PHE   B CG  
1385 C CD1 . PHE   B 107 ? 1.0755 1.1214 0.2996 0.3444  0.0665  0.0088  122 PHE   B CD1 
1386 C CD2 . PHE   B 107 ? 1.0490 1.0756 0.3024 0.3021  0.0686  0.0014  122 PHE   B CD2 
1387 C CE1 . PHE   B 107 ? 1.0544 1.1274 0.2999 0.3382  0.0753  0.0176  122 PHE   B CE1 
1388 C CE2 . PHE   B 107 ? 1.0337 1.0856 0.3072 0.2971  0.0769  0.0095  122 PHE   B CE2 
1389 C CZ  . PHE   B 107 ? 1.0308 1.1053 0.3004 0.3144  0.0801  0.0178  122 PHE   B CZ  
1390 N N   . LYS   B 108 ? 1.2147 1.1817 0.3571 0.3704  0.0387  -0.0107 123 LYS   B N   
1391 C CA  . LYS   B 108 ? 1.2306 1.1750 0.3554 0.3699  0.0322  -0.0152 123 LYS   B CA  
1392 C C   . LYS   B 108 ? 1.2022 1.1626 0.3498 0.3481  0.0410  -0.0099 123 LYS   B C   
1393 O O   . LYS   B 108 ? 1.1547 1.1500 0.3161 0.3501  0.0508  0.0000  123 LYS   B O   
1394 C CB  . LYS   B 108 ? 1.2860 1.2339 0.3829 0.3983  0.0283  -0.0130 123 LYS   B CB  
1395 C CG  . LYS   B 108 ? 1.3548 1.2751 0.4206 0.4207  0.0158  -0.0210 123 LYS   B CG  
1396 C CD  . LYS   B 108 ? 1.4058 1.3456 0.4517 0.4525  0.0162  -0.0160 123 LYS   B CD  
1397 C CE  . LYS   B 108 ? 1.4939 1.3997 0.5002 0.4762  0.0017  -0.0246 123 LYS   B CE  
1398 N NZ  . LYS   B 108 ? 1.5544 1.4718 0.5424 0.5064  -0.0001 -0.0232 123 LYS   B NZ  
1399 N N   . THR   B 109 ? 1.1945 1.1315 0.3471 0.3275  0.0376  -0.0162 124 THR   B N   
1400 C CA  . THR   B 109 ? 1.2068 1.1520 0.3767 0.3068  0.0439  -0.0132 124 THR   B CA  
1401 C C   . THR   B 109 ? 1.2346 1.1516 0.3841 0.3060  0.0357  -0.0186 124 THR   B C   
1402 O O   . THR   B 109 ? 1.2382 1.1240 0.3629 0.3162  0.0240  -0.0260 124 THR   B O   
1403 C CB  . THR   B 109 ? 1.1848 1.1325 0.3826 0.2812  0.0491  -0.0146 124 THR   B CB  
1404 O OG1 . THR   B 109 ? 1.1922 1.1080 0.3850 0.2680  0.0412  -0.0237 124 THR   B OG1 
1405 C CG2 . THR   B 109 ? 1.1782 1.1413 0.3897 0.2836  0.0532  -0.0124 124 THR   B CG2 
1406 N N   . LYS   B 110 ? 1.2465 1.1734 0.4061 0.2936  0.0411  -0.0149 125 LYS   B N   
1407 C CA  . LYS   B 110 ? 1.2915 1.1951 0.4353 0.2897  0.0350  -0.0186 125 LYS   B CA  
1408 C C   . LYS   B 110 ? 1.3174 1.1882 0.4606 0.2720  0.0275  -0.0273 125 LYS   B C   
1409 O O   . LYS   B 110 ? 1.3766 1.2176 0.4980 0.2732  0.0178  -0.0322 125 LYS   B O   
1410 C CB  . LYS   B 110 ? 1.2746 1.2013 0.4345 0.2783  0.0442  -0.0119 125 LYS   B CB  
1411 C CG  . LYS   B 110 ? 1.2576 1.1928 0.4470 0.2515  0.0513  -0.0114 125 LYS   B CG  
1412 C CD  . LYS   B 110 ? 1.2622 1.2207 0.4675 0.2408  0.0601  -0.0048 125 LYS   B CD  
1413 C CE  . LYS   B 110 ? 1.2586 1.2072 0.4786 0.2156  0.0618  -0.0082 125 LYS   B CE  
1414 N NZ  . LYS   B 110 ? 1.2577 1.2053 0.4967 0.2011  0.0639  -0.0114 125 LYS   B NZ  
1415 N N   . ASP   B 111 ? 1.2767 1.1530 0.4421 0.2565  0.0313  -0.0287 126 ASP   B N   
1416 C CA  . ASP   B 111 ? 1.2785 1.1286 0.4459 0.2399  0.0246  -0.0363 126 ASP   B CA  
1417 C C   . ASP   B 111 ? 1.3069 1.1392 0.4599 0.2524  0.0156  -0.0417 126 ASP   B C   
1418 O O   . ASP   B 111 ? 1.3305 1.1441 0.4863 0.2397  0.0099  -0.0475 126 ASP   B O   
1419 C CB  . ASP   B 111 ? 1.2502 1.1165 0.4489 0.2174  0.0334  -0.0353 126 ASP   B CB  
1420 C CG  . ASP   B 111 ? 1.2362 1.1133 0.4486 0.2013  0.0403  -0.0320 126 ASP   B CG  
1421 O OD1 . ASP   B 111 ? 1.2227 1.1010 0.4232 0.2087  0.0402  -0.0289 126 ASP   B OD1 
1422 O OD2 . ASP   B 111 ? 1.2622 1.1456 0.4959 0.1822  0.0451  -0.0329 126 ASP   B OD2 
1423 N N   . GLY   B 112 ? 1.3011 1.1405 0.4395 0.2763  0.0144  -0.0396 127 GLY   B N   
1424 C CA  . GLY   B 112 ? 1.3180 1.1365 0.4366 0.2914  0.0039  -0.0454 127 GLY   B CA  
1425 C C   . GLY   B 112 ? 1.2999 1.1415 0.4302 0.3009  0.0098  -0.0424 127 GLY   B C   
1426 O O   . GLY   B 112 ? 1.2593 1.1330 0.4137 0.2947  0.0219  -0.0354 127 GLY   B O   
1427 N N   . ASP   B 113 ? 1.3189 1.1425 0.4322 0.3145  0.0005  -0.0478 128 ASP   B N   
1428 C CA  . ASP   B 113 ? 1.3192 1.1593 0.4338 0.3308  0.0031  -0.0458 128 ASP   B CA  
1429 C C   . ASP   B 113 ? 1.2855 1.1309 0.4244 0.3141  0.0066  -0.0477 128 ASP   B C   
1430 O O   . ASP   B 113 ? 1.2790 1.1006 0.4187 0.2990  -0.0005 -0.0546 128 ASP   B O   
1431 C CB  . ASP   B 113 ? 1.3649 1.1802 0.4462 0.3549  -0.0096 -0.0515 128 ASP   B CB  
1432 C CG  . ASP   B 113 ? 1.4101 1.2297 0.4674 0.3794  -0.0111 -0.0482 128 ASP   B CG  
1433 O OD1 . ASP   B 113 ? 1.4467 1.2876 0.5134 0.3759  -0.0024 -0.0414 128 ASP   B OD1 
1434 O OD2 . ASP   B 113 ? 1.4746 1.2761 0.5032 0.4025  -0.0213 -0.0527 128 ASP   B OD2 
1435 N N   . ILE   B 114 ? 1.2524 1.1281 0.4089 0.3181  0.0164  -0.0415 129 ILE   B N   
1436 C CA  . ILE   B 114 ? 1.2064 1.0909 0.3857 0.3056  0.0206  -0.0424 129 ILE   B CA  
1437 C C   . ILE   B 114 ? 1.1728 1.0685 0.3457 0.3262  0.0207  -0.0403 129 ILE   B C   
1438 O O   . ILE   B 114 ? 1.1526 1.0705 0.3220 0.3412  0.0264  -0.0328 129 ILE   B O   
1439 C CB  . ILE   B 114 ? 1.1608 1.0732 0.3705 0.2879  0.0336  -0.0355 129 ILE   B CB  
1440 C CG1 . ILE   B 114 ? 1.1934 1.1105 0.4050 0.2796  0.0374  -0.0319 129 ILE   B CG1 
1441 C CG2 . ILE   B 114 ? 1.1522 1.0605 0.3819 0.2682  0.0346  -0.0399 129 ILE   B CG2 
1442 C CD1 . ILE   B 114 ? 1.1730 1.1118 0.4135 0.2591  0.0485  -0.0267 129 ILE   B CD1 
1443 N N   . GLY   B 115 ? 1.1564 1.0411 0.3313 0.3247  0.0159  -0.0460 130 GLY   B N   
1444 C CA  . GLY   B 115 ? 1.1517 1.0504 0.3271 0.3399  0.0179  -0.0436 130 GLY   B CA  
1445 C C   . GLY   B 115 ? 1.1124 1.0477 0.3114 0.3365  0.0318  -0.0331 130 GLY   B C   
1446 O O   . GLY   B 115 ? 1.0882 1.0348 0.3092 0.3164  0.0394  -0.0299 130 GLY   B O   
1447 N N   . ALA   B 116 ? 1.1070 1.0613 0.3004 0.3560  0.0350  -0.0271 131 ALA   B N   
1448 C CA  . ALA   B 116 ? 1.0826 1.0723 0.2969 0.3536  0.0473  -0.0158 131 ALA   B CA  
1449 C C   . ALA   B 116 ? 1.0806 1.0811 0.2924 0.3691  0.0478  -0.0134 131 ALA   B C   
1450 O O   . ALA   B 116 ? 1.1066 1.0993 0.2945 0.3917  0.0412  -0.0159 131 ALA   B O   
1451 C CB  . ALA   B 116 ? 1.0832 1.0937 0.2940 0.3606  0.0530  -0.0068 131 ALA   B CB  
1452 N N   A VAL   B 117 ? 1.0597 1.0769 0.2942 0.3583  0.0551  -0.0088 132 VAL   B N   
1453 N N   B VAL   B 117 ? 1.0610 1.0783 0.2956 0.3581  0.0552  -0.0087 132 VAL   B N   
1454 N N   C VAL   B 117 ? 1.0596 1.0768 0.2941 0.3583  0.0551  -0.0088 132 VAL   B N   
1455 N N   D VAL   B 117 ? 1.0609 1.0783 0.2956 0.3581  0.0552  -0.0087 132 VAL   B N   
1456 C CA  A VAL   B 117 ? 1.0685 1.0977 0.3032 0.3712  0.0565  -0.0056 132 VAL   B CA  
1457 C CA  B VAL   B 117 ? 1.0701 1.0998 0.3061 0.3701  0.0569  -0.0053 132 VAL   B CA  
1458 C CA  C VAL   B 117 ? 1.0685 1.0976 0.3032 0.3712  0.0565  -0.0056 132 VAL   B CA  
1459 C CA  D VAL   B 117 ? 1.0701 1.0998 0.3061 0.3701  0.0569  -0.0053 132 VAL   B CA  
1460 C C   A VAL   B 117 ? 1.0557 1.1214 0.3021 0.3750  0.0673  0.0089  132 VAL   B C   
1461 C C   B VAL   B 117 ? 1.0573 1.1235 0.3037 0.3749  0.0675  0.0091  132 VAL   B C   
1462 C C   C VAL   B 117 ? 1.0557 1.1214 0.3021 0.3750  0.0673  0.0089  132 VAL   B C   
1463 C C   D VAL   B 117 ? 1.0574 1.1235 0.3037 0.3749  0.0675  0.0091  132 VAL   B C   
1464 O O   A VAL   B 117 ? 1.0321 1.1114 0.3002 0.3564  0.0748  0.0147  132 VAL   B O   
1465 O O   B VAL   B 117 ? 1.0342 1.1145 0.3015 0.3568  0.0750  0.0153  132 VAL   B O   
1466 O O   C VAL   B 117 ? 1.0321 1.1114 0.3001 0.3564  0.0748  0.0147  132 VAL   B O   
1467 O O   D VAL   B 117 ? 1.0342 1.1145 0.3015 0.3568  0.0750  0.0153  132 VAL   B O   
1468 C CB  A VAL   B 117 ? 1.0604 1.0781 0.3094 0.3576  0.0551  -0.0118 132 VAL   B CB  
1469 C CB  B VAL   B 117 ? 1.0617 1.0817 0.3143 0.3546  0.0564  -0.0109 132 VAL   B CB  
1470 C CB  C VAL   B 117 ? 1.0604 1.0781 0.3094 0.3576  0.0551  -0.0118 132 VAL   B CB  
1471 C CB  D VAL   B 117 ? 1.0617 1.0817 0.3143 0.3546  0.0564  -0.0109 132 VAL   B CB  
1472 C CG1 A VAL   B 117 ? 1.0768 1.0608 0.3151 0.3525  0.0441  -0.0252 132 VAL   B CG1 
1473 C CG1 B VAL   B 117 ? 1.0505 1.0939 0.3175 0.3564  0.0638  -0.0026 132 VAL   B CG1 
1474 C CG1 C VAL   B 117 ? 1.0769 1.0608 0.3151 0.3525  0.0441  -0.0252 132 VAL   B CG1 
1475 C CG1 D VAL   B 117 ? 1.0505 1.0939 0.3175 0.3563  0.0638  -0.0026 132 VAL   B CG1 
1476 C CG2 A VAL   B 117 ? 1.0300 1.0613 0.3070 0.3348  0.0638  -0.0071 132 VAL   B CG2 
1477 C CG2 B VAL   B 117 ? 1.0806 1.0709 0.3173 0.3605  0.0448  -0.0232 132 VAL   B CG2 
1478 C CG2 C VAL   B 117 ? 1.0299 1.0612 0.3068 0.3348  0.0638  -0.0071 132 VAL   B CG2 
1479 C CG2 D VAL   B 117 ? 1.0806 1.0709 0.3173 0.3606  0.0448  -0.0232 132 VAL   B CG2 
1480 N N   . ALA   B 118 ? 1.0671 1.1481 0.2987 0.3984  0.0676  0.0147  133 ALA   B N   
1481 C CA  . ALA   B 118 ? 1.0677 1.1863 0.3083 0.4042  0.0773  0.0299  133 ALA   B CA  
1482 C C   . ALA   B 118 ? 1.0806 1.2102 0.3326 0.4042  0.0807  0.0340  133 ALA   B C   
1483 O O   . ALA   B 118 ? 1.0758 1.2079 0.3132 0.4245  0.0778  0.0340  133 ALA   B O   
1484 C CB  . ALA   B 118 ? 1.0949 1.2267 0.3129 0.4303  0.0760  0.0344  133 ALA   B CB  
1485 N N   . LEU   B 119 ? 1.0618 1.1926 0.3372 0.3820  0.0852  0.0355  134 LEU   B N   
1486 C CA  . LEU   B 119 ? 1.0426 1.1814 0.3313 0.3781  0.0884  0.0392  134 LEU   B CA  
1487 C C   . LEU   B 119 ? 1.0358 1.1909 0.3491 0.3564  0.0965  0.0483  134 LEU   B C   
1488 O O   . LEU   B 119 ? 1.0481 1.1905 0.3713 0.3378  0.0963  0.0431  134 LEU   B O   
1489 C CB  . LEU   B 119 ? 1.0521 1.1613 0.3396 0.3730  0.0812  0.0253  134 LEU   B CB  
1490 C CG  . LEU   B 119 ? 1.0734 1.1635 0.3366 0.3934  0.0718  0.0158  134 LEU   B CG  
1491 C CD1 . LEU   B 119 ? 1.0675 1.1296 0.3330 0.3839  0.0647  0.0027  134 LEU   B CD1 
1492 C CD2 . LEU   B 119 ? 1.0964 1.2049 0.3495 0.4157  0.0733  0.0231  134 LEU   B CD2 
1493 N N   . ASP   B 120 ? 1.0313 1.2140 0.3531 0.3587  0.1031  0.0620  135 ASP   B N   
1494 C CA  . ASP   B 120 ? 1.0322 1.2328 0.3755 0.3396  0.1103  0.0731  135 ASP   B CA  
1495 C C   . ASP   B 120 ? 1.0098 1.2010 0.3670 0.3275  0.1106  0.0709  135 ASP   B C   
1496 O O   . ASP   B 120 ? 1.0274 1.2200 0.3795 0.3390  0.1095  0.0714  135 ASP   B O   
1497 C CB  . ASP   B 120 ? 1.0758 1.3122 0.4189 0.3496  0.1163  0.0902  135 ASP   B CB  
1498 C CG  . ASP   B 120 ? 1.1034 1.3581 0.4597 0.3344  0.1216  0.1003  135 ASP   B CG  
1499 O OD1 . ASP   B 120 ? 1.0831 1.3310 0.4568 0.3127  0.1233  0.1003  135 ASP   B OD1 
1500 O OD2 . ASP   B 120 ? 1.1485 1.4237 0.4966 0.3453  0.1236  0.1077  135 ASP   B OD2 
1501 N N   A TYR   B 121 ? 0.9918 1.1731 0.3649 0.3056  0.1118  0.0679  136 TYR   B N   
1502 N N   B TYR   B 121 ? 0.9917 1.1730 0.3648 0.3056  0.1118  0.0679  136 TYR   B N   
1503 N N   C TYR   B 121 ? 0.9921 1.1741 0.3654 0.3056  0.1119  0.0683  136 TYR   B N   
1504 N N   D TYR   B 121 ? 0.9920 1.1740 0.3653 0.3056  0.1119  0.0683  136 TYR   B N   
1505 C CA  A TYR   B 121 ? 0.9847 1.1586 0.3724 0.2925  0.1126  0.0669  136 TYR   B CA  
1506 C CA  B TYR   B 121 ? 0.9846 1.1585 0.3723 0.2925  0.1126  0.0669  136 TYR   B CA  
1507 C CA  C TYR   B 121 ? 0.9859 1.1593 0.3731 0.2928  0.1124  0.0666  136 TYR   B CA  
1508 C CA  D TYR   B 121 ? 0.9858 1.1592 0.3731 0.2929  0.1124  0.0666  136 TYR   B CA  
1509 C C   A TYR   B 121 ? 0.9716 1.1503 0.3766 0.2708  0.1166  0.0724  136 TYR   B C   
1510 C C   B TYR   B 121 ? 0.9716 1.1502 0.3765 0.2708  0.1166  0.0724  136 TYR   B C   
1511 C C   C TYR   B 121 ? 0.9724 1.1504 0.3773 0.2710  0.1165  0.0721  136 TYR   B C   
1512 C C   D TYR   B 121 ? 0.9724 1.1504 0.3772 0.2710  0.1165  0.0721  136 TYR   B C   
1513 O O   A TYR   B 121 ? 0.9729 1.1548 0.3787 0.2645  0.1178  0.0733  136 TYR   B O   
1514 O O   B TYR   B 121 ? 0.9729 1.1548 0.3787 0.2645  0.1178  0.0733  136 TYR   B O   
1515 O O   C TYR   B 121 ? 0.9736 1.1550 0.3796 0.2643  0.1177  0.0732  136 TYR   B O   
1516 O O   D TYR   B 121 ? 0.9736 1.1551 0.3797 0.2643  0.1177  0.0732  136 TYR   B O   
1517 C CB  A TYR   B 121 ? 0.9900 1.1358 0.3748 0.2911  0.1066  0.0507  136 TYR   B CB  
1518 C CB  B TYR   B 121 ? 0.9899 1.1357 0.3747 0.2911  0.1066  0.0507  136 TYR   B CB  
1519 C CB  C TYR   B 121 ? 0.9924 1.1375 0.3761 0.2919  0.1063  0.0502  136 TYR   B CB  
1520 C CB  D TYR   B 121 ? 0.9923 1.1374 0.3760 0.2919  0.1063  0.0502  136 TYR   B CB  
1521 C CG  A TYR   B 121 ? 1.0122 1.1522 0.3823 0.3106  0.1021  0.0459  136 TYR   B CG  
1522 C CG  B TYR   B 121 ? 1.0122 1.1522 0.3823 0.3106  0.1021  0.0459  136 TYR   B CG  
1523 C CG  C TYR   B 121 ? 1.0148 1.1540 0.3844 0.3110  0.1018  0.0454  136 TYR   B CG  
1524 C CG  D TYR   B 121 ? 1.0148 1.1540 0.3843 0.3110  0.1018  0.0454  136 TYR   B CG  
1525 C CD1 A TYR   B 121 ? 1.0177 1.1638 0.3903 0.3164  0.1031  0.0502  136 TYR   B CD1 
1526 C CD1 B TYR   B 121 ? 1.0177 1.1638 0.3903 0.3164  0.1031  0.0502  136 TYR   B CD1 
1527 C CD1 C TYR   B 121 ? 1.0201 1.1668 0.3927 0.3165  0.1032  0.0505  136 TYR   B CD1 
1528 C CD1 D TYR   B 121 ? 1.0201 1.1668 0.3927 0.3165  0.1032  0.0505  136 TYR   B CD1 
1529 C CD2 A TYR   B 121 ? 1.0291 1.1567 0.3814 0.3238  0.0963  0.0372  136 TYR   B CD2 
1530 C CD2 B TYR   B 121 ? 1.0291 1.1567 0.3814 0.3238  0.0963  0.0372  136 TYR   B CD2 
1531 C CD2 C TYR   B 121 ? 1.0321 1.1573 0.3841 0.3238  0.0956  0.0359  136 TYR   B CD2 
1532 C CD2 D TYR   B 121 ? 1.0321 1.1573 0.3841 0.3238  0.0956  0.0359  136 TYR   B CD2 
1533 C CE1 A TYR   B 121 ? 1.0323 1.1734 0.3908 0.3349  0.0988  0.0458  136 TYR   B CE1 
1534 C CE1 B TYR   B 121 ? 1.0323 1.1734 0.3908 0.3349  0.0988  0.0458  136 TYR   B CE1 
1535 C CE1 C TYR   B 121 ? 1.0348 1.1764 0.3940 0.3345  0.0990  0.0461  136 TYR   B CE1 
1536 C CE1 D TYR   B 121 ? 1.0348 1.1764 0.3940 0.3345  0.0990  0.0461  136 TYR   B CE1 
1537 C CE2 A TYR   B 121 ? 1.0472 1.1682 0.3846 0.3422  0.0913  0.0325  136 TYR   B CE2 
1538 C CE2 B TYR   B 121 ? 1.0472 1.1683 0.3846 0.3422  0.0913  0.0325  136 TYR   B CE2 
1539 C CE2 C TYR   B 121 ? 1.0502 1.1687 0.3880 0.3417  0.0907  0.0312  136 TYR   B CE2 
1540 C CE2 D TYR   B 121 ? 1.0502 1.1688 0.3881 0.3417  0.0907  0.0312  136 TYR   B CE2 
1541 C CZ  A TYR   B 121 ? 1.0473 1.1758 0.3880 0.3480  0.0927  0.0367  136 TYR   B CZ  
1542 C CZ  B TYR   B 121 ? 1.0473 1.1759 0.3881 0.3480  0.0927  0.0367  136 TYR   B CZ  
1543 C CZ  C TYR   B 121 ? 1.0501 1.1775 0.3917 0.3473  0.0926  0.0362  136 TYR   B CZ  
1544 C CZ  D TYR   B 121 ? 1.0501 1.1776 0.3917 0.3473  0.0926  0.0362  136 TYR   B CZ  
1545 O OH  A TYR   B 121 ? 1.0681 1.1902 0.3936 0.3666  0.0876  0.0319  136 TYR   B OH  
1546 O OH  B TYR   B 121 ? 1.0682 1.1903 0.3937 0.3666  0.0876  0.0319  136 TYR   B OH  
1547 O OH  C TYR   B 121 ? 1.0716 1.1926 0.3988 0.3653  0.0876  0.0315  136 TYR   B OH  
1548 O OH  D TYR   B 121 ? 1.0717 1.1927 0.3989 0.3653  0.0875  0.0315  136 TYR   B OH  
1549 N N   A PRO   B 122 ? 0.9644 1.1423 0.3826 0.2591  0.1183  0.0759  137 PRO   B N   
1550 N N   B PRO   B 122 ? 0.9643 1.1422 0.3825 0.2591  0.1183  0.0759  137 PRO   B N   
1551 N N   C PRO   B 122 ? 0.9655 1.1423 0.3833 0.2597  0.1180  0.0752  137 PRO   B N   
1552 N N   D PRO   B 122 ? 0.9655 1.1422 0.3832 0.2597  0.1180  0.0752  137 PRO   B N   
1553 C CA  A PRO   B 122 ? 0.9558 1.1347 0.3890 0.2386  0.1209  0.0802  137 PRO   B CA  
1554 C CA  B PRO   B 122 ? 0.9558 1.1348 0.3890 0.2386  0.1209  0.0802  137 PRO   B CA  
1555 C CA  C PRO   B 122 ? 0.9565 1.1344 0.3894 0.2392  0.1207  0.0796  137 PRO   B CA  
1556 C CA  D PRO   B 122 ? 0.9565 1.1344 0.3894 0.2392  0.1207  0.0796  137 PRO   B CA  
1557 C C   A PRO   B 122 ? 0.9437 1.1023 0.3794 0.2271  0.1185  0.0670  137 PRO   B C   
1558 C C   B PRO   B 122 ? 0.9438 1.1023 0.3794 0.2271  0.1185  0.0670  137 PRO   B C   
1559 C C   C PRO   B 122 ? 0.9443 1.1021 0.3798 0.2276  0.1183  0.0666  137 PRO   B C   
1560 C C   D PRO   B 122 ? 0.9444 1.1022 0.3799 0.2276  0.1183  0.0666  137 PRO   B C   
1561 O O   A PRO   B 122 ? 0.9470 1.0874 0.3767 0.2316  0.1144  0.0542  137 PRO   B O   
1562 O O   B PRO   B 122 ? 0.9471 1.0875 0.3768 0.2316  0.1144  0.0542  137 PRO   B O   
1563 O O   C PRO   B 122 ? 0.9469 1.0864 0.3769 0.2317  0.1142  0.0538  137 PRO   B O   
1564 O O   D PRO   B 122 ? 0.9470 1.0864 0.3770 0.2317  0.1142  0.0538  137 PRO   B O   
1565 C CB  A PRO   B 122 ? 0.9598 1.1345 0.4025 0.2315  0.1211  0.0829  137 PRO   B CB  
1566 C CB  B PRO   B 122 ? 0.9599 1.1346 0.4026 0.2315  0.1211  0.0829  137 PRO   B CB  
1567 C CB  C PRO   B 122 ? 0.9613 1.1346 0.4031 0.2330  0.1207  0.0819  137 PRO   B CB  
1568 C CB  D PRO   B 122 ? 0.9613 1.1347 0.4032 0.2330  0.1207  0.0819  137 PRO   B CB  
1569 C CG  A PRO   B 122 ? 0.9696 1.1493 0.4030 0.2496  0.1202  0.0847  137 PRO   B CG  
1570 C CG  B PRO   B 122 ? 0.9696 1.1494 0.4030 0.2496  0.1202  0.0847  137 PRO   B CG  
1571 C CG  C PRO   B 122 ? 0.9715 1.1511 0.4036 0.2516  0.1199  0.0842  137 PRO   B CG  
1572 C CG  D PRO   B 122 ? 0.9715 1.1511 0.4036 0.2516  0.1199  0.0842  137 PRO   B CG  
1573 C CD  A PRO   B 122 ? 0.9784 1.1530 0.3966 0.2654  0.1172  0.0758  137 PRO   B CD  
1574 C CD  B PRO   B 122 ? 0.9785 1.1530 0.3967 0.2654  0.1172  0.0758  137 PRO   B CD  
1575 C CD  C PRO   B 122 ? 0.9799 1.1525 0.3972 0.2665  0.1167  0.0744  137 PRO   B CD  
1576 C CD  D PRO   B 122 ? 0.9800 1.1526 0.3973 0.2665  0.1167  0.0744  137 PRO   B CD  
1577 N N   A ALA   B 123 ? 0.9264 1.0892 0.3708 0.2124  0.1208  0.0710  138 ALA   B N   
1578 N N   B ALA   B 123 ? 0.9265 1.0892 0.3708 0.2124  0.1208  0.0710  138 ALA   B N   
1579 N N   C ALA   B 123 ? 0.9268 1.0891 0.3704 0.2135  0.1206  0.0706  138 ALA   B N   
1580 N N   D ALA   B 123 ? 0.9268 1.0892 0.3704 0.2135  0.1206  0.0706  138 ALA   B N   
1581 C CA  A ALA   B 123 ? 0.9108 1.0576 0.3589 0.1997  0.1194  0.0606  138 ALA   B CA  
1582 C CA  B ALA   B 123 ? 0.9108 1.0576 0.3589 0.1997  0.1194  0.0606  138 ALA   B CA  
1583 C CA  C ALA   B 123 ? 0.9113 1.0577 0.3583 0.2012  0.1191  0.0601  138 ALA   B CA  
1584 C CA  D ALA   B 123 ? 0.9113 1.0577 0.3583 0.2012  0.1191  0.0601  138 ALA   B CA  
1585 C C   A ALA   B 123 ? 0.9015 1.0266 0.3539 0.1937  0.1163  0.0479  138 ALA   B C   
1586 C C   B ALA   B 123 ? 0.9016 1.0266 0.3540 0.1937  0.1163  0.0479  138 ALA   B C   
1587 C C   C ALA   B 123 ? 0.9020 1.0268 0.3539 0.1944  0.1162  0.0477  138 ALA   B C   
1588 C C   D ALA   B 123 ? 0.9020 1.0269 0.3539 0.1944  0.1162  0.0477  138 ALA   B C   
1589 O O   A ALA   B 123 ? 0.8855 0.9953 0.3356 0.1901  0.1137  0.0362  138 ALA   B O   
1590 O O   B ALA   B 123 ? 0.8853 0.9952 0.3355 0.1901  0.1137  0.0362  138 ALA   B O   
1591 O O   C ALA   B 123 ? 0.8865 0.9961 0.3364 0.1905  0.1136  0.0360  138 ALA   B O   
1592 O O   D ALA   B 123 ? 0.8864 0.9960 0.3363 0.1905  0.1136  0.0360  138 ALA   B O   
1593 C CB  A ALA   B 123 ? 0.9051 1.0612 0.3638 0.1840  0.1224  0.0688  138 ALA   B CB  
1594 C CB  B ALA   B 123 ? 0.9051 1.0612 0.3639 0.1840  0.1224  0.0688  138 ALA   B CB  
1595 C CB  C ALA   B 123 ? 0.9052 1.0610 0.3624 0.1858  0.1222  0.0681  138 ALA   B CB  
1596 C CB  D ALA   B 123 ? 0.9052 1.0610 0.3624 0.1858  0.1222  0.0681  138 ALA   B CB  
1597 N N   . GLY   B 124 ? 0.8924 1.0168 0.3501 0.1935  0.1164  0.0505  139 GLY   B N   
1598 C CA  . GLY   B 124 ? 0.8737 0.9803 0.3361 0.1887  0.1137  0.0396  139 GLY   B CA  
1599 C C   . GLY   B 124 ? 0.8436 0.9392 0.2966 0.2007  0.1097  0.0286  139 GLY   B C   
1600 O O   . GLY   B 124 ? 0.8335 0.9146 0.2903 0.1964  0.1071  0.0181  139 GLY   B O   
1601 N N   . THR   B 125 ? 0.8401 0.9418 0.2808 0.2148  0.1087  0.0305  140 THR   B N   
1602 C CA  . THR   B 125 ? 0.8564 0.9458 0.2853 0.2265  0.1036  0.0200  140 THR   B CA  
1603 C C   . THR   B 125 ? 0.8558 0.9323 0.2811 0.2203  0.1007  0.0103  140 THR   B C   
1604 O O   . THR   B 125 ? 0.8613 0.9242 0.2773 0.2272  0.0951  0.0006  140 THR   B O   
1605 C CB  . THR   B 125 ? 0.8802 0.9801 0.2954 0.2460  0.1029  0.0260  140 THR   B CB  
1606 O OG1 . THR   B 125 ? 0.8873 1.0006 0.3066 0.2502  0.1060  0.0361  140 THR   B OG1 
1607 C CG2 . THR   B 125 ? 0.8874 0.9737 0.2894 0.2595  0.0966  0.0158  140 THR   B CG2 
1608 N N   A SER   B 126 ? 0.8469 0.9269 0.2785 0.2079  0.1037  0.0131  141 SER   B N   
1609 N N   B SER   B 126 ? 0.8469 0.9269 0.2786 0.2079  0.1037  0.0131  141 SER   B N   
1610 N N   C SER   B 126 ? 0.8472 0.9273 0.2787 0.2081  0.1037  0.0131  141 SER   B N   
1611 N N   D SER   B 126 ? 0.8472 0.9273 0.2787 0.2081  0.1037  0.0131  141 SER   B N   
1612 C CA  A SER   B 126 ? 0.8428 0.9121 0.2714 0.2008  0.1016  0.0056  141 SER   B CA  
1613 C CA  B SER   B 126 ? 0.8428 0.9121 0.2714 0.2008  0.1016  0.0056  141 SER   B CA  
1614 C CA  C SER   B 126 ? 0.8435 0.9127 0.2716 0.2014  0.1015  0.0055  141 SER   B CA  
1615 C CA  D SER   B 126 ? 0.8435 0.9127 0.2716 0.2014  0.1015  0.0055  141 SER   B CA  
1616 C C   A SER   B 126 ? 0.8369 0.8887 0.2687 0.1943  0.0975  -0.0073 141 SER   B C   
1617 C C   B SER   B 126 ? 0.8368 0.8886 0.2687 0.1943  0.0975  -0.0073 141 SER   B C   
1618 C C   C SER   B 126 ? 0.8370 0.8889 0.2687 0.1946  0.0974  -0.0072 141 SER   B C   
1619 C C   D SER   B 126 ? 0.8370 0.8888 0.2687 0.1946  0.0974  -0.0072 141 SER   B C   
1620 O O   A SER   B 126 ? 0.8367 0.8874 0.2805 0.1863  0.0989  -0.0092 141 SER   B O   
1621 O O   B SER   B 126 ? 0.8368 0.8874 0.2806 0.1863  0.0989  -0.0092 141 SER   B O   
1622 O O   C SER   B 126 ? 0.8368 0.8877 0.2804 0.1868  0.0989  -0.0089 141 SER   B O   
1623 O O   D SER   B 126 ? 0.8368 0.8877 0.2804 0.1868  0.0989  -0.0089 141 SER   B O   
1624 C CB  A SER   B 126 ? 0.8349 0.9113 0.2726 0.1868  0.1059  0.0106  141 SER   B CB  
1625 C CB  B SER   B 126 ? 0.8349 0.9112 0.2726 0.1868  0.1059  0.0106  141 SER   B CB  
1626 C CB  C SER   B 126 ? 0.8362 0.9124 0.2727 0.1879  0.1057  0.0105  141 SER   B CB  
1627 C CB  D SER   B 126 ? 0.8362 0.9124 0.2727 0.1879  0.1057  0.0105  141 SER   B CB  
1628 O OG  A SER   B 126 ? 0.8367 0.9291 0.2693 0.1931  0.1087  0.0214  141 SER   B OG  
1629 O OG  B SER   B 126 ? 0.8367 0.9291 0.2693 0.1931  0.1087  0.0214  141 SER   B OG  
1630 O OG  C SER   B 126 ? 0.8389 0.9310 0.2699 0.1948  0.1083  0.0211  141 SER   B OG  
1631 O OG  D SER   B 126 ? 0.8389 0.9310 0.2699 0.1948  0.1083  0.0211  141 SER   B OG  
1632 N N   . GLY   B 127 ? 0.8434 0.8825 0.2634 0.1993  0.0919  -0.0152 142 GLY   B N   
1633 C CA  . GLY   B 127 ? 0.8465 0.8707 0.2692 0.1924  0.0873  -0.0268 142 GLY   B CA  
1634 C C   . GLY   B 127 ? 0.8628 0.8789 0.2757 0.2051  0.0813  -0.0320 142 GLY   B C   
1635 O O   . GLY   B 127 ? 0.8698 0.8734 0.2824 0.2007  0.0762  -0.0414 142 GLY   B O   
1636 N N   . SER   B 128 ? 0.8671 0.8913 0.2731 0.2200  0.0820  -0.0256 143 SER   B N   
1637 C CA  . SER   B 128 ? 0.8796 0.8968 0.2746 0.2343  0.0762  -0.0299 143 SER   B CA  
1638 C C   . SER   B 128 ? 0.8903 0.8909 0.2689 0.2393  0.0682  -0.0373 143 SER   B C   
1639 O O   . SER   B 128 ? 0.9042 0.9042 0.2736 0.2417  0.0680  -0.0346 143 SER   B O   
1640 C CB  . SER   B 128 ? 0.8854 0.9159 0.2741 0.2502  0.0787  -0.0206 143 SER   B CB  
1641 O OG  . SER   B 128 ? 0.8753 0.9167 0.2773 0.2465  0.0838  -0.0151 143 SER   B OG  
1642 N N   . PRO   B 129 ? 0.8887 0.8754 0.2635 0.2400  0.0610  -0.0465 144 PRO   B N   
1643 C CA  . PRO   B 129 ? 0.9036 0.8715 0.2634 0.2420  0.0520  -0.0541 144 PRO   B CA  
1644 C C   . PRO   B 129 ? 0.9382 0.9001 0.2763 0.2623  0.0464  -0.0532 144 PRO   B C   
1645 O O   . PRO   B 129 ? 0.9566 0.9264 0.2916 0.2759  0.0474  -0.0498 144 PRO   B O   
1646 C CB  . PRO   B 129 ? 0.9026 0.8603 0.2675 0.2355  0.0461  -0.0633 144 PRO   B CB  
1647 C CG  . PRO   B 129 ? 0.8909 0.8609 0.2666 0.2397  0.0505  -0.0607 144 PRO   B CG  
1648 C CD  . PRO   B 129 ? 0.8808 0.8677 0.2668 0.2362  0.0605  -0.0509 144 PRO   B CD  
1649 N N   . ILE   B 130 ? 0.9463 0.8926 0.2690 0.2638  0.0398  -0.0570 145 ILE   B N   
1650 C CA  . ILE   B 130 ? 0.9750 0.9103 0.2732 0.2832  0.0323  -0.0581 145 ILE   B CA  
1651 C C   . ILE   B 130 ? 1.0045 0.9155 0.2930 0.2800  0.0205  -0.0687 145 ILE   B C   
1652 O O   . ILE   B 130 ? 0.9779 0.8814 0.2753 0.2620  0.0190  -0.0728 145 ILE   B O   
1653 C CB  . ILE   B 130 ? 0.9767 0.9138 0.2641 0.2878  0.0341  -0.0532 145 ILE   B CB  
1654 C CG1 . ILE   B 130 ? 0.9637 0.9274 0.2633 0.2885  0.0458  -0.0420 145 ILE   B CG1 
1655 C CG2 . ILE   B 130 ? 1.0075 0.9309 0.2676 0.3085  0.0254  -0.0554 145 ILE   B CG2 
1656 C CD1 . ILE   B 130 ? 0.9702 0.9382 0.2683 0.2836  0.0493  -0.0375 145 ILE   B CD1 
1657 N N   . LEU   B 131 ? 1.0353 0.9374 0.3094 0.2957  0.0131  -0.0722 146 LEU   B N   
1658 C CA  . LEU   B 131 ? 1.0751 0.9552 0.3407 0.2937  0.0010  -0.0820 146 LEU   B CA  
1659 C C   . LEU   B 131 ? 1.1082 0.9663 0.3441 0.3104  -0.0105 -0.0858 146 LEU   B C   
1660 O O   . LEU   B 131 ? 1.1193 0.9844 0.3421 0.3299  -0.0084 -0.0810 146 LEU   B O   
1661 C CB  . LEU   B 131 ? 1.1038 0.9913 0.3769 0.2992  0.0013  -0.0836 146 LEU   B CB  
1662 C CG  . LEU   B 131 ? 1.0943 1.0054 0.3922 0.2908  0.0132  -0.0781 146 LEU   B CG  
1663 C CD1 . LEU   B 131 ? 1.1131 1.0272 0.4152 0.2970  0.0113  -0.0809 146 LEU   B CD1 
1664 C CD2 . LEU   B 131 ? 1.0940 1.0073 0.4104 0.2678  0.0169  -0.0797 146 LEU   B CD2 
1665 N N   . ASP   B 132 ? 1.1301 0.9634 0.3566 0.3023  -0.0226 -0.0940 147 ASP   B N   
1666 C CA  . ASP   B 132 ? 1.1812 0.9878 0.3782 0.3171  -0.0370 -0.0998 147 ASP   B CA  
1667 C C   . ASP   B 132 ? 1.2136 1.0162 0.4071 0.3266  -0.0433 -0.1046 147 ASP   B C   
1668 O O   . ASP   B 132 ? 1.1873 1.0083 0.4021 0.3204  -0.0361 -0.1032 147 ASP   B O   
1669 C CB  . ASP   B 132 ? 1.1914 0.9716 0.3778 0.3039  -0.0478 -0.1051 147 ASP   B CB  
1670 C CG  . ASP   B 132 ? 1.1893 0.9632 0.3907 0.2814  -0.0525 -0.1104 147 ASP   B CG  
1671 O OD1 . ASP   B 132 ? 1.1787 0.9613 0.3926 0.2794  -0.0519 -0.1125 147 ASP   B OD1 
1672 O OD2 . ASP   B 132 ? 1.2221 0.9846 0.4240 0.2652  -0.0559 -0.1115 147 ASP   B OD2 
1673 N N   . LYS   B 133 ? 1.2700 1.0484 0.4370 0.3409  -0.0569 -0.1103 148 LYS   B N   
1674 C CA  . LYS   B 133 ? 1.3240 1.0967 0.4830 0.3535  -0.0642 -0.1151 148 LYS   B CA  
1675 C C   . LYS   B 133 ? 1.3105 1.0778 0.4852 0.3335  -0.0695 -0.1210 148 LYS   B C   
1676 O O   . LYS   B 133 ? 1.3040 1.0758 0.4828 0.3387  -0.0714 -0.1236 148 LYS   B O   
1677 C CB  . LYS   B 133 ? 1.3950 1.1415 0.5190 0.3752  -0.0781 -0.1199 148 LYS   B CB  
1678 C CG  . LYS   B 133 ? 1.4407 1.1987 0.5494 0.4005  -0.0724 -0.1140 148 LYS   B CG  
1679 C CD  . LYS   B 133 ? 1.5069 1.2388 0.5813 0.4171  -0.0838 -0.1172 148 LYS   B CD  
1680 C CE  . LYS   B 133 ? 1.5255 1.2754 0.5892 0.4393  -0.0753 -0.1097 148 LYS   B CE  
1681 N NZ  . LYS   B 133 ? 1.5728 1.2979 0.5996 0.4617  -0.0875 -0.1139 148 LYS   B NZ  
1682 N N   . CYS   B 134 ? 1.2875 1.0488 0.4723 0.3112  -0.0708 -0.1222 149 CYS   B N   
1683 C CA  . CYS   B 134 ? 1.2773 1.0375 0.4788 0.2908  -0.0751 -0.1269 149 CYS   B CA  
1684 C C   . CYS   B 134 ? 1.2181 1.0089 0.4512 0.2789  -0.0600 -0.1225 149 CYS   B C   
1685 O O   . CYS   B 134 ? 1.2095 1.0048 0.4590 0.2631  -0.0612 -0.1256 149 CYS   B O   
1686 C CB  . CYS   B 134 ? 1.3118 1.0508 0.5075 0.2729  -0.0848 -0.1301 149 CYS   B CB  
1687 S SG  . CYS   B 134 ? 1.3818 1.0797 0.5411 0.2834  -0.1071 -0.1375 149 CYS   B SG  
1688 N N   . GLY   B 135 ? 1.1817 0.9930 0.4226 0.2869  -0.0466 -0.1154 150 GLY   B N   
1689 C CA  . GLY   B 135 ? 1.1368 0.9748 0.4058 0.2761  -0.0328 -0.1109 150 GLY   B CA  
1690 C C   . GLY   B 135 ? 1.1068 0.9508 0.3910 0.2555  -0.0266 -0.1087 150 GLY   B C   
1691 O O   . GLY   B 135 ? 1.0757 0.9392 0.3819 0.2459  -0.0166 -0.1060 150 GLY   B O   
1692 N N   . ARG   B 136 ? 1.1169 0.9441 0.3888 0.2496  -0.0326 -0.1098 151 ARG   B N   
1693 C CA  . ARG   B 136 ? 1.1090 0.9400 0.3926 0.2305  -0.0275 -0.1077 151 ARG   B CA  
1694 C C   . ARG   B 136 ? 1.0663 0.9130 0.3545 0.2351  -0.0151 -0.0999 151 ARG   B C   
1695 O O   . ARG   B 136 ? 1.0664 0.9102 0.3379 0.2530  -0.0153 -0.0968 151 ARG   B O   
1696 C CB  . ARG   B 136 ? 1.1500 0.9549 0.4162 0.2237  -0.0400 -0.1116 151 ARG   B CB  
1697 C CG  . ARG   B 136 ? 1.1773 0.9721 0.4473 0.2099  -0.0503 -0.1179 151 ARG   B CG  
1698 C CD  . ARG   B 136 ? 1.2319 0.9991 0.4829 0.2031  -0.0636 -0.1209 151 ARG   B CD  
1699 N NE  . ARG   B 136 ? 1.2973 1.0440 0.5197 0.2240  -0.0717 -0.1220 151 ARG   B NE  
1700 C CZ  . ARG   B 136 ? 1.3410 1.0649 0.5415 0.2267  -0.0794 -0.1221 151 ARG   B CZ  
1701 N NH1 . ARG   B 136 ? 1.3844 1.1022 0.5881 0.2089  -0.0802 -0.1209 151 ARG   B NH1 
1702 N NH2 . ARG   B 136 ? 1.3827 1.0902 0.5572 0.2484  -0.0863 -0.1235 151 ARG   B NH2 
1703 N N   . VAL   B 137 ? 1.0317 0.8956 0.3415 0.2203  -0.0049 -0.0968 152 VAL   B N   
1704 C CA  . VAL   B 137 ? 0.9995 0.8794 0.3157 0.2223  0.0068  -0.0890 152 VAL   B CA  
1705 C C   . VAL   B 137 ? 1.0114 0.8790 0.3144 0.2196  0.0040  -0.0878 152 VAL   B C   
1706 O O   . VAL   B 137 ? 1.0128 0.8738 0.3208 0.2024  0.0019  -0.0903 152 VAL   B O   
1707 C CB  . VAL   B 137 ? 0.9718 0.8722 0.3136 0.2082  0.0177  -0.0863 152 VAL   B CB  
1708 C CG1 . VAL   B 137 ? 0.9669 0.8827 0.3134 0.2117  0.0283  -0.0780 152 VAL   B CG1 
1709 C CG2 . VAL   B 137 ? 0.9595 0.8699 0.3146 0.2085  0.0195  -0.0885 152 VAL   B CG2 
1710 N N   . ILE   B 138 ? 1.0105 0.8770 0.2977 0.2359  0.0046  -0.0837 153 ILE   B N   
1711 C CA  . ILE   B 138 ? 1.0280 0.8821 0.2994 0.2370  0.0014  -0.0825 153 ILE   B CA  
1712 C C   . ILE   B 138 ? 0.9984 0.8720 0.2817 0.2325  0.0134  -0.0749 153 ILE   B C   
1713 O O   . ILE   B 138 ? 1.0253 0.8911 0.2973 0.2324  0.0121  -0.0732 153 ILE   B O   
1714 C CB  . ILE   B 138 ? 1.0518 0.8912 0.2953 0.2594  -0.0067 -0.0833 153 ILE   B CB  
1715 C CG1 . ILE   B 138 ? 1.0493 0.9084 0.2929 0.2780  0.0004  -0.0772 153 ILE   B CG1 
1716 C CG2 . ILE   B 138 ? 1.0705 0.8844 0.2989 0.2612  -0.0211 -0.0915 153 ILE   B CG2 
1717 C CD1 . ILE   B 138 ? 1.0884 0.9383 0.3047 0.3014  -0.0052 -0.0763 153 ILE   B CD1 
1718 N N   . GLY   B 139 ? 0.9745 0.8710 0.2774 0.2299  0.0239  -0.0701 154 GLY   B N   
1719 C CA  . GLY   B 139 ? 0.9563 0.8712 0.2725 0.2229  0.0349  -0.0629 154 GLY   B CA  
1720 C C   . GLY   B 139 ? 0.9385 0.8759 0.2713 0.2248  0.0443  -0.0571 154 GLY   B C   
1721 O O   . GLY   B 139 ? 0.9269 0.8658 0.2594 0.2337  0.0425  -0.0585 154 GLY   B O   
1722 N N   . LEU   B 140 ? 0.9157 0.8693 0.2606 0.2179  0.0534  -0.0503 155 LEU   B N   
1723 C CA  . LEU   B 140 ? 0.9078 0.8820 0.2680 0.2182  0.0621  -0.0435 155 LEU   B CA  
1724 C C   . LEU   B 140 ? 0.9146 0.9040 0.2694 0.2291  0.0673  -0.0335 155 LEU   B C   
1725 O O   . LEU   B 140 ? 0.9090 0.8968 0.2553 0.2296  0.0672  -0.0314 155 LEU   B O   
1726 C CB  . LEU   B 140 ? 0.8848 0.8660 0.2655 0.1991  0.0681  -0.0437 155 LEU   B CB  
1727 C CG  . LEU   B 140 ? 0.8823 0.8534 0.2712 0.1860  0.0645  -0.0527 155 LEU   B CG  
1728 C CD1 . LEU   B 140 ? 0.8744 0.8565 0.2828 0.1710  0.0718  -0.0512 155 LEU   B CD1 
1729 C CD2 . LEU   B 140 ? 0.8997 0.8658 0.2876 0.1927  0.0596  -0.0578 155 LEU   B CD2 
1730 N N   A TYR   B 141 ? 0.9075 0.9118 0.2666 0.2379  0.0715  -0.0272 156 TYR   B N   
1731 N N   B TYR   B 141 ? 0.9074 0.9117 0.2666 0.2379  0.0715  -0.0272 156 TYR   B N   
1732 N N   C TYR   B 141 ? 0.9097 0.9148 0.2699 0.2370  0.0720  -0.0269 156 TYR   B N   
1733 N N   D TYR   B 141 ? 0.9097 0.9147 0.2699 0.2370  0.0720  -0.0269 156 TYR   B N   
1734 C CA  A TYR   B 141 ? 0.9075 0.9323 0.2655 0.2477  0.0776  -0.0156 156 TYR   B CA  
1735 C CA  B TYR   B 141 ? 0.9075 0.9323 0.2655 0.2477  0.0776  -0.0156 156 TYR   B CA  
1736 C CA  C TYR   B 141 ? 0.9119 0.9368 0.2698 0.2473  0.0777  -0.0155 156 TYR   B CA  
1737 C CA  D TYR   B 141 ? 0.9119 0.9367 0.2698 0.2473  0.0777  -0.0155 156 TYR   B CA  
1738 C C   A TYR   B 141 ? 0.8952 0.9346 0.2715 0.2322  0.0856  -0.0089 156 TYR   B C   
1739 C C   B TYR   B 141 ? 0.8952 0.9346 0.2715 0.2322  0.0856  -0.0089 156 TYR   B C   
1740 C C   C TYR   B 141 ? 0.8992 0.9399 0.2760 0.2326  0.0859  -0.0083 156 TYR   B C   
1741 C C   D TYR   B 141 ? 0.8992 0.9398 0.2760 0.2326  0.0859  -0.0083 156 TYR   B C   
1742 O O   A TYR   B 141 ? 0.8934 0.9293 0.2845 0.2179  0.0871  -0.0128 156 TYR   B O   
1743 O O   B TYR   B 141 ? 0.8935 0.9293 0.2845 0.2179  0.0871  -0.0128 156 TYR   B O   
1744 O O   C TYR   B 141 ? 0.8974 0.9362 0.2889 0.2204  0.0877  -0.0112 156 TYR   B O   
1745 O O   D TYR   B 141 ? 0.8974 0.9363 0.2889 0.2204  0.0877  -0.0112 156 TYR   B O   
1746 C CB  A TYR   B 141 ? 0.9150 0.9486 0.2715 0.2612  0.0781  -0.0120 156 TYR   B CB  
1747 C CB  B TYR   B 141 ? 0.9150 0.9486 0.2715 0.2612  0.0781  -0.0120 156 TYR   B CB  
1748 C CB  C TYR   B 141 ? 0.9245 0.9569 0.2778 0.2631  0.0773  -0.0123 156 TYR   B CB  
1749 C CB  D TYR   B 141 ? 0.9246 0.9569 0.2779 0.2631  0.0773  -0.0123 156 TYR   B CB  
1750 C CG  A TYR   B 141 ? 0.9110 0.9682 0.2673 0.2714  0.0842  0.0007  156 TYR   B CG  
1751 C CG  B TYR   B 141 ? 0.9109 0.9682 0.2673 0.2714  0.0842  0.0007  156 TYR   B CG  
1752 C CG  C TYR   B 141 ? 0.9198 0.9764 0.2746 0.2723  0.0839  0.0005  156 TYR   B CG  
1753 C CG  D TYR   B 141 ? 0.9198 0.9764 0.2745 0.2723  0.0839  0.0005  156 TYR   B CG  
1754 C CD1 A TYR   B 141 ? 0.8973 0.9714 0.2703 0.2632  0.0912  0.0093  156 TYR   B CD1 
1755 C CD1 B TYR   B 141 ? 0.8973 0.9714 0.2703 0.2632  0.0912  0.0093  156 TYR   B CD1 
1756 C CD1 C TYR   B 141 ? 0.9061 0.9786 0.2784 0.2627  0.0908  0.0084  156 TYR   B CD1 
1757 C CD1 D TYR   B 141 ? 0.9061 0.9786 0.2784 0.2627  0.0908  0.0084  156 TYR   B CD1 
1758 C CD2 A TYR   B 141 ? 0.9232 0.9863 0.2619 0.2899  0.0826  0.0047  156 TYR   B CD2 
1759 C CD2 B TYR   B 141 ? 0.9232 0.9863 0.2619 0.2899  0.0826  0.0047  156 TYR   B CD2 
1760 C CD2 C TYR   B 141 ? 0.9322 0.9962 0.2699 0.2912  0.0826  0.0052  156 TYR   B CD2 
1761 C CD2 D TYR   B 141 ? 0.9322 0.9962 0.2699 0.2912  0.0826  0.0052  156 TYR   B CD2 
1762 C CE1 A TYR   B 141 ? 0.8967 0.9939 0.2701 0.2712  0.0965  0.0222  156 TYR   B CE1 
1763 C CE1 B TYR   B 141 ? 0.8967 0.9939 0.2701 0.2712  0.0965  0.0222  156 TYR   B CE1 
1764 C CE1 C TYR   B 141 ? 0.9046 1.0003 0.2786 0.2697  0.0963  0.0214  156 TYR   B CE1 
1765 C CE1 D TYR   B 141 ? 0.9046 1.0003 0.2786 0.2698  0.0963  0.0214  156 TYR   B CE1 
1766 C CE2 A TYR   B 141 ? 0.9234 1.0115 0.2624 0.2995  0.0884  0.0173  156 TYR   B CE2 
1767 C CE2 B TYR   B 141 ? 0.9234 1.0115 0.2624 0.2995  0.0884  0.0173  156 TYR   B CE2 
1768 C CE2 C TYR   B 141 ? 0.9316 1.0210 0.2711 0.2997  0.0887  0.0179  156 TYR   B CE2 
1769 C CE2 D TYR   B 141 ? 0.9316 1.0210 0.2710 0.2997  0.0887  0.0179  156 TYR   B CE2 
1770 C CZ  A TYR   B 141 ? 0.9101 1.0160 0.2670 0.2895  0.0954  0.0265  156 TYR   B CZ  
1771 C CZ  B TYR   B 141 ? 0.9101 1.0160 0.2670 0.2895  0.0954  0.0265  156 TYR   B CZ  
1772 C CZ  C TYR   B 141 ? 0.9180 1.0238 0.2762 0.2883  0.0956  0.0265  156 TYR   B CZ  
1773 C CZ  D TYR   B 141 ? 0.9180 1.0239 0.2762 0.2883  0.0956  0.0265  156 TYR   B CZ  
1774 O OH  A TYR   B 141 ? 0.9070 1.0389 0.2646 0.2979  0.1008  0.0400  156 TYR   B OH  
1775 O OH  B TYR   B 141 ? 0.9070 1.0389 0.2646 0.2979  0.1008  0.0400  156 TYR   B OH  
1776 O OH  C TYR   B 141 ? 0.9152 1.0471 0.2752 0.2958  0.1012  0.0402  156 TYR   B OH  
1777 O OH  D TYR   B 141 ? 0.9152 1.0471 0.2752 0.2958  0.1012  0.0402  156 TYR   B OH  
1778 N N   A GLY   B 142 ? 0.9003 0.9558 0.2755 0.2352  0.0902  0.0006  157 GLY   B N   
1779 N N   B GLY   B 142 ? 0.9003 0.9557 0.2755 0.2352  0.0902  0.0006  157 GLY   B N   
1780 N N   C GLY   B 142 ? 0.9036 0.9591 0.2797 0.2340  0.0905  0.0006  157 GLY   B N   
1781 N N   D GLY   B 142 ? 0.9036 0.9591 0.2797 0.2340  0.0905  0.0006  157 GLY   B N   
1782 C CA  A GLY   B 142 ? 0.8928 0.9646 0.2848 0.2223  0.0975  0.0090  157 GLY   B CA  
1783 C CA  B GLY   B 142 ? 0.8928 0.9646 0.2847 0.2223  0.0975  0.0090  157 GLY   B CA  
1784 C CA  C GLY   B 142 ? 0.8958 0.9665 0.2889 0.2202  0.0976  0.0084  157 GLY   B CA  
1785 C CA  D GLY   B 142 ? 0.8958 0.9665 0.2889 0.2202  0.0976  0.0084  157 GLY   B CA  
1786 C C   A GLY   B 142 ? 0.8956 0.9716 0.2884 0.2141  0.0999  0.0120  157 GLY   B C   
1787 C C   B GLY   B 142 ? 0.8956 0.9717 0.2885 0.2141  0.0999  0.0120  157 GLY   B C   
1788 C C   C GLY   B 142 ? 0.8995 0.9762 0.2921 0.2142  0.1000  0.0124  157 GLY   B C   
1789 C C   D GLY   B 142 ? 0.8995 0.9762 0.2921 0.2142  0.1000  0.0124  157 GLY   B C   
1790 O O   A GLY   B 142 ? 0.8884 0.9773 0.2948 0.2028  0.1053  0.0190  157 GLY   B O   
1791 O O   B GLY   B 142 ? 0.8884 0.9774 0.2948 0.2028  0.1053  0.0190  157 GLY   B O   
1792 O O   C GLY   B 142 ? 0.8943 0.9862 0.2991 0.2050  0.1056  0.0208  157 GLY   B O   
1793 O O   D GLY   B 142 ? 0.8944 0.9863 0.2992 0.2050  0.1056  0.0207  157 GLY   B O   
1794 N N   A ASN   B 143 ? 0.9094 0.9742 0.2882 0.2189  0.0956  0.0070  158 ASN   B N   
1795 N N   B ASN   B 143 ? 0.9094 0.9742 0.2882 0.2189  0.0956  0.0070  158 ASN   B N   
1796 N N   C ASN   B 143 ? 0.9123 0.9766 0.2913 0.2183  0.0956  0.0068  158 ASN   B N   
1797 N N   D ASN   B 143 ? 0.9124 0.9766 0.2913 0.2183  0.0956  0.0068  158 ASN   B N   
1798 C CA  A ASN   B 143 ? 0.9099 0.9799 0.2870 0.2141  0.0977  0.0106  158 ASN   B CA  
1799 C CA  B ASN   B 143 ? 0.9099 0.9799 0.2870 0.2141  0.0977  0.0106  158 ASN   B CA  
1800 C CA  C ASN   B 143 ? 0.9128 0.9821 0.2894 0.2141  0.0975  0.0102  158 ASN   B CA  
1801 C CA  D ASN   B 143 ? 0.9128 0.9821 0.2893 0.2141  0.0975  0.0102  158 ASN   B CA  
1802 C C   A ASN   B 143 ? 0.9264 1.0009 0.2841 0.2332  0.0953  0.0140  158 ASN   B C   
1803 C C   B ASN   B 143 ? 0.9264 1.0009 0.2841 0.2332  0.0953  0.0140  158 ASN   B C   
1804 C C   C ASN   B 143 ? 0.9281 1.0026 0.2855 0.2336  0.0952  0.0140  158 ASN   B C   
1805 C C   D ASN   B 143 ? 0.9281 1.0026 0.2855 0.2336  0.0952  0.0140  158 ASN   B C   
1806 O O   A ASN   B 143 ? 0.9488 1.0039 0.2895 0.2424  0.0881  0.0058  158 ASN   B O   
1807 O O   B ASN   B 143 ? 0.9489 1.0039 0.2895 0.2424  0.0881  0.0058  158 ASN   B O   
1808 O O   C ASN   B 143 ? 0.9508 1.0063 0.2909 0.2435  0.0881  0.0060  158 ASN   B O   
1809 O O   D ASN   B 143 ? 0.9508 1.0064 0.2910 0.2435  0.0881  0.0060  158 ASN   B O   
1810 C CB  A ASN   B 143 ? 0.9107 0.9622 0.2890 0.2000  0.0949  0.0015  158 ASN   B CB  
1811 C CB  B ASN   B 143 ? 0.9107 0.9622 0.2890 0.2000  0.0949  0.0015  158 ASN   B CB  
1812 C CB  C ASN   B 143 ? 0.9149 0.9649 0.2915 0.2008  0.0943  0.0009  158 ASN   B CB  
1813 C CB  D ASN   B 143 ? 0.9149 0.9649 0.2915 0.2008  0.0943  0.0009  158 ASN   B CB  
1814 C CG  A ASN   B 143 ? 0.9072 0.9664 0.2891 0.1910  0.0985  0.0059  158 ASN   B CG  
1815 C CG  B ASN   B 143 ? 0.9072 0.9664 0.2891 0.1910  0.0985  0.0059  158 ASN   B CG  
1816 C CG  C ASN   B 143 ? 0.9129 0.9698 0.2921 0.1923  0.0976  0.0050  158 ASN   B CG  
1817 C CG  D ASN   B 143 ? 0.9129 0.9698 0.2922 0.1923  0.0976  0.0050  158 ASN   B CG  
1818 O OD1 A ASN   B 143 ? 0.9009 0.9804 0.2905 0.1898  0.1040  0.0158  158 ASN   B OD1 
1819 O OD1 B ASN   B 143 ? 0.9010 0.9804 0.2906 0.1897  0.1040  0.0158  158 ASN   B OD1 
1820 O OD1 C ASN   B 143 ? 0.9072 0.9843 0.2936 0.1914  0.1030  0.0148  158 ASN   B OD1 
1821 O OD1 D ASN   B 143 ? 0.9072 0.9843 0.2936 0.1914  0.1031  0.0148  158 ASN   B OD1 
1822 N ND2 A ASN   B 143 ? 0.9094 0.9529 0.2858 0.1841  0.0952  -0.0009 158 ASN   B ND2 
1823 N ND2 B ASN   B 143 ? 0.9094 0.9529 0.2858 0.1841  0.0952  -0.0009 158 ASN   B ND2 
1824 N ND2 C ASN   B 143 ? 0.9156 0.9562 0.2890 0.1857  0.0940  -0.0020 158 ASN   B ND2 
1825 N ND2 D ASN   B 143 ? 0.9156 0.9562 0.2890 0.1857  0.0940  -0.0020 158 ASN   B ND2 
1826 N N   . GLY   B 144 ? 0.9232 1.0223 0.2831 0.2385  0.1006  0.0258  159 GLY   B N   
1827 C CA  . GLY   B 144 ? 0.9562 1.0644 0.2980 0.2587  0.0991  0.0303  159 GLY   B CA  
1828 C C   . GLY   B 144 ? 0.9754 1.1136 0.3237 0.2597  0.1057  0.0438  159 GLY   B C   
1829 O O   . GLY   B 144 ? 0.9493 1.0938 0.3116 0.2430  0.1096  0.0471  159 GLY   B O   
1830 N N   . VAL   B 145 ? 1.0014 1.1583 0.3395 0.2789  0.1067  0.0516  160 VAL   B N   
1831 C CA  . VAL   B 145 ? 1.0231 1.2099 0.3625 0.2836  0.1118  0.0644  160 VAL   B CA  
1832 C C   . VAL   B 145 ? 1.0669 1.2808 0.4061 0.2978  0.1154  0.0759  160 VAL   B C   
1833 O O   . VAL   B 145 ? 1.0921 1.2982 0.4209 0.3121  0.1121  0.0719  160 VAL   B O   
1834 C CB  . VAL   B 145 ? 1.0425 1.2218 0.3623 0.2959  0.1078  0.0603  160 VAL   B CB  
1835 C CG1 . VAL   B 145 ? 1.0462 1.2231 0.3424 0.3226  0.1032  0.0582  160 VAL   B CG1 
1836 C CG2 . VAL   B 145 ? 1.0540 1.2577 0.3797 0.2917  0.1128  0.0704  160 VAL   B CG2 
1837 N N   . VAL   B 146 ? 1.0901 1.3354 0.4401 0.2941  0.1215  0.0901  161 VAL   B N   
1838 C CA  . VAL   B 146 ? 1.1442 1.4219 0.4934 0.3082  0.1255  0.1038  161 VAL   B CA  
1839 C C   . VAL   B 146 ? 1.1900 1.4829 0.5207 0.3296  0.1248  0.1071  161 VAL   B C   
1840 O O   . VAL   B 146 ? 1.1910 1.4879 0.5212 0.3253  0.1254  0.1080  161 VAL   B O   
1841 C CB  . VAL   B 146 ? 1.1276 1.4311 0.4989 0.2910  0.1317  0.1181  161 VAL   B CB  
1842 C CG1 . VAL   B 146 ? 1.1586 1.4935 0.5303 0.3036  0.1355  0.1322  161 VAL   B CG1 
1843 C CG2 . VAL   B 146 ? 1.1173 1.4005 0.5046 0.2697  0.1313  0.1126  161 VAL   B CG2 
1844 N N   A ILE   B 147 ? 1.2213 1.5229 0.5364 0.3532  0.1235  0.1088  162 ILE   B N   
1845 N N   B ILE   B 147 ? 1.2212 1.5228 0.5363 0.3532  0.1235  0.1088  162 ILE   B N   
1846 N N   C ILE   B 147 ? 1.2203 1.5212 0.5354 0.3532  0.1234  0.1085  162 ILE   B N   
1847 N N   D ILE   B 147 ? 1.2202 1.5211 0.5353 0.3532  0.1234  0.1086  162 ILE   B N   
1848 C CA  A ILE   B 147 ? 1.2569 1.5687 0.5495 0.3785  0.1214  0.1096  162 ILE   B CA  
1849 C CA  B ILE   B 147 ? 1.2567 1.5685 0.5493 0.3785  0.1214  0.1096  162 ILE   B CA  
1850 C CA  C ILE   B 147 ? 1.2545 1.5683 0.5478 0.3784  0.1218  0.1105  162 ILE   B CA  
1851 C CA  D ILE   B 147 ? 1.2543 1.5682 0.5477 0.3784  0.1218  0.1105  162 ILE   B CA  
1852 C C   A ILE   B 147 ? 1.2793 1.6377 0.5761 0.3887  0.1282  0.1276  162 ILE   B C   
1853 C C   B ILE   B 147 ? 1.2793 1.6377 0.5761 0.3887  0.1282  0.1276  162 ILE   B C   
1854 C C   C ILE   B 147 ? 1.2728 1.6336 0.5730 0.3856  0.1290  0.1291  162 ILE   B C   
1855 C C   D ILE   B 147 ? 1.2727 1.6336 0.5730 0.3855  0.1290  0.1291  162 ILE   B C   
1856 O O   A ILE   B 147 ? 1.2570 1.6354 0.5729 0.3761  0.1334  0.1386  162 ILE   B O   
1857 O O   B ILE   B 147 ? 1.2568 1.6352 0.5727 0.3762  0.1334  0.1386  162 ILE   B O   
1858 O O   C ILE   B 147 ? 1.2500 1.6284 0.5704 0.3707  0.1340  0.1393  162 ILE   B O   
1859 O O   D ILE   B 147 ? 1.2499 1.6283 0.5703 0.3707  0.1340  0.1393  162 ILE   B O   
1860 C CB  A ILE   B 147 ? 1.2832 1.5697 0.5523 0.3996  0.1141  0.0976  162 ILE   B CB  
1861 C CB  B ILE   B 147 ? 1.2831 1.5696 0.5522 0.3996  0.1141  0.0977  162 ILE   B CB  
1862 C CB  C ILE   B 147 ? 1.2828 1.5746 0.5525 0.4011  0.1149  0.0997  162 ILE   B CB  
1863 C CB  D ILE   B 147 ? 1.2828 1.5745 0.5524 0.4011  0.1149  0.0997  162 ILE   B CB  
1864 C CG1 A ILE   B 147 ? 1.2833 1.5794 0.5543 0.4081  0.1155  0.1019  162 ILE   B CG1 
1865 C CG1 B ILE   B 147 ? 1.2829 1.5791 0.5540 0.4081  0.1155  0.1019  162 ILE   B CG1 
1866 C CG1 C ILE   B 147 ? 1.2795 1.5791 0.5531 0.4067  0.1164  0.1036  162 ILE   B CG1 
1867 C CG1 D ILE   B 147 ? 1.2792 1.5789 0.5528 0.4068  0.1164  0.1036  162 ILE   B CG1 
1868 C CG2 A ILE   B 147 ? 1.2815 1.5241 0.5464 0.3884  0.1070  0.0809  162 ILE   B CG2 
1869 C CG2 B ILE   B 147 ? 1.2813 1.5240 0.5463 0.3883  0.1070  0.0809  162 ILE   B CG2 
1870 C CG2 C ILE   B 147 ? 1.2850 1.5323 0.5466 0.3935  0.1071  0.0824  162 ILE   B CG2 
1871 C CG2 D ILE   B 147 ? 1.2849 1.5322 0.5465 0.3935  0.1071  0.0824  162 ILE   B CG2 
1872 C CD1 A ILE   B 147 ? 1.3024 1.5731 0.5505 0.4282  0.1077  0.0900  162 ILE   B CD1 
1873 C CD1 B ILE   B 147 ? 1.3020 1.5726 0.5501 0.4283  0.1077  0.0899  162 ILE   B CD1 
1874 C CD1 C ILE   B 147 ? 1.2973 1.5720 0.5488 0.4266  0.1089  0.0919  162 ILE   B CD1 
1875 C CD1 D ILE   B 147 ? 1.2970 1.5716 0.5484 0.4266  0.1088  0.0918  162 ILE   B CD1 
1876 N N   A LYS   B 148 ? 1.3236 1.6985 0.6027 0.4105  0.1276  0.1307  163 LYS   B N   
1877 N N   B LYS   B 148 ? 1.3236 1.6985 0.6027 0.4105  0.1276  0.1307  163 LYS   B N   
1878 N N   C LYS   B 148 ? 1.3139 1.6943 0.5974 0.4076  0.1290  0.1333  163 LYS   B N   
1879 N N   D LYS   B 148 ? 1.3140 1.6943 0.5974 0.4076  0.1290  0.1334  163 LYS   B N   
1880 C CA  A LYS   B 148 ? 1.3532 1.7760 0.6332 0.4240  0.1337  0.1480  163 LYS   B CA  
1881 C CA  B LYS   B 148 ? 1.3533 1.7761 0.6333 0.4240  0.1337  0.1480  163 LYS   B CA  
1882 C CA  C LYS   B 148 ? 1.3371 1.7666 0.6255 0.4164  0.1357  0.1517  163 LYS   B CA  
1883 C CA  D LYS   B 148 ? 1.3372 1.7667 0.6256 0.4164  0.1357  0.1517  163 LYS   B CA  
1884 C C   A LYS   B 148 ? 1.3524 1.7960 0.6463 0.4204  0.1384  0.1590  163 LYS   B C   
1885 C C   B LYS   B 148 ? 1.3526 1.7962 0.6465 0.4204  0.1384  0.1590  163 LYS   B C   
1886 C C   C LYS   B 148 ? 1.3425 1.7921 0.6393 0.4189  0.1395  0.1617  163 LYS   B C   
1887 C C   D LYS   B 148 ? 1.3427 1.7923 0.6395 0.4189  0.1395  0.1618  163 LYS   B C   
1888 O O   A LYS   B 148 ? 1.3540 1.8282 0.6681 0.4055  0.1445  0.1740  163 LYS   B O   
1889 O O   B LYS   B 148 ? 1.3544 1.8286 0.6685 0.4055  0.1445  0.1740  163 LYS   B O   
1890 O O   C LYS   B 148 ? 1.3504 1.8374 0.6636 0.4110  0.1459  0.1787  163 LYS   B O   
1891 O O   D LYS   B 148 ? 1.3508 1.8378 0.6640 0.4110  0.1459  0.1787  163 LYS   B O   
1892 C CB  A LYS   B 148 ? 1.3902 1.8189 0.6416 0.4574  0.1303  0.1454  163 LYS   B CB  
1893 C CB  B LYS   B 148 ? 1.3902 1.8189 0.6416 0.4574  0.1303  0.1454  163 LYS   B CB  
1894 C CB  C LYS   B 148 ? 1.3657 1.8085 0.6291 0.4460  0.1338  0.1519  163 LYS   B CB  
1895 C CB  D LYS   B 148 ? 1.3657 1.8085 0.6291 0.4460  0.1338  0.1519  163 LYS   B CB  
1896 C CG  A LYS   B 148 ? 1.4147 1.8296 0.6495 0.4653  0.1260  0.1375  163 LYS   B CG  
1897 C CG  B LYS   B 148 ? 1.4148 1.8297 0.6495 0.4654  0.1260  0.1375  163 LYS   B CG  
1898 C CG  C LYS   B 148 ? 1.3878 1.7975 0.6328 0.4515  0.1268  0.1371  163 LYS   B CG  
1899 C CG  D LYS   B 148 ? 1.3879 1.7975 0.6328 0.4515  0.1268  0.1371  163 LYS   B CG  
1900 C CD  A LYS   B 148 ? 1.4554 1.8727 0.6593 0.5000  0.1215  0.1341  163 LYS   B CD  
1901 C CD  B LYS   B 148 ? 1.4555 1.8728 0.6594 0.5000  0.1215  0.1341  163 LYS   B CD  
1902 C CD  C LYS   B 148 ? 1.4064 1.8400 0.6409 0.4650  0.1281  0.1429  163 LYS   B CD  
1903 C CD  D LYS   B 148 ? 1.4064 1.8400 0.6410 0.4650  0.1281  0.1429  163 LYS   B CD  
1904 C CE  A LYS   B 148 ? 1.4719 1.9412 0.6746 0.5190  0.1280  0.1509  163 LYS   B CE  
1905 C CE  B LYS   B 148 ? 1.4721 1.9414 0.6748 0.5190  0.1280  0.1509  163 LYS   B CE  
1906 C CE  C LYS   B 148 ? 1.4272 1.9026 0.6511 0.4918  0.1316  0.1553  163 LYS   B CE  
1907 C CE  D LYS   B 148 ? 1.4273 1.9027 0.6512 0.4918  0.1316  0.1553  163 LYS   B CE  
1908 N NZ  A LYS   B 148 ? 1.4746 1.9758 0.6849 0.5151  0.1328  0.1615  163 LYS   B NZ  
1909 N NZ  B LYS   B 148 ? 1.4749 1.9761 0.6852 0.5151  0.1328  0.1615  163 LYS   B NZ  
1910 N NZ  C LYS   B 148 ? 1.4343 1.9352 0.6502 0.5032  0.1332  0.1614  163 LYS   B NZ  
1911 N NZ  D LYS   B 148 ? 1.4344 1.9352 0.6503 0.5032  0.1332  0.1614  163 LYS   B NZ  
1912 N N   A ASN   B 149 ? 1.3588 1.7847 0.6415 0.4331  0.1348  0.1516  164 ASN   B N   
1913 N N   B ASN   B 149 ? 1.3590 1.7849 0.6417 0.4331  0.1348  0.1516  164 ASN   B N   
1914 N N   C ASN   B 149 ? 1.3480 1.7729 0.6339 0.4289  0.1351  0.1517  164 ASN   B N   
1915 N N   D ASN   B 149 ? 1.3482 1.7731 0.6341 0.4289  0.1351  0.1517  164 ASN   B N   
1916 C CA  A ASN   B 149 ? 1.3433 1.7840 0.6344 0.4339  0.1380  0.1599  164 ASN   B CA  
1917 C CA  B ASN   B 149 ? 1.3434 1.7841 0.6345 0.4339  0.1380  0.1599  164 ASN   B CA  
1918 C CA  C ASN   B 149 ? 1.3330 1.7707 0.6230 0.4343  0.1375  0.1585  164 ASN   B CA  
1919 C CA  D ASN   B 149 ? 1.3330 1.7708 0.6230 0.4343  0.1375  0.1586  164 ASN   B CA  
1920 C C   A ASN   B 149 ? 1.3019 1.7508 0.6214 0.4043  0.1428  0.1691  164 ASN   B C   
1921 C C   B ASN   B 149 ? 1.3019 1.7509 0.6215 0.4042  0.1428  0.1691  164 ASN   B C   
1922 C C   C ASN   B 149 ? 1.2975 1.7388 0.6148 0.4059  0.1416  0.1659  164 ASN   B C   
1923 C C   D ASN   B 149 ? 1.2976 1.7389 0.6148 0.4059  0.1416  0.1660  164 ASN   B C   
1924 O O   A ASN   B 149 ? 1.3241 1.8086 0.6550 0.4024  0.1485  0.1859  164 ASN   B O   
1925 O O   B ASN   B 149 ? 1.3246 1.8092 0.6555 0.4024  0.1485  0.1859  164 ASN   B O   
1926 O O   C ASN   B 149 ? 1.3149 1.7792 0.6400 0.4071  0.1455  0.1778  164 ASN   B O   
1927 O O   D ASN   B 149 ? 1.3152 1.7795 0.6403 0.4071  0.1455  0.1778  164 ASN   B O   
1928 C CB  A ASN   B 149 ? 1.3650 1.7705 0.6434 0.4429  0.1317  0.1454  164 ASN   B CB  
1929 C CB  B ASN   B 149 ? 1.3651 1.7706 0.6435 0.4429  0.1318  0.1454  164 ASN   B CB  
1930 C CB  C ASN   B 149 ? 1.3542 1.7576 0.6259 0.4491  0.1305  0.1433  164 ASN   B CB  
1931 C CB  D ASN   B 149 ? 1.3542 1.7577 0.6260 0.4491  0.1305  0.1433  164 ASN   B CB  
1932 C CG  A ASN   B 149 ? 1.3937 1.7797 0.6426 0.4690  0.1246  0.1330  164 ASN   B CG  
1933 C CG  B ASN   B 149 ? 1.3938 1.7799 0.6427 0.4689  0.1246  0.1330  164 ASN   B CG  
1934 C CG  C ASN   B 149 ? 1.3783 1.7676 0.6213 0.4744  0.1241  0.1330  164 ASN   B CG  
1935 C CG  D ASN   B 149 ? 1.3783 1.7676 0.6213 0.4744  0.1241  0.1330  164 ASN   B CG  
1936 O OD1 A ASN   B 149 ? 1.4164 1.8252 0.6506 0.4899  0.1254  0.1386  164 ASN   B OD1 
1937 O OD1 B ASN   B 149 ? 1.4167 1.8254 0.6508 0.4899  0.1254  0.1386  164 ASN   B OD1 
1938 O OD1 C ASN   B 149 ? 1.3761 1.7662 0.6136 0.4751  0.1234  0.1317  164 ASN   B OD1 
1939 O OD1 D ASN   B 149 ? 1.3760 1.7661 0.6135 0.4751  0.1234  0.1317  164 ASN   B OD1 
1940 N ND2 A ASN   B 149 ? 1.3975 1.7415 0.6370 0.4680  0.1170  0.1164  164 ASN   B ND2 
1941 N ND2 B ASN   B 149 ? 1.3975 1.7415 0.6370 0.4680  0.1170  0.1164  164 ASN   B ND2 
1942 N ND2 C ASN   B 149 ? 1.3930 1.7679 0.6164 0.4955  0.1189  0.1254  164 ASN   B ND2 
1943 N ND2 D ASN   B 149 ? 1.3930 1.7679 0.6163 0.4955  0.1189  0.1254  164 ASN   B ND2 
1944 N N   . GLY   B 150 ? 1.2663 1.6839 0.5960 0.3822  0.1402  0.1587  165 GLY   B N   
1945 C CA  . GLY   B 150 ? 1.1855 1.5985 0.5386 0.3554  0.1425  0.1625  165 GLY   B CA  
1946 C C   . GLY   B 150 ? 1.1355 1.5087 0.4873 0.3501  0.1376  0.1471  165 GLY   B C   
1947 O O   . GLY   B 150 ? 1.1030 1.4631 0.4722 0.3275  0.1382  0.1458  165 GLY   B O   
1948 N N   A SER   B 151 ? 1.1335 1.4875 0.4649 0.3702  0.1325  0.1354  166 SER   B N   
1949 N N   B SER   B 151 ? 1.1403 1.4945 0.4717 0.3703  0.1325  0.1354  166 SER   B N   
1950 N N   C SER   B 151 ? 1.1335 1.4876 0.4649 0.3703  0.1325  0.1354  166 SER   B N   
1951 N N   D SER   B 151 ? 1.1404 1.4946 0.4717 0.3703  0.1325  0.1354  166 SER   B N   
1952 C CA  A SER   B 151 ? 1.1241 1.4417 0.4514 0.3687  0.1269  0.1203  166 SER   B CA  
1953 C CA  B SER   B 151 ? 1.1353 1.4528 0.4620 0.3692  0.1268  0.1201  166 SER   B CA  
1954 C CA  C SER   B 151 ? 1.1244 1.4420 0.4516 0.3688  0.1269  0.1203  166 SER   B CA  
1955 C CA  D SER   B 151 ? 1.1356 1.4532 0.4623 0.3693  0.1269  0.1202  166 SER   B CA  
1956 C C   A SER   B 151 ? 1.1115 1.3960 0.4404 0.3535  0.1226  0.1061  166 SER   B C   
1957 C C   B SER   B 151 ? 1.1184 1.4029 0.4473 0.3534  0.1226  0.1061  166 SER   B C   
1958 C C   C SER   B 151 ? 1.1125 1.3972 0.4412 0.3537  0.1226  0.1062  166 SER   B C   
1959 C C   D SER   B 151 ? 1.1194 1.4041 0.4481 0.3537  0.1226  0.1062  166 SER   B C   
1960 O O   A SER   B 151 ? 1.1055 1.3944 0.4351 0.3478  0.1236  0.1073  166 SER   B O   
1961 O O   B SER   B 151 ? 1.1111 1.4000 0.4412 0.3472  0.1237  0.1074  166 SER   B O   
1962 O O   C SER   B 151 ? 1.1059 1.3950 0.4357 0.3477  0.1236  0.1074  166 SER   B O   
1963 O O   D SER   B 151 ? 1.1115 1.4006 0.4417 0.3471  0.1237  0.1075  166 SER   B O   
1964 C CB  A SER   B 151 ? 1.1410 1.4513 0.4453 0.3955  0.1223  0.1140  166 SER   B CB  
1965 C CB  B SER   B 151 ? 1.1590 1.4695 0.4622 0.3964  0.1222  0.1138  166 SER   B CB  
1966 C CB  C SER   B 151 ? 1.1411 1.4514 0.4454 0.3956  0.1223  0.1140  166 SER   B CB  
1967 C CB  D SER   B 151 ? 1.1592 1.4698 0.4624 0.3965  0.1222  0.1139  166 SER   B CB  
1968 O OG  A SER   B 151 ? 1.1353 1.4140 0.4377 0.3928  0.1171  0.1011  166 SER   B OG  
1969 O OG  B SER   B 151 ? 1.1797 1.4905 0.4641 0.4126  0.1194  0.1105  166 SER   B OG  
1970 O OG  C SER   B 151 ? 1.1351 1.4137 0.4375 0.3928  0.1171  0.1011  166 SER   B OG  
1971 O OG  D SER   B 151 ? 1.1800 1.4910 0.4645 0.4126  0.1194  0.1106  166 SER   B OG  
1972 N N   A TYR   B 152 ? 1.0945 1.3484 0.4243 0.3469  0.1182  0.0936  167 TYR   B N   
1973 N N   B TYR   B 152 ? 1.0968 1.3508 0.4266 0.3469  0.1182  0.0936  167 TYR   B N   
1974 N N   C TYR   B 152 ? 1.0979 1.3517 0.4257 0.3489  0.1178  0.0933  167 TYR   B N   
1975 N N   D TYR   B 152 ? 1.1002 1.3541 0.4281 0.3489  0.1179  0.0933  167 TYR   B N   
1976 C CA  A TYR   B 152 ? 1.0826 1.3055 0.4164 0.3301  0.1143  0.0804  167 TYR   B CA  
1977 C CA  B TYR   B 152 ? 1.0838 1.3067 0.4177 0.3301  0.1143  0.0804  167 TYR   B CA  
1978 C CA  C TYR   B 152 ? 1.0860 1.3097 0.4189 0.3313  0.1143  0.0806  167 TYR   B CA  
1979 C CA  D TYR   B 152 ? 1.0872 1.3110 0.4202 0.3313  0.1143  0.0806  167 TYR   B CA  
1980 C C   A TYR   B 152 ? 1.0817 1.2752 0.3947 0.3435  0.1060  0.0656  167 TYR   B C   
1981 C C   B TYR   B 152 ? 1.0821 1.2757 0.3951 0.3435  0.1060  0.0656  167 TYR   B C   
1982 C C   C TYR   B 152 ? 1.0832 1.2763 0.3962 0.3433  0.1059  0.0654  167 TYR   B C   
1983 C C   D TYR   B 152 ? 1.0837 1.2768 0.3967 0.3433  0.1059  0.0654  167 TYR   B C   
1984 O O   A TYR   B 152 ? 1.0708 1.2584 0.3730 0.3583  0.1026  0.0622  167 TYR   B O   
1985 O O   B TYR   B 152 ? 1.0708 1.2584 0.3729 0.3583  0.1026  0.0622  167 TYR   B O   
1986 O O   C TYR   B 152 ? 1.0710 1.2568 0.3740 0.3570  0.1024  0.0615  167 TYR   B O   
1987 O O   D TYR   B 152 ? 1.0710 1.2569 0.3740 0.3570  0.1024  0.0615  167 TYR   B O   
1988 C CB  A TYR   B 152 ? 1.0723 1.2852 0.4252 0.3103  0.1156  0.0784  167 TYR   B CB  
1989 C CB  B TYR   B 152 ? 1.0729 1.2858 0.4258 0.3103  0.1156  0.0784  167 TYR   B CB  
1990 C CB  C TYR   B 152 ? 1.0765 1.2932 0.4297 0.3108  0.1163  0.0802  167 TYR   B CB  
1991 C CB  D TYR   B 152 ? 1.0771 1.2939 0.4303 0.3108  0.1163  0.0802  167 TYR   B CB  
1992 C CG  A TYR   B 152 ? 1.0691 1.2551 0.4286 0.2922  0.1127  0.0664  167 TYR   B CG  
1993 C CG  B TYR   B 152 ? 1.0695 1.2554 0.4289 0.2922  0.1127  0.0664  167 TYR   B CG  
1994 C CG  C TYR   B 152 ? 1.0744 1.2643 0.4345 0.2925  0.1135  0.0683  167 TYR   B CG  
1995 C CG  D TYR   B 152 ? 1.0748 1.2646 0.4348 0.2925  0.1135  0.0683  167 TYR   B CG  
1996 C CD1 A TYR   B 152 ? 1.0624 1.2512 0.4310 0.2768  0.1152  0.0684  167 TYR   B CD1 
1997 C CD1 B TYR   B 152 ? 1.0626 1.2514 0.4312 0.2768  0.1152  0.0684  167 TYR   B CD1 
1998 C CD1 C TYR   B 152 ? 1.0674 1.2610 0.4382 0.2759  0.1163  0.0708  167 TYR   B CD1 
1999 C CD1 D TYR   B 152 ? 1.0676 1.2612 0.4384 0.2759  0.1163  0.0708  167 TYR   B CD1 
2000 C CD2 A TYR   B 152 ? 1.0729 1.2317 0.4295 0.2905  0.1074  0.0533  167 TYR   B CD2 
2001 C CD2 B TYR   B 152 ? 1.0731 1.2319 0.4296 0.2905  0.1074  0.0533  167 TYR   B CD2 
2002 C CD2 C TYR   B 152 ? 1.0815 1.2434 0.4369 0.2920  0.1078  0.0547  167 TYR   B CD2 
2003 C CD2 D TYR   B 152 ? 1.0817 1.2436 0.4371 0.2920  0.1078  0.0547  167 TYR   B CD2 
2004 C CE1 A TYR   B 152 ? 1.0565 1.2222 0.4308 0.2608  0.1128  0.0577  167 TYR   B CE1 
2005 C CE1 B TYR   B 152 ? 1.0566 1.2223 0.4309 0.2608  0.1128  0.0577  167 TYR   B CE1 
2006 C CE1 C TYR   B 152 ? 1.0622 1.2325 0.4386 0.2599  0.1139  0.0602  167 TYR   B CE1 
2007 C CE1 D TYR   B 152 ? 1.0623 1.2326 0.4387 0.2599  0.1139  0.0602  167 TYR   B CE1 
2008 C CE2 A TYR   B 152 ? 1.0725 1.2094 0.4353 0.2741  0.1049  0.0430  167 TYR   B CE2 
2009 C CE2 B TYR   B 152 ? 1.0727 1.2095 0.4355 0.2741  0.1049  0.0430  167 TYR   B CE2 
2010 C CE2 C TYR   B 152 ? 1.0810 1.2208 0.4428 0.2755  0.1053  0.0445  167 TYR   B CE2 
2011 C CE2 D TYR   B 152 ? 1.0812 1.2210 0.4429 0.2755  0.1053  0.0445  167 TYR   B CE2 
2012 C CZ  A TYR   B 152 ? 1.0614 1.2017 0.4329 0.2595  0.1078  0.0453  167 TYR   B CZ  
2013 C CZ  B TYR   B 152 ? 1.0615 1.2018 0.4329 0.2595  0.1078  0.0453  167 TYR   B CZ  
2014 C CZ  C TYR   B 152 ? 1.0685 1.2127 0.4406 0.2597  0.1086  0.0472  167 TYR   B CZ  
2015 C CZ  D TYR   B 152 ? 1.0686 1.2128 0.4407 0.2597  0.1086  0.0472  167 TYR   B CZ  
2016 O OH  A TYR   B 152 ? 1.0640 1.1842 0.4414 0.2439  0.1056  0.0355  167 TYR   B OH  
2017 O OH  B TYR   B 152 ? 1.0643 1.1844 0.4416 0.2439  0.1056  0.0355  167 TYR   B OH  
2018 O OH  C TYR   B 152 ? 1.0724 1.1962 0.4504 0.2441  0.1064  0.0374  167 TYR   B OH  
2019 O OH  D TYR   B 152 ? 1.0726 1.1965 0.4506 0.2441  0.1065  0.0374  167 TYR   B OH  
2020 N N   . VAL   B 153 ? 1.0684 1.2432 0.3758 0.3374  0.1023  0.0572  168 VAL   B N   
2021 C CA  . VAL   B 153 ? 1.0654 1.2072 0.3543 0.3447  0.0932  0.0425  168 VAL   B CA  
2022 C C   . VAL   B 153 ? 1.0281 1.1463 0.3286 0.3214  0.0913  0.0331  168 VAL   B C   
2023 O O   . VAL   B 153 ? 0.9951 1.1183 0.3035 0.3090  0.0944  0.0359  168 VAL   B O   
2024 C CB  . VAL   B 153 ? 1.0841 1.2271 0.3504 0.3638  0.0898  0.0425  168 VAL   B CB  
2025 C CG1 . VAL   B 153 ? 1.1011 1.2091 0.3452 0.3731  0.0791  0.0283  168 VAL   B CG1 
2026 C CG2 . VAL   B 153 ? 1.1161 1.2886 0.3734 0.3861  0.0932  0.0535  168 VAL   B CG2 
2027 N N   . SER   B 154 ? 1.0073 1.1024 0.3089 0.3159  0.0864  0.0229  169 SER   B N   
2028 C CA  . SER   B 154 ? 0.9788 1.0527 0.2911 0.2948  0.0843  0.0137  169 SER   B CA  
2029 C C   . SER   B 154 ? 0.9877 1.0333 0.2815 0.2983  0.0752  0.0025  169 SER   B C   
2030 O O   . SER   B 154 ? 1.0005 1.0320 0.2759 0.3144  0.0678  -0.0031 169 SER   B O   
2031 C CB  . SER   B 154 ? 0.9644 1.0318 0.2892 0.2867  0.0841  0.0095  169 SER   B CB  
2032 O OG  . SER   B 154 ? 0.9561 1.0033 0.2889 0.2690  0.0812  -0.0001 169 SER   B OG  
2033 N N   . ALA   B 155 ? 0.9739 1.0091 0.2730 0.2822  0.0749  -0.0012 170 ALA   B N   
2034 C CA  . ALA   B 155 ? 0.9794 0.9847 0.2662 0.2782  0.0661  -0.0124 170 ALA   B CA  
2035 C C   . ALA   B 155 ? 0.9860 0.9770 0.2781 0.2737  0.0617  -0.0204 170 ALA   B C   
2036 O O   . ALA   B 155 ? 0.9917 0.9930 0.3035 0.2631  0.0670  -0.0187 170 ALA   B O   
2037 C CB  . ALA   B 155 ? 0.9776 0.9780 0.2730 0.2592  0.0680  -0.0138 170 ALA   B CB  
2038 N N   . ILE   B 156 ? 0.9995 0.9656 0.2722 0.2813  0.0515  -0.0289 171 ILE   B N   
2039 C CA  . ILE   B 156 ? 0.9924 0.9377 0.2681 0.2712  0.0448  -0.0388 171 ILE   B CA  
2040 C C   . ILE   B 156 ? 0.9773 0.9138 0.2632 0.2493  0.0452  -0.0423 171 ILE   B C   
2041 O O   . ILE   B 156 ? 0.9794 0.8958 0.2500 0.2487  0.0377  -0.0471 171 ILE   B O   
2042 C CB  . ILE   B 156 ? 1.0160 0.9371 0.2671 0.2860  0.0326  -0.0463 171 ILE   B CB  
2043 C CG1 . ILE   B 156 ? 1.0302 0.9613 0.2675 0.3105  0.0324  -0.0421 171 ILE   B CG1 
2044 C CG2 . ILE   B 156 ? 1.0120 0.9175 0.2695 0.2749  0.0267  -0.0548 171 ILE   B CG2 
2045 C CD1 . ILE   B 156 ? 1.0639 0.9705 0.2726 0.3282  0.0199  -0.0490 171 ILE   B CD1 
2046 N N   . THR   B 157 ? 0.9549 0.9064 0.2643 0.2332  0.0535  -0.0395 172 THR   B N   
2047 C CA  . THR   B 157 ? 0.9433 0.8903 0.2652 0.2120  0.0553  -0.0424 172 THR   B CA  
2048 C C   . THR   B 157 ? 0.9449 0.8763 0.2713 0.2010  0.0493  -0.0514 172 THR   B C   
2049 O O   . THR   B 157 ? 0.9411 0.8797 0.2812 0.1975  0.0516  -0.0527 172 THR   B O   
2050 C CB  . THR   B 157 ? 0.9233 0.8921 0.2669 0.2008  0.0659  -0.0360 172 THR   B CB  
2051 O OG1 . THR   B 157 ? 0.9330 0.9198 0.2732 0.2116  0.0713  -0.0262 172 THR   B OG1 
2052 C CG2 . THR   B 157 ? 0.9112 0.8764 0.2653 0.1813  0.0678  -0.0386 172 THR   B CG2 
2053 N N   . GLN   B 158 ? 0.9462 0.8579 0.2627 0.1936  0.0421  -0.0568 173 GLN   B N   
2054 C CA  . GLN   B 158 ? 0.9538 0.8508 0.2735 0.1810  0.0355  -0.0645 173 GLN   B CA  
2055 C C   . GLN   B 158 ? 0.9571 0.8530 0.2865 0.1613  0.0378  -0.0655 173 GLN   B C   
2056 O O   . GLN   B 158 ? 0.9526 0.8440 0.2733 0.1608  0.0377  -0.0632 173 GLN   B O   
2057 C CB  . GLN   B 158 ? 0.9786 0.8511 0.2749 0.1909  0.0228  -0.0697 173 GLN   B CB  
2058 C CG  . GLN   B 158 ? 0.9911 0.8498 0.2899 0.1798  0.0148  -0.0770 173 GLN   B CG  
2059 C CD  . GLN   B 158 ? 0.9712 0.8439 0.2886 0.1763  0.0187  -0.0786 173 GLN   B CD  
2060 O OE1 . GLN   B 158 ? 0.9518 0.8429 0.2899 0.1665  0.0282  -0.0762 173 GLN   B OE1 
2061 N NE2 . GLN   B 158 ? 0.9698 0.8323 0.2795 0.1836  0.0107  -0.0832 173 GLN   B NE2 
2062 N N   . GLY   B 159 ? 0.9650 0.8650 0.3109 0.1464  0.0392  -0.0690 174 GLY   B N   
2063 C CA  . GLY   B 159 ? 0.9821 0.8810 0.3366 0.1275  0.0405  -0.0706 174 GLY   B CA  
2064 C C   . GLY   B 159 ? 1.0363 0.9133 0.3780 0.1211  0.0295  -0.0756 174 GLY   B C   
2065 O O   . GLY   B 159 ? 1.0653 0.9259 0.3899 0.1314  0.0203  -0.0781 174 GLY   B O   
2066 N N   . LYS   B 160 ? 1.1098 0.9865 0.4592 0.1039  0.0300  -0.0768 175 LYS   B N   
2067 C CA  . LYS   B 160 ? 1.1869 1.0449 0.5270 0.0932  0.0200  -0.0804 175 LYS   B CA  
2068 C C   . LYS   B 160 ? 1.1958 1.0629 0.5530 0.0806  0.0198  -0.0841 175 LYS   B C   
2069 O O   . LYS   B 160 ? 1.1608 1.0481 0.5375 0.0742  0.0292  -0.0834 175 LYS   B O   
2070 C CB  . LYS   B 160 ? 1.2467 1.1011 0.5833 0.0836  0.0219  -0.0776 175 LYS   B CB  
2071 C CG  . LYS   B 160 ? 1.3205 1.1550 0.6461 0.0715  0.0119  -0.0797 175 LYS   B CG  
2072 C CD  . LYS   B 160 ? 1.3621 1.1819 0.6708 0.0722  0.0093  -0.0770 175 LYS   B CD  
2073 C CE  . LYS   B 160 ? 1.4140 1.2100 0.7084 0.0614  -0.0026 -0.0788 175 LYS   B CE  
2074 N NZ  . LYS   B 160 ? 1.4573 1.2614 0.7643 0.0412  0.0011  -0.0772 175 LYS   B NZ  
2075 N N   . ARG   B 161 ? 1.2336 1.0867 0.5833 0.0778  0.0092  -0.0881 176 ARG   B N   
2076 C CA  . ARG   B 161 ? 1.2718 1.1335 0.6367 0.0631  0.0076  -0.0912 176 ARG   B CA  
2077 C C   . ARG   B 161 ? 1.3136 1.1677 0.6763 0.0454  0.0035  -0.0904 176 ARG   B C   
2078 O O   . ARG   B 161 ? 1.3295 1.1614 0.6722 0.0472  -0.0045 -0.0896 176 ARG   B O   
2079 C CB  . ARG   B 161 ? 1.2934 1.1457 0.6519 0.0701  -0.0018 -0.0953 176 ARG   B CB  
2080 C CG  . ARG   B 161 ? 1.2768 1.1426 0.6525 0.0587  -0.0024 -0.0984 176 ARG   B CG  
2081 C CD  . ARG   B 161 ? 1.3077 1.1609 0.6744 0.0641  -0.0140 -0.1024 176 ARG   B CD  
2082 N NE  . ARG   B 161 ? 1.3167 1.1843 0.7002 0.0518  -0.0150 -0.1050 176 ARG   B NE  
2083 C CZ  . ARG   B 161 ? 1.3109 1.1923 0.7059 0.0574  -0.0129 -0.1078 176 ARG   B CZ  
2084 N NH1 . ARG   B 161 ? 1.2584 1.1406 0.6502 0.0751  -0.0096 -0.1081 176 ARG   B NH1 
2085 N NH2 . ARG   B 161 ? 1.3152 1.2107 0.7251 0.0451  -0.0141 -0.1098 176 ARG   B NH2 
2086 N N   . GLU   B 162 ? 1.3405 1.2123 0.7219 0.0298  0.0087  -0.0905 177 GLU   B N   
2087 C CA  . GLU   B 162 ? 1.4067 1.2759 0.7888 0.0116  0.0063  -0.0889 177 GLU   B CA  
2088 C C   . GLU   B 162 ? 1.4055 1.2761 0.7932 -0.0014 -0.0016 -0.0910 177 GLU   B C   
2089 O O   . GLU   B 162 ? 1.4396 1.2883 0.8115 -0.0054 -0.0143 -0.0913 177 GLU   B O   
2090 C CB  . GLU   B 162 ? 1.4349 1.3256 0.8336 0.0038  0.0188  -0.0866 177 GLU   B CB  
2091 C CG  . GLU   B 162 ? 1.4728 1.3624 0.8661 0.0135  0.0260  -0.0836 177 GLU   B CG  
2092 C CD  . GLU   B 162 ? 1.5245 1.4023 0.9062 0.0071  0.0246  -0.0803 177 GLU   B CD  
2093 O OE1 . GLU   B 162 ? 1.4659 1.3526 0.8566 -0.0081 0.0277  -0.0792 177 GLU   B OE1 
2094 O OE2 . GLU   B 162 ? 1.5209 1.3813 0.8842 0.0180  0.0207  -0.0788 177 GLU   B OE2 
2095 S S   A DMS   C .   ? 1.2598 1.4320 0.6812 0.2267  0.1200  0.0681  201 DMS   B S   
2096 S S   B DMS   C .   ? 1.2597 1.4319 0.6811 0.2267  0.1200  0.0681  201 DMS   B S   
2097 O O   A DMS   C .   ? 1.2771 1.4720 0.6900 0.2387  0.1223  0.0784  201 DMS   B O   
2098 O O   B DMS   C .   ? 1.2772 1.4721 0.6901 0.2387  0.1223  0.0784  201 DMS   B O   
2099 C C1  A DMS   C .   ? 1.2605 1.4141 0.6863 0.2101  0.1185  0.0576  201 DMS   B C1  
2100 C C1  B DMS   C .   ? 1.2606 1.4141 0.6863 0.2101  0.1185  0.0576  201 DMS   B C1  
2101 C C2  A DMS   C .   ? 1.2677 1.4182 0.6738 0.2420  0.1139  0.0541  201 DMS   B C2  
2102 C C2  B DMS   C .   ? 1.2675 1.4180 0.6736 0.2420  0.1139  0.0541  201 DMS   B C2  
2103 S S   A DMS   D .   ? 2.7718 2.7954 2.2977 0.0390  0.1176  -0.0427 202 DMS   B S   
2104 S S   B DMS   D .   ? 2.7731 2.7967 2.2990 0.0390  0.1176  -0.0427 202 DMS   B S   
2105 O O   A DMS   D .   ? 2.7373 2.7630 2.2616 0.0440  0.1174  -0.0482 202 DMS   B O   
2106 O O   B DMS   D .   ? 2.7384 2.7641 2.2627 0.0440  0.1174  -0.0481 202 DMS   B O   
2107 C C1  A DMS   D .   ? 2.7530 2.7698 2.2817 0.0427  0.1154  -0.0459 202 DMS   B C1  
2108 C C1  B DMS   D .   ? 2.7536 2.7704 2.2823 0.0427  0.1154  -0.0459 202 DMS   B C1  
2109 C C2  A DMS   D .   ? 2.7547 2.7831 2.2778 0.0436  0.1174  -0.0298 202 DMS   B C2  
2110 C C2  B DMS   D .   ? 2.7552 2.7837 2.2784 0.0436  0.1174  -0.0298 202 DMS   B C2  
2111 S S   A DMS   E .   ? 1.6806 1.8375 1.0955 0.2044  0.1189  0.0565  203 DMS   B S   
2112 S S   B DMS   E .   ? 1.6807 1.8376 1.0955 0.2044  0.1189  0.0565  203 DMS   B S   
2113 O O   A DMS   E .   ? 1.6649 1.8196 1.0646 0.2143  0.1167  0.0537  203 DMS   B O   
2114 O O   B DMS   E .   ? 1.6646 1.8192 1.0643 0.2143  0.1167  0.0537  203 DMS   B O   
2115 C C1  A DMS   E .   ? 1.6837 1.8181 1.1100 0.1833  0.1177  0.0452  203 DMS   B C1  
2116 C C1  B DMS   E .   ? 1.6840 1.8184 1.1103 0.1833  0.1177  0.0452  203 DMS   B C1  
2117 C C2  A DMS   E .   ? 1.6677 1.8515 1.0970 0.1930  0.1247  0.0721  203 DMS   B C2  
2118 C C2  B DMS   E .   ? 1.6677 1.8514 1.0970 0.1930  0.1247  0.0721  203 DMS   B C2  
2119 N N1  C A1BHB F .   ? 0.8824 1.0182 0.3193 0.1770  0.1191  0.0474  204 A1BHB B N1  
2120 N N1  D A1BHB F .   ? 0.8824 1.0182 0.3193 0.1770  0.1191  0.0474  204 A1BHB B N1  
2121 N N3  C A1BHB F .   ? 0.8448 0.9549 0.2937 0.1415  0.1188  0.0321  204 A1BHB B N3  
2122 N N3  D A1BHB F .   ? 0.8448 0.9549 0.2938 0.1415  0.1188  0.0321  204 A1BHB B N3  
2123 C C4  C A1BHB F .   ? 0.8486 0.9632 0.2867 0.1583  0.1173  0.0344  204 A1BHB B C4  
2124 C C4  D A1BHB F .   ? 0.8485 0.9632 0.2867 0.1583  0.1174  0.0344  204 A1BHB B C4  
2125 C C5  C A1BHB F .   ? 0.8556 0.9611 0.2772 0.1702  0.1136  0.0287  204 A1BHB B C5  
2126 C C5  D A1BHB F .   ? 0.8555 0.9611 0.2772 0.1702  0.1136  0.0287  204 A1BHB B C5  
2127 C C6  C A1BHB F .   ? 0.8412 0.9278 0.2733 0.1438  0.1134  0.0177  204 A1BHB B C6  
2128 C C6  D A1BHB F .   ? 0.8412 0.9277 0.2732 0.1438  0.1134  0.0177  204 A1BHB B C6  
2129 C C7  C A1BHB F .   ? 0.8325 0.9310 0.2799 0.1328  0.1177  0.0246  204 A1BHB B C7  
2130 C C7  D A1BHB F .   ? 0.8324 0.9309 0.2799 0.1328  0.1177  0.0247  204 A1BHB B C7  
2131 C C8  C A1BHB F .   ? 0.9130 1.0764 0.3481 0.1957  0.1218  0.0639  204 A1BHB B C8  
2132 C C8  D A1BHB F .   ? 0.9131 1.0764 0.3481 0.1957  0.1218  0.0639  204 A1BHB B C8  
2133 C C10 C A1BHB F .   ? 0.9237 1.1317 0.3541 0.2132  0.1269  0.0875  204 A1BHB B C10 
2134 C C10 D A1BHB F .   ? 0.9237 1.1317 0.3542 0.2132  0.1269  0.0875  204 A1BHB B C10 
2135 C C13 C A1BHB F .   ? 0.9361 1.0781 0.3377 0.2427  0.1119  0.0488  204 A1BHB B C13 
2136 C C13 D A1BHB F .   ? 0.9360 1.0781 0.3377 0.2427  0.1119  0.0488  204 A1BHB B C13 
2137 C C15 C A1BHB F .   ? 0.9192 1.0504 0.3402 0.2106  0.1142  0.0442  204 A1BHB B C15 
2138 C C15 D A1BHB F .   ? 0.9191 1.0504 0.3402 0.2106  0.1142  0.0442  204 A1BHB B C15 
2139 O O1  C A1BHB F .   ? 0.9129 1.0559 0.3684 0.1658  0.1219  0.0556  204 A1BHB B O1  
2140 O O1  D A1BHB F .   ? 0.9132 1.0561 0.3687 0.1658  0.1219  0.0556  204 A1BHB B O1  
2141 C C1  C A1BHB F .   ? 0.9004 1.0471 0.3441 0.1782  0.1210  0.0552  204 A1BHB B C1  
2142 C C1  D A1BHB F .   ? 0.9005 1.0471 0.3441 0.1782  0.1210  0.0552  204 A1BHB B C1  
2143 C C2  C A1BHB F .   ? 0.8617 0.9884 0.3061 0.1610  0.1194  0.0424  204 A1BHB B C2  
2144 C C2  D A1BHB F .   ? 0.8617 0.9884 0.3061 0.1610  0.1194  0.0424  204 A1BHB B C2  
2145 C C3  C A1BHB F .   ? 0.8507 0.9781 0.3093 0.1450  0.1215  0.0446  204 A1BHB B C3  
2146 C C3  D A1BHB F .   ? 0.8507 0.9781 0.3093 0.1450  0.1215  0.0446  204 A1BHB B C3  
2147 N N2  C A1BHB F .   ? 0.8425 0.9599 0.3036 0.1337  0.1211  0.0381  204 A1BHB B N2  
2148 N N2  D A1BHB F .   ? 0.8425 0.9599 0.3037 0.1337  0.1211  0.0381  204 A1BHB B N2  
2149 N N4  C A1BHB F .   ? 0.8497 0.9480 0.2701 0.1610  0.1131  0.0247  204 A1BHB B N4  
2150 N N4  D A1BHB F .   ? 0.8496 0.9479 0.2700 0.1610  0.1131  0.0247  204 A1BHB B N4  
2151 C C9  C A1BHB F .   ? 0.9180 1.1065 0.3560 0.1966  0.1256  0.0782  204 A1BHB B C9  
2152 C C9  D A1BHB F .   ? 0.9181 1.1066 0.3561 0.1966  0.1256  0.0782  204 A1BHB B C9  
2153 C C11 C A1BHB F .   ? 0.9350 1.1354 0.3544 0.2292  0.1242  0.0821  204 A1BHB B C11 
2154 C C11 D A1BHB F .   ? 0.9351 1.1355 0.3545 0.2292  0.1242  0.0821  204 A1BHB B C11 
2155 C C12 C A1BHB F .   ? 0.9315 1.1046 0.3474 0.2283  0.1198  0.0671  204 A1BHB B C12 
2156 C C12 D A1BHB F .   ? 0.9315 1.1046 0.3474 0.2283  0.1198  0.0671  204 A1BHB B C12 
2157 N N5  C A1BHB F .   ? 0.9357 1.1020 0.3399 0.2446  0.1165  0.0622  204 A1BHB B N5  
2158 N N5  D A1BHB F .   ? 0.9357 1.1019 0.3399 0.2446  0.1165  0.0622  204 A1BHB B N5  
2159 C C14 C A1BHB F .   ? 0.9310 1.0558 0.3412 0.2258  0.1107  0.0397  204 A1BHB B C14 
2160 C C14 D A1BHB F .   ? 0.9310 1.0558 0.3412 0.2258  0.1107  0.0397  204 A1BHB B C14 
2161 C C16 C A1BHB F .   ? 0.9224 1.0776 0.3466 0.2112  0.1186  0.0581  204 A1BHB B C16 
2162 C C16 D A1BHB F .   ? 0.9225 1.0777 0.3466 0.2112  0.1186  0.0581  204 A1BHB B C16 
2163 S S   C SO4   G .   ? 1.8863 1.9113 1.4114 0.0385  0.1180  -0.0444 205 SO4   B S   
2164 S S   D SO4   G .   ? 1.8863 1.9113 1.4114 0.0385  0.1180  -0.0444 205 SO4   B S   
2165 O O1  C SO4   G .   ? 1.9031 1.9233 1.4317 0.0356  0.1175  -0.0511 205 SO4   B O1  
2166 O O1  D SO4   G .   ? 1.9031 1.9233 1.4317 0.0356  0.1175  -0.0511 205 SO4   B O1  
2167 O O2  C SO4   G .   ? 1.9207 1.9483 1.4440 0.0318  0.1194  -0.0402 205 SO4   B O2  
2168 O O2  D SO4   G .   ? 1.9207 1.9483 1.4440 0.0318  0.1194  -0.0402 205 SO4   B O2  
2169 O O3  C SO4   G .   ? 1.8743 1.9009 1.3976 0.0427  0.1177  -0.0496 205 SO4   B O3  
2170 O O3  D SO4   G .   ? 1.8743 1.9009 1.3976 0.0427  0.1177  -0.0496 205 SO4   B O3  
2171 O O4  C SO4   G .   ? 1.9111 1.9369 1.4354 0.0443  0.1171  -0.0365 205 SO4   B O4  
2172 O O4  D SO4   G .   ? 1.9111 1.9369 1.4354 0.0443  0.1171  -0.0365 205 SO4   B O4  
# 
