data_7HP4
# 
_entry.id   7HP4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HP4         pdb_00007hp4 10.2210/pdb7hp4/pdb 
WWPDB D_1001407754 ?            ?                   
# 
_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       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HP4 
_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    5  ? ?    ? ? 
4 non-polymer syn '(2M)-2-[6-(methylamino)pyridin-3-yl]-N-(1-methyl-1H-pyrazol-4-yl)benzamide' 307.350   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 '(2M)-2-[6-(methylamino)pyridin-3-yl]-N-(1-methyl-1H-pyrazol-4-yl)benzamide' A1BG4 
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 
A1BG4 non-polymer         . '(2M)-2-[6-(methylamino)pyridin-3-yl]-N-(1-methyl-1H-pyrazol-4-yl)benzamide' ? 'C17 H17 N5 O'   
307.350 
ALA   'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'     89.093 
ARG   'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ? 'C2 H6 O S'      78.133 
GLN   'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'     75.067 
HIS   'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                        ? 'H2 O'           18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                      ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                       ? 'C3 H7 N O3'     
105.093 
SO4   non-polymer         . 'SULFATE ION'                                                                ? 'O4 S -2'        96.063 
THR   'L-peptide linking' y THREONINE                                                                    ? 'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                   ? 'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                     ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                       ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BG4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BG4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  101 303 DMS   DMS A . 
D 3 DMS   1  201 201 DMS   DMS B . 
E 3 DMS   1  202 202 DMS   DMS B . 
F 3 DMS   1  203 203 DMS   DMS B . 
G 4 A1BG4 1  204 301 A1BG4 LIG B . 
H 5 SO4   1  205 302 SO4   SO4 B . 
I 3 DMS   1  206 305 DMS   DMS B . 
J 6 HOH   1  201 65  HOH   HOH A . 
J 6 HOH   2  202 105 HOH   HOH A . 
J 6 HOH   3  203 34  HOH   HOH A . 
J 6 HOH   4  204 48  HOH   HOH A . 
J 6 HOH   5  205 120 HOH   HOH A . 
J 6 HOH   6  206 98  HOH   HOH A . 
J 6 HOH   7  207 118 HOH   HOH A . 
J 6 HOH   8  208 16  HOH   HOH A . 
J 6 HOH   9  209 54  HOH   HOH A . 
J 6 HOH   10 210 36  HOH   HOH A . 
J 6 HOH   11 211 50  HOH   HOH A . 
J 6 HOH   12 212 110 HOH   HOH A . 
J 6 HOH   13 213 29  HOH   HOH A . 
J 6 HOH   14 214 121 HOH   HOH A . 
J 6 HOH   15 215 49  HOH   HOH A . 
J 6 HOH   16 216 119 HOH   HOH A . 
J 6 HOH   17 217 70  HOH   HOH A . 
J 6 HOH   18 218 27  HOH   HOH A . 
J 6 HOH   19 219 129 HOH   HOH A . 
K 6 HOH   1  301 40  HOH   HOH B . 
K 6 HOH   2  302 11  HOH   HOH B . 
K 6 HOH   3  303 5   HOH   HOH B . 
K 6 HOH   4  304 1   HOH   HOH B . 
K 6 HOH   5  305 90  HOH   HOH B . 
K 6 HOH   6  306 57  HOH   HOH B . 
K 6 HOH   7  307 51  HOH   HOH B . 
K 6 HOH   8  308 122 HOH   HOH B . 
K 6 HOH   9  309 117 HOH   HOH B . 
K 6 HOH   10 310 83  HOH   HOH B . 
K 6 HOH   11 311 92  HOH   HOH B . 
K 6 HOH   12 312 60  HOH   HOH B . 
K 6 HOH   13 313 46  HOH   HOH B . 
K 6 HOH   14 314 100 HOH   HOH B . 
K 6 HOH   15 315 63  HOH   HOH B . 
K 6 HOH   16 316 56  HOH   HOH B . 
K 6 HOH   17 317 9   HOH   HOH B . 
K 6 HOH   18 318 35  HOH   HOH B . 
K 6 HOH   19 319 23  HOH   HOH B . 
K 6 HOH   20 320 128 HOH   HOH B . 
K 6 HOH   21 321 4   HOH   HOH B . 
K 6 HOH   22 322 58  HOH   HOH B . 
K 6 HOH   23 323 81  HOH   HOH B . 
K 6 HOH   24 324 42  HOH   HOH B . 
K 6 HOH   25 325 89  HOH   HOH B . 
K 6 HOH   26 326 69  HOH   HOH B . 
K 6 HOH   27 327 77  HOH   HOH B . 
K 6 HOH   28 328 66  HOH   HOH B . 
K 6 HOH   29 329 14  HOH   HOH B . 
K 6 HOH   30 330 115 HOH   HOH B . 
K 6 HOH   31 331 32  HOH   HOH B . 
K 6 HOH   32 332 43  HOH   HOH B . 
K 6 HOH   33 333 13  HOH   HOH B . 
K 6 HOH   34 334 21  HOH   HOH B . 
K 6 HOH   35 335 44  HOH   HOH B . 
K 6 HOH   36 336 20  HOH   HOH B . 
K 6 HOH   37 337 31  HOH   HOH B . 
K 6 HOH   38 338 116 HOH   HOH B . 
K 6 HOH   39 339 126 HOH   HOH B . 
K 6 HOH   40 340 30  HOH   HOH B . 
K 6 HOH   41 341 68  HOH   HOH B . 
K 6 HOH   42 342 62  HOH   HOH B . 
K 6 HOH   43 343 72  HOH   HOH B . 
K 6 HOH   44 344 82  HOH   HOH B . 
K 6 HOH   45 345 2   HOH   HOH B . 
K 6 HOH   46 346 80  HOH   HOH B . 
K 6 HOH   47 347 125 HOH   HOH B . 
K 6 HOH   48 348 28  HOH   HOH B . 
K 6 HOH   49 349 10  HOH   HOH B . 
K 6 HOH   50 350 103 HOH   HOH B . 
K 6 HOH   51 351 130 HOH   HOH B . 
K 6 HOH   52 352 107 HOH   HOH B . 
K 6 HOH   53 353 131 HOH   HOH B . 
K 6 HOH   54 354 3   HOH   HOH B . 
K 6 HOH   55 355 12  HOH   HOH B . 
K 6 HOH   56 356 102 HOH   HOH B . 
K 6 HOH   57 357 24  HOH   HOH B . 
K 6 HOH   58 358 64  HOH   HOH B . 
K 6 HOH   59 359 18  HOH   HOH B . 
K 6 HOH   60 360 94  HOH   HOH B . 
K 6 HOH   61 361 108 HOH   HOH B . 
K 6 HOH   62 362 67  HOH   HOH B . 
K 6 HOH   63 363 73  HOH   HOH B . 
K 6 HOH   64 364 106 HOH   HOH B . 
K 6 HOH   65 365 112 HOH   HOH B . 
K 6 HOH   66 366 17  HOH   HOH B . 
K 6 HOH   67 367 26  HOH   HOH B . 
K 6 HOH   68 368 127 HOH   HOH B . 
K 6 HOH   69 369 45  HOH   HOH B . 
K 6 HOH   70 370 87  HOH   HOH B . 
K 6 HOH   71 371 61  HOH   HOH B . 
K 6 HOH   72 372 79  HOH   HOH B . 
K 6 HOH   73 373 75  HOH   HOH B . 
K 6 HOH   74 374 124 HOH   HOH B . 
K 6 HOH   75 375 59  HOH   HOH B . 
K 6 HOH   76 376 39  HOH   HOH B . 
K 6 HOH   77 377 109 HOH   HOH B . 
K 6 HOH   78 378 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           7HP4 
_cell.length_a           42.570 
_cell.length_b           42.570 
_cell.length_c           216.080 
_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                         7HP4 
_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          7HP4 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.74 
_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   2023-10-05 
_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                     7HP4 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.09 
_reflns.d_resolution_high            1.48 
_reflns.number_obs                   34650 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.069 
_reflns.pdbx_netI_over_sigmaI        16.3 
_reflns.pdbx_redundancy              24.6 
_reflns.pdbx_Rrim_I_all              0.071 
_reflns.pdbx_Rpim_I_all              0.014 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_number_measured_all     853792 
_reflns.pdbx_chi_squared             0.39 
_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                  1.48 
_reflns_shell.d_res_low                   1.51 
_reflns_shell.number_measured_all         33300 
_reflns_shell.number_unique_obs           1725 
_reflns_shell.Rmerge_I_obs                7.670 
_reflns_shell.pdbx_chi_squared            0.14 
_reflns_shell.pdbx_redundancy             19.3 
_reflns_shell.percent_possible_obs        99.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             7.877 
_reflns_shell.pdbx_Rpim_I_all             1.778 
_reflns_shell.pdbx_CC_half                0.325 
_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                                 7HP4 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     30848 
_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                             54.02 
_refine.ls_d_res_high                            1.48 
_refine.ls_percent_reflns_obs                    94.07 
_refine.ls_R_factor_obs                          0.27303 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.27177 
_refine.ls_R_factor_R_free                       0.29674 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1645 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_refine.B_iso_mean                               50.500 
_refine.aniso_B[1][1]                            -0.66 
_refine.aniso_B[2][2]                            -0.66 
_refine.aniso_B[3][3]                            1.32 
_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                       0.142 
_refine.pdbx_overall_ESU_R_Free                  0.128 
_refine.overall_SU_ML                            0.262 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             17.897 
_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                       1.48 
_refine_hist.d_res_low                        54.02 
# 
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             0.021  0.014  ? 3000 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.017  0.015  ? 2194 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.103  1.638  ? 3312 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.461  1.585  ? 5069 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.470  5.000  ? 331  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       31.466 23.168 ? 101  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.025 15.000 ? 361  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       18.431 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.093  0.200  ? 294  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.014  0.020  ? 2934 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.004  0.020  ? 558  '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                  1.105  1.748  ? 1533 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.112  1.625  ? 1496 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.087  2.480  ? 1581 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.086  2.482  ? 1582 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.279  2.195  ? 1467 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.278  2.198  ? 1468 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.194  3.001  ? 1732 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       19.402 20.956 ? 2668 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         19.399 20.648 ? 2654 '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                       1.480 
_refine_ls_shell.d_res_low                        1.519 
_refine_ls_shell.number_reflns_R_work             634 
_refine_ls_shell.R_factor_R_work                  0.670 
_refine_ls_shell.percent_reflns_obs               26.76 
_refine_ls_shell.R_factor_R_free                  0.621 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             34 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HP4 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014856-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HP4 
_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 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 3 ? 
J N N 6 ? 
K 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 7HP4 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HP4 B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 177 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HP4 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HP4 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HP4 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HP4 LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5850 ? 
1 MORE         -23  ? 
1 'SSA (A^2)'  9670 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_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             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_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               2.229 
_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                        143 
_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       143 
_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 63  LEU B 65  
AA1 2  LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3  MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4  GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5  THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6  VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7  LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8  PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1  GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2  LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3  VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4  PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5  VAL B 137 ? VAL B 146 ? VAL B 146 VAL B 155 
AA2 6  TYR B 152 ? THR B 157 ? TYR B 161 THR B 166 
AA2 7  GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA2 8  GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
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 65  N LEU B 49  ? N LEU B 58  
AA1 2 3  O ARG B 50  ? O ARG B 59  N MET A 8   ? N MET A 51  
AA1 3 4  N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5  N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6  N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7  N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8  O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2  N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3  O ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4  N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5  N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA2 5 6  N LEU B 140 ? N LEU B 149 O THR B 157 ? O THR B 166 
AA2 6 7  O SER B 154 ? O SER B 163 N VAL B 117 ? N VAL B 126 
AA2 7 8  O ILE B 114 ? O ILE B 123 N PHE B 107 ? N PHE B 116 
AA2 8 9  O LYS B 108 ? O LYS B 117 N VAL A 33  ? N VAL A 76  
AA2 9 10 N ALA A 34  ? N ALA A 77  O SER A 42  ? O SER A 85  
# 
_pdbx_entry_details.entry_id                   7HP4 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    90 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    93 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.05 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CG B HIS 47  ? ? CD2 B HIS 47  ? ? 1.452 1.354 0.098 0.009 N 
2  1 C  B TRP 50  ? B O   B TRP 50  ? B 1.363 1.229 0.134 0.019 N 
3  1 C  B TRP 50  ? D O   B TRP 50  ? D 1.363 1.229 0.134 0.019 N 
4  1 C  B CYS 80  ? A O   B CYS 80  ? A 1.374 1.229 0.145 0.019 N 
5  1 C  B CYS 80  ? B O   B CYS 80  ? B 1.374 1.229 0.145 0.019 N 
6  1 CD B PRO 82  ? A N   B PRO 82  ? A 1.584 1.474 0.110 0.014 N 
7  1 CD B PRO 82  ? B N   B PRO 82  ? B 1.584 1.474 0.110 0.014 N 
8  1 CD B PRO 82  ? C N   B PRO 82  ? C 1.571 1.474 0.097 0.014 N 
9  1 CD B PRO 82  ? D N   B PRO 82  ? D 1.571 1.474 0.097 0.014 N 
10 1 CB B SER 137 ? ? OG  B SER 137 ? ? 1.497 1.418 0.079 0.013 N 
11 1 C  B SER 137 ? ? O   B SER 137 ? ? 1.460 1.229 0.231 0.019 N 
12 1 C  B LEU 149 ? C O   B LEU 149 ? C 1.482 1.229 0.253 0.019 N 
13 1 C  B LEU 149 ? D O   B LEU 149 ? D 1.485 1.229 0.256 0.019 N 
14 1 C  B ASN 152 ? A O   B ASN 152 ? A 1.363 1.229 0.134 0.019 N 
15 1 C  B ASN 152 ? B O   B ASN 152 ? B 1.368 1.229 0.139 0.019 N 
16 1 C  B ASN 152 ? C O   B ASN 152 ? C 1.372 1.229 0.143 0.019 N 
17 1 C  B ASN 152 ? D O   B ASN 152 ? D 1.373 1.229 0.144 0.019 N 
18 1 C  B ASN 152 ? A N   B GLY 153 ? ? 1.483 1.336 0.147 0.023 Y 
19 1 C  B ASN 152 ? B N   B GLY 153 ? ? 1.482 1.336 0.146 0.023 Y 
20 1 C  B ASN 152 ? C N   B GLY 153 ? ? 1.516 1.336 0.180 0.023 Y 
21 1 C  B ASN 152 ? D N   B GLY 153 ? ? 1.516 1.336 0.180 0.023 Y 
22 1 C  B ALA 164 ? A N   B ILE 165 ? A 1.492 1.336 0.156 0.023 Y 
23 1 C  B ALA 164 ? B N   B ILE 165 ? B 1.485 1.336 0.149 0.023 Y 
24 1 C  B ALA 164 ? C N   B ILE 165 ? C 1.597 1.336 0.261 0.023 Y 
25 1 C  B ALA 164 ? D N   B ILE 165 ? D 1.598 1.336 0.262 0.023 Y 
26 1 CB B THR 166 ? C OG1 B THR 166 ? C 1.570 1.428 0.142 0.020 N 
27 1 CB B THR 166 ? D OG1 B THR 166 ? D 1.570 1.428 0.142 0.020 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB B GLU 94  ? ? CA B GLU 94  ? ? C B GLU 94  ? ? 123.44 110.40 13.04 2.00 N 
2 1 O  B GLU 94  ? ? C  B GLU 94  ? ? N B VAL 95  ? ? 133.97 122.70 11.27 1.60 Y 
3 1 O  B ALA 164 ? A C  B ALA 164 ? A N B ILE 165 ? A 137.20 122.70 14.50 1.60 Y 
4 1 O  B ALA 164 ? B C  B ALA 164 ? B N B ILE 165 ? B 136.61 122.70 13.91 1.60 Y 
5 1 O  B ALA 164 ? C C  B ALA 164 ? C N B ILE 165 ? C 145.30 122.70 22.60 1.60 Y 
6 1 O  B ALA 164 ? D C  B ALA 164 ? D N B ILE 165 ? D 145.30 122.70 22.60 1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 64  ? A 62.91   73.64   
2  1 ASP A 64  ? B 62.84   73.58   
3  1 ASP A 64  ? C 73.25   40.52   
4  1 ASP A 64  ? D 73.26   40.51   
5  1 ASP B 20  ? ? -45.68  151.47  
6  1 LEU B 30  ? ? -120.45 -168.21 
7  1 CYS B 80  ? A 87.89   -28.07  
8  1 CYS B 80  ? B 87.89   -28.07  
9  1 CYS B 80  ? C 75.22   -10.75  
10 1 CYS B 80  ? D 75.22   -10.75  
11 1 LEU B 92  ? ? -129.82 -50.20  
12 1 GLU B 94  ? ? -54.81  171.54  
13 1 LEU B 98  ? A -66.85  79.95   
14 1 LEU B 98  ? B -66.85  80.13   
15 1 ALA B 127 ? ? -101.90 69.74   
16 1 ALA B 127 ? ? -101.92 69.74   
17 1 ALA B 127 ? ? -101.92 69.74   
18 1 SER B 135 ? ? -38.42  124.65  
19 1 LYS B 157 ? A -34.86  -38.74  
20 1 LYS B 157 ? B -34.86  -38.74  
21 1 LYS B 157 ? C -38.37  -35.27  
22 1 LYS B 157 ? D -38.37  -35.27  
23 1 ALA B 164 ? C -49.75  160.79  
24 1 ALA B 164 ? D -49.83  160.82  
25 1 ILE B 165 ? A -100.37 77.56   
26 1 ILE B 165 ? B -100.77 77.43   
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 THR B 111 ? ? 13.85  
2 1 ASN B 152 ? A -13.71 
3 1 ASN B 152 ? B -13.80 
4 1 ASN B 152 ? C -10.20 
5 1 ASN B 152 ? D -10.33 
6 1 ALA B 164 ? A -14.08 
7 1 ALA B 164 ? B -14.56 
# 
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 335 ? K HOH . 
2 1 B HOH 369 ? K HOH . 
3 1 B HOH 374 ? K 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 -13.2039 -1.7189 -18.0571 0.4965 0.5336 0.5051 0.3179 0.3053 0.2869 1.5214 4.3002 0.4939 0.2474  
0.2987 0.5552 0.4642 0.3465 0.7294 -0.5112 -0.5675 -0.6747 0.0262 0.2174 0.1033  
'X-RAY DIFFRACTION' 2 ? refined -18.4939 0.8072  -15.7003 0.4395 0.4155 0.0379 0.1555 0.0436 0.0211 1.9152 0.7519 0.5036 -0.2212 
0.3387 0.0676 0.3544 0.1398 0.1696 -0.1159 -0.3358 0.0505  0.0734 0.0346 -0.0187 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 305 ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BG4 N1   N N N 1   
A1BG4 N3   N Y N 2   
A1BG4 C4   C Y N 3   
A1BG4 C5   C Y N 4   
A1BG4 C6   C Y N 5   
A1BG4 C7   C Y N 6   
A1BG4 C8   C Y N 7   
A1BG4 C10  C Y N 8   
A1BG4 C13  C Y N 9   
A1BG4 C15  C N N 10  
A1BG4 C17  C Y N 11  
A1BG4 C1   C N N 12  
A1BG4 C2   C Y N 13  
A1BG4 C3   C Y N 14  
A1BG4 C9   C Y N 15  
A1BG4 C11  C Y N 16  
A1BG4 C12  C N N 17  
A1BG4 O1   O N N 18  
A1BG4 N2   N N N 19  
A1BG4 C14  C Y N 20  
A1BG4 N4   N Y N 21  
A1BG4 C16  C Y N 22  
A1BG4 N5   N Y N 23  
A1BG4 H4   H N N 24  
A1BG4 H6   H N N 25  
A1BG4 H7   H N N 26  
A1BG4 H8   H N N 27  
A1BG4 H10  H N N 28  
A1BG4 H13  H N N 29  
A1BG4 H15  H N N 30  
A1BG4 H14  H N N 31  
A1BG4 H17  H N N 32  
A1BG4 H3   H N N 33  
A1BG4 H2   H N N 34  
A1BG4 H1   H N N 35  
A1BG4 H5   H N N 36  
A1BG4 H9   H N N 37  
A1BG4 H11  H N N 38  
A1BG4 H12  H N N 39  
A1BG4 H16  H N N 40  
ALA   N    N N N 41  
ALA   CA   C N S 42  
ALA   C    C N N 43  
ALA   O    O N N 44  
ALA   CB   C N N 45  
ALA   OXT  O N N 46  
ALA   H    H N N 47  
ALA   H2   H N N 48  
ALA   HA   H N N 49  
ALA   HB1  H N N 50  
ALA   HB2  H N N 51  
ALA   HB3  H N N 52  
ALA   HXT  H N N 53  
ARG   N    N N N 54  
ARG   CA   C N S 55  
ARG   C    C N N 56  
ARG   O    O N N 57  
ARG   CB   C N N 58  
ARG   CG   C N N 59  
ARG   CD   C N N 60  
ARG   NE   N N N 61  
ARG   CZ   C N N 62  
ARG   NH1  N N N 63  
ARG   NH2  N N N 64  
ARG   OXT  O N N 65  
ARG   H    H N N 66  
ARG   H2   H N N 67  
ARG   HA   H N N 68  
ARG   HB2  H N N 69  
ARG   HB3  H N N 70  
ARG   HG2  H N N 71  
ARG   HG3  H N N 72  
ARG   HD2  H N N 73  
ARG   HD3  H N N 74  
ARG   HE   H N N 75  
ARG   HH11 H N N 76  
ARG   HH12 H N N 77  
ARG   HH21 H N N 78  
ARG   HH22 H N N 79  
ARG   HXT  H N N 80  
ASN   N    N N N 81  
ASN   CA   C N S 82  
ASN   C    C N N 83  
ASN   O    O N N 84  
ASN   CB   C N N 85  
ASN   CG   C N N 86  
ASN   OD1  O N N 87  
ASN   ND2  N N N 88  
ASN   OXT  O N N 89  
ASN   H    H N N 90  
ASN   H2   H N N 91  
ASN   HA   H N N 92  
ASN   HB2  H N N 93  
ASN   HB3  H N N 94  
ASN   HD21 H N N 95  
ASN   HD22 H N N 96  
ASN   HXT  H N N 97  
ASP   N    N N N 98  
ASP   CA   C N S 99  
ASP   C    C N N 100 
ASP   O    O N N 101 
ASP   CB   C N N 102 
ASP   CG   C N N 103 
ASP   OD1  O N N 104 
ASP   OD2  O N N 105 
ASP   OXT  O N N 106 
ASP   H    H N N 107 
ASP   H2   H N N 108 
ASP   HA   H N N 109 
ASP   HB2  H N N 110 
ASP   HB3  H N N 111 
ASP   HD2  H N N 112 
ASP   HXT  H N N 113 
CYS   N    N N N 114 
CYS   CA   C N R 115 
CYS   C    C N N 116 
CYS   O    O N N 117 
CYS   CB   C N N 118 
CYS   SG   S N N 119 
CYS   OXT  O N N 120 
CYS   H    H N N 121 
CYS   H2   H N N 122 
CYS   HA   H N N 123 
CYS   HB2  H N N 124 
CYS   HB3  H N N 125 
CYS   HG   H N N 126 
CYS   HXT  H N N 127 
DMS   S    S N N 128 
DMS   O    O N N 129 
DMS   C1   C N N 130 
DMS   C2   C N N 131 
DMS   H11  H N N 132 
DMS   H12  H N N 133 
DMS   H13  H N N 134 
DMS   H21  H N N 135 
DMS   H22  H N N 136 
DMS   H23  H N N 137 
GLN   N    N N N 138 
GLN   CA   C N S 139 
GLN   C    C N N 140 
GLN   O    O N N 141 
GLN   CB   C N N 142 
GLN   CG   C N N 143 
GLN   CD   C N N 144 
GLN   OE1  O N N 145 
GLN   NE2  N N N 146 
GLN   OXT  O N N 147 
GLN   H    H N N 148 
GLN   H2   H N N 149 
GLN   HA   H N N 150 
GLN   HB2  H N N 151 
GLN   HB3  H N N 152 
GLN   HG2  H N N 153 
GLN   HG3  H N N 154 
GLN   HE21 H N N 155 
GLN   HE22 H N N 156 
GLN   HXT  H N N 157 
GLU   N    N N N 158 
GLU   CA   C N S 159 
GLU   C    C N N 160 
GLU   O    O N N 161 
GLU   CB   C N N 162 
GLU   CG   C N N 163 
GLU   CD   C N N 164 
GLU   OE1  O N N 165 
GLU   OE2  O N N 166 
GLU   OXT  O N N 167 
GLU   H    H N N 168 
GLU   H2   H N N 169 
GLU   HA   H N N 170 
GLU   HB2  H N N 171 
GLU   HB3  H N N 172 
GLU   HG2  H N N 173 
GLU   HG3  H N N 174 
GLU   HE2  H N N 175 
GLU   HXT  H N N 176 
GLY   N    N N N 177 
GLY   CA   C N N 178 
GLY   C    C N N 179 
GLY   O    O N N 180 
GLY   OXT  O N N 181 
GLY   H    H N N 182 
GLY   H2   H N N 183 
GLY   HA2  H N N 184 
GLY   HA3  H N N 185 
GLY   HXT  H N N 186 
HIS   N    N N N 187 
HIS   CA   C N S 188 
HIS   C    C N N 189 
HIS   O    O N N 190 
HIS   CB   C N N 191 
HIS   CG   C Y N 192 
HIS   ND1  N Y N 193 
HIS   CD2  C Y N 194 
HIS   CE1  C Y N 195 
HIS   NE2  N Y N 196 
HIS   OXT  O N N 197 
HIS   H    H N N 198 
HIS   H2   H N N 199 
HIS   HA   H N N 200 
HIS   HB2  H N N 201 
HIS   HB3  H N N 202 
HIS   HD1  H N N 203 
HIS   HD2  H N N 204 
HIS   HE1  H N N 205 
HIS   HE2  H N N 206 
HIS   HXT  H N N 207 
HOH   O    O N N 208 
HOH   H1   H N N 209 
HOH   H2   H N N 210 
ILE   N    N N N 211 
ILE   CA   C N S 212 
ILE   C    C N N 213 
ILE   O    O N N 214 
ILE   CB   C N S 215 
ILE   CG1  C N N 216 
ILE   CG2  C N N 217 
ILE   CD1  C N N 218 
ILE   OXT  O N N 219 
ILE   H    H N N 220 
ILE   H2   H N N 221 
ILE   HA   H N N 222 
ILE   HB   H N N 223 
ILE   HG12 H N N 224 
ILE   HG13 H N N 225 
ILE   HG21 H N N 226 
ILE   HG22 H N N 227 
ILE   HG23 H N N 228 
ILE   HD11 H N N 229 
ILE   HD12 H N N 230 
ILE   HD13 H N N 231 
ILE   HXT  H N N 232 
LEU   N    N N N 233 
LEU   CA   C N S 234 
LEU   C    C N N 235 
LEU   O    O N N 236 
LEU   CB   C N N 237 
LEU   CG   C N N 238 
LEU   CD1  C N N 239 
LEU   CD2  C N N 240 
LEU   OXT  O N N 241 
LEU   H    H N N 242 
LEU   H2   H N N 243 
LEU   HA   H N N 244 
LEU   HB2  H N N 245 
LEU   HB3  H N N 246 
LEU   HG   H N N 247 
LEU   HD11 H N N 248 
LEU   HD12 H N N 249 
LEU   HD13 H N N 250 
LEU   HD21 H N N 251 
LEU   HD22 H N N 252 
LEU   HD23 H N N 253 
LEU   HXT  H N N 254 
LYS   N    N N N 255 
LYS   CA   C N S 256 
LYS   C    C N N 257 
LYS   O    O N N 258 
LYS   CB   C N N 259 
LYS   CG   C N N 260 
LYS   CD   C N N 261 
LYS   CE   C N N 262 
LYS   NZ   N N N 263 
LYS   OXT  O N N 264 
LYS   H    H N N 265 
LYS   H2   H N N 266 
LYS   HA   H N N 267 
LYS   HB2  H N N 268 
LYS   HB3  H N N 269 
LYS   HG2  H N N 270 
LYS   HG3  H N N 271 
LYS   HD2  H N N 272 
LYS   HD3  H N N 273 
LYS   HE2  H N N 274 
LYS   HE3  H N N 275 
LYS   HZ1  H N N 276 
LYS   HZ2  H N N 277 
LYS   HZ3  H N N 278 
LYS   HXT  H N N 279 
MET   N    N N N 280 
MET   CA   C N S 281 
MET   C    C N N 282 
MET   O    O N N 283 
MET   CB   C N N 284 
MET   CG   C N N 285 
MET   SD   S N N 286 
MET   CE   C N N 287 
MET   OXT  O N N 288 
MET   H    H N N 289 
MET   H2   H N N 290 
MET   HA   H N N 291 
MET   HB2  H N N 292 
MET   HB3  H N N 293 
MET   HG2  H N N 294 
MET   HG3  H N N 295 
MET   HE1  H N N 296 
MET   HE2  H N N 297 
MET   HE3  H N N 298 
MET   HXT  H N N 299 
PHE   N    N N N 300 
PHE   CA   C N S 301 
PHE   C    C N N 302 
PHE   O    O N N 303 
PHE   CB   C N N 304 
PHE   CG   C Y N 305 
PHE   CD1  C Y N 306 
PHE   CD2  C Y N 307 
PHE   CE1  C Y N 308 
PHE   CE2  C Y N 309 
PHE   CZ   C Y N 310 
PHE   OXT  O N N 311 
PHE   H    H N N 312 
PHE   H2   H N N 313 
PHE   HA   H N N 314 
PHE   HB2  H N N 315 
PHE   HB3  H N N 316 
PHE   HD1  H N N 317 
PHE   HD2  H N N 318 
PHE   HE1  H N N 319 
PHE   HE2  H N N 320 
PHE   HZ   H N N 321 
PHE   HXT  H N N 322 
PRO   N    N N N 323 
PRO   CA   C N S 324 
PRO   C    C N N 325 
PRO   O    O N N 326 
PRO   CB   C N N 327 
PRO   CG   C N N 328 
PRO   CD   C N N 329 
PRO   OXT  O N N 330 
PRO   H    H N N 331 
PRO   HA   H N N 332 
PRO   HB2  H N N 333 
PRO   HB3  H N N 334 
PRO   HG2  H N N 335 
PRO   HG3  H N N 336 
PRO   HD2  H N N 337 
PRO   HD3  H N N 338 
PRO   HXT  H N N 339 
SER   N    N N N 340 
SER   CA   C N S 341 
SER   C    C N N 342 
SER   O    O N N 343 
SER   CB   C N N 344 
SER   OG   O N N 345 
SER   OXT  O N N 346 
SER   H    H N N 347 
SER   H2   H N N 348 
SER   HA   H N N 349 
SER   HB2  H N N 350 
SER   HB3  H N N 351 
SER   HG   H N N 352 
SER   HXT  H N N 353 
SO4   S    S N N 354 
SO4   O1   O N N 355 
SO4   O2   O N N 356 
SO4   O3   O N N 357 
SO4   O4   O N N 358 
THR   N    N N N 359 
THR   CA   C N S 360 
THR   C    C N N 361 
THR   O    O N N 362 
THR   CB   C N R 363 
THR   OG1  O N N 364 
THR   CG2  C N N 365 
THR   OXT  O N N 366 
THR   H    H N N 367 
THR   H2   H N N 368 
THR   HA   H N N 369 
THR   HB   H N N 370 
THR   HG1  H N N 371 
THR   HG21 H N N 372 
THR   HG22 H N N 373 
THR   HG23 H N N 374 
THR   HXT  H N N 375 
TRP   N    N N N 376 
TRP   CA   C N S 377 
TRP   C    C N N 378 
TRP   O    O N N 379 
TRP   CB   C N N 380 
TRP   CG   C Y N 381 
TRP   CD1  C Y N 382 
TRP   CD2  C Y N 383 
TRP   NE1  N Y N 384 
TRP   CE2  C Y N 385 
TRP   CE3  C Y N 386 
TRP   CZ2  C Y N 387 
TRP   CZ3  C Y N 388 
TRP   CH2  C Y N 389 
TRP   OXT  O N N 390 
TRP   H    H N N 391 
TRP   H2   H N N 392 
TRP   HA   H N N 393 
TRP   HB2  H N N 394 
TRP   HB3  H N N 395 
TRP   HD1  H N N 396 
TRP   HE1  H N N 397 
TRP   HE3  H N N 398 
TRP   HZ2  H N N 399 
TRP   HZ3  H N N 400 
TRP   HH2  H N N 401 
TRP   HXT  H N N 402 
TYR   N    N N N 403 
TYR   CA   C N S 404 
TYR   C    C N N 405 
TYR   O    O N N 406 
TYR   CB   C N N 407 
TYR   CG   C Y N 408 
TYR   CD1  C Y N 409 
TYR   CD2  C Y N 410 
TYR   CE1  C Y N 411 
TYR   CE2  C Y N 412 
TYR   CZ   C Y N 413 
TYR   OH   O N N 414 
TYR   OXT  O N N 415 
TYR   H    H N N 416 
TYR   H2   H N N 417 
TYR   HA   H N N 418 
TYR   HB2  H N N 419 
TYR   HB3  H N N 420 
TYR   HD1  H N N 421 
TYR   HD2  H N N 422 
TYR   HE1  H N N 423 
TYR   HE2  H N N 424 
TYR   HH   H N N 425 
TYR   HXT  H N N 426 
VAL   N    N N N 427 
VAL   CA   C N S 428 
VAL   C    C N N 429 
VAL   O    O N N 430 
VAL   CB   C N N 431 
VAL   CG1  C N N 432 
VAL   CG2  C N N 433 
VAL   OXT  O N N 434 
VAL   H    H N N 435 
VAL   H2   H N N 436 
VAL   HA   H N N 437 
VAL   HB   H N N 438 
VAL   HG11 H N N 439 
VAL   HG12 H N N 440 
VAL   HG13 H N N 441 
VAL   HG21 H N N 442 
VAL   HG22 H N N 443 
VAL   HG23 H N N 444 
VAL   HXT  H N N 445 
# 
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 
A1BG4 C1  N1   sing N N 1   
A1BG4 N1  C2   sing N N 2   
A1BG4 C2  C3   doub Y N 3   
A1BG4 C3  C4   sing Y N 4   
A1BG4 C4  C5   doub Y N 5   
A1BG4 C5  C6   sing N N 6   
A1BG4 C6  C7   doub Y N 7   
A1BG4 C7  C8   sing Y N 8   
A1BG4 C8  C9   doub Y N 9   
A1BG4 C9  C10  sing Y N 10  
A1BG4 C10 C11  doub Y N 11  
A1BG4 C11 C12  sing N N 12  
A1BG4 C12 O1   doub N N 13  
A1BG4 C12 N2   sing N N 14  
A1BG4 N2  C13  sing N N 15  
A1BG4 C13 C14  sing Y N 16  
A1BG4 C14 N3   doub Y N 17  
A1BG4 N3  N4   sing Y N 18  
A1BG4 N4  C15  sing N N 19  
A1BG4 N4  C16  sing Y N 20  
A1BG4 C5  C17  sing Y N 21  
A1BG4 C17 N5   doub Y N 22  
A1BG4 C2  N5   sing Y N 23  
A1BG4 C6  C11  sing Y N 24  
A1BG4 C13 C16  doub Y N 25  
A1BG4 N1  H4   sing N N 26  
A1BG4 C4  H6   sing N N 27  
A1BG4 C7  H7   sing N N 28  
A1BG4 C8  H8   sing N N 29  
A1BG4 C10 H10  sing N N 30  
A1BG4 C15 H13  sing N N 31  
A1BG4 C15 H15  sing N N 32  
A1BG4 C15 H14  sing N N 33  
A1BG4 C17 H17  sing N N 34  
A1BG4 C1  H3   sing N N 35  
A1BG4 C1  H2   sing N N 36  
A1BG4 C1  H1   sing N N 37  
A1BG4 C3  H5   sing N N 38  
A1BG4 C9  H9   sing N N 39  
A1BG4 N2  H11  sing N N 40  
A1BG4 C14 H12  sing N N 41  
A1BG4 C16 H16  sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
SO4   S   O1   doub N N 341 
SO4   S   O2   doub N N 342 
SO4   S   O3   sing N N 343 
SO4   S   O4   sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TRP   N   CA   sing N N 361 
TRP   N   H    sing N N 362 
TRP   N   H2   sing N N 363 
TRP   CA  C    sing N N 364 
TRP   CA  CB   sing N N 365 
TRP   CA  HA   sing N N 366 
TRP   C   O    doub N N 367 
TRP   C   OXT  sing N N 368 
TRP   CB  CG   sing N N 369 
TRP   CB  HB2  sing N N 370 
TRP   CB  HB3  sing N N 371 
TRP   CG  CD1  doub Y N 372 
TRP   CG  CD2  sing Y N 373 
TRP   CD1 NE1  sing Y N 374 
TRP   CD1 HD1  sing N N 375 
TRP   CD2 CE2  doub Y N 376 
TRP   CD2 CE3  sing Y N 377 
TRP   NE1 CE2  sing Y N 378 
TRP   NE1 HE1  sing N N 379 
TRP   CE2 CZ2  sing Y N 380 
TRP   CE3 CZ3  doub Y N 381 
TRP   CE3 HE3  sing N N 382 
TRP   CZ2 CH2  doub Y N 383 
TRP   CZ2 HZ2  sing N N 384 
TRP   CZ3 CH2  sing Y N 385 
TRP   CZ3 HZ3  sing N N 386 
TRP   CH2 HH2  sing N N 387 
TRP   OXT HXT  sing N N 388 
TYR   N   CA   sing N N 389 
TYR   N   H    sing N N 390 
TYR   N   H2   sing N N 391 
TYR   CA  C    sing N N 392 
TYR   CA  CB   sing N N 393 
TYR   CA  HA   sing N N 394 
TYR   C   O    doub N N 395 
TYR   C   OXT  sing N N 396 
TYR   CB  CG   sing N N 397 
TYR   CB  HB2  sing N N 398 
TYR   CB  HB3  sing N N 399 
TYR   CG  CD1  doub Y N 400 
TYR   CG  CD2  sing Y N 401 
TYR   CD1 CE1  sing Y N 402 
TYR   CD1 HD1  sing N N 403 
TYR   CD2 CE2  doub Y N 404 
TYR   CD2 HD2  sing N N 405 
TYR   CE1 CZ   doub Y N 406 
TYR   CE1 HE1  sing N N 407 
TYR   CE2 CZ   sing Y N 408 
TYR   CE2 HE2  sing N N 409 
TYR   CZ  OH   sing N N 410 
TYR   OH  HH   sing N N 411 
TYR   OXT HXT  sing N N 412 
VAL   N   CA   sing N N 413 
VAL   N   H    sing N N 414 
VAL   N   H2   sing N N 415 
VAL   CA  C    sing N N 416 
VAL   CA  CB   sing N N 417 
VAL   CA  HA   sing N N 418 
VAL   C   O    doub N N 419 
VAL   C   OXT  sing N N 420 
VAL   CB  CG1  sing N N 421 
VAL   CB  CG2  sing N N 422 
VAL   CB  HB   sing N N 423 
VAL   CG1 HG11 sing N N 424 
VAL   CG1 HG12 sing N N 425 
VAL   CG1 HG13 sing N N 426 
VAL   CG2 HG21 sing N N 427 
VAL   CG2 HG22 sing N N 428 
VAL   CG2 HG23 sing N N 429 
VAL   OXT HXT  sing N N 430 
# 
_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   
;XDomainX of XOrganismX None screened against the XXX Fragment Library by X-ray Crystallography at the XChem facility of Diamond Light Source beamline I04-1
;
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HP4 
_atom_sites.fract_transf_matrix[1][1]   0.023491 
_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]   0.023491 
_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]   0.004628 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -21.415 18.802  -7.093  1.00 77.90  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.624 17.954  -7.333  1.00 76.10  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.442 17.327  -8.722  1.00 73.25  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.160 18.059  -9.690  1.00 75.92  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.925 18.750  -7.160  1.00 77.76  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -25.037 18.028  -6.415  1.00 79.23  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.660 18.658  -5.526  1.00 82.74  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.306 16.853  -6.735  1.00 80.49  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.483 16.006  -8.787  1.00 69.03  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.371 15.238  -10.046 1.00 65.79  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.788 14.971  -10.533 1.00 63.97  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.675 14.815  -9.683  1.00 63.29  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.648 13.912  -9.824  1.00 63.83  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.236 14.112  -9.417  1.00 64.14  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.354 12.561  -9.278  1.00 62.60  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.736 13.190  -8.849  1.00 63.68  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.978 14.955  -11.848 1.00 62.06  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.274 14.679  -12.504 1.00 61.04  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.033 13.709  -13.652 1.00 59.20  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.892 13.557  -14.087 1.00 58.96  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.932 15.977  -12.965 1.00 63.17  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.117 16.794  -13.926 1.00 64.69  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.096 17.610  -13.475 1.00 65.56  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.352 16.735  -15.290 1.00 65.74  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.327 18.358  -14.354 1.00 67.28  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.596 17.482  -16.184 1.00 67.32  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.588 18.306  -15.712 1.00 67.93  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.818 19.041  -16.562 1.00 69.70  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.102 13.053  -14.090 1.00 58.36  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.047 12.044  -15.184 1.00 57.59  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.833 12.566  -16.403 1.00 59.14  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.795 13.328  -16.217 1.00 59.93  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.516 10.663  -14.689 1.00 55.71  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -27.961 10.640  -14.207 1.00 56.31  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.562 10.129  -13.634 1.00 54.49  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.529 9.244   -14.179 1.00 55.34  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.352 12.224  -17.613 1.00 59.67  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.020 12.486  -18.928 1.00 61.29  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.046 11.167  -19.718 1.00 59.88  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -25.997 10.496  -19.772 1.00 58.39  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.242 13.515  -19.750 1.00 63.54  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.429 14.962  -19.365 1.00 65.57  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.389 15.856  -20.027 1.00 67.61  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.637 15.357  -20.884 1.00 68.77  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.309 17.029  -19.676 1.00 69.87  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.205 10.791  -20.269 1.00 60.32  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.340 9.557   -21.085 1.00 60.03  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.445 9.708   -22.331 1.00 61.18  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.342 10.843  -22.854 1.00 63.02  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.810 9.302   -21.415 1.00 61.15  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.118 7.890   -21.877 1.00 61.11  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.581 7.502   -21.761 1.00 62.05  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.808 6.099   -22.052 1.00 62.09  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.564 5.520   -23.235 1.00 63.77  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.136 6.240   -24.260 1.00 66.91  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.772 4.229   -23.414 1.00 62.60  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.748 8.639   -22.717 1.00 60.54  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.758 8.610   -23.827 1.00 62.01  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.129 7.548   -24.866 1.00 62.85  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.515 7.584   -25.945 1.00 64.99  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.353 8.349   -23.310 1.00 61.17  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.044 6.626   -24.578 1.00 61.65  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.472 5.626   -25.563 1.00 62.67  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.218 4.457   -24.970 1.00 62.40  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.257 4.321   -23.701 1.00 61.33  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.727 3.587   -25.850 1.00 63.45  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.245 2.242   -25.504 1.00 62.50  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.075 1.286   -25.320 1.00 61.64  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.969 1.564   -25.835 1.00 62.87  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.156 1.642   -26.569 1.00 64.29  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.488 2.337   -26.694 1.00 66.63  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.623 3.451   -26.147 1.00 66.50  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.379 1.788   -27.370 1.00 69.04  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.321 0.167   -24.656 1.00 60.07  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.289 -0.884  -24.507 1.00 59.22  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.652 -2.045  -25.437 1.00 59.47  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.601 -2.813  -25.136 1.00 58.33  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.124 -1.295  -23.028 1.00 57.60  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.630 -0.100  -22.211 1.00 57.76  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.203 -2.478  -22.911 1.00 57.02  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.638 -0.340  -20.718 1.00 55.97  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.892 -2.165  -26.535 0.20 60.80  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.928 -2.165  -26.553 0.18 60.82  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.890 -2.167  -26.535 0.31 60.79  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.927 -2.166  -26.553 0.31 60.81  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.177 -3.044  -27.704 0.20 61.94  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.223 -3.141  -27.636 0.18 61.74  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.174 -3.044  -27.706 0.31 61.93  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.220 -3.143  -27.636 0.31 61.71  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.880 -3.650  -28.260 0.20 62.13  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -25.922 -3.651  -28.266 0.18 62.15  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.878 -3.651  -28.266 0.31 62.07  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -25.919 -3.652  -28.266 0.31 62.08  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.868 -2.900  -28.385 0.20 62.84  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -24.966 -2.844  -28.430 0.18 62.99  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.864 -2.903  -28.407 0.31 62.85  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -24.956 -2.849  -28.426 0.31 62.97  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -27.886 -2.254  -28.816 0.20 64.38  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.153 -2.514  -28.682 0.18 63.93  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -27.885 -2.254  -28.816 0.31 64.32  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.151 -2.515  -28.682 0.31 63.85  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -26.961 -1.369  -29.449 0.20 65.89  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.323 -2.071  -27.996 0.18 63.33  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -26.965 -1.363  -29.446 0.31 65.83  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.320 -2.075  -27.994 0.31 63.27  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.043 -1.421  -28.317 0.20 64.60  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.563 -3.465  -29.782 0.18 65.31  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.042 -1.422  -28.315 0.31 64.56  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.561 -3.468  -29.781 0.31 65.25  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.915 -4.942  -28.623 1.00 61.77  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.841 -5.538  -29.454 1.00 64.02  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.030 -4.963  -30.859 1.00 68.80  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.198 -4.832  -31.249 1.00 70.89  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.914 -7.057  -29.471 1.00 63.34  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.785 -7.648  -30.245 1.00 65.37  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.758 -7.835  -31.595 1.00 68.06  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.503 -8.087  -29.751 1.00 64.78  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.558 -8.373  -31.964 1.00 69.01  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.769 -8.550  -30.866 1.00 67.14  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.897 -8.138  -28.492 1.00 62.91  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.470 -9.049  -30.762 1.00 67.27  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.620 -8.642  -28.378 1.00 63.08  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -19.919 -9.109  -29.497 1.00 64.87  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -23.964 -4.502  -31.515 1.00 71.78  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -24.060 -3.929  -32.882 1.00 77.45  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.198 -4.768  -33.829 1.00 80.37  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -21.977 -4.905  -33.600 1.00 78.14  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -23.680 -2.451  -32.865 1.00 79.70  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -24.636 -1.617  -32.006 1.00 80.63  ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -25.977 -1.225  -32.622 1.00 83.13  ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -25.958 -0.441  -33.595 1.00 88.30  ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -27.042 -1.685  -32.124 1.00 81.24  ? 62  GLU   A OE2 1 
ATOM   133  N N   A LYS   A 1 20  ? -23.834 -5.356  -34.848 0.20 82.31  ? 63  LYS   A N   1 
ATOM   134  N N   B LYS   A 1 20  ? -23.834 -5.357  -34.848 0.18 82.29  ? 63  LYS   A N   1 
ATOM   135  N N   C LYS   A 1 20  ? -23.822 -5.274  -34.900 0.31 83.37  ? 63  LYS   A N   1 
ATOM   136  N N   D LYS   A 1 20  ? -23.822 -5.274  -34.900 0.31 83.36  ? 63  LYS   A N   1 
ATOM   137  C CA  A LYS   A 1 20  ? -23.162 -6.198  -35.876 0.20 84.09  ? 63  LYS   A CA  1 
ATOM   138  C CA  B LYS   A 1 20  ? -23.162 -6.198  -35.876 0.18 84.09  ? 63  LYS   A CA  1 
ATOM   139  C CA  C LYS   A 1 20  ? -23.139 -6.036  -35.982 0.31 85.65  ? 63  LYS   A CA  1 
ATOM   140  C CA  D LYS   A 1 20  ? -23.139 -6.036  -35.982 0.31 85.65  ? 63  LYS   A CA  1 
ATOM   141  C C   A LYS   A 1 20  ? -22.247 -5.309  -36.722 0.20 86.54  ? 63  LYS   A C   1 
ATOM   142  C C   B LYS   A 1 20  ? -22.247 -5.308  -36.722 0.18 86.55  ? 63  LYS   A C   1 
ATOM   143  C C   C LYS   A 1 20  ? -22.266 -5.060  -36.776 0.31 87.85  ? 63  LYS   A C   1 
ATOM   144  C C   D LYS   A 1 20  ? -22.266 -5.059  -36.776 0.31 87.85  ? 63  LYS   A C   1 
ATOM   145  O O   A LYS   A 1 20  ? -22.709 -4.242  -37.165 0.20 88.20  ? 63  LYS   A O   1 
ATOM   146  O O   B LYS   A 1 20  ? -22.710 -4.241  -37.164 0.18 88.21  ? 63  LYS   A O   1 
ATOM   147  O O   C LYS   A 1 20  ? -22.768 -3.979  -37.127 0.31 89.47  ? 63  LYS   A O   1 
ATOM   148  O O   D LYS   A 1 20  ? -22.768 -3.979  -37.127 0.31 89.47  ? 63  LYS   A O   1 
ATOM   149  C CB  A LYS   A 1 20  ? -24.191 -6.938  -36.736 0.20 85.69  ? 63  LYS   A CB  1 
ATOM   150  C CB  B LYS   A 1 20  ? -24.191 -6.938  -36.735 0.18 85.70  ? 63  LYS   A CB  1 
ATOM   151  C CB  C LYS   A 1 20  ? -24.136 -6.726  -36.921 0.31 88.24  ? 63  LYS   A CB  1 
ATOM   152  C CB  D LYS   A 1 20  ? -24.136 -6.726  -36.921 0.31 88.24  ? 63  LYS   A CB  1 
ATOM   153  C CG  A LYS   A 1 20  ? -24.684 -8.255  -36.154 0.20 83.62  ? 63  LYS   A CG  1 
ATOM   154  C CG  B LYS   A 1 20  ? -24.684 -8.255  -36.153 0.18 83.63  ? 63  LYS   A CG  1 
ATOM   155  C CG  C LYS   A 1 20  ? -25.369 -7.353  -36.280 0.31 87.07  ? 63  LYS   A CG  1 
ATOM   156  C CG  D LYS   A 1 20  ? -25.369 -7.353  -36.280 0.31 87.07  ? 63  LYS   A CG  1 
ATOM   157  C CD  A LYS   A 1 20  ? -25.877 -8.833  -36.879 0.20 85.22  ? 63  LYS   A CD  1 
ATOM   158  C CD  B LYS   A 1 20  ? -25.876 -8.833  -36.879 0.18 85.22  ? 63  LYS   A CD  1 
ATOM   159  C CD  C LYS   A 1 20  ? -25.072 -8.300  -35.143 0.31 84.61  ? 63  LYS   A CD  1 
ATOM   160  C CD  D LYS   A 1 20  ? -25.071 -8.300  -35.143 0.31 84.60  ? 63  LYS   A CD  1 
ATOM   161  C CE  A LYS   A 1 20  ? -26.147 -10.275 -36.510 0.20 83.74  ? 63  LYS   A CE  1 
ATOM   162  C CE  B LYS   A 1 20  ? -26.147 -10.275 -36.509 0.18 83.74  ? 63  LYS   A CE  1 
ATOM   163  C CE  C LYS   A 1 20  ? -24.539 -9.636  -35.614 0.31 85.38  ? 63  LYS   A CE  1 
ATOM   164  C CE  D LYS   A 1 20  ? -24.539 -9.637  -35.614 0.31 85.37  ? 63  LYS   A CE  1 
ATOM   165  N NZ  A LYS   A 1 20  ? -27.499 -10.704 -36.937 0.20 84.72  ? 63  LYS   A NZ  1 
ATOM   166  N NZ  B LYS   A 1 20  ? -27.498 -10.704 -36.938 0.18 84.72  ? 63  LYS   A NZ  1 
ATOM   167  N NZ  C LYS   A 1 20  ? -23.906 -10.383 -34.506 0.31 82.70  ? 63  LYS   A NZ  1 
ATOM   168  N NZ  D LYS   A 1 20  ? -23.906 -10.383 -34.506 0.31 82.69  ? 63  LYS   A NZ  1 
ATOM   169  N N   A ASP   A 1 21  ? -20.999 -5.740  -36.927 0.20 86.90  ? 64  ASP   A N   1 
ATOM   170  N N   B ASP   A 1 21  ? -20.999 -5.740  -36.928 0.18 86.90  ? 64  ASP   A N   1 
ATOM   171  N N   C ASP   A 1 21  ? -21.013 -5.431  -37.049 0.31 88.18  ? 64  ASP   A N   1 
ATOM   172  N N   D ASP   A 1 21  ? -21.013 -5.431  -37.049 0.31 88.18  ? 64  ASP   A N   1 
ATOM   173  C CA  A ASP   A 1 21  ? -19.941 -4.974  -37.643 0.20 89.28  ? 64  ASP   A CA  1 
ATOM   174  C CA  B ASP   A 1 21  ? -19.942 -4.974  -37.644 0.18 89.29  ? 64  ASP   A CA  1 
ATOM   175  C CA  C ASP   A 1 21  ? -20.046 -4.622  -37.842 0.31 90.28  ? 64  ASP   A CA  1 
ATOM   176  C CA  D ASP   A 1 21  ? -20.047 -4.622  -37.842 0.31 90.29  ? 64  ASP   A CA  1 
ATOM   177  C C   A ASP   A 1 21  ? -19.643 -3.684  -36.863 0.20 87.60  ? 64  ASP   A C   1 
ATOM   178  C C   B ASP   A 1 21  ? -19.643 -3.683  -36.865 0.18 87.61  ? 64  ASP   A C   1 
ATOM   179  C C   C ASP   A 1 21  ? -19.558 -3.422  -37.009 0.31 88.00  ? 64  ASP   A C   1 
ATOM   180  C C   D ASP   A 1 21  ? -19.558 -3.422  -37.010 0.31 88.01  ? 64  ASP   A C   1 
ATOM   181  O O   A ASP   A 1 21  ? -20.087 -2.611  -37.301 0.20 88.80  ? 64  ASP   A O   1 
ATOM   182  O O   B ASP   A 1 21  ? -20.085 -2.610  -37.304 0.18 88.84  ? 64  ASP   A O   1 
ATOM   183  O O   C ASP   A 1 21  ? -19.416 -2.332  -37.580 0.31 90.52  ? 64  ASP   A O   1 
ATOM   184  O O   D ASP   A 1 21  ? -19.417 -2.331  -37.581 0.31 90.53  ? 64  ASP   A O   1 
ATOM   185  C CB  A ASP   A 1 21  ? -20.330 -4.700  -39.102 0.20 93.97  ? 64  ASP   A CB  1 
ATOM   186  C CB  B ASP   A 1 21  ? -20.330 -4.699  -39.102 0.18 93.95  ? 64  ASP   A CB  1 
ATOM   187  C CB  C ASP   A 1 21  ? -20.649 -4.156  -39.178 0.31 94.88  ? 64  ASP   A CB  1 
ATOM   188  C CB  D ASP   A 1 21  ? -20.649 -4.156  -39.179 0.31 94.88  ? 64  ASP   A CB  1 
ATOM   189  C CG  A ASP   A 1 21  ? -20.283 -5.926  -39.999 0.20 95.86  ? 64  ASP   A CG  1 
ATOM   190  C CG  B ASP   A 1 21  ? -20.284 -5.925  -39.999 0.18 95.85  ? 64  ASP   A CG  1 
ATOM   191  C CG  C ASP   A 1 21  ? -21.255 -5.255  -40.040 0.31 96.65  ? 64  ASP   A CG  1 
ATOM   192  C CG  D ASP   A 1 21  ? -21.255 -5.256  -40.039 0.31 96.64  ? 64  ASP   A CG  1 
ATOM   193  O OD1 A ASP   A 1 21  ? -19.342 -6.011  -40.821 0.20 98.41  ? 64  ASP   A OD1 1 
ATOM   194  O OD1 B ASP   A 1 21  ? -19.341 -6.014  -40.819 0.18 98.40  ? 64  ASP   A OD1 1 
ATOM   195  O OD1 C ASP   A 1 21  ? -20.480 -6.102  -40.541 0.31 97.86  ? 64  ASP   A OD1 1 
ATOM   196  O OD1 D ASP   A 1 21  ? -20.480 -6.103  -40.540 0.31 97.85  ? 64  ASP   A OD1 1 
ATOM   197  O OD2 A ASP   A 1 21  ? -21.191 -6.781  -39.873 0.20 94.94  ? 64  ASP   A OD2 1 
ATOM   198  O OD2 B ASP   A 1 21  ? -21.194 -6.778  -39.875 0.18 94.93  ? 64  ASP   A OD2 1 
ATOM   199  O OD2 C ASP   A 1 21  ? -22.496 -5.242  -40.219 0.31 97.05  ? 64  ASP   A OD2 1 
ATOM   200  O OD2 D ASP   A 1 21  ? -22.496 -5.243  -40.220 0.31 97.05  ? 64  ASP   A OD2 1 
ATOM   201  N N   A ALA   A 1 22  ? -18.950 -3.800  -35.721 0.20 83.96  ? 65  ALA   A N   1 
ATOM   202  N N   B ALA   A 1 22  ? -18.950 -3.800  -35.723 0.18 83.98  ? 65  ALA   A N   1 
ATOM   203  N N   C ALA   A 1 22  ? -19.292 -3.606  -35.706 0.31 83.55  ? 65  ALA   A N   1 
ATOM   204  N N   D ALA   A 1 22  ? -19.291 -3.606  -35.707 0.31 83.56  ? 65  ALA   A N   1 
ATOM   205  C CA  A ALA   A 1 22  ? -18.318 -2.675  -34.987 0.20 82.64  ? 65  ALA   A CA  1 
ATOM   206  C CA  B ALA   A 1 22  ? -18.318 -2.675  -34.988 0.18 82.67  ? 65  ALA   A CA  1 
ATOM   207  C CA  C ALA   A 1 22  ? -18.560 -2.621  -34.871 0.31 81.52  ? 65  ALA   A CA  1 
ATOM   208  C CA  D ALA   A 1 22  ? -18.560 -2.621  -34.871 0.31 81.53  ? 65  ALA   A CA  1 
ATOM   209  C C   A ALA   A 1 22  ? -16.820 -2.666  -35.315 0.20 83.50  ? 65  ALA   A C   1 
ATOM   210  C C   B ALA   A 1 22  ? -16.820 -2.666  -35.315 0.18 83.53  ? 65  ALA   A C   1 
ATOM   211  C C   C ALA   A 1 22  ? -17.062 -2.718  -35.199 0.31 82.06  ? 65  ALA   A C   1 
ATOM   212  C C   D ALA   A 1 22  ? -17.062 -2.718  -35.199 0.31 82.08  ? 65  ALA   A C   1 
ATOM   213  O O   A ALA   A 1 22  ? -16.344 -3.681  -35.846 0.20 84.08  ? 65  ALA   A O   1 
ATOM   214  O O   B ALA   A 1 22  ? -16.343 -3.682  -35.847 0.18 84.10  ? 65  ALA   A O   1 
ATOM   215  O O   C ALA   A 1 22  ? -16.642 -3.802  -35.638 0.31 81.84  ? 65  ALA   A O   1 
ATOM   216  O O   D ALA   A 1 22  ? -16.642 -3.801  -35.639 0.31 81.86  ? 65  ALA   A O   1 
ATOM   217  C CB  A ALA   A 1 22  ? -18.563 -2.820  -33.504 0.20 79.23  ? 65  ALA   A CB  1 
ATOM   218  C CB  B ALA   A 1 22  ? -18.563 -2.820  -33.506 0.18 79.24  ? 65  ALA   A CB  1 
ATOM   219  C CB  C ALA   A 1 22  ? -18.827 -2.876  -33.404 0.31 78.03  ? 65  ALA   A CB  1 
ATOM   220  C CB  D ALA   A 1 22  ? -18.826 -2.876  -33.405 0.31 78.04  ? 65  ALA   A CB  1 
ATOM   221  N N   A GLU   A 1 23  ? -16.108 -1.571  -35.022 0.20 83.76  ? 66  GLU   A N   1 
ATOM   222  N N   B GLU   A 1 23  ? -16.108 -1.571  -35.021 0.18 83.78  ? 66  GLU   A N   1 
ATOM   223  N N   C GLU   A 1 23  ? -16.304 -1.627  -35.014 0.31 82.76  ? 66  GLU   A N   1 
ATOM   224  N N   D GLU   A 1 23  ? -16.303 -1.627  -35.013 0.31 82.77  ? 66  GLU   A N   1 
ATOM   225  C CA  A GLU   A 1 23  ? -14.632 -1.485  -35.205 0.20 85.32  ? 66  GLU   A CA  1 
ATOM   226  C CA  B GLU   A 1 23  ? -14.632 -1.485  -35.205 0.18 85.33  ? 66  GLU   A CA  1 
ATOM   227  C CA  C GLU   A 1 23  ? -14.817 -1.580  -35.134 0.31 84.37  ? 66  GLU   A CA  1 
ATOM   228  C CA  D GLU   A 1 23  ? -14.817 -1.580  -35.133 0.31 84.38  ? 66  GLU   A CA  1 
ATOM   229  C C   A GLU   A 1 23  ? -13.983 -2.504  -34.253 0.20 83.01  ? 66  GLU   A C   1 
ATOM   230  C C   B GLU   A 1 23  ? -13.983 -2.504  -34.253 0.18 83.01  ? 66  GLU   A C   1 
ATOM   231  C C   C GLU   A 1 23  ? -14.204 -2.680  -34.251 0.31 82.35  ? 66  GLU   A C   1 
ATOM   232  C C   D GLU   A 1 23  ? -14.204 -2.679  -34.251 0.31 82.35  ? 66  GLU   A C   1 
ATOM   233  O O   A GLU   A 1 23  ? -14.118 -2.341  -33.017 0.20 79.62  ? 66  GLU   A O   1 
ATOM   234  O O   B GLU   A 1 23  ? -14.118 -2.340  -33.018 0.18 79.64  ? 66  GLU   A O   1 
ATOM   235  O O   C GLU   A 1 23  ? -14.569 -2.747  -33.053 0.31 77.99  ? 66  GLU   A O   1 
ATOM   236  O O   D GLU   A 1 23  ? -14.568 -2.746  -33.053 0.31 78.00  ? 66  GLU   A O   1 
ATOM   237  C CB  A GLU   A 1 23  ? -14.139 -0.044  -35.013 0.20 86.61  ? 66  GLU   A CB  1 
ATOM   238  C CB  B GLU   A 1 23  ? -14.140 -0.044  -35.013 0.18 86.62  ? 66  GLU   A CB  1 
ATOM   239  C CB  C GLU   A 1 23  ? -14.307 -0.193  -34.730 0.31 85.32  ? 66  GLU   A CB  1 
ATOM   240  C CB  D GLU   A 1 23  ? -14.307 -0.192  -34.730 0.31 85.33  ? 66  GLU   A CB  1 
ATOM   241  C CG  A GLU   A 1 23  ? -12.767 0.224   -35.630 0.20 89.60  ? 66  GLU   A CG  1 
ATOM   242  C CG  B GLU   A 1 23  ? -12.767 0.224   -35.629 0.18 89.60  ? 66  GLU   A CG  1 
ATOM   243  C CG  C GLU   A 1 23  ? -12.804 -0.121  -34.512 0.31 86.57  ? 66  GLU   A CG  1 
ATOM   244  C CG  D GLU   A 1 23  ? -12.804 -0.120  -34.513 0.31 86.58  ? 66  GLU   A CG  1 
ATOM   245  C CD  A GLU   A 1 23  ? -12.573 1.574   -36.310 0.20 92.62  ? 66  GLU   A CD  1 
ATOM   246  C CD  B GLU   A 1 23  ? -12.574 1.573   -36.309 0.18 92.62  ? 66  GLU   A CD  1 
ATOM   247  C CD  C GLU   A 1 23  ? -12.278 1.257   -34.141 0.31 87.92  ? 66  GLU   A CD  1 
ATOM   248  C CD  D GLU   A 1 23  ? -12.278 1.258   -34.141 0.31 87.92  ? 66  GLU   A CD  1 
ATOM   249  O OE1 A GLU   A 1 23  ? -13.226 2.556   -35.897 0.20 91.68  ? 66  GLU   A OE1 1 
ATOM   250  O OE1 B GLU   A 1 23  ? -13.230 2.554   -35.897 0.18 91.69  ? 66  GLU   A OE1 1 
ATOM   251  O OE1 C GLU   A 1 23  ? -13.117 2.186   -33.943 0.31 87.47  ? 66  GLU   A OE1 1 
ATOM   252  O OE1 D GLU   A 1 23  ? -13.117 2.186   -33.944 0.31 87.47  ? 66  GLU   A OE1 1 
ATOM   253  O OE2 A GLU   A 1 23  ? -11.763 1.639   -37.268 0.20 95.80  ? 66  GLU   A OE2 1 
ATOM   254  O OE2 B GLU   A 1 23  ? -11.764 1.640   -37.266 0.18 95.80  ? 66  GLU   A OE2 1 
ATOM   255  O OE2 C GLU   A 1 23  ? -11.025 1.400   -34.058 0.31 89.39  ? 66  GLU   A OE2 1 
ATOM   256  O OE2 D GLU   A 1 23  ? -11.025 1.400   -34.056 0.31 89.38  ? 66  GLU   A OE2 1 
ATOM   257  N N   . VAL   A 1 24  ? -13.349 -3.539  -34.819 1.00 83.79  ? 67  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 24  ? -12.746 -4.682  -34.058 1.00 82.62  ? 67  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 24  ? -11.243 -4.421  -33.912 1.00 83.88  ? 67  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 24  ? -10.531 -4.418  -34.927 1.00 86.44  ? 67  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 24  ? -13.031 -6.052  -34.706 1.00 83.74  ? 67  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 24  ? -12.385 -7.173  -33.928 1.00 82.01  ? 67  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 24  ? -14.519 -6.328  -34.857 1.00 83.40  ? 67  VAL   A CG2 1 
ATOM   264  N N   A THR   A 1 25  ? -10.786 -4.220  -32.670 0.20 81.72  ? 68  THR   A N   1 
ATOM   265  N N   B THR   A 1 25  ? -10.786 -4.219  -32.670 0.18 81.73  ? 68  THR   A N   1 
ATOM   266  N N   C THR   A 1 25  ? -10.785 -4.237  -32.668 0.31 81.40  ? 68  THR   A N   1 
ATOM   267  N N   D THR   A 1 25  ? -10.785 -4.237  -32.668 0.31 81.41  ? 68  THR   A N   1 
ATOM   268  C CA  A THR   A 1 25  ? -9.409  -3.778  -32.319 0.20 82.99  ? 68  THR   A CA  1 
ATOM   269  C CA  B THR   A 1 25  ? -9.408  -3.778  -32.319 0.18 83.00  ? 68  THR   A CA  1 
ATOM   270  C CA  C THR   A 1 25  ? -9.402  -3.819  -32.311 0.31 82.52  ? 68  THR   A CA  1 
ATOM   271  C CA  D THR   A 1 25  ? -9.402  -3.819  -32.311 0.31 82.52  ? 68  THR   A CA  1 
ATOM   272  C C   A THR   A 1 25  ? -9.010  -4.370  -30.959 0.20 80.29  ? 68  THR   A C   1 
ATOM   273  C C   B THR   A 1 25  ? -9.010  -4.370  -30.959 0.18 80.30  ? 68  THR   A C   1 
ATOM   274  C C   C THR   A 1 25  ? -9.048  -4.413  -30.939 0.31 79.79  ? 68  THR   A C   1 
ATOM   275  C C   D THR   A 1 25  ? -9.048  -4.413  -30.940 0.31 79.79  ? 68  THR   A C   1 
ATOM   276  O O   A THR   A 1 25  ? -9.805  -5.147  -30.395 0.20 77.39  ? 68  THR   A O   1 
ATOM   277  O O   B THR   A 1 25  ? -9.807  -5.144  -30.393 0.18 77.40  ? 68  THR   A O   1 
ATOM   278  O O   C THR   A 1 25  ? -9.865  -5.184  -30.405 0.31 76.81  ? 68  THR   A O   1 
ATOM   279  O O   D THR   A 1 25  ? -9.866  -5.184  -30.405 0.31 76.82  ? 68  THR   A O   1 
ATOM   280  C CB  A THR   A 1 25  ? -9.319  -2.245  -32.352 0.20 84.54  ? 68  THR   A CB  1 
ATOM   281  C CB  B THR   A 1 25  ? -9.318  -2.245  -32.352 0.18 84.55  ? 68  THR   A CB  1 
ATOM   282  C CB  C THR   A 1 25  ? -9.285  -2.289  -32.385 0.31 84.14  ? 68  THR   A CB  1 
ATOM   283  C CB  D THR   A 1 25  ? -9.284  -2.289  -32.385 0.31 84.15  ? 68  THR   A CB  1 
ATOM   284  O OG1 A THR   A 1 25  ? -7.959  -1.858  -32.156 0.20 86.43  ? 68  THR   A OG1 1 
ATOM   285  O OG1 B THR   A 1 25  ? -7.958  -1.858  -32.155 0.18 86.42  ? 68  THR   A OG1 1 
ATOM   286  O OG1 C THR   A 1 25  ? -7.908  -1.920  -32.478 0.31 86.49  ? 68  THR   A OG1 1 
ATOM   287  O OG1 D THR   A 1 25  ? -7.908  -1.921  -32.478 0.31 86.49  ? 68  THR   A OG1 1 
ATOM   288  C CG2 A THR   A 1 25  ? -10.197 -1.574  -31.317 0.20 82.03  ? 68  THR   A CG2 1 
ATOM   289  C CG2 B THR   A 1 25  ? -10.196 -1.574  -31.318 0.18 82.03  ? 68  THR   A CG2 1 
ATOM   290  C CG2 C THR   A 1 25  ? -9.930  -1.584  -31.210 0.31 81.69  ? 68  THR   A CG2 1 
ATOM   291  C CG2 D THR   A 1 25  ? -9.930  -1.585  -31.211 0.31 81.69  ? 68  THR   A CG2 1 
ATOM   292  N N   A GLY   A 1 26  ? -7.809  -4.032  -30.477 0.20 81.30  ? 69  GLY   A N   1 
ATOM   293  N N   B GLY   A 1 26  ? -7.808  -4.033  -30.478 0.18 81.31  ? 69  GLY   A N   1 
ATOM   294  N N   C GLY   A 1 26  ? -7.861  -4.090  -30.418 0.31 80.87  ? 69  GLY   A N   1 
ATOM   295  N N   D GLY   A 1 26  ? -7.860  -4.090  -30.419 0.31 80.88  ? 69  GLY   A N   1 
ATOM   296  C CA  A GLY   A 1 26  ? -7.249  -4.514  -29.200 0.20 79.57  ? 69  GLY   A CA  1 
ATOM   297  C CA  B GLY   A 1 26  ? -7.249  -4.514  -29.200 0.18 79.58  ? 69  GLY   A CA  1 
ATOM   298  C CA  C GLY   A 1 26  ? -7.360  -4.568  -29.115 0.31 79.28  ? 69  GLY   A CA  1 
ATOM   299  C CA  D GLY   A 1 26  ? -7.360  -4.568  -29.115 0.31 79.28  ? 69  GLY   A CA  1 
ATOM   300  C C   A GLY   A 1 26  ? -6.722  -5.937  -29.304 0.20 79.93  ? 69  GLY   A C   1 
ATOM   301  C C   B GLY   A 1 26  ? -6.724  -5.938  -29.303 0.18 79.92  ? 69  GLY   A C   1 
ATOM   302  C C   C GLY   A 1 26  ? -6.877  -6.010  -29.170 0.31 79.83  ? 69  GLY   A C   1 
ATOM   303  C C   D GLY   A 1 26  ? -6.877  -6.010  -29.169 0.31 79.83  ? 69  GLY   A C   1 
ATOM   304  O O   A GLY   A 1 26  ? -7.203  -6.689  -30.177 0.20 80.40  ? 69  GLY   A O   1 
ATOM   305  O O   B GLY   A 1 26  ? -7.206  -6.690  -30.173 0.18 80.40  ? 69  GLY   A O   1 
ATOM   306  O O   C GLY   A 1 26  ? -7.499  -6.827  -29.881 0.31 79.94  ? 69  GLY   A O   1 
ATOM   307  O O   D GLY   A 1 26  ? -7.499  -6.827  -29.880 0.31 79.94  ? 69  GLY   A O   1 
ATOM   308  N N   A ASN   A 1 27  ? -5.768  -6.292  -28.437 0.20 79.83  ? 70  ASN   A N   1 
ATOM   309  N N   B ASN   A 1 27  ? -5.769  -6.292  -28.437 0.18 79.83  ? 70  ASN   A N   1 
ATOM   310  N N   C ASN   A 1 27  ? -5.814  -6.313  -28.417 0.31 80.39  ? 70  ASN   A N   1 
ATOM   311  N N   D ASN   A 1 27  ? -5.814  -6.313  -28.417 0.31 80.38  ? 70  ASN   A N   1 
ATOM   312  C CA  A ASN   A 1 27  ? -5.196  -7.661  -28.306 0.20 79.95  ? 70  ASN   A CA  1 
ATOM   313  C CA  B ASN   A 1 27  ? -5.196  -7.661  -28.305 0.18 79.95  ? 70  ASN   A CA  1 
ATOM   314  C CA  C ASN   A 1 27  ? -5.218  -7.669  -28.266 0.31 80.66  ? 70  ASN   A CA  1 
ATOM   315  C CA  D ASN   A 1 27  ? -5.218  -7.669  -28.266 0.31 80.66  ? 70  ASN   A CA  1 
ATOM   316  C C   A ASN   A 1 27  ? -5.737  -8.293  -27.013 0.20 76.56  ? 70  ASN   A C   1 
ATOM   317  C C   B ASN   A 1 27  ? -5.736  -8.293  -27.011 0.18 76.57  ? 70  ASN   A C   1 
ATOM   318  C C   C ASN   A 1 27  ? -5.847  -8.361  -27.044 0.31 76.94  ? 70  ASN   A C   1 
ATOM   319  C C   D ASN   A 1 27  ? -5.847  -8.361  -27.044 0.31 76.95  ? 70  ASN   A C   1 
ATOM   320  O O   A ASN   A 1 27  ? -6.578  -7.641  -26.354 0.20 74.31  ? 70  ASN   A O   1 
ATOM   321  O O   B ASN   A 1 27  ? -6.575  -7.640  -26.351 0.18 74.33  ? 70  ASN   A O   1 
ATOM   322  O O   C ASN   A 1 27  ? -6.871  -7.843  -26.536 0.31 74.52  ? 70  ASN   A O   1 
ATOM   323  O O   D ASN   A 1 27  ? -6.871  -7.843  -26.535 0.31 74.52  ? 70  ASN   A O   1 
ATOM   324  C CB  A ASN   A 1 27  ? -3.665  -7.625  -28.403 0.20 82.69  ? 70  ASN   A CB  1 
ATOM   325  C CB  B ASN   A 1 27  ? -3.666  -7.625  -28.402 0.18 82.69  ? 70  ASN   A CB  1 
ATOM   326  C CB  C ASN   A 1 27  ? -3.691  -7.571  -28.188 0.31 83.50  ? 70  ASN   A CB  1 
ATOM   327  C CB  D ASN   A 1 27  ? -3.691  -7.572  -28.188 0.31 83.50  ? 70  ASN   A CB  1 
ATOM   328  C CG  A ASN   A 1 27  ? -3.003  -6.779  -27.335 0.20 82.60  ? 70  ASN   A CG  1 
ATOM   329  C CG  B ASN   A 1 27  ? -3.003  -6.779  -27.335 0.18 82.60  ? 70  ASN   A CG  1 
ATOM   330  C CG  C ASN   A 1 27  ? -3.213  -6.888  -26.923 0.31 83.08  ? 70  ASN   A CG  1 
ATOM   331  C CG  D ASN   A 1 27  ? -3.213  -6.887  -26.923 0.31 83.08  ? 70  ASN   A CG  1 
ATOM   332  O OD1 A ASN   A 1 27  ? -3.601  -5.836  -26.818 0.20 81.41  ? 70  ASN   A OD1 1 
ATOM   333  O OD1 B ASN   A 1 27  ? -3.600  -5.836  -26.819 0.18 81.41  ? 70  ASN   A OD1 1 
ATOM   334  O OD1 C ASN   A 1 27  ? -3.461  -5.699  -26.723 0.31 83.22  ? 70  ASN   A OD1 1 
ATOM   335  O OD1 D ASN   A 1 27  ? -3.460  -5.698  -26.724 0.31 83.21  ? 70  ASN   A OD1 1 
ATOM   336  N ND2 A ASN   A 1 27  ? -1.765  -7.107  -26.998 0.20 84.08  ? 70  ASN   A ND2 1 
ATOM   337  N ND2 B ASN   A 1 27  ? -1.765  -7.108  -26.996 0.18 84.07  ? 70  ASN   A ND2 1 
ATOM   338  N ND2 C ASN   A 1 27  ? -2.535  -7.628  -26.059 0.31 82.98  ? 70  ASN   A ND2 1 
ATOM   339  N ND2 D ASN   A 1 27  ? -2.534  -7.627  -26.059 0.31 82.97  ? 70  ASN   A ND2 1 
ATOM   340  N N   A SER   A 1 28  ? -5.311  -9.523  -26.692 0.20 76.26  ? 71  SER   A N   1 
ATOM   341  N N   B SER   A 1 28  ? -5.311  -9.523  -26.692 0.18 76.28  ? 71  SER   A N   1 
ATOM   342  N N   C SER   A 1 28  ? -5.270  -9.485  -26.595 0.31 76.41  ? 71  SER   A N   1 
ATOM   343  N N   D SER   A 1 28  ? -5.270  -9.486  -26.595 0.31 76.41  ? 71  SER   A N   1 
ATOM   344  C CA  A SER   A 1 28  ? -5.752  -10.330 -25.518 0.20 73.95  ? 71  SER   A CA  1 
ATOM   345  C CA  B SER   A 1 28  ? -5.752  -10.330 -25.518 0.18 73.95  ? 71  SER   A CA  1 
ATOM   346  C CA  C SER   A 1 28  ? -5.776  -10.341 -25.484 0.31 74.01  ? 71  SER   A CA  1 
ATOM   347  C CA  D SER   A 1 28  ? -5.776  -10.341 -25.484 0.31 74.01  ? 71  SER   A CA  1 
ATOM   348  C C   A SER   A 1 28  ? -4.554  -10.738 -24.661 0.20 74.60  ? 71  SER   A C   1 
ATOM   349  C C   B SER   A 1 28  ? -4.554  -10.738 -24.661 0.18 74.60  ? 71  SER   A C   1 
ATOM   350  C C   C SER   A 1 28  ? -4.639  -10.772 -24.559 0.31 74.33  ? 71  SER   A C   1 
ATOM   351  C C   D SER   A 1 28  ? -4.639  -10.772 -24.559 0.31 74.33  ? 71  SER   A C   1 
ATOM   352  O O   A SER   A 1 28  ? -4.104  -11.879 -24.731 0.20 75.31  ? 71  SER   A O   1 
ATOM   353  O O   B SER   A 1 28  ? -4.104  -11.879 -24.732 0.18 75.30  ? 71  SER   A O   1 
ATOM   354  O O   C SER   A 1 28  ? -4.358  -11.960 -24.439 0.31 74.43  ? 71  SER   A O   1 
ATOM   355  O O   D SER   A 1 28  ? -4.358  -11.960 -24.439 0.31 74.43  ? 71  SER   A O   1 
ATOM   356  C CB  A SER   A 1 28  ? -6.529  -11.548 -25.958 0.20 73.03  ? 71  SER   A CB  1 
ATOM   357  C CB  B SER   A 1 28  ? -6.529  -11.548 -25.959 0.18 73.03  ? 71  SER   A CB  1 
ATOM   358  C CB  C SER   A 1 28  ? -6.514  -11.542 -26.019 0.31 73.24  ? 71  SER   A CB  1 
ATOM   359  C CB  D SER   A 1 28  ? -6.514  -11.542 -26.019 0.31 73.24  ? 71  SER   A CB  1 
ATOM   360  O OG  A SER   A 1 28  ? -7.495  -11.206 -26.939 0.20 73.68  ? 71  SER   A OG  1 
ATOM   361  O OG  B SER   A 1 28  ? -7.495  -11.205 -26.940 0.18 73.66  ? 71  SER   A OG  1 
ATOM   362  O OG  C SER   A 1 28  ? -7.376  -11.165 -27.082 0.31 74.23  ? 71  SER   A OG  1 
ATOM   363  O OG  D SER   A 1 28  ? -7.377  -11.165 -27.081 0.31 74.23  ? 71  SER   A OG  1 
ATOM   364  N N   . PRO   A 1 29  ? -4.003  -9.838  -23.815 1.00 74.78  ? 72  PRO   A N   1 
ATOM   365  C CA  . PRO   A 1 29  ? -2.803  -10.162 -23.050 1.00 75.92  ? 72  PRO   A CA  1 
ATOM   366  C C   . PRO   A 1 29  ? -3.149  -10.959 -21.780 1.00 73.17  ? 72  PRO   A C   1 
ATOM   367  O O   . PRO   A 1 29  ? -4.132  -10.641 -21.127 1.00 70.13  ? 72  PRO   A O   1 
ATOM   368  C CB  . PRO   A 1 29  ? -2.211  -8.769  -22.780 1.00 77.35  ? 72  PRO   A CB  1 
ATOM   369  C CG  . PRO   A 1 29  ? -3.420  -7.846  -22.696 1.00 75.74  ? 72  PRO   A CG  1 
ATOM   370  C CD  . PRO   A 1 29  ? -4.483  -8.463  -23.590 1.00 74.94  ? 72  PRO   A CD  1 
ATOM   371  N N   . ARG   A 1 30  ? -2.360  -11.994 -21.492 1.00 74.45  ? 73  ARG   A N   1 
ATOM   372  C CA  . ARG   A 1 30  ? -2.463  -12.793 -20.237 1.00 74.01  ? 73  ARG   A CA  1 
ATOM   373  C C   . ARG   A 1 30  ? -1.511  -12.164 -19.210 1.00 73.12  ? 73  ARG   A C   1 
ATOM   374  O O   . ARG   A 1 30  ? -0.310  -12.208 -19.428 1.00 73.59  ? 73  ARG   A O   1 
ATOM   375  C CB  . ARG   A 1 30  ? -2.195  -14.281 -20.504 1.00 76.41  ? 73  ARG   A CB  1 
ATOM   376  C CG  . ARG   A 1 30  ? -3.329  -14.985 -21.246 1.00 77.41  ? 73  ARG   A CG  1 
ATOM   377  C CD  . ARG   A 1 30  ? -2.923  -16.141 -22.177 1.00 81.41  ? 73  ARG   A CD  1 
ATOM   378  N NE  . ARG   A 1 30  ? -4.072  -16.660 -22.946 1.00 82.06  ? 73  ARG   A NE  1 
ATOM   379  C CZ  . ARG   A 1 30  ? -4.858  -17.691 -22.588 1.00 80.51  ? 73  ARG   A CZ  1 
ATOM   380  N NH1 . ARG   A 1 30  ? -4.613  -18.367 -21.476 1.00 81.01  ? 73  ARG   A NH1 1 
ATOM   381  N NH2 . ARG   A 1 30  ? -5.888  -18.048 -23.344 1.00 77.50  ? 73  ARG   A NH2 1 
ATOM   382  N N   . LEU   A 1 31  ? -2.057  -11.537 -18.161 1.00 70.56  ? 74  LEU   A N   1 
ATOM   383  C CA  . LEU   A 1 31  ? -1.278  -10.698 -17.215 1.00 70.51  ? 74  LEU   A CA  1 
ATOM   384  C C   . LEU   A 1 31  ? -1.418  -11.268 -15.796 1.00 67.80  ? 74  LEU   A C   1 
ATOM   385  O O   . LEU   A 1 31  ? -2.553  -11.541 -15.384 1.00 65.26  ? 74  LEU   A O   1 
ATOM   386  C CB  . LEU   A 1 31  ? -1.778  -9.256  -17.304 1.00 70.47  ? 74  LEU   A CB  1 
ATOM   387  C CG  . LEU   A 1 31  ? -1.493  -8.535  -18.620 1.00 72.82  ? 74  LEU   A CG  1 
ATOM   388  C CD1 . LEU   A 1 31  ? -1.975  -7.097  -18.553 1.00 72.57  ? 74  LEU   A CD1 1 
ATOM   389  C CD2 . LEU   A 1 31  ? -0.012  -8.587  -18.967 1.00 75.87  ? 74  LEU   A CD2 1 
ATOM   390  N N   . ASP   A 1 32  ? -0.284  -11.467 -15.115 1.00 68.00  ? 75  ASP   A N   1 
ATOM   391  C CA  . ASP   A 1 32  ? -0.201  -11.750 -13.661 1.00 66.68  ? 75  ASP   A CA  1 
ATOM   392  C C   . ASP   A 1 32  ? -0.362  -10.455 -12.869 1.00 64.51  ? 75  ASP   A C   1 
ATOM   393  O O   . ASP   A 1 32  ? 0.493   -9.538  -13.007 1.00 66.31  ? 75  ASP   A O   1 
ATOM   394  C CB  . ASP   A 1 32  ? 1.124   -12.417 -13.325 1.00 70.06  ? 75  ASP   A CB  1 
ATOM   395  C CG  . ASP   A 1 32  ? 1.144   -13.867 -13.746 1.00 70.82  ? 75  ASP   A CG  1 
ATOM   396  O OD1 . ASP   A 1 32  ? 0.052   -14.487 -13.737 1.00 69.75  ? 75  ASP   A OD1 1 
ATOM   397  O OD2 . ASP   A 1 32  ? 2.231   -14.357 -14.063 1.00 74.39  ? 75  ASP   A OD2 1 
ATOM   398  N N   . VAL   A 1 33  ? -1.416  -10.384 -12.063 1.00 60.89  ? 76  VAL   A N   1 
ATOM   399  C CA  . VAL   A 1 33  ? -1.788  -9.125  -11.358 1.00 60.07  ? 76  VAL   A CA  1 
ATOM   400  C C   . VAL   A 1 33  ? -2.152  -9.451  -9.909  1.00 58.59  ? 76  VAL   A C   1 
ATOM   401  O O   . VAL   A 1 33  ? -2.624  -10.578 -9.648  1.00 57.06  ? 76  VAL   A O   1 
ATOM   402  C CB  . VAL   A 1 33  ? -2.944  -8.380  -12.060 1.00 58.40  ? 76  VAL   A CB  1 
ATOM   403  C CG1 . VAL   A 1 33  ? -2.632  -8.094  -13.527 1.00 59.57  ? 76  VAL   A CG1 1 
ATOM   404  C CG2 . VAL   A 1 33  ? -4.278  -9.099  -11.921 1.00 56.07  ? 76  VAL   A CG2 1 
ATOM   405  N N   . ALA   A 1 34  ? -2.046  -8.436  -9.050  1.00 58.49  ? 77  ALA   A N   1 
ATOM   406  C CA  . ALA   A 1 34  ? -2.486  -8.472  -7.637  1.00 57.36  ? 77  ALA   A CA  1 
ATOM   407  C C   . ALA   A 1 34  ? -3.474  -7.334  -7.414  1.00 55.43  ? 77  ALA   A C   1 
ATOM   408  O O   . ALA   A 1 34  ? -3.326  -6.308  -8.056  1.00 55.70  ? 77  ALA   A O   1 
ATOM   409  C CB  . ALA   A 1 34  ? -1.293  -8.360  -6.720  1.00 59.64  ? 77  ALA   A CB  1 
ATOM   410  N N   . LEU   A 1 35  ? -4.452  -7.549  -6.545  1.00 53.49  ? 78  LEU   A N   1 
ATOM   411  C CA  . LEU   A 1 35  ? -5.512  -6.579  -6.196  1.00 52.30  ? 78  LEU   A CA  1 
ATOM   412  C C   . LEU   A 1 35  ? -5.348  -6.221  -4.713  1.00 53.35  ? 78  LEU   A C   1 
ATOM   413  O O   . LEU   A 1 35  ? -5.378  -7.164  -3.873  1.00 53.36  ? 78  LEU   A O   1 
ATOM   414  C CB  . LEU   A 1 35  ? -6.867  -7.236  -6.484  1.00 50.25  ? 78  LEU   A CB  1 
ATOM   415  C CG  . LEU   A 1 35  ? -8.108  -6.401  -6.162  1.00 49.07  ? 78  LEU   A CG  1 
ATOM   416  C CD1 . LEU   A 1 35  ? -8.115  -5.075  -6.905  1.00 49.55  ? 78  LEU   A CD1 1 
ATOM   417  C CD2 . LEU   A 1 35  ? -9.373  -7.194  -6.460  1.00 47.20  ? 78  LEU   A CD2 1 
ATOM   418  N N   . ASP   A 1 36  ? -5.084  -4.947  -4.427  1.00 54.05  ? 79  ASP   A N   1 
ATOM   419  C CA  . ASP   A 1 36  ? -4.797  -4.445  -3.058  1.00 55.33  ? 79  ASP   A CA  1 
ATOM   420  C C   . ASP   A 1 36  ? -6.122  -4.036  -2.382  1.00 54.05  ? 79  ASP   A C   1 
ATOM   421  O O   . ASP   A 1 36  ? -7.211  -4.094  -3.028  1.00 51.25  ? 79  ASP   A O   1 
ATOM   422  C CB  . ASP   A 1 36  ? -3.725  -3.346  -3.094  1.00 57.19  ? 79  ASP   A CB  1 
ATOM   423  C CG  . ASP   A 1 36  ? -4.196  -1.949  -3.466  1.00 57.03  ? 79  ASP   A CG  1 
ATOM   424  O OD1 . ASP   A 1 36  ? -5.406  -1.765  -3.675  1.00 55.31  ? 79  ASP   A OD1 1 
ATOM   425  O OD2 . ASP   A 1 36  ? -3.340  -1.039  -3.530  1.00 58.77  ? 79  ASP   A OD2 1 
ATOM   426  N N   . GLU   A 1 37  ? -6.035  -3.638  -1.110  1.00 55.01  ? 80  GLU   A N   1 
ATOM   427  C CA  . GLU   A 1 37  ? -7.231  -3.332  -0.292  1.00 54.47  ? 80  GLU   A CA  1 
ATOM   428  C C   . GLU   A 1 37  ? -7.918  -2.058  -0.800  1.00 53.69  ? 80  GLU   A C   1 
ATOM   429  O O   . GLU   A 1 37  ? -9.121  -1.932  -0.548  1.00 52.25  ? 80  GLU   A O   1 
ATOM   430  C CB  . GLU   A 1 37  ? -6.839  -3.221  1.183   1.00 56.31  ? 80  GLU   A CB  1 
ATOM   431  C CG  . GLU   A 1 37  ? -8.038  -3.250  2.108   1.00 55.97  ? 80  GLU   A CG  1 
ATOM   432  C CD  . GLU   A 1 37  ? -7.683  -3.240  3.594   1.00 57.96  ? 80  GLU   A CD  1 
ATOM   433  O OE1 . GLU   A 1 37  ? -7.127  -2.236  4.067   1.00 59.33  ? 80  GLU   A OE1 1 
ATOM   434  O OE2 . GLU   A 1 37  ? -7.957  -4.250  4.250   1.00 58.00  ? 80  GLU   A OE2 1 
ATOM   435  N N   . SER   A 1 38  ? -7.180  -1.163  -1.477  1.00 54.79  ? 81  SER   A N   1 
ATOM   436  C CA  . SER   A 1 38  ? -7.699  0.094   -2.070  1.00 54.72  ? 81  SER   A CA  1 
ATOM   437  C C   . SER   A 1 38  ? -8.357  -0.154  -3.434  1.00 53.05  ? 81  SER   A C   1 
ATOM   438  O O   . SER   A 1 38  ? -8.832  0.827   -4.017  1.00 52.68  ? 81  SER   A O   1 
ATOM   439  C CB  . SER   A 1 38  ? -6.618  1.101   -2.207  1.00 56.90  ? 81  SER   A CB  1 
ATOM   440  O OG  . SER   A 1 38  ? -6.139  1.485   -0.935  1.00 59.12  ? 81  SER   A OG  1 
ATOM   441  N N   . GLY   A 1 39  ? -8.394  -1.402  -3.913  1.00 52.21  ? 82  GLY   A N   1 
ATOM   442  C CA  . GLY   A 1 39  ? -8.961  -1.778  -5.227  1.00 51.27  ? 82  GLY   A CA  1 
ATOM   443  C C   . GLY   A 1 39  ? -8.083  -1.334  -6.404  1.00 52.27  ? 82  GLY   A C   1 
ATOM   444  O O   . GLY   A 1 39  ? -8.650  -1.103  -7.473  1.00 51.07  ? 82  GLY   A O   1 
ATOM   445  N N   . ASP   A 1 40  ? -6.774  -1.165  -6.199  1.00 54.52  ? 83  ASP   A N   1 
ATOM   446  C CA  . ASP   A 1 40  ? -5.782  -0.905  -7.273  1.00 56.17  ? 83  ASP   A CA  1 
ATOM   447  C C   . ASP   A 1 40  ? -5.197  -2.250  -7.700  1.00 56.10  ? 83  ASP   A C   1 
ATOM   448  O O   . ASP   A 1 40  ? -4.648  -2.983  -6.819  1.00 55.90  ? 83  ASP   A O   1 
ATOM   449  C CB  . ASP   A 1 40  ? -4.670  0.057   -6.839  1.00 59.17  ? 83  ASP   A CB  1 
ATOM   450  C CG  . ASP   A 1 40  ? -5.147  1.423   -6.374  1.00 60.33  ? 83  ASP   A CG  1 
ATOM   451  O OD1 . ASP   A 1 40  ? -6.095  1.948   -6.943  1.00 59.50  ? 83  ASP   A OD1 1 
ATOM   452  O OD2 . ASP   A 1 40  ? -4.563  1.943   -5.417  1.00 64.06  ? 83  ASP   A OD2 1 
ATOM   453  N N   . PHE   A 1 41  ? -5.277  -2.574  -8.998  1.00 55.46  ? 84  PHE   A N   1 
ATOM   454  C CA  . PHE   A 1 41  ? -4.551  -3.736  -9.575  1.00 55.76  ? 84  PHE   A CA  1 
ATOM   455  C C   . PHE   A 1 41  ? -3.105  -3.333  -9.812  1.00 58.98  ? 84  PHE   A C   1 
ATOM   456  O O   . PHE   A 1 41  ? -2.870  -2.134  -10.010 1.00 60.07  ? 84  PHE   A O   1 
ATOM   457  C CB  . PHE   A 1 41  ? -5.155  -4.226  -10.886 1.00 53.88  ? 84  PHE   A CB  1 
ATOM   458  C CG  . PHE   A 1 41  ? -6.457  -4.972  -10.779 1.00 50.87  ? 84  PHE   A CG  1 
ATOM   459  C CD1 . PHE   A 1 41  ? -6.481  -6.310  -10.435 1.00 49.87  ? 84  PHE   A CD1 1 
ATOM   460  C CD2 . PHE   A 1 41  ? -7.652  -4.343  -11.089 1.00 49.08  ? 84  PHE   A CD2 1 
ATOM   461  C CE1 . PHE   A 1 41  ? -7.683  -7.001  -10.382 1.00 47.85  ? 84  PHE   A CE1 1 
ATOM   462  C CE2 . PHE   A 1 41  ? -8.845  -5.041  -11.061 1.00 47.14  ? 84  PHE   A CE2 1 
ATOM   463  C CZ  . PHE   A 1 41  ? -8.864  -6.357  -10.701 1.00 46.59  ? 84  PHE   A CZ  1 
ATOM   464  N N   . SER   A 1 42  ? -2.196  -4.307  -9.811  1.00 60.91  ? 85  SER   A N   1 
ATOM   465  C CA  . SER   A 1 42  ? -0.760  -4.117  -10.108 1.00 64.91  ? 85  SER   A CA  1 
ATOM   466  C C   . SER   A 1 42  ? -0.206  -5.351  -10.839 1.00 66.59  ? 85  SER   A C   1 
ATOM   467  O O   . SER   A 1 42  ? -0.749  -6.456  -10.644 1.00 64.84  ? 85  SER   A O   1 
ATOM   468  C CB  . SER   A 1 42  ? -0.006  -3.836  -8.835  1.00 66.58  ? 85  SER   A CB  1 
ATOM   469  O OG  . SER   A 1 42  ? -0.305  -4.806  -7.848  1.00 65.28  ? 85  SER   A OG  1 
ATOM   470  N N   . LEU   A 1 43  ? 0.842   -5.171  -11.647 1.00 70.54  ? 86  LEU   A N   1 
ATOM   471  C CA  . LEU   A 1 43  ? 1.516   -6.292  -12.363 1.00 73.07  ? 86  LEU   A CA  1 
ATOM   472  C C   . LEU   A 1 43  ? 2.455   -7.023  -11.415 1.00 75.42  ? 86  LEU   A C   1 
ATOM   473  O O   . LEU   A 1 43  ? 3.302   -6.368  -10.801 1.00 77.02  ? 86  LEU   A O   1 
ATOM   474  C CB  . LEU   A 1 43  ? 2.303   -5.775  -13.568 1.00 75.78  ? 86  LEU   A CB  1 
ATOM   475  C CG  . LEU   A 1 43  ? 1.440   -5.278  -14.723 1.00 75.78  ? 86  LEU   A CG  1 
ATOM   476  C CD1 . LEU   A 1 43  ? 2.289   -4.538  -15.740 1.00 79.32  ? 86  LEU   A CD1 1 
ATOM   477  C CD2 . LEU   A 1 43  ? 0.682   -6.420  -15.387 1.00 74.52  ? 86  LEU   A CD2 1 
ATOM   478  N N   . VAL   A 1 44  ? 2.318   -8.342  -11.366 1.00 76.79  ? 87  VAL   A N   1 
ATOM   479  C CA  . VAL   A 1 44  ? 3.230   -9.275  -10.648 1.00 80.59  ? 87  VAL   A CA  1 
ATOM   480  C C   . VAL   A 1 44  ? 4.131   -9.941  -11.691 1.00 85.11  ? 87  VAL   A C   1 
ATOM   481  O O   . VAL   A 1 44  ? 3.623   -10.812 -12.402 1.00 85.21  ? 87  VAL   A O   1 
ATOM   482  C CB  . VAL   A 1 44  ? 2.407   -10.330 -9.889  1.00 78.21  ? 87  VAL   A CB  1 
ATOM   483  C CG1 . VAL   A 1 44  ? 3.297   -11.387 -9.248  1.00 80.11  ? 87  VAL   A CG1 1 
ATOM   484  C CG2 . VAL   A 1 44  ? 1.472   -9.690  -8.873  1.00 76.12  ? 87  VAL   A CG2 1 
ATOM   485  N N   . GLU   A 1 45  ? 5.405   -9.568  -11.795 1.00 91.17  ? 88  GLU   A N   1 
ATOM   486  C CA  . GLU   A 1 45  ? 6.371   -10.291 -12.675 1.00 96.51  ? 88  GLU   A CA  1 
ATOM   487  C C   . GLU   A 1 45  ? 7.136   -11.333 -11.852 1.00 98.08  ? 88  GLU   A C   1 
ATOM   488  O O   . GLU   A 1 45  ? 6.541   -12.295 -11.367 1.00 96.77  ? 88  GLU   A O   1 
ATOM   489  C CB  . GLU   A 1 45  ? 7.323   -9.319  -13.370 1.00 101.43 ? 88  GLU   A CB  1 
ATOM   490  C CG  . GLU   A 1 45  ? 6.611   -8.137  -14.004 1.00 101.75 ? 88  GLU   A CG  1 
ATOM   491  C CD  . GLU   A 1 45  ? 5.563   -8.501  -15.036 1.00 101.12 ? 88  GLU   A CD  1 
ATOM   492  O OE1 . GLU   A 1 45  ? 4.436   -8.885  -14.636 1.00 99.57  ? 88  GLU   A OE1 1 
ATOM   493  O OE2 . GLU   A 1 45  ? 5.878   -8.388  -16.235 1.00 104.60 ? 88  GLU   A OE2 1 
ATOM   494  N N   . GLY   B 2 7   ? -36.011 11.886  -11.532 1.00 59.62  ? 16  GLY   B N   1 
ATOM   495  C CA  . GLY   B 2 7   ? -35.121 12.028  -12.739 1.00 58.82  ? 16  GLY   B CA  1 
ATOM   496  C C   . GLY   B 2 7   ? -35.469 11.057  -13.859 1.00 57.63  ? 16  GLY   B C   1 
ATOM   497  O O   . GLY   B 2 7   ? -36.550 10.411  -13.800 1.00 57.14  ? 16  GLY   B O   1 
ATOM   498  N N   . GLU   B 2 8   ? -34.582 10.975  -14.859 1.00 54.95  ? 17  GLU   B N   1 
ATOM   499  C CA  . GLU   B 2 8   ? -34.665 10.019  -15.990 1.00 54.14  ? 17  GLU   B CA  1 
ATOM   500  C C   . GLU   B 2 8   ? -34.264 8.633   -15.480 1.00 51.25  ? 17  GLU   B C   1 
ATOM   501  O O   . GLU   B 2 8   ? -33.143 8.467   -14.992 1.00 49.68  ? 17  GLU   B O   1 
ATOM   502  C CB  . GLU   B 2 8   ? -33.744 10.456  -17.131 1.00 53.70  ? 17  GLU   B CB  1 
ATOM   503  C CG  . GLU   B 2 8   ? -33.936 9.637   -18.388 1.00 55.25  ? 17  GLU   B CG  1 
ATOM   504  C CD  . GLU   B 2 8   ? -33.155 10.182  -19.573 1.00 55.27  ? 17  GLU   B CD  1 
ATOM   505  O OE1 . GLU   B 2 8   ? -32.178 10.976  -19.349 1.00 52.77  ? 17  GLU   B OE1 1 
ATOM   506  O OE2 . GLU   B 2 8   ? -33.550 9.838   -20.716 1.00 60.08  ? 17  GLU   B OE2 1 
ATOM   507  N N   A THR   B 2 9   ? -35.166 7.657   -15.595 0.25 51.28  ? 18  THR   B N   1 
ATOM   508  N N   B THR   B 2 9   ? -35.191 7.677   -15.602 0.25 51.08  ? 18  THR   B N   1 
ATOM   509  N N   C THR   B 2 9   ? -35.166 7.657   -15.595 0.25 51.28  ? 18  THR   B N   1 
ATOM   510  N N   D THR   B 2 9   ? -35.191 7.677   -15.602 0.25 51.08  ? 18  THR   B N   1 
ATOM   511  C CA  A THR   B 2 9   ? -34.977 6.279   -15.069 0.25 51.07  ? 18  THR   B CA  1 
ATOM   512  C CA  B THR   B 2 9   ? -35.094 6.297   -15.056 0.25 50.75  ? 18  THR   B CA  1 
ATOM   513  C CA  C THR   B 2 9   ? -34.977 6.279   -15.069 0.25 51.07  ? 18  THR   B CA  1 
ATOM   514  C CA  D THR   B 2 9   ? -35.094 6.297   -15.056 0.25 50.75  ? 18  THR   B CA  1 
ATOM   515  C C   A THR   B 2 9   ? -35.075 5.260   -16.207 0.25 50.00  ? 18  THR   B C   1 
ATOM   516  C C   B THR   B 2 9   ? -34.928 5.287   -16.204 0.25 49.77  ? 18  THR   B C   1 
ATOM   517  C C   C THR   B 2 9   ? -35.075 5.260   -16.207 0.25 50.00  ? 18  THR   B C   1 
ATOM   518  C C   D THR   B 2 9   ? -34.928 5.287   -16.204 0.25 49.77  ? 18  THR   B C   1 
ATOM   519  O O   A THR   B 2 9   ? -35.152 4.056   -15.906 0.25 49.77  ? 18  THR   B O   1 
ATOM   520  O O   B THR   B 2 9   ? -34.625 4.118   -15.910 0.25 49.57  ? 18  THR   B O   1 
ATOM   521  O O   C THR   B 2 9   ? -35.152 4.056   -15.906 0.25 49.77  ? 18  THR   B O   1 
ATOM   522  O O   D THR   B 2 9   ? -34.625 4.118   -15.910 0.25 49.57  ? 18  THR   B O   1 
ATOM   523  C CB  A THR   B 2 9   ? -35.988 5.993   -13.954 0.25 51.93  ? 18  THR   B CB  1 
ATOM   524  C CB  B THR   B 2 9   ? -36.310 5.988   -14.167 0.25 51.35  ? 18  THR   B CB  1 
ATOM   525  C CB  C THR   B 2 9   ? -35.988 5.993   -13.954 0.25 51.93  ? 18  THR   B CB  1 
ATOM   526  C CB  D THR   B 2 9   ? -36.310 5.988   -14.167 0.25 51.35  ? 18  THR   B CB  1 
ATOM   527  O OG1 A THR   B 2 9   ? -35.977 7.146   -13.114 0.25 53.05  ? 18  THR   B OG1 1 
ATOM   528  O OG1 B THR   B 2 9   ? -37.495 5.958   -14.961 0.25 52.08  ? 18  THR   B OG1 1 
ATOM   529  O OG1 C THR   B 2 9   ? -35.977 7.146   -13.114 0.25 53.05  ? 18  THR   B OG1 1 
ATOM   530  O OG1 D THR   B 2 9   ? -37.495 5.958   -14.961 0.25 52.08  ? 18  THR   B OG1 1 
ATOM   531  C CG2 A THR   B 2 9   ? -35.667 4.749   -13.155 0.25 51.93  ? 18  THR   B CG2 1 
ATOM   532  C CG2 B THR   B 2 9   ? -36.520 7.000   -13.062 0.25 52.13  ? 18  THR   B CG2 1 
ATOM   533  C CG2 C THR   B 2 9   ? -35.667 4.749   -13.155 0.25 51.93  ? 18  THR   B CG2 1 
ATOM   534  C CG2 D THR   B 2 9   ? -36.520 7.000   -13.062 0.25 52.13  ? 18  THR   B CG2 1 
ATOM   535  N N   . THR   B 2 10  ? -35.080 5.714   -17.465 1.00 49.52  ? 19  THR   B N   1 
ATOM   536  C CA  . THR   B 2 10  ? -35.032 4.797   -18.629 1.00 47.73  ? 19  THR   B CA  1 
ATOM   537  C C   . THR   B 2 10  ? -33.708 4.014   -18.602 1.00 43.84  ? 19  THR   B C   1 
ATOM   538  O O   . THR   B 2 10  ? -32.657 4.635   -18.420 1.00 43.98  ? 19  THR   B O   1 
ATOM   539  C CB  . THR   B 2 10  ? -35.219 5.543   -19.965 1.00 48.27  ? 19  THR   B CB  1 
ATOM   540  O OG1 . THR   B 2 10  ? -36.262 6.514   -19.832 1.00 51.18  ? 19  THR   B OG1 1 
ATOM   541  C CG2 . THR   B 2 10  ? -35.591 4.589   -21.071 1.00 49.68  ? 19  THR   B CG2 1 
ATOM   542  N N   . ASP   B 2 11  ? -33.758 2.695   -18.759 1.00 42.57  ? 20  ASP   B N   1 
ATOM   543  C CA  . ASP   B 2 11  ? -32.556 1.851   -19.000 1.00 42.64  ? 20  ASP   B CA  1 
ATOM   544  C C   . ASP   B 2 11  ? -31.635 2.465   -20.064 1.00 43.13  ? 20  ASP   B C   1 
ATOM   545  O O   . ASP   B 2 11  ? -32.170 3.180   -20.970 1.00 42.57  ? 20  ASP   B O   1 
ATOM   546  C CB  . ASP   B 2 11  ? -32.950 0.450   -19.441 1.00 43.68  ? 20  ASP   B CB  1 
ATOM   547  C CG  . ASP   B 2 11  ? -33.515 -0.453  -18.358 1.00 44.46  ? 20  ASP   B CG  1 
ATOM   548  O OD1 . ASP   B 2 11  ? -33.737 0.018   -17.229 1.00 43.56  ? 20  ASP   B OD1 1 
ATOM   549  O OD2 . ASP   B 2 11  ? -33.736 -1.639  -18.674 1.00 46.22  ? 20  ASP   B OD2 1 
ATOM   550  N N   . GLY   B 2 12  ? -30.331 2.187   -19.974 1.00 40.48  ? 21  GLY   B N   1 
ATOM   551  C CA  . GLY   B 2 12  ? -29.308 2.501   -20.989 1.00 39.99  ? 21  GLY   B CA  1 
ATOM   552  C C   . GLY   B 2 12  ? -28.041 2.997   -20.348 1.00 39.08  ? 21  GLY   B C   1 
ATOM   553  O O   . GLY   B 2 12  ? -27.879 2.832   -19.107 1.00 36.32  ? 21  GLY   B O   1 
ATOM   554  N N   . VAL   B 2 13  ? -27.198 3.680   -21.089 1.00 36.46  ? 22  VAL   B N   1 
ATOM   555  C CA  . VAL   B 2 13  ? -25.836 4.100   -20.651 1.00 36.17  ? 22  VAL   B CA  1 
ATOM   556  C C   . VAL   B 2 13  ? -25.867 5.602   -20.476 1.00 36.74  ? 22  VAL   B C   1 
ATOM   557  O O   . VAL   B 2 13  ? -26.582 6.287   -21.249 1.00 39.42  ? 22  VAL   B O   1 
ATOM   558  C CB  . VAL   B 2 13  ? -24.719 3.579   -21.567 1.00 35.27  ? 22  VAL   B CB  1 
ATOM   559  C CG1 . VAL   B 2 13  ? -24.827 4.095   -23.055 1.00 35.97  ? 22  VAL   B CG1 1 
ATOM   560  C CG2 . VAL   B 2 13  ? -23.303 3.804   -21.054 1.00 34.72  ? 22  VAL   B CG2 1 
ATOM   561  N N   . TYR   B 2 14  ? -25.237 6.098   -19.405 1.00 35.58  ? 23  TYR   B N   1 
ATOM   562  C CA  . TYR   B 2 14  ? -25.278 7.521   -19.011 1.00 35.19  ? 23  TYR   B CA  1 
ATOM   563  C C   . TYR   B 2 14  ? -23.847 7.985   -18.767 1.00 35.85  ? 23  TYR   B C   1 
ATOM   564  O O   . TYR   B 2 14  ? -22.995 7.239   -18.189 1.00 36.38  ? 23  TYR   B O   1 
ATOM   565  C CB  . TYR   B 2 14  ? -26.076 7.744   -17.709 1.00 34.69  ? 23  TYR   B CB  1 
ATOM   566  C CG  . TYR   B 2 14  ? -27.559 7.529   -17.793 1.00 34.29  ? 23  TYR   B CG  1 
ATOM   567  C CD1 . TYR   B 2 14  ? -28.074 6.271   -18.062 1.00 34.16  ? 23  TYR   B CD1 1 
ATOM   568  C CD2 . TYR   B 2 14  ? -28.424 8.607   -17.658 1.00 34.95  ? 23  TYR   B CD2 1 
ATOM   569  C CE1 . TYR   B 2 14  ? -29.437 6.074   -18.190 1.00 35.19  ? 23  TYR   B CE1 1 
ATOM   570  C CE2 . TYR   B 2 14  ? -29.801 8.426   -17.717 1.00 35.98  ? 23  TYR   B CE2 1 
ATOM   571  C CZ  . TYR   B 2 14  ? -30.291 7.153   -18.016 1.00 36.65  ? 23  TYR   B CZ  1 
ATOM   572  O OH  . TYR   B 2 14  ? -31.633 6.988   -18.143 1.00 39.98  ? 23  TYR   B OH  1 
ATOM   573  N N   . ARG   B 2 15  ? -23.640 9.257   -19.055 1.00 36.61  ? 24  ARG   B N   1 
ATOM   574  C CA  . ARG   B 2 15  ? -22.429 10.032  -18.699 1.00 36.89  ? 24  ARG   B CA  1 
ATOM   575  C C   . ARG   B 2 15  ? -22.561 10.504  -17.234 1.00 36.55  ? 24  ARG   B C   1 
ATOM   576  O O   . ARG   B 2 15  ? -23.629 11.022  -16.832 1.00 35.75  ? 24  ARG   B O   1 
ATOM   577  C CB  . ARG   B 2 15  ? -22.308 11.264  -19.576 1.00 38.51  ? 24  ARG   B CB  1 
ATOM   578  C CG  . ARG   B 2 15  ? -22.167 10.946  -21.056 1.00 39.50  ? 24  ARG   B CG  1 
ATOM   579  C CD  . ARG   B 2 15  ? -22.086 12.237  -21.826 1.00 40.86  ? 24  ARG   B CD  1 
ATOM   580  N NE  . ARG   B 2 15  ? -22.179 11.938  -23.259 1.00 41.58  ? 24  ARG   B NE  1 
ATOM   581  C CZ  . ARG   B 2 15  ? -21.130 11.672  -24.033 1.00 42.25  ? 24  ARG   B CZ  1 
ATOM   582  N NH1 . ARG   B 2 15  ? -19.888 11.750  -23.569 1.00 40.84  ? 24  ARG   B NH1 1 
ATOM   583  N NH2 . ARG   B 2 15  ? -21.329 11.392  -25.317 1.00 43.00  ? 24  ARG   B NH2 1 
ATOM   584  N N   . VAL   B 2 16  ? -21.436 10.501  -16.525 1.00 37.60  ? 25  VAL   B N   1 
ATOM   585  C CA  . VAL   B 2 16  ? -21.383 11.097  -15.167 1.00 37.72  ? 25  VAL   B CA  1 
ATOM   586  C C   . VAL   B 2 16  ? -20.560 12.389  -15.231 1.00 38.66  ? 25  VAL   B C   1 
ATOM   587  O O   . VAL   B 2 16  ? -19.410 12.317  -15.591 1.00 38.98  ? 25  VAL   B O   1 
ATOM   588  C CB  . VAL   B 2 16  ? -20.824 10.058  -14.172 1.00 37.02  ? 25  VAL   B CB  1 
ATOM   589  C CG1 . VAL   B 2 16  ? -20.787 10.645  -12.758 1.00 36.97  ? 25  VAL   B CG1 1 
ATOM   590  C CG2 . VAL   B 2 16  ? -21.658 8.779   -14.185 1.00 36.36  ? 25  VAL   B CG2 1 
ATOM   591  N N   . MET   B 2 17  ? -21.128 13.521  -14.836 1.00 41.15  ? 26  MET   B N   1 
ATOM   592  C CA  . MET   B 2 17  ? -20.555 14.874  -15.068 1.00 43.62  ? 26  MET   B CA  1 
ATOM   593  C C   . MET   B 2 17  ? -20.390 15.624  -13.739 1.00 45.13  ? 26  MET   B C   1 
ATOM   594  O O   . MET   B 2 17  ? -21.212 15.399  -12.810 1.00 43.16  ? 26  MET   B O   1 
ATOM   595  C CB  . MET   B 2 17  ? -21.476 15.705  -15.962 1.00 44.36  ? 26  MET   B CB  1 
ATOM   596  C CG  . MET   B 2 17  ? -21.956 14.985  -17.226 1.00 45.04  ? 26  MET   B CG  1 
ATOM   597  S SD  . MET   B 2 17  ? -20.673 14.680  -18.483 1.00 44.41  ? 26  MET   B SD  1 
ATOM   598  C CE  . MET   B 2 17  ? -19.904 16.293  -18.584 1.00 46.71  ? 26  MET   B CE  1 
ATOM   599  N N   . THR   B 2 18  ? -19.408 16.528  -13.682 1.00 47.43  ? 27  THR   B N   1 
ATOM   600  C CA  . THR   B 2 18  ? -19.237 17.519  -12.595 1.00 51.59  ? 27  THR   B CA  1 
ATOM   601  C C   . THR   B 2 18  ? -19.069 18.930  -13.176 1.00 56.02  ? 27  THR   B C   1 
ATOM   602  O O   . THR   B 2 18  ? -18.463 19.076  -14.275 1.00 52.95  ? 27  THR   B O   1 
ATOM   603  C CB  . THR   B 2 18  ? -18.047 17.177  -11.685 1.00 51.80  ? 27  THR   B CB  1 
ATOM   604  O OG1 . THR   B 2 18  ? -18.137 18.083  -10.577 1.00 53.81  ? 27  THR   B OG1 1 
ATOM   605  C CG2 . THR   B 2 18  ? -16.701 17.295  -12.364 1.00 52.20  ? 27  THR   B CG2 1 
ATOM   606  N N   . ARG   B 2 19  ? -19.505 19.937  -12.410 1.00 60.09  ? 28  ARG   B N   1 
ATOM   607  C CA  . ARG   B 2 19  ? -19.195 21.366  -12.685 1.00 65.73  ? 28  ARG   B CA  1 
ATOM   608  C C   . ARG   B 2 19  ? -18.178 21.905  -11.663 1.00 67.00  ? 28  ARG   B C   1 
ATOM   609  O O   . ARG   B 2 19  ? -17.878 23.106  -11.715 1.00 67.38  ? 28  ARG   B O   1 
ATOM   610  C CB  . ARG   B 2 19  ? -20.501 22.158  -12.719 1.00 69.03  ? 28  ARG   B CB  1 
ATOM   611  C CG  . ARG   B 2 19  ? -21.494 21.618  -13.737 1.00 70.90  ? 28  ARG   B CG  1 
ATOM   612  C CD  . ARG   B 2 19  ? -22.017 22.718  -14.629 1.00 74.04  ? 28  ARG   B CD  1 
ATOM   613  N NE  . ARG   B 2 19  ? -23.001 22.251  -15.599 1.00 76.51  ? 28  ARG   B NE  1 
ATOM   614  C CZ  . ARG   B 2 19  ? -24.306 22.096  -15.363 1.00 78.29  ? 28  ARG   B CZ  1 
ATOM   615  N NH1 . ARG   B 2 19  ? -24.816 22.356  -14.167 1.00 80.41  ? 28  ARG   B NH1 1 
ATOM   616  N NH2 . ARG   B 2 19  ? -25.104 21.676  -16.330 1.00 78.24  ? 28  ARG   B NH2 1 
ATOM   617  N N   . ARG   B 2 20  ? -17.595 21.032  -10.838 1.00 69.89  ? 29  ARG   B N   1 
ATOM   618  C CA  . ARG   B 2 20  ? -16.658 21.397  -9.736  1.00 74.95  ? 29  ARG   B CA  1 
ATOM   619  C C   . ARG   B 2 20  ? -15.294 21.822  -10.311 1.00 73.31  ? 29  ARG   B C   1 
ATOM   620  O O   . ARG   B 2 20  ? -14.437 22.285  -9.535  1.00 72.69  ? 29  ARG   B O   1 
ATOM   621  C CB  . ARG   B 2 20  ? -16.541 20.213  -8.770  1.00 78.50  ? 29  ARG   B CB  1 
ATOM   622  C CG  . ARG   B 2 20  ? -16.119 20.578  -7.354  1.00 84.47  ? 29  ARG   B CG  1 
ATOM   623  C CD  . ARG   B 2 20  ? -15.662 19.341  -6.594  1.00 89.80  ? 29  ARG   B CD  1 
ATOM   624  N NE  . ARG   B 2 20  ? -14.547 18.651  -7.256  1.00 93.73  ? 29  ARG   B NE  1 
ATOM   625  C CZ  . ARG   B 2 20  ? -13.266 18.663  -6.861  1.00 97.49  ? 29  ARG   B CZ  1 
ATOM   626  N NH1 . ARG   B 2 20  ? -12.893 19.325  -5.775  1.00 100.92 ? 29  ARG   B NH1 1 
ATOM   627  N NH2 . ARG   B 2 20  ? -12.353 18.004  -7.561  1.00 95.56  ? 29  ARG   B NH2 1 
ATOM   628  N N   . LEU   B 2 21  ? -15.088 21.636  -11.617 1.00 71.72  ? 30  LEU   B N   1 
ATOM   629  C CA  . LEU   B 2 21  ? -13.858 22.018  -12.361 1.00 70.03  ? 30  LEU   B CA  1 
ATOM   630  C C   . LEU   B 2 21  ? -14.250 23.011  -13.467 1.00 68.14  ? 30  LEU   B C   1 
ATOM   631  O O   . LEU   B 2 21  ? -15.377 23.524  -13.415 1.00 67.84  ? 30  LEU   B O   1 
ATOM   632  C CB  . LEU   B 2 21  ? -13.232 20.736  -12.911 1.00 70.29  ? 30  LEU   B CB  1 
ATOM   633  C CG  . LEU   B 2 21  ? -12.144 20.079  -12.063 1.00 72.09  ? 30  LEU   B CG  1 
ATOM   634  C CD1 . LEU   B 2 21  ? -12.456 20.133  -10.575 1.00 72.62  ? 30  LEU   B CD1 1 
ATOM   635  C CD2 . LEU   B 2 21  ? -11.917 18.638  -12.509 1.00 71.57  ? 30  LEU   B CD2 1 
ATOM   636  N N   . LEU   B 2 22  ? -13.343 23.301  -14.407 1.00 67.60  ? 31  LEU   B N   1 
ATOM   637  C CA  . LEU   B 2 22  ? -13.593 24.211  -15.557 1.00 65.95  ? 31  LEU   B CA  1 
ATOM   638  C C   . LEU   B 2 22  ? -14.692 23.614  -16.438 1.00 64.30  ? 31  LEU   B C   1 
ATOM   639  O O   . LEU   B 2 22  ? -14.626 22.394  -16.701 1.00 64.03  ? 31  LEU   B O   1 
ATOM   640  C CB  . LEU   B 2 22  ? -12.298 24.376  -16.350 1.00 66.26  ? 31  LEU   B CB  1 
ATOM   641  C CG  . LEU   B 2 22  ? -12.317 25.488  -17.393 1.00 66.51  ? 31  LEU   B CG  1 
ATOM   642  C CD1 . LEU   B 2 22  ? -12.128 26.850  -16.743 1.00 67.17  ? 31  LEU   B CD1 1 
ATOM   643  C CD2 . LEU   B 2 22  ? -11.253 25.241  -18.447 1.00 66.83  ? 31  LEU   B CD2 1 
ATOM   644  N N   . GLY   B 2 23  ? -15.656 24.432  -16.874 1.00 62.58  ? 32  GLY   B N   1 
ATOM   645  C CA  . GLY   B 2 23  ? -16.808 23.975  -17.678 1.00 60.38  ? 32  GLY   B CA  1 
ATOM   646  C C   . GLY   B 2 23  ? -17.540 22.821  -17.003 1.00 57.57  ? 32  GLY   B C   1 
ATOM   647  O O   . GLY   B 2 23  ? -17.613 22.809  -15.759 1.00 56.66  ? 32  GLY   B O   1 
ATOM   648  N N   . SER   B 2 24  ? -18.125 21.933  -17.807 1.00 54.63  ? 33  SER   B N   1 
ATOM   649  C CA  . SER   B 2 24  ? -18.738 20.646  -17.410 1.00 51.80  ? 33  SER   B CA  1 
ATOM   650  C C   . SER   B 2 24  ? -17.737 19.565  -17.771 1.00 50.30  ? 33  SER   B C   1 
ATOM   651  O O   . SER   B 2 24  ? -17.355 19.558  -18.909 1.00 49.31  ? 33  SER   B O   1 
ATOM   652  C CB  . SER   B 2 24  ? -20.039 20.419  -18.116 1.00 51.27  ? 33  SER   B CB  1 
ATOM   653  O OG  . SER   B 2 24  ? -20.869 21.545  -17.958 1.00 54.37  ? 33  SER   B OG  1 
ATOM   654  N N   . THR   B 2 25  ? -17.301 18.734  -16.828 1.00 47.50  ? 34  THR   B N   1 
ATOM   655  C CA  . THR   B 2 25  ? -16.254 17.708  -17.050 1.00 46.84  ? 34  THR   B CA  1 
ATOM   656  C C   . THR   B 2 25  ? -16.865 16.321  -16.840 1.00 45.56  ? 34  THR   B C   1 
ATOM   657  O O   . THR   B 2 25  ? -17.602 16.127  -15.821 1.00 42.72  ? 34  THR   B O   1 
ATOM   658  C CB  . THR   B 2 25  ? -15.009 17.979  -16.197 1.00 47.74  ? 34  THR   B CB  1 
ATOM   659  O OG1 . THR   B 2 25  ? -14.605 19.341  -16.363 1.00 49.46  ? 34  THR   B OG1 1 
ATOM   660  C CG2 . THR   B 2 25  ? -13.850 17.077  -16.557 1.00 47.56  ? 34  THR   B CG2 1 
ATOM   661  N N   . GLN   B 2 26  ? -16.634 15.403  -17.781 1.00 43.62  ? 35  GLN   B N   1 
ATOM   662  C CA  . GLN   B 2 26  ? -17.131 14.009  -17.634 1.00 42.55  ? 35  GLN   B CA  1 
ATOM   663  C C   . GLN   B 2 26  ? -16.098 13.238  -16.799 1.00 42.37  ? 35  GLN   B C   1 
ATOM   664  O O   . GLN   B 2 26  ? -14.935 13.157  -17.253 1.00 43.61  ? 35  GLN   B O   1 
ATOM   665  C CB  . GLN   B 2 26  ? -17.297 13.314  -18.989 1.00 41.01  ? 35  GLN   B CB  1 
ATOM   666  C CG  . GLN   B 2 26  ? -17.940 11.930  -18.913 1.00 39.31  ? 35  GLN   B CG  1 
ATOM   667  C CD  . GLN   B 2 26  ? -18.156 11.297  -20.271 1.00 38.49  ? 35  GLN   B CD  1 
ATOM   668  O OE1 . GLN   B 2 26  ? -18.791 11.907  -21.140 1.00 39.96  ? 35  GLN   B OE1 1 
ATOM   669  N NE2 . GLN   B 2 26  ? -17.678 10.082  -20.463 1.00 36.32  ? 35  GLN   B NE2 1 
ATOM   670  N N   . VAL   B 2 27  ? -16.491 12.745  -15.625 1.00 43.15  ? 36  VAL   B N   1 
ATOM   671  C CA  . VAL   B 2 27  ? -15.605 11.992  -14.681 1.00 41.74  ? 36  VAL   B CA  1 
ATOM   672  C C   . VAL   B 2 27  ? -15.786 10.485  -14.902 1.00 39.61  ? 36  VAL   B C   1 
ATOM   673  O O   . VAL   B 2 27  ? -14.873 9.721   -14.557 1.00 39.94  ? 36  VAL   B O   1 
ATOM   674  C CB  . VAL   B 2 27  ? -15.890 12.426  -13.236 1.00 43.40  ? 36  VAL   B CB  1 
ATOM   675  C CG1 . VAL   B 2 27  ? -15.317 13.808  -12.990 1.00 45.76  ? 36  VAL   B CG1 1 
ATOM   676  C CG2 . VAL   B 2 27  ? -17.359 12.388  -12.883 1.00 42.97  ? 36  VAL   B CG2 1 
ATOM   677  N N   . GLY   B 2 28  ? -16.896 10.065  -15.513 1.00 38.00  ? 37  GLY   B N   1 
ATOM   678  C CA  . GLY   B 2 28  ? -17.099 8.676   -15.964 1.00 35.27  ? 37  GLY   B CA  1 
ATOM   679  C C   . GLY   B 2 28  ? -18.484 8.433   -16.530 1.00 35.04  ? 37  GLY   B C   1 
ATOM   680  O O   . GLY   B 2 28  ? -19.133 9.384   -17.060 1.00 35.42  ? 37  GLY   B O   1 
ATOM   681  N N   . VAL   B 2 29  ? -18.925 7.180   -16.446 1.00 34.05  ? 38  VAL   B N   1 
ATOM   682  C CA  . VAL   B 2 29  ? -20.057 6.576   -17.203 1.00 34.70  ? 38  VAL   B CA  1 
ATOM   683  C C   . VAL   B 2 29  ? -20.734 5.574   -16.271 1.00 34.59  ? 38  VAL   B C   1 
ATOM   684  O O   . VAL   B 2 29  ? -20.042 5.061   -15.334 1.00 36.13  ? 38  VAL   B O   1 
ATOM   685  C CB  . VAL   B 2 29  ? -19.507 5.883   -18.479 1.00 35.33  ? 38  VAL   B CB  1 
ATOM   686  C CG1 . VAL   B 2 29  ? -20.590 5.142   -19.257 1.00 35.10  ? 38  VAL   B CG1 1 
ATOM   687  C CG2 . VAL   B 2 29  ? -18.770 6.864   -19.357 1.00 36.28  ? 38  VAL   B CG2 1 
ATOM   688  N N   . GLY   B 2 30  ? -21.985 5.225   -16.547 1.00 34.46  ? 39  GLY   B N   1 
ATOM   689  C CA  . GLY   B 2 30  ? -22.654 4.126   -15.861 1.00 33.10  ? 39  GLY   B CA  1 
ATOM   690  C C   . GLY   B 2 30  ? -23.894 3.628   -16.521 1.00 33.29  ? 39  GLY   B C   1 
ATOM   691  O O   . GLY   B 2 30  ? -24.223 4.066   -17.675 1.00 32.69  ? 39  GLY   B O   1 
ATOM   692  N N   . VAL   B 2 31  ? -24.444 2.591   -15.924 1.00 32.00  ? 40  VAL   B N   1 
ATOM   693  C CA  . VAL   B 2 31  ? -25.517 1.726   -16.468 1.00 32.94  ? 40  VAL   B CA  1 
ATOM   694  C C   . VAL   B 2 31  ? -26.765 1.828   -15.646 1.00 33.62  ? 40  VAL   B C   1 
ATOM   695  O O   . VAL   B 2 31  ? -26.694 1.563   -14.385 1.00 32.32  ? 40  VAL   B O   1 
ATOM   696  C CB  . VAL   B 2 31  ? -25.115 0.258   -16.635 1.00 33.47  ? 40  VAL   B CB  1 
ATOM   697  C CG1 . VAL   B 2 31  ? -26.273 -0.581  -17.147 1.00 34.39  ? 40  VAL   B CG1 1 
ATOM   698  C CG2 . VAL   B 2 31  ? -23.931 0.096   -17.560 1.00 33.40  ? 40  VAL   B CG2 1 
ATOM   699  N N   . MET   B 2 32  ? -27.860 2.252   -16.239 1.00 33.42  ? 41  MET   B N   1 
ATOM   700  C CA  . MET   B 2 32  ? -29.206 2.236   -15.646 1.00 34.98  ? 41  MET   B CA  1 
ATOM   701  C C   . MET   B 2 32  ? -29.920 0.949   -16.084 1.00 35.88  ? 41  MET   B C   1 
ATOM   702  O O   . MET   B 2 32  ? -30.114 0.703   -17.303 1.00 34.92  ? 41  MET   B O   1 
ATOM   703  C CB  . MET   B 2 32  ? -29.981 3.503   -15.990 1.00 36.06  ? 41  MET   B CB  1 
ATOM   704  C CG  . MET   B 2 32  ? -31.276 3.707   -15.221 1.00 37.02  ? 41  MET   B CG  1 
ATOM   705  S SD  . MET   B 2 32  ? -31.014 4.261   -13.485 1.00 38.51  ? 41  MET   B SD  1 
ATOM   706  C CE  . MET   B 2 32  ? -30.112 5.785   -13.749 1.00 38.95  ? 41  MET   B CE  1 
ATOM   707  N N   . GLN   B 2 33  ? -30.287 0.100   -15.127 1.00 35.47  ? 42  GLN   B N   1 
ATOM   708  C CA  . GLN   B 2 33  ? -31.008 -1.173  -15.322 1.00 37.95  ? 42  GLN   B CA  1 
ATOM   709  C C   . GLN   B 2 33  ? -31.995 -1.413  -14.196 1.00 39.88  ? 42  GLN   B C   1 
ATOM   710  O O   . GLN   B 2 33  ? -31.597 -1.367  -12.949 1.00 38.40  ? 42  GLN   B O   1 
ATOM   711  C CB  . GLN   B 2 33  ? -30.048 -2.362  -15.536 1.00 39.25  ? 42  GLN   B CB  1 
ATOM   712  C CG  . GLN   B 2 33  ? -30.802 -3.613  -15.975 1.00 41.44  ? 42  GLN   B CG  1 
ATOM   713  C CD  . GLN   B 2 33  ? -29.975 -4.690  -16.649 1.00 43.08  ? 42  GLN   B CD  1 
ATOM   714  O OE1 . GLN   B 2 33  ? -30.140 -5.873  -16.368 1.00 47.81  ? 42  GLN   B OE1 1 
ATOM   715  N NE2 . GLN   B 2 33  ? -28.998 -4.299  -17.443 1.00 40.32  ? 42  GLN   B NE2 1 
ATOM   716  N N   . GLU   B 2 34  ? -33.237 -1.732  -14.522 1.00 41.20  ? 43  GLU   B N   1 
ATOM   717  C CA  . GLU   B 2 34  ? -34.252 -2.054  -13.483 1.00 43.08  ? 43  GLU   B CA  1 
ATOM   718  C C   . GLU   B 2 34  ? -34.252 -0.966  -12.381 1.00 42.38  ? 43  GLU   B C   1 
ATOM   719  O O   . GLU   B 2 34  ? -34.398 -1.340  -11.184 1.00 43.44  ? 43  GLU   B O   1 
ATOM   720  C CB  . GLU   B 2 34  ? -33.948 -3.435  -12.874 1.00 44.54  ? 43  GLU   B CB  1 
ATOM   721  C CG  . GLU   B 2 34  ? -34.154 -4.597  -13.846 1.00 48.47  ? 43  GLU   B CG  1 
ATOM   722  C CD  . GLU   B 2 34  ? -33.437 -5.903  -13.554 1.00 49.24  ? 43  GLU   B CD  1 
ATOM   723  O OE1 . GLU   B 2 34  ? -33.787 -6.558  -12.565 1.00 52.60  ? 43  GLU   B OE1 1 
ATOM   724  O OE2 . GLU   B 2 34  ? -32.525 -6.267  -14.334 1.00 52.84  ? 43  GLU   B OE2 1 
ATOM   725  N N   . GLY   B 2 35  ? -34.112 0.322   -12.727 1.00 41.30  ? 44  GLY   B N   1 
ATOM   726  C CA  . GLY   B 2 35  ? -34.287 1.463   -11.795 1.00 40.31  ? 44  GLY   B CA  1 
ATOM   727  C C   . GLY   B 2 35  ? -33.043 1.716   -10.966 1.00 39.12  ? 44  GLY   B C   1 
ATOM   728  O O   . GLY   B 2 35  ? -33.075 2.636   -10.102 1.00 38.44  ? 44  GLY   B O   1 
ATOM   729  N N   . VAL   B 2 36  ? -31.974 0.959   -11.220 1.00 36.88  ? 45  VAL   B N   1 
ATOM   730  C CA  . VAL   B 2 36  ? -30.692 1.043   -10.468 1.00 35.22  ? 45  VAL   B CA  1 
ATOM   731  C C   . VAL   B 2 36  ? -29.597 1.616   -11.351 1.00 34.39  ? 45  VAL   B C   1 
ATOM   732  O O   . VAL   B 2 36  ? -29.401 1.109   -12.467 1.00 33.61  ? 45  VAL   B O   1 
ATOM   733  C CB  . VAL   B 2 36  ? -30.336 -0.325  -9.873  1.00 35.26  ? 45  VAL   B CB  1 
ATOM   734  C CG1 . VAL   B 2 36  ? -28.955 -0.356  -9.241  1.00 34.59  ? 45  VAL   B CG1 1 
ATOM   735  C CG2 . VAL   B 2 36  ? -31.373 -0.692  -8.826  1.00 35.45  ? 45  VAL   B CG2 1 
ATOM   736  N N   . PHE   B 2 37  ? -28.891 2.616   -10.866 1.00 32.78  ? 46  PHE   B N   1 
ATOM   737  C CA  . PHE   B 2 37  ? -27.708 3.195   -11.501 1.00 32.58  ? 46  PHE   B CA  1 
ATOM   738  C C   . PHE   B 2 37  ? -26.457 2.478   -11.022 1.00 31.98  ? 46  PHE   B C   1 
ATOM   739  O O   . PHE   B 2 37  ? -26.227 2.395   -9.791  1.00 30.28  ? 46  PHE   B O   1 
ATOM   740  C CB  . PHE   B 2 37  ? -27.589 4.695   -11.383 1.00 33.18  ? 46  PHE   B CB  1 
ATOM   741  C CG  . PHE   B 2 37  ? -26.582 5.253   -12.346 1.00 34.51  ? 46  PHE   B CG  1 
ATOM   742  C CD1 . PHE   B 2 37  ? -26.756 5.126   -13.710 1.00 35.11  ? 46  PHE   B CD1 1 
ATOM   743  C CD2 . PHE   B 2 37  ? -25.487 5.940   -11.867 1.00 35.31  ? 46  PHE   B CD2 1 
ATOM   744  C CE1 . PHE   B 2 37  ? -25.817 5.647   -14.581 1.00 35.52  ? 46  PHE   B CE1 1 
ATOM   745  C CE2 . PHE   B 2 37  ? -24.534 6.437   -12.735 1.00 35.46  ? 46  PHE   B CE2 1 
ATOM   746  C CZ  . PHE   B 2 37  ? -24.728 6.335   -14.101 1.00 35.23  ? 46  PHE   B CZ  1 
ATOM   747  N N   . HIS   B 2 38  ? -25.689 1.940   -11.934 1.00 30.78  ? 47  HIS   B N   1 
ATOM   748  C CA  . HIS   B 2 38  ? -24.441 1.167   -11.715 1.00 30.80  ? 47  HIS   B CA  1 
ATOM   749  C C   . HIS   B 2 38  ? -23.233 1.909   -12.251 1.00 31.66  ? 47  HIS   B C   1 
ATOM   750  O O   . HIS   B 2 38  ? -23.231 2.177   -13.486 1.00 30.50  ? 47  HIS   B O   1 
ATOM   751  C CB  . HIS   B 2 38  ? -24.482 -0.217  -12.283 1.00 30.59  ? 47  HIS   B CB  1 
ATOM   752  C CG  . HIS   B 2 38  ? -25.703 -1.013  -12.035 1.00 31.39  ? 47  HIS   B CG  1 
ATOM   753  N ND1 . HIS   B 2 38  ? -26.957 -0.601  -12.446 1.00 32.85  ? 47  HIS   B ND1 1 
ATOM   754  C CD2 . HIS   B 2 38  ? -25.807 -2.349  -11.475 1.00 31.58  ? 47  HIS   B CD2 1 
ATOM   755  C CE1 . HIS   B 2 38  ? -27.826 -1.537  -12.088 1.00 32.45  ? 47  HIS   B CE1 1 
ATOM   756  N NE2 . HIS   B 2 38  ? -27.134 -2.638  -11.513 1.00 32.69  ? 47  HIS   B NE2 1 
ATOM   757  N N   . THR   B 2 39  ? -22.217 2.191   -11.445 1.00 31.84  ? 48  THR   B N   1 
ATOM   758  C CA  . THR   B 2 39  ? -20.951 2.793   -11.887 1.00 32.44  ? 48  THR   B CA  1 
ATOM   759  C C   . THR   B 2 39  ? -19.770 2.212   -11.131 1.00 33.03  ? 48  THR   B C   1 
ATOM   760  O O   . THR   B 2 39  ? -20.009 1.249   -10.332 1.00 30.57  ? 48  THR   B O   1 
ATOM   761  C CB  . THR   B 2 39  ? -21.063 4.312   -11.941 1.00 33.62  ? 48  THR   B CB  1 
ATOM   762  O OG1 . THR   B 2 39  ? -19.978 4.871   -12.667 1.00 33.37  ? 48  THR   B OG1 1 
ATOM   763  C CG2 . THR   B 2 39  ? -21.062 4.959   -10.584 1.00 33.49  ? 48  THR   B CG2 1 
ATOM   764  N N   . MET   B 2 40  ? -18.566 2.735   -11.388 1.00 32.60  ? 49  MET   B N   1 
ATOM   765  C CA  . MET   B 2 40  ? -17.351 2.349   -10.615 1.00 33.87  ? 49  MET   B CA  1 
ATOM   766  C C   . MET   B 2 40  ? -17.194 3.332   -9.436  1.00 33.42  ? 49  MET   B C   1 
ATOM   767  O O   . MET   B 2 40  ? -17.520 4.516   -9.530  1.00 33.39  ? 49  MET   B O   1 
ATOM   768  C CB  . MET   B 2 40  ? -16.077 2.235   -11.460 1.00 34.08  ? 49  MET   B CB  1 
ATOM   769  C CG  . MET   B 2 40  ? -16.336 1.531   -12.826 1.00 35.76  ? 49  MET   B CG  1 
ATOM   770  S SD  . MET   B 2 40  ? -14.884 0.644   -13.384 1.00 38.51  ? 49  MET   B SD  1 
ATOM   771  C CE  . MET   B 2 40  ? -14.902 -0.885  -12.444 1.00 39.62  ? 49  MET   B CE  1 
ATOM   772  N N   A TRP   B 2 41  ? -16.687 2.826   -8.304  0.25 33.37  ? 50  TRP   B N   1 
ATOM   773  N N   B TRP   B 2 41  ? -16.724 2.826   -8.282  0.25 33.40  ? 50  TRP   B N   1 
ATOM   774  N N   C TRP   B 2 41  ? -16.687 2.826   -8.304  0.25 33.37  ? 50  TRP   B N   1 
ATOM   775  N N   D TRP   B 2 41  ? -16.724 2.826   -8.282  0.25 33.40  ? 50  TRP   B N   1 
ATOM   776  C CA  A TRP   B 2 41  ? -16.555 3.618   -7.059  0.25 33.99  ? 50  TRP   B CA  1 
ATOM   777  C CA  B TRP   B 2 41  ? -16.564 3.646   -7.052  0.25 34.07  ? 50  TRP   B CA  1 
ATOM   778  C CA  C TRP   B 2 41  ? -16.555 3.618   -7.059  0.25 33.99  ? 50  TRP   B CA  1 
ATOM   779  C CA  D TRP   B 2 41  ? -16.564 3.646   -7.052  0.25 34.07  ? 50  TRP   B CA  1 
ATOM   780  C C   A TRP   B 2 41  ? -15.605 4.817   -7.244  0.25 34.35  ? 50  TRP   B C   1 
ATOM   781  C C   B TRP   B 2 41  ? -15.650 4.855   -7.311  0.25 34.41  ? 50  TRP   B C   1 
ATOM   782  C C   C TRP   B 2 41  ? -15.605 4.817   -7.244  0.25 34.35  ? 50  TRP   B C   1 
ATOM   783  C C   D TRP   B 2 41  ? -15.650 4.855   -7.311  0.25 34.41  ? 50  TRP   B C   1 
ATOM   784  O O   A TRP   B 2 41  ? -15.859 5.940   -6.558  0.25 34.93  ? 50  TRP   B O   1 
ATOM   785  O O   B TRP   B 2 41  ? -15.995 6.040   -6.733  0.25 35.04  ? 50  TRP   B O   1 
ATOM   786  O O   C TRP   B 2 41  ? -15.859 5.940   -6.558  0.25 34.93  ? 50  TRP   B O   1 
ATOM   787  O O   D TRP   B 2 41  ? -15.995 6.040   -6.733  0.25 35.04  ? 50  TRP   B O   1 
ATOM   788  C CB  A TRP   B 2 41  ? -16.067 2.727   -5.912  0.25 33.85  ? 50  TRP   B CB  1 
ATOM   789  C CB  B TRP   B 2 41  ? -16.002 2.813   -5.894  0.25 34.01  ? 50  TRP   B CB  1 
ATOM   790  C CB  C TRP   B 2 41  ? -16.067 2.727   -5.912  0.25 33.85  ? 50  TRP   B CB  1 
ATOM   791  C CB  D TRP   B 2 41  ? -16.002 2.813   -5.894  0.25 34.01  ? 50  TRP   B CB  1 
ATOM   792  C CG  A TRP   B 2 41  ? -16.183 3.455   -4.612  0.25 34.08  ? 50  TRP   B CG  1 
ATOM   793  C CG  B TRP   B 2 41  ? -15.842 3.623   -4.642  0.25 34.29  ? 50  TRP   B CG  1 
ATOM   794  C CG  C TRP   B 2 41  ? -16.183 3.455   -4.612  0.25 34.08  ? 50  TRP   B CG  1 
ATOM   795  C CG  D TRP   B 2 41  ? -15.842 3.623   -4.642  0.25 34.29  ? 50  TRP   B CG  1 
ATOM   796  C CD1 A TRP   B 2 41  ? -17.260 3.460   -3.780  0.25 34.43  ? 50  TRP   B CD1 1 
ATOM   797  C CD1 B TRP   B 2 41  ? -14.809 4.453   -4.309  0.25 34.59  ? 50  TRP   B CD1 1 
ATOM   798  C CD1 C TRP   B 2 41  ? -17.260 3.460   -3.780  0.25 34.43  ? 50  TRP   B CD1 1 
ATOM   799  C CD1 D TRP   B 2 41  ? -14.809 4.453   -4.309  0.25 34.59  ? 50  TRP   B CD1 1 
ATOM   800  C CD2 A TRP   B 2 41  ? -15.238 4.387   -4.055  0.25 34.45  ? 50  TRP   B CD2 1 
ATOM   801  C CD2 B TRP   B 2 41  ? -16.792 3.735   -3.570  0.25 34.77  ? 50  TRP   B CD2 1 
ATOM   802  C CD2 C TRP   B 2 41  ? -15.238 4.387   -4.055  0.25 34.45  ? 50  TRP   B CD2 1 
ATOM   803  C CD2 D TRP   B 2 41  ? -16.792 3.735   -3.570  0.25 34.77  ? 50  TRP   B CD2 1 
ATOM   804  N NE1 A TRP   B 2 41  ? -17.028 4.288   -2.711  0.25 34.68  ? 50  TRP   B NE1 1 
ATOM   805  N NE1 B TRP   B 2 41  ? -15.037 5.042   -3.093  0.25 34.92  ? 50  TRP   B NE1 1 
ATOM   806  N NE1 C TRP   B 2 41  ? -17.028 4.288   -2.711  0.25 34.68  ? 50  TRP   B NE1 1 
ATOM   807  N NE1 D TRP   B 2 41  ? -15.037 5.042   -3.093  0.25 34.92  ? 50  TRP   B NE1 1 
ATOM   808  C CE2 A TRP   B 2 41  ? -15.800 4.877   -2.860  0.25 34.70  ? 50  TRP   B CE2 1 
ATOM   809  C CE2 B TRP   B 2 41  ? -16.253 4.630   -2.618  0.25 34.90  ? 50  TRP   B CE2 1 
ATOM   810  C CE2 C TRP   B 2 41  ? -15.800 4.877   -2.860  0.25 34.70  ? 50  TRP   B CE2 1 
ATOM   811  C CE2 D TRP   B 2 41  ? -16.253 4.630   -2.618  0.25 34.90  ? 50  TRP   B CE2 1 
ATOM   812  C CE3 A TRP   B 2 41  ? -13.965 4.831   -4.428  0.25 34.57  ? 50  TRP   B CE3 1 
ATOM   813  C CE3 B TRP   B 2 41  ? -18.038 3.154   -3.316  0.25 34.95  ? 50  TRP   B CE3 1 
ATOM   814  C CE3 C TRP   B 2 41  ? -13.965 4.831   -4.428  0.25 34.57  ? 50  TRP   B CE3 1 
ATOM   815  C CE3 D TRP   B 2 41  ? -18.038 3.154   -3.316  0.25 34.95  ? 50  TRP   B CE3 1 
ATOM   816  C CZ2 A TRP   B 2 41  ? -15.132 5.796   -2.055  0.25 35.56  ? 50  TRP   B CZ2 1 
ATOM   817  C CZ2 B TRP   B 2 41  ? -16.912 4.939   -1.423  0.25 35.59  ? 50  TRP   B CZ2 1 
ATOM   818  C CZ2 C TRP   B 2 41  ? -15.132 5.796   -2.055  0.25 35.56  ? 50  TRP   B CZ2 1 
ATOM   819  C CZ2 D TRP   B 2 41  ? -16.912 4.939   -1.423  0.25 35.59  ? 50  TRP   B CZ2 1 
ATOM   820  C CZ3 A TRP   B 2 41  ? -13.307 5.738   -3.631  0.25 35.01  ? 50  TRP   B CZ3 1 
ATOM   821  C CZ3 B TRP   B 2 41  ? -18.685 3.462   -2.138  0.25 35.28  ? 50  TRP   B CZ3 1 
ATOM   822  C CZ3 C TRP   B 2 41  ? -13.307 5.738   -3.631  0.25 35.01  ? 50  TRP   B CZ3 1 
ATOM   823  C CZ3 D TRP   B 2 41  ? -18.685 3.462   -2.138  0.25 35.28  ? 50  TRP   B CZ3 1 
ATOM   824  C CH2 A TRP   B 2 41  ? -13.880 6.204   -2.451  0.25 35.48  ? 50  TRP   B CH2 1 
ATOM   825  C CH2 B TRP   B 2 41  ? -18.139 4.355   -1.215  0.25 35.46  ? 50  TRP   B CH2 1 
ATOM   826  C CH2 C TRP   B 2 41  ? -13.880 6.204   -2.451  0.25 35.48  ? 50  TRP   B CH2 1 
ATOM   827  C CH2 D TRP   B 2 41  ? -18.139 4.355   -1.215  0.25 35.46  ? 50  TRP   B CH2 1 
ATOM   828  N N   . HIS   B 2 42  ? -14.530 4.615   -8.083  1.00 34.04  ? 51  HIS   B N   1 
ATOM   829  C CA  . HIS   B 2 42  ? -13.512 5.697   -8.250  1.00 35.15  ? 51  HIS   B CA  1 
ATOM   830  C C   . HIS   B 2 42  ? -14.098 6.879   -9.075  1.00 36.63  ? 51  HIS   B C   1 
ATOM   831  O O   . HIS   B 2 42  ? -13.500 7.955   -9.073  1.00 38.52  ? 51  HIS   B O   1 
ATOM   832  C CB  . HIS   B 2 42  ? -12.186 5.182   -8.777  1.00 37.09  ? 51  HIS   B CB  1 
ATOM   833  C CG  . HIS   B 2 42  ? -12.217 4.916   -10.238 1.00 37.10  ? 51  HIS   B CG  1 
ATOM   834  N ND1 . HIS   B 2 42  ? -12.357 3.644   -10.747 1.00 37.88  ? 51  HIS   B ND1 1 
ATOM   835  C CD2 . HIS   B 2 42  ? -12.037 5.739   -11.312 1.00 38.86  ? 51  HIS   B CD2 1 
ATOM   836  C CE1 . HIS   B 2 42  ? -12.333 3.706   -12.073 1.00 37.60  ? 51  HIS   B CE1 1 
ATOM   837  N NE2 . HIS   B 2 42  ? -12.137 4.973   -12.427 1.00 37.40  ? 51  HIS   B NE2 1 
ATOM   838  N N   . VAL   B 2 43  ? -15.233 6.708   -9.740  1.00 36.69  ? 52  VAL   B N   1 
ATOM   839  C CA  . VAL   B 2 43  ? -15.925 7.768   -10.536 1.00 36.38  ? 52  VAL   B CA  1 
ATOM   840  C C   . VAL   B 2 43  ? -16.623 8.741   -9.577  1.00 38.03  ? 52  VAL   B C   1 
ATOM   841  O O   . VAL   B 2 43  ? -16.404 9.959   -9.739  1.00 38.86  ? 52  VAL   B O   1 
ATOM   842  C CB  . VAL   B 2 43  ? -16.904 7.106   -11.516 1.00 36.49  ? 52  VAL   B CB  1 
ATOM   843  C CG1 . VAL   B 2 43  ? -17.893 8.092   -12.135 1.00 36.59  ? 52  VAL   B CG1 1 
ATOM   844  C CG2 . VAL   B 2 43  ? -16.147 6.411   -12.649 1.00 36.24  ? 52  VAL   B CG2 1 
ATOM   845  N N   . THR   B 2 44  ? -17.422 8.232   -8.603  1.00 35.26  ? 53  THR   B N   1 
ATOM   846  C CA  . THR   B 2 44  ? -18.313 9.080   -7.767  1.00 36.88  ? 53  THR   B CA  1 
ATOM   847  C C   . THR   B 2 44  ? -17.739 9.201   -6.352  1.00 37.56  ? 53  THR   B C   1 
ATOM   848  O O   . THR   B 2 44  ? -18.129 10.143  -5.662  1.00 39.14  ? 53  THR   B O   1 
ATOM   849  C CB  . THR   B 2 44  ? -19.759 8.559   -7.705  1.00 35.98  ? 53  THR   B CB  1 
ATOM   850  O OG1 . THR   B 2 44  ? -19.717 7.302   -7.015  1.00 33.84  ? 53  THR   B OG1 1 
ATOM   851  C CG2 . THR   B 2 44  ? -20.320 8.432   -9.123  1.00 35.46  ? 53  THR   B CG2 1 
ATOM   852  N N   . LYS   B 2 45  ? -16.833 8.302   -5.980  1.00 38.52  ? 54  LYS   B N   1 
ATOM   853  C CA  . LYS   B 2 45  ? -16.308 8.135   -4.590  1.00 41.35  ? 54  LYS   B CA  1 
ATOM   854  C C   . LYS   B 2 45  ? -17.497 7.954   -3.629  1.00 41.73  ? 54  LYS   B C   1 
ATOM   855  O O   . LYS   B 2 45  ? -17.357 8.329   -2.441  1.00 43.83  ? 54  LYS   B O   1 
ATOM   856  C CB  . LYS   B 2 45  ? -15.450 9.332   -4.154  1.00 44.97  ? 54  LYS   B CB  1 
ATOM   857  C CG  . LYS   B 2 45  ? -14.339 9.793   -5.078  1.00 50.37  ? 54  LYS   B CG  1 
ATOM   858  C CD  . LYS   B 2 45  ? -13.267 8.768   -5.365  1.00 54.10  ? 54  LYS   B CD  1 
ATOM   859  C CE  . LYS   B 2 45  ? -12.055 9.383   -6.045  1.00 57.24  ? 54  LYS   B CE  1 
ATOM   860  N NZ  . LYS   B 2 45  ? -11.667 8.657   -7.282  1.00 58.46  ? 54  LYS   B NZ  1 
ATOM   861  N N   . GLY   B 2 46  ? -18.624 7.413   -4.091  1.00 41.37  ? 55  GLY   B N   1 
ATOM   862  C CA  . GLY   B 2 46  ? -19.834 7.127   -3.299  1.00 41.09  ? 55  GLY   B CA  1 
ATOM   863  C C   . GLY   B 2 46  ? -20.744 8.338   -3.078  1.00 42.62  ? 55  GLY   B C   1 
ATOM   864  O O   . GLY   B 2 46  ? -21.672 8.203   -2.267  1.00 42.45  ? 55  GLY   B O   1 
ATOM   865  N N   . ALA   B 2 47  ? -20.488 9.506   -3.693  1.00 42.10  ? 56  ALA   B N   1 
ATOM   866  C CA  . ALA   B 2 47  ? -21.348 10.724  -3.597  1.00 43.09  ? 56  ALA   B CA  1 
ATOM   867  C C   . ALA   B 2 47  ? -22.730 10.501  -4.229  1.00 41.95  ? 56  ALA   B C   1 
ATOM   868  O O   . ALA   B 2 47  ? -22.816 9.721   -5.173  1.00 42.01  ? 56  ALA   B O   1 
ATOM   869  C CB  . ALA   B 2 47  ? -20.678 11.904  -4.276  1.00 43.39  ? 56  ALA   B CB  1 
ATOM   870  N N   . ALA   B 2 48  ? -23.762 11.242  -3.806  1.00 41.55  ? 57  ALA   B N   1 
ATOM   871  C CA  . ALA   B 2 48  ? -25.090 11.312  -4.471  1.00 41.63  ? 57  ALA   B CA  1 
ATOM   872  C C   . ALA   B 2 48  ? -24.960 11.971  -5.859  1.00 41.63  ? 57  ALA   B C   1 
ATOM   873  O O   . ALA   B 2 48  ? -24.003 12.703  -6.077  1.00 42.94  ? 57  ALA   B O   1 
ATOM   874  C CB  . ALA   B 2 48  ? -26.091 12.059  -3.633  1.00 43.45  ? 57  ALA   B CB  1 
ATOM   875  N N   . LEU   B 2 49  ? -25.933 11.717  -6.728  1.00 40.94  ? 58  LEU   B N   1 
ATOM   876  C CA  . LEU   B 2 49  ? -25.982 12.147  -8.160  1.00 42.82  ? 58  LEU   B CA  1 
ATOM   877  C C   . LEU   B 2 49  ? -27.323 12.828  -8.432  1.00 45.35  ? 58  LEU   B C   1 
ATOM   878  O O   . LEU   B 2 49  ? -28.358 12.434  -7.803  1.00 47.51  ? 58  LEU   B O   1 
ATOM   879  C CB  . LEU   B 2 49  ? -25.865 10.911  -9.036  1.00 40.10  ? 58  LEU   B CB  1 
ATOM   880  C CG  . LEU   B 2 49  ? -24.601 10.068  -8.879  1.00 38.75  ? 58  LEU   B CG  1 
ATOM   881  C CD1 . LEU   B 2 49  ? -24.670 8.837   -9.759  1.00 38.35  ? 58  LEU   B CD1 1 
ATOM   882  C CD2 . LEU   B 2 49  ? -23.318 10.836  -9.179  1.00 38.99  ? 58  LEU   B CD2 1 
ATOM   883  N N   . ARG   B 2 50  ? -27.310 13.814  -9.314  1.00 46.64  ? 59  ARG   B N   1 
ATOM   884  C CA  . ARG   B 2 50  ? -28.534 14.472  -9.800  1.00 49.65  ? 59  ARG   B CA  1 
ATOM   885  C C   . ARG   B 2 50  ? -28.960 13.793  -11.099 1.00 50.04  ? 59  ARG   B C   1 
ATOM   886  O O   . ARG   B 2 50  ? -28.076 13.446  -11.932 1.00 46.12  ? 59  ARG   B O   1 
ATOM   887  C CB  . ARG   B 2 50  ? -28.206 15.954  -9.905  1.00 54.00  ? 59  ARG   B CB  1 
ATOM   888  C CG  . ARG   B 2 50  ? -29.403 16.850  -10.164 1.00 57.90  ? 59  ARG   B CG  1 
ATOM   889  C CD  . ARG   B 2 50  ? -29.129 18.254  -9.652  1.00 61.28  ? 59  ARG   B CD  1 
ATOM   890  N NE  . ARG   B 2 50  ? -27.705 18.562  -9.749  1.00 62.50  ? 59  ARG   B NE  1 
ATOM   891  C CZ  . ARG   B 2 50  ? -27.072 18.930  -10.859 1.00 63.25  ? 59  ARG   B CZ  1 
ATOM   892  N NH1 . ARG   B 2 50  ? -27.736 19.037  -12.000 1.00 63.48  ? 59  ARG   B NH1 1 
ATOM   893  N NH2 . ARG   B 2 50  ? -25.770 19.178  -10.818 1.00 63.92  ? 59  ARG   B NH2 1 
ATOM   894  N N   . SER   B 2 51  ? -30.250 13.526  -11.245 1.00 51.65  ? 60  SER   B N   1 
ATOM   895  C CA  . SER   B 2 51  ? -30.871 13.282  -12.574 1.00 54.46  ? 60  SER   B CA  1 
ATOM   896  C C   . SER   B 2 51  ? -32.050 14.249  -12.733 1.00 57.39  ? 60  SER   B C   1 
ATOM   897  O O   . SER   B 2 51  ? -33.061 14.031  -12.043 1.00 60.32  ? 60  SER   B O   1 
ATOM   898  C CB  . SER   B 2 51  ? -31.302 11.855  -12.711 1.00 53.73  ? 60  SER   B CB  1 
ATOM   899  O OG  . SER   B 2 51  ? -31.851 11.612  -13.991 1.00 54.98  ? 60  SER   B OG  1 
ATOM   900  N N   . GLY   B 2 52  ? -31.907 15.284  -13.568 1.00 61.49  ? 61  GLY   B N   1 
ATOM   901  C CA  . GLY   B 2 52  ? -32.841 16.428  -13.616 1.00 64.99  ? 61  GLY   B CA  1 
ATOM   902  C C   . GLY   B 2 52  ? -32.864 17.153  -12.280 1.00 67.68  ? 61  GLY   B C   1 
ATOM   903  O O   . GLY   B 2 52  ? -31.801 17.645  -11.842 1.00 67.92  ? 61  GLY   B O   1 
ATOM   904  N N   . GLU   B 2 53  ? -34.020 17.187  -11.622 1.00 71.39  ? 62  GLU   B N   1 
ATOM   905  C CA  . GLU   B 2 53  ? -34.140 17.672  -10.222 1.00 74.38  ? 62  GLU   B CA  1 
ATOM   906  C C   . GLU   B 2 53  ? -34.275 16.485  -9.257  1.00 70.66  ? 62  GLU   B C   1 
ATOM   907  O O   . GLU   B 2 53  ? -34.346 16.742  -8.044  1.00 69.81  ? 62  GLU   B O   1 
ATOM   908  C CB  . GLU   B 2 53  ? -35.292 18.668  -10.122 1.00 79.37  ? 62  GLU   B CB  1 
ATOM   909  C CG  . GLU   B 2 53  ? -34.901 20.030  -10.659 1.00 84.95  ? 62  GLU   B CG  1 
ATOM   910  C CD  . GLU   B 2 53  ? -36.028 21.044  -10.728 1.00 90.96  ? 62  GLU   B CD  1 
ATOM   911  O OE1 . GLU   B 2 53  ? -37.214 20.622  -10.727 1.00 95.10  ? 62  GLU   B OE1 1 
ATOM   912  O OE2 . GLU   B 2 53  ? -35.718 22.251  -10.811 1.00 96.98  ? 62  GLU   B OE2 1 
ATOM   913  N N   . GLY   B 2 54  ? -34.266 15.251  -9.774  1.00 65.99  ? 63  GLY   B N   1 
ATOM   914  C CA  . GLY   B 2 54  ? -34.211 14.009  -8.981  1.00 63.72  ? 63  GLY   B CA  1 
ATOM   915  C C   . GLY   B 2 54  ? -32.831 13.799  -8.375  1.00 62.23  ? 63  GLY   B C   1 
ATOM   916  O O   . GLY   B 2 54  ? -31.846 14.279  -8.962  1.00 63.25  ? 63  GLY   B O   1 
ATOM   917  N N   . ARG   B 2 55  ? -32.765 13.144  -7.211  1.00 58.59  ? 64  ARG   B N   1 
ATOM   918  C CA  . ARG   B 2 55  ? -31.499 12.781  -6.514  1.00 55.43  ? 64  ARG   B CA  1 
ATOM   919  C C   . ARG   B 2 55  ? -31.343 11.257  -6.598  1.00 50.97  ? 64  ARG   B C   1 
ATOM   920  O O   . ARG   B 2 55  ? -32.349 10.536  -6.505  1.00 51.25  ? 64  ARG   B O   1 
ATOM   921  C CB  . ARG   B 2 55  ? -31.531 13.309  -5.074  1.00 57.16  ? 64  ARG   B CB  1 
ATOM   922  C CG  . ARG   B 2 55  ? -30.224 13.179  -4.301  1.00 59.21  ? 64  ARG   B CG  1 
ATOM   923  C CD  . ARG   B 2 55  ? -30.508 13.341  -2.807  1.00 61.80  ? 64  ARG   B CD  1 
ATOM   924  N NE  . ARG   B 2 55  ? -29.357 13.128  -1.927  1.00 64.24  ? 64  ARG   B NE  1 
ATOM   925  C CZ  . ARG   B 2 55  ? -28.618 14.075  -1.337  1.00 66.39  ? 64  ARG   B CZ  1 
ATOM   926  N NH1 . ARG   B 2 55  ? -28.884 15.361  -1.507  1.00 68.23  ? 64  ARG   B NH1 1 
ATOM   927  N NH2 . ARG   B 2 55  ? -27.594 13.724  -0.571  1.00 65.92  ? 64  ARG   B NH2 1 
ATOM   928  N N   . LEU   B 2 56  ? -30.132 10.771  -6.831  1.00 46.55  ? 65  LEU   B N   1 
ATOM   929  C CA  . LEU   B 2 56  ? -29.845 9.325   -6.766  1.00 44.04  ? 65  LEU   B CA  1 
ATOM   930  C C   . LEU   B 2 56  ? -28.960 9.145   -5.537  1.00 41.90  ? 65  LEU   B C   1 
ATOM   931  O O   . LEU   B 2 56  ? -27.847 9.736   -5.510  1.00 42.13  ? 65  LEU   B O   1 
ATOM   932  C CB  . LEU   B 2 56  ? -29.117 8.850   -8.045  1.00 42.22  ? 65  LEU   B CB  1 
ATOM   933  C CG  . LEU   B 2 56  ? -29.778 9.015   -9.413  1.00 43.97  ? 65  LEU   B CG  1 
ATOM   934  C CD1 . LEU   B 2 56  ? -29.168 7.988   -10.374 1.00 42.61  ? 65  LEU   B CD1 1 
ATOM   935  C CD2 . LEU   B 2 56  ? -31.283 8.867   -9.400  1.00 44.94  ? 65  LEU   B CD2 1 
ATOM   936  N N   . ASP   B 2 57  ? -29.428 8.418   -4.518  1.00 40.96  ? 66  ASP   B N   1 
ATOM   937  C CA  . ASP   B 2 57  ? -28.576 8.133   -3.350  1.00 38.96  ? 66  ASP   B CA  1 
ATOM   938  C C   . ASP   B 2 57  ? -27.869 6.792   -3.459  1.00 36.69  ? 66  ASP   B C   1 
ATOM   939  O O   . ASP   B 2 57  ? -28.423 5.802   -3.954  1.00 37.51  ? 66  ASP   B O   1 
ATOM   940  C CB  . ASP   B 2 57  ? -29.423 8.169   -2.065  1.00 41.32  ? 66  ASP   B CB  1 
ATOM   941  C CG  . ASP   B 2 57  ? -30.065 9.530   -1.879  1.00 44.36  ? 66  ASP   B CG  1 
ATOM   942  O OD1 . ASP   B 2 57  ? -29.354 10.521  -2.147  1.00 46.38  ? 66  ASP   B OD1 1 
ATOM   943  O OD2 . ASP   B 2 57  ? -31.239 9.602   -1.446  1.00 46.34  ? 66  ASP   B OD2 1 
ATOM   944  N N   . PRO   B 2 58  ? -26.609 6.687   -2.991  1.00 35.26  ? 67  PRO   B N   1 
ATOM   945  C CA  . PRO   B 2 58  ? -25.877 5.418   -2.993  1.00 34.39  ? 67  PRO   B CA  1 
ATOM   946  C C   . PRO   B 2 58  ? -26.693 4.375   -2.229  1.00 34.20  ? 67  PRO   B C   1 
ATOM   947  O O   . PRO   B 2 58  ? -27.334 4.781   -1.244  1.00 34.10  ? 67  PRO   B O   1 
ATOM   948  C CB  . PRO   B 2 58  ? -24.518 5.796   -2.368  1.00 34.33  ? 67  PRO   B CB  1 
ATOM   949  C CG  . PRO   B 2 58  ? -24.770 7.051   -1.597  1.00 36.55  ? 67  PRO   B CG  1 
ATOM   950  C CD  . PRO   B 2 58  ? -25.788 7.777   -2.446  1.00 36.90  ? 67  PRO   B CD  1 
ATOM   951  N N   . TYR   B 2 59  ? -26.630 3.116   -2.636  1.00 32.77  ? 68  TYR   B N   1 
ATOM   952  C CA  . TYR   B 2 59  ? -27.340 1.966   -2.033  1.00 32.89  ? 68  TYR   B CA  1 
ATOM   953  C C   . TYR   B 2 59  ? -26.340 0.931   -1.482  1.00 32.26  ? 68  TYR   B C   1 
ATOM   954  O O   . TYR   B 2 59  ? -26.562 0.385   -0.363  1.00 32.83  ? 68  TYR   B O   1 
ATOM   955  C CB  . TYR   B 2 59  ? -28.323 1.330   -3.020  1.00 33.79  ? 68  TYR   B CB  1 
ATOM   956  C CG  . TYR   B 2 59  ? -29.211 0.293   -2.376  1.00 33.79  ? 68  TYR   B CG  1 
ATOM   957  C CD1 . TYR   B 2 59  ? -28.736 -1.002  -2.253  1.00 34.25  ? 68  TYR   B CD1 1 
ATOM   958  C CD2 . TYR   B 2 59  ? -30.521 0.570   -1.994  1.00 34.59  ? 68  TYR   B CD2 1 
ATOM   959  C CE1 . TYR   B 2 59  ? -29.531 -2.008  -1.735  1.00 34.98  ? 68  TYR   B CE1 1 
ATOM   960  C CE2 . TYR   B 2 59  ? -31.361 -0.434  -1.513  1.00 35.34  ? 68  TYR   B CE2 1 
ATOM   961  C CZ  . TYR   B 2 59  ? -30.857 -1.731  -1.406  1.00 36.02  ? 68  TYR   B CZ  1 
ATOM   962  O OH  . TYR   B 2 59  ? -31.601 -2.789  -0.947  1.00 38.33  ? 68  TYR   B OH  1 
ATOM   963  N N   . TRP   B 2 60  ? -25.384 0.548   -2.288  1.00 30.76  ? 69  TRP   B N   1 
ATOM   964  C CA  . TRP   B 2 60  ? -24.349 -0.486  -2.088  1.00 29.97  ? 69  TRP   B CA  1 
ATOM   965  C C   . TRP   B 2 60  ? -23.043 0.008   -2.621  1.00 30.36  ? 69  TRP   B C   1 
ATOM   966  O O   . TRP   B 2 60  ? -23.054 0.524   -3.793  1.00 28.66  ? 69  TRP   B O   1 
ATOM   967  C CB  . TRP   B 2 60  ? -24.764 -1.884  -2.522  1.00 29.89  ? 69  TRP   B CB  1 
ATOM   968  C CG  . TRP   B 2 60  ? -23.621 -2.842  -2.508  1.00 29.58  ? 69  TRP   B CG  1 
ATOM   969  C CD1 . TRP   B 2 60  ? -23.126 -3.548  -1.435  1.00 30.35  ? 69  TRP   B CD1 1 
ATOM   970  C CD2 . TRP   B 2 60  ? -22.692 -3.061  -3.575  1.00 28.90  ? 69  TRP   B CD2 1 
ATOM   971  N NE1 . TRP   B 2 60  ? -21.999 -4.224  -1.818  1.00 29.53  ? 69  TRP   B NE1 1 
ATOM   972  C CE2 . TRP   B 2 60  ? -21.753 -3.995  -3.141  1.00 29.31  ? 69  TRP   B CE2 1 
ATOM   973  C CE3 . TRP   B 2 60  ? -22.641 -2.709  -4.952  1.00 28.75  ? 69  TRP   B CE3 1 
ATOM   974  C CZ2 . TRP   B 2 60  ? -20.713 -4.498  -3.887  1.00 28.78  ? 69  TRP   B CZ2 1 
ATOM   975  C CZ3 . TRP   B 2 60  ? -21.578 -3.154  -5.696  1.00 29.06  ? 69  TRP   B CZ3 1 
ATOM   976  C CH2 . TRP   B 2 60  ? -20.614 -4.009  -5.161  1.00 28.77  ? 69  TRP   B CH2 1 
ATOM   977  N N   . GLY   B 2 61  ? -21.924 -0.242  -1.974  1.00 30.70  ? 70  GLY   B N   1 
ATOM   978  C CA  . GLY   B 2 61  ? -20.626 -0.023  -2.643  1.00 30.76  ? 70  GLY   B CA  1 
ATOM   979  C C   . GLY   B 2 61  ? -19.527 -0.827  -2.043  1.00 31.49  ? 70  GLY   B C   1 
ATOM   980  O O   . GLY   B 2 61  ? -19.675 -1.164  -0.792  1.00 30.84  ? 70  GLY   B O   1 
ATOM   981  N N   . ASP   B 2 62  ? -18.401 -0.943  -2.710  1.00 31.45  ? 71  ASP   B N   1 
ATOM   982  C CA  . ASP   B 2 62  ? -17.223 -1.727  -2.241  1.00 32.83  ? 71  ASP   B CA  1 
ATOM   983  C C   . ASP   B 2 62  ? -16.003 -1.146  -2.898  1.00 33.04  ? 71  ASP   B C   1 
ATOM   984  O O   . ASP   B 2 62  ? -15.925 -1.313  -4.146  1.00 31.66  ? 71  ASP   B O   1 
ATOM   985  C CB  . ASP   B 2 62  ? -17.475 -3.225  -2.388  1.00 34.59  ? 71  ASP   B CB  1 
ATOM   986  C CG  . ASP   B 2 62  ? -16.346 -4.096  -1.886  1.00 37.05  ? 71  ASP   B CG  1 
ATOM   987  O OD1 . ASP   B 2 62  ? -15.228 -3.995  -2.412  1.00 39.14  ? 71  ASP   B OD1 1 
ATOM   988  O OD2 . ASP   B 2 62  ? -16.609 -4.771  -0.830  1.00 43.92  ? 71  ASP   B OD2 1 
ATOM   989  N N   . VAL   B 2 63  ? -15.159 -0.413  -2.173  1.00 32.76  ? 72  VAL   B N   1 
ATOM   990  C CA  . VAL   B 2 63  ? -13.896 0.195   -2.693  1.00 33.51  ? 72  VAL   B CA  1 
ATOM   991  C C   . VAL   B 2 63  ? -13.016 -0.909  -3.303  1.00 33.89  ? 72  VAL   B C   1 
ATOM   992  O O   . VAL   B 2 63  ? -12.361 -0.640  -4.401  1.00 32.79  ? 72  VAL   B O   1 
ATOM   993  C CB  . VAL   B 2 63  ? -13.141 0.994   -1.598  1.00 34.95  ? 72  VAL   B CB  1 
ATOM   994  C CG1 . VAL   B 2 63  ? -11.678 1.187   -1.975  1.00 35.60  ? 72  VAL   B CG1 1 
ATOM   995  C CG2 . VAL   B 2 63  ? -13.783 2.351   -1.371  1.00 34.51  ? 72  VAL   B CG2 1 
ATOM   996  N N   . LYS   B 2 64  ? -13.018 -2.129  -2.770  1.00 33.76  ? 73  LYS   B N   1 
ATOM   997  C CA  . LYS   B 2 64  ? -12.074 -3.164  -3.297  1.00 35.17  ? 73  LYS   B CA  1 
ATOM   998  C C   . LYS   B 2 64  ? -12.570 -3.669  -4.669  1.00 34.01  ? 73  LYS   B C   1 
ATOM   999  O O   . LYS   B 2 64  ? -11.729 -3.848  -5.662  1.00 36.92  ? 73  LYS   B O   1 
ATOM   1000 C CB  . LYS   B 2 64  ? -11.892 -4.335  -2.335  1.00 35.53  ? 73  LYS   B CB  1 
ATOM   1001 C CG  . LYS   B 2 64  ? -10.764 -5.252  -2.763  1.00 36.83  ? 73  LYS   B CG  1 
ATOM   1002 C CD  . LYS   B 2 64  ? -10.327 -6.255  -1.800  1.00 38.58  ? 73  LYS   B CD  1 
ATOM   1003 C CE  . LYS   B 2 64  ? -9.379  -7.249  -2.438  1.00 39.80  ? 73  LYS   B CE  1 
ATOM   1004 N NZ  . LYS   B 2 64  ? -8.921  -8.204  -1.396  1.00 41.26  ? 73  LYS   B NZ  1 
ATOM   1005 N N   . GLN   B 2 65  ? -13.879 -3.936  -4.773  1.00 34.30  ? 74  GLN   B N   1 
ATOM   1006 C CA  . GLN   B 2 65  ? -14.521 -4.318  -6.055  1.00 34.90  ? 74  GLN   B CA  1 
ATOM   1007 C C   . GLN   B 2 65  ? -14.511 -3.112  -6.982  1.00 33.71  ? 74  GLN   B C   1 
ATOM   1008 O O   . GLN   B 2 65  ? -14.640 -3.421  -8.187  1.00 30.24  ? 74  GLN   B O   1 
ATOM   1009 C CB  . GLN   B 2 65  ? -15.947 -4.826  -5.905  1.00 37.13  ? 74  GLN   B CB  1 
ATOM   1010 C CG  . GLN   B 2 65  ? -16.045 -6.046  -4.996  1.00 41.24  ? 74  GLN   B CG  1 
ATOM   1011 C CD  . GLN   B 2 65  ? -17.479 -6.527  -4.959  1.00 44.39  ? 74  GLN   B CD  1 
ATOM   1012 O OE1 . GLN   B 2 65  ? -18.183 -6.568  -5.979  1.00 47.65  ? 74  GLN   B OE1 1 
ATOM   1013 N NE2 . GLN   B 2 65  ? -17.942 -6.848  -3.778  1.00 47.31  ? 74  GLN   B NE2 1 
ATOM   1014 N N   . ASP   B 2 66  ? -14.267 -1.875  -6.516  1.00 32.61  ? 75  ASP   B N   1 
ATOM   1015 C CA  . ASP   B 2 66  ? -14.431 -0.564  -7.230  1.00 32.58  ? 75  ASP   B CA  1 
ATOM   1016 C C   . ASP   B 2 66  ? -15.791 -0.473  -7.937  1.00 32.04  ? 75  ASP   B C   1 
ATOM   1017 O O   . ASP   B 2 66  ? -15.809 -0.058  -9.128  1.00 31.00  ? 75  ASP   B O   1 
ATOM   1018 C CB  . ASP   B 2 66  ? -13.352 -0.352  -8.308  1.00 33.21  ? 75  ASP   B CB  1 
ATOM   1019 C CG  . ASP   B 2 66  ? -13.192 1.064   -8.833  1.00 32.67  ? 75  ASP   B CG  1 
ATOM   1020 O OD1 . ASP   B 2 66  ? -13.579 2.042   -8.202  1.00 32.42  ? 75  ASP   B OD1 1 
ATOM   1021 O OD2 . ASP   B 2 66  ? -12.733 1.150   -10.059 1.00 33.29  ? 75  ASP   B OD2 1 
ATOM   1022 N N   . LEU   B 2 67  ? -16.893 -0.892  -7.330  1.00 31.10  ? 76  LEU   B N   1 
ATOM   1023 C CA  . LEU   B 2 67  ? -18.295 -0.759  -7.794  1.00 30.50  ? 76  LEU   B CA  1 
ATOM   1024 C C   . LEU   B 2 67  ? -19.164 0.020   -6.810  1.00 31.29  ? 76  LEU   B C   1 
ATOM   1025 O O   . LEU   B 2 67  ? -18.902 -0.020  -5.578  1.00 30.49  ? 76  LEU   B O   1 
ATOM   1026 C CB  . LEU   B 2 67  ? -18.835 -2.166  -8.037  1.00 31.25  ? 76  LEU   B CB  1 
ATOM   1027 C CG  . LEU   B 2 67  ? -18.188 -2.957  -9.197  1.00 32.64  ? 76  LEU   B CG  1 
ATOM   1028 C CD1 . LEU   B 2 67  ? -18.852 -4.310  -9.257  1.00 33.78  ? 76  LEU   B CD1 1 
ATOM   1029 C CD2 . LEU   B 2 67  ? -18.389 -2.229  -10.529 1.00 32.77  ? 76  LEU   B CD2 1 
ATOM   1030 N N   . VAL   B 2 68  ? -20.302 0.513   -7.254  1.00 30.27  ? 77  VAL   B N   1 
ATOM   1031 C CA  . VAL   B 2 68  ? -21.329 1.260   -6.489  1.00 29.91  ? 77  VAL   B CA  1 
ATOM   1032 C C   . VAL   B 2 68  ? -22.643 1.186   -7.270  1.00 29.54  ? 77  VAL   B C   1 
ATOM   1033 O O   . VAL   B 2 68  ? -22.608 1.283   -8.581  1.00 28.06  ? 77  VAL   B O   1 
ATOM   1034 C CB  . VAL   B 2 68  ? -20.854 2.680   -6.122  1.00 30.47  ? 77  VAL   B CB  1 
ATOM   1035 C CG1 . VAL   B 2 68  ? -20.470 3.554   -7.329  1.00 31.25  ? 77  VAL   B CG1 1 
ATOM   1036 C CG2 . VAL   B 2 68  ? -21.861 3.411   -5.233  1.00 31.18  ? 77  VAL   B CG2 1 
ATOM   1037 N N   A SER   B 2 69  ? -23.756 0.943   -6.592  0.25 29.57  ? 78  SER   B N   1 
ATOM   1038 N N   B SER   B 2 69  ? -23.756 0.943   -6.592  0.25 29.57  ? 78  SER   B N   1 
ATOM   1039 N N   C SER   B 2 69  ? -23.757 0.943   -6.592  0.25 29.57  ? 78  SER   B N   1 
ATOM   1040 N N   D SER   B 2 69  ? -23.757 0.943   -6.592  0.25 29.57  ? 78  SER   B N   1 
ATOM   1041 C CA  A SER   B 2 69  ? -25.142 1.017   -7.109  0.25 29.85  ? 78  SER   B CA  1 
ATOM   1042 C CA  B SER   B 2 69  ? -25.142 1.017   -7.109  0.25 29.85  ? 78  SER   B CA  1 
ATOM   1043 C CA  C SER   B 2 69  ? -25.142 1.016   -7.109  0.25 29.85  ? 78  SER   B CA  1 
ATOM   1044 C CA  D SER   B 2 69  ? -25.142 1.016   -7.109  0.25 29.85  ? 78  SER   B CA  1 
ATOM   1045 C C   A SER   B 2 69  ? -25.918 2.150   -6.429  0.25 30.84  ? 78  SER   B C   1 
ATOM   1046 C C   B SER   B 2 69  ? -25.918 2.150   -6.429  0.25 30.84  ? 78  SER   B C   1 
ATOM   1047 C C   C SER   B 2 69  ? -25.919 2.149   -6.430  0.25 30.85  ? 78  SER   B C   1 
ATOM   1048 C C   D SER   B 2 69  ? -25.919 2.149   -6.430  0.25 30.85  ? 78  SER   B C   1 
ATOM   1049 O O   A SER   B 2 69  ? -25.648 2.443   -5.226  0.25 30.95  ? 78  SER   B O   1 
ATOM   1050 O O   B SER   B 2 69  ? -25.648 2.443   -5.226  0.25 30.95  ? 78  SER   B O   1 
ATOM   1051 O O   C SER   B 2 69  ? -25.649 2.443   -5.226  0.25 30.95  ? 78  SER   B O   1 
ATOM   1052 O O   D SER   B 2 69  ? -25.649 2.443   -5.226  0.25 30.95  ? 78  SER   B O   1 
ATOM   1053 C CB  A SER   B 2 69  ? -25.849 -0.313  -6.999  0.25 29.94  ? 78  SER   B CB  1 
ATOM   1054 C CB  B SER   B 2 69  ? -25.849 -0.313  -6.999  0.25 29.94  ? 78  SER   B CB  1 
ATOM   1055 C CB  C SER   B 2 69  ? -25.851 -0.314  -6.999  0.25 29.95  ? 78  SER   B CB  1 
ATOM   1056 C CB  D SER   B 2 69  ? -25.851 -0.314  -6.999  0.25 29.95  ? 78  SER   B CB  1 
ATOM   1057 O OG  A SER   B 2 69  ? -26.123 -0.660  -5.642  0.25 30.11  ? 78  SER   B OG  1 
ATOM   1058 O OG  B SER   B 2 69  ? -26.123 -0.660  -5.642  0.25 30.11  ? 78  SER   B OG  1 
ATOM   1059 O OG  C SER   B 2 69  ? -26.122 -0.661  -5.642  0.25 30.12  ? 78  SER   B OG  1 
ATOM   1060 O OG  D SER   B 2 69  ? -26.122 -0.661  -5.642  0.25 30.12  ? 78  SER   B OG  1 
ATOM   1061 N N   A TYR   B 2 70  ? -26.851 2.768   -7.158  0.25 31.45  ? 79  TYR   B N   1 
ATOM   1062 N N   B TYR   B 2 70  ? -26.851 2.768   -7.158  0.25 31.45  ? 79  TYR   B N   1 
ATOM   1063 N N   C TYR   B 2 70  ? -26.856 2.761   -7.159  0.25 31.51  ? 79  TYR   B N   1 
ATOM   1064 N N   D TYR   B 2 70  ? -26.856 2.761   -7.159  0.25 31.51  ? 79  TYR   B N   1 
ATOM   1065 C CA  A TYR   B 2 70  ? -27.728 3.861   -6.661  0.25 32.12  ? 79  TYR   B CA  1 
ATOM   1066 C CA  B TYR   B 2 70  ? -27.728 3.861   -6.661  0.25 32.12  ? 79  TYR   B CA  1 
ATOM   1067 C CA  C TYR   B 2 70  ? -27.725 3.861   -6.666  0.25 32.23  ? 79  TYR   B CA  1 
ATOM   1068 C CA  D TYR   B 2 70  ? -27.725 3.861   -6.666  0.25 32.23  ? 79  TYR   B CA  1 
ATOM   1069 C C   A TYR   B 2 70  ? -29.192 3.424   -6.759  0.25 33.00  ? 79  TYR   B C   1 
ATOM   1070 C C   B TYR   B 2 70  ? -29.192 3.424   -6.759  0.25 33.00  ? 79  TYR   B C   1 
ATOM   1071 C C   C TYR   B 2 70  ? -29.191 3.440   -6.756  0.25 33.13  ? 79  TYR   B C   1 
ATOM   1072 C C   D TYR   B 2 70  ? -29.191 3.440   -6.756  0.25 33.13  ? 79  TYR   B C   1 
ATOM   1073 O O   A TYR   B 2 70  ? -29.547 2.860   -7.802  0.25 32.70  ? 79  TYR   B O   1 
ATOM   1074 O O   B TYR   B 2 70  ? -29.547 2.860   -7.802  0.25 32.70  ? 79  TYR   B O   1 
ATOM   1075 O O   C TYR   B 2 70  ? -29.548 2.805   -7.761  0.25 32.82  ? 79  TYR   B O   1 
ATOM   1076 O O   D TYR   B 2 70  ? -29.548 2.805   -7.761  0.25 32.82  ? 79  TYR   B O   1 
ATOM   1077 C CB  A TYR   B 2 70  ? -27.474 5.151   -7.449  0.25 31.99  ? 79  TYR   B CB  1 
ATOM   1078 C CB  B TYR   B 2 70  ? -27.474 5.151   -7.449  0.25 31.99  ? 79  TYR   B CB  1 
ATOM   1079 C CB  C TYR   B 2 70  ? -27.485 5.145   -7.465  0.25 32.12  ? 79  TYR   B CB  1 
ATOM   1080 C CB  D TYR   B 2 70  ? -27.485 5.145   -7.465  0.25 32.12  ? 79  TYR   B CB  1 
ATOM   1081 C CG  A TYR   B 2 70  ? -26.129 5.783   -7.170  0.25 31.90  ? 79  TYR   B CG  1 
ATOM   1082 C CG  B TYR   B 2 70  ? -26.129 5.783   -7.170  0.25 31.90  ? 79  TYR   B CG  1 
ATOM   1083 C CG  C TYR   B 2 70  ? -26.119 5.740   -7.229  0.25 32.05  ? 79  TYR   B CG  1 
ATOM   1084 C CG  D TYR   B 2 70  ? -26.119 5.740   -7.229  0.25 32.05  ? 79  TYR   B CG  1 
ATOM   1085 C CD1 A TYR   B 2 70  ? -24.951 5.302   -7.737  0.25 31.36  ? 79  TYR   B CD1 1 
ATOM   1086 C CD1 B TYR   B 2 70  ? -24.951 5.302   -7.737  0.25 31.36  ? 79  TYR   B CD1 1 
ATOM   1087 C CD1 C TYR   B 2 70  ? -24.975 5.173   -7.777  0.25 31.51  ? 79  TYR   B CD1 1 
ATOM   1088 C CD1 D TYR   B 2 70  ? -24.975 5.173   -7.777  0.25 31.51  ? 79  TYR   B CD1 1 
ATOM   1089 C CD2 A TYR   B 2 70  ? -26.016 6.843   -6.288  0.25 32.32  ? 79  TYR   B CD2 1 
ATOM   1090 C CD2 B TYR   B 2 70  ? -26.016 6.843   -6.288  0.25 32.32  ? 79  TYR   B CD2 1 
ATOM   1091 C CD2 C TYR   B 2 70  ? -25.952 6.833   -6.397  0.25 32.45  ? 79  TYR   B CD2 1 
ATOM   1092 C CD2 D TYR   B 2 70  ? -25.952 6.833   -6.397  0.25 32.45  ? 79  TYR   B CD2 1 
ATOM   1093 C CE1 A TYR   B 2 70  ? -23.712 5.882   -7.455  0.25 31.33  ? 79  TYR   B CE1 1 
ATOM   1094 C CE1 B TYR   B 2 70  ? -23.712 5.882   -7.455  0.25 31.33  ? 79  TYR   B CE1 1 
ATOM   1095 C CE1 C TYR   B 2 70  ? -23.710 5.707   -7.542  0.25 31.49  ? 79  TYR   B CE1 1 
ATOM   1096 C CE1 D TYR   B 2 70  ? -23.710 5.707   -7.542  0.25 31.49  ? 79  TYR   B CE1 1 
ATOM   1097 C CE2 A TYR   B 2 70  ? -24.789 7.432   -5.999  0.25 32.33  ? 79  TYR   B CE2 1 
ATOM   1098 C CE2 B TYR   B 2 70  ? -24.789 7.432   -5.999  0.25 32.33  ? 79  TYR   B CE2 1 
ATOM   1099 C CE2 C TYR   B 2 70  ? -24.696 7.377   -6.151  0.25 32.50  ? 79  TYR   B CE2 1 
ATOM   1100 C CE2 D TYR   B 2 70  ? -24.696 7.377   -6.151  0.25 32.50  ? 79  TYR   B CE2 1 
ATOM   1101 C CZ  A TYR   B 2 70  ? -23.630 6.948   -6.570  0.25 31.94  ? 79  TYR   B CZ  1 
ATOM   1102 C CZ  B TYR   B 2 70  ? -23.630 6.948   -6.570  0.25 31.94  ? 79  TYR   B CZ  1 
ATOM   1103 C CZ  C TYR   B 2 70  ? -23.570 6.814   -6.721  0.25 32.17  ? 79  TYR   B CZ  1 
ATOM   1104 C CZ  D TYR   B 2 70  ? -23.570 6.814   -6.721  0.25 32.17  ? 79  TYR   B CZ  1 
ATOM   1105 O OH  A TYR   B 2 70  ? -22.456 7.576   -6.147  0.25 32.28  ? 79  TYR   B OH  1 
ATOM   1106 O OH  B TYR   B 2 70  ? -22.456 7.576   -6.147  0.25 32.28  ? 79  TYR   B OH  1 
ATOM   1107 O OH  C TYR   B 2 70  ? -22.344 7.359   -6.371  0.25 32.66  ? 79  TYR   B OH  1 
ATOM   1108 O OH  D TYR   B 2 70  ? -22.344 7.359   -6.371  0.25 32.66  ? 79  TYR   B OH  1 
ATOM   1109 N N   A CYS   B 2 71  ? -29.995 3.652   -5.703  0.25 33.91  ? 80  CYS   B N   1 
ATOM   1110 N N   B CYS   B 2 71  ? -29.995 3.652   -5.703  0.25 33.91  ? 80  CYS   B N   1 
ATOM   1111 N N   C CYS   B 2 71  ? -29.996 3.781   -5.735  0.25 34.08  ? 80  CYS   B N   1 
ATOM   1112 N N   D CYS   B 2 71  ? -29.996 3.781   -5.735  0.25 34.08  ? 80  CYS   B N   1 
ATOM   1113 C CA  A CYS   B 2 71  ? -31.482 3.556   -5.718  0.25 35.05  ? 80  CYS   B CA  1 
ATOM   1114 C CA  B CYS   B 2 71  ? -31.482 3.556   -5.718  0.25 35.05  ? 80  CYS   B CA  1 
ATOM   1115 C CA  C CYS   B 2 71  ? -31.478 3.650   -5.740  0.25 35.24  ? 80  CYS   B CA  1 
ATOM   1116 C CA  D CYS   B 2 71  ? -31.478 3.650   -5.740  0.25 35.24  ? 80  CYS   B CA  1 
ATOM   1117 C C   A CYS   B 2 71  ? -31.935 2.130   -5.412  0.25 35.03  ? 80  CYS   B C   1 
ATOM   1118 C C   B CYS   B 2 71  ? -31.935 2.130   -5.412  0.25 35.03  ? 80  CYS   B C   1 
ATOM   1119 C C   C CYS   B 2 71  ? -31.887 2.183   -5.565  0.25 35.15  ? 80  CYS   B C   1 
ATOM   1120 C C   D CYS   B 2 71  ? -31.887 2.183   -5.565  0.25 35.15  ? 80  CYS   B C   1 
ATOM   1121 O O   A CYS   B 2 71  ? -33.159 2.010   -4.799  0.25 36.05  ? 80  CYS   B O   1 
ATOM   1122 O O   B CYS   B 2 71  ? -33.159 2.010   -4.799  0.25 36.05  ? 80  CYS   B O   1 
ATOM   1123 O O   C CYS   B 2 71  ? -33.116 1.910   -5.578  0.25 35.91  ? 80  CYS   B O   1 
ATOM   1124 O O   D CYS   B 2 71  ? -33.116 1.910   -5.578  0.25 35.91  ? 80  CYS   B O   1 
ATOM   1125 C CB  A CYS   B 2 71  ? -32.029 3.943   -7.075  0.25 35.70  ? 80  CYS   B CB  1 
ATOM   1126 C CB  B CYS   B 2 71  ? -32.029 3.943   -7.075  0.25 35.70  ? 80  CYS   B CB  1 
ATOM   1127 C CB  C CYS   B 2 71  ? -32.084 4.079   -7.063  0.25 35.93  ? 80  CYS   B CB  1 
ATOM   1128 C CB  D CYS   B 2 71  ? -32.084 4.079   -7.063  0.25 35.93  ? 80  CYS   B CB  1 
ATOM   1129 S SG  A CYS   B 2 71  ? -31.184 5.511   -7.617  0.25 36.93  ? 80  CYS   B SG  1 
ATOM   1130 S SG  B CYS   B 2 71  ? -31.184 5.511   -7.617  0.25 36.93  ? 80  CYS   B SG  1 
ATOM   1131 S SG  C CYS   B 2 71  ? -31.920 5.915   -7.261  0.25 37.53  ? 80  CYS   B SG  1 
ATOM   1132 S SG  D CYS   B 2 71  ? -31.920 5.915   -7.261  0.25 37.53  ? 80  CYS   B SG  1 
ATOM   1133 N N   A GLY   B 2 72  ? -30.985 1.110   -5.798  0.25 34.43  ? 81  GLY   B N   1 
ATOM   1134 N N   B GLY   B 2 72  ? -30.985 1.110   -5.798  0.25 34.43  ? 81  GLY   B N   1 
ATOM   1135 N N   C GLY   B 2 72  ? -30.868 1.258   -5.670  0.25 34.68  ? 81  GLY   B N   1 
ATOM   1136 N N   D GLY   B 2 72  ? -30.868 1.258   -5.670  0.25 34.68  ? 81  GLY   B N   1 
ATOM   1137 C CA  A GLY   B 2 72  ? -31.245 -0.305  -5.516  0.25 34.59  ? 81  GLY   B CA  1 
ATOM   1138 C CA  B GLY   B 2 72  ? -31.245 -0.305  -5.516  0.25 34.59  ? 81  GLY   B CA  1 
ATOM   1139 C CA  C GLY   B 2 72  ? -31.140 -0.166  -5.468  0.25 34.74  ? 81  GLY   B CA  1 
ATOM   1140 C CA  D GLY   B 2 72  ? -31.140 -0.166  -5.468  0.25 34.74  ? 81  GLY   B CA  1 
ATOM   1141 C C   A GLY   B 2 72  ? -29.878 -1.117  -5.559  0.25 34.02  ? 81  GLY   B C   1 
ATOM   1142 C C   B GLY   B 2 72  ? -29.878 -1.117  -5.559  0.25 34.02  ? 81  GLY   B C   1 
ATOM   1143 C C   C GLY   B 2 72  ? -29.802 -0.991  -5.522  0.25 34.13  ? 81  GLY   B C   1 
ATOM   1144 C C   D GLY   B 2 72  ? -29.802 -0.991  -5.522  0.25 34.13  ? 81  GLY   B C   1 
ATOM   1145 O O   A GLY   B 2 72  ? -28.795 -0.622  -5.772  0.25 33.90  ? 81  GLY   B O   1 
ATOM   1146 O O   B GLY   B 2 72  ? -28.795 -0.622  -5.772  0.25 33.90  ? 81  GLY   B O   1 
ATOM   1147 O O   C GLY   B 2 72  ? -28.748 -0.529  -5.751  0.25 34.01  ? 81  GLY   B O   1 
ATOM   1148 O O   D GLY   B 2 72  ? -28.748 -0.529  -5.751  0.25 34.01  ? 81  GLY   B O   1 
ATOM   1149 N N   A PRO   B 2 73  ? -30.100 -2.461  -5.284  0.25 34.34  ? 82  PRO   B N   1 
ATOM   1150 N N   B PRO   B 2 73  ? -30.100 -2.461  -5.284  0.25 34.34  ? 82  PRO   B N   1 
ATOM   1151 N N   C PRO   B 2 73  ? -30.041 -2.334  -5.323  0.25 34.32  ? 82  PRO   B N   1 
ATOM   1152 N N   D PRO   B 2 73  ? -30.041 -2.334  -5.323  0.25 34.32  ? 82  PRO   B N   1 
ATOM   1153 C CA  A PRO   B 2 73  ? -29.009 -3.498  -5.066  0.25 34.20  ? 82  PRO   B CA  1 
ATOM   1154 C CA  B PRO   B 2 73  ? -29.009 -3.498  -5.066  0.25 34.20  ? 82  PRO   B CA  1 
ATOM   1155 C CA  C PRO   B 2 73  ? -28.958 -3.365  -5.078  0.25 34.22  ? 82  PRO   B CA  1 
ATOM   1156 C CA  D PRO   B 2 73  ? -28.958 -3.365  -5.078  0.25 34.22  ? 82  PRO   B CA  1 
ATOM   1157 C C   A PRO   B 2 73  ? -28.475 -3.684  -6.500  0.25 33.78  ? 82  PRO   B C   1 
ATOM   1158 C C   B PRO   B 2 73  ? -28.475 -3.684  -6.500  0.25 33.78  ? 82  PRO   B C   1 
ATOM   1159 C C   C PRO   B 2 73  ? -28.461 -3.644  -6.506  0.25 33.79  ? 82  PRO   B C   1 
ATOM   1160 C C   D PRO   B 2 73  ? -28.461 -3.644  -6.506  0.25 33.79  ? 82  PRO   B C   1 
ATOM   1161 O O   A PRO   B 2 73  ? -29.246 -3.460  -7.448  0.25 34.28  ? 82  PRO   B O   1 
ATOM   1162 O O   B PRO   B 2 73  ? -29.246 -3.460  -7.448  0.25 34.28  ? 82  PRO   B O   1 
ATOM   1163 O O   C PRO   B 2 73  ? -29.242 -3.455  -7.450  0.25 34.31  ? 82  PRO   B O   1 
ATOM   1164 O O   D PRO   B 2 73  ? -29.242 -3.455  -7.450  0.25 34.31  ? 82  PRO   B O   1 
ATOM   1165 C CB  A PRO   B 2 73  ? -29.645 -4.767  -4.459  0.25 34.91  ? 82  PRO   B CB  1 
ATOM   1166 C CB  B PRO   B 2 73  ? -29.645 -4.767  -4.459  0.25 34.91  ? 82  PRO   B CB  1 
ATOM   1167 C CB  C PRO   B 2 73  ? -29.605 -4.576  -4.380  0.25 34.94  ? 82  PRO   B CB  1 
ATOM   1168 C CB  D PRO   B 2 73  ? -29.605 -4.576  -4.380  0.25 34.94  ? 82  PRO   B CB  1 
ATOM   1169 C CG  A PRO   B 2 73  ? -31.125 -4.641  -4.748  0.25 35.20  ? 82  PRO   B CG  1 
ATOM   1170 C CG  B PRO   B 2 73  ? -31.125 -4.641  -4.748  0.25 35.20  ? 82  PRO   B CG  1 
ATOM   1171 C CG  C PRO   B 2 73  ? -31.069 -4.477  -4.740  0.25 35.16  ? 82  PRO   B CG  1 
ATOM   1172 C CG  D PRO   B 2 73  ? -31.069 -4.477  -4.740  0.25 35.16  ? 82  PRO   B CG  1 
ATOM   1173 C CD  A PRO   B 2 73  ? -31.428 -3.152  -4.765  0.25 34.92  ? 82  PRO   B CD  1 
ATOM   1174 C CD  B PRO   B 2 73  ? -31.428 -3.152  -4.765  0.25 34.92  ? 82  PRO   B CD  1 
ATOM   1175 C CD  C PRO   B 2 73  ? -31.372 -2.990  -4.807  0.25 34.87  ? 82  PRO   B CD  1 
ATOM   1176 C CD  D PRO   B 2 73  ? -31.372 -2.990  -4.807  0.25 34.87  ? 82  PRO   B CD  1 
ATOM   1177 N N   . TRP   B 2 74  ? -27.191 -4.044  -6.622  1.00 33.36  ? 83  TRP   B N   1 
ATOM   1178 C CA  . TRP   B 2 74  ? -26.583 -4.411  -7.930  1.00 33.00  ? 83  TRP   B CA  1 
ATOM   1179 C C   . TRP   B 2 74  ? -27.500 -5.400  -8.629  1.00 34.73  ? 83  TRP   B C   1 
ATOM   1180 O O   . TRP   B 2 74  ? -27.849 -6.413  -8.066  1.00 34.69  ? 83  TRP   B O   1 
ATOM   1181 C CB  . TRP   B 2 74  ? -25.206 -5.007  -7.680  1.00 32.91  ? 83  TRP   B CB  1 
ATOM   1182 C CG  . TRP   B 2 74  ? -24.388 -5.167  -8.912  1.00 32.00  ? 83  TRP   B CG  1 
ATOM   1183 C CD1 . TRP   B 2 74  ? -24.342 -6.268  -9.703  1.00 32.89  ? 83  TRP   B CD1 1 
ATOM   1184 C CD2 . TRP   B 2 74  ? -23.508 -4.188  -9.486  1.00 31.91  ? 83  TRP   B CD2 1 
ATOM   1185 N NE1 . TRP   B 2 74  ? -23.503 -6.051  -10.752 1.00 31.94  ? 83  TRP   B NE1 1 
ATOM   1186 C CE2 . TRP   B 2 74  ? -23.002 -4.775  -10.676 1.00 31.73  ? 83  TRP   B CE2 1 
ATOM   1187 C CE3 . TRP   B 2 74  ? -23.195 -2.847  -9.206  1.00 31.37  ? 83  TRP   B CE3 1 
ATOM   1188 C CZ2 . TRP   B 2 74  ? -22.108 -4.105  -11.521 1.00 31.17  ? 83  TRP   B CZ2 1 
ATOM   1189 C CZ3 . TRP   B 2 74  ? -22.317 -2.189  -10.055 1.00 31.30  ? 83  TRP   B CZ3 1 
ATOM   1190 C CH2 . TRP   B 2 74  ? -21.821 -2.797  -11.228 1.00 30.57  ? 83  TRP   B CH2 1 
ATOM   1191 N N   . LYS   B 2 75  ? -27.801 -5.115  -9.916  1.00 34.55  ? 84  LYS   B N   1 
ATOM   1192 C CA  . LYS   B 2 75  ? -28.764 -5.876  -10.749 1.00 37.13  ? 84  LYS   B CA  1 
ATOM   1193 C C   . LYS   B 2 75  ? -28.014 -6.715  -11.785 1.00 38.15  ? 84  LYS   B C   1 
ATOM   1194 O O   . LYS   B 2 75  ? -28.680 -7.602  -12.388 1.00 40.10  ? 84  LYS   B O   1 
ATOM   1195 C CB  . LYS   B 2 75  ? -29.690 -4.880  -11.453 1.00 37.54  ? 84  LYS   B CB  1 
ATOM   1196 C CG  . LYS   B 2 75  ? -30.559 -4.022  -10.542 1.00 38.13  ? 84  LYS   B CG  1 
ATOM   1197 C CD  . LYS   B 2 75  ? -31.656 -4.832  -9.924  1.00 39.71  ? 84  LYS   B CD  1 
ATOM   1198 C CE  . LYS   B 2 75  ? -32.409 -4.052  -8.863  1.00 40.91  ? 84  LYS   B CE  1 
ATOM   1199 N NZ  . LYS   B 2 75  ? -33.516 -4.869  -8.329  1.00 43.12  ? 84  LYS   B NZ  1 
ATOM   1200 N N   . LEU   B 2 76  ? -26.748 -6.405  -12.077 1.00 38.00  ? 85  LEU   B N   1 
ATOM   1201 C CA  . LEU   B 2 76  ? -26.063 -6.949  -13.301 1.00 38.78  ? 85  LEU   B CA  1 
ATOM   1202 C C   . LEU   B 2 76  ? -25.327 -8.245  -12.960 1.00 41.05  ? 85  LEU   B C   1 
ATOM   1203 O O   . LEU   B 2 76  ? -24.404 -8.214  -12.101 1.00 41.60  ? 85  LEU   B O   1 
ATOM   1204 C CB  . LEU   B 2 76  ? -25.101 -5.912  -13.881 1.00 37.48  ? 85  LEU   B CB  1 
ATOM   1205 C CG  . LEU   B 2 76  ? -25.717 -4.533  -14.067 1.00 36.74  ? 85  LEU   B CG  1 
ATOM   1206 C CD1 . LEU   B 2 76  ? -24.699 -3.550  -14.585 1.00 36.02  ? 85  LEU   B CD1 1 
ATOM   1207 C CD2 . LEU   B 2 76  ? -26.979 -4.581  -14.906 1.00 38.30  ? 85  LEU   B CD2 1 
ATOM   1208 N N   . ASP   B 2 77  ? -25.720 -9.340  -13.619 1.00 44.43  ? 86  ASP   B N   1 
ATOM   1209 C CA  . ASP   B 2 77  ? -25.372 -10.716 -13.194 1.00 47.54  ? 86  ASP   B CA  1 
ATOM   1210 C C   . ASP   B 2 77  ? -24.756 -11.516 -14.352 1.00 45.59  ? 86  ASP   B C   1 
ATOM   1211 O O   . ASP   B 2 77  ? -24.421 -12.685 -14.162 1.00 43.89  ? 86  ASP   B O   1 
ATOM   1212 C CB  . ASP   B 2 77  ? -26.584 -11.421 -12.572 1.00 52.35  ? 86  ASP   B CB  1 
ATOM   1213 C CG  . ASP   B 2 77  ? -27.776 -11.631 -13.493 1.00 57.51  ? 86  ASP   B CG  1 
ATOM   1214 O OD1 . ASP   B 2 77  ? -27.823 -11.008 -14.585 1.00 58.23  ? 86  ASP   B OD1 1 
ATOM   1215 O OD2 . ASP   B 2 77  ? -28.685 -12.400 -13.093 1.00 63.66  ? 86  ASP   B OD2 1 
ATOM   1216 N N   . ALA   B 2 78  ? -24.562 -10.937 -15.528 1.00 44.38  ? 87  ALA   B N   1 
ATOM   1217 C CA  . ALA   B 2 78  ? -23.987 -11.731 -16.628 1.00 43.46  ? 87  ALA   B CA  1 
ATOM   1218 C C   . ALA   B 2 78  ? -22.460 -11.786 -16.522 1.00 42.49  ? 87  ALA   B C   1 
ATOM   1219 O O   . ALA   B 2 78  ? -21.813 -10.791 -16.076 1.00 40.60  ? 87  ALA   B O   1 
ATOM   1220 C CB  . ALA   B 2 78  ? -24.425 -11.193 -17.967 1.00 43.41  ? 87  ALA   B CB  1 
ATOM   1221 N N   . ALA   B 2 79  ? -21.908 -12.855 -17.122 1.00 43.58  ? 88  ALA   B N   1 
ATOM   1222 C CA  . ALA   B 2 79  ? -20.484 -13.231 -17.064 1.00 44.96  ? 88  ALA   B CA  1 
ATOM   1223 C C   . ALA   B 2 79  ? -19.908 -13.476 -18.467 1.00 43.91  ? 88  ALA   B C   1 
ATOM   1224 O O   . ALA   B 2 79  ? -20.588 -14.153 -19.269 1.00 45.54  ? 88  ALA   B O   1 
ATOM   1225 C CB  . ALA   B 2 79  ? -20.350 -14.444 -16.166 1.00 46.46  ? 88  ALA   B CB  1 
ATOM   1226 N N   . TRP   B 2 80  ? -18.698 -12.956 -18.730 1.00 43.02  ? 89  TRP   B N   1 
ATOM   1227 C CA  . TRP   B 2 80  ? -17.834 -13.378 -19.865 1.00 45.12  ? 89  TRP   B CA  1 
ATOM   1228 C C   . TRP   B 2 80  ? -17.745 -14.898 -19.867 1.00 46.85  ? 89  TRP   B C   1 
ATOM   1229 O O   . TRP   B 2 80  ? -17.570 -15.507 -18.746 1.00 43.05  ? 89  TRP   B O   1 
ATOM   1230 C CB  . TRP   B 2 80  ? -16.447 -12.734 -19.889 1.00 44.61  ? 89  TRP   B CB  1 
ATOM   1231 C CG  . TRP   B 2 80  ? -15.646 -13.106 -21.098 1.00 45.88  ? 89  TRP   B CG  1 
ATOM   1232 C CD1 . TRP   B 2 80  ? -16.081 -13.191 -22.397 1.00 46.75  ? 89  TRP   B CD1 1 
ATOM   1233 C CD2 . TRP   B 2 80  ? -14.250 -13.447 -21.116 1.00 46.27  ? 89  TRP   B CD2 1 
ATOM   1234 N NE1 . TRP   B 2 80  ? -15.046 -13.540 -23.216 1.00 47.75  ? 89  TRP   B NE1 1 
ATOM   1235 C CE2 . TRP   B 2 80  ? -13.921 -13.751 -22.454 1.00 47.77  ? 89  TRP   B CE2 1 
ATOM   1236 C CE3 . TRP   B 2 80  ? -13.274 -13.587 -20.108 1.00 45.23  ? 89  TRP   B CE3 1 
ATOM   1237 C CZ2 . TRP   B 2 80  ? -12.633 -14.124 -22.835 1.00 47.65  ? 89  TRP   B CZ2 1 
ATOM   1238 C CZ3 . TRP   B 2 80  ? -12.000 -13.968 -20.491 1.00 46.18  ? 89  TRP   B CZ3 1 
ATOM   1239 C CH2 . TRP   B 2 80  ? -11.694 -14.224 -21.831 1.00 47.17  ? 89  TRP   B CH2 1 
ATOM   1240 N N   . ASP   B 2 81  ? -17.958 -15.487 -21.050 1.00 47.78  ? 90  ASP   B N   1 
ATOM   1241 C CA  . ASP   B 2 81  ? -18.016 -16.962 -21.236 1.00 51.26  ? 90  ASP   B CA  1 
ATOM   1242 C C   . ASP   B 2 81  ? -16.600 -17.539 -21.160 1.00 52.07  ? 90  ASP   B C   1 
ATOM   1243 O O   . ASP   B 2 81  ? -16.524 -18.758 -20.987 1.00 55.14  ? 90  ASP   B O   1 
ATOM   1244 C CB  . ASP   B 2 81  ? -18.772 -17.385 -22.518 1.00 51.39  ? 90  ASP   B CB  1 
ATOM   1245 C CG  . ASP   B 2 81  ? -18.162 -16.952 -23.836 1.00 53.46  ? 90  ASP   B CG  1 
ATOM   1246 O OD1 . ASP   B 2 81  ? -17.037 -16.403 -23.824 1.00 54.63  ? 90  ASP   B OD1 1 
ATOM   1247 O OD2 . ASP   B 2 81  ? -18.829 -17.142 -24.876 1.00 55.33  ? 90  ASP   B OD2 1 
ATOM   1248 N N   . GLY   B 2 82  ? -15.555 -16.699 -21.276 1.00 52.83  ? 91  GLY   B N   1 
ATOM   1249 C CA  . GLY   B 2 82  ? -14.130 -17.092 -21.329 1.00 52.90  ? 91  GLY   B CA  1 
ATOM   1250 C C   . GLY   B 2 82  ? -13.674 -17.468 -22.742 1.00 55.19  ? 91  GLY   B C   1 
ATOM   1251 O O   . GLY   B 2 82  ? -12.508 -17.897 -22.906 1.00 55.99  ? 91  GLY   B O   1 
ATOM   1252 N N   . LEU   B 2 83  ? -14.546 -17.310 -23.746 1.00 54.17  ? 92  LEU   B N   1 
ATOM   1253 C CA  . LEU   B 2 83  ? -14.303 -17.784 -25.148 1.00 56.34  ? 92  LEU   B CA  1 
ATOM   1254 C C   . LEU   B 2 83  ? -14.567 -16.681 -26.178 1.00 56.58  ? 92  LEU   B C   1 
ATOM   1255 O O   . LEU   B 2 83  ? -13.785 -16.573 -27.194 1.00 57.68  ? 92  LEU   B O   1 
ATOM   1256 C CB  . LEU   B 2 83  ? -15.248 -18.951 -25.436 1.00 58.42  ? 92  LEU   B CB  1 
ATOM   1257 C CG  . LEU   B 2 83  ? -14.745 -20.362 -25.149 1.00 61.45  ? 92  LEU   B CG  1 
ATOM   1258 C CD1 . LEU   B 2 83  ? -15.559 -21.358 -25.961 1.00 62.73  ? 92  LEU   B CD1 1 
ATOM   1259 C CD2 . LEU   B 2 83  ? -13.263 -20.543 -25.468 1.00 61.56  ? 92  LEU   B CD2 1 
ATOM   1260 N N   . SER   B 2 84  ? -15.724 -16.031 -26.089 1.00 54.58  ? 93  SER   B N   1 
ATOM   1261 C CA  . SER   B 2 84  ? -16.315 -15.268 -27.224 1.00 55.28  ? 93  SER   B CA  1 
ATOM   1262 C C   . SER   B 2 84  ? -15.810 -13.825 -27.178 1.00 53.71  ? 93  SER   B C   1 
ATOM   1263 O O   . SER   B 2 84  ? -15.435 -13.364 -26.077 1.00 53.53  ? 93  SER   B O   1 
ATOM   1264 C CB  . SER   B 2 84  ? -17.810 -15.346 -27.188 1.00 55.58  ? 93  SER   B CB  1 
ATOM   1265 O OG  . SER   B 2 84  ? -18.198 -16.648 -26.759 1.00 55.28  ? 93  SER   B OG  1 
ATOM   1266 N N   . GLU   B 2 85  ? -15.757 -13.139 -28.324 1.00 52.54  ? 94  GLU   B N   1 
ATOM   1267 C CA  . GLU   B 2 85  ? -15.449 -11.679 -28.302 1.00 50.16  ? 94  GLU   B CA  1 
ATOM   1268 C C   . GLU   B 2 85  ? -16.573 -11.072 -27.282 1.00 46.24  ? 94  GLU   B C   1 
ATOM   1269 O O   . GLU   B 2 85  ? -17.610 -11.817 -27.021 1.00 46.39  ? 94  GLU   B O   1 
ATOM   1270 C CB  . GLU   B 2 85  ? -15.221 -11.140 -29.754 1.00 51.55  ? 94  GLU   B CB  1 
ATOM   1271 C CG  . GLU   B 2 85  ? -13.765 -11.384 -30.270 1.00 51.83  ? 94  GLU   B CG  1 
ATOM   1272 C CD  . GLU   B 2 85  ? -13.365 -10.826 -31.661 1.00 55.82  ? 94  GLU   B CD  1 
ATOM   1273 O OE1 . GLU   B 2 85  ? -14.182 -10.130 -32.273 1.00 57.32  ? 94  GLU   B OE1 1 
ATOM   1274 O OE2 . GLU   B 2 85  ? -12.215 -11.095 -32.143 1.00 58.20  ? 94  GLU   B OE2 1 
ATOM   1275 N N   . VAL   B 2 86  ? -16.254 -9.735  -27.038 1.00 42.81  ? 95  VAL   B N   1 
ATOM   1276 C CA  . VAL   B 2 86  ? -17.234 -8.847  -26.339 1.00 40.87  ? 95  VAL   B CA  1 
ATOM   1277 C C   . VAL   B 2 86  ? -17.153 -7.483  -27.003 1.00 40.49  ? 95  VAL   B C   1 
ATOM   1278 O O   . VAL   B 2 86  ? -16.319 -7.295  -27.931 1.00 42.75  ? 95  VAL   B O   1 
ATOM   1279 C CB  . VAL   B 2 86  ? -16.911 -8.797  -24.824 1.00 38.86  ? 95  VAL   B CB  1 
ATOM   1280 C CG1 . VAL   B 2 86  ? -16.839 -10.192 -24.280 1.00 39.80  ? 95  VAL   B CG1 1 
ATOM   1281 C CG2 . VAL   B 2 86  ? -15.596 -8.086  -24.589 1.00 38.92  ? 95  VAL   B CG2 1 
ATOM   1282 N N   A GLN   B 2 87  ? -18.010 -6.547  -26.584 0.20 39.59  ? 96  GLN   B N   1 
ATOM   1283 N N   B GLN   B 2 87  ? -18.008 -6.546  -26.581 0.18 39.60  ? 96  GLN   B N   1 
ATOM   1284 N N   C GLN   B 2 87  ? -18.054 -6.562  -26.637 0.31 39.51  ? 96  GLN   B N   1 
ATOM   1285 N N   D GLN   B 2 87  ? -18.053 -6.562  -26.636 0.31 39.52  ? 96  GLN   B N   1 
ATOM   1286 C CA  A GLN   B 2 87  ? -17.988 -5.140  -27.064 0.20 39.71  ? 96  GLN   B CA  1 
ATOM   1287 C CA  B GLN   B 2 87  ? -17.987 -5.140  -27.062 0.18 39.71  ? 96  GLN   B CA  1 
ATOM   1288 C CA  C GLN   B 2 87  ? -18.015 -5.149  -27.098 0.31 39.75  ? 96  GLN   B CA  1 
ATOM   1289 C CA  D GLN   B 2 87  ? -18.015 -5.149  -27.098 0.31 39.75  ? 96  GLN   B CA  1 
ATOM   1290 C C   A GLN   B 2 87  ? -17.929 -4.168  -25.883 0.20 38.68  ? 96  GLN   B C   1 
ATOM   1291 C C   B GLN   B 2 87  ? -17.928 -4.169  -25.880 0.18 38.68  ? 96  GLN   B C   1 
ATOM   1292 C C   C GLN   B 2 87  ? -18.013 -4.172  -25.924 0.31 38.24  ? 96  GLN   B C   1 
ATOM   1293 C C   D GLN   B 2 87  ? -18.013 -4.172  -25.923 0.31 38.24  ? 96  GLN   B C   1 
ATOM   1294 O O   A GLN   B 2 87  ? -18.812 -4.274  -24.983 0.20 38.70  ? 96  GLN   B O   1 
ATOM   1295 O O   B GLN   B 2 87  ? -18.811 -4.276  -24.978 0.18 38.69  ? 96  GLN   B O   1 
ATOM   1296 O O   C GLN   B 2 87  ? -19.032 -4.162  -25.157 0.31 38.78  ? 96  GLN   B O   1 
ATOM   1297 O O   D GLN   B 2 87  ? -19.032 -4.161  -25.156 0.31 38.77  ? 96  GLN   B O   1 
ATOM   1298 C CB  A GLN   B 2 87  ? -19.192 -4.864  -27.980 0.20 39.71  ? 96  GLN   B CB  1 
ATOM   1299 C CB  B GLN   B 2 87  ? -19.192 -4.866  -27.977 0.18 39.72  ? 96  GLN   B CB  1 
ATOM   1300 C CB  C GLN   B 2 87  ? -19.215 -4.792  -27.992 0.31 39.87  ? 96  GLN   B CB  1 
ATOM   1301 C CB  D GLN   B 2 87  ? -19.216 -4.792  -27.991 0.31 39.87  ? 96  GLN   B CB  1 
ATOM   1302 C CG  A GLN   B 2 87  ? -19.078 -5.600  -29.313 0.20 40.72  ? 96  GLN   B CG  1 
ATOM   1303 C CG  B GLN   B 2 87  ? -19.075 -5.598  -29.311 0.18 40.72  ? 96  GLN   B CG  1 
ATOM   1304 C CG  C GLN   B 2 87  ? -19.129 -5.353  -29.409 0.31 41.27  ? 96  GLN   B CG  1 
ATOM   1305 C CG  D GLN   B 2 87  ? -19.130 -5.352  -29.408 0.31 41.27  ? 96  GLN   B CG  1 
ATOM   1306 C CD  A GLN   B 2 87  ? -20.318 -5.592  -30.250 0.20 40.96  ? 96  GLN   B CD  1 
ATOM   1307 C CD  B GLN   B 2 87  ? -20.310 -5.583  -30.248 0.18 40.98  ? 96  GLN   B CD  1 
ATOM   1308 C CD  C GLN   B 2 87  ? -20.292 -4.884  -30.370 0.31 41.51  ? 96  GLN   B CD  1 
ATOM   1309 C CD  D GLN   B 2 87  ? -20.293 -4.884  -30.369 0.31 41.51  ? 96  GLN   B CD  1 
ATOM   1310 O OE1 A GLN   B 2 87  ? -21.472 -5.188  -30.032 0.20 40.02  ? 96  GLN   B OE1 1 
ATOM   1311 O OE1 B GLN   B 2 87  ? -21.457 -5.171  -30.030 0.18 40.06  ? 96  GLN   B OE1 1 
ATOM   1312 O OE1 C GLN   B 2 87  ? -21.259 -4.128  -30.162 0.31 40.80  ? 96  GLN   B OE1 1 
ATOM   1313 O OE1 D GLN   B 2 87  ? -21.260 -4.131  -30.158 0.31 40.80  ? 96  GLN   B OE1 1 
ATOM   1314 N NE2 A GLN   B 2 87  ? -20.081 -6.052  -31.477 0.20 41.96  ? 96  GLN   B NE2 1 
ATOM   1315 N NE2 B GLN   B 2 87  ? -20.068 -6.034  -31.479 0.18 41.98  ? 96  GLN   B NE2 1 
ATOM   1316 N NE2 C GLN   B 2 87  ? -20.224 -5.306  -31.637 0.31 42.84  ? 96  GLN   B NE2 1 
ATOM   1317 N NE2 D GLN   B 2 87  ? -20.223 -5.305  -31.636 0.31 42.84  ? 96  GLN   B NE2 1 
ATOM   1318 N N   A LEU   B 2 88  ? -16.912 -3.275  -25.897 0.20 38.70  ? 97  LEU   B N   1 
ATOM   1319 N N   B LEU   B 2 88  ? -16.911 -3.277  -25.894 0.18 38.70  ? 97  LEU   B N   1 
ATOM   1320 N N   C LEU   B 2 88  ? -16.955 -3.338  -25.847 0.31 38.09  ? 97  LEU   B N   1 
ATOM   1321 N N   D LEU   B 2 88  ? -16.955 -3.338  -25.846 0.31 38.09  ? 97  LEU   B N   1 
ATOM   1322 C CA  A LEU   B 2 88  ? -16.866 -2.092  -24.999 0.20 38.02  ? 97  LEU   B CA  1 
ATOM   1323 C CA  B LEU   B 2 88  ? -16.866 -2.093  -24.996 0.18 38.02  ? 97  LEU   B CA  1 
ATOM   1324 C CA  C LEU   B 2 88  ? -16.962 -2.143  -24.968 0.31 37.14  ? 97  LEU   B CA  1 
ATOM   1325 C CA  D LEU   B 2 88  ? -16.962 -2.143  -24.967 0.31 37.13  ? 97  LEU   B CA  1 
ATOM   1326 C C   A LEU   B 2 88  ? -17.771 -1.032  -25.628 0.20 38.36  ? 97  LEU   B C   1 
ATOM   1327 C C   B LEU   B 2 88  ? -17.772 -1.034  -25.627 0.18 38.36  ? 97  LEU   B C   1 
ATOM   1328 C C   C LEU   B 2 88  ? -17.899 -1.142  -25.642 0.31 37.55  ? 97  LEU   B C   1 
ATOM   1329 C C   D LEU   B 2 88  ? -17.898 -1.142  -25.642 0.31 37.54  ? 97  LEU   B C   1 
ATOM   1330 O O   A LEU   B 2 88  ? -17.367 -0.401  -26.690 0.20 38.67  ? 97  LEU   B O   1 
ATOM   1331 O O   B LEU   B 2 88  ? -17.366 -0.403  -26.685 0.18 38.68  ? 97  LEU   B O   1 
ATOM   1332 O O   C LEU   B 2 88  ? -17.714 -0.828  -26.871 0.31 37.37  ? 97  LEU   B O   1 
ATOM   1333 O O   D LEU   B 2 88  ? -17.713 -0.828  -26.870 0.31 37.38  ? 97  LEU   B O   1 
ATOM   1334 C CB  A LEU   B 2 88  ? -15.427 -1.590  -24.819 0.20 38.18  ? 97  LEU   B CB  1 
ATOM   1335 C CB  B LEU   B 2 88  ? -15.427 -1.590  -24.819 0.18 38.18  ? 97  LEU   B CB  1 
ATOM   1336 C CB  C LEU   B 2 88  ? -15.545 -1.584  -24.770 0.31 37.09  ? 97  LEU   B CB  1 
ATOM   1337 C CB  D LEU   B 2 88  ? -15.544 -1.583  -24.771 0.31 37.09  ? 97  LEU   B CB  1 
ATOM   1338 C CG  A LEU   B 2 88  ? -15.277 -0.269  -24.068 0.20 37.74  ? 97  LEU   B CG  1 
ATOM   1339 C CG  B LEU   B 2 88  ? -15.277 -0.269  -24.066 0.18 37.73  ? 97  LEU   B CG  1 
ATOM   1340 C CG  C LEU   B 2 88  ? -15.451 -0.228  -24.072 0.31 36.57  ? 97  LEU   B CG  1 
ATOM   1341 C CG  D LEU   B 2 88  ? -15.451 -0.228  -24.072 0.31 36.57  ? 97  LEU   B CG  1 
ATOM   1342 C CD1 A LEU   B 2 88  ? -15.639 -0.442  -22.597 0.20 36.71  ? 97  LEU   B CD1 1 
ATOM   1343 C CD1 B LEU   B 2 88  ? -15.639 -0.443  -22.596 0.18 36.71  ? 97  LEU   B CD1 1 
ATOM   1344 C CD1 C LEU   B 2 88  ? -15.867 -0.366  -22.610 0.31 35.53  ? 97  LEU   B CD1 1 
ATOM   1345 C CD1 D LEU   B 2 88  ? -15.867 -0.366  -22.610 0.31 35.53  ? 97  LEU   B CD1 1 
ATOM   1346 C CD2 A LEU   B 2 88  ? -13.866 0.279   -24.201 0.20 38.12  ? 97  LEU   B CD2 1 
ATOM   1347 C CD2 B LEU   B 2 88  ? -13.866 0.279   -24.200 0.18 38.11  ? 97  LEU   B CD2 1 
ATOM   1348 C CD2 C LEU   B 2 88  ? -14.047 0.347   -24.170 0.31 36.89  ? 97  LEU   B CD2 1 
ATOM   1349 C CD2 D LEU   B 2 88  ? -14.046 0.347   -24.169 0.31 36.89  ? 97  LEU   B CD2 1 
ATOM   1350 N N   A LEU   B 2 89  ? -19.002 -0.937  -25.119 0.20 37.50  ? 98  LEU   B N   1 
ATOM   1351 N N   B LEU   B 2 89  ? -19.003 -0.938  -25.118 0.18 37.50  ? 98  LEU   B N   1 
ATOM   1352 N N   C LEU   B 2 89  ? -18.955 -0.740  -24.956 0.31 36.82  ? 98  LEU   B N   1 
ATOM   1353 N N   D LEU   B 2 89  ? -18.955 -0.740  -24.956 0.31 36.82  ? 98  LEU   B N   1 
ATOM   1354 C CA  A LEU   B 2 89  ? -19.886 0.215   -25.383 0.20 37.61  ? 98  LEU   B CA  1 
ATOM   1355 C CA  B LEU   B 2 89  ? -19.886 0.215   -25.380 0.18 37.62  ? 98  LEU   B CA  1 
ATOM   1356 C CA  C LEU   B 2 89  ? -19.760 0.411   -25.393 0.31 36.85  ? 98  LEU   B CA  1 
ATOM   1357 C CA  D LEU   B 2 89  ? -19.761 0.412   -25.392 0.31 36.85  ? 98  LEU   B CA  1 
ATOM   1358 C C   A LEU   B 2 89  ? -19.246 1.427   -24.707 0.20 37.51  ? 98  LEU   B C   1 
ATOM   1359 C C   B LEU   B 2 89  ? -19.245 1.426   -24.702 0.18 37.51  ? 98  LEU   B C   1 
ATOM   1360 C C   C LEU   B 2 89  ? -19.146 1.684   -24.799 0.31 36.86  ? 98  LEU   B C   1 
ATOM   1361 C C   D LEU   B 2 89  ? -19.147 1.684   -24.798 0.31 36.86  ? 98  LEU   B C   1 
ATOM   1362 O O   A LEU   B 2 89  ? -19.655 1.760   -23.595 0.20 36.73  ? 98  LEU   B O   1 
ATOM   1363 O O   B LEU   B 2 89  ? -19.653 1.757   -23.587 0.18 36.73  ? 98  LEU   B O   1 
ATOM   1364 O O   C LEU   B 2 89  ? -19.735 2.274   -23.808 0.31 36.57  ? 98  LEU   B O   1 
ATOM   1365 O O   D LEU   B 2 89  ? -19.736 2.274   -23.807 0.31 36.57  ? 98  LEU   B O   1 
ATOM   1366 C CB  A LEU   B 2 89  ? -21.299 -0.112  -24.889 0.20 37.53  ? 98  LEU   B CB  1 
ATOM   1367 C CB  B LEU   B 2 89  ? -21.300 -0.111  -24.886 0.18 37.54  ? 98  LEU   B CB  1 
ATOM   1368 C CB  C LEU   B 2 89  ? -21.222 0.186   -25.001 0.31 37.04  ? 98  LEU   B CB  1 
ATOM   1369 C CB  D LEU   B 2 89  ? -21.222 0.187   -25.000 0.31 37.04  ? 98  LEU   B CB  1 
ATOM   1370 C CG  A LEU   B 2 89  ? -22.318 1.030   -24.822 0.20 37.85  ? 98  LEU   B CG  1 
ATOM   1371 C CG  B LEU   B 2 89  ? -22.319 1.031   -24.820 0.18 37.85  ? 98  LEU   B CG  1 
ATOM   1372 C CG  C LEU   B 2 89  ? -22.199 1.288   -25.417 0.31 37.68  ? 98  LEU   B CG  1 
ATOM   1373 C CG  D LEU   B 2 89  ? -22.200 1.288   -25.417 0.31 37.68  ? 98  LEU   B CG  1 
ATOM   1374 C CD1 A LEU   B 2 89  ? -21.923 2.253   -25.641 0.20 38.28  ? 98  LEU   B CD1 1 
ATOM   1375 C CD1 B LEU   B 2 89  ? -21.923 2.253   -25.638 0.18 38.29  ? 98  LEU   B CD1 1 
ATOM   1376 C CD1 C LEU   B 2 89  ? -21.885 1.878   -26.793 0.31 39.08  ? 98  LEU   B CD1 1 
ATOM   1377 C CD1 D LEU   B 2 89  ? -21.885 1.878   -26.792 0.31 39.08  ? 98  LEU   B CD1 1 
ATOM   1378 C CD2 A LEU   B 2 89  ? -23.698 0.529   -25.224 0.20 38.37  ? 98  LEU   B CD2 1 
ATOM   1379 C CD2 B LEU   B 2 89  ? -23.698 0.530   -25.225 0.18 38.36  ? 98  LEU   B CD2 1 
ATOM   1380 C CD2 C LEU   B 2 89  ? -23.617 0.743   -25.382 0.31 38.15  ? 98  LEU   B CD2 1 
ATOM   1381 C CD2 D LEU   B 2 89  ? -23.617 0.744   -25.381 0.31 38.14  ? 98  LEU   B CD2 1 
ATOM   1382 N N   A ALA   B 2 90  ? -18.239 2.019   -25.357 0.20 38.06  ? 99  ALA   B N   1 
ATOM   1383 N N   B ALA   B 2 90  ? -18.240 2.020   -25.354 0.18 38.07  ? 99  ALA   B N   1 
ATOM   1384 N N   C ALA   B 2 90  ? -17.994 2.092   -25.356 0.31 37.34  ? 99  ALA   B N   1 
ATOM   1385 N N   D ALA   B 2 90  ? -17.994 2.092   -25.355 0.31 37.34  ? 99  ALA   B N   1 
ATOM   1386 C CA  A ALA   B 2 90  ? -17.461 3.174   -24.850 0.20 38.16  ? 99  ALA   B CA  1 
ATOM   1387 C CA  B ALA   B 2 90  ? -17.460 3.174   -24.848 0.18 38.16  ? 99  ALA   B CA  1 
ATOM   1388 C CA  C ALA   B 2 90  ? -17.235 3.289   -24.923 0.31 37.37  ? 99  ALA   B CA  1 
ATOM   1389 C CA  D ALA   B 2 90  ? -17.235 3.289   -24.922 0.31 37.37  ? 99  ALA   B CA  1 
ATOM   1390 C C   A ALA   B 2 90  ? -18.253 4.471   -25.041 0.20 38.84  ? 99  ALA   B C   1 
ATOM   1391 C C   B ALA   B 2 90  ? -18.251 4.471   -25.040 0.18 38.84  ? 99  ALA   B C   1 
ATOM   1392 C C   C ALA   B 2 90  ? -18.099 4.546   -25.093 0.31 38.43  ? 99  ALA   B C   1 
ATOM   1393 C C   D ALA   B 2 90  ? -18.099 4.545   -25.093 0.31 38.43  ? 99  ALA   B C   1 
ATOM   1394 O O   A ALA   B 2 90  ? -18.880 4.663   -26.139 0.20 39.57  ? 99  ALA   B O   1 
ATOM   1395 O O   B ALA   B 2 90  ? -18.875 4.663   -26.138 0.18 39.57  ? 99  ALA   B O   1 
ATOM   1396 O O   C ALA   B 2 90  ? -18.644 4.791   -26.230 0.31 38.89  ? 99  ALA   B O   1 
ATOM   1397 O O   D ALA   B 2 90  ? -18.643 4.791   -26.229 0.31 38.89  ? 99  ALA   B O   1 
ATOM   1398 C CB  A ALA   B 2 90  ? -16.113 3.250   -25.515 0.20 38.91  ? 99  ALA   B CB  1 
ATOM   1399 C CB  B ALA   B 2 90  ? -16.113 3.248   -25.514 0.18 38.91  ? 99  ALA   B CB  1 
ATOM   1400 C CB  C ALA   B 2 90  ? -15.924 3.389   -25.656 0.31 38.37  ? 99  ALA   B CB  1 
ATOM   1401 C CB  D ALA   B 2 90  ? -15.924 3.388   -25.655 0.31 38.37  ? 99  ALA   B CB  1 
ATOM   1402 N N   . VAL   B 2 91  ? -18.217 5.320   -24.004 1.00 38.61  ? 100 VAL   B N   1 
ATOM   1403 C CA  . VAL   B 2 91  ? -18.774 6.685   -24.025 1.00 39.20  ? 100 VAL   B CA  1 
ATOM   1404 C C   . VAL   B 2 91  ? -17.643 7.630   -23.618 1.00 40.58  ? 100 VAL   B C   1 
ATOM   1405 O O   . VAL   B 2 91  ? -17.496 7.954   -22.441 1.00 38.89  ? 100 VAL   B O   1 
ATOM   1406 C CB  . VAL   B 2 91  ? -19.936 6.757   -23.030 1.00 38.39  ? 100 VAL   B CB  1 
ATOM   1407 C CG1 . VAL   B 2 91  ? -20.590 8.127   -23.111 1.00 39.36  ? 100 VAL   B CG1 1 
ATOM   1408 C CG2 . VAL   B 2 91  ? -20.942 5.626   -23.268 1.00 38.15  ? 100 VAL   B CG2 1 
ATOM   1409 N N   . PRO   B 2 92  ? -16.780 8.089   -24.545 1.00 40.93  ? 101 PRO   B N   1 
ATOM   1410 C CA  . PRO   B 2 92  ? -15.665 8.984   -24.217 1.00 41.06  ? 101 PRO   B CA  1 
ATOM   1411 C C   . PRO   B 2 92  ? -16.138 10.423  -24.021 1.00 41.66  ? 101 PRO   B C   1 
ATOM   1412 O O   . PRO   B 2 92  ? -17.211 10.807  -24.522 1.00 42.47  ? 101 PRO   B O   1 
ATOM   1413 C CB  . PRO   B 2 92  ? -14.757 8.927   -25.474 1.00 42.23  ? 101 PRO   B CB  1 
ATOM   1414 C CG  . PRO   B 2 92  ? -15.259 7.723   -26.223 1.00 42.06  ? 101 PRO   B CG  1 
ATOM   1415 C CD  . PRO   B 2 92  ? -16.744 7.714   -25.972 1.00 41.94  ? 101 PRO   B CD  1 
ATOM   1416 N N   . PRO   B 2 93  ? -15.326 11.254  -23.327 1.00 42.73  ? 102 PRO   B N   1 
ATOM   1417 C CA  . PRO   B 2 93  ? -15.731 12.612  -23.011 1.00 44.36  ? 102 PRO   B CA  1 
ATOM   1418 C C   . PRO   B 2 93  ? -15.909 13.462  -24.273 1.00 45.30  ? 102 PRO   B C   1 
ATOM   1419 O O   . PRO   B 2 93  ? -14.981 13.476  -25.069 1.00 47.95  ? 102 PRO   B O   1 
ATOM   1420 C CB  . PRO   B 2 93  ? -14.611 13.142  -22.102 1.00 44.60  ? 102 PRO   B CB  1 
ATOM   1421 C CG  . PRO   B 2 93  ? -14.070 11.874  -21.426 1.00 43.86  ? 102 PRO   B CG  1 
ATOM   1422 C CD  . PRO   B 2 93  ? -14.142 10.837  -22.537 1.00 43.94  ? 102 PRO   B CD  1 
ATOM   1423 N N   . GLY   B 2 94  ? -17.084 14.069  -24.434 1.00 45.59  ? 103 GLY   B N   1 
ATOM   1424 C CA  . GLY   B 2 94  ? -17.437 14.925  -25.584 1.00 47.19  ? 103 GLY   B CA  1 
ATOM   1425 C C   . GLY   B 2 94  ? -17.591 14.187  -26.913 1.00 48.05  ? 103 GLY   B C   1 
ATOM   1426 O O   . GLY   B 2 94  ? -17.633 14.899  -27.917 1.00 48.40  ? 103 GLY   B O   1 
ATOM   1427 N N   . GLU   B 2 95  ? -17.737 12.861  -26.943 1.00 47.80  ? 104 GLU   B N   1 
ATOM   1428 C CA  . GLU   B 2 95  ? -17.799 12.017  -28.167 1.00 48.98  ? 104 GLU   B CA  1 
ATOM   1429 C C   . GLU   B 2 95  ? -18.975 11.039  -28.054 1.00 48.20  ? 104 GLU   B C   1 
ATOM   1430 O O   . GLU   B 2 95  ? -19.379 10.683  -26.922 1.00 44.08  ? 104 GLU   B O   1 
ATOM   1431 C CB  . GLU   B 2 95  ? -16.465 11.292  -28.427 1.00 51.02  ? 104 GLU   B CB  1 
ATOM   1432 C CG  . GLU   B 2 95  ? -15.210 12.186  -28.331 1.00 53.02  ? 104 GLU   B CG  1 
ATOM   1433 C CD  . GLU   B 2 95  ? -13.836 11.532  -28.531 1.00 53.76  ? 104 GLU   B CD  1 
ATOM   1434 O OE1 . GLU   B 2 95  ? -13.697 10.333  -28.197 1.00 54.58  ? 104 GLU   B OE1 1 
ATOM   1435 O OE2 . GLU   B 2 95  ? -12.880 12.239  -29.029 1.00 56.31  ? 104 GLU   B OE2 1 
ATOM   1436 N N   . ARG   B 2 96  ? -19.593 10.653  -29.165 1.00 48.64  ? 105 ARG   B N   1 
ATOM   1437 C CA  . ARG   B 2 96  ? -20.800 9.787   -29.130 1.00 50.42  ? 105 ARG   B CA  1 
ATOM   1438 C C   . ARG   B 2 96  ? -20.437 8.404   -28.569 1.00 48.84  ? 105 ARG   B C   1 
ATOM   1439 O O   . ARG   B 2 96  ? -19.247 7.953   -28.725 1.00 47.69  ? 105 ARG   B O   1 
ATOM   1440 C CB  . ARG   B 2 96  ? -21.379 9.665   -30.540 1.00 55.76  ? 105 ARG   B CB  1 
ATOM   1441 C CG  . ARG   B 2 96  ? -22.774 9.057   -30.586 1.00 58.42  ? 105 ARG   B CG  1 
ATOM   1442 C CD  . ARG   B 2 96  ? -23.539 9.567   -31.800 1.00 63.47  ? 105 ARG   B CD  1 
ATOM   1443 N NE  . ARG   B 2 96  ? -22.730 9.604   -33.014 1.00 67.11  ? 105 ARG   B NE  1 
ATOM   1444 C CZ  . ARG   B 2 96  ? -22.210 10.696  -33.596 1.00 72.17  ? 105 ARG   B CZ  1 
ATOM   1445 N NH1 . ARG   B 2 96  ? -22.402 11.912  -33.106 1.00 73.61  ? 105 ARG   B NH1 1 
ATOM   1446 N NH2 . ARG   B 2 96  ? -21.510 10.565  -34.712 1.00 76.85  ? 105 ARG   B NH2 1 
ATOM   1447 N N   . ALA   B 2 97  ? -21.424 7.732   -27.960 1.00 46.76  ? 106 ALA   B N   1 
ATOM   1448 C CA  . ALA   B 2 97  ? -21.321 6.301   -27.600 1.00 46.32  ? 106 ALA   B CA  1 
ATOM   1449 C C   . ALA   B 2 97  ? -20.873 5.521   -28.840 1.00 46.47  ? 106 ALA   B C   1 
ATOM   1450 O O   . ALA   B 2 97  ? -21.540 5.690   -29.917 1.00 45.15  ? 106 ALA   B O   1 
ATOM   1451 C CB  . ALA   B 2 97  ? -22.636 5.777   -27.082 1.00 46.46  ? 106 ALA   B CB  1 
ATOM   1452 N N   . LYS   B 2 98  ? -19.836 4.692   -28.714 1.00 45.43  ? 107 LYS   B N   1 
ATOM   1453 C CA  . LYS   B 2 98  ? -19.270 3.928   -29.879 1.00 49.30  ? 107 LYS   B CA  1 
ATOM   1454 C C   . LYS   B 2 98  ? -18.940 2.498   -29.384 1.00 47.51  ? 107 LYS   B C   1 
ATOM   1455 O O   . LYS   B 2 98  ? -18.347 2.365   -28.255 1.00 45.33  ? 107 LYS   B O   1 
ATOM   1456 C CB  . LYS   B 2 98  ? -18.028 4.672   -30.397 1.00 53.18  ? 107 LYS   B CB  1 
ATOM   1457 C CG  . LYS   B 2 98  ? -17.345 4.068   -31.624 1.00 57.66  ? 107 LYS   B CG  1 
ATOM   1458 C CD  . LYS   B 2 98  ? -15.880 4.528   -31.809 1.00 61.88  ? 107 LYS   B CD  1 
ATOM   1459 C CE  . LYS   B 2 98  ? -15.188 4.802   -30.481 1.00 62.31  ? 107 LYS   B CE  1 
ATOM   1460 N NZ  . LYS   B 2 98  ? -13.714 4.833   -30.604 1.00 65.81  ? 107 LYS   B NZ  1 
ATOM   1461 N N   . ASN   B 2 99  ? -19.420 1.441   -30.059 1.00 45.77  ? 108 ASN   B N   1 
ATOM   1462 C CA  . ASN   B 2 99  ? -19.141 0.017   -29.694 1.00 45.02  ? 108 ASN   B CA  1 
ATOM   1463 C C   . ASN   B 2 99  ? -17.795 -0.414  -30.285 1.00 45.40  ? 108 ASN   B C   1 
ATOM   1464 O O   . ASN   B 2 99  ? -17.525 -0.110  -31.395 1.00 44.62  ? 108 ASN   B O   1 
ATOM   1465 C CB  . ASN   B 2 99  ? -20.210 -0.976  -30.144 1.00 45.89  ? 108 ASN   B CB  1 
ATOM   1466 C CG  . ASN   B 2 99  ? -21.579 -0.739  -29.598 1.00 48.03  ? 108 ASN   B CG  1 
ATOM   1467 O OD1 . ASN   B 2 99  ? -22.102 0.420   -29.633 1.00 51.03  ? 108 ASN   B OD1 1 
ATOM   1468 N ND2 . ASN   B 2 99  ? -22.164 -1.815  -28.986 1.00 47.68  ? 108 ASN   B ND2 1 
ATOM   1469 N N   . ILE   B 2 100 ? -17.002 -1.147  -29.531 1.00 44.38  ? 109 ILE   B N   1 
ATOM   1470 C CA  . ILE   B 2 100 ? -15.626 -1.558  -29.907 1.00 44.62  ? 109 ILE   B CA  1 
ATOM   1471 C C   . ILE   B 2 100 ? -15.529 -3.021  -29.561 1.00 44.87  ? 109 ILE   B C   1 
ATOM   1472 O O   . ILE   B 2 100 ? -15.694 -3.351  -28.297 1.00 44.43  ? 109 ILE   B O   1 
ATOM   1473 C CB  . ILE   B 2 100 ? -14.534 -0.697  -29.266 1.00 45.57  ? 109 ILE   B CB  1 
ATOM   1474 C CG1 . ILE   B 2 100 ? -14.792 0.804   -29.383 1.00 47.15  ? 109 ILE   B CG1 1 
ATOM   1475 C CG2 . ILE   B 2 100 ? -13.180 -1.082  -29.819 1.00 46.48  ? 109 ILE   B CG2 1 
ATOM   1476 C CD1 . ILE   B 2 100 ? -14.433 1.388   -30.749 1.00 48.29  ? 109 ILE   B CD1 1 
ATOM   1477 N N   . GLN   B 2 101 ? -15.277 -3.877  -30.546 1.00 47.38  ? 110 GLN   B N   1 
ATOM   1478 C CA  . GLN   B 2 101 ? -15.376 -5.338  -30.372 1.00 48.55  ? 110 GLN   B CA  1 
ATOM   1479 C C   . GLN   B 2 101 ? -13.957 -5.868  -30.181 1.00 48.92  ? 110 GLN   B C   1 
ATOM   1480 O O   . GLN   B 2 101 ? -13.051 -5.334  -30.867 1.00 49.40  ? 110 GLN   B O   1 
ATOM   1481 C CB  . GLN   B 2 101 ? -16.125 -5.991  -31.518 1.00 50.15  ? 110 GLN   B CB  1 
ATOM   1482 C CG  . GLN   B 2 101 ? -16.264 -7.494  -31.339 1.00 50.60  ? 110 GLN   B CG  1 
ATOM   1483 C CD  . GLN   B 2 101 ? -17.149 -8.024  -32.448 1.00 49.87  ? 110 GLN   B CD  1 
ATOM   1484 O OE1 . GLN   B 2 101 ? -18.277 -7.455  -32.712 1.00 51.66  ? 110 GLN   B OE1 1 
ATOM   1485 N NE2 . GLN   B 2 101 ? -16.628 -9.121  -33.086 1.00 50.46  ? 110 GLN   B NE2 1 
ATOM   1486 N N   . THR   B 2 102 ? -13.754 -6.780  -29.196 1.00 47.43  ? 111 THR   B N   1 
ATOM   1487 C CA  . THR   B 2 102 ? -12.420 -7.230  -28.719 1.00 48.07  ? 111 THR   B CA  1 
ATOM   1488 C C   . THR   B 2 102 ? -12.567 -8.604  -27.959 1.00 45.31  ? 111 THR   B C   1 
ATOM   1489 O O   . THR   B 2 102 ? -13.717 -8.987  -27.623 1.00 49.93  ? 111 THR   B O   1 
ATOM   1490 C CB  . THR   B 2 102 ? -11.729 -6.151  -27.866 1.00 46.69  ? 111 THR   B CB  1 
ATOM   1491 O OG1 . THR   B 2 102 ? -10.271 -6.367  -27.725 1.00 49.18  ? 111 THR   B OG1 1 
ATOM   1492 C CG2 . THR   B 2 102 ? -12.224 -6.081  -26.432 1.00 45.13  ? 111 THR   B CG2 1 
ATOM   1493 N N   . LEU   B 2 103 ? -11.562 -9.470  -28.226 1.00 45.05  ? 112 LEU   B N   1 
ATOM   1494 C CA  . LEU   B 2 103 ? -11.461 -10.757 -27.491 1.00 46.21  ? 112 LEU   B CA  1 
ATOM   1495 C C   . LEU   B 2 103 ? -10.710 -10.460 -26.202 1.00 43.84  ? 112 LEU   B C   1 
ATOM   1496 O O   . LEU   B 2 103 ? -9.517  -10.075 -26.234 1.00 44.55  ? 112 LEU   B O   1 
ATOM   1497 C CB  . LEU   B 2 103 ? -10.734 -11.854 -28.282 1.00 46.35  ? 112 LEU   B CB  1 
ATOM   1498 C CG  . LEU   B 2 103 ? -10.606 -13.152 -27.471 1.00 46.30  ? 112 LEU   B CG  1 
ATOM   1499 C CD1 . LEU   B 2 103 ? -11.906 -13.936 -27.546 1.00 47.25  ? 112 LEU   B CD1 1 
ATOM   1500 C CD2 . LEU   B 2 103 ? -9.451  -14.028 -27.915 1.00 48.38  ? 112 LEU   B CD2 1 
ATOM   1501 N N   . PRO   B 2 104 ? -11.361 -10.546 -25.001 1.00 43.14  ? 113 PRO   B N   1 
ATOM   1502 C CA  . PRO   B 2 104 ? -10.653 -10.217 -23.792 1.00 42.86  ? 113 PRO   B CA  1 
ATOM   1503 C C   . PRO   B 2 104 ? -9.467  -11.157 -23.545 1.00 44.26  ? 113 PRO   B C   1 
ATOM   1504 O O   . PRO   B 2 104 ? -9.535  -12.366 -23.879 1.00 45.14  ? 113 PRO   B O   1 
ATOM   1505 C CB  . PRO   B 2 104 ? -11.700 -10.387 -22.667 1.00 41.72  ? 113 PRO   B CB  1 
ATOM   1506 C CG  . PRO   B 2 104 ? -13.054 -10.495 -23.387 1.00 40.17  ? 113 PRO   B CG  1 
ATOM   1507 C CD  . PRO   B 2 104 ? -12.731 -11.039 -24.788 1.00 41.54  ? 113 PRO   B CD  1 
ATOM   1508 N N   . GLY   B 2 105 ? -8.420  -10.566 -22.914 1.00 43.91  ? 114 GLY   B N   1 
ATOM   1509 C CA  . GLY   B 2 105 ? -7.356  -11.347 -22.266 1.00 43.76  ? 114 GLY   B CA  1 
ATOM   1510 C C   . GLY   B 2 105 ? -7.792  -11.716 -20.851 1.00 43.80  ? 114 GLY   B C   1 
ATOM   1511 O O   . GLY   B 2 105 ? -9.026  -11.751 -20.600 1.00 42.32  ? 114 GLY   B O   1 
ATOM   1512 N N   . ILE   B 2 106 ? -6.798  -12.050 -20.040 1.00 44.97  ? 115 ILE   B N   1 
ATOM   1513 C CA  . ILE   B 2 106 ? -6.970  -12.606 -18.662 1.00 46.37  ? 115 ILE   B CA  1 
ATOM   1514 C C   . ILE   B 2 106 ? -6.095  -11.820 -17.698 1.00 45.68  ? 115 ILE   B C   1 
ATOM   1515 O O   . ILE   B 2 106 ? -4.918  -11.647 -17.951 1.00 46.54  ? 115 ILE   B O   1 
ATOM   1516 C CB  . ILE   B 2 106 ? -6.591  -14.094 -18.649 1.00 48.54  ? 115 ILE   B CB  1 
ATOM   1517 C CG1 . ILE   B 2 106 ? -7.378  -14.920 -19.665 1.00 51.07  ? 115 ILE   B CG1 1 
ATOM   1518 C CG2 . ILE   B 2 106 ? -6.734  -14.673 -17.254 1.00 49.18  ? 115 ILE   B CG2 1 
ATOM   1519 C CD1 . ILE   B 2 106 ? -8.857  -15.004 -19.403 1.00 51.22  ? 115 ILE   B CD1 1 
ATOM   1520 N N   . PHE   B 2 107 ? -6.667  -11.428 -16.561 1.00 44.09  ? 116 PHE   B N   1 
ATOM   1521 C CA  . PHE   B 2 107 ? -5.927  -11.120 -15.317 1.00 44.40  ? 116 PHE   B CA  1 
ATOM   1522 C C   . PHE   B 2 107 ? -5.888  -12.420 -14.514 1.00 45.14  ? 116 PHE   B C   1 
ATOM   1523 O O   . PHE   B 2 107 ? -6.978  -13.012 -14.280 1.00 45.83  ? 116 PHE   B O   1 
ATOM   1524 C CB  . PHE   B 2 107 ? -6.669  -10.028 -14.559 1.00 42.65  ? 116 PHE   B CB  1 
ATOM   1525 C CG  . PHE   B 2 107 ? -6.417  -8.597  -14.951 1.00 42.71  ? 116 PHE   B CG  1 
ATOM   1526 C CD1 . PHE   B 2 107 ? -5.736  -8.258  -16.098 1.00 42.37  ? 116 PHE   B CD1 1 
ATOM   1527 C CD2 . PHE   B 2 107 ? -6.924  -7.564  -14.162 1.00 40.89  ? 116 PHE   B CD2 1 
ATOM   1528 C CE1 . PHE   B 2 107 ? -5.531  -6.936  -16.442 1.00 42.31  ? 116 PHE   B CE1 1 
ATOM   1529 C CE2 . PHE   B 2 107 ? -6.691  -6.236  -14.490 1.00 41.40  ? 116 PHE   B CE2 1 
ATOM   1530 C CZ  . PHE   B 2 107 ? -6.067  -5.927  -15.694 1.00 42.81  ? 116 PHE   B CZ  1 
ATOM   1531 N N   . LYS   B 2 108 ? -4.671  -12.888 -14.214 1.00 46.40  ? 117 LYS   B N   1 
ATOM   1532 C CA  . LYS   B 2 108 ? -4.362  -14.051 -13.349 1.00 48.76  ? 117 LYS   B CA  1 
ATOM   1533 C C   . LYS   B 2 108 ? -4.109  -13.484 -11.949 1.00 46.53  ? 117 LYS   B C   1 
ATOM   1534 O O   . LYS   B 2 108 ? -3.207  -12.590 -11.823 1.00 44.50  ? 117 LYS   B O   1 
ATOM   1535 C CB  . LYS   B 2 108 ? -3.148  -14.826 -13.870 1.00 52.94  ? 117 LYS   B CB  1 
ATOM   1536 C CG  . LYS   B 2 108 ? -3.487  -16.040 -14.724 1.00 60.31  ? 117 LYS   B CG  1 
ATOM   1537 C CD  . LYS   B 2 108 ? -2.553  -16.274 -15.916 1.00 66.31  ? 117 LYS   B CD  1 
ATOM   1538 C CE  . LYS   B 2 108 ? -3.194  -17.068 -17.039 1.00 71.98  ? 117 LYS   B CE  1 
ATOM   1539 N NZ  . LYS   B 2 108 ? -2.279  -17.296 -18.197 1.00 76.95  ? 117 LYS   B NZ  1 
ATOM   1540 N N   . THR   B 2 109 ? -4.930  -13.906 -10.983 1.00 47.06  ? 118 THR   B N   1 
ATOM   1541 C CA  . THR   B 2 109 ? -4.827  -13.488 -9.559  1.00 47.64  ? 118 THR   B CA  1 
ATOM   1542 C C   . THR   B 2 109 ? -4.863  -14.705 -8.630  1.00 48.76  ? 118 THR   B C   1 
ATOM   1543 O O   . THR   B 2 109 ? -5.562  -15.698 -8.925  1.00 48.12  ? 118 THR   B O   1 
ATOM   1544 C CB  . THR   B 2 109 ? -5.959  -12.550 -9.106  1.00 46.24  ? 118 THR   B CB  1 
ATOM   1545 O OG1 . THR   B 2 109 ? -7.118  -13.287 -8.690  1.00 45.34  ? 118 THR   B OG1 1 
ATOM   1546 C CG2 . THR   B 2 109 ? -6.323  -11.534 -10.158 1.00 46.32  ? 118 THR   B CG2 1 
ATOM   1547 N N   . LYS   B 2 110 ? -4.238  -14.561 -7.470  1.00 50.54  ? 119 LYS   B N   1 
ATOM   1548 C CA  . LYS   B 2 110 ? -4.237  -15.587 -6.392  1.00 51.35  ? 119 LYS   B CA  1 
ATOM   1549 C C   . LYS   B 2 110 ? -5.664  -16.102 -6.121  1.00 52.88  ? 119 LYS   B C   1 
ATOM   1550 O O   . LYS   B 2 110 ? -5.774  -17.237 -5.613  1.00 55.80  ? 119 LYS   B O   1 
ATOM   1551 C CB  . LYS   B 2 110 ? -3.600  -15.010 -5.121  1.00 51.77  ? 119 LYS   B CB  1 
ATOM   1552 C CG  . LYS   B 2 110 ? -4.230  -13.740 -4.562  1.00 51.24  ? 119 LYS   B CG  1 
ATOM   1553 C CD  . LYS   B 2 110 ? -3.662  -13.344 -3.191  1.00 54.27  ? 119 LYS   B CD  1 
ATOM   1554 C CE  . LYS   B 2 110 ? -4.649  -13.620 -2.088  1.00 55.53  ? 119 LYS   B CE  1 
ATOM   1555 N NZ  . LYS   B 2 110 ? -5.771  -12.650 -2.098  1.00 56.06  ? 119 LYS   B NZ  1 
ATOM   1556 N N   . ASP   B 2 111 ? -6.707  -15.300 -6.389  1.00 51.79  ? 120 ASP   B N   1 
ATOM   1557 C CA  . ASP   B 2 111 ? -8.128  -15.635 -6.087  1.00 52.99  ? 120 ASP   B CA  1 
ATOM   1558 C C   . ASP   B 2 111 ? -8.894  -15.991 -7.355  1.00 53.15  ? 120 ASP   B C   1 
ATOM   1559 O O   . ASP   B 2 111 ? -10.127 -16.150 -7.279  1.00 55.23  ? 120 ASP   B O   1 
ATOM   1560 C CB  . ASP   B 2 111 ? -8.833  -14.483 -5.368  1.00 53.32  ? 120 ASP   B CB  1 
ATOM   1561 C CG  . ASP   B 2 111 ? -8.234  -14.225 -3.998  1.00 55.17  ? 120 ASP   B CG  1 
ATOM   1562 O OD1 . ASP   B 2 111 ? -7.888  -15.203 -3.323  1.00 57.71  ? 120 ASP   B OD1 1 
ATOM   1563 O OD2 . ASP   B 2 111 ? -8.085  -13.050 -3.641  1.00 57.13  ? 120 ASP   B OD2 1 
ATOM   1564 N N   . GLY   B 2 112 ? -8.215  -16.100 -8.491  1.00 52.07  ? 121 GLY   B N   1 
ATOM   1565 C CA  . GLY   B 2 112 ? -8.897  -16.495 -9.730  1.00 53.34  ? 121 GLY   B CA  1 
ATOM   1566 C C   . GLY   B 2 112 ? -8.544  -15.610 -10.902 1.00 51.89  ? 121 GLY   B C   1 
ATOM   1567 O O   . GLY   B 2 112 ? -7.903  -14.569 -10.713 1.00 51.33  ? 121 GLY   B O   1 
ATOM   1568 N N   . ASP   B 2 113 ? -8.959  -16.067 -12.080 1.00 52.86  ? 122 ASP   B N   1 
ATOM   1569 C CA  . ASP   B 2 113 ? -8.777  -15.423 -13.406 1.00 51.62  ? 122 ASP   B CA  1 
ATOM   1570 C C   . ASP   B 2 113 ? -9.958  -14.482 -13.660 1.00 49.32  ? 122 ASP   B C   1 
ATOM   1571 O O   . ASP   B 2 113 ? -11.116 -14.867 -13.339 1.00 47.89  ? 122 ASP   B O   1 
ATOM   1572 C CB  . ASP   B 2 113 ? -8.721  -16.477 -14.502 1.00 54.76  ? 122 ASP   B CB  1 
ATOM   1573 C CG  . ASP   B 2 113 ? -7.429  -17.269 -14.602 1.00 56.64  ? 122 ASP   B CG  1 
ATOM   1574 O OD1 . ASP   B 2 113 ? -6.517  -17.046 -13.768 1.00 57.82  ? 122 ASP   B OD1 1 
ATOM   1575 O OD2 . ASP   B 2 113 ? -7.361  -18.121 -15.531 1.00 59.35  ? 122 ASP   B OD2 1 
ATOM   1576 N N   . ILE   B 2 114 ? -9.669  -13.290 -14.179 1.00 46.25  ? 123 ILE   B N   1 
ATOM   1577 C CA  . ILE   B 2 114 ? -10.724 -12.307 -14.541 1.00 47.02  ? 123 ILE   B CA  1 
ATOM   1578 C C   . ILE   B 2 114 ? -10.516 -11.947 -16.026 1.00 44.61  ? 123 ILE   B C   1 
ATOM   1579 O O   . ILE   B 2 114 ? -9.357  -11.721 -16.390 1.00 44.05  ? 123 ILE   B O   1 
ATOM   1580 C CB  . ILE   B 2 114 ? -10.653 -11.065 -13.620 1.00 46.58  ? 123 ILE   B CB  1 
ATOM   1581 C CG1 . ILE   B 2 114 ? -10.201 -11.353 -12.194 1.00 50.06  ? 123 ILE   B CG1 1 
ATOM   1582 C CG2 . ILE   B 2 114 ? -11.977 -10.330 -13.634 1.00 48.82  ? 123 ILE   B CG2 1 
ATOM   1583 C CD1 . ILE   B 2 114 ? -9.854  -10.086 -11.413 1.00 49.01  ? 123 ILE   B CD1 1 
ATOM   1584 N N   . GLY   B 2 115 ? -11.577 -11.818 -16.833 1.00 45.06  ? 124 GLY   B N   1 
ATOM   1585 C CA  . GLY   B 2 115 ? -11.464 -11.239 -18.188 1.00 42.06  ? 124 GLY   B CA  1 
ATOM   1586 C C   . GLY   B 2 115 ? -10.876 -9.833  -18.122 1.00 41.51  ? 124 GLY   B C   1 
ATOM   1587 O O   . GLY   B 2 115 ? -11.100 -9.116  -17.085 1.00 38.84  ? 124 GLY   B O   1 
ATOM   1588 N N   . ALA   B 2 116 ? -10.150 -9.398  -19.146 1.00 39.76  ? 125 ALA   B N   1 
ATOM   1589 C CA  . ALA   B 2 116 ? -9.504  -8.066  -19.219 1.00 40.46  ? 125 ALA   B CA  1 
ATOM   1590 C C   . ALA   B 2 116 ? -9.607  -7.577  -20.653 1.00 42.50  ? 125 ALA   B C   1 
ATOM   1591 O O   . ALA   B 2 116 ? -9.468  -8.414  -21.544 1.00 43.79  ? 125 ALA   B O   1 
ATOM   1592 C CB  . ALA   B 2 116 ? -8.043  -8.137  -18.879 1.00 41.09  ? 125 ALA   B CB  1 
ATOM   1593 N N   A VAL   B 2 117 ? -9.822  -6.274  -20.858 0.20 42.43  ? 126 VAL   B N   1 
ATOM   1594 N N   B VAL   B 2 117 ? -9.774  -6.263  -20.852 0.18 42.47  ? 126 VAL   B N   1 
ATOM   1595 N N   C VAL   B 2 117 ? -9.825  -6.275  -20.854 0.31 42.38  ? 126 VAL   B N   1 
ATOM   1596 N N   D VAL   B 2 117 ? -9.825  -6.274  -20.855 0.31 42.38  ? 126 VAL   B N   1 
ATOM   1597 C CA  A VAL   B 2 117 ? -9.926  -5.674  -22.224 0.20 43.20  ? 126 VAL   B CA  1 
ATOM   1598 C CA  B VAL   B 2 117 ? -9.964  -5.610  -22.188 0.18 43.19  ? 126 VAL   B CA  1 
ATOM   1599 C CA  C VAL   B 2 117 ? -9.927  -5.672  -22.221 0.31 43.12  ? 126 VAL   B CA  1 
ATOM   1600 C CA  D VAL   B 2 117 ? -9.927  -5.672  -22.221 0.31 43.12  ? 126 VAL   B CA  1 
ATOM   1601 C C   A VAL   B 2 117 ? -8.809  -4.643  -22.435 0.20 44.14  ? 126 VAL   B C   1 
ATOM   1602 C C   B VAL   B 2 117 ? -8.830  -4.604  -22.446 0.18 44.12  ? 126 VAL   B C   1 
ATOM   1603 C C   C VAL   B 2 117 ? -8.809  -4.643  -22.434 0.31 44.16  ? 126 VAL   B C   1 
ATOM   1604 C C   D VAL   B 2 117 ? -8.809  -4.643  -22.434 0.31 44.16  ? 126 VAL   B C   1 
ATOM   1605 O O   A VAL   B 2 117 ? -8.612  -3.782  -21.568 0.20 43.95  ? 126 VAL   B O   1 
ATOM   1606 O O   B VAL   B 2 117 ? -8.668  -3.685  -21.629 0.18 43.87  ? 126 VAL   B O   1 
ATOM   1607 O O   C VAL   B 2 117 ? -8.613  -3.781  -21.574 0.31 43.99  ? 126 VAL   B O   1 
ATOM   1608 O O   D VAL   B 2 117 ? -8.614  -3.781  -21.574 0.31 43.99  ? 126 VAL   B O   1 
ATOM   1609 C CB  A VAL   B 2 117 ? -11.324 -5.092  -22.499 0.20 43.09  ? 126 VAL   B CB  1 
ATOM   1610 C CB  B VAL   B 2 117 ? -11.353 -4.949  -22.265 0.18 43.07  ? 126 VAL   B CB  1 
ATOM   1611 C CB  C VAL   B 2 117 ? -11.323 -5.091  -22.498 0.31 43.05  ? 126 VAL   B CB  1 
ATOM   1612 C CB  D VAL   B 2 117 ? -11.323 -5.091  -22.498 0.31 43.05  ? 126 VAL   B CB  1 
ATOM   1613 C CG1 A VAL   B 2 117 ? -12.363 -6.201  -22.561 0.20 42.97  ? 126 VAL   B CG1 1 
ATOM   1614 C CG1 B VAL   B 2 117 ? -11.509 -4.021  -23.458 0.18 43.62  ? 126 VAL   B CG1 1 
ATOM   1615 C CG1 C VAL   B 2 117 ? -12.358 -6.204  -22.572 0.31 42.90  ? 126 VAL   B CG1 1 
ATOM   1616 C CG1 D VAL   B 2 117 ? -12.359 -6.204  -22.571 0.31 42.90  ? 126 VAL   B CG1 1 
ATOM   1617 C CG2 A VAL   B 2 117 ? -11.723 -4.018  -21.498 0.20 42.74  ? 126 VAL   B CG2 1 
ATOM   1618 C CG2 B VAL   B 2 117 ? -12.457 -5.994  -22.263 0.18 43.21  ? 126 VAL   B CG2 1 
ATOM   1619 C CG2 C VAL   B 2 117 ? -11.727 -4.020  -21.492 0.31 42.77  ? 126 VAL   B CG2 1 
ATOM   1620 C CG2 D VAL   B 2 117 ? -11.727 -4.020  -21.492 0.31 42.77  ? 126 VAL   B CG2 1 
ATOM   1621 N N   . ALA   B 2 118 ? -8.104  -4.741  -23.568 1.00 44.87  ? 127 ALA   B N   1 
ATOM   1622 C CA  . ALA   B 2 118 ? -6.901  -3.907  -23.877 1.00 46.40  ? 127 ALA   B CA  1 
ATOM   1623 C C   . ALA   B 2 118 ? -7.253  -2.774  -24.844 1.00 48.85  ? 127 ALA   B C   1 
ATOM   1624 O O   . ALA   B 2 118 ? -6.866  -2.812  -26.017 1.00 48.19  ? 127 ALA   B O   1 
ATOM   1625 C CB  . ALA   B 2 118 ? -5.778  -4.759  -24.440 1.00 46.58  ? 127 ALA   B CB  1 
ATOM   1626 N N   . LEU   B 2 119 ? -8.014  -1.801  -24.374 1.00 49.32  ? 128 LEU   B N   1 
ATOM   1627 C CA  . LEU   B 2 119 ? -8.497  -0.660  -25.161 1.00 50.74  ? 128 LEU   B CA  1 
ATOM   1628 C C   . LEU   B 2 119 ? -8.147  0.587   -24.361 1.00 54.32  ? 128 LEU   B C   1 
ATOM   1629 O O   . LEU   B 2 119 ? -8.325  0.561   -23.094 1.00 56.56  ? 128 LEU   B O   1 
ATOM   1630 C CB  . LEU   B 2 119 ? -9.990  -0.867  -25.394 1.00 51.11  ? 128 LEU   B CB  1 
ATOM   1631 C CG  . LEU   B 2 119 ? -10.368 -2.150  -26.141 1.00 51.11  ? 128 LEU   B CG  1 
ATOM   1632 C CD1 . LEU   B 2 119 ? -11.874 -2.357  -26.196 1.00 50.75  ? 128 LEU   B CD1 1 
ATOM   1633 C CD2 . LEU   B 2 119 ? -9.852  -2.108  -27.576 1.00 53.74  ? 128 LEU   B CD2 1 
ATOM   1634 N N   . ASP   B 2 120 ? -7.534  1.552   -25.023 1.00 60.96  ? 129 ASP   B N   1 
ATOM   1635 C CA  . ASP   B 2 120 ? -6.942  2.755   -24.395 1.00 62.17  ? 129 ASP   B CA  1 
ATOM   1636 C C   . ASP   B 2 120 ? -7.924  3.904   -24.639 1.00 59.95  ? 129 ASP   B C   1 
ATOM   1637 O O   . ASP   B 2 120 ? -8.088  4.298   -25.789 1.00 60.90  ? 129 ASP   B O   1 
ATOM   1638 C CB  . ASP   B 2 120 ? -5.547  3.026   -24.976 1.00 66.99  ? 129 ASP   B CB  1 
ATOM   1639 C CG  . ASP   B 2 120 ? -4.547  3.583   -23.968 1.00 69.05  ? 129 ASP   B CG  1 
ATOM   1640 O OD1 . ASP   B 2 120 ? -4.858  3.566   -22.750 1.00 68.01  ? 129 ASP   B OD1 1 
ATOM   1641 O OD2 . ASP   B 2 120 ? -3.457  4.028   -24.404 1.00 74.14  ? 129 ASP   B OD2 1 
ATOM   1642 N N   . TYR   B 2 121 ? -8.584  4.377   -23.591 1.00 55.25  ? 130 TYR   B N   1 
ATOM   1643 C CA  . TYR   B 2 121 ? -9.557  5.488   -23.627 1.00 53.50  ? 130 TYR   B CA  1 
ATOM   1644 C C   . TYR   B 2 121 ? -9.278  6.403   -22.450 1.00 51.16  ? 130 TYR   B C   1 
ATOM   1645 O O   . TYR   B 2 121 ? -8.639  5.988   -21.484 1.00 48.70  ? 130 TYR   B O   1 
ATOM   1646 C CB  . TYR   B 2 121 ? -10.995 4.972   -23.578 1.00 55.58  ? 130 TYR   B CB  1 
ATOM   1647 C CG  . TYR   B 2 121 ? -11.533 4.454   -24.884 1.00 57.50  ? 130 TYR   B CG  1 
ATOM   1648 C CD1 . TYR   B 2 121 ? -11.968 5.323   -25.879 1.00 59.26  ? 130 TYR   B CD1 1 
ATOM   1649 C CD2 . TYR   B 2 121 ? -11.637 3.088   -25.121 1.00 58.72  ? 130 TYR   B CD2 1 
ATOM   1650 C CE1 . TYR   B 2 121 ? -12.461 4.846   -27.081 1.00 62.06  ? 130 TYR   B CE1 1 
ATOM   1651 C CE2 . TYR   B 2 121 ? -12.116 2.596   -26.326 1.00 61.28  ? 130 TYR   B CE2 1 
ATOM   1652 C CZ  . TYR   B 2 121 ? -12.538 3.480   -27.306 1.00 62.97  ? 130 TYR   B CZ  1 
ATOM   1653 O OH  . TYR   B 2 121 ? -13.023 3.008   -28.490 1.00 68.07  ? 130 TYR   B OH  1 
ATOM   1654 N N   . PRO   B 2 122 ? -9.768  7.656   -22.470 1.00 48.83  ? 131 PRO   B N   1 
ATOM   1655 C CA  . PRO   B 2 122 ? -9.464  8.580   -21.398 1.00 47.41  ? 131 PRO   B CA  1 
ATOM   1656 C C   . PRO   B 2 122 ? -10.140 8.030   -20.132 1.00 45.10  ? 131 PRO   B C   1 
ATOM   1657 O O   . PRO   B 2 122 ? -11.085 7.222   -20.230 1.00 42.74  ? 131 PRO   B O   1 
ATOM   1658 C CB  . PRO   B 2 122 ? -10.061 9.919   -21.827 1.00 49.02  ? 131 PRO   B CB  1 
ATOM   1659 C CG  . PRO   B 2 122 ? -10.359 9.739   -23.299 1.00 49.82  ? 131 PRO   B CG  1 
ATOM   1660 C CD  . PRO   B 2 122 ? -10.652 8.261   -23.478 1.00 50.03  ? 131 PRO   B CD  1 
ATOM   1661 N N   . ALA   B 2 123 ? -9.586  8.434   -19.008 1.00 45.11  ? 132 ALA   B N   1 
ATOM   1662 C CA  . ALA   B 2 123 ? -10.058 8.034   -17.659 1.00 43.78  ? 132 ALA   B CA  1 
ATOM   1663 C C   . ALA   B 2 123 ? -11.554 8.312   -17.476 1.00 43.18  ? 132 ALA   B C   1 
ATOM   1664 O O   . ALA   B 2 123 ? -12.269 7.458   -16.831 1.00 40.43  ? 132 ALA   B O   1 
ATOM   1665 C CB  . ALA   B 2 123 ? -9.207  8.702   -16.611 1.00 44.53  ? 132 ALA   B CB  1 
ATOM   1666 N N   . GLY   B 2 124 ? -12.063 9.395   -18.083 1.00 42.22  ? 133 GLY   B N   1 
ATOM   1667 C CA  . GLY   B 2 124 ? -13.493 9.758   -17.989 1.00 41.71  ? 133 GLY   B CA  1 
ATOM   1668 C C   . GLY   B 2 124 ? -14.416 8.788   -18.761 1.00 39.65  ? 133 GLY   B C   1 
ATOM   1669 O O   . GLY   B 2 124 ? -15.651 9.035   -18.706 1.00 39.80  ? 133 GLY   B O   1 
ATOM   1670 N N   . THR   B 2 125 ? -13.868 7.731   -19.391 1.00 38.50  ? 134 THR   B N   1 
ATOM   1671 C CA  . THR   B 2 125 ? -14.638 6.577   -19.991 1.00 38.97  ? 134 THR   B CA  1 
ATOM   1672 C C   . THR   B 2 125 ? -14.936 5.507   -18.895 1.00 38.35  ? 134 THR   B C   1 
ATOM   1673 O O   . THR   B 2 125 ? -15.825 4.559   -19.129 1.00 37.99  ? 134 THR   B O   1 
ATOM   1674 C CB  . THR   B 2 125 ? -13.918 6.012   -21.225 1.00 41.68  ? 134 THR   B CB  1 
ATOM   1675 O OG1 . THR   B 2 125 ? -13.465 7.119   -22.009 1.00 41.00  ? 134 THR   B OG1 1 
ATOM   1676 C CG2 . THR   B 2 125 ? -14.795 5.233   -22.186 1.00 41.70  ? 134 THR   B CG2 1 
ATOM   1677 N N   . SER   B 2 126 ? -14.223 5.610   -17.748 1.00 37.40  ? 135 SER   B N   1 
ATOM   1678 C CA  . SER   B 2 126 ? -14.434 4.706   -16.589 1.00 37.41  ? 135 SER   B CA  1 
ATOM   1679 C C   . SER   B 2 126 ? -16.011 4.456   -16.495 1.00 35.89  ? 135 SER   B C   1 
ATOM   1680 O O   . SER   B 2 126 ? -16.789 5.451   -16.418 1.00 38.26  ? 135 SER   B O   1 
ATOM   1681 C CB  . SER   B 2 126 ? -13.842 5.258   -15.317 1.00 37.32  ? 135 SER   B CB  1 
ATOM   1682 O OG  . SER   B 2 126 ? -12.426 5.079   -15.229 1.00 38.29  ? 135 SER   B OG  1 
ATOM   1683 N N   . GLY   B 2 127 ? -16.401 3.186   -16.512 1.00 35.15  ? 136 GLY   B N   1 
ATOM   1684 C CA  . GLY   B 2 127 ? -17.872 2.827   -16.221 1.00 34.78  ? 136 GLY   B CA  1 
ATOM   1685 C C   . GLY   B 2 127 ? -18.684 2.393   -17.381 1.00 35.30  ? 136 GLY   B C   1 
ATOM   1686 O O   . GLY   B 2 127 ? -19.813 1.876   -17.139 1.00 33.79  ? 136 GLY   B O   1 
ATOM   1687 N N   . SER   B 2 128 ? -18.068 2.554   -18.578 1.00 35.12  ? 137 SER   B N   1 
ATOM   1688 C CA  . SER   B 2 128 ? -18.705 2.112   -19.816 1.00 35.39  ? 137 SER   B CA  1 
ATOM   1689 C C   . SER   B 2 128 ? -18.897 0.610   -19.728 1.00 34.26  ? 137 SER   B C   1 
ATOM   1690 O O   . SER   B 2 128 ? -17.939 -0.124  -18.907 1.00 35.62  ? 137 SER   B O   1 
ATOM   1691 C CB  . SER   B 2 128 ? -17.906 2.551   -21.039 1.00 35.22  ? 137 SER   B CB  1 
ATOM   1692 O OG  . SER   B 2 128 ? -17.622 4.014   -20.902 1.00 36.29  ? 137 SER   B OG  1 
ATOM   1693 N N   . PRO   B 2 129 ? -20.061 0.090   -20.279 1.00 34.01  ? 138 PRO   B N   1 
ATOM   1694 C CA  . PRO   B 2 129 ? -20.345 -1.315  -20.148 1.00 33.47  ? 138 PRO   B CA  1 
ATOM   1695 C C   . PRO   B 2 129 ? -19.669 -2.201  -21.173 1.00 34.76  ? 138 PRO   B C   1 
ATOM   1696 O O   . PRO   B 2 129 ? -19.620 -1.778  -22.367 1.00 34.90  ? 138 PRO   B O   1 
ATOM   1697 C CB  . PRO   B 2 129 ? -21.845 -1.431  -20.347 1.00 33.83  ? 138 PRO   B CB  1 
ATOM   1698 C CG  . PRO   B 2 129 ? -22.300 -0.129  -21.000 1.00 33.84  ? 138 PRO   B CG  1 
ATOM   1699 C CD  . PRO   B 2 129 ? -21.212 0.907   -20.750 1.00 33.27  ? 138 PRO   B CD  1 
ATOM   1700 N N   . ILE   B 2 130 ? -19.419 -3.422  -20.768 1.00 34.89  ? 139 ILE   B N   1 
ATOM   1701 C CA  . ILE   B 2 130 ? -18.860 -4.513  -21.606 1.00 36.38  ? 139 ILE   B CA  1 
ATOM   1702 C C   . ILE   B 2 130 ? -20.022 -5.476  -21.796 1.00 37.92  ? 139 ILE   B C   1 
ATOM   1703 O O   . ILE   B 2 130 ? -20.762 -5.693  -20.874 1.00 36.94  ? 139 ILE   B O   1 
ATOM   1704 C CB  . ILE   B 2 130 ? -17.613 -5.156  -21.022 1.00 36.94  ? 139 ILE   B CB  1 
ATOM   1705 C CG1 . ILE   B 2 130 ? -16.463 -4.149  -20.930 1.00 37.31  ? 139 ILE   B CG1 1 
ATOM   1706 C CG2 . ILE   B 2 130 ? -17.242 -6.419  -21.780 1.00 37.55  ? 139 ILE   B CG2 1 
ATOM   1707 C CD1 . ILE   B 2 130 ? -15.690 -4.326  -19.654 1.00 38.04  ? 139 ILE   B CD1 1 
ATOM   1708 N N   . LEU   B 2 131 ? -20.322 -5.816  -23.058 1.00 39.92  ? 140 LEU   B N   1 
ATOM   1709 C CA  . LEU   B 2 131 ? -21.549 -6.597  -23.361 1.00 41.95  ? 140 LEU   B CA  1 
ATOM   1710 C C   . LEU   B 2 131 ? -21.181 -7.946  -23.988 1.00 42.92  ? 140 LEU   B C   1 
ATOM   1711 O O   . LEU   B 2 131 ? -20.056 -8.037  -24.631 1.00 44.46  ? 140 LEU   B O   1 
ATOM   1712 C CB  . LEU   B 2 131 ? -22.384 -5.844  -24.401 1.00 43.86  ? 140 LEU   B CB  1 
ATOM   1713 C CG  . LEU   B 2 131 ? -22.661 -4.378  -24.134 1.00 44.78  ? 140 LEU   B CG  1 
ATOM   1714 C CD1 . LEU   B 2 131 ? -23.493 -3.797  -25.266 1.00 47.25  ? 140 LEU   B CD1 1 
ATOM   1715 C CD2 . LEU   B 2 131 ? -23.379 -4.222  -22.808 1.00 44.32  ? 140 LEU   B CD2 1 
ATOM   1716 N N   . ASP   B 2 132 ? -22.122 -8.906  -23.862 1.00 43.35  ? 141 ASP   B N   1 
ATOM   1717 C CA  . ASP   B 2 132 ? -22.050 -10.170 -24.621 1.00 45.40  ? 141 ASP   B CA  1 
ATOM   1718 C C   . ASP   B 2 132 ? -22.956 -10.050 -25.852 1.00 46.82  ? 141 ASP   B C   1 
ATOM   1719 O O   . ASP   B 2 132 ? -23.548 -8.961  -26.098 1.00 44.33  ? 141 ASP   B O   1 
ATOM   1720 C CB  . ASP   B 2 132 ? -22.420 -11.400 -23.790 1.00 45.86  ? 141 ASP   B CB  1 
ATOM   1721 C CG  . ASP   B 2 132 ? -23.855 -11.446 -23.307 1.00 46.72  ? 141 ASP   B CG  1 
ATOM   1722 O OD1 . ASP   B 2 132 ? -24.703 -10.696 -23.817 1.00 46.48  ? 141 ASP   B OD1 1 
ATOM   1723 O OD2 . ASP   B 2 132 ? -24.094 -12.189 -22.326 1.00 48.95  ? 141 ASP   B OD2 1 
ATOM   1724 N N   . LYS   B 2 133 ? -23.110 -11.180 -26.531 1.00 50.59  ? 142 LYS   B N   1 
ATOM   1725 C CA  . LYS   B 2 133 ? -23.649 -11.223 -27.911 1.00 55.21  ? 142 LYS   B CA  1 
ATOM   1726 C C   . LYS   B 2 133 ? -25.149 -10.962 -27.847 1.00 53.77  ? 142 LYS   B C   1 
ATOM   1727 O O   . LYS   B 2 133 ? -25.692 -10.505 -28.851 1.00 51.56  ? 142 LYS   B O   1 
ATOM   1728 C CB  . LYS   B 2 133 ? -23.294 -12.564 -28.573 1.00 59.77  ? 142 LYS   B CB  1 
ATOM   1729 C CG  . LYS   B 2 133 ? -21.962 -12.552 -29.320 1.00 66.25  ? 142 LYS   B CG  1 
ATOM   1730 C CD  . LYS   B 2 133 ? -21.137 -13.858 -29.267 1.00 71.62  ? 142 LYS   B CD  1 
ATOM   1731 C CE  . LYS   B 2 133 ? -19.902 -13.791 -30.160 1.00 75.79  ? 142 LYS   B CE  1 
ATOM   1732 N NZ  . LYS   B 2 133 ? -19.349 -15.119 -30.542 1.00 77.51  ? 142 LYS   B NZ  1 
ATOM   1733 N N   . CYS   B 2 134 ? -25.765 -11.227 -26.685 1.00 55.36  ? 143 CYS   B N   1 
ATOM   1734 C CA  . CYS   B 2 134 ? -27.209 -11.034 -26.417 1.00 55.27  ? 143 CYS   B CA  1 
ATOM   1735 C C   . CYS   B 2 134 ? -27.497 -9.627  -25.846 1.00 53.08  ? 143 CYS   B C   1 
ATOM   1736 O O   . CYS   B 2 134 ? -28.671 -9.374  -25.507 1.00 51.29  ? 143 CYS   B O   1 
ATOM   1737 C CB  . CYS   B 2 134 ? -27.703 -12.065 -25.412 1.00 59.23  ? 143 CYS   B CB  1 
ATOM   1738 S SG  . CYS   B 2 134 ? -27.985 -13.725 -26.076 1.00 62.69  ? 143 CYS   B SG  1 
ATOM   1739 N N   . GLY   B 2 135 ? -26.492 -8.743  -25.730 1.00 50.68  ? 144 GLY   B N   1 
ATOM   1740 C CA  . GLY   B 2 135 ? -26.678 -7.374  -25.201 1.00 48.22  ? 144 GLY   B CA  1 
ATOM   1741 C C   . GLY   B 2 135 ? -26.675 -7.286  -23.669 1.00 46.14  ? 144 GLY   B C   1 
ATOM   1742 O O   . GLY   B 2 135 ? -27.066 -6.255  -23.146 1.00 46.00  ? 144 GLY   B O   1 
ATOM   1743 N N   . ARG   B 2 136 ? -26.238 -8.321  -22.971 1.00 43.70  ? 145 ARG   B N   1 
ATOM   1744 C CA  . ARG   B 2 136 ? -26.184 -8.259  -21.472 1.00 43.42  ? 145 ARG   B CA  1 
ATOM   1745 C C   . ARG   B 2 136 ? -24.884 -7.625  -21.003 1.00 41.34  ? 145 ARG   B C   1 
ATOM   1746 O O   . ARG   B 2 136 ? -23.827 -7.979  -21.556 1.00 41.34  ? 145 ARG   B O   1 
ATOM   1747 C CB  . ARG   B 2 136 ? -26.475 -9.651  -20.955 1.00 46.05  ? 145 ARG   B CB  1 
ATOM   1748 C CG  . ARG   B 2 136 ? -27.967 -9.937  -21.040 1.00 50.26  ? 145 ARG   B CG  1 
ATOM   1749 C CD  . ARG   B 2 136 ? -28.275 -11.370 -20.706 1.00 54.83  ? 145 ARG   B CD  1 
ATOM   1750 N NE  . ARG   B 2 136 ? -27.363 -12.195 -21.477 1.00 60.91  ? 145 ARG   B NE  1 
ATOM   1751 C CZ  . ARG   B 2 136 ? -26.799 -13.323 -21.065 1.00 64.70  ? 145 ARG   B CZ  1 
ATOM   1752 N NH1 . ARG   B 2 136 ? -27.037 -13.812 -19.853 1.00 65.51  ? 145 ARG   B NH1 1 
ATOM   1753 N NH2 . ARG   B 2 136 ? -25.997 -13.968 -21.894 1.00 68.72  ? 145 ARG   B NH2 1 
ATOM   1754 N N   . VAL   B 2 137 ? -24.952 -6.840  -19.895 1.00 38.73  ? 146 VAL   B N   1 
ATOM   1755 C CA  . VAL   B 2 137 ? -23.749 -6.174  -19.300 1.00 37.05  ? 146 VAL   B CA  1 
ATOM   1756 C C   . VAL   B 2 137 ? -23.040 -7.252  -18.476 1.00 37.01  ? 146 VAL   B C   1 
ATOM   1757 O O   . VAL   B 2 137 ? -23.613 -7.666  -17.427 1.00 37.33  ? 146 VAL   B O   1 
ATOM   1758 C CB  . VAL   B 2 137 ? -24.062 -4.873  -18.538 1.00 35.40  ? 146 VAL   B CB  1 
ATOM   1759 C CG1 . VAL   B 2 137 ? -22.799 -4.216  -17.996 1.00 34.20  ? 146 VAL   B CG1 1 
ATOM   1760 C CG2 . VAL   B 2 137 ? -24.753 -3.872  -19.481 1.00 35.93  ? 146 VAL   B CG2 1 
ATOM   1761 N N   . ILE   B 2 138 ? -21.858 -7.663  -18.931 1.00 36.52  ? 147 ILE   B N   1 
ATOM   1762 C CA  . ILE   B 2 138 ? -20.984 -8.667  -18.261 1.00 36.71  ? 147 ILE   B CA  1 
ATOM   1763 C C   . ILE   B 2 138 ? -19.988 -7.973  -17.305 1.00 35.72  ? 147 ILE   B C   1 
ATOM   1764 O O   . ILE   B 2 138 ? -19.261 -8.690  -16.553 1.00 35.80  ? 147 ILE   B O   1 
ATOM   1765 C CB  . ILE   B 2 138 ? -20.286 -9.593  -19.305 1.00 37.36  ? 147 ILE   B CB  1 
ATOM   1766 C CG1 . ILE   B 2 138 ? -19.346 -8.826  -20.233 1.00 37.42  ? 147 ILE   B CG1 1 
ATOM   1767 C CG2 . ILE   B 2 138 ? -21.318 -10.412 -20.029 1.00 37.80  ? 147 ILE   B CG2 1 
ATOM   1768 C CD1 . ILE   B 2 138 ? -18.367 -9.707  -21.012 1.00 39.06  ? 147 ILE   B CD1 1 
ATOM   1769 N N   . GLY   B 2 139 ? -19.937 -6.643  -17.304 1.00 35.28  ? 148 GLY   B N   1 
ATOM   1770 C CA  . GLY   B 2 139 ? -19.146 -5.890  -16.320 1.00 34.39  ? 148 GLY   B CA  1 
ATOM   1771 C C   . GLY   B 2 139 ? -18.869 -4.526  -16.841 1.00 34.07  ? 148 GLY   B C   1 
ATOM   1772 O O   . GLY   B 2 139 ? -19.402 -4.144  -17.992 1.00 33.17  ? 148 GLY   B O   1 
ATOM   1773 N N   A LEU   B 2 140 ? -18.100 -3.764  -16.073 0.20 33.44  ? 149 LEU   B N   1 
ATOM   1774 N N   B LEU   B 2 140 ? -18.103 -3.763  -16.069 0.18 33.45  ? 149 LEU   B N   1 
ATOM   1775 N N   C LEU   B 2 140 ? -17.982 -3.812  -16.156 0.31 32.74  ? 149 LEU   B N   1 
ATOM   1776 N N   D LEU   B 2 140 ? -17.983 -3.811  -16.155 0.31 32.74  ? 149 LEU   B N   1 
ATOM   1777 C CA  A LEU   B 2 140 ? -17.822 -2.325  -16.277 0.20 33.54  ? 149 LEU   B CA  1 
ATOM   1778 C CA  B LEU   B 2 140 ? -17.822 -2.324  -16.276 0.18 33.55  ? 149 LEU   B CA  1 
ATOM   1779 C CA  C LEU   B 2 140 ? -17.739 -2.359  -16.324 0.31 32.87  ? 149 LEU   B CA  1 
ATOM   1780 C CA  D LEU   B 2 140 ? -17.739 -2.358  -16.324 0.31 32.87  ? 149 LEU   B CA  1 
ATOM   1781 C C   A LEU   B 2 140 ? -16.328 -2.196  -16.612 0.20 34.05  ? 149 LEU   B C   1 
ATOM   1782 C C   B LEU   B 2 140 ? -16.327 -2.199  -16.607 0.18 34.05  ? 149 LEU   B C   1 
ATOM   1783 C C   C LEU   B 2 140 ? -16.248 -2.191  -16.707 0.31 33.86  ? 149 LEU   B C   1 
ATOM   1784 C C   D LEU   B 2 140 ? -16.248 -2.192  -16.707 0.31 33.85  ? 149 LEU   B C   1 
ATOM   1785 O O   A LEU   B 2 140 ? -15.445 -2.995  -16.057 0.20 34.20  ? 149 LEU   B O   1 
ATOM   1786 O O   B LEU   B 2 140 ? -15.447 -3.001  -16.042 0.18 34.20  ? 149 LEU   B O   1 
ATOM   1787 O O   C LEU   B 2 140 ? -15.294 -3.180  -16.152 0.31 33.62  ? 149 LEU   B O   1 
ATOM   1788 O O   D LEU   B 2 140 ? -15.294 -3.183  -16.148 0.31 33.62  ? 149 LEU   B O   1 
ATOM   1789 C CB  A LEU   B 2 140 ? -18.230 -1.496  -15.048 0.20 33.24  ? 149 LEU   B CB  1 
ATOM   1790 C CB  B LEU   B 2 140 ? -18.230 -1.495  -15.047 0.18 33.24  ? 149 LEU   B CB  1 
ATOM   1791 C CB  C LEU   B 2 140 ? -18.149 -1.564  -15.070 0.31 32.31  ? 149 LEU   B CB  1 
ATOM   1792 C CB  D LEU   B 2 140 ? -18.149 -1.563  -15.070 0.31 32.31  ? 149 LEU   B CB  1 
ATOM   1793 C CG  A LEU   B 2 140 ? -19.730 -1.421  -14.729 0.20 32.94  ? 149 LEU   B CG  1 
ATOM   1794 C CG  B LEU   B 2 140 ? -19.730 -1.421  -14.729 0.18 32.95  ? 149 LEU   B CG  1 
ATOM   1795 C CG  C LEU   B 2 140 ? -19.653 -1.463  -14.756 0.31 31.71  ? 149 LEU   B CG  1 
ATOM   1796 C CG  D LEU   B 2 140 ? -19.653 -1.462  -14.756 0.31 31.72  ? 149 LEU   B CG  1 
ATOM   1797 C CD1 A LEU   B 2 140 ? -20.007 -0.276  -13.761 0.20 32.93  ? 149 LEU   B CD1 1 
ATOM   1798 C CD1 B LEU   B 2 140 ? -20.009 -0.276  -13.761 0.18 32.93  ? 149 LEU   B CD1 1 
ATOM   1799 C CD1 C LEU   B 2 140 ? -19.913 -0.287  -13.819 0.31 31.62  ? 149 LEU   B CD1 1 
ATOM   1800 C CD1 D LEU   B 2 140 ? -19.914 -0.287  -13.820 0.31 31.62  ? 149 LEU   B CD1 1 
ATOM   1801 C CD2 A LEU   B 2 140 ? -20.585 -1.245  -15.980 0.20 33.39  ? 149 LEU   B CD2 1 
ATOM   1802 C CD2 B LEU   B 2 140 ? -20.584 -1.246  -15.981 0.18 33.40  ? 149 LEU   B CD2 1 
ATOM   1803 C CD2 C LEU   B 2 140 ? -20.515 -1.294  -16.006 0.31 32.22  ? 149 LEU   B CD2 1 
ATOM   1804 C CD2 D LEU   B 2 140 ? -20.514 -1.294  -16.007 0.31 32.22  ? 149 LEU   B CD2 1 
ATOM   1805 N N   A TYR   B 2 141 ? -16.053 -1.306  -17.596 0.20 33.98  ? 150 TYR   B N   1 
ATOM   1806 N N   B TYR   B 2 141 ? -16.050 -1.311  -17.593 0.18 34.01  ? 150 TYR   B N   1 
ATOM   1807 N N   C TYR   B 2 141 ? -15.981 -1.087  -17.493 0.31 33.83  ? 150 TYR   B N   1 
ATOM   1808 N N   D TYR   B 2 141 ? -15.980 -1.088  -17.492 0.31 33.85  ? 150 TYR   B N   1 
ATOM   1809 C CA  A TYR   B 2 141 ? -14.666 -0.978  -17.995 0.20 34.94  ? 150 TYR   B CA  1 
ATOM   1810 C CA  B TYR   B 2 141 ? -14.663 -0.980  -17.994 0.18 34.95  ? 150 TYR   B CA  1 
ATOM   1811 C CA  C TYR   B 2 141 ? -14.591 -0.803  -17.914 0.31 35.42  ? 150 TYR   B CA  1 
ATOM   1812 C CA  D TYR   B 2 141 ? -14.590 -0.803  -17.914 0.31 35.43  ? 150 TYR   B CA  1 
ATOM   1813 C C   A TYR   B 2 141 ? -14.189 0.192   -17.119 0.20 34.61  ? 150 TYR   B C   1 
ATOM   1814 C C   B TYR   B 2 141 ? -14.189 0.191   -17.118 0.18 34.63  ? 150 TYR   B C   1 
ATOM   1815 C C   C TYR   B 2 141 ? -14.005 0.348   -17.084 0.31 35.29  ? 150 TYR   B C   1 
ATOM   1816 C C   D TYR   B 2 141 ? -14.005 0.349   -17.084 0.31 35.30  ? 150 TYR   B C   1 
ATOM   1817 O O   A TYR   B 2 141 ? -15.068 1.018   -16.693 0.20 35.60  ? 150 TYR   B O   1 
ATOM   1818 O O   B TYR   B 2 141 ? -15.069 1.019   -16.694 0.18 35.58  ? 150 TYR   B O   1 
ATOM   1819 O O   C TYR   B 2 141 ? -14.756 1.373   -16.793 0.31 37.13  ? 150 TYR   B O   1 
ATOM   1820 O O   D TYR   B 2 141 ? -14.757 1.373   -16.795 0.31 37.11  ? 150 TYR   B O   1 
ATOM   1821 C CB  A TYR   B 2 141 ? -14.696 -0.676  -19.501 0.20 35.66  ? 150 TYR   B CB  1 
ATOM   1822 C CB  B TYR   B 2 141 ? -14.694 -0.679  -19.500 0.18 35.67  ? 150 TYR   B CB  1 
ATOM   1823 C CB  C TYR   B 2 141 ? -14.600 -0.427  -19.407 0.31 36.53  ? 150 TYR   B CB  1 
ATOM   1824 C CB  D TYR   B 2 141 ? -14.599 -0.428  -19.407 0.31 36.54  ? 150 TYR   B CB  1 
ATOM   1825 C CG  A TYR   B 2 141 ? -13.480 -0.018  -20.107 0.20 36.72  ? 150 TYR   B CG  1 
ATOM   1826 C CG  B TYR   B 2 141 ? -13.479 -0.022  -20.106 0.18 36.71  ? 150 TYR   B CG  1 
ATOM   1827 C CG  C TYR   B 2 141 ? -13.329 0.207   -19.922 0.31 38.13  ? 150 TYR   B CG  1 
ATOM   1828 C CG  D TYR   B 2 141 ? -13.329 0.206   -19.922 0.31 38.13  ? 150 TYR   B CG  1 
ATOM   1829 C CD1 A TYR   B 2 141 ? -13.394 1.363   -20.204 0.20 37.17  ? 150 TYR   B CD1 1 
ATOM   1830 C CD1 B TYR   B 2 141 ? -13.393 1.360   -20.200 0.18 37.17  ? 150 TYR   B CD1 1 
ATOM   1831 C CD1 C TYR   B 2 141 ? -13.095 1.567   -19.781 0.31 38.80  ? 150 TYR   B CD1 1 
ATOM   1832 C CD1 D TYR   B 2 141 ? -13.095 1.567   -19.781 0.31 38.80  ? 150 TYR   B CD1 1 
ATOM   1833 C CD2 A TYR   B 2 141 ? -12.445 -0.773  -20.640 0.20 37.32  ? 150 TYR   B CD2 1 
ATOM   1834 C CD2 B TYR   B 2 141 ? -12.444 -0.776  -20.643 0.18 37.31  ? 150 TYR   B CD2 1 
ATOM   1835 C CD2 C TYR   B 2 141 ? -12.352 -0.558  -20.543 0.31 39.34  ? 150 TYR   B CD2 1 
ATOM   1836 C CD2 D TYR   B 2 141 ? -12.352 -0.558  -20.544 0.31 39.34  ? 150 TYR   B CD2 1 
ATOM   1837 C CE1 A TYR   B 2 141 ? -12.298 1.980   -20.789 0.20 38.15  ? 150 TYR   B CE1 1 
ATOM   1838 C CE1 B TYR   B 2 141 ? -12.298 1.978   -20.785 0.18 38.13  ? 150 TYR   B CE1 1 
ATOM   1839 C CE1 C TYR   B 2 141 ? -11.920 2.151   -20.237 0.31 39.98  ? 150 TYR   B CE1 1 
ATOM   1840 C CE1 D TYR   B 2 141 ? -11.920 2.150   -20.238 0.31 39.97  ? 150 TYR   B CE1 1 
ATOM   1841 C CE2 A TYR   B 2 141 ? -11.349 -0.173  -21.248 0.20 38.19  ? 150 TYR   B CE2 1 
ATOM   1842 C CE2 B TYR   B 2 141 ? -11.348 -0.173  -21.249 0.18 38.17  ? 150 TYR   B CE2 1 
ATOM   1843 C CE2 C TYR   B 2 141 ? -11.191 0.015   -21.048 0.31 40.63  ? 150 TYR   B CE2 1 
ATOM   1844 C CE2 D TYR   B 2 141 ? -11.191 0.015   -21.048 0.31 40.62  ? 150 TYR   B CE2 1 
ATOM   1845 C CZ  A TYR   B 2 141 ? -11.279 1.209   -21.326 0.20 38.35  ? 150 TYR   B CZ  1 
ATOM   1846 C CZ  B TYR   B 2 141 ? -11.278 1.209   -21.324 0.18 38.34  ? 150 TYR   B CZ  1 
ATOM   1847 C CZ  C TYR   B 2 141 ? -10.969 1.373   -20.890 0.31 41.04  ? 150 TYR   B CZ  1 
ATOM   1848 C CZ  D TYR   B 2 141 ? -10.969 1.373   -20.890 0.31 41.03  ? 150 TYR   B CZ  1 
ATOM   1849 O OH  A TYR   B 2 141 ? -10.184 1.808   -21.879 0.20 39.20  ? 150 TYR   B OH  1 
ATOM   1850 O OH  B TYR   B 2 141 ? -10.185 1.810   -21.878 0.18 39.18  ? 150 TYR   B OH  1 
ATOM   1851 O OH  C TYR   B 2 141 ? -9.798  1.895   -21.375 0.31 42.05  ? 150 TYR   B OH  1 
ATOM   1852 O OH  D TYR   B 2 141 ? -9.799  1.896   -21.375 0.31 42.04  ? 150 TYR   B OH  1 
ATOM   1853 N N   A GLY   B 2 142 ? -12.864 0.201   -16.784 0.20 34.71  ? 151 GLY   B N   1 
ATOM   1854 N N   B GLY   B 2 142 ? -12.865 0.203   -16.780 0.18 34.73  ? 151 GLY   B N   1 
ATOM   1855 N N   C GLY   B 2 142 ? -12.681 0.227   -16.716 0.31 35.41  ? 151 GLY   B N   1 
ATOM   1856 N N   D GLY   B 2 142 ? -12.682 0.228   -16.715 0.31 35.41  ? 151 GLY   B N   1 
ATOM   1857 C CA  A GLY   B 2 142 ? -12.239 1.390   -16.162 0.20 35.18  ? 151 GLY   B CA  1 
ATOM   1858 C CA  B GLY   B 2 142 ? -12.241 1.390   -16.157 0.18 35.18  ? 151 GLY   B CA  1 
ATOM   1859 C CA  C GLY   B 2 142 ? -11.965 1.379   -16.121 0.31 36.24  ? 151 GLY   B CA  1 
ATOM   1860 C CA  D GLY   B 2 142 ? -11.966 1.380   -16.120 0.31 36.24  ? 151 GLY   B CA  1 
ATOM   1861 C C   A GLY   B 2 142 ? -11.441 1.111   -14.883 0.20 35.16  ? 151 GLY   B C   1 
ATOM   1862 C C   B GLY   B 2 142 ? -11.438 1.110   -14.881 0.18 35.18  ? 151 GLY   B C   1 
ATOM   1863 C C   C GLY   B 2 142 ? -11.138 1.037   -14.875 0.31 36.34  ? 151 GLY   B C   1 
ATOM   1864 C C   D GLY   B 2 142 ? -11.139 1.038   -14.874 0.31 36.34  ? 151 GLY   B C   1 
ATOM   1865 O O   A GLY   B 2 142 ? -10.899 2.117   -14.339 0.20 35.35  ? 151 GLY   B O   1 
ATOM   1866 O O   B GLY   B 2 142 ? -10.893 2.114   -14.336 0.18 35.35  ? 151 GLY   B O   1 
ATOM   1867 O O   C GLY   B 2 142 ? -10.358 1.955   -14.412 0.31 36.60  ? 151 GLY   B O   1 
ATOM   1868 O O   D GLY   B 2 142 ? -10.358 1.956   -14.412 0.31 36.60  ? 151 GLY   B O   1 
ATOM   1869 N N   A ASN   B 2 143 ? -11.297 -0.162  -14.453 0.20 35.53  ? 152 ASN   B N   1 
ATOM   1870 N N   B ASN   B 2 143 ? -11.299 -0.163  -14.450 0.18 35.53  ? 152 ASN   B N   1 
ATOM   1871 N N   C ASN   B 2 143 ? -11.238 -0.213  -14.377 0.31 36.90  ? 152 ASN   B N   1 
ATOM   1872 N N   D ASN   B 2 143 ? -11.238 -0.212  -14.376 0.31 36.90  ? 152 ASN   B N   1 
ATOM   1873 C CA  A ASN   B 2 143 ? -10.324 -0.566  -13.364 0.20 35.90  ? 152 ASN   B CA  1 
ATOM   1874 C CA  B ASN   B 2 143 ? -10.324 -0.570  -13.365 0.18 35.90  ? 152 ASN   B CA  1 
ATOM   1875 C CA  C ASN   B 2 143 ? -10.369 -0.728  -13.245 0.31 37.19  ? 152 ASN   B CA  1 
ATOM   1876 C CA  D ASN   B 2 143 ? -10.369 -0.728  -13.245 0.31 37.19  ? 152 ASN   B CA  1 
ATOM   1877 C C   A ASN   B 2 143 ? -9.388  -1.741  -13.859 0.20 36.59  ? 152 ASN   B C   1 
ATOM   1878 C C   B ASN   B 2 143 ? -9.387  -1.741  -13.865 0.18 36.60  ? 152 ASN   B C   1 
ATOM   1879 C C   C ASN   B 2 143 ? -9.381  -1.852  -13.814 0.31 37.30  ? 152 ASN   B C   1 
ATOM   1880 C C   D ASN   B 2 143 ? -9.381  -1.851  -13.816 0.31 37.31  ? 152 ASN   B C   1 
ATOM   1881 O O   A ASN   B 2 143 ? -9.835  -3.018  -13.694 0.20 36.98  ? 152 ASN   B O   1 
ATOM   1882 O O   B ASN   B 2 143 ? -9.834  -3.024  -13.706 0.18 36.96  ? 152 ASN   B O   1 
ATOM   1883 O O   C ASN   B 2 143 ? -9.756  -3.172  -13.794 0.31 38.03  ? 152 ASN   B O   1 
ATOM   1884 O O   D ASN   B 2 143 ? -9.756  -3.172  -13.794 0.31 38.02  ? 152 ASN   B O   1 
ATOM   1885 C CB  A ASN   B 2 143 ? -10.947 -1.004  -12.013 0.20 35.46  ? 152 ASN   B CB  1 
ATOM   1886 C CB  B ASN   B 2 143 ? -10.946 -1.008  -12.014 0.18 35.46  ? 152 ASN   B CB  1 
ATOM   1887 C CB  C ASN   B 2 143 ? -11.125 -1.311  -12.026 0.31 37.42  ? 152 ASN   B CB  1 
ATOM   1888 C CB  D ASN   B 2 143 ? -11.125 -1.312  -12.027 0.31 37.41  ? 152 ASN   B CB  1 
ATOM   1889 C CG  A ASN   B 2 143 ? -10.009 -0.736  -10.835 0.20 35.10  ? 152 ASN   B CG  1 
ATOM   1890 C CG  B ASN   B 2 143 ? -10.010 -0.738  -10.836 0.18 35.10  ? 152 ASN   B CG  1 
ATOM   1891 C CG  C ASN   B 2 143 ? -10.242 -1.351  -10.784 0.31 37.55  ? 152 ASN   B CG  1 
ATOM   1892 C CG  D ASN   B 2 143 ? -10.242 -1.352  -10.784 0.31 37.54  ? 152 ASN   B CG  1 
ATOM   1893 O OD1 A ASN   B 2 143 ? -9.209  0.215   -10.851 0.20 35.33  ? 152 ASN   B OD1 1 
ATOM   1894 O OD1 B ASN   B 2 143 ? -9.212  0.214   -10.853 0.18 35.34  ? 152 ASN   B OD1 1 
ATOM   1895 O OD1 C ASN   B 2 143 ? -9.312  -0.544  -10.639 0.31 38.49  ? 152 ASN   B OD1 1 
ATOM   1896 O OD1 D ASN   B 2 143 ? -9.312  -0.544  -10.640 0.31 38.48  ? 152 ASN   B OD1 1 
ATOM   1897 N ND2 A ASN   B 2 143 ? -10.092 -1.554  -9.779  0.20 34.44  ? 152 ASN   B ND2 1 
ATOM   1898 N ND2 B ASN   B 2 143 ? -10.093 -1.555  -9.780  0.18 34.46  ? 152 ASN   B ND2 1 
ATOM   1899 N ND2 C ASN   B 2 143 ? -10.521 -2.276  -9.862  0.31 37.00  ? 152 ASN   B ND2 1 
ATOM   1900 N ND2 D ASN   B 2 143 ? -10.521 -2.277  -9.862  0.31 37.00  ? 152 ASN   B ND2 1 
ATOM   1901 N N   . GLY   B 2 144 ? -7.984  -1.263  -13.836 1.00 37.10  ? 153 GLY   B N   1 
ATOM   1902 C CA  . GLY   B 2 144 ? -6.968  -2.213  -14.311 1.00 40.70  ? 153 GLY   B CA  1 
ATOM   1903 C C   . GLY   B 2 144 ? -5.591  -1.662  -14.153 1.00 43.27  ? 153 GLY   B C   1 
ATOM   1904 O O   . GLY   B 2 144 ? -5.289  -1.033  -13.102 1.00 43.30  ? 153 GLY   B O   1 
ATOM   1905 N N   A VAL   B 2 145 ? -4.747  -1.861  -15.170 0.20 44.68  ? 154 VAL   B N   1 
ATOM   1906 N N   B VAL   B 2 145 ? -4.747  -1.861  -15.170 0.18 44.68  ? 154 VAL   B N   1 
ATOM   1907 N N   C VAL   B 2 145 ? -4.748  -1.861  -15.172 0.31 44.63  ? 154 VAL   B N   1 
ATOM   1908 N N   D VAL   B 2 145 ? -4.783  -1.817  -15.208 0.31 43.27  ? 154 VAL   B N   1 
ATOM   1909 C CA  A VAL   B 2 145 ? -3.276  -1.677  -15.034 0.20 46.15  ? 154 VAL   B CA  1 
ATOM   1910 C CA  B VAL   B 2 145 ? -3.276  -1.677  -15.034 0.18 46.16  ? 154 VAL   B CA  1 
ATOM   1911 C CA  C VAL   B 2 145 ? -3.277  -1.676  -15.036 0.31 46.10  ? 154 VAL   B CA  1 
ATOM   1912 C CA  D VAL   B 2 145 ? -3.298  -1.771  -15.143 0.31 43.99  ? 154 VAL   B CA  1 
ATOM   1913 C C   A VAL   B 2 145 ? -2.695  -1.060  -16.311 0.20 48.14  ? 154 VAL   B C   1 
ATOM   1914 C C   B VAL   B 2 145 ? -2.695  -1.061  -16.311 0.18 48.12  ? 154 VAL   B C   1 
ATOM   1915 C C   C VAL   B 2 145 ? -2.696  -1.059  -16.313 0.31 48.20  ? 154 VAL   B C   1 
ATOM   1916 C C   D VAL   B 2 145 ? -2.765  -0.963  -16.335 0.31 46.67  ? 154 VAL   B C   1 
ATOM   1917 O O   A VAL   B 2 145 ? -3.221  -1.339  -17.400 0.20 47.26  ? 154 VAL   B O   1 
ATOM   1918 O O   B VAL   B 2 145 ? -3.221  -1.339  -17.401 0.18 47.29  ? 154 VAL   B O   1 
ATOM   1919 O O   C VAL   B 2 145 ? -3.222  -1.338  -17.399 0.31 47.08  ? 154 VAL   B O   1 
ATOM   1920 O O   D VAL   B 2 145 ? -3.434  -0.963  -17.377 0.31 45.35  ? 154 VAL   B O   1 
ATOM   1921 C CB  A VAL   B 2 145 ? -2.616  -3.019  -14.667 0.20 46.77  ? 154 VAL   B CB  1 
ATOM   1922 C CB  B VAL   B 2 145 ? -2.615  -3.019  -14.667 0.18 46.76  ? 154 VAL   B CB  1 
ATOM   1923 C CB  C VAL   B 2 145 ? -2.617  -3.019  -14.670 0.31 46.81  ? 154 VAL   B CB  1 
ATOM   1924 C CB  D VAL   B 2 145 ? -2.771  -3.220  -15.092 0.31 43.17  ? 154 VAL   B CB  1 
ATOM   1925 C CG1 A VAL   B 2 145 ? -2.514  -3.974  -15.847 0.20 46.62  ? 154 VAL   B CG1 1 
ATOM   1926 C CG1 B VAL   B 2 145 ? -2.513  -3.973  -15.847 0.18 46.64  ? 154 VAL   B CG1 1 
ATOM   1927 C CG1 C VAL   B 2 145 ? -2.516  -3.976  -15.848 0.31 46.51  ? 154 VAL   B CG1 1 
ATOM   1928 C CG1 D VAL   B 2 145 ? -1.333  -3.340  -15.542 0.31 43.75  ? 154 VAL   B CG1 1 
ATOM   1929 C CG2 A VAL   B 2 145 ? -1.266  -2.810  -14.003 0.20 47.61  ? 154 VAL   B CG2 1 
ATOM   1930 C CG2 B VAL   B 2 145 ? -1.265  -2.810  -14.003 0.18 47.57  ? 154 VAL   B CG2 1 
ATOM   1931 C CG2 C VAL   B 2 145 ? -1.268  -2.808  -14.004 0.31 47.77  ? 154 VAL   B CG2 1 
ATOM   1932 C CG2 D VAL   B 2 145 ? -2.958  -3.823  -13.696 0.31 42.17  ? 154 VAL   B CG2 1 
ATOM   1933 N N   . VAL   B 2 146 ? -1.648  -0.248  -16.138 1.00 49.62  ? 155 VAL   B N   1 
ATOM   1934 C CA  . VAL   B 2 146 ? -0.813  0.330   -17.224 1.00 52.36  ? 155 VAL   B CA  1 
ATOM   1935 C C   . VAL   B 2 146 ? 0.265   -0.711  -17.528 1.00 57.85  ? 155 VAL   B C   1 
ATOM   1936 O O   . VAL   B 2 146 ? 0.894   -1.182  -16.554 1.00 57.22  ? 155 VAL   B O   1 
ATOM   1937 C CB  . VAL   B 2 146 ? -0.212  1.661   -16.733 1.00 53.39  ? 155 VAL   B CB  1 
ATOM   1938 C CG1 . VAL   B 2 146 ? 0.749   2.269   -17.725 1.00 54.81  ? 155 VAL   B CG1 1 
ATOM   1939 C CG2 . VAL   B 2 146 ? -1.300  2.665   -16.390 1.00 54.32  ? 155 VAL   B CG2 1 
ATOM   1940 N N   . ILE   B 2 147 ? 0.453   -1.103  -18.794 1.00 62.95  ? 156 ILE   B N   1 
ATOM   1941 C CA  . ILE   B 2 147 ? 1.224   -2.331  -19.171 1.00 68.30  ? 156 ILE   B CA  1 
ATOM   1942 C C   . ILE   B 2 147 ? 2.600   -1.930  -19.714 1.00 73.64  ? 156 ILE   B C   1 
ATOM   1943 O O   . ILE   B 2 147 ? 2.834   -0.730  -19.937 1.00 73.08  ? 156 ILE   B O   1 
ATOM   1944 C CB  . ILE   B 2 147 ? 0.434   -3.224  -20.156 1.00 67.44  ? 156 ILE   B CB  1 
ATOM   1945 C CG1 . ILE   B 2 147 ? -0.078  -2.481  -21.395 1.00 68.30  ? 156 ILE   B CG1 1 
ATOM   1946 C CG2 . ILE   B 2 147 ? -0.701  -3.942  -19.440 1.00 64.90  ? 156 ILE   B CG2 1 
ATOM   1947 C CD1 . ILE   B 2 147 ? -0.455  -3.416  -22.523 1.00 67.68  ? 156 ILE   B CD1 1 
ATOM   1948 N N   A LYS   B 2 148 ? 3.481   -2.922  -19.902 0.25 75.22  ? 157 LYS   B N   1 
ATOM   1949 N N   B LYS   B 2 148 ? 3.481   -2.922  -19.902 0.25 75.22  ? 157 LYS   B N   1 
ATOM   1950 N N   C LYS   B 2 148 ? 3.483   -2.917  -19.911 0.25 75.25  ? 157 LYS   B N   1 
ATOM   1951 N N   D LYS   B 2 148 ? 3.483   -2.917  -19.911 0.25 75.25  ? 157 LYS   B N   1 
ATOM   1952 C CA  A LYS   B 2 148 ? 4.866   -2.760  -20.426 0.25 77.40  ? 157 LYS   B CA  1 
ATOM   1953 C CA  B LYS   B 2 148 ? 4.866   -2.760  -20.426 0.25 77.40  ? 157 LYS   B CA  1 
ATOM   1954 C CA  C LYS   B 2 148 ? 4.877   -2.734  -20.405 0.25 77.44  ? 157 LYS   B CA  1 
ATOM   1955 C CA  D LYS   B 2 148 ? 4.877   -2.734  -20.405 0.25 77.44  ? 157 LYS   B CA  1 
ATOM   1956 C C   A LYS   B 2 148 ? 4.903   -1.639  -21.471 0.25 78.79  ? 157 LYS   B C   1 
ATOM   1957 C C   B LYS   B 2 148 ? 4.903   -1.639  -21.471 0.25 78.79  ? 157 LYS   B C   1 
ATOM   1958 C C   C LYS   B 2 148 ? 4.913   -1.642  -21.482 0.25 78.85  ? 157 LYS   B C   1 
ATOM   1959 C C   D LYS   B 2 148 ? 4.913   -1.642  -21.482 0.25 78.85  ? 157 LYS   B C   1 
ATOM   1960 O O   A LYS   B 2 148 ? 5.879   -0.867  -21.469 0.25 80.43  ? 157 LYS   B O   1 
ATOM   1961 O O   B LYS   B 2 148 ? 5.879   -0.867  -21.469 0.25 80.43  ? 157 LYS   B O   1 
ATOM   1962 O O   C LYS   B 2 148 ? 5.905   -0.892  -21.517 0.25 80.59  ? 157 LYS   B O   1 
ATOM   1963 O O   D LYS   B 2 148 ? 5.905   -0.892  -21.517 0.25 80.59  ? 157 LYS   B O   1 
ATOM   1964 C CB  A LYS   B 2 148 ? 5.356   -4.070  -21.052 0.25 78.61  ? 157 LYS   B CB  1 
ATOM   1965 C CB  B LYS   B 2 148 ? 5.356   -4.070  -21.052 0.25 78.61  ? 157 LYS   B CB  1 
ATOM   1966 C CB  C LYS   B 2 148 ? 5.420   -4.053  -20.964 0.25 78.70  ? 157 LYS   B CB  1 
ATOM   1967 C CB  D LYS   B 2 148 ? 5.420   -4.053  -20.964 0.25 78.70  ? 157 LYS   B CB  1 
ATOM   1968 C CG  A LYS   B 2 148 ? 5.773   -5.148  -20.060 0.25 78.34  ? 157 LYS   B CG  1 
ATOM   1969 C CG  B LYS   B 2 148 ? 5.773   -5.148  -20.060 0.25 78.34  ? 157 LYS   B CG  1 
ATOM   1970 C CG  C LYS   B 2 148 ? 6.800   -3.973  -21.606 0.25 79.76  ? 157 LYS   B CG  1 
ATOM   1971 C CG  D LYS   B 2 148 ? 6.800   -3.973  -21.606 0.25 79.76  ? 157 LYS   B CG  1 
ATOM   1972 C CD  A LYS   B 2 148 ? 6.078   -6.484  -20.710 0.25 78.89  ? 157 LYS   B CD  1 
ATOM   1973 C CD  B LYS   B 2 148 ? 6.078   -6.484  -20.710 0.25 78.89  ? 157 LYS   B CD  1 
ATOM   1974 C CD  C LYS   B 2 148 ? 7.920   -3.732  -20.618 0.25 80.00  ? 157 LYS   B CD  1 
ATOM   1975 C CD  D LYS   B 2 148 ? 7.920   -3.732  -20.618 0.25 80.00  ? 157 LYS   B CD  1 
ATOM   1976 C CE  A LYS   B 2 148 ? 7.278   -6.445  -21.632 0.25 79.84  ? 157 LYS   B CE  1 
ATOM   1977 C CE  B LYS   B 2 148 ? 7.278   -6.445  -21.632 0.25 79.84  ? 157 LYS   B CE  1 
ATOM   1978 C CE  C LYS   B 2 148 ? 7.718   -4.457  -19.303 0.25 79.46  ? 157 LYS   B CE  1 
ATOM   1979 C CE  D LYS   B 2 148 ? 7.718   -4.457  -19.303 0.25 79.46  ? 157 LYS   B CE  1 
ATOM   1980 N NZ  A LYS   B 2 148 ? 8.551   -6.383  -20.877 0.25 79.69  ? 157 LYS   B NZ  1 
ATOM   1981 N NZ  B LYS   B 2 148 ? 8.551   -6.383  -20.877 0.25 79.69  ? 157 LYS   B NZ  1 
ATOM   1982 N NZ  C LYS   B 2 148 ? 8.962   -4.517  -18.499 0.25 79.70  ? 157 LYS   B NZ  1 
ATOM   1983 N NZ  D LYS   B 2 148 ? 8.962   -4.517  -18.499 0.25 79.70  ? 157 LYS   B NZ  1 
ATOM   1984 N N   . ASN   B 2 149 ? 3.859   -1.555  -22.303 1.00 78.93  ? 158 ASN   B N   1 
ATOM   1985 C CA  . ASN   B 2 149 ? 3.775   -0.632  -23.468 1.00 79.41  ? 158 ASN   B CA  1 
ATOM   1986 C C   . ASN   B 2 149 ? 3.350   0.804   -23.117 1.00 75.79  ? 158 ASN   B C   1 
ATOM   1987 O O   . ASN   B 2 149 ? 3.418   1.653   -24.039 1.00 77.62  ? 158 ASN   B O   1 
ATOM   1988 C CB  . ASN   B 2 149 ? 2.740   -1.134  -24.482 1.00 84.03  ? 158 ASN   B CB  1 
ATOM   1989 C CG  . ASN   B 2 149 ? 2.574   -2.640  -24.509 1.00 84.40  ? 158 ASN   B CG  1 
ATOM   1990 O OD1 . ASN   B 2 149 ? 3.495   -3.385  -24.167 1.00 89.15  ? 158 ASN   B OD1 1 
ATOM   1991 N ND2 . ASN   B 2 149 ? 1.403   -3.094  -24.931 1.00 85.92  ? 158 ASN   B ND2 1 
ATOM   1992 N N   . GLY   B 2 150 ? 2.840   1.061   -21.905 1.00 70.64  ? 159 GLY   B N   1 
ATOM   1993 C CA  . GLY   B 2 150 ? 2.334   2.393   -21.485 1.00 64.65  ? 159 GLY   B CA  1 
ATOM   1994 C C   . GLY   B 2 150 ? 0.823   2.599   -21.664 1.00 61.39  ? 159 GLY   B C   1 
ATOM   1995 O O   . GLY   B 2 150 ? 0.275   3.576   -21.106 1.00 59.90  ? 159 GLY   B O   1 
ATOM   1996 N N   A SER   B 2 151 ? 0.189   1.720   -22.457 0.20 60.63  ? 160 SER   B N   1 
ATOM   1997 N N   B SER   B 2 151 ? 0.195   1.719   -22.457 0.18 61.30  ? 160 SER   B N   1 
ATOM   1998 N N   C SER   B 2 151 ? 0.157   1.716   -22.420 0.31 59.87  ? 160 SER   B N   1 
ATOM   1999 N N   D SER   B 2 151 ? 0.157   1.715   -22.419 0.31 59.87  ? 160 SER   B N   1 
ATOM   2000 C CA  A SER   B 2 151 ? -1.283  1.635   -22.668 0.20 58.65  ? 160 SER   B CA  1 
ATOM   2001 C CA  B SER   B 2 151 ? -1.273  1.615   -22.671 0.18 59.74  ? 160 SER   B CA  1 
ATOM   2002 C CA  C SER   B 2 151 ? -1.324  1.657   -22.576 0.31 57.16  ? 160 SER   B CA  1 
ATOM   2003 C CA  D SER   B 2 151 ? -1.324  1.657   -22.577 0.31 57.16  ? 160 SER   B CA  1 
ATOM   2004 C C   A SER   B 2 151 ? -1.952  1.067   -21.409 0.20 56.90  ? 160 SER   B C   1 
ATOM   2005 C C   B SER   B 2 151 ? -1.947  1.071   -21.404 0.18 57.62  ? 160 SER   B C   1 
ATOM   2006 C C   C SER   B 2 151 ? -1.980  1.218   -21.255 0.31 54.46  ? 160 SER   B C   1 
ATOM   2007 C C   D SER   B 2 151 ? -1.980  1.218   -21.256 0.31 54.46  ? 160 SER   B C   1 
ATOM   2008 O O   A SER   B 2 151 ? -1.234  0.489   -20.564 0.20 56.38  ? 160 SER   B O   1 
ATOM   2009 O O   B SER   B 2 151 ? -1.231  0.510   -20.546 0.18 57.06  ? 160 SER   B O   1 
ATOM   2010 O O   C SER   B 2 151 ? -1.229  0.827   -20.334 0.31 53.92  ? 160 SER   B O   1 
ATOM   2011 O O   D SER   B 2 151 ? -1.230  0.827   -20.334 0.31 53.92  ? 160 SER   B O   1 
ATOM   2012 C CB  A SER   B 2 151 ? -1.618  0.796   -23.879 0.20 59.02  ? 160 SER   B CB  1 
ATOM   2013 C CB  B SER   B 2 151 ? -1.564  0.730   -23.853 0.18 60.72  ? 160 SER   B CB  1 
ATOM   2014 C CB  C SER   B 2 151 ? -1.681  0.716   -23.691 0.31 57.76  ? 160 SER   B CB  1 
ATOM   2015 C CB  D SER   B 2 151 ? -1.681  0.716   -23.692 0.31 57.76  ? 160 SER   B CB  1 
ATOM   2016 O OG  A SER   B 2 151 ? -2.995  0.906   -24.209 0.20 57.66  ? 160 SER   B OG  1 
ATOM   2017 O OG  B SER   B 2 151 ? -0.844  -0.492  -23.740 0.18 60.96  ? 160 SER   B OG  1 
ATOM   2018 O OG  C SER   B 2 151 ? -0.967  -0.505  -23.538 0.31 57.54  ? 160 SER   B OG  1 
ATOM   2019 O OG  D SER   B 2 151 ? -0.968  -0.505  -23.539 0.31 57.55  ? 160 SER   B OG  1 
ATOM   2020 N N   A TYR   B 2 152 ? -3.277  1.216   -21.311 0.20 55.47  ? 161 TYR   B N   1 
ATOM   2021 N N   B TYR   B 2 152 ? -3.273  1.216   -21.311 0.18 55.73  ? 161 TYR   B N   1 
ATOM   2022 N N   C TYR   B 2 152 ? -3.318  1.277   -21.172 0.31 52.09  ? 161 TYR   B N   1 
ATOM   2023 N N   D TYR   B 2 152 ? -3.318  1.278   -21.173 0.31 52.09  ? 161 TYR   B N   1 
ATOM   2024 C CA  A TYR   B 2 152 ? -4.107  0.759   -20.164 0.20 53.72  ? 161 TYR   B CA  1 
ATOM   2025 C CA  B TYR   B 2 152 ? -4.105  0.760   -20.164 0.18 53.83  ? 161 TYR   B CA  1 
ATOM   2026 C CA  C TYR   B 2 152 ? -4.133  0.784   -20.023 0.31 49.77  ? 161 TYR   B CA  1 
ATOM   2027 C CA  D TYR   B 2 152 ? -4.133  0.785   -20.024 0.31 49.77  ? 161 TYR   B CA  1 
ATOM   2028 C C   A TYR   B 2 152 ? -4.827  -0.537  -20.544 0.20 51.00  ? 161 TYR   B C   1 
ATOM   2029 C C   B TYR   B 2 152 ? -4.826  -0.536  -20.544 0.18 51.03  ? 161 TYR   B C   1 
ATOM   2030 C C   C TYR   B 2 152 ? -4.906  -0.466  -20.462 0.31 48.80  ? 161 TYR   B C   1 
ATOM   2031 C C   D TYR   B 2 152 ? -4.906  -0.466  -20.462 0.31 48.79  ? 161 TYR   B C   1 
ATOM   2032 O O   A TYR   B 2 152 ? -5.319  -0.641  -21.686 0.20 50.79  ? 161 TYR   B O   1 
ATOM   2033 O O   B TYR   B 2 152 ? -5.319  -0.640  -21.686 0.18 50.83  ? 161 TYR   B O   1 
ATOM   2034 O O   C TYR   B 2 152 ? -5.507  -0.472  -21.562 0.31 48.47  ? 161 TYR   B O   1 
ATOM   2035 O O   D TYR   B 2 152 ? -5.507  -0.472  -21.563 0.31 48.48  ? 161 TYR   B O   1 
ATOM   2036 C CB  A TYR   B 2 152 ? -5.116  1.837   -19.761 0.20 55.02  ? 161 TYR   B CB  1 
ATOM   2037 C CB  B TYR   B 2 152 ? -5.115  1.838   -19.762 0.18 55.07  ? 161 TYR   B CB  1 
ATOM   2038 C CB  C TYR   B 2 152 ? -5.088  1.866   -19.498 0.31 48.94  ? 161 TYR   B CB  1 
ATOM   2039 C CB  D TYR   B 2 152 ? -5.088  1.866   -19.499 0.31 48.94  ? 161 TYR   B CB  1 
ATOM   2040 C CG  A TYR   B 2 152 ? -5.833  1.575   -18.460 0.20 55.88  ? 161 TYR   B CG  1 
ATOM   2041 C CG  B TYR   B 2 152 ? -5.832  1.575   -18.460 0.18 55.89  ? 161 TYR   B CG  1 
ATOM   2042 C CG  C TYR   B 2 152 ? -5.629  1.666   -18.097 0.31 47.72  ? 161 TYR   B CG  1 
ATOM   2043 C CG  D TYR   B 2 152 ? -5.629  1.667   -18.097 0.31 47.72  ? 161 TYR   B CG  1 
ATOM   2044 C CD1 A TYR   B 2 152 ? -5.241  1.883   -17.247 0.20 56.21  ? 161 TYR   B CD1 1 
ATOM   2045 C CD1 B TYR   B 2 152 ? -5.240  1.883   -17.247 0.18 56.21  ? 161 TYR   B CD1 1 
ATOM   2046 C CD1 C TYR   B 2 152 ? -4.906  2.061   -16.981 0.31 47.51  ? 161 TYR   B CD1 1 
ATOM   2047 C CD1 D TYR   B 2 152 ? -4.906  2.061   -16.982 0.31 47.51  ? 161 TYR   B CD1 1 
ATOM   2048 C CD2 A TYR   B 2 152 ? -7.109  1.031   -18.436 0.20 56.39  ? 161 TYR   B CD2 1 
ATOM   2049 C CD2 B TYR   B 2 152 ? -7.108  1.031   -18.436 0.18 56.37  ? 161 TYR   B CD2 1 
ATOM   2050 C CD2 C TYR   B 2 152 ? -6.899  1.154   -17.877 0.31 46.89  ? 161 TYR   B CD2 1 
ATOM   2051 C CD2 D TYR   B 2 152 ? -6.899  1.154   -17.878 0.31 46.90  ? 161 TYR   B CD2 1 
ATOM   2052 C CE1 A TYR   B 2 152 ? -5.890  1.654   -16.045 0.20 56.26  ? 161 TYR   B CE1 1 
ATOM   2053 C CE1 B TYR   B 2 152 ? -5.890  1.654   -16.045 0.18 56.25  ? 161 TYR   B CE1 1 
ATOM   2054 C CE1 C TYR   B 2 152 ? -5.403  1.907   -15.693 0.31 46.55  ? 161 TYR   B CE1 1 
ATOM   2055 C CE1 D TYR   B 2 152 ? -5.403  1.907   -15.693 0.31 46.55  ? 161 TYR   B CE1 1 
ATOM   2056 C CE2 A TYR   B 2 152 ? -7.773  0.798   -17.241 0.20 56.27  ? 161 TYR   B CE2 1 
ATOM   2057 C CE2 B TYR   B 2 152 ? -7.772  0.798   -17.242 0.18 56.24  ? 161 TYR   B CE2 1 
ATOM   2058 C CE2 C TYR   B 2 152 ? -7.416  1.001   -16.596 0.31 45.82  ? 161 TYR   B CE2 1 
ATOM   2059 C CE2 D TYR   B 2 152 ? -7.416  1.001   -16.597 0.31 45.82  ? 161 TYR   B CE2 1 
ATOM   2060 C CZ  A TYR   B 2 152 ? -7.162  1.109   -16.039 0.20 56.13  ? 161 TYR   B CZ  1 
ATOM   2061 C CZ  B TYR   B 2 152 ? -7.162  1.108   -16.040 0.18 56.11  ? 161 TYR   B CZ  1 
ATOM   2062 C CZ  C TYR   B 2 152 ? -6.665  1.373   -15.490 0.31 45.96  ? 161 TYR   B CZ  1 
ATOM   2063 C CZ  D TYR   B 2 152 ? -6.664  1.373   -15.491 0.31 45.96  ? 161 TYR   B CZ  1 
ATOM   2064 O OH  A TYR   B 2 152 ? -7.805  0.886   -14.852 0.20 56.87  ? 161 TYR   B OH  1 
ATOM   2065 O OH  B TYR   B 2 152 ? -7.805  0.885   -14.853 0.18 56.81  ? 161 TYR   B OH  1 
ATOM   2066 O OH  C TYR   B 2 152 ? -7.149  1.241   -14.205 0.31 44.53  ? 161 TYR   B OH  1 
ATOM   2067 O OH  D TYR   B 2 152 ? -7.149  1.241   -14.206 0.31 44.55  ? 161 TYR   B OH  1 
ATOM   2068 N N   . VAL   B 2 153 ? -4.863  -1.500  -19.618 1.00 47.81  ? 162 VAL   B N   1 
ATOM   2069 C CA  . VAL   B 2 153 ? -5.638  -2.751  -19.802 1.00 43.92  ? 162 VAL   B CA  1 
ATOM   2070 C C   . VAL   B 2 153 ? -6.540  -2.825  -18.578 1.00 40.94  ? 162 VAL   B C   1 
ATOM   2071 O O   . VAL   B 2 153 ? -6.036  -2.830  -17.446 1.00 40.66  ? 162 VAL   B O   1 
ATOM   2072 C CB  . VAL   B 2 153 ? -4.768  -4.009  -19.894 1.00 42.32  ? 162 VAL   B CB  1 
ATOM   2073 C CG1 . VAL   B 2 153 ? -5.654  -5.255  -19.878 1.00 40.89  ? 162 VAL   B CG1 1 
ATOM   2074 C CG2 . VAL   B 2 153 ? -3.917  -3.980  -21.172 1.00 44.27  ? 162 VAL   B CG2 1 
ATOM   2075 N N   A SER   B 2 154 ? -7.858  -2.851  -18.813 0.20 40.75  ? 163 SER   B N   1 
ATOM   2076 N N   B SER   B 2 154 ? -7.858  -2.856  -18.811 0.18 40.73  ? 163 SER   B N   1 
ATOM   2077 N N   C SER   B 2 154 ? -7.836  -2.990  -18.824 0.31 39.88  ? 163 SER   B N   1 
ATOM   2078 N N   D SER   B 2 154 ? -7.836  -2.990  -18.824 0.31 39.87  ? 163 SER   B N   1 
ATOM   2079 C CA  A SER   B 2 154 ? -8.909  -2.863  -17.763 0.20 39.30  ? 163 SER   B CA  1 
ATOM   2080 C CA  B SER   B 2 154 ? -8.910  -2.863  -17.761 0.18 39.30  ? 163 SER   B CA  1 
ATOM   2081 C CA  C SER   B 2 154 ? -8.895  -2.906  -17.796 0.31 37.77  ? 163 SER   B CA  1 
ATOM   2082 C CA  D SER   B 2 154 ? -8.895  -2.906  -17.796 0.31 37.77  ? 163 SER   B CA  1 
ATOM   2083 C C   A SER   B 2 154 ? -9.292  -4.309  -17.448 0.20 38.61  ? 163 SER   B C   1 
ATOM   2084 C C   B SER   B 2 154 ? -9.295  -4.306  -17.437 0.18 38.60  ? 163 SER   B C   1 
ATOM   2085 C C   C SER   B 2 154 ? -9.406  -4.321  -17.548 0.31 36.58  ? 163 SER   B C   1 
ATOM   2086 C C   D SER   B 2 154 ? -9.406  -4.321  -17.548 0.31 36.58  ? 163 SER   B C   1 
ATOM   2087 O O   A SER   B 2 154 ? -9.058  -5.197  -18.289 0.20 38.48  ? 163 SER   B O   1 
ATOM   2088 O O   B SER   B 2 154 ? -9.058  -5.198  -18.274 0.18 38.50  ? 163 SER   B O   1 
ATOM   2089 O O   C SER   B 2 154 ? -9.755  -5.019  -18.534 0.31 36.31  ? 163 SER   B O   1 
ATOM   2090 O O   D SER   B 2 154 ? -9.754  -5.019  -18.534 0.31 36.32  ? 163 SER   B O   1 
ATOM   2091 C CB  A SER   B 2 154 ? -10.119 -2.071  -18.193 0.20 39.73  ? 163 SER   B CB  1 
ATOM   2092 C CB  B SER   B 2 154 ? -10.118 -2.070  -18.195 0.18 39.71  ? 163 SER   B CB  1 
ATOM   2093 C CB  C SER   B 2 154 ? -10.000 -2.004  -18.258 0.31 38.35  ? 163 SER   B CB  1 
ATOM   2094 C CB  D SER   B 2 154 ? -10.000 -2.003  -18.258 0.31 38.34  ? 163 SER   B CB  1 
ATOM   2095 O OG  A SER   B 2 154 ? -11.175 -2.180  -17.195 0.20 38.84  ? 163 SER   B OG  1 
ATOM   2096 O OG  B SER   B 2 154 ? -11.179 -2.179  -17.203 0.18 38.84  ? 163 SER   B OG  1 
ATOM   2097 O OG  C SER   B 2 154 ? -11.036 -1.913  -17.225 0.31 37.17  ? 163 SER   B OG  1 
ATOM   2098 O OG  D SER   B 2 154 ? -11.037 -1.912  -17.226 0.31 37.17  ? 163 SER   B OG  1 
ATOM   2099 N N   A ALA   B 2 155 ? -9.867  -4.526  -16.267 0.20 36.93  ? 164 ALA   B N   1 
ATOM   2100 N N   B ALA   B 2 155 ? -9.872  -4.519  -16.256 0.18 36.95  ? 164 ALA   B N   1 
ATOM   2101 N N   C ALA   B 2 155 ? -9.551  -4.711  -16.279 0.31 34.68  ? 164 ALA   B N   1 
ATOM   2102 N N   D ALA   B 2 155 ? -9.551  -4.710  -16.279 0.31 34.69  ? 164 ALA   B N   1 
ATOM   2103 C CA  A ALA   B 2 155 ? -10.675 -5.739  -16.002 0.20 36.68  ? 164 ALA   B CA  1 
ATOM   2104 C CA  B ALA   B 2 155 ? -10.677 -5.733  -15.988 0.18 36.69  ? 164 ALA   B CA  1 
ATOM   2105 C CA  C ALA   B 2 155 ? -10.494 -5.814  -15.994 0.31 33.85  ? 164 ALA   B CA  1 
ATOM   2106 C CA  D ALA   B 2 155 ? -10.493 -5.814  -15.993 0.31 33.85  ? 164 ALA   B CA  1 
ATOM   2107 C C   A ALA   B 2 155 ? -12.045 -5.533  -16.726 0.20 36.76  ? 164 ALA   B C   1 
ATOM   2108 C C   B ALA   B 2 155 ? -12.052 -5.535  -16.726 0.18 36.75  ? 164 ALA   B C   1 
ATOM   2109 C C   C ALA   B 2 155 ? -11.771 -5.497  -16.665 0.31 34.49  ? 164 ALA   B C   1 
ATOM   2110 C C   D ALA   B 2 155 ? -11.771 -5.497  -16.664 0.31 34.50  ? 164 ALA   B C   1 
ATOM   2111 O O   A ALA   B 2 155 ? -12.341 -4.248  -16.699 0.20 37.86  ? 164 ALA   B O   1 
ATOM   2112 O O   B ALA   B 2 155 ? -12.364 -4.256  -16.695 0.18 37.79  ? 164 ALA   B O   1 
ATOM   2113 O O   C ALA   B 2 155 ? -11.849 -4.297  -16.799 0.31 35.94  ? 164 ALA   B O   1 
ATOM   2114 O O   D ALA   B 2 155 ? -11.849 -4.297  -16.800 0.31 35.93  ? 164 ALA   B O   1 
ATOM   2115 C CB  A ALA   B 2 155 ? -10.817 -5.939  -14.442 0.20 36.27  ? 164 ALA   B CB  1 
ATOM   2116 C CB  B ALA   B 2 155 ? -10.809 -5.937  -14.431 0.18 36.28  ? 164 ALA   B CB  1 
ATOM   2117 C CB  C ALA   B 2 155 ? -10.826 -5.883  -14.439 0.31 33.32  ? 164 ALA   B CB  1 
ATOM   2118 C CB  D ALA   B 2 155 ? -10.823 -5.883  -14.437 0.31 33.33  ? 164 ALA   B CB  1 
ATOM   2119 N N   A ILE   B 2 156 ? -12.781 -6.828  -16.639 0.20 36.71  ? 165 ILE   B N   1 
ATOM   2120 N N   B ILE   B 2 156 ? -12.780 -6.826  -16.632 0.18 36.71  ? 165 ILE   B N   1 
ATOM   2121 N N   C ILE   B 2 156 ? -12.556 -6.884  -16.771 0.31 34.64  ? 165 ILE   B N   1 
ATOM   2122 N N   D ILE   B 2 156 ? -12.556 -6.885  -16.769 0.31 34.64  ? 165 ILE   B N   1 
ATOM   2123 C CA  A ILE   B 2 156 ? -14.263 -6.853  -16.795 0.20 36.48  ? 165 ILE   B CA  1 
ATOM   2124 C CA  B ILE   B 2 156 ? -14.261 -6.851  -16.791 0.18 36.48  ? 165 ILE   B CA  1 
ATOM   2125 C CA  C ILE   B 2 156 ? -14.044 -6.843  -16.834 0.31 34.49  ? 165 ILE   B CA  1 
ATOM   2126 C CA  D ILE   B 2 156 ? -14.044 -6.843  -16.833 0.31 34.49  ? 165 ILE   B CA  1 
ATOM   2127 C C   A ILE   B 2 156 ? -14.848 -6.940  -15.377 0.20 35.48  ? 165 ILE   B C   1 
ATOM   2128 C C   B ILE   B 2 156 ? -14.849 -6.939  -15.375 0.18 35.49  ? 165 ILE   B C   1 
ATOM   2129 C C   C ILE   B 2 156 ? -14.501 -6.949  -15.373 0.31 33.67  ? 165 ILE   B C   1 
ATOM   2130 C C   D ILE   B 2 156 ? -14.502 -6.950  -15.372 0.31 33.68  ? 165 ILE   B C   1 
ATOM   2131 O O   A ILE   B 2 156 ? -15.251 -8.046  -14.937 0.20 35.45  ? 165 ILE   B O   1 
ATOM   2132 O O   B ILE   B 2 156 ? -15.253 -8.046  -14.939 0.18 35.46  ? 165 ILE   B O   1 
ATOM   2133 O O   C ILE   B 2 156 ? -14.387 -8.053  -14.792 0.31 33.88  ? 165 ILE   B O   1 
ATOM   2134 O O   D ILE   B 2 156 ? -14.389 -8.054  -14.792 0.31 33.89  ? 165 ILE   B O   1 
ATOM   2135 C CB  A ILE   B 2 156 ? -14.674 -8.005  -17.727 0.20 37.26  ? 165 ILE   B CB  1 
ATOM   2136 C CB  B ILE   B 2 156 ? -14.673 -8.002  -17.725 0.18 37.26  ? 165 ILE   B CB  1 
ATOM   2137 C CB  C ILE   B 2 156 ? -14.551 -7.997  -17.715 0.31 35.28  ? 165 ILE   B CB  1 
ATOM   2138 C CB  D ILE   B 2 156 ? -14.551 -7.997  -17.714 0.31 35.28  ? 165 ILE   B CB  1 
ATOM   2139 C CG1 A ILE   B 2 156 ? -13.883 -7.913  -19.037 0.20 38.16  ? 165 ILE   B CG1 1 
ATOM   2140 C CG1 B ILE   B 2 156 ? -13.883 -7.911  -19.036 0.18 38.14  ? 165 ILE   B CG1 1 
ATOM   2141 C CG1 C ILE   B 2 156 ? -13.841 -7.965  -19.072 0.31 36.21  ? 165 ILE   B CG1 1 
ATOM   2142 C CG1 D ILE   B 2 156 ? -13.841 -7.966  -19.070 0.31 36.21  ? 165 ILE   B CG1 1 
ATOM   2143 C CG2 A ILE   B 2 156 ? -16.181 -8.001  -17.960 0.20 37.32  ? 165 ILE   B CG2 1 
ATOM   2144 C CG2 B ILE   B 2 156 ? -16.180 -7.999  -17.957 0.18 37.32  ? 165 ILE   B CG2 1 
ATOM   2145 C CG2 C ILE   B 2 156 ? -16.069 -7.955  -17.863 0.31 35.38  ? 165 ILE   B CG2 1 
ATOM   2146 C CG2 D ILE   B 2 156 ? -16.069 -7.955  -17.862 0.31 35.38  ? 165 ILE   B CG2 1 
ATOM   2147 C CD1 A ILE   B 2 156 ? -14.163 -9.023  -20.006 0.20 38.96  ? 165 ILE   B CD1 1 
ATOM   2148 C CD1 B ILE   B 2 156 ? -14.164 -9.022  -20.004 0.18 38.94  ? 165 ILE   B CD1 1 
ATOM   2149 C CD1 C ILE   B 2 156 ? -14.163 -9.140  -19.935 0.31 37.03  ? 165 ILE   B CD1 1 
ATOM   2150 C CD1 D ILE   B 2 156 ? -14.164 -9.139  -19.935 0.31 37.02  ? 165 ILE   B CD1 1 
ATOM   2151 N N   A THR   B 2 157 ? -14.858 -5.806  -14.679 0.20 34.86  ? 166 THR   B N   1 
ATOM   2152 N N   B THR   B 2 157 ? -14.859 -5.807  -14.674 0.18 34.86  ? 166 THR   B N   1 
ATOM   2153 N N   C THR   B 2 157 ? -14.962 -5.835  -14.819 0.31 33.43  ? 166 THR   B N   1 
ATOM   2154 N N   D THR   B 2 157 ? -14.961 -5.835  -14.817 0.31 33.44  ? 166 THR   B N   1 
ATOM   2155 C CA  A THR   B 2 157 ? -15.403 -5.721  -13.288 0.20 34.20  ? 166 THR   B CA  1 
ATOM   2156 C CA  B THR   B 2 157 ? -15.404 -5.722  -13.284 0.18 34.21  ? 166 THR   B CA  1 
ATOM   2157 C CA  C THR   B 2 157 ? -15.378 -5.772  -13.380 0.31 33.19  ? 166 THR   B CA  1 
ATOM   2158 C CA  D THR   B 2 157 ? -15.378 -5.771  -13.379 0.31 33.20  ? 166 THR   B CA  1 
ATOM   2159 C C   A THR   B 2 157 ? -16.921 -5.999  -13.353 0.20 34.19  ? 166 THR   B C   1 
ATOM   2160 C C   B THR   B 2 157 ? -16.921 -5.999  -13.349 0.18 34.19  ? 166 THR   B C   1 
ATOM   2161 C C   C THR   B 2 157 ? -16.918 -5.944  -13.376 0.31 33.83  ? 166 THR   B C   1 
ATOM   2162 C C   D THR   B 2 157 ? -16.918 -5.943  -13.376 0.31 33.83  ? 166 THR   B C   1 
ATOM   2163 O O   A THR   B 2 157 ? -17.665 -5.204  -14.087 0.20 34.29  ? 166 THR   B O   1 
ATOM   2164 O O   B THR   B 2 157 ? -17.665 -5.200  -14.079 0.18 34.30  ? 166 THR   B O   1 
ATOM   2165 O O   C THR   B 2 157 ? -17.672 -4.972  -13.781 0.31 34.55  ? 166 THR   B O   1 
ATOM   2166 O O   D THR   B 2 157 ? -17.672 -4.972  -13.780 0.31 34.54  ? 166 THR   B O   1 
ATOM   2167 C CB  A THR   B 2 157 ? -15.145 -4.344  -12.653 0.20 34.16  ? 166 THR   B CB  1 
ATOM   2168 C CB  B THR   B 2 157 ? -15.142 -4.348  -12.645 0.18 34.15  ? 166 THR   B CB  1 
ATOM   2169 C CB  C THR   B 2 157 ? -14.963 -4.420  -12.764 0.31 33.10  ? 166 THR   B CB  1 
ATOM   2170 C CB  D THR   B 2 157 ? -14.964 -4.420  -12.762 0.31 33.10  ? 166 THR   B CB  1 
ATOM   2171 O OG1 A THR   B 2 157 ? -13.691 -4.020  -13.029 0.20 34.10  ? 166 THR   B OG1 1 
ATOM   2172 O OG1 B THR   B 2 157 ? -13.686 -4.040  -13.003 0.18 34.09  ? 166 THR   B OG1 1 
ATOM   2173 O OG1 C THR   B 2 157 ? -13.424 -4.307  -13.053 0.31 33.21  ? 166 THR   B OG1 1 
ATOM   2174 O OG1 D THR   B 2 157 ? -13.426 -4.303  -13.055 0.31 33.21  ? 166 THR   B OG1 1 
ATOM   2175 C CG2 A THR   B 2 157 ? -15.615 -4.334  -11.181 0.20 33.80  ? 166 THR   B CG2 1 
ATOM   2176 C CG2 B THR   B 2 157 ? -15.618 -4.334  -11.175 0.18 33.80  ? 166 THR   B CG2 1 
ATOM   2177 C CG2 C THR   B 2 157 ? -15.479 -4.330  -11.281 0.31 32.52  ? 166 THR   B CG2 1 
ATOM   2178 C CG2 D THR   B 2 157 ? -15.475 -4.332  -11.278 0.31 32.53  ? 166 THR   B CG2 1 
ATOM   2179 N N   . GLN   B 2 158 ? -17.350 -7.098  -12.633 1.00 34.29  ? 167 GLN   B N   1 
ATOM   2180 C CA  . GLN   B 2 158 ? -18.792 -7.422  -12.436 1.00 33.73  ? 167 GLN   B CA  1 
ATOM   2181 C C   . GLN   B 2 158 ? -19.074 -7.530  -10.905 1.00 33.98  ? 167 GLN   B C   1 
ATOM   2182 O O   . GLN   B 2 158 ? -18.199 -8.058  -10.177 1.00 33.07  ? 167 GLN   B O   1 
ATOM   2183 C CB  . GLN   B 2 158 ? -19.168 -8.683  -13.217 1.00 33.93  ? 167 GLN   B CB  1 
ATOM   2184 C CG  . GLN   B 2 158 ? -20.633 -9.088  -13.163 1.00 33.52  ? 167 GLN   B CG  1 
ATOM   2185 C CD  . GLN   B 2 158 ? -21.543 -8.012  -13.707 1.00 34.03  ? 167 GLN   B CD  1 
ATOM   2186 O OE1 . GLN   B 2 158 ? -21.610 -6.903  -13.191 1.00 33.14  ? 167 GLN   B OE1 1 
ATOM   2187 N NE2 . GLN   B 2 158 ? -22.181 -8.317  -14.844 1.00 32.95  ? 167 GLN   B NE2 1 
ATOM   2188 N N   . GLY   B 2 159 ? -20.258 -7.108  -10.484 1.00 34.12  ? 168 GLY   B N   1 
ATOM   2189 C CA  . GLY   B 2 159 ? -20.694 -7.262  -9.075  1.00 36.17  ? 168 GLY   B CA  1 
ATOM   2190 C C   . GLY   B 2 159 ? -21.527 -8.505  -8.878  1.00 39.23  ? 168 GLY   B C   1 
ATOM   2191 O O   . GLY   B 2 159 ? -21.714 -9.282  -9.713  1.00 38.37  ? 168 GLY   B O   1 
ATOM   2192 N N   . LYS   B 2 160 ? -21.956 -8.788  -7.674  1.00 43.05  ? 169 LYS   B N   1 
ATOM   2193 C CA  . LYS   B 2 160 ? -22.795 -9.978  -7.418  1.00 48.64  ? 169 LYS   B CA  1 
ATOM   2194 C C   . LYS   B 2 160 ? -24.231 -9.468  -7.254  1.00 52.05  ? 169 LYS   B C   1 
ATOM   2195 O O   . LYS   B 2 160 ? -24.402 -8.383  -6.617  1.00 50.75  ? 169 LYS   B O   1 
ATOM   2196 C CB  . LYS   B 2 160 ? -22.251 -10.679 -6.171  1.00 52.52  ? 169 LYS   B CB  1 
ATOM   2197 C CG  . LYS   B 2 160 ? -22.963 -11.973 -5.809  1.00 56.87  ? 169 LYS   B CG  1 
ATOM   2198 C CD  . LYS   B 2 160 ? -22.595 -12.536 -4.457  1.00 59.25  ? 169 LYS   B CD  1 
ATOM   2199 C CE  . LYS   B 2 160 ? -23.630 -13.535 -3.991  1.00 61.52  ? 169 LYS   B CE  1 
ATOM   2200 N NZ  . LYS   B 2 160 ? -23.387 -13.962 -2.596  1.00 65.78  ? 169 LYS   B NZ  1 
ATOM   2201 N N   . ARG   B 2 161 ? -25.217 -10.219 -7.757  1.00 55.17  ? 170 ARG   B N   1 
ATOM   2202 C CA  . ARG   B 2 161 ? -26.673 -9.941  -7.596  1.00 58.99  ? 170 ARG   B CA  1 
ATOM   2203 C C   . ARG   B 2 161 ? -27.215 -10.874 -6.503  1.00 64.46  ? 170 ARG   B C   1 
ATOM   2204 O O   . ARG   B 2 161 ? -27.082 -12.099 -6.673  1.00 65.50  ? 170 ARG   B O   1 
ATOM   2205 C CB  . ARG   B 2 161 ? -27.383 -10.129 -8.950  1.00 60.89  ? 170 ARG   B CB  1 
ATOM   2206 C CG  . ARG   B 2 161 ? -28.838 -9.682  -8.979  1.00 61.70  ? 170 ARG   B CG  1 
ATOM   2207 C CD  . ARG   B 2 161 ? -29.591 -10.156 -10.217 1.00 63.56  ? 170 ARG   B CD  1 
ATOM   2208 N NE  . ARG   B 2 161 ? -31.032 -9.947  -10.068 1.00 65.50  ? 170 ARG   B NE  1 
ATOM   2209 C CZ  . ARG   B 2 161 ? -31.789 -9.093  -10.768 1.00 66.58  ? 170 ARG   B CZ  1 
ATOM   2210 N NH1 . ARG   B 2 161 ? -31.282 -8.334  -11.729 1.00 63.36  ? 170 ARG   B NH1 1 
ATOM   2211 N NH2 . ARG   B 2 161 ? -33.081 -9.015  -10.494 1.00 70.14  ? 170 ARG   B NH2 1 
ATOM   2212 N N   . GLU   B 2 162 ? -27.768 -10.326 -5.410  1.00 68.35  ? 171 GLU   B N   1 
ATOM   2213 C CA  . GLU   B 2 162 ? -28.469 -11.107 -4.351  1.00 72.70  ? 171 GLU   B CA  1 
ATOM   2214 C C   . GLU   B 2 162 ? -29.945 -11.259 -4.738  1.00 72.39  ? 171 GLU   B C   1 
ATOM   2215 O O   . GLU   B 2 162 ? -30.498 -12.357 -4.643  1.00 77.89  ? 171 GLU   B O   1 
ATOM   2216 C CB  . GLU   B 2 162 ? -28.307 -10.415 -2.998  1.00 76.23  ? 171 GLU   B CB  1 
ATOM   2217 C CG  . GLU   B 2 162 ? -26.874 -10.403 -2.484  1.00 79.30  ? 171 GLU   B CG  1 
ATOM   2218 C CD  . GLU   B 2 162 ? -26.532 -11.523 -1.508  1.00 82.84  ? 171 GLU   B CD  1 
ATOM   2219 O OE1 . GLU   B 2 162 ? -25.842 -11.236 -0.506  1.00 85.87  ? 171 GLU   B OE1 1 
ATOM   2220 O OE2 . GLU   B 2 162 ? -26.956 -12.681 -1.748  1.00 84.21  ? 171 GLU   B OE2 1 
HETATM 2221 S S   C DMS   C 3 .   ? -22.066 15.380  -23.727 0.50 102.88 ? 101 DMS   A S   1 
HETATM 2222 S S   D DMS   C 3 .   ? -22.066 15.380  -23.727 0.50 102.88 ? 101 DMS   A S   1 
HETATM 2223 O O   C DMS   C 3 .   ? -20.962 15.766  -24.668 0.50 102.48 ? 101 DMS   A O   1 
HETATM 2224 O O   D DMS   C 3 .   ? -20.962 15.766  -24.668 0.50 102.48 ? 101 DMS   A O   1 
HETATM 2225 C C1  C DMS   C 3 .   ? -23.544 16.135  -24.364 0.50 101.70 ? 101 DMS   A C1  1 
HETATM 2226 C C1  D DMS   C 3 .   ? -23.544 16.135  -24.364 0.50 101.70 ? 101 DMS   A C1  1 
HETATM 2227 C C2  C DMS   C 3 .   ? -21.851 16.392  -22.286 0.50 100.08 ? 101 DMS   A C2  1 
HETATM 2228 C C2  D DMS   C 3 .   ? -21.851 16.392  -22.286 0.50 100.08 ? 101 DMS   A C2  1 
HETATM 2229 S S   A DMS   D 3 .   ? -7.885  5.409   -18.071 0.20 64.38  ? 201 DMS   B S   1 
HETATM 2230 S S   B DMS   D 3 .   ? -7.884  5.408   -18.074 0.18 64.41  ? 201 DMS   B S   1 
HETATM 2231 O O   A DMS   D 3 .   ? -6.489  5.149   -18.574 0.20 65.46  ? 201 DMS   B O   1 
HETATM 2232 O O   B DMS   D 3 .   ? -6.488  5.145   -18.575 0.18 65.46  ? 201 DMS   B O   1 
HETATM 2233 C C1  A DMS   D 3 .   ? -7.916  4.879   -16.383 0.20 64.46  ? 201 DMS   B C1  1 
HETATM 2234 C C1  B DMS   D 3 .   ? -7.916  4.880   -16.385 0.18 64.44  ? 201 DMS   B C1  1 
HETATM 2235 C C2  A DMS   D 3 .   ? -8.915  4.129   -18.749 0.20 64.53  ? 201 DMS   B C2  1 
HETATM 2236 C C2  B DMS   D 3 .   ? -8.915  4.129   -18.750 0.18 64.52  ? 201 DMS   B C2  1 
HETATM 2237 S S   A DMS   E 3 .   ? -18.403 11.044  -0.429  0.50 414.97 ? 202 DMS   B S   1 
HETATM 2238 S S   B DMS   E 3 .   ? -18.403 11.044  -0.429  0.50 414.97 ? 202 DMS   B S   1 
HETATM 2239 O O   A DMS   E 3 .   ? -19.121 9.771   -0.778  0.50 409.95 ? 202 DMS   B O   1 
HETATM 2240 O O   B DMS   E 3 .   ? -19.121 9.771   -0.778  0.50 409.95 ? 202 DMS   B O   1 
HETATM 2241 C C1  A DMS   E 3 .   ? -19.594 12.346  -0.610  0.50 411.42 ? 202 DMS   B C1  1 
HETATM 2242 C C1  B DMS   E 3 .   ? -19.594 12.346  -0.610  0.50 411.42 ? 202 DMS   B C1  1 
HETATM 2243 C C2  A DMS   E 3 .   ? -17.395 11.446  -1.832  0.50 402.11 ? 202 DMS   B C2  1 
HETATM 2244 C C2  B DMS   E 3 .   ? -17.395 11.446  -1.832  0.50 402.11 ? 202 DMS   B C2  1 
HETATM 2245 S S   A DMS   F 3 .   ? -7.368  3.492   -13.358 0.20 111.34 ? 203 DMS   B S   1 
HETATM 2246 S S   B DMS   F 3 .   ? -7.368  3.492   -13.359 0.18 111.25 ? 203 DMS   B S   1 
HETATM 2247 O O   A DMS   F 3 .   ? -6.498  2.316   -13.013 0.20 108.75 ? 203 DMS   B O   1 
HETATM 2248 O O   B DMS   F 3 .   ? -6.499  2.316   -13.014 0.18 108.77 ? 203 DMS   B O   1 
HETATM 2249 C C1  A DMS   F 3 .   ? -8.359  3.809   -11.921 0.20 110.49 ? 203 DMS   B C1  1 
HETATM 2250 C C1  B DMS   F 3 .   ? -8.360  3.808   -11.921 0.18 110.44 ? 203 DMS   B C1  1 
HETATM 2251 C C2  A DMS   F 3 .   ? -6.322  4.922   -13.261 0.20 111.36 ? 203 DMS   B C2  1 
HETATM 2252 C C2  B DMS   F 3 .   ? -6.322  4.922   -13.261 0.18 111.32 ? 203 DMS   B C2  1 
HETATM 2253 N N1  C A1BG4 G 4 .   ? -2.405  7.268   -16.031 0.31 56.57  ? 204 A1BG4 B N1  1 
HETATM 2254 N N1  D A1BG4 G 4 .   ? -2.405  7.267   -16.031 0.31 56.56  ? 204 A1BG4 B N1  1 
HETATM 2255 N N3  C A1BG4 G 4 .   ? -8.868  3.896   -10.195 0.31 45.65  ? 204 A1BG4 B N3  1 
HETATM 2256 N N3  D A1BG4 G 4 .   ? -8.868  3.896   -10.194 0.31 45.65  ? 204 A1BG4 B N3  1 
HETATM 2257 C C4  C A1BG4 G 4 .   ? -5.356  5.177   -15.676 0.31 53.40  ? 204 A1BG4 B C4  1 
HETATM 2258 C C4  D A1BG4 G 4 .   ? -5.356  5.178   -15.676 0.31 53.39  ? 204 A1BG4 B C4  1 
HETATM 2259 C C5  C A1BG4 G 4 .   ? -6.107  5.615   -16.762 0.31 52.49  ? 204 A1BG4 B C5  1 
HETATM 2260 C C5  D A1BG4 G 4 .   ? -6.107  5.615   -16.762 0.31 52.49  ? 204 A1BG4 B C5  1 
HETATM 2261 C C6  C A1BG4 G 4 .   ? -7.449  5.028   -17.072 0.31 50.74  ? 204 A1BG4 B C6  1 
HETATM 2262 C C6  D A1BG4 G 4 .   ? -7.449  5.028   -17.072 0.31 50.74  ? 204 A1BG4 B C6  1 
HETATM 2263 C C7  C A1BG4 G 4 .   ? -7.714  4.607   -18.376 0.31 50.55  ? 204 A1BG4 B C7  1 
HETATM 2264 C C7  D A1BG4 G 4 .   ? -7.713  4.607   -18.376 0.31 50.55  ? 204 A1BG4 B C7  1 
HETATM 2265 C C8  C A1BG4 G 4 .   ? -8.930  4.056   -18.730 0.31 49.98  ? 204 A1BG4 B C8  1 
HETATM 2266 C C8  D A1BG4 G 4 .   ? -8.929  4.056   -18.730 0.31 49.98  ? 204 A1BG4 B C8  1 
HETATM 2267 C C10 C A1BG4 G 4 .   ? -9.693  4.302   -16.489 0.31 48.49  ? 204 A1BG4 B C10 1 
HETATM 2268 C C10 D A1BG4 G 4 .   ? -9.692  4.302   -16.489 0.31 48.49  ? 204 A1BG4 B C10 1 
HETATM 2269 C C13 C A1BG4 G 4 .   ? -8.737  4.463   -12.374 0.31 46.01  ? 204 A1BG4 B C13 1 
HETATM 2270 C C13 D A1BG4 G 4 .   ? -8.737  4.463   -12.374 0.31 46.01  ? 204 A1BG4 B C13 1 
HETATM 2271 C C15 C A1BG4 G 4 .   ? -8.210  5.986   -9.126  0.31 45.88  ? 204 A1BG4 B C15 1 
HETATM 2272 C C15 D A1BG4 G 4 .   ? -8.210  5.987   -9.125  0.31 45.88  ? 204 A1BG4 B C15 1 
HETATM 2273 C C17 C A1BG4 G 4 .   ? -5.511  6.592   -17.556 0.31 54.69  ? 204 A1BG4 B C17 1 
HETATM 2274 C C17 D A1BG4 G 4 .   ? -5.511  6.592   -17.556 0.31 54.67  ? 204 A1BG4 B C17 1 
HETATM 2275 C C1  C A1BG4 G 4 .   ? -1.986  8.538   -16.600 0.31 57.40  ? 204 A1BG4 B C1  1 
HETATM 2276 C C1  D A1BG4 G 4 .   ? -1.986  8.538   -16.599 0.31 57.39  ? 204 A1BG4 B C1  1 
HETATM 2277 C C2  C A1BG4 G 4 .   ? -3.620  6.705   -16.255 0.31 55.21  ? 204 A1BG4 B C2  1 
HETATM 2278 C C2  D A1BG4 G 4 .   ? -3.620  6.705   -16.255 0.31 55.21  ? 204 A1BG4 B C2  1 
HETATM 2279 C C3  C A1BG4 G 4 .   ? -4.118  5.715   -15.403 0.31 54.54  ? 204 A1BG4 B C3  1 
HETATM 2280 C C3  D A1BG4 G 4 .   ? -4.118  5.715   -15.403 0.31 54.53  ? 204 A1BG4 B C3  1 
HETATM 2281 C C9  C A1BG4 G 4 .   ? -9.920  3.902   -17.786 0.31 48.67  ? 204 A1BG4 B C9  1 
HETATM 2282 C C9  D A1BG4 G 4 .   ? -9.919  3.902   -17.786 0.31 48.68  ? 204 A1BG4 B C9  1 
HETATM 2283 C C11 C A1BG4 G 4 .   ? -8.468  4.861   -16.114 0.31 48.80  ? 204 A1BG4 B C11 1 
HETATM 2284 C C11 D A1BG4 G 4 .   ? -8.468  4.861   -16.115 0.31 48.80  ? 204 A1BG4 B C11 1 
HETATM 2285 C C12 C A1BG4 G 4 .   ? -8.357  5.264   -14.677 0.31 47.64  ? 204 A1BG4 B C12 1 
HETATM 2286 C C12 D A1BG4 G 4 .   ? -8.357  5.263   -14.677 0.31 47.64  ? 204 A1BG4 B C12 1 
HETATM 2287 O O1  C A1BG4 G 4 .   ? -7.902  6.354   -14.371 0.31 47.21  ? 204 A1BG4 B O1  1 
HETATM 2288 O O1  D A1BG4 G 4 .   ? -7.902  6.354   -14.371 0.31 47.22  ? 204 A1BG4 B O1  1 
HETATM 2289 N N2  C A1BG4 G 4 .   ? -8.806  4.346   -13.769 0.31 46.14  ? 204 A1BG4 B N2  1 
HETATM 2290 N N2  D A1BG4 G 4 .   ? -8.805  4.346   -13.769 0.31 46.15  ? 204 A1BG4 B N2  1 
HETATM 2291 C C14 C A1BG4 G 4 .   ? -9.024  3.460   -11.428 0.31 45.53  ? 204 A1BG4 B C14 1 
HETATM 2292 C C14 D A1BG4 G 4 .   ? -9.024  3.460   -11.428 0.31 45.53  ? 204 A1BG4 B C14 1 
HETATM 2293 N N4  C A1BG4 G 4 .   ? -8.476  5.201   -10.329 0.31 45.66  ? 204 A1BG4 B N4  1 
HETATM 2294 N N4  D A1BG4 G 4 .   ? -8.476  5.201   -10.329 0.31 45.67  ? 204 A1BG4 B N4  1 
HETATM 2295 C C16 C A1BG4 G 4 .   ? -8.382  5.574   -11.625 0.31 46.61  ? 204 A1BG4 B C16 1 
HETATM 2296 C C16 D A1BG4 G 4 .   ? -8.382  5.574   -11.625 0.31 46.61  ? 204 A1BG4 B C16 1 
HETATM 2297 N N5  C A1BG4 G 4 .   ? -4.307  7.140   -17.329 0.31 55.70  ? 204 A1BG4 B N5  1 
HETATM 2298 N N5  D A1BG4 G 4 .   ? -4.307  7.140   -17.329 0.31 55.69  ? 204 A1BG4 B N5  1 
HETATM 2299 S S   C SO4   H 5 .   ? -18.731 11.211  -0.343  0.50 104.71 ? 205 SO4   B S   1 
HETATM 2300 S S   D SO4   H 5 .   ? -18.731 11.211  -0.343  0.50 104.71 ? 205 SO4   B S   1 
HETATM 2301 O O1  C SO4   H 5 .   ? -19.331 9.912   -0.170  0.50 101.36 ? 205 SO4   B O1  1 
HETATM 2302 O O1  D SO4   H 5 .   ? -19.331 9.912   -0.170  0.50 101.36 ? 205 SO4   B O1  1 
HETATM 2303 O O2  C SO4   H 5 .   ? -17.370 11.059  -0.791  0.50 104.24 ? 205 SO4   B O2  1 
HETATM 2304 O O2  D SO4   H 5 .   ? -17.370 11.059  -0.791  0.50 104.24 ? 205 SO4   B O2  1 
HETATM 2305 O O3  C SO4   H 5 .   ? -19.470 11.962  -1.321  0.50 103.78 ? 205 SO4   B O3  1 
HETATM 2306 O O3  D SO4   H 5 .   ? -19.470 11.962  -1.321  0.50 103.78 ? 205 SO4   B O3  1 
HETATM 2307 O O4  C SO4   H 5 .   ? -18.752 11.919  0.910   0.50 106.68 ? 205 SO4   B O4  1 
HETATM 2308 O O4  D SO4   H 5 .   ? -18.752 11.919  0.910   0.50 106.68 ? 205 SO4   B O4  1 
HETATM 2309 S S   C DMS   I 3 .   ? -4.885  11.343  -16.160 0.31 91.47  ? 206 DMS   B S   1 
HETATM 2310 S S   D DMS   I 3 .   ? -4.886  11.343  -16.160 0.31 91.46  ? 206 DMS   B S   1 
HETATM 2311 O O   C DMS   I 3 .   ? -5.063  9.909   -16.577 0.31 88.78  ? 206 DMS   B O   1 
HETATM 2312 O O   D DMS   I 3 .   ? -5.064  9.909   -16.577 0.31 88.79  ? 206 DMS   B O   1 
HETATM 2313 C C1  C DMS   I 3 .   ? -4.581  11.321  -14.410 0.31 90.05  ? 206 DMS   B C1  1 
HETATM 2314 C C1  D DMS   I 3 .   ? -4.582  11.321  -14.410 0.31 90.05  ? 206 DMS   B C1  1 
HETATM 2315 C C2  C DMS   I 3 .   ? -3.257  11.807  -16.686 0.31 91.95  ? 206 DMS   B C2  1 
HETATM 2316 C C2  D DMS   I 3 .   ? -3.257  11.807  -16.686 0.31 91.94  ? 206 DMS   B C2  1 
HETATM 2317 O O   . HOH   J 6 .   ? -24.086 8.931   -27.508 1.00 41.32  ? 201 HOH   A O   1 
HETATM 2318 O O   A HOH   J 6 .   ? -28.022 -6.202  -28.091 0.20 32.50  ? 202 HOH   A O   1 
HETATM 2319 O O   B HOH   J 6 .   ? -28.022 -6.213  -28.090 0.18 32.35  ? 202 HOH   A O   1 
HETATM 2320 O O   . HOH   J 6 .   ? -2.359  -4.129  -6.535  1.00 55.33  ? 203 HOH   A O   1 
HETATM 2321 O O   . HOH   J 6 .   ? -8.086  0.072   3.577   1.00 51.37  ? 204 HOH   A O   1 
HETATM 2322 O O   . HOH   J 6 .   ? -21.611 -9.090  -34.833 1.00 55.66  ? 205 HOH   A O   1 
HETATM 2323 O O   A HOH   J 6 .   ? -23.192 18.638  -19.537 0.50 54.26  ? 206 HOH   A O   1 
HETATM 2324 O O   B HOH   J 6 .   ? -23.192 18.638  -19.537 0.50 54.26  ? 206 HOH   A O   1 
HETATM 2325 O O   . HOH   J 6 .   ? -3.860  -14.463 -25.457 1.00 42.38  ? 207 HOH   A O   1 
HETATM 2326 O O   . HOH   J 6 .   ? -28.911 15.417  -14.929 1.00 59.35  ? 208 HOH   A O   1 
HETATM 2327 O O   . HOH   J 6 .   ? 6.150   -5.797  -17.029 1.00 85.54  ? 209 HOH   A O   1 
HETATM 2328 O O   . HOH   J 6 .   ? -30.343 12.293  -16.423 1.00 50.27  ? 210 HOH   A O   1 
HETATM 2329 O O   . HOH   J 6 .   ? -30.628 0.218   -23.005 1.00 56.02  ? 211 HOH   A O   1 
HETATM 2330 O O   . HOH   J 6 .   ? -3.654  -4.414  0.291   1.00 53.02  ? 212 HOH   A O   1 
HETATM 2331 O O   . HOH   J 6 .   ? -4.509  -10.310 -5.595  1.00 45.89  ? 213 HOH   A O   1 
HETATM 2332 O O   . HOH   J 6 .   ? -32.047 -0.703  -28.949 1.00 58.96  ? 214 HOH   A O   1 
HETATM 2333 O O   . HOH   J 6 .   ? -8.276  -1.684  6.905   1.00 64.90  ? 215 HOH   A O   1 
HETATM 2334 O O   . HOH   J 6 .   ? -4.188  -0.899  -0.261  1.00 54.61  ? 216 HOH   A O   1 
HETATM 2335 O O   A HOH   J 6 .   ? -26.664 -3.965  -35.097 0.20 35.17  ? 217 HOH   A O   1 
HETATM 2336 O O   B HOH   J 6 .   ? -26.666 -3.968  -35.102 0.18 35.14  ? 217 HOH   A O   1 
HETATM 2337 O O   . HOH   J 6 .   ? -2.913  -9.433  -3.365  1.00 54.77  ? 218 HOH   A O   1 
HETATM 2338 O O   C HOH   J 6 .   ? -4.452  5.058   -7.184  0.31 50.22  ? 219 HOH   A O   1 
HETATM 2339 O O   D HOH   J 6 .   ? -4.452  5.058   -7.186  0.31 50.23  ? 219 HOH   A O   1 
HETATM 2340 O O   . HOH   K 6 .   ? -5.475  2.780   -11.003 1.00 53.39  ? 301 HOH   B O   1 
HETATM 2341 O O   . HOH   K 6 .   ? -33.793 1.347   -15.341 1.00 48.14  ? 302 HOH   B O   1 
HETATM 2342 O O   . HOH   K 6 .   ? -25.724 -8.414  -16.791 1.00 42.26  ? 303 HOH   B O   1 
HETATM 2343 O O   . HOH   K 6 .   ? -12.964 -2.715  -14.822 1.00 33.50  ? 304 HOH   B O   1 
HETATM 2344 O O   . HOH   K 6 .   ? -19.360 -12.315 -25.559 1.00 61.61  ? 305 HOH   B O   1 
HETATM 2345 O O   . HOH   K 6 .   ? -16.452 25.519  -12.704 1.00 60.73  ? 306 HOH   B O   1 
HETATM 2346 O O   . HOH   K 6 .   ? -30.491 12.675  -19.453 1.00 55.85  ? 307 HOH   B O   1 
HETATM 2347 O O   A HOH   K 6 .   ? -19.660 -16.680 -18.542 0.50 72.36  ? 308 HOH   B O   1 
HETATM 2348 O O   B HOH   K 6 .   ? -19.660 -16.680 -18.542 0.50 72.36  ? 308 HOH   B O   1 
HETATM 2349 O O   . HOH   K 6 .   ? -9.322  -6.769  -25.467 1.00 50.83  ? 309 HOH   B O   1 
HETATM 2350 O O   . HOH   K 6 .   ? -9.842  7.186   -6.337  1.00 69.17  ? 310 HOH   B O   1 
HETATM 2351 O O   . HOH   K 6 .   ? -15.375 -10.543 -15.350 1.00 50.69  ? 311 HOH   B O   1 
HETATM 2352 O O   . HOH   K 6 .   ? -21.228 5.641   -32.432 1.00 62.40  ? 312 HOH   B O   1 
HETATM 2353 O O   . HOH   K 6 .   ? -16.257 20.339  -14.275 1.00 45.90  ? 313 HOH   B O   1 
HETATM 2354 O O   . HOH   K 6 .   ? -35.058 3.951   -9.152  1.00 61.30  ? 314 HOH   B O   1 
HETATM 2355 O O   . HOH   K 6 .   ? -27.745 -7.399  -5.696  1.00 56.17  ? 315 HOH   B O   1 
HETATM 2356 O O   . HOH   K 6 .   ? -16.113 -15.038 -16.664 1.00 49.29  ? 316 HOH   B O   1 
HETATM 2357 O O   . HOH   K 6 .   ? -15.345 -4.962  1.441   1.00 44.28  ? 317 HOH   B O   1 
HETATM 2358 O O   . HOH   K 6 .   ? -15.843 -14.190 -30.732 1.00 54.74  ? 318 HOH   B O   1 
HETATM 2359 O O   A HOH   K 6 .   ? -31.577 6.921   -4.770  0.50 63.15  ? 319 HOH   B O   1 
HETATM 2360 O O   B HOH   K 6 .   ? -31.577 6.921   -4.770  0.50 63.15  ? 319 HOH   B O   1 
HETATM 2361 O O   C HOH   K 6 .   ? -23.815 -6.644  -4.678  0.50 47.48  ? 320 HOH   B O   1 
HETATM 2362 O O   D HOH   K 6 .   ? -23.815 -6.644  -4.678  0.50 47.48  ? 320 HOH   B O   1 
HETATM 2363 O O   . HOH   K 6 .   ? -17.823 -10.941 -16.517 1.00 41.11  ? 321 HOH   B O   1 
HETATM 2364 O O   . HOH   K 6 .   ? -17.084 12.596  -5.437  1.00 52.99  ? 322 HOH   B O   1 
HETATM 2365 O O   . HOH   K 6 .   ? -35.265 -5.447  -10.290 1.00 53.78  ? 323 HOH   B O   1 
HETATM 2366 O O   A HOH   K 6 .   ? -20.222 -7.796  -2.704  0.50 68.54  ? 324 HOH   B O   1 
HETATM 2367 O O   B HOH   K 6 .   ? -20.222 -7.796  -2.704  0.50 68.54  ? 324 HOH   B O   1 
HETATM 2368 O O   A HOH   K 6 .   ? -28.739 -4.299  -22.349 0.20 46.52  ? 325 HOH   B O   1 
HETATM 2369 O O   B HOH   K 6 .   ? -28.743 -4.295  -22.349 0.18 46.48  ? 325 HOH   B O   1 
HETATM 2370 O O   . HOH   K 6 .   ? -7.037  -11.229 -5.338  1.00 49.71  ? 326 HOH   B O   1 
HETATM 2371 O O   . HOH   K 6 .   ? -9.296  1.836   -8.464  1.00 52.37  ? 327 HOH   B O   1 
HETATM 2372 O O   . HOH   K 6 .   ? -24.830 12.501  -23.549 1.00 57.08  ? 328 HOH   B O   1 
HETATM 2373 O O   . HOH   K 6 .   ? -6.569  -0.756  -10.710 1.00 45.09  ? 329 HOH   B O   1 
HETATM 2374 O O   . HOH   K 6 .   ? -15.425 8.886   -0.582  1.00 51.64  ? 330 HOH   B O   1 
HETATM 2375 O O   . HOH   K 6 .   ? -12.598 -4.022  -10.302 1.00 40.83  ? 331 HOH   B O   1 
HETATM 2376 O O   . HOH   K 6 .   ? -18.850 25.002  -14.646 1.00 59.71  ? 332 HOH   B O   1 
HETATM 2377 O O   . HOH   K 6 .   ? -29.668 -1.182  -19.260 1.00 49.56  ? 333 HOH   B O   1 
HETATM 2378 O O   . HOH   K 6 .   ? -14.987 16.181  -19.849 1.00 52.39  ? 334 HOH   B O   1 
HETATM 2379 O O   A HOH   K 6 .   ? -21.285 6.681   0.000   0.25 49.65  ? 335 HOH   B O   1 
HETATM 2380 O O   B HOH   K 6 .   ? -21.285 6.681   0.000   0.25 49.65  ? 335 HOH   B O   1 
HETATM 2381 O O   . HOH   K 6 .   ? -7.009  -9.264  -3.086  1.00 44.09  ? 336 HOH   B O   1 
HETATM 2382 O O   A HOH   K 6 .   ? -12.336 1.778   -5.741  0.50 57.01  ? 337 HOH   B O   1 
HETATM 2383 O O   B HOH   K 6 .   ? -12.336 1.778   -5.741  0.50 57.01  ? 337 HOH   B O   1 
HETATM 2384 O O   . HOH   K 6 .   ? -14.218 -12.561 -16.486 1.00 45.11  ? 338 HOH   B O   1 
HETATM 2385 O O   C HOH   K 6 .   ? -21.504 13.834  -1.631  0.50 62.37  ? 339 HOH   B O   1 
HETATM 2386 O O   D HOH   K 6 .   ? -21.504 13.834  -1.631  0.50 62.37  ? 339 HOH   B O   1 
HETATM 2387 O O   . HOH   K 6 .   ? -10.810 11.649  -19.156 1.00 52.94  ? 340 HOH   B O   1 
HETATM 2388 O O   . HOH   K 6 .   ? -21.528 -13.850 -21.893 1.00 48.73  ? 341 HOH   B O   1 
HETATM 2389 O O   . HOH   K 6 .   ? -14.669 -6.767  -1.421  1.00 52.35  ? 342 HOH   B O   1 
HETATM 2390 O O   . HOH   K 6 .   ? -17.076 14.726  -30.744 1.00 59.31  ? 343 HOH   B O   1 
HETATM 2391 O O   . HOH   K 6 .   ? -11.548 -5.339  -8.147  1.00 43.04  ? 344 HOH   B O   1 
HETATM 2392 O O   . HOH   K 6 .   ? -27.759 -6.702  -18.569 1.00 48.85  ? 345 HOH   B O   1 
HETATM 2393 O O   A HOH   K 6 .   ? -32.424 -7.163  -6.865  0.50 56.05  ? 346 HOH   B O   1 
HETATM 2394 O O   B HOH   K 6 .   ? -32.424 -7.163  -6.865  0.50 56.05  ? 346 HOH   B O   1 
HETATM 2395 O O   C HOH   K 6 .   ? -20.426 24.233  -16.869 0.50 51.15  ? 347 HOH   B O   1 
HETATM 2396 O O   D HOH   K 6 .   ? -20.426 24.233  -16.869 0.50 51.15  ? 347 HOH   B O   1 
HETATM 2397 O O   . HOH   K 6 .   ? -2.866  -11.993 -7.081  1.00 45.70  ? 348 HOH   B O   1 
HETATM 2398 O O   . HOH   K 6 .   ? -18.728 14.780  -22.079 1.00 41.58  ? 349 HOH   B O   1 
HETATM 2399 O O   . HOH   K 6 .   ? -20.897 2.415   -32.437 1.00 50.07  ? 350 HOH   B O   1 
HETATM 2400 O O   C HOH   K 6 .   ? -6.784  10.244  -18.980 0.31 56.68  ? 351 HOH   B O   1 
HETATM 2401 O O   D HOH   K 6 .   ? -6.785  10.244  -18.982 0.31 56.68  ? 351 HOH   B O   1 
HETATM 2402 O O   . HOH   K 6 .   ? -8.658  -11.030 -7.503  1.00 60.85  ? 352 HOH   B O   1 
HETATM 2403 O O   C HOH   K 6 .   ? -4.674  -0.896  -24.409 0.31 52.31  ? 353 HOH   B O   1 
HETATM 2404 O O   D HOH   K 6 .   ? -4.674  -0.896  -24.410 0.31 52.31  ? 353 HOH   B O   1 
HETATM 2405 O O   . HOH   K 6 .   ? -25.954 -4.991  -4.057  1.00 42.87  ? 354 HOH   B O   1 
HETATM 2406 O O   A HOH   K 6 .   ? -7.211  -6.511  0.431   0.50 68.44  ? 355 HOH   B O   1 
HETATM 2407 O O   B HOH   K 6 .   ? -7.211  -6.511  0.431   0.50 68.44  ? 355 HOH   B O   1 
HETATM 2408 O O   . HOH   K 6 .   ? -30.808 4.349   -2.704  1.00 48.47  ? 356 HOH   B O   1 
HETATM 2409 O O   A HOH   K 6 .   ? -15.868 -7.159  -8.404  0.20 30.43  ? 357 HOH   B O   1 
HETATM 2410 O O   B HOH   K 6 .   ? -15.868 -7.161  -8.402  0.18 30.38  ? 357 HOH   B O   1 
HETATM 2411 O O   C HOH   K 6 .   ? -17.170 -7.727  -8.103  0.25 35.93  ? 357 HOH   B O   1 
HETATM 2412 O O   D HOH   K 6 .   ? -17.170 -7.727  -8.103  0.25 35.93  ? 357 HOH   B O   1 
HETATM 2413 O O   . HOH   K 6 .   ? -19.649 -5.925  -0.813  1.00 42.34  ? 358 HOH   B O   1 
HETATM 2414 O O   A HOH   K 6 .   ? -19.330 -13.539 -23.071 0.50 49.60  ? 359 HOH   B O   1 
HETATM 2415 O O   B HOH   K 6 .   ? -19.330 -13.539 -23.071 0.50 49.60  ? 359 HOH   B O   1 
HETATM 2416 O O   . HOH   K 6 .   ? -10.205 -18.951 -12.019 1.00 60.95  ? 360 HOH   B O   1 
HETATM 2417 O O   A HOH   K 6 .   ? -21.406 -12.395 -13.220 0.50 58.62  ? 361 HOH   B O   1 
HETATM 2418 O O   B HOH   K 6 .   ? -21.406 -12.395 -13.220 0.50 58.62  ? 361 HOH   B O   1 
HETATM 2419 O O   . HOH   K 6 .   ? -23.977 -15.209 -17.654 1.00 65.13  ? 362 HOH   B O   1 
HETATM 2420 O O   . HOH   K 6 .   ? -10.769 7.597   -13.615 1.00 48.80  ? 363 HOH   B O   1 
HETATM 2421 O O   A HOH   K 6 .   ? -19.382 18.942  -21.298 0.50 88.75  ? 364 HOH   B O   1 
HETATM 2422 O O   B HOH   K 6 .   ? -19.382 18.942  -21.298 0.50 88.75  ? 364 HOH   B O   1 
HETATM 2423 O O   A HOH   K 6 .   ? -30.222 -8.101  -5.451  0.50 66.07  ? 365 HOH   B O   1 
HETATM 2424 O O   B HOH   K 6 .   ? -30.222 -8.101  -5.451  0.50 66.07  ? 365 HOH   B O   1 
HETATM 2425 O O   A HOH   K 6 .   ? -0.551  0.390   -12.986 0.20 33.50  ? 366 HOH   B O   1 
HETATM 2426 O O   B HOH   K 6 .   ? -0.549  0.392   -12.979 0.18 33.46  ? 366 HOH   B O   1 
HETATM 2427 O O   . HOH   K 6 .   ? -16.873 16.116  -21.640 1.00 65.77  ? 367 HOH   B O   1 
HETATM 2428 O O   C HOH   K 6 .   ? -9.795  -16.063 -24.107 0.50 53.77  ? 368 HOH   B O   1 
HETATM 2429 O O   D HOH   K 6 .   ? -9.795  -16.063 -24.107 0.50 53.77  ? 368 HOH   B O   1 
HETATM 2430 O O   A HOH   K 6 .   ? -30.763 -11.807 -27.010 0.25 141.51 ? 369 HOH   B O   1 
HETATM 2431 O O   B HOH   K 6 .   ? -30.763 -11.807 -27.010 0.25 141.51 ? 369 HOH   B O   1 
HETATM 2432 O O   . HOH   K 6 .   ? -1.317  -15.095 -10.032 1.00 63.18  ? 370 HOH   B O   1 
HETATM 2433 O O   . HOH   K 6 .   ? -29.565 -5.831  -1.039  1.00 52.76  ? 371 HOH   B O   1 
HETATM 2434 O O   A HOH   K 6 .   ? -23.460 -7.564  -2.501  0.50 66.76  ? 372 HOH   B O   1 
HETATM 2435 O O   B HOH   K 6 .   ? -23.460 -7.564  -2.501  0.50 66.76  ? 372 HOH   B O   1 
HETATM 2436 O O   . HOH   K 6 .   ? -10.949 11.393  -15.158 1.00 64.32  ? 373 HOH   B O   1 
HETATM 2437 O O   C HOH   K 6 .   ? -21.285 -7.506  0.000   0.50 80.99  ? 374 HOH   B O   1 
HETATM 2438 O O   D HOH   K 6 .   ? -21.285 -7.506  0.000   0.50 80.99  ? 374 HOH   B O   1 
HETATM 2439 O O   A HOH   K 6 .   ? -19.140 -12.340 -13.709 0.50 53.85  ? 375 HOH   B O   1 
HETATM 2440 O O   B HOH   K 6 .   ? -19.140 -12.340 -13.709 0.50 53.85  ? 375 HOH   B O   1 
HETATM 2441 O O   A HOH   K 6 .   ? -20.474 4.108   -0.057  0.50 70.67  ? 376 HOH   B O   1 
HETATM 2442 O O   B HOH   K 6 .   ? -20.474 4.108   -0.057  0.50 70.67  ? 376 HOH   B O   1 
HETATM 2443 O O   . HOH   K 6 .   ? -11.313 -7.650  2.404   1.00 51.79  ? 377 HOH   B O   1 
HETATM 2444 O O   A HOH   K 6 .   ? -8.355  6.804   -10.126 0.20 50.05  ? 378 HOH   B O   1 
HETATM 2445 O O   B HOH   K 6 .   ? -8.359  6.803   -10.128 0.18 50.02  ? 378 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 0.7498 0.7439 1.4660 0.0603  0.3002  0.0374  50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.7385 0.7314 1.4215 0.0671  0.3005  0.0217  50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.7090 0.7075 1.3667 0.0948  0.2965  0.0557  50  ASP   A C   
4    O O   . ASP   A 7   ? 0.7329 0.7318 1.4199 0.1118  0.2965  0.0830  50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.7472 0.7348 1.4723 0.0637  0.3048  -0.0051 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.7761 0.7589 1.4754 0.0504  0.3097  -0.0423 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 0.8131 0.7891 1.5415 0.0324  0.3179  -0.0746 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.8069 0.7920 1.4592 0.0581  0.3069  -0.0396 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.6735 0.6739 1.2753 0.0981  0.2936  0.0552  51  MET   A N   
10   C CA  . MET   A 8   ? 0.6426 0.6461 1.2108 0.1236  0.2899  0.0832  51  MET   A CA  
11   C C   . MET   A 8   ? 0.6228 0.6222 1.1854 0.1345  0.2859  0.0689  51  MET   A C   
12   O O   . MET   A 8   ? 0.6141 0.6111 1.1795 0.1187  0.2878  0.0350  51  MET   A O   
13   C CB  . MET   A 8   ? 0.6347 0.6422 1.1481 0.1211  0.2876  0.0887  51  MET   A CB  
14   C CG  . MET   A 8   ? 0.6340 0.6458 1.1571 0.1123  0.2887  0.1038  51  MET   A CG  
15   S SD  . MET   A 8   ? 0.6325 0.6485 1.0975 0.1125  0.2837  0.1129  51  MET   A SD  
16   C CE  . MET   A 8   ? 0.6323 0.6535 1.1337 0.1026  0.2837  0.1303  51  MET   A CE  
17   N N   . TYR   A 9   ? 0.6018 0.5983 1.1578 0.1601  0.2808  0.0935  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.5924 0.5832 1.1435 0.1745  0.2722  0.0841  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.5876 0.5757 1.0860 0.1979  0.2659  0.1099  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.5908 0.5807 1.0686 0.2052  0.2707  0.1381  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.6032 0.5868 1.2102 0.1824  0.2683  0.0855  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.6201 0.5977 1.2400 0.1983  0.2687  0.1235  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.6197 0.6011 1.2699 0.1867  0.2783  0.1338  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.6442 0.6098 1.2436 0.2246  0.2595  0.1494  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.6390 0.6141 1.3030 0.2003  0.2814  0.1695  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.6652 0.6214 1.2713 0.2384  0.2626  0.1856  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.6595 0.6212 1.3003 0.2259  0.2749  0.1957  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.6821 0.6342 1.3321 0.2380  0.2808  0.2315  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.5848 0.5684 1.0641 0.2086  0.2559  0.0982  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.5950 0.5732 1.0199 0.2313  0.2477  0.1180  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.6163 0.5796 1.0510 0.2551  0.2340  0.1308  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.6114 0.5715 1.0938 0.2517  0.2277  0.1127  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.5825 0.5656 0.9685 0.2243  0.2449  0.0953  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.5814 0.5637 0.9943 0.2159  0.2394  0.0600  53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.5702 0.5628 0.9373 0.2037  0.2556  0.0899  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.5828 0.5657 0.9540 0.2174  0.2336  0.0452  53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.6410 0.5935 1.0324 0.2781  0.2300  0.1623  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.6724 0.6040 1.0523 0.3037  0.2135  0.1786  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.6796 0.6041 0.9914 0.3211  0.2055  0.1869  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.6719 0.6019 0.9444 0.3216  0.2179  0.2022  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.7035 0.6214 1.0893 0.3156  0.2193  0.2147  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.7069 0.6239 1.1604 0.3061  0.2208  0.2113  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.7354 0.6413 1.1920 0.3139  0.2321  0.2488  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 0.7706 0.6672 1.1750 0.3286  0.2386  0.2772  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 0.7456 0.6519 1.2572 0.3048  0.2361  0.2492  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.6923 0.6052 0.9943 0.3343  0.1847  0.1752  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.7134 0.6163 0.9509 0.3523  0.1739  0.1814  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.7509 0.6337 0.9398 0.3739  0.1777  0.2217  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.7725 0.6404 0.9813 0.3811  0.1770  0.2414  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.7275 0.6205 0.9753 0.3616  0.1482  0.1599  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.7472 0.6354 0.9393 0.3734  0.1366  0.1543  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.7508 0.6381 0.9687 0.3740  0.1149  0.1230  55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.7684 0.6539 0.9367 0.3820  0.1057  0.1155  55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.8176 0.6825 0.9225 0.4059  0.0934  0.1370  55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.8730 0.7151 0.9539 0.4240  0.0891  0.1679  55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.8168 0.6811 0.8804 0.4116  0.0856  0.1275  55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.7626 0.6450 0.8925 0.3820  0.1848  0.2336  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.8046 0.6689 0.8826 0.4006  0.1953  0.2704  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.8450 0.6890 0.8538 0.4231  0.1804  0.2750  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.8959 0.7175 0.8557 0.4412  0.1869  0.3046  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.7886 0.6717 0.8638 0.3890  0.2222  0.2818  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.8300 0.6798 0.8324 0.4218  0.1629  0.2474  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.8708 0.7000 0.8101 0.4432  0.1455  0.2494  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.8628 0.7064 0.8015 0.4360  0.1333  0.2174  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.8261 0.6967 0.8074 0.4122  0.1429  0.1946  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.8998 0.7238 0.7869 0.4555  0.1139  0.2164  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.8898 0.7237 0.7611 0.4525  0.1039  0.1911  58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.8885 0.7341 0.7193 0.4495  0.1256  0.2001  58  ASP   A C   
69   O O   . ASP   A 15  ? 0.9157 0.7543 0.7184 0.4572  0.1440  0.2283  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.9352 0.7421 0.7653 0.4755  0.0736  0.1874  58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.9531 0.7497 0.8286 0.4787  0.0459  0.1721  58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.9288 0.7348 0.8629 0.4663  0.0519  0.1700  58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.9969 0.7748 0.8512 0.4943  0.0171  0.1624  58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.8644 0.7253 0.6925 0.4393  0.1232  0.1773  59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.8634 0.7336 0.6528 0.4379  0.1394  0.1838  59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.8925 0.7440 0.6228 0.4588  0.1225  0.1817  59  ILE   A C   
77   O O   . ILE   A 16  ? 0.8752 0.7297 0.6114 0.4553  0.1049  0.1561  59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.8218 0.7200 0.6467 0.4099  0.1505  0.1626  59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.8019 0.7145 0.6782 0.3912  0.1671  0.1672  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.8250 0.7301 0.6113 0.4099  0.1609  0.1672  59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.7606 0.6949 0.6709 0.3624  0.1750  0.1439  59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.9344 0.7661 0.6093 0.4796  0.1295  0.2077  60  THR   A N   
83   N N   B THR   A 17  ? 0.9350 0.7660 0.6096 0.4800  0.1286  0.2073  60  THR   A N   
84   N N   C THR   A 17  ? 0.9343 0.7660 0.6091 0.4796  0.1295  0.2077  60  THR   A N   
85   N N   D THR   A 17  ? 0.9349 0.7660 0.6095 0.4799  0.1287  0.2073  60  THR   A N   
86   C CA  A THR   A 17  ? 0.9801 0.7847 0.5885 0.5044  0.1132  0.2109  60  THR   A CA  
87   C CA  B THR   A 17  ? 0.9766 0.7828 0.5861 0.5033  0.1124  0.2084  60  THR   A CA  
88   C CA  C THR   A 17  ? 0.9800 0.7846 0.5882 0.5044  0.1133  0.2110  60  THR   A CA  
89   C CA  D THR   A 17  ? 0.9764 0.7826 0.5858 0.5034  0.1124  0.2085  60  THR   A CA  
90   C C   A THR   A 17  ? 1.0019 0.8012 0.5573 0.5152  0.1360  0.2323  60  THR   A C   
91   C C   B THR   A 17  ? 1.0023 0.8011 0.5578 0.5154  0.1351  0.2317  60  THR   A C   
92   C C   C THR   A 17  ? 1.0014 0.8005 0.5564 0.5153  0.1361  0.2324  60  THR   A C   
93   C C   D THR   A 17  ? 1.0015 0.8003 0.5569 0.5154  0.1352  0.2318  60  THR   A C   
94   O O   A THR   A 17  ? 1.0091 0.8096 0.5686 0.5143  0.1607  0.2563  60  THR   A O   
95   O O   B THR   A 17  ? 1.0118 0.8103 0.5712 0.5151  0.1586  0.2560  60  THR   A O   
96   O O   C THR   A 17  ? 1.0099 0.8098 0.5683 0.5147  0.1607  0.2566  60  THR   A O   
97   O O   D THR   A 17  ? 1.0114 0.8101 0.5708 0.5150  0.1588  0.2560  60  THR   A O   
98   C CB  A THR   A 17  ? 1.0289 0.7999 0.6172 0.5242  0.0924  0.2221  60  THR   A CB  
99   C CB  B THR   A 17  ? 1.0209 0.7948 0.6130 0.5227  0.0866  0.2136  60  THR   A CB  
100  C CB  C THR   A 17  ? 1.0281 0.7992 0.6164 0.5242  0.0925  0.2222  60  THR   A CB  
101  C CB  D THR   A 17  ? 1.0200 0.7938 0.6120 0.5227  0.0866  0.2136  60  THR   A CB  
102  O OG1 A THR   A 17  ? 1.0597 0.8161 0.6277 0.5324  0.1125  0.2541  60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.9892 0.7741 0.6428 0.5099  0.0677  0.1895  60  THR   A OG1 
104  O OG1 C THR   A 17  ? 1.0588 0.8152 0.6270 0.5324  0.1124  0.2541  60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.9884 0.7734 0.6420 0.5099  0.0677  0.1895  60  THR   A OG1 
106  C CG2 A THR   A 17  ? 1.0091 0.7854 0.6599 0.5142  0.0728  0.2046  60  THR   A CG2 
107  C CG2 B THR   A 17  ? 1.0708 0.8152 0.5951 0.5465  0.0652  0.2123  60  THR   A CG2 
108  C CG2 C THR   A 17  ? 1.0085 0.7849 0.6594 0.5142  0.0728  0.2046  60  THR   A CG2 
109  C CG2 D THR   A 17  ? 1.0701 0.8146 0.5945 0.5465  0.0653  0.2123  60  THR   A CG2 
110  N N   . TRP   A 18  ? 1.0149 0.8073 0.5246 0.5258  0.1286  0.2238  61  TRP   A N   
111  C CA  . TRP   A 18  ? 1.0678 0.8465 0.5181 0.5421  0.1474  0.2435  61  TRP   A CA  
112  C C   . TRP   A 18  ? 1.1599 0.8980 0.5560 0.5665  0.1404  0.2637  61  TRP   A C   
113  O O   . TRP   A 18  ? 1.1950 0.9143 0.5841 0.5748  0.1096  0.2528  61  TRP   A O   
114  C CB  . TRP   A 18  ? 1.0696 0.8498 0.4871 0.5472  0.1391  0.2271  61  TRP   A CB  
115  C CG  . TRP   A 18  ? 1.1172 0.8855 0.4809 0.5627  0.1610  0.2452  61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 1.1870 0.9187 0.4800 0.5882  0.1586  0.2580  61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 1.0984 0.8885 0.4744 0.5543  0.1894  0.2528  61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 1.2099 0.9405 0.4716 0.5957  0.1868  0.2719  61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 1.1564 0.9235 0.4711 0.5758  0.2052  0.2689  61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 1.0446 0.8691 0.4765 0.5309  0.2021  0.2471  61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 1.1533 0.9336 0.4688 0.5750  0.2341  0.2789  61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 1.0430 0.8794 0.4741 0.5303  0.2265  0.2576  61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 1.0904 0.9066 0.4677 0.5522  0.2427  0.2726  61  TRP   A CH2 
124  N N   . GLU   A 19  ? 1.2119 0.9368 0.5785 0.5756  0.1677  0.2920  62  GLU   A N   
125  C CA  . GLU   A 19  ? 1.3189 0.9993 0.6245 0.5982  0.1644  0.3143  62  GLU   A CA  
126  C C   . GLU   A 19  ? 1.3880 1.0466 0.6190 0.6165  0.1841  0.3276  62  GLU   A C   
127  O O   . GLU   A 19  ? 1.3508 1.0266 0.5915 0.6109  0.2189  0.3396  62  GLU   A O   
128  C CB  . GLU   A 19  ? 1.3374 1.0156 0.6749 0.5920  0.1804  0.3371  62  GLU   A CB  
129  C CG  . GLU   A 19  ? 1.3194 1.0153 0.7286 0.5757  0.1590  0.3216  62  GLU   A CG  
130  C CD  . GLU   A 19  ? 1.3658 1.0315 0.7612 0.5882  0.1206  0.3149  62  GLU   A CD  
131  O OE1 . GLU   A 19  ? 1.4559 1.0853 0.8137 0.6029  0.1185  0.3382  62  GLU   A OE1 
132  O OE2 . GLU   A 19  ? 1.3284 1.0055 0.7526 0.5827  0.0926  0.2866  62  GLU   A OE2 
133  N N   A LYS   A 20  ? 1.4486 1.0698 0.6089 0.6378  0.1614  0.3237  63  LYS   A N   
134  N N   B LYS   A 20  ? 1.4482 1.0695 0.6086 0.6378  0.1614  0.3237  63  LYS   A N   
135  N N   C LYS   A 20  ? 1.4631 1.0823 0.6220 0.6384  0.1620  0.3255  63  LYS   A N   
136  N N   D LYS   A 20  ? 1.4630 1.0822 0.6218 0.6384  0.1620  0.3255  63  LYS   A N   
137  C CA  A LYS   A 20  ? 1.5077 1.1007 0.5863 0.6578  0.1774  0.3337  63  LYS   A CA  
138  C CA  B LYS   A 20  ? 1.5077 1.1007 0.5863 0.6578  0.1774  0.3337  63  LYS   A CA  
139  C CA  C LYS   A 20  ? 1.5302 1.1189 0.6051 0.6589  0.1787  0.3374  63  LYS   A CA  
140  C CA  D LYS   A 20  ? 1.5302 1.1189 0.6051 0.6589  0.1787  0.3374  63  LYS   A CA  
141  C C   A LYS   A 20  ? 1.5607 1.1261 0.6012 0.6669  0.2101  0.3676  63  LYS   A C   
142  C C   B LYS   A 20  ? 1.5608 1.1262 0.6013 0.6669  0.2101  0.3676  63  LYS   A C   
143  C C   C LYS   A 20  ? 1.5780 1.1401 0.6197 0.6668  0.2104  0.3715  63  LYS   A C   
144  C C   D LYS   A 20  ? 1.5780 1.1401 0.6197 0.6668  0.2104  0.3715  63  LYS   A C   
145  O O   A LYS   A 20  ? 1.5931 1.1328 0.6251 0.6711  0.1988  0.3818  63  LYS   A O   
146  O O   B LYS   A 20  ? 1.5931 1.1329 0.6252 0.6711  0.1988  0.3818  63  LYS   A O   
147  O O   C LYS   A 20  ? 1.6066 1.1461 0.6465 0.6695  0.1978  0.3842  63  LYS   A O   
148  O O   D LYS   A 20  ? 1.6066 1.1461 0.6465 0.6695  0.1978  0.3842  63  LYS   A O   
149  C CB  A LYS   A 20  ? 1.5623 1.1183 0.5752 0.6776  0.1401  0.3195  63  LYS   A CB  
150  C CB  B LYS   A 20  ? 1.5624 1.1184 0.5753 0.6776  0.1401  0.3195  63  LYS   A CB  
151  C CB  C LYS   A 20  ? 1.5999 1.1485 0.6043 0.6799  0.1423  0.3252  63  LYS   A CB  
152  C CB  D LYS   A 20  ? 1.5999 1.1485 0.6043 0.6799  0.1423  0.3252  63  LYS   A CB  
153  C CG  A LYS   A 20  ? 1.5233 1.1018 0.5520 0.6732  0.1204  0.2887  63  LYS   A CG  
154  C CG  B LYS   A 20  ? 1.5234 1.1019 0.5522 0.6732  0.1204  0.2886  63  LYS   A CG  
155  C CG  C LYS   A 20  ? 1.5669 1.1327 0.6085 0.6733  0.1019  0.2926  63  LYS   A CG  
156  C CG  D LYS   A 20  ? 1.5669 1.1327 0.6084 0.6733  0.1019  0.2926  63  LYS   A CG  
157  C CD  A LYS   A 20  ? 1.5707 1.1156 0.5513 0.6902  0.0774  0.2720  63  LYS   A CD  
158  C CD  B LYS   A 20  ? 1.5708 1.1158 0.5514 0.6902  0.0774  0.2720  63  LYS   A CD  
159  C CD  C LYS   A 20  ? 1.5035 1.1151 0.5961 0.6558  0.1113  0.2720  63  LYS   A CD  
160  C CD  D LYS   A 20  ? 1.5034 1.1150 0.5960 0.6558  0.1113  0.2720  63  LYS   A CD  
161  C CE  A LYS   A 20  ? 1.5462 1.1072 0.5281 0.6891  0.0644  0.2450  63  LYS   A CE  
162  C CE  B LYS   A 20  ? 1.5461 1.1072 0.5281 0.6891  0.0643  0.2450  63  LYS   A CE  
163  C CE  C LYS   A 20  ? 1.5346 1.1374 0.5718 0.6684  0.1203  0.2668  63  LYS   A CE  
164  C CE  D LYS   A 20  ? 1.5345 1.1373 0.5717 0.6684  0.1203  0.2667  63  LYS   A CE  
165  N NZ  A LYS   A 20  ? 1.5732 1.1103 0.5353 0.7003  0.0171  0.2243  63  LYS   A NZ  
166  N NZ  B LYS   A 20  ? 1.5733 1.1104 0.5353 0.7003  0.0171  0.2243  63  LYS   A NZ  
167  N NZ  C LYS   A 20  ? 1.4691 1.1157 0.5570 0.6504  0.1379  0.2548  63  LYS   A NZ  
168  N NZ  D LYS   A 20  ? 1.4691 1.1157 0.5570 0.6504  0.1379  0.2548  63  LYS   A NZ  
169  N N   A ASP   A 21  ? 1.5701 1.1402 0.5915 0.6695  0.2495  0.3800  64  ASP   A N   
170  N N   B ASP   A 21  ? 1.5701 1.1402 0.5915 0.6696  0.2495  0.3800  64  ASP   A N   
171  N N   C ASP   A 21  ? 1.5891 1.1531 0.6082 0.6703  0.2506  0.3855  64  ASP   A N   
172  N N   D ASP   A 21  ? 1.5891 1.1531 0.6081 0.6703  0.2506  0.3856  64  ASP   A N   
173  C CA  A ASP   A 21  ? 1.6168 1.1654 0.6100 0.6757  0.2900  0.4123  64  ASP   A CA  
174  C CA  B ASP   A 21  ? 1.6170 1.1655 0.6101 0.6757  0.2900  0.4123  64  ASP   A CA  
175  C CA  C ASP   A 21  ? 1.6355 1.1737 0.6211 0.6776  0.2885  0.4185  64  ASP   A CA  
176  C CA  D ASP   A 21  ? 1.6356 1.1737 0.6211 0.6776  0.2885  0.4185  64  ASP   A CA  
177  C C   A ASP   A 21  ? 1.5602 1.1354 0.6326 0.6563  0.3029  0.4251  64  ASP   A C   
178  C C   B ASP   A 21  ? 1.5603 1.1355 0.6327 0.6563  0.3029  0.4251  64  ASP   A C   
179  C C   C ASP   A 21  ? 1.5686 1.1377 0.6371 0.6573  0.3073  0.4317  64  ASP   A C   
180  C C   D ASP   A 21  ? 1.5687 1.1378 0.6371 0.6573  0.3073  0.4317  64  ASP   A C   
181  O O   A ASP   A 21  ? 1.5878 1.1366 0.6495 0.6597  0.2936  0.4404  64  ASP   A O   
182  O O   B ASP   A 21  ? 1.5883 1.1370 0.6499 0.6598  0.2937  0.4405  64  ASP   A O   
183  O O   C ASP   A 21  ? 1.6148 1.1572 0.6674 0.6612  0.3186  0.4563  64  ASP   A O   
184  O O   D ASP   A 21  ? 1.6149 1.1572 0.6675 0.6612  0.3185  0.4563  64  ASP   A O   
185  C CB  A ASP   A 21  ? 1.7305 1.2153 0.6244 0.6993  0.2818  0.4288  64  ASP   A CB  
186  C CB  B ASP   A 21  ? 1.7304 1.2151 0.6242 0.6993  0.2818  0.4289  64  ASP   A CB  
187  C CB  C ASP   A 21  ? 1.7441 1.2198 0.6410 0.6989  0.2727  0.4341  64  ASP   A CB  
188  C CB  D ASP   A 21  ? 1.7441 1.2198 0.6410 0.6989  0.2726  0.4341  64  ASP   A CB  
189  C CG  A ASP   A 21  ? 1.7939 1.2477 0.6006 0.7196  0.2809  0.4210  64  ASP   A CG  
190  C CG  B ASP   A 21  ? 1.7937 1.2475 0.6004 0.7196  0.2809  0.4210  64  ASP   A CG  
191  C CG  C ASP   A 21  ? 1.8071 1.2465 0.6184 0.7197  0.2478  0.4200  64  ASP   A CG  
192  C CG  D ASP   A 21  ? 1.8070 1.2464 0.6183 0.7197  0.2478  0.4200  64  ASP   A CG  
193  O OD1 A ASP   A 21  ? 1.8537 1.2814 0.6037 0.7307  0.3187  0.4401  64  ASP   A OD1 
194  O OD1 B ASP   A 21  ? 1.8534 1.2813 0.6037 0.7307  0.3187  0.4400  64  ASP   A OD1 
195  O OD1 C ASP   A 21  ? 1.8422 1.2717 0.6043 0.7297  0.2743  0.4220  64  ASP   A OD1 
196  O OD1 D ASP   A 21  ? 1.8420 1.2716 0.6043 0.7297  0.2743  0.4219  64  ASP   A OD1 
197  O OD2 A ASP   A 21  ? 1.7849 1.2401 0.5821 0.7238  0.2436  0.3952  64  ASP   A OD2 
198  O OD2 B ASP   A 21  ? 1.7849 1.2399 0.5819 0.7238  0.2435  0.3953  64  ASP   A OD2 
199  O OD2 C ASP   A 21  ? 1.8235 1.2439 0.6200 0.7260  0.2017  0.4066  64  ASP   A OD2 
200  O OD2 D ASP   A 21  ? 1.8235 1.2438 0.6199 0.7260  0.2017  0.4066  64  ASP   A OD2 
201  N N   A ALA   A 22  ? 1.4720 1.0963 0.6217 0.6364  0.3204  0.4180  65  ALA   A N   
202  N N   B ALA   A 22  ? 1.4723 1.0966 0.6219 0.6364  0.3204  0.4180  65  ALA   A N   
203  N N   C ALA   A 22  ? 1.4673 1.0882 0.6190 0.6360  0.3103  0.4163  65  ALA   A N   
204  N N   D ALA   A 22  ? 1.4674 1.0883 0.6190 0.6360  0.3103  0.4163  65  ALA   A N   
205  C CA  A ALA   A 22  ? 1.4214 1.0725 0.6461 0.6178  0.3415  0.4317  65  ALA   A CA  
206  C CA  B ALA   A 22  ? 1.4217 1.0728 0.6463 0.6178  0.3415  0.4317  65  ALA   A CA  
207  C CA  C ALA   A 22  ? 1.4046 1.0573 0.6352 0.6161  0.3337  0.4281  65  ALA   A CA  
208  C CA  D ALA   A 22  ? 1.4047 1.0574 0.6353 0.6162  0.3337  0.4281  65  ALA   A CA  
209  C C   A ALA   A 22  ? 1.4320 1.0856 0.6549 0.6196  0.3903  0.4537  65  ALA   A C   
210  C C   B ALA   A 22  ? 1.4324 1.0860 0.6552 0.6196  0.3903  0.4537  65  ALA   A C   
211  C C   C ALA   A 22  ? 1.4122 1.0678 0.6379 0.6185  0.3816  0.4487  65  ALA   A C   
212  C C   D ALA   A 22  ? 1.4124 1.0680 0.6380 0.6185  0.3817  0.4487  65  ALA   A C   
213  O O   A ALA   A 22  ? 1.4582 1.1022 0.6341 0.6320  0.4046  0.4516  65  ALA   A O   
214  O O   B ALA   A 22  ? 1.4585 1.1025 0.6344 0.6320  0.4046  0.4516  65  ALA   A O   
215  O O   C ALA   A 22  ? 1.4260 1.0751 0.6083 0.6299  0.3929  0.4440  65  ALA   A O   
216  O O   D ALA   A 22  ? 1.4263 1.0753 0.6085 0.6299  0.3929  0.4441  65  ALA   A O   
217  C CB  A ALA   A 22  ? 1.3342 1.0337 0.6422 0.5944  0.3262  0.4081  65  ALA   A CB  
218  C CB  B ALA   A 22  ? 1.3343 1.0339 0.6423 0.5944  0.3262  0.4081  65  ALA   A CB  
219  C CB  C ALA   A 22  ? 1.3179 1.0186 0.6280 0.5935  0.3178  0.4029  65  ALA   A CB  
220  C CB  D ALA   A 22  ? 1.3180 1.0187 0.6281 0.5935  0.3179  0.4029  65  ALA   A CB  
221  N N   A GLU   A 23  ? 1.4140 1.0796 0.6887 0.6079  0.4153  0.4731  66  GLU   A N   
222  N N   B GLU   A 23  ? 1.4143 1.0799 0.6890 0.6079  0.4153  0.4731  66  GLU   A N   
223  N N   C GLU   A 23  ? 1.4031 1.0673 0.6740 0.6085  0.4089  0.4700  66  GLU   A N   
224  N N   D GLU   A 23  ? 1.4032 1.0674 0.6741 0.6085  0.4089  0.4700  66  GLU   A N   
225  C CA  A GLU   A 23  ? 1.4255 1.0991 0.7169 0.6067  0.4635  0.4932  66  GLU   A CA  
226  C CA  B GLU   A 23  ? 1.4257 1.0993 0.7171 0.6067  0.4635  0.4931  66  GLU   A CA  
227  C CA  C GLU   A 23  ? 1.4136 1.0883 0.7039 0.6065  0.4566  0.4889  66  GLU   A CA  
228  C CA  D GLU   A 23  ? 1.4137 1.0884 0.7040 0.6065  0.4566  0.4889  66  GLU   A CA  
229  C C   A GLU   A 23  ? 1.3647 1.0822 0.7069 0.5955  0.4686  0.4742  66  GLU   A C   
230  C C   B GLU   A 23  ? 1.3647 1.0822 0.7069 0.5955  0.4686  0.4742  66  GLU   A C   
231  C C   C GLU   A 23  ? 1.3596 1.0756 0.6936 0.5969  0.4610  0.4694  66  GLU   A C   
232  C C   D GLU   A 23  ? 1.3596 1.0756 0.6936 0.5969  0.4610  0.4694  66  GLU   A C   
233  O O   A GLU   A 23  ? 1.2850 1.0400 0.6999 0.5754  0.4522  0.4594  66  GLU   A O   
234  O O   B GLU   A 23  ? 1.2854 1.0403 0.7002 0.5754  0.4522  0.4595  66  GLU   A O   
235  O O   C GLU   A 23  ? 1.2724 1.0233 0.6673 0.5788  0.4377  0.4497  66  GLU   A O   
236  O O   D GLU   A 23  ? 1.2725 1.0235 0.6675 0.5788  0.4377  0.4498  66  GLU   A O   
237  C CB  A GLU   A 23  ? 1.4228 1.1008 0.7670 0.5950  0.4837  0.5159  66  GLU   A CB  
238  C CB  B GLU   A 23  ? 1.4229 1.1009 0.7671 0.5950  0.4837  0.5159  66  GLU   A CB  
239  C CB  C GLU   A 23  ? 1.3998 1.0868 0.7551 0.5918  0.4749  0.5082  66  GLU   A CB  
240  C CB  D GLU   A 23  ? 1.3999 1.0869 0.7551 0.5918  0.4749  0.5082  66  GLU   A CB  
241  C CG  A GLU   A 23  ? 1.4643 1.1336 0.8062 0.5993  0.5356  0.5427  66  GLU   A CG  
242  C CG  B GLU   A 23  ? 1.4643 1.1336 0.8062 0.5993  0.5356  0.5427  66  GLU   A CG  
243  C CG  C GLU   A 23  ? 1.3918 1.1017 0.7957 0.5842  0.5192  0.5224  66  GLU   A CG  
244  C CG  D GLU   A 23  ? 1.3919 1.1017 0.7958 0.5842  0.5192  0.5224  66  GLU   A CG  
245  C CD  A GLU   A 23  ? 1.5164 1.1547 0.8479 0.6015  0.5565  0.5736  66  GLU   A CD  
246  C CD  B GLU   A 23  ? 1.5164 1.1547 0.8479 0.6015  0.5565  0.5736  66  GLU   A CD  
247  C CD  C GLU   A 23  ? 1.3831 1.1039 0.8534 0.5698  0.5373  0.5416  66  GLU   A CD  
248  C CD  D GLU   A 23  ? 1.3831 1.1039 0.8534 0.5698  0.5373  0.5416  66  GLU   A CD  
249  O OE1 A GLU   A 23  ? 1.4925 1.1329 0.8580 0.5920  0.5341  0.5749  66  GLU   A OE1 
250  O OE1 B GLU   A 23  ? 1.4926 1.1329 0.8580 0.5920  0.5340  0.5748  66  GLU   A OE1 
251  O OE1 C GLU   A 23  ? 1.3755 1.0889 0.8588 0.5642  0.5135  0.5424  66  GLU   A OE1 
252  O OE1 D GLU   A 23  ? 1.3755 1.0890 0.8588 0.5642  0.5135  0.5424  66  GLU   A OE1 
253  O OE2 A GLU   A 23  ? 1.5803 1.1905 0.8689 0.6126  0.5967  0.5965  66  GLU   A OE2 
254  O OE2 B GLU   A 23  ? 1.5803 1.1906 0.8690 0.6125  0.5966  0.5964  66  GLU   A OE2 
255  O OE2 C GLU   A 23  ? 1.3823 1.1189 0.8950 0.5643  0.5750  0.5552  66  GLU   A OE2 
256  O OE2 D GLU   A 23  ? 1.3822 1.1188 0.8950 0.5643  0.5749  0.5552  66  GLU   A OE2 
257  N N   . VAL   A 24  ? 1.3908 1.1005 0.6922 0.6085  0.4888  0.4736  67  VAL   A N   
258  C CA  . VAL   A 24  ? 1.3513 1.0967 0.6910 0.6014  0.4913  0.4553  67  VAL   A CA  
259  C C   . VAL   A 24  ? 1.3425 1.1078 0.7365 0.5950  0.5349  0.4720  67  VAL   A C   
260  O O   . VAL   A 24  ? 1.3962 1.1370 0.7509 0.6092  0.5714  0.4902  67  VAL   A O   
261  C CB  . VAL   A 24  ? 1.3955 1.1218 0.6642 0.6194  0.4830  0.4409  67  VAL   A CB  
262  C CG1 . VAL   A 24  ? 1.3479 1.1091 0.6589 0.6120  0.4852  0.4239  67  VAL   A CG1 
263  C CG2 . VAL   A 24  ? 1.4136 1.1204 0.6345 0.6258  0.4384  0.4235  67  VAL   A CG2 
264  N N   A THR   A 25  ? 1.2718 1.0791 0.7539 0.5737  0.5306  0.4649  68  THR   A N   
265  N N   B THR   A 25  ? 1.2719 1.0792 0.7540 0.5737  0.5306  0.4649  68  THR   A N   
266  N N   C THR   A 25  ? 1.2678 1.0752 0.7497 0.5738  0.5305  0.4647  68  THR   A N   
267  N N   D THR   A 25  ? 1.2679 1.0753 0.7497 0.5738  0.5305  0.4647  68  THR   A N   
268  C CA  A THR   A 25  ? 1.2558 1.0871 0.8100 0.5635  0.5655  0.4795  68  THR   A CA  
269  C CA  B THR   A 25  ? 1.2560 1.0873 0.8101 0.5635  0.5655  0.4795  68  THR   A CA  
270  C CA  C THR   A 25  ? 1.2498 1.0816 0.8038 0.5636  0.5653  0.4790  68  THR   A CA  
271  C CA  D THR   A 25  ? 1.2499 1.0816 0.8038 0.5636  0.5653  0.4790  68  THR   A CA  
272  C C   A THR   A 25  ? 1.1828 1.0573 0.8105 0.5452  0.5489  0.4602  68  THR   A C   
273  C C   B THR   A 25  ? 1.1829 1.0575 0.8106 0.5452  0.5489  0.4602  68  THR   A C   
274  C C   C THR   A 25  ? 1.1767 1.0514 0.8032 0.5452  0.5473  0.4591  68  THR   A C   
275  C C   D THR   A 25  ? 1.1768 1.0515 0.8033 0.5452  0.5473  0.4591  68  THR   A C   
276  O O   A THR   A 25  ? 1.1482 1.0302 0.7618 0.5416  0.5144  0.4372  68  THR   A O   
277  O O   B THR   A 25  ? 1.1484 1.0304 0.7620 0.5415  0.5143  0.4372  68  THR   A O   
278  O O   C THR   A 25  ? 1.1423 1.0234 0.7526 0.5420  0.5128  0.4363  68  THR   A O   
279  O O   D THR   A 25  ? 1.1423 1.0235 0.7527 0.5420  0.5128  0.4363  68  THR   A O   
280  C CB  A THR   A 25  ? 1.2666 1.0926 0.8529 0.5552  0.5779  0.5007  68  THR   A CB  
281  C CB  B THR   A 25  ? 1.2667 1.0926 0.8529 0.5552  0.5779  0.5007  68  THR   A CB  
282  C CB  C THR   A 25  ? 1.2622 1.0878 0.8469 0.5559  0.5791  0.5008  68  THR   A CB  
283  C CB  D THR   A 25  ? 1.2623 1.0878 0.8469 0.5559  0.5792  0.5009  68  THR   A CB  
284  O OG1 A THR   A 25  ? 1.2615 1.1074 0.9149 0.5474  0.6141  0.5157  68  THR   A OG1 
285  O OG1 B THR   A 25  ? 1.2613 1.1072 0.9148 0.5474  0.6141  0.5157  68  THR   A OG1 
286  O OG1 C THR   A 25  ? 1.2709 1.1082 0.9071 0.5525  0.6211  0.5193  68  THR   A OG1 
287  O OG1 D THR   A 25  ? 1.2708 1.1082 0.9071 0.5525  0.6212  0.5193  68  THR   A OG1 
288  C CG2 A THR   A 25  ? 1.2154 1.0584 0.8428 0.5372  0.5413  0.4881  68  THR   A CG2 
289  C CG2 B THR   A 25  ? 1.2154 1.0584 0.8428 0.5372  0.5414  0.4881  68  THR   A CG2 
290  C CG2 C THR   A 25  ? 1.2045 1.0535 0.8458 0.5351  0.5466  0.4892  68  THR   A CG2 
291  C CG2 D THR   A 25  ? 1.2045 1.0535 0.8458 0.5351  0.5466  0.4892  68  THR   A CG2 
292  N N   A GLY   A 26  ? 1.1623 1.0618 0.8647 0.5342  0.5724  0.4697  69  GLY   A N   
293  N N   B GLY   A 26  ? 1.1624 1.0620 0.8648 0.5343  0.5725  0.4697  69  GLY   A N   
294  N N   C GLY   A 26  ? 1.1566 1.0572 0.8588 0.5337  0.5697  0.4679  69  GLY   A N   
295  N N   D GLY   A 26  ? 1.1567 1.0573 0.8589 0.5337  0.5697  0.4679  69  GLY   A N   
296  C CA  A GLY   A 26  ? 1.1034 1.0408 0.8790 0.5166  0.5578  0.4545  69  GLY   A CA  
297  C CA  B GLY   A 26  ? 1.1035 1.0409 0.8791 0.5166  0.5578  0.4546  69  GLY   A CA  
298  C CA  C GLY   A 26  ? 1.1000 1.0382 0.8740 0.5157  0.5532  0.4520  69  GLY   A CA  
299  C CA  D GLY   A 26  ? 1.1000 1.0382 0.8741 0.5157  0.5532  0.4520  69  GLY   A CA  
300  C C   A GLY   A 26  ? 1.1095 1.0533 0.8739 0.5259  0.5618  0.4433  69  GLY   A C   
301  C C   B GLY   A 26  ? 1.1094 1.0532 0.8738 0.5259  0.5617  0.4433  69  GLY   A C   
302  C C   C GLY   A 26  ? 1.1084 1.0535 0.8713 0.5243  0.5550  0.4398  69  GLY   A C   
303  C C   D GLY   A 26  ? 1.1084 1.0535 0.8713 0.5243  0.5550  0.4398  69  GLY   A C   
304  O O   A GLY   A 26  ? 1.1484 1.0680 0.8384 0.5443  0.5628  0.4391  69  GLY   A O   
305  O O   B GLY   A 26  ? 1.1483 1.0679 0.8383 0.5442  0.5626  0.4390  69  GLY   A O   
306  O O   C GLY   A 26  ? 1.1414 1.0646 0.8312 0.5407  0.5489  0.4320  69  GLY   A O   
307  O O   D GLY   A 26  ? 1.1413 1.0646 0.8312 0.5406  0.5488  0.4320  69  GLY   A O   
308  N N   A ASN   A 27  ? 1.0741 1.0479 0.9110 0.5138  0.5621  0.4381  70  ASN   A N   
309  N N   B ASN   A 27  ? 1.0741 1.0479 0.9110 0.5137  0.5621  0.4381  70  ASN   A N   
310  N N   C ASN   A 27  ? 1.0816 1.0554 0.9171 0.5136  0.5605  0.4373  70  ASN   A N   
311  N N   D ASN   A 27  ? 1.0816 1.0554 0.9171 0.5136  0.5605  0.4373  70  ASN   A N   
312  C CA  A ASN   A 27  ? 1.0701 1.0547 0.9130 0.5195  0.5608  0.4255  70  ASN   A CA  
313  C CA  B ASN   A 27  ? 1.0701 1.0547 0.9130 0.5195  0.5608  0.4255  70  ASN   A CA  
314  C CA  C ASN   A 27  ? 1.0787 1.0638 0.9221 0.5189  0.5594  0.4249  70  ASN   A CA  
315  C CA  D ASN   A 27  ? 1.0787 1.0638 0.9221 0.5189  0.5594  0.4249  70  ASN   A CA  
316  C C   A ASN   A 27  ? 1.0154 1.0179 0.8755 0.5028  0.5158  0.4023  70  ASN   A C   
317  C C   B ASN   A 27  ? 1.0155 1.0180 0.8757 0.5028  0.5157  0.4023  70  ASN   A C   
318  C C   C ASN   A 27  ? 1.0233 1.0240 0.8761 0.5037  0.5137  0.4010  70  ASN   A C   
319  C C   D ASN   A 27  ? 1.0233 1.0240 0.8761 0.5037  0.5137  0.4009  70  ASN   A C   
320  O O   A ASN   A 27  ? 0.9860 0.9900 0.8472 0.4886  0.4907  0.3963  70  ASN   A O   
321  O O   B ASN   A 27  ? 0.9861 0.9902 0.8476 0.4886  0.4907  0.3963  70  ASN   A O   
322  O O   C ASN   A 27  ? 0.9983 0.9961 0.8368 0.4927  0.4873  0.3935  70  ASN   A O   
323  O O   D ASN   A 27  ? 0.9984 0.9962 0.8369 0.4927  0.4873  0.3935  70  ASN   A O   
324  C CB  A ASN   A 27  ? 1.0762 1.0774 0.9882 0.5202  0.5962  0.4382  70  ASN   A CB  
325  C CB  B ASN   A 27  ? 1.0762 1.0774 0.9881 0.5202  0.5962  0.4382  70  ASN   A CB  
326  C CB  C ASN   A 27  ? 1.0822 1.0872 1.0030 0.5165  0.5908  0.4367  70  ASN   A CB  
327  C CB  D ASN   A 27  ? 1.0822 1.0872 1.0030 0.5165  0.5908  0.4367  70  ASN   A CB  
328  C CG  A ASN   A 27  ? 1.0348 1.0636 1.0400 0.4983  0.5901  0.4426  70  ASN   A CG  
329  C CG  B ASN   A 27  ? 1.0348 1.0635 1.0399 0.4983  0.5901  0.4426  70  ASN   A CG  
330  C CG  C ASN   A 27  ? 1.0381 1.0715 1.0469 0.4927  0.5746  0.4359  70  ASN   A CG  
331  C CG  D ASN   A 27  ? 1.0380 1.0714 1.0469 0.4927  0.5746  0.4359  70  ASN   A CG  
332  O OD1 A ASN   A 27  ? 1.0166 1.0464 1.0302 0.4848  0.5729  0.4436  70  ASN   A OD1 
333  O OD1 B ASN   A 27  ? 1.0165 1.0463 1.0301 0.4848  0.5729  0.4437  70  ASN   A OD1 
334  O OD1 C ASN   A 27  ? 1.0339 1.0670 1.0609 0.4825  0.5744  0.4452  70  ASN   A OD1 
335  O OD1 D ASN   A 27  ? 1.0339 1.0669 1.0608 0.4825  0.5744  0.4452  70  ASN   A OD1 
336  N ND2 A ASN   A 27  ? 1.0221 1.0724 1.0999 0.4948  0.6032  0.4442  70  ASN   A ND2 
337  N ND2 B ASN   A 27  ? 1.0220 1.0723 1.0998 0.4948  0.6032  0.4442  70  ASN   A ND2 
338  N ND2 C ASN   A 27  ? 1.0113 1.0673 1.0742 0.4837  0.5590  0.4245  70  ASN   A ND2 
339  N ND2 D ASN   A 27  ? 1.0112 1.0672 1.0741 0.4837  0.5590  0.4246  70  ASN   A ND2 
340  N N   A SER   A 28  ? 1.0051 1.0177 0.8747 0.5048  0.5066  0.3895  71  SER   A N   
341  N N   B SER   A 28  ? 1.0052 1.0179 0.8749 0.5048  0.5066  0.3895  71  SER   A N   
342  N N   C SER   A 28  ? 1.0042 1.0189 0.8800 0.5030  0.5055  0.3894  71  SER   A N   
343  N N   D SER   A 28  ? 1.0042 1.0189 0.8801 0.5030  0.5055  0.3894  71  SER   A N   
344  C CA  A SER   A 28  ? 0.9687 0.9937 0.8471 0.4902  0.4655  0.3678  71  SER   A CA  
345  C CA  B SER   A 28  ? 0.9688 0.9937 0.8471 0.4902  0.4655  0.3678  71  SER   A CA  
346  C CA  C SER   A 28  ? 0.9694 0.9946 0.8477 0.4896  0.4642  0.3672  71  SER   A CA  
347  C CA  D SER   A 28  ? 0.9695 0.9946 0.8477 0.4896  0.4642  0.3672  71  SER   A CA  
348  C C   A SER   A 28  ? 0.9434 0.9927 0.8983 0.4791  0.4621  0.3660  71  SER   A C   
349  C C   B SER   A 28  ? 0.9434 0.9927 0.8983 0.4791  0.4621  0.3660  71  SER   A C   
350  C C   C SER   A 28  ? 0.9403 0.9898 0.8938 0.4776  0.4580  0.3642  71  SER   A C   
351  C C   D SER   A 28  ? 0.9403 0.9898 0.8939 0.4776  0.4581  0.3642  71  SER   A C   
352  O O   A SER   A 28  ? 0.9514 1.0032 0.9066 0.4872  0.4607  0.3585  71  SER   A O   
353  O O   B SER   A 28  ? 0.9513 1.0031 0.9064 0.4872  0.4607  0.3585  71  SER   A O   
354  O O   C SER   A 28  ? 0.9416 0.9938 0.8923 0.4826  0.4489  0.3537  71  SER   A O   
355  O O   D SER   A 28  ? 0.9416 0.9938 0.8923 0.4826  0.4489  0.3537  71  SER   A O   
356  C CB  A SER   A 28  ? 0.9858 0.9944 0.7944 0.5038  0.4510  0.3527  71  SER   A CB  
357  C CB  B SER   A 28  ? 0.9858 0.9945 0.7944 0.5038  0.4510  0.3527  71  SER   A CB  
358  C CB  C SER   A 28  ? 0.9891 0.9971 0.7963 0.5047  0.4526  0.3533  71  SER   A CB  
359  C CB  D SER   A 28  ? 0.9891 0.9971 0.7964 0.5047  0.4526  0.3533  71  SER   A CB  
360  O OG  A SER   A 28  ? 1.0259 1.0090 0.7644 0.5177  0.4565  0.3561  71  SER   A OG  
361  O OG  B SER   A 28  ? 1.0257 1.0088 0.7642 0.5177  0.4565  0.3561  71  SER   A OG  
362  O OG  C SER   A 28  ? 1.0332 1.0153 0.7718 0.5198  0.4619  0.3586  71  SER   A OG  
363  O OG  D SER   A 28  ? 1.0332 1.0153 0.7717 0.5198  0.4619  0.3586  71  SER   A OG  
364  N N   . PRO   A 29  ? 0.9169 0.9837 0.9406 0.4606  0.4583  0.3720  72  PRO   A N   
365  C CA  . PRO   A 29  ? 0.8987 0.9866 0.9994 0.4509  0.4535  0.3714  72  PRO   A CA  
366  C C   . PRO   A 29  ? 0.8618 0.9546 0.9638 0.4343  0.4088  0.3518  72  PRO   A C   
367  O O   . PRO   A 29  ? 0.8345 0.9215 0.9085 0.4204  0.3838  0.3421  72  PRO   A O   
368  C CB  . PRO   A 29  ? 0.8915 0.9910 1.0564 0.4389  0.4674  0.3862  72  PRO   A CB  
369  C CG  . PRO   A 29  ? 0.8893 0.9769 1.0116 0.4314  0.4566  0.3851  72  PRO   A CG  
370  C CD  . PRO   A 29  ? 0.9164 0.9819 0.9491 0.4488  0.4577  0.3794  72  PRO   A CD  
371  N N   . ARG   A 30  ? 0.8652 0.9661 0.9973 0.4364  0.4008  0.3462  73  ARG   A N   
372  C CA  . ARG   A 30  ? 0.8562 0.9596 0.9962 0.4198  0.3582  0.3301  73  ARG   A CA  
373  C C   . ARG   A 30  ? 0.8122 0.9316 1.0342 0.4007  0.3454  0.3344  73  ARG   A C   
374  O O   . ARG   A 30  ? 0.7925 0.9250 1.0786 0.4067  0.3618  0.3434  73  ARG   A O   
375  C CB  . ARG   A 30  ? 0.8929 0.9929 1.0174 0.4332  0.3531  0.3216  73  ARG   A CB  
376  C CG  . ARG   A 30  ? 0.9406 1.0220 0.9786 0.4476  0.3536  0.3124  73  ARG   A CG  
377  C CD  . ARG   A 30  ? 0.9987 1.0751 1.0193 0.4707  0.3706  0.3103  73  ARG   A CD  
378  N NE  . ARG   A 30  ? 1.0420 1.0983 0.9774 0.4845  0.3708  0.3019  73  ARG   A NE  
379  C CZ  . ARG   A 30  ? 1.0403 1.0863 0.9322 0.4825  0.3417  0.2853  73  ARG   A CZ  
380  N NH1 . ARG   A 30  ? 1.0354 1.0871 0.9553 0.4673  0.3107  0.2762  73  ARG   A NH1 
381  N NH2 . ARG   A 30  ? 1.0321 1.0600 0.8522 0.4955  0.3427  0.2782  73  ARG   A NH2 
382  N N   . LEU   A 31  ? 0.7812 0.8982 1.0014 0.3784  0.3184  0.3278  74  LEU   A N   
383  C CA  . LEU   A 31  ? 0.7528 0.8814 1.0447 0.3593  0.3060  0.3319  74  LEU   A CA  
384  C C   . LEU   A 31  ? 0.7220 0.8436 1.0102 0.3378  0.2598  0.3166  74  LEU   A C   
385  O O   . LEU   A 31  ? 0.7161 0.8229 0.9405 0.3295  0.2412  0.3037  74  LEU   A O   
386  C CB  . LEU   A 31  ? 0.7525 0.8810 1.0440 0.3519  0.3194  0.3388  74  LEU   A CB  
387  C CG  . LEU   A 31  ? 0.7775 0.9100 1.0792 0.3704  0.3647  0.3572  74  LEU   A CG  
388  C CD1 . LEU   A 31  ? 0.7733 0.9043 1.0796 0.3607  0.3721  0.3636  74  LEU   A CD1 
389  C CD2 . LEU   A 31  ? 0.7849 0.9333 1.1642 0.3784  0.3870  0.3699  74  LEU   A CD2 
390  N N   . ASP   A 32  ? 0.6995 0.8297 1.0542 0.3299  0.2426  0.3182  75  ASP   A N   
391  C CA  . ASP   A 32  ? 0.6839 0.8045 1.0450 0.3065  0.1969  0.3067  75  ASP   A CA  
392  C C   . ASP   A 32  ? 0.6506 0.7702 1.0301 0.2854  0.1871  0.3062  75  ASP   A C   
393  O O   . ASP   A 32  ? 0.6451 0.7796 1.0945 0.2851  0.2015  0.3177  75  ASP   A O   
394  C CB  . ASP   A 32  ? 0.7011 0.8297 1.1309 0.3080  0.1810  0.3096  75  ASP   A CB  
395  C CG  . ASP   A 32  ? 0.7212 0.8451 1.1244 0.3234  0.1781  0.3047  75  ASP   A CG  
396  O OD1 . ASP   A 32  ? 0.7391 0.8471 1.0639 0.3233  0.1696  0.2946  75  ASP   A OD1 
397  O OD2 . ASP   A 32  ? 0.7423 0.8780 1.2059 0.3349  0.1843  0.3103  75  ASP   A OD2 
398  N N   . VAL   A 33  ? 0.6301 0.7321 0.9511 0.2681  0.1647  0.2927  76  VAL   A N   
399  C CA  . VAL   A 33  ? 0.6191 0.7174 0.9459 0.2483  0.1584  0.2894  76  VAL   A CA  
400  C C   . VAL   A 33  ? 0.6186 0.6950 0.9123 0.2229  0.1166  0.2733  76  VAL   A C   
401  O O   . VAL   A 33  ? 0.6215 0.6831 0.8632 0.2219  0.0997  0.2639  76  VAL   A O   
402  C CB  . VAL   A 33  ? 0.6127 0.7102 0.8958 0.2542  0.1850  0.2895  76  VAL   A CB  
403  C CG1 . VAL   A 33  ? 0.6160 0.7284 0.9189 0.2794  0.2261  0.3063  76  VAL   A CG1 
404  C CG2 . VAL   A 33  ? 0.6166 0.6967 0.8170 0.2517  0.1749  0.2742  76  VAL   A CG2 
405  N N   . ALA   A 34  ? 0.6112 0.6832 0.9279 0.2029  0.1035  0.2699  77  ALA   A N   
406  C CA  . ALA   A 34  ? 0.6180 0.6646 0.8965 0.1759  0.0677  0.2538  77  ALA   A CA  
407  C C   . ALA   A 34  ? 0.6037 0.6453 0.8568 0.1637  0.0791  0.2458  77  ALA   A C   
408  O O   . ALA   A 34  ? 0.5880 0.6468 0.8814 0.1715  0.1043  0.2555  77  ALA   A O   
409  C CB  . ALA   A 34  ? 0.6298 0.6724 0.9638 0.1626  0.0363  0.2557  77  ALA   A CB  
410  N N   . LEU   A 35  ? 0.6087 0.6263 0.7974 0.1453  0.0623  0.2286  78  LEU   A N   
411  C CA  . LEU   A 35  ? 0.6059 0.6154 0.7659 0.1314  0.0713  0.2167  78  LEU   A CA  
412  C C   . LEU   A 35  ? 0.6298 0.6153 0.7817 0.1024  0.0402  0.2038  78  LEU   A C   
413  O O   . LEU   A 35  ? 0.6525 0.6137 0.7611 0.0897  0.0126  0.1949  78  LEU   A O   
414  C CB  . LEU   A 35  ? 0.6066 0.6066 0.6959 0.1351  0.0812  0.2055  78  LEU   A CB  
415  C CG  . LEU   A 35  ? 0.6053 0.5962 0.6629 0.1219  0.0915  0.1906  78  LEU   A CG  
416  C CD1 . LEU   A 35  ? 0.5894 0.6002 0.6928 0.1315  0.1171  0.1998  78  LEU   A CD1 
417  C CD2 . LEU   A 35  ? 0.6052 0.5874 0.6007 0.1263  0.0991  0.1793  78  LEU   A CD2 
418  N N   . ASP   A 36  ? 0.6233 0.6136 0.8165 0.0930  0.0432  0.2041  79  ASP   A N   
419  C CA  . ASP   A 36  ? 0.6476 0.6147 0.8398 0.0661  0.0137  0.1923  79  ASP   A CA  
420  C C   . ASP   A 36  ? 0.6596 0.6048 0.7893 0.0471  0.0179  0.1714  79  ASP   A C   
421  O O   . ASP   A 36  ? 0.6323 0.5841 0.7306 0.0561  0.0432  0.1673  79  ASP   A O   
422  C CB  . ASP   A 36  ? 0.6381 0.6213 0.9134 0.0662  0.0129  0.2029  79  ASP   A CB  
423  C CG  . ASP   A 36  ? 0.6230 0.6192 0.9247 0.0663  0.0396  0.2027  79  ASP   A CG  
424  O OD1 . ASP   A 36  ? 0.6176 0.6100 0.8738 0.0660  0.0582  0.1932  79  ASP   A OD1 
425  O OD2 . ASP   A 36  ? 0.6173 0.6267 0.9889 0.0664  0.0406  0.2119  79  ASP   A OD2 
426  N N   . GLU   A 37  ? 0.6864 0.6046 0.7990 0.0213  -0.0066 0.1577  80  GLU   A N   
427  C CA  . GLU   A 37  ? 0.7093 0.6013 0.7589 -0.0001 -0.0037 0.1352  80  GLU   A CA  
428  C C   . GLU   A 37  ? 0.6844 0.5942 0.7614 0.0036  0.0268  0.1317  80  GLU   A C   
429  O O   . GLU   A 37  ? 0.6856 0.5830 0.7163 -0.0059 0.0401  0.1147  80  GLU   A O   
430  C CB  . GLU   A 37  ? 0.7539 0.6089 0.7766 -0.0282 -0.0383 0.1222  80  GLU   A CB  
431  C CG  . GLU   A 37  ? 0.7873 0.6083 0.7308 -0.0516 -0.0360 0.0983  80  GLU   A CG  
432  C CD  . GLU   A 37  ? 0.8413 0.6180 0.7428 -0.0804 -0.0706 0.0850  80  GLU   A CD  
433  O OE1 . GLU   A 37  ? 0.8482 0.6210 0.7849 -0.0904 -0.0817 0.0821  80  GLU   A OE1 
434  O OE2 . GLU   A 37  ? 0.8755 0.6200 0.7081 -0.0925 -0.0869 0.0781  80  GLU   A OE2 
435  N N   . SER   A 38  ? 0.6647 0.6011 0.8158 0.0165  0.0377  0.1471  81  SER   A N   
436  C CA  . SER   A 38  ? 0.6464 0.6004 0.8319 0.0224  0.0658  0.1477  81  SER   A CA  
437  C C   . SER   A 38  ? 0.6187 0.5951 0.8016 0.0476  0.0961  0.1583  81  SER   A C   
438  O O   . SER   A 38  ? 0.6012 0.5905 0.8097 0.0545  0.1186  0.1605  81  SER   A O   
439  C CB  . SER   A 38  ? 0.6429 0.6126 0.9064 0.0248  0.0642  0.1607  81  SER   A CB  
440  O OG  . SER   A 38  ? 0.6783 0.6248 0.9430 0.0006  0.0354  0.1483  81  SER   A OG  
441  N N   . GLY   A 39  ? 0.6176 0.5961 0.7698 0.0608  0.0951  0.1643  82  GLY   A N   
442  C CA  . GLY   A 39  ? 0.6026 0.5989 0.7462 0.0858  0.1203  0.1742  82  GLY   A CA  
443  C C   . GLY   A 39  ? 0.5860 0.6090 0.7910 0.1089  0.1386  0.1989  82  GLY   A C   
444  O O   . GLY   A 39  ? 0.5674 0.6022 0.7707 0.1269  0.1629  0.2065  82  GLY   A O   
445  N N   . ASP   A 40  ? 0.5944 0.6246 0.8524 0.1075  0.1277  0.2105  83  ASP   A N   
446  C CA  . ASP   A 40  ? 0.5868 0.6412 0.9062 0.1286  0.1464  0.2346  83  ASP   A CA  
447  C C   . ASP   A 40  ? 0.5874 0.6462 0.8977 0.1431  0.1416  0.2431  83  ASP   A C   
448  O O   . ASP   A 40  ? 0.5906 0.6377 0.8957 0.1313  0.1123  0.2368  83  ASP   A O   
449  C CB  . ASP   A 40  ? 0.5980 0.6593 0.9906 0.1193  0.1389  0.2417  83  ASP   A CB  
450  C CG  . ASP   A 40  ? 0.6093 0.6657 1.0169 0.1044  0.1422  0.2328  83  ASP   A CG  
451  O OD1 . ASP   A 40  ? 0.6041 0.6629 0.9936 0.1109  0.1637  0.2316  83  ASP   A OD1 
452  O OD2 . ASP   A 40  ? 0.6491 0.6976 1.0869 0.0862  0.1211  0.2263  83  ASP   A OD2 
453  N N   . PHE   A 41  ? 0.5754 0.6482 0.8832 0.1679  0.1681  0.2569  84  PHE   A N   
454  C CA  . PHE   A 41  ? 0.5751 0.6555 0.8876 0.1848  0.1691  0.2672  84  PHE   A CA  
455  C C   . PHE   A 41  ? 0.5830 0.6805 0.9773 0.1903  0.1750  0.2841  84  PHE   A C   
456  O O   . PHE   A 41  ? 0.5788 0.6853 1.0181 0.1888  0.1902  0.2922  84  PHE   A O   
457  C CB  . PHE   A 41  ? 0.5616 0.6475 0.8380 0.2092  0.1959  0.2745  84  PHE   A CB  
458  C CG  . PHE   A 41  ? 0.5539 0.6246 0.7543 0.2077  0.1885  0.2585  84  PHE   A CG  
459  C CD1 . PHE   A 41  ? 0.5564 0.6175 0.7208 0.2068  0.1697  0.2504  84  PHE   A CD1 
460  C CD2 . PHE   A 41  ? 0.5430 0.6093 0.7124 0.2083  0.2011  0.2521  84  PHE   A CD2 
461  C CE1 . PHE   A 41  ? 0.5574 0.6048 0.6558 0.2056  0.1648  0.2360  84  PHE   A CE1 
462  C CE2 . PHE   A 41  ? 0.5433 0.5971 0.6504 0.2080  0.1957  0.2373  84  PHE   A CE2 
463  C CZ  . PHE   A 41  ? 0.5513 0.5959 0.6230 0.2062  0.1784  0.2292  84  PHE   A CZ  
464  N N   . SER   A 42  ? 0.5989 0.7006 1.0145 0.1968  0.1641  0.2887  85  SER   A N   
465  C CA  . SER   A 42  ? 0.6154 0.7350 1.1156 0.2042  0.1710  0.3042  85  SER   A CA  
466  C C   . SER   A 42  ? 0.6332 0.7606 1.1364 0.2242  0.1793  0.3115  85  SER   A C   
467  O O   . SER   A 42  ? 0.6347 0.7495 1.0792 0.2252  0.1637  0.3013  85  SER   A O   
468  C CB  . SER   A 42  ? 0.6242 0.7374 1.1681 0.1825  0.1351  0.2974  85  SER   A CB  
469  O OG  . SER   A 42  ? 0.6319 0.7236 1.1248 0.1692  0.0982  0.2820  85  SER   A OG  
470  N N   . LEU   A 43  ? 0.6541 0.8008 1.2250 0.2393  0.2045  0.3281  86  LEU   A N   
471  C CA  . LEU   A 43  ? 0.6784 0.8338 1.2639 0.2589  0.2157  0.3346  86  LEU   A CA  
472  C C   . LEU   A 43  ? 0.6943 0.8481 1.3232 0.2491  0.1778  0.3287  86  LEU   A C   
473  O O   . LEU   A 43  ? 0.6891 0.8490 1.3881 0.2371  0.1634  0.3312  86  LEU   A O   
474  C CB  . LEU   A 43  ? 0.6868 0.8616 1.3308 0.2775  0.2605  0.3540  86  LEU   A CB  
475  C CG  . LEU   A 43  ? 0.7045 0.8768 1.2978 0.2922  0.2994  0.3625  86  LEU   A CG  
476  C CD1 . LEU   A 43  ? 0.7239 0.9110 1.3786 0.3055  0.3428  0.3828  86  LEU   A CD1 
477  C CD2 . LEU   A 43  ? 0.7180 0.8803 1.2330 0.3084  0.3055  0.3570  86  LEU   A CD2 
478  N N   . VAL   A 44  ? 0.7274 0.8727 1.3175 0.2552  0.1625  0.3216  87  VAL   A N   
479  C CA  . VAL   A 44  ? 0.7638 0.9059 1.3920 0.2507  0.1272  0.3174  87  VAL   A CA  
480  C C   . VAL   A 44  ? 0.7979 0.9587 1.4770 0.2746  0.1544  0.3278  87  VAL   A C   
481  O O   . VAL   A 44  ? 0.8178 0.9753 1.4443 0.2902  0.1696  0.3261  87  VAL   A O   
482  C CB  . VAL   A 44  ? 0.7694 0.8862 1.3158 0.2409  0.0923  0.3023  87  VAL   A CB  
483  C CG1 . VAL   A 44  ? 0.7848 0.8950 1.3638 0.2384  0.0555  0.2993  87  VAL   A CG1 
484  C CG2 . VAL   A 44  ? 0.7679 0.8641 1.2602 0.2168  0.0702  0.2906  87  VAL   A CG2 
485  N N   . GLU   A 45  ? 0.8355 1.0145 1.6140 0.2776  0.1615  0.3372  88  GLU   A N   
486  C CA  . GLU   A 45  ? 0.8782 1.0743 1.7144 0.2991  0.1860  0.3449  88  GLU   A CA  
487  C C   . GLU   A 45  ? 0.8870 1.0780 1.7615 0.2943  0.1418  0.3372  88  GLU   A C   
488  O O   . GLU   A 45  ? 0.8988 1.0706 1.7075 0.2905  0.1122  0.3267  88  GLU   A O   
489  C CB  . GLU   A 45  ? 0.9020 1.1215 1.8300 0.3065  0.2250  0.3598  88  GLU   A CB  
490  C CG  . GLU   A 45  ? 0.9169 1.1375 1.8114 0.3074  0.2615  0.3685  88  GLU   A CG  
491  C CD  . GLU   A 45  ? 0.9428 1.1547 1.7445 0.3239  0.2929  0.3697  88  GLU   A CD  
492  O OE1 . GLU   A 45  ? 0.9579 1.1520 1.6732 0.3176  0.2703  0.3583  88  GLU   A OE1 
493  O OE2 . GLU   A 45  ? 0.9789 1.2001 1.7951 0.3427  0.3400  0.3818  88  GLU   A OE2 
494  N N   . GLY   B 7   ? 0.7997 0.8309 0.6347 0.1103  0.0809  -0.1094 16  GLY   B N   
495  C CA  . GLY   B 7   ? 0.7960 0.8160 0.6226 0.1233  0.0778  -0.0932 16  GLY   B CA  
496  C C   . GLY   B 7   ? 0.7875 0.8042 0.5979 0.1335  0.0691  -0.0860 16  GLY   B C   
497  O O   . GLY   B 7   ? 0.7795 0.8017 0.5898 0.1316  0.0648  -0.0939 16  GLY   B O   
498  N N   . GLU   B 8   ? 0.7601 0.7693 0.5584 0.1443  0.0665  -0.0718 17  GLU   B N   
499  C CA  . GLU   B 8   ? 0.7568 0.7632 0.5369 0.1553  0.0579  -0.0645 17  GLU   B CA  
500  C C   . GLU   B 8   ? 0.7268 0.7332 0.4870 0.1469  0.0546  -0.0663 17  GLU   B C   
501  O O   . GLU   B 8   ? 0.7108 0.7146 0.4622 0.1411  0.0581  -0.0617 17  GLU   B O   
502  C CB  . GLU   B 8   ? 0.7552 0.7558 0.5290 0.1690  0.0576  -0.0488 17  GLU   B CB  
503  C CG  . GLU   B 8   ? 0.7808 0.7807 0.5376 0.1825  0.0487  -0.0427 17  GLU   B CG  
504  C CD  . GLU   B 8   ? 0.7837 0.7809 0.5354 0.1971  0.0491  -0.0269 17  GLU   B CD  
505  O OE1 . GLU   B 8   ? 0.7509 0.7452 0.5089 0.1951  0.0564  -0.0189 17  GLU   B OE1 
506  O OE2 . GLU   B 8   ? 0.8472 0.8461 0.5895 0.2105  0.0420  -0.0226 17  GLU   B OE2 
507  N N   A THR   B 9   ? 0.7281 0.7373 0.4829 0.1462  0.0477  -0.0725 18  THR   B N   
508  N N   B THR   B 9   ? 0.7254 0.7346 0.4806 0.1463  0.0477  -0.0726 18  THR   B N   
509  N N   C THR   B 9   ? 0.7281 0.7373 0.4829 0.1462  0.0477  -0.0725 18  THR   B N   
510  N N   D THR   B 9   ? 0.7254 0.7346 0.4806 0.1463  0.0477  -0.0726 18  THR   B N   
511  C CA  A THR   B 9   ? 0.7305 0.7397 0.4700 0.1374  0.0436  -0.0748 18  THR   B CA  
512  C CA  B THR   B 9   ? 0.7259 0.7355 0.4666 0.1372  0.0435  -0.0756 18  THR   B CA  
513  C CA  C THR   B 9   ? 0.7305 0.7397 0.4700 0.1374  0.0436  -0.0748 18  THR   B CA  
514  C CA  D THR   B 9   ? 0.7259 0.7355 0.4666 0.1372  0.0435  -0.0756 18  THR   B CA  
515  C C   A THR   B 9   ? 0.7233 0.7285 0.4480 0.1489  0.0332  -0.0707 18  THR   B C   
516  C C   B THR   B 9   ? 0.7208 0.7255 0.4446 0.1490  0.0337  -0.0697 18  THR   B C   
517  C C   C THR   B 9   ? 0.7233 0.7285 0.4480 0.1489  0.0332  -0.0707 18  THR   B C   
518  C C   D THR   B 9   ? 0.7208 0.7255 0.4446 0.1490  0.0337  -0.0697 18  THR   B C   
519  O O   A THR   B 9   ? 0.7237 0.7283 0.4390 0.1429  0.0279  -0.0736 18  THR   B O   
520  O O   B THR   B 9   ? 0.7232 0.7259 0.4344 0.1435  0.0294  -0.0701 18  THR   B O   
521  O O   C THR   B 9   ? 0.7237 0.7283 0.4390 0.1429  0.0279  -0.0736 18  THR   B O   
522  O O   D THR   B 9   ? 0.7232 0.7259 0.4344 0.1435  0.0294  -0.0701 18  THR   B O   
523  C CB  A THR   B 9   ? 0.7354 0.7527 0.4848 0.1233  0.0452  -0.0870 18  THR   B CB  
524  C CB  B THR   B 9   ? 0.7272 0.7451 0.4788 0.1256  0.0437  -0.0882 18  THR   B CB  
525  C CB  C THR   B 9   ? 0.7354 0.7527 0.4848 0.1233  0.0452  -0.0870 18  THR   B CB  
526  C CB  D THR   B 9   ? 0.7272 0.7451 0.4788 0.1256  0.0437  -0.0882 18  THR   B CB  
527  O OG1 A THR   B 9   ? 0.7428 0.7649 0.5077 0.1162  0.0546  -0.0920 18  THR   B OG1 
528  O OG1 B THR   B 9   ? 0.7330 0.7532 0.4925 0.1342  0.0375  -0.0924 18  THR   B OG1 
529  O OG1 C THR   B 9   ? 0.7428 0.7649 0.5077 0.1162  0.0546  -0.0920 18  THR   B OG1 
530  O OG1 D THR   B 9   ? 0.7330 0.7532 0.4925 0.1342  0.0375  -0.0924 18  THR   B OG1 
531  C CG2 A THR   B 9   ? 0.7395 0.7574 0.4760 0.1113  0.0431  -0.0877 18  THR   B CG2 
532  C CG2 B THR   B 9   ? 0.7291 0.7539 0.4974 0.1151  0.0533  -0.0958 18  THR   B CG2 
533  C CG2 C THR   B 9   ? 0.7395 0.7574 0.4760 0.1113  0.0431  -0.0877 18  THR   B CG2 
534  C CG2 D THR   B 9   ? 0.7291 0.7539 0.4974 0.1151  0.0533  -0.0958 18  THR   B CG2 
535  N N   . THR   B 10  ? 0.7182 0.7215 0.4417 0.1649  0.0301  -0.0644 19  THR   B N   
536  C CA  . THR   B 10  ? 0.7016 0.7024 0.4093 0.1776  0.0202  -0.0608 19  THR   B CA  
537  C C   . THR   B 10  ? 0.6602 0.6559 0.3494 0.1769  0.0196  -0.0539 19  THR   B C   
538  O O   . THR   B 10  ? 0.6632 0.6570 0.3509 0.1763  0.0267  -0.0460 19  THR   B O   
539  C CB  . THR   B 10  ? 0.7077 0.7095 0.4165 0.1953  0.0179  -0.0541 19  THR   B CB  
540  O OG1 . THR   B 10  ? 0.7364 0.7424 0.4656 0.1948  0.0205  -0.0591 19  THR   B OG1 
541  C CG2 . THR   B 10  ? 0.7296 0.7323 0.4255 0.2076  0.0064  -0.0553 19  THR   B CG2 
542  N N   . ASP   B 11  ? 0.6487 0.6423 0.3263 0.1770  0.0110  -0.0572 20  ASP   B N   
543  C CA  . ASP   B 11  ? 0.6571 0.6459 0.3169 0.1801  0.0082  -0.0510 20  ASP   B CA  
544  C C   . ASP   B 11  ? 0.6662 0.6549 0.3173 0.1952  0.0106  -0.0400 20  ASP   B C   
545  O O   . ASP   B 11  ? 0.6565 0.6488 0.3119 0.2070  0.0098  -0.0379 20  ASP   B O   
546  C CB  . ASP   B 11  ? 0.6738 0.6605 0.3250 0.1836  -0.0036 -0.0568 20  ASP   B CB  
547  C CG  . ASP   B 11  ? 0.6822 0.6679 0.3391 0.1677  -0.0064 -0.0645 20  ASP   B CG  
548  O OD1 . ASP   B 11  ? 0.6665 0.6550 0.3335 0.1537  0.0010  -0.0664 20  ASP   B OD1 
549  O OD2 . ASP   B 11  ? 0.7073 0.6899 0.3589 0.1698  -0.0164 -0.0686 20  ASP   B OD2 
550  N N   . GLY   B 12  ? 0.6374 0.6232 0.2774 0.1951  0.0131  -0.0328 21  GLY   B N   
551  C CA  . GLY   B 12  ? 0.6344 0.6214 0.2636 0.2092  0.0149  -0.0218 21  GLY   B CA  
552  C C   . GLY   B 12  ? 0.6232 0.6085 0.2529 0.2024  0.0240  -0.0136 21  GLY   B C   
553  O O   . GLY   B 12  ? 0.5874 0.5703 0.2222 0.1869  0.0271  -0.0176 21  GLY   B O   
554  N N   . VAL   B 13  ? 0.5903 0.5780 0.2168 0.2126  0.0289  -0.0023 22  VAL   B N   
555  C CA  . VAL   B 13  ? 0.5868 0.5737 0.2135 0.2081  0.0370  0.0066  22  VAL   B CA  
556  C C   . VAL   B 13  ? 0.5878 0.5759 0.2320 0.2059  0.0460  0.0123  22  VAL   B C   
557  O O   . VAL   B 13  ? 0.6189 0.6096 0.2692 0.2152  0.0458  0.0149  22  VAL   B O   
558  C CB  . VAL   B 13  ? 0.5801 0.5693 0.1905 0.2205  0.0354  0.0152  22  VAL   B CB  
559  C CG1 . VAL   B 13  ? 0.5884 0.5844 0.1938 0.2392  0.0351  0.0238  22  VAL   B CG1 
560  C CG2 . VAL   B 13  ? 0.5733 0.5620 0.1839 0.2150  0.0426  0.0233  22  VAL   B CG2 
561  N N   . TYR   B 14  ? 0.5706 0.5567 0.2245 0.1931  0.0531  0.0128  23  TYR   B N   
562  C CA  . TYR   B 14  ? 0.5588 0.5451 0.2331 0.1884  0.0614  0.0155  23  TYR   B CA  
563  C C   . TYR   B 14  ? 0.5664 0.5525 0.2432 0.1858  0.0684  0.0252  23  TYR   B C   
564  O O   . TYR   B 14  ? 0.5766 0.5617 0.2438 0.1792  0.0678  0.0244  23  TYR   B O   
565  C CB  . TYR   B 14  ? 0.5482 0.5337 0.2359 0.1729  0.0630  0.0025  23  TYR   B CB  
566  C CG  . TYR   B 14  ? 0.5415 0.5283 0.2329 0.1735  0.0578  -0.0074 23  TYR   B CG  
567  C CD1 . TYR   B 14  ? 0.5447 0.5314 0.2218 0.1758  0.0492  -0.0128 23  TYR   B CD1 
568  C CD2 . TYR   B 14  ? 0.5429 0.5311 0.2539 0.1725  0.0612  -0.0114 23  TYR   B CD2 
569  C CE1 . TYR   B 14  ? 0.5555 0.5441 0.2374 0.1767  0.0441  -0.0217 23  TYR   B CE1 
570  C CE2 . TYR   B 14  ? 0.5535 0.5439 0.2694 0.1730  0.0566  -0.0209 23  TYR   B CE2 
571  C CZ  . TYR   B 14  ? 0.5669 0.5577 0.2678 0.1753  0.0480  -0.0256 23  TYR   B CZ  
572  O OH  . TYR   B 14  ? 0.6061 0.5996 0.3132 0.1762  0.0431  -0.0345 23  TYR   B OH  
573  N N   . ARG   B 15  ? 0.5705 0.5572 0.2632 0.1890  0.0749  0.0335  24  ARG   B N   
574  C CA  . ARG   B 15  ? 0.5706 0.5569 0.2741 0.1845  0.0827  0.0420  24  ARG   B CA  
575  C C   . ARG   B 15  ? 0.5616 0.5459 0.2809 0.1676  0.0862  0.0306  24  ARG   B C   
576  O O   . ARG   B 15  ? 0.5472 0.5310 0.2798 0.1634  0.0863  0.0213  24  ARG   B O   
577  C CB  . ARG   B 15  ? 0.5858 0.5733 0.3038 0.1942  0.0878  0.0552  24  ARG   B CB  
578  C CG  . ARG   B 15  ? 0.6019 0.5941 0.3046 0.2115  0.0852  0.0676  24  ARG   B CG  
579  C CD  . ARG   B 15  ? 0.6132 0.6071 0.3322 0.2198  0.0907  0.0821  24  ARG   B CD  
580  N NE  . ARG   B 15  ? 0.6254 0.6259 0.3284 0.2371  0.0876  0.0929  24  ARG   B NE  
581  C CZ  . ARG   B 15  ? 0.6359 0.6429 0.3262 0.2460  0.0899  0.1059  24  ARG   B CZ  
582  N NH1 . ARG   B 15  ? 0.6169 0.6239 0.3109 0.2397  0.0957  0.1113  24  ARG   B NH1 
583  N NH2 . ARG   B 15  ? 0.6480 0.6628 0.3229 0.2621  0.0867  0.1140  24  ARG   B NH2 
584  N N   . VAL   B 16  ? 0.5746 0.5589 0.2951 0.1594  0.0897  0.0323  25  VAL   B N   
585  C CA  . VAL   B 16  ? 0.5708 0.5550 0.3073 0.1442  0.0936  0.0223  25  VAL   B CA  
586  C C   . VAL   B 16  ? 0.5759 0.5593 0.3337 0.1443  0.1007  0.0309  25  VAL   B C   
587  O O   . VAL   B 16  ? 0.5809 0.5652 0.3348 0.1477  0.1028  0.0420  25  VAL   B O   
588  C CB  . VAL   B 16  ? 0.5662 0.5517 0.2885 0.1333  0.0910  0.0159  25  VAL   B CB  
589  C CG1 . VAL   B 16  ? 0.5601 0.5477 0.2968 0.1180  0.0947  0.0048  25  VAL   B CG1 
590  C CG2 . VAL   B 16  ? 0.5640 0.5495 0.2679 0.1335  0.0836  0.0090  25  VAL   B CG2 
591  N N   . MET   B 17  ? 0.6000 0.5822 0.3812 0.1402  0.1042  0.0251  26  MET   B N   
592  C CA  . MET   B 17  ? 0.6236 0.6037 0.4299 0.1420  0.1102  0.0340  26  MET   B CA  
593  C C   . MET   B 17  ? 0.6357 0.6160 0.4628 0.1279  0.1136  0.0213  26  MET   B C   
594  O O   . MET   B 17  ? 0.6103 0.5928 0.4366 0.1191  0.1118  0.0048  26  MET   B O   
595  C CB  . MET   B 17  ? 0.6290 0.6069 0.4493 0.1522  0.1106  0.0392  26  MET   B CB  
596  C CG  . MET   B 17  ? 0.6440 0.6233 0.4437 0.1664  0.1060  0.0480  26  MET   B CG  
597  S SD  . MET   B 17  ? 0.6400 0.6223 0.4250 0.1791  0.1078  0.0700  26  MET   B SD  
598  C CE  . MET   B 17  ? 0.6590 0.6392 0.4764 0.1784  0.1159  0.0831  26  MET   B CE  
599  N N   . THR   B 18  ? 0.6589 0.6378 0.5053 0.1262  0.1184  0.0285  27  THR   B N   
600  C CA  . THR   B 18  ? 0.7029 0.6816 0.5754 0.1148  0.1216  0.0172  27  THR   B CA  
601  C C   . THR   B 18  ? 0.7503 0.7240 0.6539 0.1200  0.1258  0.0270  27  THR   B C   
602  O O   . THR   B 18  ? 0.7121 0.6844 0.6153 0.1300  0.1277  0.0465  27  THR   B O   
603  C CB  . THR   B 18  ? 0.7060 0.6881 0.5739 0.1045  0.1223  0.0139  27  THR   B CB  
604  O OG1 . THR   B 18  ? 0.7231 0.7064 0.6150 0.0937  0.1243  -0.0010 27  THR   B OG1 
605  C CG2 . THR   B 18  ? 0.7106 0.6921 0.5805 0.1096  0.1250  0.0319  27  THR   B CG2 
606  N N   . ARG   B 19  ? 0.7933 0.7655 0.7241 0.1130  0.1274  0.0139  28  ARG   B N   
607  C CA  . ARG   B 19  ? 0.8546 0.8214 0.8212 0.1150  0.1311  0.0209  28  ARG   B CA  
608  C C   . ARG   B 19  ? 0.8641 0.8320 0.8493 0.1033  0.1333  0.0133  28  ARG   B C   
609  O O   . ARG   B 19  ? 0.8595 0.8226 0.8778 0.1029  0.1360  0.0165  28  ARG   B O   
610  C CB  . ARG   B 19  ? 0.8908 0.8543 0.8776 0.1176  0.1303  0.0120  28  ARG   B CB  
611  C CG  . ARG   B 19  ? 0.9206 0.8839 0.8894 0.1293  0.1274  0.0194  28  ARG   B CG  
612  C CD  . ARG   B 19  ? 0.9538 0.9112 0.9481 0.1390  0.1282  0.0302  28  ARG   B CD  
613  N NE  . ARG   B 19  ? 0.9902 0.9484 0.9683 0.1505  0.1247  0.0366  28  ARG   B NE  
614  C CZ  . ARG   B 19  ? 1.0127 0.9724 0.9895 0.1507  0.1214  0.0224  28  ARG   B CZ  
615  N NH1 . ARG   B 19  ? 1.0346 0.9960 1.0243 0.1401  0.1217  0.0007  28  ARG   B NH1 
616  N NH2 . ARG   B 19  ? 1.0165 0.9771 0.9790 0.1618  0.1177  0.0295  28  ARG   B NH2 
617  N N   . ARG   B 20  ? 0.9055 0.8793 0.8707 0.0948  0.1319  0.0052  29  ARG   B N   
618  C CA  . ARG   B 20  ? 0.9639 0.9408 0.9428 0.0830  0.1329  -0.0046 29  ARG   B CA  
619  C C   . ARG   B 20  ? 0.9396 0.9140 0.9316 0.0856  0.1359  0.0136  29  ARG   B C   
620  O O   . ARG   B 20  ? 0.9255 0.9019 0.9345 0.0767  0.1366  0.0074  29  ARG   B O   
621  C CB  . ARG   B 20  ? 1.0159 1.0008 0.9659 0.0743  0.1298  -0.0167 29  ARG   B CB  
622  C CG  . ARG   B 20  ? 1.0854 1.0763 1.0476 0.0609  0.1295  -0.0350 29  ARG   B CG  
623  C CD  . ARG   B 20  ? 1.1603 1.1592 1.0923 0.0536  0.1264  -0.0398 29  ARG   B CD  
624  N NE  . ARG   B 20  ? 1.2156 1.2133 1.1324 0.0582  0.1260  -0.0216 29  ARG   B NE  
625  C CZ  . ARG   B 20  ? 1.2608 1.2615 1.1817 0.0530  0.1260  -0.0186 29  ARG   B CZ  
626  N NH1 . ARG   B 20  ? 1.2966 1.3018 1.2359 0.0427  0.1259  -0.0329 29  ARG   B NH1 
627  N NH2 . ARG   B 20  ? 1.2412 1.2412 1.1481 0.0586  0.1259  -0.0018 29  ARG   B NH2 
628  N N   . LEU   B 21  ? 0.9230 0.8948 0.9070 0.0973  0.1375  0.0352  30  LEU   B N   
629  C CA  . LEU   B 21  ? 0.8980 0.8691 0.8936 0.1016  0.1413  0.0560  30  LEU   B CA  
630  C C   . LEU   B 21  ? 0.8685 0.8337 0.8865 0.1117  0.1443  0.0719  30  LEU   B C   
631  O O   . LEU   B 21  ? 0.8623 0.8233 0.8918 0.1132  0.1429  0.0634  30  LEU   B O   
632  C CB  . LEU   B 21  ? 0.9110 0.8874 0.8721 0.1070  0.1405  0.0674  30  LEU   B CB  
633  C CG  . LEU   B 21  ? 0.9354 0.9175 0.8860 0.0979  0.1393  0.0619  30  LEU   B CG  
634  C CD1 . LEU   B 21  ? 0.9401 0.9239 0.8952 0.0845  0.1362  0.0379  30  LEU   B CD1 
635  C CD2 . LEU   B 21  ? 0.9397 0.9262 0.8531 0.1036  0.1368  0.0682  30  LEU   B CD2 
636  N N   . LEU   B 22  ? 0.8591 0.8247 0.8844 0.1183  0.1483  0.0946  31  LEU   B N   
637  C CA  . LEU   B 22  ? 0.8329 0.7944 0.8784 0.1286  0.1515  0.1142  31  LEU   B CA  
638  C C   . LEU   B 22  ? 0.8203 0.7825 0.8403 0.1403  0.1490  0.1186  31  LEU   B C   
639  O O   . LEU   B 22  ? 0.8267 0.7947 0.8113 0.1443  0.1471  0.1193  31  LEU   B O   
640  C CB  . LEU   B 22  ? 0.8336 0.7991 0.8849 0.1329  0.1566  0.1383  31  LEU   B CB  
641  C CG  . LEU   B 22  ? 0.8287 0.7907 0.9075 0.1411  0.1608  0.1605  31  LEU   B CG  
642  C CD1 . LEU   B 22  ? 0.8241 0.7782 0.9498 0.1321  0.1619  0.1555  31  LEU   B CD1 
643  C CD2 . LEU   B 22  ? 0.8330 0.8032 0.9028 0.1491  0.1660  0.1866  31  LEU   B CD2 
644  N N   . GLY   B 23  ? 0.7942 0.7508 0.8326 0.1458  0.1485  0.1211  32  GLY   B N   
645  C CA  . GLY   B 23  ? 0.7730 0.7303 0.7908 0.1569  0.1454  0.1237  32  GLY   B CA  
646  C C   . GLY   B 23  ? 0.7463 0.7065 0.7343 0.1529  0.1403  0.1029  32  GLY   B C   
647  O O   . GLY   B 23  ? 0.7330 0.6924 0.7271 0.1409  0.1391  0.0826  32  GLY   B O   
648  N N   . SER   B 24  ? 0.7177 0.6815 0.6762 0.1630  0.1373  0.1078  33  SER   B N   
649  C CA  . SER   B 24  ? 0.6914 0.6586 0.6181 0.1612  0.1322  0.0925  33  SER   B CA  
650  C C   . SER   B 24  ? 0.6798 0.6529 0.5783 0.1641  0.1324  0.1014  33  SER   B C   
651  O O   . SER   B 24  ? 0.6684 0.6448 0.5604 0.1753  0.1342  0.1202  33  SER   B O   
652  C CB  . SER   B 24  ? 0.6882 0.6554 0.6044 0.1709  0.1280  0.0918  33  SER   B CB  
653  O OG  . SER   B 24  ? 0.7193 0.6812 0.6651 0.1702  0.1283  0.0870  33  SER   B OG  
654  N N   . THR   B 25  ? 0.6485 0.6237 0.5325 0.1544  0.1307  0.0888  34  THR   B N   
655  C CA  . THR   B 25  ? 0.6464 0.6268 0.5064 0.1562  0.1305  0.0960  34  THR   B CA  
656  C C   . THR   B 25  ? 0.6399 0.6222 0.4688 0.1562  0.1242  0.0843  34  THR   B C   
657  O O   . THR   B 25  ? 0.6044 0.5850 0.4336 0.1465  0.1212  0.0662  34  THR   B O   
658  C CB  . THR   B 25  ? 0.6531 0.6345 0.5262 0.1454  0.1338  0.0948  34  THR   B CB  
659  O OG1 . THR   B 25  ? 0.6647 0.6433 0.5710 0.1448  0.1390  0.1043  34  THR   B OG1 
660  C CG2 . THR   B 25  ? 0.6556 0.6428 0.5085 0.1488  0.1342  0.1048  34  THR   B CG2 
661  N N   . GLN   B 26  ? 0.6222 0.6086 0.4265 0.1670  0.1220  0.0939  35  GLN   B N   
662  C CA  . GLN   B 26  ? 0.6176 0.6051 0.3936 0.1673  0.1153  0.0835  35  GLN   B CA  
663  C C   . GLN   B 26  ? 0.6181 0.6074 0.3841 0.1583  0.1146  0.0790  35  GLN   B C   
664  O O   . GLN   B 26  ? 0.6333 0.6264 0.3970 0.1625  0.1175  0.0914  35  GLN   B O   
665  C CB  . GLN   B 26  ? 0.6040 0.5955 0.3585 0.1831  0.1124  0.0938  35  GLN   B CB  
666  C CG  . GLN   B 26  ? 0.5910 0.5825 0.3200 0.1841  0.1045  0.0824  35  GLN   B CG  
667  C CD  . GLN   B 26  ? 0.5857 0.5817 0.2950 0.2005  0.1008  0.0905  35  GLN   B CD  
668  O OE1 . GLN   B 26  ? 0.6021 0.5996 0.3165 0.2102  0.1014  0.0974  35  GLN   B OE1 
669  N NE2 . GLN   B 26  ? 0.5645 0.5632 0.2520 0.2040  0.0966  0.0891  35  GLN   B NE2 
670  N N   . VAL   B 27  ? 0.6299 0.6177 0.3918 0.1463  0.1111  0.0629  36  VAL   B N   
671  C CA  . VAL   B 27  ? 0.6146 0.6042 0.3671 0.1364  0.1095  0.0577  36  VAL   B CA  
672  C C   . VAL   B 27  ? 0.5966 0.5869 0.3212 0.1403  0.1026  0.0552  36  VAL   B C   
673  O O   . VAL   B 27  ? 0.6038 0.5959 0.3176 0.1372  0.1008  0.0563  36  VAL   B O   
674  C CB  . VAL   B 27  ? 0.6312 0.6205 0.3970 0.1209  0.1100  0.0424  36  VAL   B CB  
675  C CG1 . VAL   B 27  ? 0.6518 0.6407 0.4462 0.1170  0.1161  0.0453  36  VAL   B CG1 
676  C CG2 . VAL   B 27  ? 0.6264 0.6143 0.3917 0.1179  0.1073  0.0294  36  VAL   B CG2 
677  N N   . GLY   B 28  ? 0.5802 0.5690 0.2945 0.1475  0.0985  0.0524  37  GLY   B N   
678  C CA  . GLY   B 28  ? 0.5537 0.5426 0.2437 0.1537  0.0915  0.0511  37  GLY   B CA  
679  C C   . GLY   B 28  ? 0.5532 0.5406 0.2375 0.1602  0.0869  0.0459  37  GLY   B C   
680  O O   . GLY   B 28  ? 0.5539 0.5410 0.2507 0.1656  0.0898  0.0487  37  GLY   B O   
681  N N   . VAL   B 29  ? 0.5468 0.5330 0.2138 0.1600  0.0795  0.0389  38  VAL   B N   
682  C CA  . VAL   B 29  ? 0.5587 0.5441 0.2155 0.1687  0.0731  0.0349  38  VAL   B CA  
683  C C   . VAL   B 29  ? 0.5604 0.5434 0.2101 0.1580  0.0669  0.0223  38  VAL   B C   
684  O O   . VAL   B 29  ? 0.5813 0.5638 0.2274 0.1476  0.0665  0.0202  38  VAL   B O   
685  C CB  . VAL   B 29  ? 0.5713 0.5592 0.2116 0.1844  0.0697  0.0436  38  VAL   B CB  
686  C CG1 . VAL   B 29  ? 0.5724 0.5601 0.2012 0.1938  0.0616  0.0381  38  VAL   B CG1 
687  C CG2 . VAL   B 29  ? 0.5796 0.5719 0.2267 0.1944  0.0767  0.0578  38  VAL   B CG2 
688  N N   . GLY   B 30  ? 0.5599 0.5421 0.2073 0.1606  0.0618  0.0152  39  GLY   B N   
689  C CA  . GLY   B 30  ? 0.5457 0.5262 0.1857 0.1521  0.0551  0.0051  39  GLY   B CA  
690  C C   . GLY   B 30  ? 0.5495 0.5294 0.1858 0.1589  0.0483  -0.0005 39  GLY   B C   
691  O O   . GLY   B 30  ? 0.5414 0.5227 0.1780 0.1726  0.0478  0.0036  39  GLY   B O   
692  N N   . VAL   B 31  ? 0.5354 0.5137 0.1666 0.1510  0.0421  -0.0084 40  VAL   B N   
693  C CA  . VAL   B 31  ? 0.5495 0.5265 0.1756 0.1562  0.0333  -0.0148 40  VAL   B CA  
694  C C   . VAL   B 31  ? 0.5537 0.5328 0.1906 0.1448  0.0334  -0.0245 40  VAL   B C   
695  O O   . VAL   B 31  ? 0.5362 0.5163 0.1753 0.1296  0.0353  -0.0281 40  VAL   B O   
696  C CB  . VAL   B 31  ? 0.5621 0.5352 0.1742 0.1582  0.0244  -0.0153 40  VAL   B CB  
697  C CG1 . VAL   B 31  ? 0.5748 0.5466 0.1850 0.1627  0.0148  -0.0230 40  VAL   B CG1 
698  C CG2 . VAL   B 31  ? 0.5650 0.5378 0.1662 0.1713  0.0239  -0.0068 40  VAL   B CG2 
699  N N   . MET   B 32  ? 0.5481 0.5292 0.1922 0.1512  0.0320  -0.0286 41  MET   B N   
700  C CA  . MET   B 32  ? 0.5633 0.5474 0.2180 0.1425  0.0309  -0.0387 41  MET   B CA  
701  C C   . MET   B 32  ? 0.5777 0.5598 0.2256 0.1457  0.0200  -0.0437 41  MET   B C   
702  O O   . MET   B 32  ? 0.5680 0.5488 0.2100 0.1603  0.0137  -0.0426 41  MET   B O   
703  C CB  . MET   B 32  ? 0.5710 0.5587 0.2404 0.1473  0.0355  -0.0406 41  MET   B CB  
704  C CG  . MET   B 32  ? 0.5768 0.5695 0.2603 0.1372  0.0367  -0.0515 41  MET   B CG  
705  S SD  . MET   B 32  ? 0.5907 0.5886 0.2838 0.1178  0.0464  -0.0565 41  MET   B SD  
706  C CE  . MET   B 32  ? 0.5937 0.5902 0.2960 0.1237  0.0550  -0.0496 41  MET   B CE  
707  N N   . GLN   B 33  ? 0.5722 0.5544 0.2208 0.1324  0.0173  -0.0488 42  GLN   B N   
708  C CA  . GLN   B 33  ? 0.6053 0.5852 0.2513 0.1321  0.0069  -0.0539 42  GLN   B CA  
709  C C   . GLN   B 33  ? 0.6246 0.6094 0.2813 0.1161  0.0081  -0.0607 42  GLN   B C   
710  O O   . GLN   B 33  ? 0.6045 0.5923 0.2619 0.1016  0.0141  -0.0594 42  GLN   B O   
711  C CB  . GLN   B 33  ? 0.6285 0.6016 0.2609 0.1348  0.0000  -0.0495 42  GLN   B CB  
712  C CG  . GLN   B 33  ? 0.6576 0.6273 0.2896 0.1375  -0.0120 -0.0553 42  GLN   B CG  
713  C CD  . GLN   B 33  ? 0.6847 0.6475 0.3046 0.1466  -0.0209 -0.0529 42  GLN   B CD  
714  O OE1 . GLN   B 33  ? 0.7460 0.7041 0.3664 0.1413  -0.0291 -0.0555 42  GLN   B OE1 
715  N NE2 . GLN   B 33  ? 0.6532 0.6155 0.2632 0.1593  -0.0187 -0.0474 42  GLN   B NE2 
716  N N   . GLU   B 34  ? 0.6378 0.6248 0.3026 0.1176  0.0025  -0.0678 43  GLU   B N   
717  C CA  . GLU   B 34  ? 0.6558 0.6492 0.3318 0.1023  0.0035  -0.0740 43  GLU   B CA  
718  C C   . GLU   B 34  ? 0.6415 0.6432 0.3253 0.0911  0.0157  -0.0754 43  GLU   B C   
719  O O   . GLU   B 34  ? 0.6524 0.6597 0.3383 0.0756  0.0187  -0.0766 43  GLU   B O   
720  C CB  . GLU   B 34  ? 0.6776 0.6669 0.3476 0.0925  -0.0024 -0.0713 43  GLU   B CB  
721  C CG  . GLU   B 34  ? 0.7311 0.7127 0.3977 0.1019  -0.0155 -0.0727 43  GLU   B CG  
722  C CD  . GLU   B 34  ? 0.7459 0.7199 0.4048 0.0973  -0.0226 -0.0679 43  GLU   B CD  
723  O OE1 . GLU   B 34  ? 0.7860 0.7620 0.4504 0.0825  -0.0232 -0.0672 43  GLU   B OE1 
724  O OE2 . GLU   B 34  ? 0.7978 0.7643 0.4456 0.1088  -0.0276 -0.0646 43  GLU   B OE2 
725  N N   . GLY   B 35  ? 0.6256 0.6291 0.3144 0.0982  0.0223  -0.0755 44  GLY   B N   
726  C CA  . GLY   B 35  ? 0.6065 0.6183 0.3066 0.0894  0.0330  -0.0797 44  GLY   B CA  
727  C C   . GLY   B 35  ? 0.5939 0.6054 0.2870 0.0818  0.0394  -0.0747 44  GLY   B C   
728  O O   . GLY   B 35  ? 0.5798 0.5987 0.2819 0.0738  0.0480  -0.0792 44  GLY   B O   
729  N N   . VAL   B 36  ? 0.5730 0.5768 0.2513 0.0846  0.0350  -0.0666 45  VAL   B N   
730  C CA  . VAL   B 36  ? 0.5548 0.5580 0.2254 0.0777  0.0395  -0.0610 45  VAL   B CA  
731  C C   . VAL   B 36  ? 0.5480 0.5447 0.2136 0.0903  0.0408  -0.0534 45  VAL   B C   
732  O O   . VAL   B 36  ? 0.5430 0.5332 0.2008 0.1029  0.0343  -0.0490 45  VAL   B O   
733  C CB  . VAL   B 36  ? 0.5596 0.5608 0.2193 0.0689  0.0338  -0.0574 45  VAL   B CB  
734  C CG1 . VAL   B 36  ? 0.5545 0.5545 0.2050 0.0637  0.0366  -0.0507 45  VAL   B CG1 
735  C CG2 . VAL   B 36  ? 0.5566 0.5671 0.2231 0.0544  0.0350  -0.0635 45  VAL   B CG2 
736  N N   . PHE   B 37  ? 0.5253 0.5244 0.1956 0.0871  0.0488  -0.0521 46  PHE   B N   
737  C CA  . PHE   B 37  ? 0.5254 0.5198 0.1926 0.0964  0.0513  -0.0437 46  PHE   B CA  
738  C C   . PHE   B 37  ? 0.5227 0.5146 0.1775 0.0914  0.0499  -0.0374 46  PHE   B C   
739  O O   . PHE   B 37  ? 0.4996 0.4964 0.1545 0.0776  0.0528  -0.0401 46  PHE   B O   
740  C CB  . PHE   B 37  ? 0.5272 0.5243 0.2091 0.0970  0.0599  -0.0449 46  PHE   B CB  
741  C CG  . PHE   B 37  ? 0.5461 0.5382 0.2267 0.1092  0.0615  -0.0346 46  PHE   B CG  
742  C CD1 . PHE   B 37  ? 0.5565 0.5447 0.2325 0.1245  0.0573  -0.0289 46  PHE   B CD1 
743  C CD2 . PHE   B 37  ? 0.5546 0.5472 0.2395 0.1052  0.0676  -0.0307 46  PHE   B CD2 
744  C CE1 . PHE   B 37  ? 0.5631 0.5487 0.2375 0.1355  0.0596  -0.0182 46  PHE   B CE1 
745  C CE2 . PHE   B 37  ? 0.5579 0.5468 0.2427 0.1157  0.0696  -0.0201 46  PHE   B CE2 
746  C CZ  . PHE   B 37  ? 0.5575 0.5435 0.2375 0.1310  0.0662  -0.0134 46  PHE   B CZ  
747  N N   . HIS   B 38  ? 0.5132 0.4989 0.1574 0.1022  0.0453  -0.0296 47  HIS   B N   
748  C CA  . HIS   B 38  ? 0.5185 0.5009 0.1509 0.1006  0.0427  -0.0228 47  HIS   B CA  
749  C C   . HIS   B 38  ? 0.5296 0.5109 0.1621 0.1088  0.0475  -0.0147 47  HIS   B C   
750  O O   . HIS   B 38  ? 0.5160 0.4952 0.1474 0.1233  0.0467  -0.0104 47  HIS   B O   
751  C CB  . HIS   B 38  ? 0.5214 0.4983 0.1422 0.1063  0.0327  -0.0212 47  HIS   B CB  
752  C CG  . HIS   B 38  ? 0.5311 0.5081 0.1533 0.1008  0.0268  -0.0280 47  HIS   B CG  
753  N ND1 . HIS   B 38  ? 0.5460 0.5254 0.1768 0.1041  0.0268  -0.0344 47  HIS   B ND1 
754  C CD2 . HIS   B 38  ? 0.5362 0.5106 0.1529 0.0927  0.0194  -0.0283 47  HIS   B CD2 
755  C CE1 . HIS   B 38  ? 0.5407 0.5201 0.1722 0.0973  0.0208  -0.0392 47  HIS   B CE1 
756  N NE2 . HIS   B 38  ? 0.5476 0.5236 0.1706 0.0904  0.0160  -0.0350 47  HIS   B NE2 
757  N N   . THR   B 39  ? 0.5311 0.5143 0.1644 0.1008  0.0517  -0.0118 48  THR   B N   
758  C CA  . THR   B 39  ? 0.5385 0.5211 0.1729 0.1075  0.0560  -0.0033 48  THR   B CA  
759  C C   . THR   B 39  ? 0.5481 0.5311 0.1756 0.1001  0.0548  0.0004  48  THR   B C   
760  O O   . THR   B 39  ? 0.5192 0.5024 0.1398 0.0907  0.0498  -0.0029 48  THR   B O   
761  C CB  . THR   B 39  ? 0.5470 0.5324 0.1977 0.1082  0.0644  -0.0037 48  THR   B CB  
762  O OG1 . THR   B 39  ? 0.5434 0.5280 0.1964 0.1173  0.0681  0.0063  48  THR   B OG1 
763  C CG2 . THR   B 39  ? 0.5402 0.5307 0.2014 0.0933  0.0695  -0.0108 48  THR   B CG2 
764  N N   . MET   B 40  ? 0.5416 0.5254 0.1716 0.1043  0.0589  0.0078  49  MET   B N   
765  C CA  . MET   B 40  ? 0.5585 0.5437 0.1845 0.0971  0.0583  0.0113  49  MET   B CA  
766  C C   . MET   B 40  ? 0.5468 0.5378 0.1849 0.0840  0.0646  0.0064  49  MET   B C   
767  O O   . MET   B 40  ? 0.5413 0.5341 0.1933 0.0846  0.0709  0.0039  49  MET   B O   
768  C CB  . MET   B 40  ? 0.5628 0.5469 0.1850 0.1081  0.0586  0.0214  49  MET   B CB  
769  C CG  . MET   B 40  ? 0.5887 0.5692 0.2008 0.1238  0.0536  0.0247  49  MET   B CG  
770  S SD  . MET   B 40  ? 0.6271 0.6073 0.2287 0.1328  0.0499  0.0332  49  MET   B SD  
771  C CE  . MET   B 40  ? 0.6458 0.6218 0.2374 0.1231  0.0400  0.0287  49  MET   B CE  
772  N N   A TRP   B 41  ? 0.5466 0.5410 0.1800 0.0724  0.0625  0.0048  50  TRP   B N   
773  N N   B TRP   B 41  ? 0.5470 0.5414 0.1804 0.0721  0.0625  0.0045  50  TRP   B N   
774  N N   C TRP   B 41  ? 0.5466 0.5410 0.1800 0.0724  0.0625  0.0048  50  TRP   B N   
775  N N   D TRP   B 41  ? 0.5470 0.5414 0.1804 0.0721  0.0625  0.0045  50  TRP   B N   
776  C CA  A TRP   B 41  ? 0.5490 0.5507 0.1916 0.0592  0.0672  -0.0016 50  TRP   B CA  
777  C CA  B TRP   B 41  ? 0.5499 0.5517 0.1928 0.0591  0.0674  -0.0017 50  TRP   B CA  
778  C CA  C TRP   B 41  ? 0.5490 0.5507 0.1916 0.0592  0.0672  -0.0016 50  TRP   B CA  
779  C CA  D TRP   B 41  ? 0.5499 0.5517 0.1928 0.0591  0.0674  -0.0017 50  TRP   B CA  
780  C C   A TRP   B 41  ? 0.5482 0.5515 0.2052 0.0619  0.0737  0.0014  50  TRP   B C   
781  C C   B TRP   B 41  ? 0.5490 0.5519 0.2063 0.0625  0.0739  0.0015  50  TRP   B C   
782  C C   C TRP   B 41  ? 0.5482 0.5515 0.2052 0.0619  0.0737  0.0014  50  TRP   B C   
783  C C   D TRP   B 41  ? 0.5490 0.5519 0.2063 0.0625  0.0739  0.0015  50  TRP   B C   
784  O O   A TRP   B 41  ? 0.5490 0.5574 0.2208 0.0545  0.0793  -0.0065 50  TRP   B O   
785  O O   B TRP   B 41  ? 0.5502 0.5577 0.2233 0.0562  0.0798  -0.0064 50  TRP   B O   
786  O O   C TRP   B 41  ? 0.5490 0.5574 0.2208 0.0545  0.0793  -0.0065 50  TRP   B O   
787  O O   D TRP   B 41  ? 0.5502 0.5577 0.2233 0.0562  0.0798  -0.0064 50  TRP   B O   
788  C CB  A TRP   B 41  ? 0.5493 0.5552 0.1817 0.0476  0.0626  -0.0019 50  TRP   B CB  
789  C CB  B TRP   B 41  ? 0.5509 0.5570 0.1842 0.0475  0.0631  -0.0019 50  TRP   B CB  
790  C CB  C TRP   B 41  ? 0.5493 0.5552 0.1817 0.0476  0.0626  -0.0019 50  TRP   B CB  
791  C CB  D TRP   B 41  ? 0.5509 0.5570 0.1842 0.0475  0.0631  -0.0019 50  TRP   B CB  
792  C CG  A TRP   B 41  ? 0.5464 0.5620 0.1862 0.0341  0.0668  -0.0107 50  TRP   B CG  
793  C CG  B TRP   B 41  ? 0.5484 0.5641 0.1901 0.0348  0.0675  -0.0095 50  TRP   B CG  
794  C CG  C TRP   B 41  ? 0.5464 0.5620 0.1862 0.0341  0.0668  -0.0107 50  TRP   B CG  
795  C CG  D TRP   B 41  ? 0.5484 0.5641 0.1901 0.0348  0.0675  -0.0095 50  TRP   B CG  
796  C CD1 A TRP   B 41  ? 0.5488 0.5710 0.1883 0.0244  0.0677  -0.0199 50  TRP   B CD1 
797  C CD1 B TRP   B 41  ? 0.5477 0.5671 0.1992 0.0325  0.0713  -0.0092 50  TRP   B CD1 
798  C CD1 C TRP   B 41  ? 0.5488 0.5710 0.1883 0.0244  0.0677  -0.0199 50  TRP   B CD1 
799  C CD1 D TRP   B 41  ? 0.5477 0.5671 0.1992 0.0325  0.0713  -0.0092 50  TRP   B CD1 
800  C CD2 A TRP   B 41  ? 0.5458 0.5668 0.1961 0.0296  0.0712  -0.0124 50  TRP   B CD2 
801  C CD2 B TRP   B 41  ? 0.5517 0.5756 0.1937 0.0229  0.0689  -0.0198 50  TRP   B CD2 
802  C CD2 C TRP   B 41  ? 0.5458 0.5668 0.1961 0.0296  0.0712  -0.0124 50  TRP   B CD2 
803  C CD2 D TRP   B 41  ? 0.5517 0.5756 0.1937 0.0229  0.0689  -0.0198 50  TRP   B CD2 
804  N NE1 A TRP   B 41  ? 0.5460 0.5781 0.1935 0.0144  0.0721  -0.0278 50  TRP   B NE1 
805  N NE1 B TRP   B 41  ? 0.5467 0.5758 0.2041 0.0203  0.0741  -0.0195 50  TRP   B NE1 
806  N NE1 C TRP   B 41  ? 0.5460 0.5781 0.1935 0.0144  0.0721  -0.0278 50  TRP   B NE1 
807  N NE1 D TRP   B 41  ? 0.5467 0.5758 0.2041 0.0203  0.0741  -0.0195 50  TRP   B NE1 
808  C CE2 A TRP   B 41  ? 0.5441 0.5752 0.1989 0.0173  0.0739  -0.0238 50  TRP   B CE2 
809  C CE2 B TRP   B 41  ? 0.5473 0.5801 0.1986 0.0144  0.0731  -0.0262 50  TRP   B CE2 
810  C CE2 C TRP   B 41  ? 0.5441 0.5752 0.1989 0.0173  0.0739  -0.0238 50  TRP   B CE2 
811  C CE2 D TRP   B 41  ? 0.5473 0.5801 0.1986 0.0144  0.0731  -0.0262 50  TRP   B CE2 
812  C CE3 A TRP   B 41  ? 0.5457 0.5651 0.2027 0.0345  0.0728  -0.0057 50  TRP   B CE3 
813  C CE3 B TRP   B 41  ? 0.5552 0.5810 0.1914 0.0187  0.0669  -0.0244 50  TRP   B CE3 
814  C CE3 C TRP   B 41  ? 0.5457 0.5651 0.2027 0.0345  0.0728  -0.0057 50  TRP   B CE3 
815  C CE3 D TRP   B 41  ? 0.5552 0.5810 0.1914 0.0187  0.0669  -0.0244 50  TRP   B CE3 
816  C CZ2 A TRP   B 41  ? 0.5489 0.5876 0.2146 0.0103  0.0776  -0.0297 50  TRP   B CZ2 
817  C CZ2 B TRP   B 41  ? 0.5516 0.5960 0.2045 0.0022  0.0755  -0.0375 50  TRP   B CZ2 
818  C CZ2 C TRP   B 41  ? 0.5489 0.5876 0.2146 0.0103  0.0776  -0.0297 50  TRP   B CZ2 
819  C CZ2 D TRP   B 41  ? 0.5516 0.5960 0.2045 0.0022  0.0755  -0.0375 50  TRP   B CZ2 
820  C CZ3 A TRP   B 41  ? 0.5449 0.5713 0.2140 0.0270  0.0765  -0.0106 50  TRP   B CZ3 
821  C CZ3 B TRP   B 41  ? 0.5549 0.5923 0.1933 0.0063  0.0699  -0.0344 50  TRP   B CZ3 
822  C CZ3 C TRP   B 41  ? 0.5449 0.5713 0.2140 0.0270  0.0765  -0.0106 50  TRP   B CZ3 
823  C CZ3 D TRP   B 41  ? 0.5549 0.5923 0.1933 0.0063  0.0699  -0.0344 50  TRP   B CZ3 
824  C CH2 A TRP   B 41  ? 0.5463 0.5820 0.2195 0.0151  0.0784  -0.0230 50  TRP   B CH2 
825  C CH2 B TRP   B 41  ? 0.5514 0.5984 0.1975 -0.0013 0.0743  -0.0413 50  TRP   B CH2 
826  C CH2 C TRP   B 41  ? 0.5463 0.5820 0.2195 0.0151  0.0784  -0.0230 50  TRP   B CH2 
827  C CH2 D TRP   B 41  ? 0.5514 0.5984 0.1975 -0.0013 0.0743  -0.0413 50  TRP   B CH2 
828  N N   . HIS   B 42  ? 0.5463 0.5463 0.2006 0.0717  0.0730  0.0121  51  HIS   B N   
829  C CA  . HIS   B 42  ? 0.5547 0.5567 0.2240 0.0736  0.0791  0.0168  51  HIS   B CA  
830  C C   . HIS   B 42  ? 0.5691 0.5690 0.2536 0.0812  0.0852  0.0176  51  HIS   B C   
831  O O   . HIS   B 42  ? 0.5868 0.5884 0.2882 0.0807  0.0908  0.0199  51  HIS   B O   
832  C CB  . HIS   B 42  ? 0.5813 0.5828 0.2450 0.0805  0.0775  0.0276  51  HIS   B CB  
833  C CG  . HIS   B 42  ? 0.5847 0.5822 0.2428 0.0963  0.0773  0.0362  51  HIS   B CG  
834  N ND1 . HIS   B 42  ? 0.6013 0.5955 0.2424 0.1030  0.0704  0.0381  51  HIS   B ND1 
835  C CD2 . HIS   B 42  ? 0.6039 0.6012 0.2712 0.1071  0.0828  0.0438  51  HIS   B CD2 
836  C CE1 . HIS   B 42  ? 0.5988 0.5917 0.2378 0.1176  0.0718  0.0450  51  HIS   B CE1 
837  N NE2 . HIS   B 42  ? 0.5905 0.5858 0.2446 0.1201  0.0795  0.0493  51  HIS   B NE2 
838  N N   . VAL   B 43  ? 0.5724 0.5689 0.2526 0.0877  0.0838  0.0158  52  VAL   B N   
839  C CA  . VAL   B 43  ? 0.5646 0.5591 0.2586 0.0953  0.0886  0.0169  52  VAL   B CA  
840  C C   . VAL   B 43  ? 0.5790 0.5764 0.2895 0.0848  0.0923  0.0050  52  VAL   B C   
841  O O   . VAL   B 43  ? 0.5831 0.5802 0.3132 0.0861  0.0979  0.0066  52  VAL   B O   
842  C CB  . VAL   B 43  ? 0.5711 0.5620 0.2531 0.1058  0.0843  0.0180  52  VAL   B CB  
843  C CG1 . VAL   B 43  ? 0.5685 0.5580 0.2637 0.1117  0.0877  0.0168  52  VAL   B CG1 
844  C CG2 . VAL   B 43  ? 0.5728 0.5620 0.2420 0.1188  0.0817  0.0295  52  VAL   B CG2 
845  N N   . THR   B 44  ? 0.5450 0.5456 0.2489 0.0746  0.0895  -0.0062 53  THR   B N   
846  C CA  . THR   B 44  ? 0.5593 0.5643 0.2775 0.0659  0.0930  -0.0193 53  THR   B CA  
847  C C   . THR   B 44  ? 0.5646 0.5773 0.2852 0.0519  0.0940  -0.0274 53  THR   B C   
848  O O   . THR   B 44  ? 0.5778 0.5953 0.3141 0.0453  0.0979  -0.0383 53  THR   B O   
849  C CB  . THR   B 44  ? 0.5498 0.5558 0.2613 0.0648  0.0903  -0.0271 53  THR   B CB  
850  O OG1 . THR   B 44  ? 0.5278 0.5368 0.2210 0.0572  0.0852  -0.0285 53  THR   B OG1 
851  C CG2 . THR   B 44  ? 0.5462 0.5456 0.2552 0.0792  0.0884  -0.0197 53  THR   B CG2 
852  N N   . LYS   B 45  ? 0.5810 0.5951 0.2872 0.0482  0.0902  -0.0224 54  LYS   B N   
853  C CA  . LYS   B 45  ? 0.6150 0.6378 0.3181 0.0347  0.0892  -0.0293 54  LYS   B CA  
854  C C   . LYS   B 45  ? 0.6185 0.6490 0.3179 0.0248  0.0891  -0.0420 54  LYS   B C   
855  O O   . LYS   B 45  ? 0.6405 0.6809 0.3439 0.0137  0.0907  -0.0517 54  LYS   B O   
856  C CB  . LYS   B 45  ? 0.6533 0.6795 0.3757 0.0310  0.0938  -0.0326 54  LYS   B CB  
857  C CG  . LYS   B 45  ? 0.7205 0.7407 0.4525 0.0400  0.0958  -0.0205 54  LYS   B CG  
858  C CD  . LYS   B 45  ? 0.7733 0.7920 0.4899 0.0432  0.0915  -0.0089 54  LYS   B CD  
859  C CE  . LYS   B 45  ? 0.8096 0.8260 0.5390 0.0498  0.0947  0.0014  54  LYS   B CE  
860  N NZ  . LYS   B 45  ? 0.8307 0.8418 0.5486 0.0626  0.0930  0.0153  54  LYS   B NZ  
861  N N   . GLY   B 46  ? 0.6171 0.6448 0.3097 0.0285  0.0872  -0.0425 55  GLY   B N   
862  C CA  . GLY   B 46  ? 0.6122 0.6477 0.3011 0.0199  0.0872  -0.0530 55  GLY   B CA  
863  C C   . GLY   B 46  ? 0.6236 0.6640 0.3316 0.0185  0.0931  -0.0656 55  GLY   B C   
864  O O   . GLY   B 46  ? 0.6188 0.6687 0.3253 0.0102  0.0941  -0.0758 55  GLY   B O   
865  N N   . ALA   B 47  ? 0.6125 0.6477 0.3392 0.0256  0.0971  -0.0653 56  ALA   B N   
866  C CA  . ALA   B 47  ? 0.6170 0.6550 0.3652 0.0259  0.1021  -0.0770 56  ALA   B CA  
867  C C   . ALA   B 47  ? 0.6033 0.6391 0.3512 0.0316  0.1013  -0.0787 56  ALA   B C   
868  O O   . ALA   B 47  ? 0.6107 0.6387 0.3466 0.0398  0.0973  -0.0682 56  ALA   B O   
869  C CB  . ALA   B 47  ? 0.6163 0.6471 0.3850 0.0334  0.1055  -0.0725 56  ALA   B CB  
870  N N   . ALA   B 48  ? 0.5911 0.6333 0.3539 0.0286  0.1050  -0.0921 57  ALA   B N   
871  C CA  . ALA   B 48  ? 0.5909 0.6311 0.3595 0.0351  0.1047  -0.0948 57  ALA   B CA  
872  C C   . ALA   B 48  ? 0.5912 0.6190 0.3713 0.0495  0.1047  -0.0846 57  ALA   B C   
873  O O   . ALA   B 48  ? 0.6059 0.6292 0.3963 0.0523  0.1069  -0.0793 57  ALA   B O   
874  C CB  . ALA   B 48  ? 0.6050 0.6562 0.3895 0.0286  0.1091  -0.1122 57  ALA   B CB  
875  N N   . LEU   B 49  ? 0.5842 0.6083 0.3630 0.0578  0.1022  -0.0820 58  LEU   B N   
876  C CA  . LEU   B 49  ? 0.6091 0.6230 0.3946 0.0727  0.1011  -0.0709 58  LEU   B CA  
877  C C   . LEU   B 49  ? 0.6350 0.6504 0.4375 0.0768  0.1021  -0.0790 58  LEU   B C   
878  O O   . LEU   B 49  ? 0.6603 0.6838 0.4611 0.0703  0.1016  -0.0906 58  LEU   B O   
879  C CB  . LEU   B 49  ? 0.5839 0.5927 0.3469 0.0799  0.0950  -0.0594 58  LEU   B CB  
880  C CG  . LEU   B 49  ? 0.5734 0.5804 0.3185 0.0773  0.0928  -0.0508 58  LEU   B CG  
881  C CD1 . LEU   B 49  ? 0.5765 0.5787 0.3016 0.0852  0.0861  -0.0422 58  LEU   B CD1 
882  C CD2 . LEU   B 49  ? 0.5750 0.5779 0.3283 0.0810  0.0963  -0.0418 58  LEU   B CD2 
883  N N   . ARG   B 50  ? 0.6479 0.6567 0.4672 0.0871  0.1035  -0.0729 59  ARG   B N   
884  C CA  . ARG   B 50  ? 0.6805 0.6892 0.5166 0.0937  0.1035  -0.0778 59  ARG   B CA  
885  C C   . ARG   B 50  ? 0.6917 0.6953 0.5142 0.1062  0.0978  -0.0666 59  ARG   B C   
886  O O   . ARG   B 50  ? 0.6482 0.6459 0.4581 0.1138  0.0959  -0.0519 59  ARG   B O   
887  C CB  . ARG   B 50  ? 0.7277 0.7324 0.5915 0.0967  0.1079  -0.0773 59  ARG   B CB  
888  C CG  . ARG   B 50  ? 0.7692 0.7743 0.6563 0.1019  0.1085  -0.0847 59  ARG   B CG  
889  C CD  . ARG   B 50  ? 0.8023 0.8064 0.7197 0.0989  0.1134  -0.0917 59  ARG   B CD  
890  N NE  . ARG   B 50  ? 0.8192 0.8175 0.7377 0.0984  0.1153  -0.0806 59  ARG   B NE  
891  C CZ  . ARG   B 50  ? 0.8305 0.8199 0.7527 0.1088  0.1150  -0.0623 59  ARG   B CZ  
892  N NH1 . ARG   B 50  ? 0.8343 0.8196 0.7579 0.1210  0.1124  -0.0526 59  ARG   B NH1 
893  N NH2 . ARG   B 50  ? 0.8394 0.8255 0.7637 0.1068  0.1173  -0.0535 59  ARG   B NH2 
894  N N   . SER   B 51  ? 0.7103 0.7176 0.5342 0.1081  0.0949  -0.0738 60  SER   B N   
895  C CA  . SER   B 51  ? 0.7489 0.7521 0.5682 0.1219  0.0895  -0.0653 60  SER   B CA  
896  C C   . SER   B 51  ? 0.7774 0.7826 0.6206 0.1260  0.0904  -0.0729 60  SER   B C   
897  O O   . SER   B 51  ? 0.8105 0.8232 0.6583 0.1191  0.0904  -0.0869 60  SER   B O   
898  C CB  . SER   B 51  ? 0.7464 0.7516 0.5434 0.1213  0.0833  -0.0662 60  SER   B CB  
899  O OG  . SER   B 51  ? 0.7649 0.7670 0.5571 0.1350  0.0774  -0.0592 60  SER   B OG  
900  N N   . GLY   B 52  ? 0.8260 0.8253 0.6848 0.1365  0.0914  -0.0638 61  GLY   B N   
901  C CA  . GLY   B 52  ? 0.8607 0.8608 0.7475 0.1399  0.0930  -0.0706 61  GLY   B CA  
902  C C   . GLY   B 52  ? 0.8867 0.8916 0.7930 0.1275  0.0990  -0.0864 61  GLY   B C   
903  O O   . GLY   B 52  ? 0.8888 0.8909 0.8007 0.1227  0.1032  -0.0840 61  GLY   B O   
904  N N   . GLU   B 53  ? 0.9275 0.9409 0.8440 0.1222  0.0995  -0.1027 62  GLU   B N   
905  C CA  . GLU   B 53  ? 0.9577 0.9795 0.8887 0.1095  0.1052  -0.1208 62  GLU   B CA  
906  C C   . GLU   B 53  ? 0.9144 0.9465 0.8237 0.0972  0.1055  -0.1297 62  GLU   B C   
907  O O   . GLU   B 53  ? 0.8980 0.9397 0.8148 0.0860  0.1102  -0.1445 62  GLU   B O   
908  C CB  . GLU   B 53  ? 1.0098 1.0355 0.9703 0.1124  0.1065  -0.1333 62  GLU   B CB  
909  C CG  . GLU   B 53  ? 1.0749 1.0908 1.0619 0.1204  0.1078  -0.1267 62  GLU   B CG  
910  C CD  . GLU   B 53  ? 1.1399 1.1577 1.1582 0.1255  0.1079  -0.1369 62  GLU   B CD  
911  O OE1 . GLU   B 53  ? 1.1902 1.2158 1.2073 0.1264  0.1057  -0.1455 62  GLU   B OE1 
912  O OE2 . GLU   B 53  ? 1.2094 1.2206 1.2546 0.1289  0.1099  -0.1360 62  GLU   B OE2 
913  N N   . GLY   B 54  ? 0.8642 0.8947 0.7484 0.0993  0.1004  -0.1207 63  GLY   B N   
914  C CA  . GLY   B 54  ? 0.8404 0.8782 0.7025 0.0882  0.0996  -0.1246 63  GLY   B CA  
915  C C   . GLY   B 54  ? 0.8262 0.8623 0.6759 0.0808  0.1020  -0.1200 63  GLY   B C   
916  O O   . GLY   B 54  ? 0.8417 0.8684 0.6931 0.0872  0.1023  -0.1089 63  GLY   B O   
917  N N   . ARG   B 55  ? 0.7804 0.8265 0.6191 0.0676  0.1039  -0.1281 64  ARG   B N   
918  C CA  . ARG   B 55  ? 0.7449 0.7913 0.5696 0.0593  0.1053  -0.1244 64  ARG   B CA  
919  C C   . ARG   B 55  ? 0.6976 0.7433 0.4957 0.0566  0.1000  -0.1162 64  ARG   B C   
920  O O   . ARG   B 55  ? 0.7007 0.7521 0.4941 0.0540  0.0976  -0.1204 64  ARG   B O   
921  C CB  . ARG   B 55  ? 0.7593 0.8189 0.5935 0.0466  0.1113  -0.1404 64  ARG   B CB  
922  C CG  . ARG   B 55  ? 0.7882 0.8493 0.6121 0.0384  0.1128  -0.1383 64  ARG   B CG  
923  C CD  . ARG   B 55  ? 0.8142 0.8927 0.6412 0.0249  0.1175  -0.1552 64  ARG   B CD  
924  N NE  . ARG   B 55  ? 0.8474 0.9302 0.6629 0.0159  0.1184  -0.1548 64  ARG   B NE  
925  C CZ  . ARG   B 55  ? 0.8695 0.9550 0.6980 0.0126  0.1217  -0.1623 64  ARG   B CZ  
926  N NH1 . ARG   B 55  ? 0.8845 0.9679 0.7399 0.0174  0.1247  -0.1712 64  ARG   B NH1 
927  N NH2 . ARG   B 55  ? 0.8662 0.9563 0.6818 0.0045  0.1214  -0.1610 64  ARG   B NH2 
928  N N   . LEU   B 56  ? 0.6490 0.6875 0.4320 0.0577  0.0978  -0.1045 65  LEU   B N   
929  C CA  . LEU   B 56  ? 0.6255 0.6631 0.3848 0.0541  0.0926  -0.0975 65  LEU   B CA  
930  C C   . LEU   B 56  ? 0.5985 0.6429 0.3502 0.0414  0.0953  -0.1000 65  LEU   B C   
931  O O   . LEU   B 56  ? 0.6017 0.6422 0.3566 0.0425  0.0975  -0.0960 65  LEU   B O   
932  C CB  . LEU   B 56  ? 0.6105 0.6354 0.3581 0.0665  0.0873  -0.0822 65  LEU   B CB  
933  C CG  . LEU   B 56  ? 0.6334 0.6516 0.3855 0.0810  0.0837  -0.0773 65  LEU   B CG  
934  C CD1 . LEU   B 56  ? 0.6254 0.6354 0.3581 0.0897  0.0770  -0.0649 65  LEU   B CD1 
935  C CD2 . LEU   B 56  ? 0.6413 0.6652 0.4007 0.0803  0.0819  -0.0868 65  LEU   B CD2 
936  N N   . ASP   B 57  ? 0.5857 0.6412 0.3291 0.0296  0.0955  -0.1063 66  ASP   B N   
937  C CA  . ASP   B 57  ? 0.5612 0.6243 0.2946 0.0177  0.0971  -0.1074 66  ASP   B CA  
938  C C   . ASP   B 57  ? 0.5414 0.5990 0.2533 0.0162  0.0909  -0.0949 66  ASP   B C   
939  O O   . ASP   B 57  ? 0.5560 0.6097 0.2593 0.0187  0.0855  -0.0898 66  ASP   B O   
940  C CB  . ASP   B 57  ? 0.5840 0.6651 0.3206 0.0049  0.1015  -0.1210 66  ASP   B CB  
941  C CG  . ASP   B 57  ? 0.6128 0.7002 0.3725 0.0063  0.1077  -0.1352 66  ASP   B CG  
942  O OD1 . ASP   B 57  ? 0.6365 0.7175 0.4080 0.0115  0.1097  -0.1355 66  ASP   B OD1 
943  O OD2 . ASP   B 57  ? 0.6314 0.7304 0.3985 0.0021  0.1105  -0.1459 66  ASP   B OD2 
944  N N   . PRO   B 58  ? 0.5263 0.5834 0.2299 0.0122  0.0907  -0.0899 67  PRO   B N   
945  C CA  . PRO   B 58  ? 0.5233 0.5757 0.2077 0.0103  0.0845  -0.0785 67  PRO   B CA  
946  C C   . PRO   B 58  ? 0.5210 0.5825 0.1960 0.0000  0.0822  -0.0803 67  PRO   B C   
947  O O   . PRO   B 58  ? 0.5130 0.5888 0.1937 -0.0096 0.0874  -0.0910 67  PRO   B O   
948  C CB  . PRO   B 58  ? 0.5226 0.5770 0.2048 0.0059  0.0864  -0.0767 67  PRO   B CB  
949  C CG  . PRO   B 58  ? 0.5418 0.6070 0.2399 0.0004  0.0935  -0.0903 67  PRO   B CG  
950  C CD  . PRO   B 58  ? 0.5424 0.6031 0.2562 0.0094  0.0958  -0.0951 67  PRO   B CD  
951  N N   . TYR   B 59  ? 0.5095 0.5637 0.1717 0.0015  0.0750  -0.0706 68  TYR   B N   
952  C CA  . TYR   B 59  ? 0.5117 0.5722 0.1658 -0.0078 0.0716  -0.0691 68  TYR   B CA  
953  C C   . TYR   B 59  ? 0.5093 0.5685 0.1479 -0.0142 0.0665  -0.0589 68  TYR   B C   
954  O O   . TYR   B 59  ? 0.5146 0.5856 0.1470 -0.0272 0.0669  -0.0587 68  TYR   B O   
955  C CB  . TYR   B 59  ? 0.5248 0.5775 0.1813 -0.0004 0.0662  -0.0674 68  TYR   B CB  
956  C CG  . TYR   B 59  ? 0.5235 0.5838 0.1765 -0.0109 0.0636  -0.0670 68  TYR   B CG  
957  C CD1 . TYR   B 59  ? 0.5351 0.5899 0.1761 -0.0145 0.0562  -0.0565 68  TYR   B CD1 
958  C CD2 . TYR   B 59  ? 0.5262 0.5983 0.1897 -0.0164 0.0678  -0.0762 68  TYR   B CD2 
959  C CE1 . TYR   B 59  ? 0.5429 0.6035 0.1826 -0.0240 0.0530  -0.0541 68  TYR   B CE1 
960  C CE2 . TYR   B 59  ? 0.5340 0.6128 0.1958 -0.0256 0.0651  -0.0742 68  TYR   B CE2 
961  C CZ  . TYR   B 59  ? 0.5486 0.6211 0.1988 -0.0294 0.0575  -0.0626 68  TYR   B CZ  
962  O OH  . TYR   B 59  ? 0.5762 0.6541 0.2261 -0.0388 0.0542  -0.0585 68  TYR   B OH  
963  N N   . TRP   B 60  ? 0.4968 0.5426 0.1292 -0.0051 0.0612  -0.0498 69  TRP   B N   
964  C CA  . TRP   B 60  ? 0.4928 0.5335 0.1121 -0.0073 0.0547  -0.0389 69  TRP   B CA  
965  C C   . TRP   B 60  ? 0.5005 0.5337 0.1190 0.0012  0.0550  -0.0346 69  TRP   B C   
966  O O   . TRP   B 60  ? 0.4800 0.5043 0.1045 0.0142  0.0557  -0.0346 69  TRP   B O   
967  C CB  . TRP   B 60  ? 0.4966 0.5292 0.1097 -0.0059 0.0459  -0.0319 69  TRP   B CB  
968  C CG  . TRP   B 60  ? 0.4989 0.5240 0.1011 -0.0053 0.0388  -0.0211 69  TRP   B CG  
969  C CD1 . TRP   B 60  ? 0.5094 0.5403 0.1033 -0.0168 0.0362  -0.0149 69  TRP   B CD1 
970  C CD2 . TRP   B 60  ? 0.4956 0.5076 0.0947 0.0078  0.0342  -0.0153 69  TRP   B CD2 
971  N NE1 . TRP   B 60  ? 0.5046 0.5254 0.0917 -0.0111 0.0296  -0.0060 69  TRP   B NE1 
972  C CE2 . TRP   B 60  ? 0.5048 0.5140 0.0948 0.0040  0.0282  -0.0064 69  TRP   B CE2 
973  C CE3 . TRP   B 60  ? 0.4957 0.4981 0.0983 0.0235  0.0335  -0.0159 69  TRP   B CE3 
974  C CZ2 . TRP   B 60  ? 0.5032 0.5018 0.0886 0.0141  0.0225  0.0004  69  TRP   B CZ2 
975  C CZ3 . TRP   B 60  ? 0.5047 0.4977 0.1014 0.0335  0.0287  -0.0089 69  TRP   B CZ3 
976  C CH2 . TRP   B 60  ? 0.5043 0.4956 0.0931 0.0289  0.0236  -0.0014 69  TRP   B CH2 
977  N N   . GLY   B 61  ? 0.5067 0.5420 0.1177 -0.0039 0.0536  -0.0293 70  GLY   B N   
978  C CA  . GLY   B 61  ? 0.5106 0.5373 0.1206 0.0054  0.0524  -0.0230 70  GLY   B CA  
979  C C   . GLY   B 61  ? 0.5233 0.5503 0.1229 0.0003  0.0474  -0.0148 70  GLY   B C   
980  O O   . GLY   B 61  ? 0.5132 0.5511 0.1074 -0.0132 0.0472  -0.0157 70  GLY   B O   
981  N N   . ASP   B 62  ? 0.5261 0.5451 0.1238 0.0092  0.0448  -0.0078 71  ASP   B N   
982  C CA  . ASP   B 62  ? 0.5467 0.5651 0.1356 0.0060  0.0392  0.0005  71  ASP   B CA  
983  C C   . ASP   B 62  ? 0.5493 0.5635 0.1424 0.0154  0.0411  0.0040  71  ASP   B C   
984  O O   . ASP   B 62  ? 0.5348 0.5394 0.1285 0.0287  0.0394  0.0075  71  ASP   B O   
985  C CB  . ASP   B 62  ? 0.5742 0.5855 0.1543 0.0061  0.0299  0.0075  71  ASP   B CB  
986  C CG  . ASP   B 62  ? 0.6084 0.6186 0.1808 0.0028  0.0232  0.0165  71  ASP   B CG  
987  O OD1 . ASP   B 62  ? 0.6362 0.6419 0.2090 0.0111  0.0223  0.0206  71  ASP   B OD1 
988  O OD2 . ASP   B 62  ? 0.6952 0.7117 0.2618 -0.0093 0.0199  0.0193  71  ASP   B OD2 
989  N N   . VAL   B 63  ? 0.5419 0.5638 0.1388 0.0097  0.0448  0.0025  72  VAL   B N   
990  C CA  . VAL   B 63  ? 0.5500 0.5697 0.1533 0.0172  0.0471  0.0064  72  VAL   B CA  
991  C C   . VAL   B 63  ? 0.5602 0.5718 0.1553 0.0251  0.0398  0.0168  72  VAL   B C   
992  O O   . VAL   B 63  ? 0.5467 0.5528 0.1462 0.0377  0.0413  0.0213  72  VAL   B O   
993  C CB  . VAL   B 63  ? 0.5628 0.5934 0.1716 0.0074  0.0506  0.0023  72  VAL   B CB  
994  C CG1 . VAL   B 63  ? 0.5702 0.5988 0.1834 0.0133  0.0502  0.0091  72  VAL   B CG1 
995  C CG2 . VAL   B 63  ? 0.5508 0.5873 0.1729 0.0043  0.0587  -0.0085 72  VAL   B CG2 
996  N N   . LYS   B 64  ? 0.5624 0.5731 0.1471 0.0197  0.0320  0.0211  73  LYS   B N   
997  C CA  . LYS   B 64  ? 0.5847 0.5879 0.1638 0.0275  0.0246  0.0301  73  LYS   B CA  
998  C C   . LYS   B 64  ? 0.5739 0.5664 0.1517 0.0413  0.0219  0.0313  73  LYS   B C   
999  O O   . LYS   B 64  ? 0.6124 0.5997 0.1905 0.0542  0.0205  0.0360  73  LYS   B O   
1000 C CB  . LYS   B 64  ? 0.5917 0.5962 0.1619 0.0180  0.0162  0.0353  73  LYS   B CB  
1001 C CG  . LYS   B 64  ? 0.6113 0.6094 0.1786 0.0256  0.0088  0.0437  73  LYS   B CG  
1002 C CD  . LYS   B 64  ? 0.6349 0.6347 0.1959 0.0168  0.0006  0.0502  73  LYS   B CD  
1003 C CE  . LYS   B 64  ? 0.6537 0.6448 0.2137 0.0268  -0.0074 0.0575  73  LYS   B CE  
1004 N NZ  . LYS   B 64  ? 0.6731 0.6662 0.2282 0.0174  -0.0159 0.0649  73  LYS   B NZ  
1005 N N   . GLN   B 65  ? 0.5789 0.5689 0.1553 0.0397  0.0208  0.0269  74  GLN   B N   
1006 C CA  . GLN   B 65  ? 0.5897 0.5708 0.1655 0.0525  0.0182  0.0259  74  GLN   B CA  
1007 C C   . GLN   B 65  ? 0.5720 0.5539 0.1547 0.0626  0.0262  0.0234  74  GLN   B C   
1008 O O   . GLN   B 65  ? 0.5307 0.5065 0.1115 0.0760  0.0238  0.0245  74  GLN   B O   
1009 C CB  . GLN   B 65  ? 0.6189 0.5981 0.1936 0.0476  0.0151  0.0214  74  GLN   B CB  
1010 C CG  . GLN   B 65  ? 0.6731 0.6514 0.2423 0.0370  0.0071  0.0254  74  GLN   B CG  
1011 C CD  . GLN   B 65  ? 0.7130 0.6898 0.2835 0.0328  0.0044  0.0215  74  GLN   B CD  
1012 O OE1 . GLN   B 65  ? 0.7554 0.7264 0.3286 0.0426  0.0032  0.0174  74  GLN   B OE1 
1013 N NE2 . GLN   B 65  ? 0.7483 0.7318 0.3174 0.0181  0.0039  0.0226  74  GLN   B NE2 
1014 N N   . ASP   B 66  ? 0.5530 0.5421 0.1436 0.0575  0.0345  0.0210  75  ASP   B N   
1015 C CA  . ASP   B 66  ? 0.5488 0.5393 0.1496 0.0646  0.0429  0.0187  75  ASP   B CA  
1016 C C   . ASP   B 66  ? 0.5428 0.5298 0.1447 0.0701  0.0432  0.0138  75  ASP   B C   
1017 O O   . ASP   B 66  ? 0.5297 0.5137 0.1342 0.0833  0.0454  0.0161  75  ASP   B O   
1018 C CB  . ASP   B 66  ? 0.5571 0.5452 0.1594 0.0782  0.0446  0.0261  75  ASP   B CB  
1019 C CG  . ASP   B 66  ? 0.5451 0.5361 0.1600 0.0832  0.0536  0.0268  75  ASP   B CG  
1020 O OD1 . ASP   B 66  ? 0.5372 0.5323 0.1623 0.0752  0.0591  0.0214  75  ASP   B OD1 
1021 O OD2 . ASP   B 66  ? 0.5538 0.5427 0.1684 0.0974  0.0549  0.0333  75  ASP   B OD2 
1022 N N   . LEU   B 67  ? 0.5312 0.5192 0.1310 0.0616  0.0407  0.0081  76  LEU   B N   
1023 C CA  . LEU   B 67  ? 0.5230 0.5096 0.1260 0.0644  0.0410  0.0021  76  LEU   B CA  
1024 C C   . LEU   B 67  ? 0.5278 0.5225 0.1387 0.0524  0.0467  -0.0062 76  LEU   B C   
1025 O O   . LEU   B 67  ? 0.5157 0.5174 0.1253 0.0394  0.0477  -0.0078 76  LEU   B O   
1026 C CB  . LEU   B 67  ? 0.5374 0.5181 0.1318 0.0659  0.0315  0.0029  76  LEU   B CB  
1027 C CG  . LEU   B 67  ? 0.5599 0.5327 0.1474 0.0803  0.0251  0.0084  76  LEU   B CG  
1028 C CD1 . LEU   B 67  ? 0.5780 0.5450 0.1604 0.0795  0.0153  0.0071  76  LEU   B CD1 
1029 C CD2 . LEU   B 67  ? 0.5610 0.5323 0.1515 0.0953  0.0285  0.0081  76  LEU   B CD2 
1030 N N   . VAL   B 68  ? 0.5125 0.5073 0.1301 0.0557  0.0491  -0.0121 77  VAL   B N   
1031 C CA  . VAL   B 68  ? 0.5021 0.5050 0.1291 0.0464  0.0546  -0.0216 77  VAL   B CA  
1032 C C   . VAL   B 68  ? 0.4972 0.4973 0.1278 0.0530  0.0528  -0.0258 77  VAL   B C   
1033 O O   . VAL   B 68  ? 0.4808 0.4738 0.1115 0.0676  0.0510  -0.0220 77  VAL   B O   
1034 C CB  . VAL   B 68  ? 0.5035 0.5117 0.1426 0.0441  0.0630  -0.0252 77  VAL   B CB  
1035 C CG1 . VAL   B 68  ? 0.5125 0.5148 0.1598 0.0580  0.0662  -0.0208 77  VAL   B CG1 
1036 C CG2 . VAL   B 68  ? 0.5058 0.5236 0.1549 0.0343  0.0683  -0.0367 77  VAL   B CG2 
1037 N N   A SER   B 69  ? 0.4948 0.5008 0.1278 0.0437  0.0527  -0.0327 78  SER   B N   
1038 N N   B SER   B 69  ? 0.4948 0.5008 0.1278 0.0437  0.0527  -0.0327 78  SER   B N   
1039 N N   C SER   B 69  ? 0.4948 0.5008 0.1278 0.0437  0.0527  -0.0327 78  SER   B N   
1040 N N   D SER   B 69  ? 0.4948 0.5008 0.1278 0.0437  0.0527  -0.0327 78  SER   B N   
1041 C CA  A SER   B 69  ? 0.4961 0.5022 0.1358 0.0475  0.0520  -0.0388 78  SER   B CA  
1042 C CA  B SER   B 69  ? 0.4961 0.5022 0.1358 0.0475  0.0520  -0.0388 78  SER   B CA  
1043 C CA  C SER   B 69  ? 0.4961 0.5022 0.1359 0.0475  0.0520  -0.0388 78  SER   B CA  
1044 C CA  D SER   B 69  ? 0.4961 0.5022 0.1359 0.0475  0.0520  -0.0388 78  SER   B CA  
1045 C C   A SER   B 69  ? 0.5008 0.5169 0.1540 0.0406  0.0600  -0.0488 78  SER   B C   
1046 C C   B SER   B 69  ? 0.5008 0.5169 0.1540 0.0406  0.0600  -0.0488 78  SER   B C   
1047 C C   C SER   B 69  ? 0.5009 0.5170 0.1541 0.0406  0.0600  -0.0488 78  SER   B C   
1048 C C   D SER   B 69  ? 0.5009 0.5170 0.1541 0.0406  0.0600  -0.0488 78  SER   B C   
1049 O O   A SER   B 69  ? 0.4988 0.5241 0.1529 0.0285  0.0645  -0.0526 78  SER   B O   
1050 O O   B SER   B 69  ? 0.4988 0.5241 0.1529 0.0285  0.0645  -0.0526 78  SER   B O   
1051 O O   C SER   B 69  ? 0.4988 0.5241 0.1529 0.0285  0.0645  -0.0526 78  SER   B O   
1052 O O   D SER   B 69  ? 0.4988 0.5241 0.1529 0.0285  0.0645  -0.0526 78  SER   B O   
1053 C CB  A SER   B 69  ? 0.4998 0.5045 0.1331 0.0434  0.0444  -0.0383 78  SER   B CB  
1054 C CB  B SER   B 69  ? 0.4998 0.5045 0.1331 0.0434  0.0444  -0.0383 78  SER   B CB  
1055 C CB  C SER   B 69  ? 0.4998 0.5046 0.1332 0.0434  0.0444  -0.0383 78  SER   B CB  
1056 C CB  D SER   B 69  ? 0.4998 0.5046 0.1332 0.0434  0.0444  -0.0383 78  SER   B CB  
1057 O OG  A SER   B 69  ? 0.4991 0.5134 0.1312 0.0274  0.0460  -0.0406 78  SER   B OG  
1058 O OG  B SER   B 69  ? 0.4991 0.5134 0.1312 0.0274  0.0460  -0.0406 78  SER   B OG  
1059 O OG  C SER   B 69  ? 0.4992 0.5136 0.1313 0.0274  0.0460  -0.0406 78  SER   B OG  
1060 O OG  D SER   B 69  ? 0.4992 0.5136 0.1313 0.0274  0.0460  -0.0406 78  SER   B OG  
1061 N N   A TYR   B 70  ? 0.5053 0.5205 0.1690 0.0483  0.0615  -0.0536 79  TYR   B N   
1062 N N   B TYR   B 70  ? 0.5053 0.5205 0.1690 0.0483  0.0615  -0.0536 79  TYR   B N   
1063 N N   C TYR   B 70  ? 0.5061 0.5213 0.1698 0.0483  0.0614  -0.0536 79  TYR   B N   
1064 N N   D TYR   B 70  ? 0.5061 0.5213 0.1698 0.0483  0.0614  -0.0536 79  TYR   B N   
1065 C CA  A TYR   B 70  ? 0.5057 0.5298 0.1850 0.0438  0.0685  -0.0644 79  TYR   B CA  
1066 C CA  B TYR   B 70  ? 0.5057 0.5298 0.1850 0.0438  0.0685  -0.0644 79  TYR   B CA  
1067 C CA  C TYR   B 70  ? 0.5070 0.5310 0.1863 0.0439  0.0685  -0.0643 79  TYR   B CA  
1068 C CA  D TYR   B 70  ? 0.5070 0.5310 0.1863 0.0439  0.0685  -0.0643 79  TYR   B CA  
1069 C C   A TYR   B 70  ? 0.5141 0.5420 0.1978 0.0426  0.0659  -0.0705 79  TYR   B C   
1070 C C   B TYR   B 70  ? 0.5141 0.5420 0.1978 0.0426  0.0659  -0.0705 79  TYR   B C   
1071 C C   C TYR   B 70  ? 0.5156 0.5435 0.1994 0.0426  0.0660  -0.0706 79  TYR   B C   
1072 C C   D TYR   B 70  ? 0.5156 0.5435 0.1994 0.0426  0.0660  -0.0706 79  TYR   B C   
1073 O O   A TYR   B 70  ? 0.5140 0.5342 0.1943 0.0524  0.0595  -0.0668 79  TYR   B O   
1074 O O   B TYR   B 70  ? 0.5140 0.5342 0.1943 0.0524  0.0595  -0.0668 79  TYR   B O   
1075 O O   C TYR   B 70  ? 0.5155 0.5359 0.1954 0.0519  0.0594  -0.0667 79  TYR   B O   
1076 O O   D TYR   B 70  ? 0.5155 0.5359 0.1954 0.0519  0.0594  -0.0667 79  TYR   B O   
1077 C CB  A TYR   B 70  ? 0.5012 0.5210 0.1929 0.0546  0.0728  -0.0639 79  TYR   B CB  
1078 C CB  B TYR   B 70  ? 0.5012 0.5210 0.1929 0.0546  0.0728  -0.0639 79  TYR   B CB  
1079 C CB  C TYR   B 70  ? 0.5030 0.5227 0.1947 0.0548  0.0727  -0.0639 79  TYR   B CB  
1080 C CB  D TYR   B 70  ? 0.5030 0.5227 0.1947 0.0548  0.0727  -0.0639 79  TYR   B CB  
1081 C CG  A TYR   B 70  ? 0.5003 0.5188 0.1928 0.0536  0.0768  -0.0597 79  TYR   B CG  
1082 C CG  B TYR   B 70  ? 0.5003 0.5188 0.1928 0.0536  0.0768  -0.0597 79  TYR   B CG  
1083 C CG  C TYR   B 70  ? 0.5025 0.5206 0.1945 0.0542  0.0764  -0.0591 79  TYR   B CG  
1084 C CG  D TYR   B 70  ? 0.5025 0.5206 0.1945 0.0542  0.0764  -0.0591 79  TYR   B CG  
1085 C CD1 A TYR   B 70  ? 0.4996 0.5106 0.1811 0.0599  0.0735  -0.0484 79  TYR   B CD1 
1086 C CD1 B TYR   B 70  ? 0.4996 0.5106 0.1811 0.0599  0.0735  -0.0484 79  TYR   B CD1 
1087 C CD1 C TYR   B 70  ? 0.5022 0.5127 0.1821 0.0601  0.0728  -0.0480 79  TYR   B CD1 
1088 C CD1 D TYR   B 70  ? 0.5022 0.5127 0.1821 0.0601  0.0728  -0.0480 79  TYR   B CD1 
1089 C CD2 A TYR   B 70  ? 0.4987 0.5247 0.2042 0.0461  0.0837  -0.0678 79  TYR   B CD2 
1090 C CD2 B TYR   B 70  ? 0.4987 0.5247 0.2042 0.0461  0.0837  -0.0678 79  TYR   B CD2 
1091 C CD2 C TYR   B 70  ? 0.5010 0.5259 0.2060 0.0472  0.0834  -0.0667 79  TYR   B CD2 
1092 C CD2 D TYR   B 70  ? 0.5010 0.5259 0.2060 0.0472  0.0834  -0.0667 79  TYR   B CD2 
1093 C CE1 A TYR   B 70  ? 0.4985 0.5092 0.1824 0.0584  0.0772  -0.0445 79  TYR   B CE1 
1094 C CE1 B TYR   B 70  ? 0.4985 0.5092 0.1824 0.0584  0.0772  -0.0445 79  TYR   B CE1 
1095 C CE1 C TYR   B 70  ? 0.5016 0.5116 0.1833 0.0592  0.0762  -0.0435 79  TYR   B CE1 
1096 C CE1 D TYR   B 70  ? 0.5016 0.5116 0.1833 0.0592  0.0762  -0.0435 79  TYR   B CE1 
1097 C CE2 A TYR   B 70  ? 0.4982 0.5234 0.2065 0.0446  0.0868  -0.0647 79  TYR   B CE2 
1098 C CE2 B TYR   B 70  ? 0.4982 0.5234 0.2065 0.0446  0.0868  -0.0647 79  TYR   B CE2 
1099 C CE2 C TYR   B 70  ? 0.5012 0.5250 0.2084 0.0461  0.0863  -0.0630 79  TYR   B CE2 
1100 C CE2 D TYR   B 70  ? 0.5012 0.5250 0.2084 0.0461  0.0863  -0.0630 79  TYR   B CE2 
1101 C CZ  A TYR   B 70  ? 0.4994 0.5171 0.1970 0.0504  0.0836  -0.0526 79  TYR   B CZ  
1102 C CZ  B TYR   B 70  ? 0.4994 0.5171 0.1970 0.0504  0.0836  -0.0526 79  TYR   B CZ  
1103 C CZ  C TYR   B 70  ? 0.5033 0.5197 0.1990 0.0519  0.0828  -0.0509 79  TYR   B CZ  
1104 C CZ  D TYR   B 70  ? 0.5033 0.5197 0.1990 0.0519  0.0828  -0.0509 79  TYR   B CZ  
1105 O OH  A TYR   B 70  ? 0.5015 0.5204 0.2044 0.0473  0.0871  -0.0508 79  TYR   B OH  
1106 O OH  B TYR   B 70  ? 0.5015 0.5204 0.2044 0.0473  0.0871  -0.0508 79  TYR   B OH  
1107 O OH  C TYR   B 70  ? 0.5081 0.5250 0.2077 0.0495  0.0858  -0.0479 79  TYR   B OH  
1108 O OH  D TYR   B 70  ? 0.5081 0.5250 0.2077 0.0495  0.0858  -0.0479 79  TYR   B OH  
1109 N N   A CYS   B 71  ? 0.5189 0.5594 0.2098 0.0309  0.0706  -0.0800 80  CYS   B N   
1110 N N   B CYS   B 71  ? 0.5189 0.5594 0.2098 0.0309  0.0706  -0.0800 80  CYS   B N   
1111 N N   C CYS   B 71  ? 0.5207 0.5611 0.2129 0.0315  0.0711  -0.0805 80  CYS   B N   
1112 N N   D CYS   B 71  ? 0.5207 0.5611 0.2129 0.0315  0.0711  -0.0805 80  CYS   B N   
1113 C CA  A CYS   B 71  ? 0.5281 0.5751 0.2285 0.0292  0.0703  -0.0880 80  CYS   B CA  
1114 C CA  B CYS   B 71  ? 0.5281 0.5751 0.2285 0.0292  0.0703  -0.0880 80  CYS   B CA  
1115 C CA  C CYS   B 71  ? 0.5302 0.5771 0.2314 0.0297  0.0707  -0.0883 80  CYS   B CA  
1116 C CA  D CYS   B 71  ? 0.5302 0.5771 0.2314 0.0297  0.0707  -0.0883 80  CYS   B CA  
1117 C C   A CYS   B 71  ? 0.5304 0.5790 0.2214 0.0219  0.0643  -0.0846 80  CYS   B C   
1118 C C   B CYS   B 71  ? 0.5304 0.5790 0.2214 0.0219  0.0643  -0.0846 80  CYS   B C   
1119 C C   C CYS   B 71  ? 0.5324 0.5795 0.2236 0.0237  0.0640  -0.0841 80  CYS   B C   
1120 C C   D CYS   B 71  ? 0.5324 0.5795 0.2236 0.0237  0.0640  -0.0841 80  CYS   B C   
1121 O O   A CYS   B 71  ? 0.5365 0.5972 0.2359 0.0134  0.0666  -0.0924 80  CYS   B O   
1122 O O   B CYS   B 71  ? 0.5365 0.5972 0.2359 0.0134  0.0666  -0.0924 80  CYS   B O   
1123 O O   C CYS   B 71  ? 0.5376 0.5902 0.2364 0.0216  0.0628  -0.0896 80  CYS   B O   
1124 O O   D CYS   B 71  ? 0.5376 0.5902 0.2364 0.0216  0.0628  -0.0896 80  CYS   B O   
1125 C CB  A CYS   B 71  ? 0.5364 0.5751 0.2447 0.0442  0.0672  -0.0876 80  CYS   B CB  
1126 C CB  B CYS   B 71  ? 0.5364 0.5751 0.2447 0.0442  0.0672  -0.0876 80  CYS   B CB  
1127 C CB  C CYS   B 71  ? 0.5385 0.5778 0.2486 0.0443  0.0680  -0.0886 80  CYS   B CB  
1128 C CB  D CYS   B 71  ? 0.5385 0.5778 0.2486 0.0443  0.0680  -0.0886 80  CYS   B CB  
1129 S SG  A CYS   B 71  ? 0.5505 0.5836 0.2688 0.0543  0.0731  -0.0862 80  CYS   B SG  
1130 S SG  B CYS   B 71  ? 0.5505 0.5836 0.2688 0.0543  0.0731  -0.0862 80  CYS   B SG  
1131 S SG  C CYS   B 71  ? 0.5525 0.5924 0.2808 0.0509  0.0761  -0.0939 80  CYS   B SG  
1132 S SG  D CYS   B 71  ? 0.5525 0.5924 0.2808 0.0509  0.0761  -0.0939 80  CYS   B SG  
1133 N N   A GLY   B 72  ? 0.5315 0.5692 0.2075 0.0249  0.0571  -0.0735 81  GLY   B N   
1134 N N   B GLY   B 72  ? 0.5315 0.5692 0.2075 0.0249  0.0571  -0.0735 81  GLY   B N   
1135 N N   C GLY   B 72  ? 0.5342 0.5730 0.2104 0.0240  0.0583  -0.0739 81  GLY   B N   
1136 N N   D GLY   B 72  ? 0.5342 0.5730 0.2104 0.0240  0.0583  -0.0739 81  GLY   B N   
1137 C CA  A GLY   B 72  ? 0.5363 0.5734 0.2044 0.0181  0.0502  -0.0687 81  GLY   B CA  
1138 C CA  B GLY   B 72  ? 0.5363 0.5734 0.2044 0.0181  0.0502  -0.0687 81  GLY   B CA  
1139 C CA  C GLY   B 72  ? 0.5381 0.5756 0.2062 0.0180  0.0511  -0.0689 81  GLY   B CA  
1140 C CA  D GLY   B 72  ? 0.5381 0.5756 0.2062 0.0180  0.0511  -0.0689 81  GLY   B CA  
1141 C C   A GLY   B 72  ? 0.5372 0.5649 0.1903 0.0190  0.0448  -0.0578 81  GLY   B C   
1142 C C   B GLY   B 72  ? 0.5372 0.5649 0.1903 0.0190  0.0448  -0.0578 81  GLY   B C   
1143 C C   C GLY   B 72  ? 0.5385 0.5666 0.1917 0.0190  0.0456  -0.0580 81  GLY   B C   
1144 C C   D GLY   B 72  ? 0.5385 0.5666 0.1917 0.0190  0.0456  -0.0580 81  GLY   B C   
1145 O O   A GLY   B 72  ? 0.5388 0.5618 0.1874 0.0243  0.0467  -0.0542 81  GLY   B O   
1146 O O   B GLY   B 72  ? 0.5388 0.5618 0.1874 0.0243  0.0467  -0.0542 81  GLY   B O   
1147 O O   C GLY   B 72  ? 0.5399 0.5633 0.1888 0.0243  0.0473  -0.0544 81  GLY   B O   
1148 O O   D GLY   B 72  ? 0.5399 0.5633 0.1888 0.0243  0.0473  -0.0544 81  GLY   B O   
1149 N N   A PRO   B 73  ? 0.5437 0.5696 0.1913 0.0125  0.0377  -0.0527 82  PRO   B N   
1150 N N   B PRO   B 73  ? 0.5437 0.5696 0.1913 0.0125  0.0377  -0.0527 82  PRO   B N   
1151 N N   C PRO   B 73  ? 0.5435 0.5693 0.1912 0.0134  0.0383  -0.0530 82  PRO   B N   
1152 N N   D PRO   B 73  ? 0.5435 0.5693 0.1912 0.0134  0.0383  -0.0530 82  PRO   B N   
1153 C CA  A PRO   B 73  ? 0.5485 0.5672 0.1835 0.0101  0.0314  -0.0423 82  PRO   B CA  
1154 C CA  B PRO   B 73  ? 0.5485 0.5672 0.1835 0.0101  0.0314  -0.0423 82  PRO   B CA  
1155 C CA  C PRO   B 73  ? 0.5486 0.5676 0.1838 0.0106  0.0322  -0.0427 82  PRO   B CA  
1156 C CA  D PRO   B 73  ? 0.5486 0.5676 0.1838 0.0106  0.0322  -0.0427 82  PRO   B CA  
1157 C C   A PRO   B 73  ? 0.5492 0.5534 0.1808 0.0272  0.0249  -0.0394 82  PRO   B C   
1158 C C   B PRO   B 73  ? 0.5492 0.5534 0.1808 0.0272  0.0249  -0.0394 82  PRO   B C   
1159 C C   C PRO   B 73  ? 0.5493 0.5536 0.1809 0.0274  0.0252  -0.0395 82  PRO   B C   
1160 C C   D PRO   B 73  ? 0.5493 0.5536 0.1809 0.0274  0.0252  -0.0395 82  PRO   B C   
1161 O O   A PRO   B 73  ? 0.5545 0.5556 0.1925 0.0369  0.0231  -0.0443 82  PRO   B O   
1162 O O   B PRO   B 73  ? 0.5545 0.5556 0.1925 0.0369  0.0231  -0.0443 82  PRO   B O   
1163 O O   C PRO   B 73  ? 0.5547 0.5559 0.1927 0.0370  0.0231  -0.0443 82  PRO   B O   
1164 O O   D PRO   B 73  ? 0.5547 0.5559 0.1927 0.0370  0.0231  -0.0443 82  PRO   B O   
1165 C CB  A PRO   B 73  ? 0.5566 0.5779 0.1916 -0.0009 0.0256  -0.0385 82  PRO   B CB  
1166 C CB  B PRO   B 73  ? 0.5566 0.5779 0.1916 -0.0009 0.0256  -0.0385 82  PRO   B CB  
1167 C CB  C PRO   B 73  ? 0.5565 0.5792 0.1916 -0.0012 0.0272  -0.0393 82  PRO   B CB  
1168 C CB  D PRO   B 73  ? 0.5565 0.5792 0.1916 -0.0012 0.0272  -0.0393 82  PRO   B CB  
1169 C CG  A PRO   B 73  ? 0.5545 0.5807 0.2020 -0.0008 0.0263  -0.0465 82  PRO   B CG  
1170 C CG  B PRO   B 73  ? 0.5545 0.5807 0.2020 -0.0008 0.0263  -0.0465 82  PRO   B CG  
1171 C CG  C PRO   B 73  ? 0.5539 0.5806 0.2013 -0.0003 0.0273  -0.0471 82  PRO   B CG  
1172 C CG  D PRO   B 73  ? 0.5539 0.5806 0.2013 -0.0003 0.0273  -0.0471 82  PRO   B CG  
1173 C CD  A PRO   B 73  ? 0.5460 0.5802 0.2007 0.0023  0.0360  -0.0558 82  PRO   B CD  
1174 C CD  B PRO   B 73  ? 0.5460 0.5802 0.2007 0.0023  0.0360  -0.0558 82  PRO   B CD  
1175 C CD  C PRO   B 73  ? 0.5453 0.5794 0.2001 0.0033  0.0368  -0.0564 82  PRO   B CD  
1176 C CD  D PRO   B 73  ? 0.5453 0.5794 0.2001 0.0033  0.0368  -0.0564 82  PRO   B CD  
1177 N N   . TRP   B 74  ? 0.5495 0.5467 0.1713 0.0308  0.0219  -0.0318 83  TRP   B N   
1178 C CA  . TRP   B 74  ? 0.5507 0.5356 0.1674 0.0467  0.0153  -0.0284 83  TRP   B CA  
1179 C C   . TRP   B 74  ? 0.5737 0.5526 0.1933 0.0514  0.0059  -0.0307 83  TRP   B C   
1180 O O   . TRP   B 74  ? 0.5730 0.5514 0.1935 0.0422  0.0005  -0.0287 83  TRP   B O   
1181 C CB  . TRP   B 74  ? 0.5544 0.5344 0.1612 0.0462  0.0120  -0.0199 83  TRP   B CB  
1182 C CG  . TRP   B 74  ? 0.5479 0.5186 0.1493 0.0624  0.0077  -0.0168 83  TRP   B CG  
1183 C CD1 . TRP   B 74  ? 0.5634 0.5250 0.1613 0.0709  -0.0024 -0.0155 83  TRP   B CD1 
1184 C CD2 . TRP   B 74  ? 0.5473 0.5181 0.1470 0.0721  0.0135  -0.0149 83  TRP   B CD2 
1185 N NE1 . TRP   B 74  ? 0.5545 0.5118 0.1471 0.0859  -0.0029 -0.0134 83  TRP   B NE1 
1186 C CE2 . TRP   B 74  ? 0.5495 0.5124 0.1434 0.0870  0.0069  -0.0122 83  TRP   B CE2 
1187 C CE3 . TRP   B 74  ? 0.5367 0.5138 0.1411 0.0705  0.0236  -0.0157 83  TRP   B CE3 
1188 C CZ2 . TRP   B 74  ? 0.5437 0.5060 0.1346 0.0994  0.0107  -0.0086 83  TRP   B CZ2 
1189 C CZ3 . TRP   B 74  ? 0.5369 0.5119 0.1403 0.0825  0.0267  -0.0118 83  TRP   B CZ3 
1190 C CH2 . TRP   B 74  ? 0.5323 0.5006 0.1286 0.0970  0.0207  -0.0078 83  TRP   B CH2 
1191 N N   . LYS   B 75  ? 0.5724 0.5467 0.1937 0.0666  0.0034  -0.0344 84  LYS   B N   
1192 C CA  . LYS   B 75  ? 0.6052 0.5747 0.2307 0.0733  -0.0056 -0.0390 84  LYS   B CA  
1193 C C   . LYS   B 75  ? 0.6244 0.5835 0.2416 0.0869  -0.0150 -0.0362 84  LYS   B C   
1194 O O   . LYS   B 75  ? 0.6496 0.6038 0.2701 0.0916  -0.0247 -0.0403 84  LYS   B O   
1195 C CB  . LYS   B 75  ? 0.6064 0.5802 0.2396 0.0813  -0.0018 -0.0459 84  LYS   B CB  
1196 C CG  . LYS   B 75  ? 0.6068 0.5915 0.2505 0.0697  0.0070  -0.0509 84  LYS   B CG  
1197 C CD  . LYS   B 75  ? 0.6228 0.6115 0.2743 0.0583  0.0032  -0.0543 84  LYS   B CD  
1198 C CE  . LYS   B 75  ? 0.6305 0.6324 0.2914 0.0456  0.0128  -0.0591 84  LYS   B CE  
1199 N NZ  . LYS   B 75  ? 0.6538 0.6610 0.3232 0.0348  0.0093  -0.0616 84  LYS   B NZ  
1200 N N   . LEU   B 76  ? 0.6262 0.5830 0.2345 0.0940  -0.0123 -0.0308 85  LEU   B N   
1201 C CA  . LEU   B 76  ? 0.6411 0.5907 0.2416 0.1106  -0.0196 -0.0298 85  LEU   B CA  
1202 C C   . LEU   B 76  ? 0.6736 0.6160 0.2699 0.1072  -0.0279 -0.0257 85  LEU   B C   
1203 O O   . LEU   B 76  ? 0.6814 0.6247 0.2742 0.0989  -0.0241 -0.0190 85  LEU   B O   
1204 C CB  . LEU   B 76  ? 0.6258 0.5780 0.2203 0.1210  -0.0120 -0.0255 85  LEU   B CB  
1205 C CG  . LEU   B 76  ? 0.6120 0.5709 0.2129 0.1228  -0.0031 -0.0279 85  LEU   B CG  
1206 C CD1 . LEU   B 76  ? 0.6034 0.5645 0.2005 0.1320  0.0041  -0.0218 85  LEU   B CD1 
1207 C CD2 . LEU   B 76  ? 0.6300 0.5894 0.2357 0.1307  -0.0081 -0.0351 85  LEU   B CD2 
1208 N N   . ASP   B 77  ? 0.7182 0.6538 0.3160 0.1138  -0.0394 -0.0299 86  ASP   B N   
1209 C CA  . ASP   B 77  ? 0.7599 0.6874 0.3588 0.1083  -0.0492 -0.0272 86  ASP   B CA  
1210 C C   . ASP   B 77  ? 0.7393 0.6595 0.3332 0.1250  -0.0591 -0.0301 86  ASP   B C   
1211 O O   . ASP   B 77  ? 0.7196 0.6319 0.3159 0.1230  -0.0685 -0.0288 86  ASP   B O   
1212 C CB  . ASP   B 77  ? 0.8174 0.7439 0.4278 0.0958  -0.0546 -0.0298 86  ASP   B CB  
1213 C CG  . ASP   B 77  ? 0.8806 0.8060 0.4984 0.1038  -0.0612 -0.0395 86  ASP   B CG  
1214 O OD1 . ASP   B 77  ? 0.8905 0.8180 0.5036 0.1188  -0.0600 -0.0446 86  ASP   B OD1 
1215 O OD2 . ASP   B 77  ? 0.9555 0.8789 0.5844 0.0947  -0.0675 -0.0415 86  ASP   B OD2 
1216 N N   . ALA   B 78  ? 0.7252 0.6483 0.3127 0.1415  -0.0573 -0.0337 87  ALA   B N   
1217 C CA  . ALA   B 78  ? 0.7169 0.6352 0.2990 0.1579  -0.0667 -0.0377 87  ALA   B CA  
1218 C C   . ALA   B 78  ? 0.7075 0.6252 0.2815 0.1614  -0.0639 -0.0305 87  ALA   B C   
1219 O O   . ALA   B 78  ? 0.6830 0.6066 0.2530 0.1573  -0.0526 -0.0232 87  ALA   B O   
1220 C CB  . ALA   B 78  ? 0.7161 0.6396 0.2936 0.1749  -0.0668 -0.0444 87  ALA   B CB  
1221 N N   . ALA   B 79  ? 0.7239 0.6356 0.2962 0.1715  -0.0742 -0.0339 88  ALA   B N   
1222 C CA  . ALA   B 79  ? 0.7437 0.6538 0.3108 0.1757  -0.0746 -0.0286 88  ALA   B CA  
1223 C C   . ALA   B 79  ? 0.7321 0.6447 0.2914 0.1971  -0.0788 -0.0346 88  ALA   B C   
1224 O O   . ALA   B 79  ? 0.7530 0.6627 0.3146 0.2065  -0.0889 -0.0448 88  ALA   B O   
1225 C CB  . ALA   B 79  ? 0.7632 0.6633 0.3385 0.1643  -0.0839 -0.0263 88  ALA   B CB  
1226 N N   . TRP   B 80  ? 0.7214 0.6402 0.2726 0.2045  -0.0715 -0.0286 89  TRP   B N   
1227 C CA  . TRP   B 80  ? 0.7494 0.6717 0.2933 0.2237  -0.0753 -0.0327 89  TRP   B CA  
1228 C C   . TRP   B 80  ? 0.7725 0.6845 0.3229 0.2257  -0.0901 -0.0398 89  TRP   B C   
1229 O O   . TRP   B 80  ? 0.7246 0.6277 0.2832 0.2112  -0.0939 -0.0349 89  TRP   B O   
1230 C CB  . TRP   B 80  ? 0.7425 0.6726 0.2798 0.2278  -0.0654 -0.0236 89  TRP   B CB  
1231 C CG  . TRP   B 80  ? 0.7589 0.6954 0.2886 0.2480  -0.0683 -0.0281 89  TRP   B CG  
1232 C CD1 . TRP   B 80  ? 0.7703 0.7129 0.2932 0.2652  -0.0720 -0.0370 89  TRP   B CD1 
1233 C CD2 . TRP   B 80  ? 0.7637 0.7028 0.2916 0.2535  -0.0675 -0.0242 89  TRP   B CD2 
1234 N NE1 . TRP   B 80  ? 0.7826 0.7324 0.2989 0.2810  -0.0730 -0.0390 89  TRP   B NE1 
1235 C CE2 . TRP   B 80  ? 0.7825 0.7297 0.3026 0.2742  -0.0706 -0.0316 89  TRP   B CE2 
1236 C CE3 . TRP   B 80  ? 0.7500 0.6858 0.2827 0.2428  -0.0653 -0.0158 89  TRP   B CE3 
1237 C CZ2 . TRP   B 80  ? 0.7801 0.7330 0.2973 0.2849  -0.0704 -0.0308 89  TRP   B CZ2 
1238 C CZ3 . TRP   B 80  ? 0.7612 0.7017 0.2917 0.2533  -0.0658 -0.0147 89  TRP   B CZ3 
1239 C CH2 . TRP   B 80  ? 0.7733 0.7223 0.2966 0.2739  -0.0679 -0.0222 89  TRP   B CH2 
1240 N N   . ASP   B 81  ? 0.7849 0.6979 0.3326 0.2426  -0.0989 -0.0513 90  ASP   B N   
1241 C CA  . ASP   B 81  ? 0.8295 0.7323 0.3857 0.2469  -0.1147 -0.0612 90  ASP   B CA  
1242 C C   . ASP   B 81  ? 0.8404 0.7420 0.3959 0.2522  -0.1166 -0.0583 90  ASP   B C   
1243 O O   . ASP   B 81  ? 0.8795 0.7704 0.4452 0.2517  -0.1293 -0.0637 90  ASP   B O   
1244 C CB  . ASP   B 81  ? 0.8309 0.7361 0.3853 0.2634  -0.1242 -0.0765 90  ASP   B CB  
1245 C CG  . ASP   B 81  ? 0.8572 0.7765 0.3971 0.2848  -0.1203 -0.0809 90  ASP   B CG  
1246 O OD1 . ASP   B 81  ? 0.8722 0.7992 0.4043 0.2880  -0.1104 -0.0721 90  ASP   B OD1 
1247 O OD2 . ASP   B 81  ? 0.8806 0.8045 0.4171 0.2982  -0.1269 -0.0930 90  ASP   B OD2 
1248 N N   . GLY   B 82  ? 0.8497 0.7618 0.3956 0.2567  -0.1048 -0.0501 91  GLY   B N   
1249 C CA  . GLY   B 82  ? 0.8503 0.7647 0.3949 0.2636  -0.1048 -0.0472 91  GLY   B CA  
1250 C C   . GLY   B 82  ? 0.8788 0.8019 0.4162 0.2869  -0.1090 -0.0582 91  GLY   B C   
1251 O O   . GLY   B 82  ? 0.8880 0.8140 0.4253 0.2949  -0.1100 -0.0580 91  GLY   B O   
1252 N N   . LEU   B 83  ? 0.8660 0.7946 0.3975 0.2981  -0.1113 -0.0680 92  LEU   B N   
1253 C CA  . LEU   B 83  ? 0.8928 0.8309 0.4169 0.3211  -0.1173 -0.0812 92  LEU   B CA  
1254 C C   . LEU   B 83  ? 0.8952 0.8503 0.4042 0.3332  -0.1074 -0.0803 92  LEU   B C   
1255 O O   . LEU   B 83  ? 0.9077 0.8777 0.4058 0.3514  -0.1040 -0.0829 92  LEU   B O   
1256 C CB  . LEU   B 83  ? 0.9195 0.8468 0.4531 0.3242  -0.1343 -0.0972 92  LEU   B CB  
1257 C CG  . LEU   B 83  ? 0.9576 0.8724 0.5046 0.3249  -0.1482 -0.1045 92  LEU   B CG  
1258 C CD1 . LEU   B 83  ? 0.9732 0.8834 0.5266 0.3361  -0.1642 -0.1238 92  LEU   B CD1 
1259 C CD2 . LEU   B 83  ? 0.9578 0.8808 0.5003 0.3367  -0.1451 -0.1034 92  LEU   B CD2 
1260 N N   . SER   B 84  ? 0.8704 0.8244 0.3789 0.3262  -0.1049 -0.0789 93  SER   B N   
1261 C CA  . SER   B 84  ? 0.8786 0.8467 0.3749 0.3397  -0.1009 -0.0820 93  SER   B CA  
1262 C C   . SER   B 84  ? 0.8576 0.8372 0.3459 0.3376  -0.0835 -0.0658 93  SER   B C   
1263 O O   . SER   B 84  ? 0.8552 0.8286 0.3500 0.3213  -0.0758 -0.0541 93  SER   B O   
1264 C CB  . SER   B 84  ? 0.8828 0.8440 0.3848 0.3340  -0.1081 -0.0893 93  SER   B CB  
1265 O OG  . SER   B 84  ? 0.8796 0.8257 0.3950 0.3284  -0.1229 -0.1000 93  SER   B OG  
1266 N N   . GLU   B 85  ? 0.8415 0.8378 0.3167 0.3535  -0.0775 -0.0648 94  GLU   B N   
1267 C CA  . GLU   B 85  ? 0.8097 0.8161 0.2800 0.3506  -0.0613 -0.0485 94  GLU   B CA  
1268 C C   . GLU   B 85  ? 0.7605 0.7548 0.2413 0.3309  -0.0592 -0.0441 94  GLU   B C   
1269 O O   . GLU   B 85  ? 0.7638 0.7470 0.2515 0.3254  -0.0707 -0.0551 94  GLU   B O   
1270 C CB  . GLU   B 85  ? 0.8255 0.8527 0.2802 0.3718  -0.0562 -0.0474 94  GLU   B CB  
1271 C CG  . GLU   B 85  ? 0.8272 0.8672 0.2748 0.3844  -0.0517 -0.0447 94  GLU   B CG  
1272 C CD  . GLU   B 85  ? 0.8751 0.9390 0.3067 0.4051  -0.0447 -0.0411 94  GLU   B CD  
1273 O OE1 . GLU   B 85  ? 0.8939 0.9650 0.3188 0.4102  -0.0426 -0.0388 94  GLU   B OE1 
1274 O OE2 . GLU   B 85  ? 0.9030 0.9794 0.3289 0.4165  -0.0413 -0.0402 94  GLU   B OE2 
1275 N N   . VAL   B 86  ? 0.7152 0.7158 0.1956 0.3253  -0.0446 -0.0291 95  VAL   B N   
1276 C CA  . VAL   B 86  ? 0.6898 0.6846 0.1782 0.3108  -0.0397 -0.0242 95  VAL   B CA  
1277 C C   . VAL   B 86  ? 0.6825 0.6904 0.1656 0.3180  -0.0277 -0.0130 95  VAL   B C   
1278 O O   . VAL   B 86  ? 0.7099 0.7313 0.1830 0.3329  -0.0232 -0.0083 95  VAL   B O   
1279 C CB  . VAL   B 86  ? 0.6643 0.6476 0.1643 0.2898  -0.0361 -0.0182 95  VAL   B CB  
1280 C CG1 . VAL   B 86  ? 0.6785 0.6503 0.1832 0.2847  -0.0481 -0.0271 95  VAL   B CG1 
1281 C CG2 . VAL   B 86  ? 0.6630 0.6529 0.1625 0.2885  -0.0243 -0.0054 95  VAL   B CG2 
1282 N N   A GLN   B 87  ? 0.6696 0.6746 0.1597 0.3083  -0.0227 -0.0086 96  GLN   B N   
1283 N N   B GLN   B 87  ? 0.6697 0.6747 0.1599 0.3082  -0.0227 -0.0086 96  GLN   B N   
1284 N N   C GLN   B 87  ? 0.6687 0.6739 0.1585 0.3090  -0.0231 -0.0090 96  GLN   B N   
1285 N N   D GLN   B 87  ? 0.6688 0.6740 0.1585 0.3090  -0.0231 -0.0090 96  GLN   B N   
1286 C CA  A GLN   B 87  ? 0.6681 0.6834 0.1573 0.3126  -0.0110 0.0037  96  GLN   B CA  
1287 C CA  B GLN   B 87  ? 0.6681 0.6833 0.1573 0.3125  -0.0110 0.0037  96  GLN   B CA  
1288 C CA  C GLN   B 87  ? 0.6686 0.6840 0.1575 0.3130  -0.0112 0.0034  96  GLN   B CA  
1289 C CA  D GLN   B 87  ? 0.6686 0.6840 0.1575 0.3130  -0.0112 0.0034  96  GLN   B CA  
1290 C C   A GLN   B 87  ? 0.6527 0.6615 0.1554 0.2943  -0.0013 0.0128  96  GLN   B C   
1291 C C   B GLN   B 87  ? 0.6527 0.6615 0.1555 0.2943  -0.0013 0.0127  96  GLN   B C   
1292 C C   C GLN   B 87  ? 0.6472 0.6560 0.1497 0.2948  -0.0017 0.0122  96  GLN   B C   
1293 C C   D GLN   B 87  ? 0.6472 0.6560 0.1497 0.2948  -0.0017 0.0122  96  GLN   B C   
1294 O O   A GLN   B 87  ? 0.6534 0.6517 0.1653 0.2804  -0.0047 0.0069  96  GLN   B O   
1295 O O   B GLN   B 87  ? 0.6532 0.6515 0.1651 0.2803  -0.0047 0.0068  96  GLN   B O   
1296 O O   C GLN   B 87  ? 0.6542 0.6536 0.1657 0.2822  -0.0049 0.0065  96  GLN   B O   
1297 O O   D GLN   B 87  ? 0.6541 0.6535 0.1655 0.2822  -0.0049 0.0065  96  GLN   B O   
1298 C CB  A GLN   B 87  ? 0.6678 0.6884 0.1525 0.3228  -0.0154 -0.0010 96  GLN   B CB  
1299 C CB  B GLN   B 87  ? 0.6679 0.6885 0.1526 0.3228  -0.0154 -0.0010 96  GLN   B CB  
1300 C CB  C GLN   B 87  ? 0.6696 0.6905 0.1544 0.3228  -0.0149 -0.0004 96  GLN   B CB  
1301 C CB  D GLN   B 87  ? 0.6697 0.6906 0.1545 0.3228  -0.0149 -0.0004 96  GLN   B CB  
1302 C CG  A GLN   B 87  ? 0.6820 0.7136 0.1514 0.3436  -0.0231 -0.0084 96  GLN   B CG  
1303 C CG  B GLN   B 87  ? 0.6820 0.7137 0.1514 0.3436  -0.0231 -0.0084 96  GLN   B CG  
1304 C CG  C GLN   B 87  ? 0.6885 0.7219 0.1576 0.3444  -0.0213 -0.0062 96  GLN   B CG  
1305 C CG  D GLN   B 87  ? 0.6884 0.7219 0.1576 0.3444  -0.0213 -0.0062 96  GLN   B CG  
1306 C CD  A GLN   B 87  ? 0.6851 0.7222 0.1488 0.3549  -0.0309 -0.0164 96  GLN   B CD  
1307 C CD  B GLN   B 87  ? 0.6853 0.7225 0.1491 0.3548  -0.0307 -0.0163 96  GLN   B CD  
1308 C CD  C GLN   B 87  ? 0.6905 0.7318 0.1547 0.3554  -0.0248 -0.0087 96  GLN   B CD  
1309 C CD  D GLN   B 87  ? 0.6906 0.7318 0.1547 0.3553  -0.0248 -0.0087 96  GLN   B CD  
1310 O OE1 A GLN   B 87  ? 0.6723 0.7047 0.1435 0.3487  -0.0329 -0.0188 96  GLN   B OE1 
1311 O OE1 B GLN   B 87  ? 0.6727 0.7052 0.1440 0.3487  -0.0327 -0.0186 96  GLN   B OE1 
1312 O OE1 C GLN   B 87  ? 0.6799 0.7182 0.1519 0.3493  -0.0230 -0.0064 96  GLN   B OE1 
1313 O OE1 D GLN   B 87  ? 0.6799 0.7182 0.1519 0.3492  -0.0230 -0.0065 96  GLN   B OE1 
1314 N NE2 A GLN   B 87  ? 0.6982 0.7486 0.1472 0.3744  -0.0358 -0.0214 96  GLN   B NE2 
1315 N NE2 B GLN   B 87  ? 0.6985 0.7490 0.1474 0.3744  -0.0355 -0.0211 96  GLN   B NE2 
1316 N NE2 C GLN   B 87  ? 0.7079 0.7626 0.1571 0.3750  -0.0302 -0.0138 96  GLN   B NE2 
1317 N NE2 D GLN   B 87  ? 0.7080 0.7626 0.1571 0.3750  -0.0302 -0.0138 96  GLN   B NE2 
1318 N N   A LEU   B 88  ? 0.6500 0.6658 0.1545 0.2947  0.0102  0.0261  97  LEU   B N   
1319 N N   B LEU   B 88  ? 0.6501 0.6657 0.1546 0.2947  0.0102  0.0261  97  LEU   B N   
1320 N N   C LEU   B 88  ? 0.6426 0.6575 0.1472 0.2941  0.0096  0.0253  97  LEU   B N   
1321 N N   D LEU   B 88  ? 0.6425 0.6574 0.1472 0.2941  0.0096  0.0253  97  LEU   B N   
1322 C CA  A LEU   B 88  ? 0.6380 0.6503 0.1562 0.2803  0.0205  0.0353  97  LEU   B CA  
1323 C CA  B LEU   B 88  ? 0.6380 0.6503 0.1562 0.2803  0.0205  0.0353  97  LEU   B CA  
1324 C CA  C LEU   B 88  ? 0.6270 0.6386 0.1453 0.2798  0.0197  0.0343  97  LEU   B CA  
1325 C CA  D LEU   B 88  ? 0.6270 0.6385 0.1453 0.2798  0.0197  0.0343  97  LEU   B CA  
1326 C C   A LEU   B 88  ? 0.6398 0.6570 0.1607 0.2856  0.0243  0.0397  97  LEU   B C   
1327 C C   B LEU   B 88  ? 0.6397 0.6569 0.1607 0.2856  0.0243  0.0397  97  LEU   B C   
1328 C C   C LEU   B 88  ? 0.6298 0.6464 0.1501 0.2858  0.0229  0.0380  97  LEU   B C   
1329 C C   D LEU   B 88  ? 0.6298 0.6464 0.1501 0.2858  0.0229  0.0380  97  LEU   B C   
1330 O O   A LEU   B 88  ? 0.6415 0.6709 0.1569 0.2994  0.0301  0.0498  97  LEU   B O   
1331 O O   B LEU   B 88  ? 0.6416 0.6709 0.1570 0.2994  0.0300  0.0498  97  LEU   B O   
1332 O O   C LEU   B 88  ? 0.6267 0.6553 0.1379 0.3023  0.0251  0.0443  97  LEU   B O   
1333 O O   D LEU   B 88  ? 0.6267 0.6553 0.1380 0.3023  0.0251  0.0443  97  LEU   B O   
1334 C CB  A LEU   B 88  ? 0.6371 0.6550 0.1584 0.2791  0.0303  0.0474  97  LEU   B CB  
1335 C CB  B LEU   B 88  ? 0.6371 0.6550 0.1583 0.2791  0.0303  0.0474  97  LEU   B CB  
1336 C CB  C LEU   B 88  ? 0.6235 0.6405 0.1452 0.2782  0.0299  0.0467  97  LEU   B CB  
1337 C CB  D LEU   B 88  ? 0.6234 0.6405 0.1452 0.2782  0.0299  0.0467  97  LEU   B CB  
1338 C CG  A LEU   B 88  ? 0.6270 0.6433 0.1635 0.2666  0.0411  0.0570  97  LEU   B CG  
1339 C CG  B LEU   B 88  ? 0.6269 0.6432 0.1634 0.2666  0.0411  0.0570  97  LEU   B CG  
1340 C CG  C LEU   B 88  ? 0.6123 0.6280 0.1491 0.2664  0.0407  0.0563  97  LEU   B CG  
1341 C CG  D LEU   B 88  ? 0.6122 0.6280 0.1491 0.2664  0.0407  0.0563  97  LEU   B CG  
1342 C CD1 A LEU   B 88  ? 0.6146 0.6189 0.1610 0.2472  0.0388  0.0500  97  LEU   B CD1 
1343 C CD1 B LEU   B 88  ? 0.6147 0.6190 0.1610 0.2471  0.0388  0.0500  97  LEU   B CD1 
1344 C CD1 C LEU   B 88  ? 0.5996 0.6034 0.1466 0.2469  0.0386  0.0493  97  LEU   B CD1 
1345 C CD1 D LEU   B 88  ? 0.5996 0.6034 0.1466 0.2469  0.0386  0.0493  97  LEU   B CD1 
1346 C CD2 A LEU   B 88  ? 0.6280 0.6525 0.1677 0.2690  0.0506  0.0699  97  LEU   B CD2 
1347 C CD2 B LEU   B 88  ? 0.6279 0.6524 0.1676 0.2690  0.0506  0.0699  97  LEU   B CD2 
1348 C CD2 C LEU   B 88  ? 0.6125 0.6361 0.1529 0.2682  0.0504  0.0693  97  LEU   B CD2 
1349 C CD2 D LEU   B 88  ? 0.6124 0.6361 0.1529 0.2682  0.0504  0.0693  97  LEU   B CD2 
1350 N N   A LEU   B 89  ? 0.6289 0.6385 0.1572 0.2769  0.0204  0.0321  98  LEU   B N   
1351 N N   B LEU   B 89  ? 0.6290 0.6385 0.1573 0.2769  0.0204  0.0321  98  LEU   B N   
1352 N N   C LEU   B 89  ? 0.6197 0.6287 0.1505 0.2745  0.0222  0.0336  98  LEU   B N   
1353 N N   D LEU   B 89  ? 0.6197 0.6287 0.1505 0.2745  0.0222  0.0336  98  LEU   B N   
1354 C CA  A LEU   B 89  ? 0.6270 0.6388 0.1631 0.2777  0.0249  0.0364  98  LEU   B CA  
1355 C CA  B LEU   B 89  ? 0.6271 0.6390 0.1633 0.2777  0.0249  0.0364  98  LEU   B CA  
1356 C CA  C LEU   B 89  ? 0.6167 0.6294 0.1539 0.2777  0.0268  0.0388  98  LEU   B CA  
1357 C CA  D LEU   B 89  ? 0.6167 0.6295 0.1539 0.2777  0.0268  0.0388  98  LEU   B CA  
1358 C C   A LEU   B 89  ? 0.6212 0.6326 0.1712 0.2677  0.0369  0.0478  98  LEU   B C   
1359 C C   B LEU   B 89  ? 0.6212 0.6326 0.1712 0.2676  0.0369  0.0478  98  LEU   B C   
1360 C C   C LEU   B 89  ? 0.6121 0.6249 0.1633 0.2686  0.0390  0.0507  98  LEU   B C   
1361 C C   D LEU   B 89  ? 0.6121 0.6249 0.1633 0.2686  0.0390  0.0507  98  LEU   B C   
1362 O O   A LEU   B 89  ? 0.6098 0.6134 0.1723 0.2522  0.0388  0.0440  98  LEU   B O   
1363 O O   B LEU   B 89  ? 0.6098 0.6134 0.1724 0.2521  0.0388  0.0440  98  LEU   B O   
1364 O O   C LEU   B 89  ? 0.6060 0.6117 0.1717 0.2543  0.0417  0.0478  98  LEU   B O   
1365 O O   D LEU   B 89  ? 0.6060 0.6116 0.1717 0.2543  0.0417  0.0478  98  LEU   B O   
1366 C CB  A LEU   B 89  ? 0.6267 0.6307 0.1686 0.2698  0.0173  0.0240  98  LEU   B CB  
1367 C CB  B LEU   B 89  ? 0.6267 0.6307 0.1686 0.2697  0.0173  0.0240  98  LEU   B CB  
1368 C CB  C LEU   B 89  ? 0.6195 0.6252 0.1624 0.2710  0.0196  0.0270  98  LEU   B CB  
1369 C CB  D LEU   B 89  ? 0.6195 0.6252 0.1624 0.2710  0.0196  0.0270  98  LEU   B CB  
1370 C CG  A LEU   B 89  ? 0.6266 0.6306 0.1808 0.2665  0.0214  0.0259  98  LEU   B CG  
1371 C CG  B LEU   B 89  ? 0.6265 0.6305 0.1808 0.2665  0.0214  0.0259  98  LEU   B CG  
1372 C CG  C LEU   B 89  ? 0.6239 0.6327 0.1748 0.2743  0.0226  0.0304  98  LEU   B CG  
1373 C CG  D LEU   B 89  ? 0.6239 0.6327 0.1748 0.2743  0.0226  0.0304  98  LEU   B CG  
1374 C CD1 A LEU   B 89  ? 0.6285 0.6413 0.1847 0.2765  0.0301  0.0404  98  LEU   B CD1 
1375 C CD1 B LEU   B 89  ? 0.6286 0.6414 0.1848 0.2765  0.0301  0.0404  98  LEU   B CD1 
1376 C CD1 C LEU   B 89  ? 0.6405 0.6614 0.1830 0.2925  0.0259  0.0416  98  LEU   B CD1 
1377 C CD1 D LEU   B 89  ? 0.6404 0.6613 0.1830 0.2924  0.0259  0.0415  98  LEU   B CD1 
1378 C CD2 A LEU   B 89  ? 0.6340 0.6372 0.1865 0.2708  0.0113  0.0145  98  LEU   B CD2 
1379 C CD2 B LEU   B 89  ? 0.6339 0.6370 0.1863 0.2708  0.0113  0.0145  98  LEU   B CD2 
1380 C CD2 C LEU   B 89  ? 0.6307 0.6355 0.1831 0.2729  0.0129  0.0170  98  LEU   B CD2 
1381 C CD2 D LEU   B 89  ? 0.6307 0.6355 0.1830 0.2729  0.0129  0.0170  98  LEU   B CD2 
1382 N N   A ALA   B 90  ? 0.6259 0.6463 0.1739 0.2763  0.0447  0.0611  99  ALA   B N   
1383 N N   B ALA   B 90  ? 0.6260 0.6463 0.1740 0.2763  0.0447  0.0611  99  ALA   B N   
1384 N N   C ALA   B 90  ? 0.6163 0.6376 0.1646 0.2764  0.0462  0.0632  99  ALA   B N   
1385 N N   D ALA   B 90  ? 0.6163 0.6376 0.1646 0.2764  0.0462  0.0632  99  ALA   B N   
1386 C CA  A ALA   B 90  ? 0.6220 0.6431 0.1846 0.2684  0.0561  0.0732  99  ALA   B CA  
1387 C CA  B ALA   B 90  ? 0.6221 0.6431 0.1846 0.2683  0.0561  0.0732  99  ALA   B CA  
1388 C CA  C ALA   B 90  ? 0.6114 0.6340 0.1744 0.2693  0.0578  0.0758  99  ALA   B CA  
1389 C CA  D ALA   B 90  ? 0.6115 0.6340 0.1744 0.2693  0.0578  0.0758  99  ALA   B CA  
1390 C C   A ALA   B 90  ? 0.6262 0.6476 0.2020 0.2682  0.0611  0.0792  99  ALA   B C   
1391 C C   B ALA   B 90  ? 0.6262 0.6476 0.2019 0.2682  0.0611  0.0792  99  ALA   B C   
1392 C C   C ALA   B 90  ? 0.6206 0.6430 0.1966 0.2688  0.0622  0.0811  99  ALA   B C   
1393 C C   D ALA   B 90  ? 0.6206 0.6430 0.1966 0.2688  0.0622  0.0811  99  ALA   B C   
1394 O O   A ALA   B 90  ? 0.6354 0.6634 0.2045 0.2818  0.0589  0.0823  99  ALA   B O   
1395 O O   B ALA   B 90  ? 0.6354 0.6635 0.2046 0.2818  0.0589  0.0823  99  ALA   B O   
1396 O O   C ALA   B 90  ? 0.6261 0.6557 0.1955 0.2829  0.0607  0.0855  99  ALA   B O   
1397 O O   D ALA   B 90  ? 0.6261 0.6558 0.1956 0.2829  0.0607  0.0855  99  ALA   B O   
1398 C CB  A ALA   B 90  ? 0.6301 0.6614 0.1869 0.2779  0.0621  0.0853  99  ALA   B CB  
1399 C CB  B ALA   B 90  ? 0.6300 0.6613 0.1868 0.2779  0.0621  0.0853  99  ALA   B CB  
1400 C CB  C ALA   B 90  ? 0.6224 0.6559 0.1794 0.2796  0.0638  0.0883  99  ALA   B CB  
1401 C CB  D ALA   B 90  ? 0.6224 0.6558 0.1794 0.2796  0.0638  0.0883  99  ALA   B CB  
1402 N N   . VAL   B 91  ? 0.6192 0.6344 0.2134 0.2536  0.0672  0.0804  100 VAL   B N   
1403 C CA  . VAL   B 91  ? 0.6210 0.6355 0.2329 0.2517  0.0731  0.0867  100 VAL   B CA  
1404 C C   . VAL   B 91  ? 0.6331 0.6486 0.2602 0.2454  0.0832  0.0984  100 VAL   B C   
1405 O O   . VAL   B 91  ? 0.6093 0.6183 0.2500 0.2304  0.0858  0.0933  100 VAL   B O   
1406 C CB  . VAL   B 91  ? 0.6102 0.6159 0.2324 0.2389  0.0696  0.0731  100 VAL   B CB  
1407 C CG1 . VAL   B 91  ? 0.6163 0.6212 0.2577 0.2384  0.0747  0.0782  100 VAL   B CG1 
1408 C CG2 . VAL   B 91  ? 0.6124 0.6164 0.2205 0.2428  0.0589  0.0604  100 VAL   B CG2 
1409 N N   . PRO   B 92  ? 0.6348 0.6595 0.2608 0.2562  0.0892  0.1144  101 PRO   B N   
1410 C CA  . PRO   B 92  ? 0.6304 0.6567 0.2729 0.2504  0.0988  0.1264  101 PRO   B CA  
1411 C C   . PRO   B 92  ? 0.6311 0.6536 0.2982 0.2454  0.1044  0.1324  101 PRO   B C   
1412 O O   . PRO   B 92  ? 0.6409 0.6627 0.3099 0.2512  0.1020  0.1322  101 PRO   B O   
1413 C CB  . PRO   B 92  ? 0.6444 0.6841 0.2760 0.2659  0.1029  0.1421  101 PRO   B CB  
1414 C CG  . PRO   B 92  ? 0.6492 0.6932 0.2556 0.2780  0.0941  0.1339  101 PRO   B CG  
1415 C CD  . PRO   B 92  ? 0.6499 0.6856 0.2580 0.2748  0.0872  0.1218  101 PRO   B CD  
1416 N N   . PRO   B 93  ? 0.6386 0.6587 0.3262 0.2352  0.1116  0.1380  102 PRO   B N   
1417 C CA  . PRO   B 93  ? 0.6519 0.6670 0.3663 0.2292  0.1163  0.1418  102 PRO   B CA  
1418 C C   . PRO   B 93  ? 0.6598 0.6812 0.3798 0.2426  0.1202  0.1597  102 PRO   B C   
1419 O O   . PRO   B 93  ? 0.6921 0.7229 0.4067 0.2513  0.1248  0.1750  102 PRO   B O   
1420 C CB  . PRO   B 93  ? 0.6495 0.6625 0.3824 0.2168  0.1224  0.1440  102 PRO   B CB  
1421 C CG  . PRO   B 93  ? 0.6462 0.6592 0.3611 0.2110  0.1180  0.1329  102 PRO   B CG  
1422 C CD  . PRO   B 93  ? 0.6538 0.6739 0.3419 0.2261  0.1136  0.1360  102 PRO   B CD  
1423 N N   . GLY   B 94  ? 0.6619 0.6790 0.3913 0.2445  0.1179  0.1574  103 GLY   B N   
1424 C CA  . GLY   B 94  ? 0.6781 0.7005 0.4143 0.2570  0.1205  0.1743  103 GLY   B CA  
1425 C C   . GLY   B 94  ? 0.6943 0.7282 0.4030 0.2745  0.1168  0.1814  103 GLY   B C   
1426 O O   . GLY   B 94  ? 0.6950 0.7360 0.4079 0.2854  0.1201  0.1988  103 GLY   B O   
1427 N N   . GLU   B 95  ? 0.6990 0.7350 0.3821 0.2775  0.1099  0.1685  104 GLU   B N   
1428 C CA  . GLU   B 95  ? 0.7191 0.7670 0.3747 0.2944  0.1056  0.1721  104 GLU   B CA  
1429 C C   . GLU   B 95  ? 0.7157 0.7593 0.3560 0.2956  0.0946  0.1528  104 GLU   B C   
1430 O O   . GLU   B 95  ? 0.6653 0.6981 0.3112 0.2821  0.0911  0.1366  104 GLU   B O   
1431 C CB  . GLU   B 95  ? 0.7469 0.8039 0.3877 0.2983  0.1087  0.1773  104 GLU   B CB  
1432 C CG  . GLU   B 95  ? 0.7650 0.8256 0.4237 0.2942  0.1198  0.1947  104 GLU   B CG  
1433 C CD  . GLU   B 95  ? 0.7749 0.8455 0.4219 0.2975  0.1236  0.2000  104 GLU   B CD  
1434 O OE1 . GLU   B 95  ? 0.7915 0.8606 0.4214 0.2964  0.1176  0.1856  104 GLU   B OE1 
1435 O OE2 . GLU   B 95  ? 0.8009 0.8810 0.4575 0.3011  0.1329  0.2194  104 GLU   B OE2 
1436 N N   . ARG   B 96  ? 0.7243 0.7766 0.3472 0.3108  0.0889  0.1541  105 ARG   B N   
1437 C CA  . ARG   B 96  ? 0.7520 0.8004 0.3631 0.3123  0.0778  0.1360  105 ARG   B CA  
1438 C C   . ARG   B 96  ? 0.7382 0.7833 0.3341 0.3072  0.0724  0.1207  105 ARG   B C   
1439 O O   . ARG   B 96  ? 0.7249 0.7757 0.3112 0.3099  0.0757  0.1260  105 ARG   B O   
1440 C CB  . ARG   B 96  ? 0.8210 0.8816 0.4159 0.3312  0.0727  0.1417  105 ARG   B CB  
1441 C CG  . ARG   B 96  ? 0.8580 0.9151 0.4466 0.3333  0.0614  0.1249  105 ARG   B CG  
1442 C CD  . ARG   B 96  ? 0.9201 0.9873 0.5042 0.3490  0.0583  0.1339  105 ARG   B CD  
1443 N NE  . ARG   B 96  ? 0.9661 1.0497 0.5339 0.3650  0.0617  0.1501  105 ARG   B NE  
1444 C CZ  . ARG   B 96  ? 1.0249 1.1163 0.6009 0.3706  0.0705  0.1723  105 ARG   B CZ  
1445 N NH1 . ARG   B 96  ? 1.0371 1.1202 0.6394 0.3619  0.0764  0.1815  105 ARG   B NH1 
1446 N NH2 . ARG   B 96  ? 1.0843 1.1930 0.6425 0.3856  0.0732  0.1856  105 ARG   B NH2 
1447 N N   . ALA   B 97  ? 0.7151 0.7519 0.3097 0.3004  0.0640  0.1029  106 ALA   B N   
1448 C CA  . ALA   B 97  ? 0.7155 0.7493 0.2949 0.2977  0.0564  0.0882  106 ALA   B CA  
1449 C C   . ALA   B 97  ? 0.7210 0.7669 0.2777 0.3154  0.0523  0.0911  106 ALA   B C   
1450 O O   . ALA   B 97  ? 0.7041 0.7584 0.2530 0.3294  0.0487  0.0941  106 ALA   B O   
1451 C CB  . ALA   B 97  ? 0.7192 0.7452 0.3008 0.2912  0.0476  0.0713  106 ALA   B CB  
1452 N N   . LYS   B 98  ? 0.7108 0.7583 0.2571 0.3155  0.0524  0.0894  107 LYS   B N   
1453 C CA  . LYS   B 98  ? 0.7624 0.8231 0.2874 0.3329  0.0492  0.0912  107 LYS   B CA  
1454 C C   . LYS   B 98  ? 0.7448 0.7998 0.2603 0.3291  0.0415  0.0763  107 LYS   B C   
1455 O O   . LYS   B 98  ? 0.7173 0.7630 0.2420 0.3144  0.0444  0.0744  107 LYS   B O   
1456 C CB  . LYS   B 98  ? 0.8075 0.8796 0.3333 0.3390  0.0606  0.1104  107 LYS   B CB  
1457 C CG  . LYS   B 98  ? 0.8656 0.9547 0.3703 0.3575  0.0598  0.1144  107 LYS   B CG  
1458 C CD  . LYS   B 98  ? 0.9149 1.0142 0.4220 0.3595  0.0713  0.1310  107 LYS   B CD  
1459 C CE  . LYS   B 98  ? 0.9184 1.0053 0.4437 0.3409  0.0770  0.1318  107 LYS   B CE  
1460 N NZ  . LYS   B 98  ? 0.9595 1.0561 0.4848 0.3430  0.0854  0.1428  107 LYS   B NZ  
1461 N N   . ASN   B 99  ? 0.7268 0.7854 0.2268 0.3401  0.0307  0.0644  108 ASN   B N   
1462 C CA  . ASN   B 99  ? 0.7218 0.7746 0.2140 0.3381  0.0219  0.0500  108 ASN   B CA  
1463 C C   . ASN   B 99  ? 0.7269 0.7908 0.2073 0.3488  0.0251  0.0553  108 ASN   B C   
1464 O O   . ASN   B 99  ? 0.7154 0.7944 0.1854 0.3642  0.0281  0.0632  108 ASN   B O   
1465 C CB  . ASN   B 99  ? 0.7361 0.7874 0.2197 0.3451  0.0081  0.0336  108 ASN   B CB  
1466 C CG  . ASN   B 99  ? 0.7628 0.8043 0.2578 0.3352  0.0036  0.0262  108 ASN   B CG  
1467 O OD1 . ASN   B 99  ? 0.7973 0.8402 0.3014 0.3333  0.0096  0.0348  108 ASN   B OD1 
1468 N ND2 . ASN   B 99  ? 0.7611 0.7920 0.2583 0.3274  -0.0066 0.0108  108 ASN   B ND2 
1469 N N   . ILE   B 100 ? 0.7155 0.7728 0.1978 0.3408  0.0241  0.0508  109 ILE   B N   
1470 C CA  . ILE   B 100 ? 0.7180 0.7850 0.1923 0.3489  0.0278  0.0555  109 ILE   B CA  
1471 C C   . ILE   B 100 ? 0.7253 0.7845 0.1949 0.3478  0.0165  0.0396  109 ILE   B C   
1472 O O   . ILE   B 100 ? 0.7212 0.7647 0.2019 0.3304  0.0136  0.0342  109 ILE   B O   
1473 C CB  . ILE   B 100 ? 0.7259 0.7934 0.2121 0.3391  0.0404  0.0703  109 ILE   B CB  
1474 C CG1 . ILE   B 100 ? 0.7412 0.8121 0.2380 0.3366  0.0506  0.0852  109 ILE   B CG1 
1475 C CG2 . ILE   B 100 ? 0.7358 0.8163 0.2138 0.3496  0.0444  0.0756  109 ILE   B CG2 
1476 C CD1 . ILE   B 100 ? 0.7524 0.8424 0.2397 0.3543  0.0569  0.0987  109 ILE   B CD1 
1477 N N   . GLN   B 101 ? 0.7586 0.8279 0.2137 0.3646  0.0102  0.0323  110 GLN   B N   
1478 C CA  . GLN   B 101 ? 0.7771 0.8385 0.2288 0.3657  -0.0029 0.0151  110 GLN   B CA  
1479 C C   . GLN   B 101 ? 0.7809 0.8456 0.2319 0.3671  -0.0001 0.0173  110 GLN   B C   
1480 O O   . GLN   B 101 ? 0.7837 0.8644 0.2287 0.3773  0.0093  0.0283  110 GLN   B O   
1481 C CB  . GLN   B 101 ? 0.7991 0.8684 0.2378 0.3828  -0.0135 0.0024  110 GLN   B CB  
1482 C CG  . GLN   B 101 ? 0.8081 0.8680 0.2465 0.3837  -0.0279 -0.0158 110 GLN   B CG  
1483 C CD  . GLN   B 101 ? 0.7998 0.8673 0.2274 0.3997  -0.0390 -0.0294 110 GLN   B CD  
1484 O OE1 . GLN   B 101 ? 0.8223 0.8903 0.2501 0.3998  -0.0404 -0.0294 110 GLN   B OE1 
1485 N NE2 . GLN   B 101 ? 0.8081 0.8818 0.2272 0.4136  -0.0473 -0.0417 110 GLN   B NE2 
1486 N N   . THR   B 102 ? 0.7644 0.8146 0.2230 0.3557  -0.0070 0.0092  111 THR   B N   
1487 C CA  . THR   B 102 ? 0.7713 0.8214 0.2333 0.3530  -0.0045 0.0121  111 THR   B CA  
1488 C C   . THR   B 102 ? 0.7399 0.7740 0.2074 0.3455  -0.0179 -0.0016 111 THR   B C   
1489 O O   . THR   B 102 ? 0.8012 0.8236 0.2723 0.3387  -0.0266 -0.0106 111 THR   B O   
1490 C CB  . THR   B 102 ? 0.7507 0.7998 0.2235 0.3391  0.0084  0.0279  111 THR   B CB  
1491 O OG1 . THR   B 102 ? 0.7796 0.8349 0.2541 0.3408  0.0132  0.0335  111 THR   B OG1 
1492 C CG2 . THR   B 102 ? 0.7325 0.7639 0.2183 0.3175  0.0066  0.0269  111 THR   B CG2 
1493 N N   . LEU   B 103 ? 0.7362 0.7747 0.2007 0.3544  -0.0214 -0.0060 112 LEU   B N   
1494 C CA  . LEU   B 103 ? 0.7533 0.7771 0.2252 0.3477  -0.0335 -0.0166 112 LEU   B CA  
1495 C C   . LEU   B 103 ? 0.7222 0.7382 0.2051 0.3301  -0.0274 -0.0060 112 LEU   B C   
1496 O O   . LEU   B 103 ? 0.7279 0.7534 0.2111 0.3327  -0.0186 0.0032  112 LEU   B O   
1497 C CB  . LEU   B 103 ? 0.7546 0.7856 0.2208 0.3648  -0.0411 -0.0273 112 LEU   B CB  
1498 C CG  . LEU   B 103 ? 0.7560 0.7703 0.2327 0.3570  -0.0538 -0.0366 112 LEU   B CG  
1499 C CD1 . LEU   B 103 ? 0.7712 0.7736 0.2503 0.3562  -0.0678 -0.0508 112 LEU   B CD1 
1500 C CD2 . LEU   B 103 ? 0.7805 0.8015 0.2562 0.3702  -0.0578 -0.0426 112 LEU   B CD2 
1501 N N   . PRO   B 104 ? 0.7155 0.7155 0.2081 0.3112  -0.0309 -0.0060 113 PRO   B N   
1502 C CA  . PRO   B 104 ? 0.7106 0.7054 0.2123 0.2952  -0.0252 0.0036  113 PRO   B CA  
1503 C C   . PRO   B 104 ? 0.7278 0.7214 0.2324 0.2977  -0.0300 0.0023  113 PRO   B C   
1504 O O   . PRO   B 104 ? 0.7407 0.7296 0.2447 0.3056  -0.0420 -0.0089 113 PRO   B O   
1505 C CB  . PRO   B 104 ? 0.6987 0.6781 0.2083 0.2768  -0.0305 0.0009  113 PRO   B CB  
1506 C CG  . PRO   B 104 ? 0.6809 0.6591 0.1862 0.2833  -0.0364 -0.0084 113 PRO   B CG  
1507 C CD  . PRO   B 104 ? 0.6982 0.6866 0.1935 0.3055  -0.0410 -0.0159 113 PRO   B CD  
1508 N N   . GLY   B 105 ? 0.7202 0.7178 0.2301 0.2902  -0.0210 0.0136  114 GLY   B N   
1509 C CA  . GLY   B 105 ? 0.7175 0.7114 0.2338 0.2865  -0.0254 0.0144  114 GLY   B CA  
1510 C C   . GLY   B 105 ? 0.7204 0.6985 0.2451 0.2666  -0.0314 0.0149  114 GLY   B C   
1511 O O   . GLY   B 105 ? 0.7045 0.6740 0.2292 0.2594  -0.0355 0.0105  114 GLY   B O   
1512 N N   . ILE   B 106 ? 0.7337 0.7096 0.2650 0.2595  -0.0325 0.0198  115 ILE   B N   
1513 C CA  . ILE   B 106 ? 0.7534 0.7161 0.2923 0.2417  -0.0396 0.0214  115 ILE   B CA  
1514 C C   . ILE   B 106 ? 0.7414 0.7084 0.2855 0.2294  -0.0309 0.0325  115 ILE   B C   
1515 O O   . ILE   B 106 ? 0.7487 0.7248 0.2945 0.2360  -0.0263 0.0370  115 ILE   B O   
1516 C CB  . ILE   B 106 ? 0.7823 0.7368 0.3252 0.2468  -0.0534 0.0148  115 ILE   B CB  
1517 C CG1 . ILE   B 106 ? 0.8167 0.7675 0.3562 0.2603  -0.0630 0.0020  115 ILE   B CG1 
1518 C CG2 . ILE   B 106 ? 0.7919 0.7339 0.3426 0.2288  -0.0606 0.0186  115 ILE   B CG2 
1519 C CD1 . ILE   B 106 ? 0.8217 0.7625 0.3616 0.2515  -0.0678 -0.0025 115 ILE   B CD1 
1520 N N   . PHE   B 107 ? 0.7221 0.6831 0.2696 0.2115  -0.0296 0.0360  116 PHE   B N   
1521 C CA  . PHE   B 107 ? 0.7238 0.6855 0.2774 0.1968  -0.0268 0.0440  116 PHE   B CA  
1522 C C   . PHE   B 107 ? 0.7358 0.6865 0.2928 0.1896  -0.0398 0.0428  116 PHE   B C   
1523 O O   . PHE   B 107 ? 0.7480 0.6889 0.3044 0.1843  -0.0472 0.0381  116 PHE   B O   
1524 C CB  . PHE   B 107 ? 0.7011 0.6633 0.2558 0.1821  -0.0190 0.0469  116 PHE   B CB  
1525 C CG  . PHE   B 107 ? 0.6979 0.6706 0.2540 0.1845  -0.0055 0.0516  116 PHE   B CG  
1526 C CD1 . PHE   B 107 ? 0.6910 0.6731 0.2455 0.2001  0.0001  0.0537  116 PHE   B CD1 
1527 C CD2 . PHE   B 107 ? 0.6733 0.6470 0.2332 0.1708  0.0014  0.0537  116 PHE   B CD2 
1528 C CE1 . PHE   B 107 ? 0.6861 0.6775 0.2438 0.2015  0.0123  0.0596  116 PHE   B CE1 
1529 C CE2 . PHE   B 107 ? 0.6755 0.6577 0.2396 0.1725  0.0131  0.0582  116 PHE   B CE2 
1530 C CZ  . PHE   B 107 ? 0.6910 0.6815 0.2539 0.1882  0.0184  0.0616  116 PHE   B CZ  
1531 N N   . LYS   B 108 ? 0.7496 0.7023 0.3111 0.1910  -0.0428 0.0468  117 LYS   B N   
1532 C CA  . LYS   B 108 ? 0.7808 0.7243 0.3474 0.1839  -0.0548 0.0485  117 LYS   B CA  
1533 C C   . LYS   B 108 ? 0.7510 0.6968 0.3201 0.1654  -0.0510 0.0569  117 LYS   B C   
1534 O O   . LYS   B 108 ? 0.7211 0.6773 0.2921 0.1647  -0.0420 0.0619  117 LYS   B O   
1535 C CB  . LYS   B 108 ? 0.8315 0.7773 0.4024 0.1971  -0.0601 0.0477  117 LYS   B CB  
1536 C CG  . LYS   B 108 ? 0.9273 0.8652 0.4990 0.2105  -0.0716 0.0380  117 LYS   B CG  
1537 C CD  . LYS   B 108 ? 1.0003 0.9471 0.5720 0.2309  -0.0707 0.0330  117 LYS   B CD  
1538 C CE  . LYS   B 108 ? 1.0743 1.0169 0.6435 0.2461  -0.0785 0.0205  117 LYS   B CE  
1539 N NZ  . LYS   B 108 ? 1.1339 1.0877 0.7021 0.2665  -0.0772 0.0147  117 LYS   B NZ  
1540 N N   . THR   B 109 ? 0.7604 0.6980 0.3295 0.1511  -0.0570 0.0581  118 THR   B N   
1541 C CA  . THR   B 109 ? 0.7665 0.7070 0.3364 0.1328  -0.0548 0.0652  118 THR   B CA  
1542 C C   . THR   B 109 ? 0.7826 0.7144 0.3556 0.1236  -0.0674 0.0696  118 THR   B C   
1543 O O   . THR   B 109 ? 0.7775 0.6986 0.3520 0.1265  -0.0767 0.0662  118 THR   B O   
1544 C CB  . THR   B 109 ? 0.7492 0.6921 0.3154 0.1214  -0.0470 0.0637  118 THR   B CB  
1545 O OG1 . THR   B 109 ? 0.7410 0.6751 0.3063 0.1134  -0.0543 0.0620  118 THR   B OG1 
1546 C CG2 . THR   B 109 ? 0.7493 0.6973 0.3133 0.1312  -0.0368 0.0588  118 THR   B CG2 
1547 N N   . LYS   B 110 ? 0.8032 0.7398 0.3773 0.1114  -0.0675 0.0772  119 LYS   B N   
1548 C CA  . LYS   B 110 ? 0.8147 0.7452 0.3910 0.1002  -0.0787 0.0842  119 LYS   B CA  
1549 C C   . LYS   B 110 ? 0.8373 0.7594 0.4122 0.0920  -0.0832 0.0829  119 LYS   B C   
1550 O O   . LYS   B 110 ? 0.8757 0.7894 0.4548 0.0870  -0.0947 0.0881  119 LYS   B O   
1551 C CB  . LYS   B 110 ? 0.8171 0.7577 0.3920 0.0863  -0.0753 0.0918  119 LYS   B CB  
1552 C CG  . LYS   B 110 ? 0.8091 0.7590 0.3786 0.0751  -0.0640 0.0898  119 LYS   B CG  
1553 C CD  . LYS   B 110 ? 0.8445 0.8047 0.4125 0.0606  -0.0630 0.0962  119 LYS   B CD  
1554 C CE  . LYS   B 110 ? 0.8621 0.8227 0.4248 0.0446  -0.0658 0.0996  119 LYS   B CE  
1555 N NZ  . LYS   B 110 ? 0.8688 0.8337 0.4276 0.0394  -0.0557 0.0926  119 LYS   B NZ  
1556 N N   . ASP   B 111 ? 0.8241 0.7488 0.3946 0.0898  -0.0749 0.0771  120 ASP   B N   
1557 C CA  . ASP   B 111 ? 0.8415 0.7606 0.4113 0.0810  -0.0775 0.0756  120 ASP   B CA  
1558 C C   . ASP   B 111 ? 0.8456 0.7565 0.4174 0.0940  -0.0803 0.0664  120 ASP   B C   
1559 O O   . ASP   B 111 ? 0.8729 0.7799 0.4453 0.0882  -0.0815 0.0636  120 ASP   B O   
1560 C CB  . ASP   B 111 ? 0.8441 0.7731 0.4086 0.0682  -0.0666 0.0750  120 ASP   B CB  
1561 C CG  . ASP   B 111 ? 0.8653 0.8034 0.4273 0.0539  -0.0653 0.0830  120 ASP   B CG  
1562 O OD1 . ASP   B 111 ? 0.8981 0.8326 0.4620 0.0482  -0.0749 0.0910  120 ASP   B OD1 
1563 O OD2 . ASP   B 111 ? 0.8875 0.8365 0.4466 0.0491  -0.0552 0.0811  120 ASP   B OD2 
1564 N N   . GLY   B 112 ? 0.8319 0.7415 0.4047 0.1111  -0.0811 0.0614  121 GLY   B N   
1565 C CA  . GLY   B 112 ? 0.8498 0.7529 0.4237 0.1247  -0.0848 0.0517  121 GLY   B CA  
1566 C C   . GLY   B 112 ? 0.8305 0.7414 0.3995 0.1398  -0.0757 0.0458  121 GLY   B C   
1567 O O   . GLY   B 112 ? 0.8210 0.7420 0.3870 0.1381  -0.0653 0.0495  121 GLY   B O   
1568 N N   . ASP   B 113 ? 0.8442 0.7507 0.4133 0.1542  -0.0802 0.0368  122 ASP   B N   
1569 C CA  . ASP   B 113 ? 0.8277 0.7418 0.3915 0.1712  -0.0734 0.0305  122 ASP   B CA  
1570 C C   . ASP   B 113 ? 0.7990 0.7164 0.3583 0.1685  -0.0655 0.0271  122 ASP   B C   
1571 O O   . ASP   B 113 ? 0.7824 0.6928 0.3442 0.1606  -0.0706 0.0241  122 ASP   B O   
1572 C CB  . ASP   B 113 ? 0.8687 0.7773 0.4345 0.1881  -0.0836 0.0214  122 ASP   B CB  
1573 C CG  . ASP   B 113 ? 0.8912 0.7991 0.4617 0.1963  -0.0900 0.0226  122 ASP   B CG  
1574 O OD1 . ASP   B 113 ? 0.9042 0.8156 0.4767 0.1883  -0.0869 0.0317  122 ASP   B OD1 
1575 O OD2 . ASP   B 113 ? 0.9258 0.8302 0.4987 0.2111  -0.0984 0.0135  122 ASP   B OD2 
1576 N N   . ILE   B 114 ? 0.7582 0.6861 0.3127 0.1742  -0.0536 0.0282  123 ILE   B N   
1577 C CA  . ILE   B 114 ? 0.7678 0.6996 0.3191 0.1737  -0.0459 0.0252  123 ILE   B CA  
1578 C C   . ILE   B 114 ? 0.7368 0.6756 0.2826 0.1933  -0.0421 0.0210  123 ILE   B C   
1579 O O   . ILE   B 114 ? 0.7276 0.6737 0.2723 0.2014  -0.0377 0.0250  123 ILE   B O   
1580 C CB  . ILE   B 114 ? 0.7596 0.6980 0.3121 0.1600  -0.0345 0.0318  123 ILE   B CB  
1581 C CG1 . ILE   B 114 ? 0.8032 0.7396 0.3592 0.1437  -0.0368 0.0380  123 ILE   B CG1 
1582 C CG2 . ILE   B 114 ? 0.7879 0.7269 0.3401 0.1549  -0.0297 0.0280  123 ILE   B CG2 
1583 C CD1 . ILE   B 114 ? 0.7865 0.7317 0.3439 0.1331  -0.0255 0.0431  123 ILE   B CD1 
1584 N N   . GLY   B 115 ? 0.7437 0.6822 0.2862 0.2004  -0.0430 0.0141  124 GLY   B N   
1585 C CA  . GLY   B 115 ? 0.7046 0.6527 0.2405 0.2178  -0.0375 0.0119  124 GLY   B CA  
1586 C C   . GLY   B 115 ? 0.6943 0.6528 0.2300 0.2159  -0.0232 0.0211  124 GLY   B C   
1587 O O   . GLY   B 115 ? 0.6592 0.6166 0.1999 0.2002  -0.0175 0.0259  124 GLY   B O   
1588 N N   . ALA   B 116 ? 0.6701 0.6393 0.2013 0.2307  -0.0172 0.0238  125 ALA   B N   
1589 C CA  . ALA   B 116 ? 0.6749 0.6545 0.2080 0.2303  -0.0037 0.0336  125 ALA   B CA  
1590 C C   . ALA   B 116 ? 0.6995 0.6897 0.2254 0.2480  0.0011  0.0339  125 ALA   B C   
1591 O O   . ALA   B 116 ? 0.7172 0.7101 0.2362 0.2625  -0.0053 0.0277  125 ALA   B O   
1592 C CB  . ALA   B 116 ? 0.6798 0.6643 0.2168 0.2298  -0.0007 0.0403  125 ALA   B CB  
1593 N N   A VAL   B 117 ? 0.6957 0.6924 0.2238 0.2470  0.0118  0.0409  126 VAL   B N   
1594 N N   B VAL   B 117 ? 0.6961 0.6931 0.2244 0.2470  0.0120  0.0412  126 VAL   B N   
1595 N N   C VAL   B 117 ? 0.6951 0.6918 0.2232 0.2470  0.0118  0.0409  126 VAL   B N   
1596 N N   D VAL   B 117 ? 0.6952 0.6918 0.2233 0.2470  0.0118  0.0409  126 VAL   B N   
1597 C CA  A VAL   B 117 ? 0.7038 0.7123 0.2252 0.2635  0.0174  0.0439  126 VAL   B CA  
1598 C CA  B VAL   B 117 ? 0.7036 0.7118 0.2254 0.2628  0.0178  0.0441  126 VAL   B CA  
1599 C CA  C VAL   B 117 ? 0.7028 0.7112 0.2241 0.2635  0.0174  0.0439  126 VAL   B CA  
1600 C CA  D VAL   B 117 ? 0.7028 0.7112 0.2242 0.2635  0.0174  0.0439  126 VAL   B CA  
1601 C C   A VAL   B 117 ? 0.7102 0.7305 0.2364 0.2658  0.0300  0.0569  126 VAL   B C   
1602 C C   B VAL   B 117 ? 0.7099 0.7303 0.2360 0.2658  0.0303  0.0571  126 VAL   B C   
1603 C C   C VAL   B 117 ? 0.7105 0.7308 0.2366 0.2658  0.0300  0.0569  126 VAL   B C   
1604 C C   D VAL   B 117 ? 0.7105 0.7307 0.2366 0.2658  0.0300  0.0569  126 VAL   B C   
1605 O O   A VAL   B 117 ? 0.7050 0.7231 0.2418 0.2524  0.0369  0.0635  126 VAL   B O   
1606 O O   B VAL   B 117 ? 0.7037 0.7223 0.2405 0.2528  0.0375  0.0639  126 VAL   B O   
1607 O O   C VAL   B 117 ? 0.7055 0.7237 0.2423 0.2525  0.0369  0.0635  126 VAL   B O   
1608 O O   D VAL   B 117 ? 0.7054 0.7236 0.2422 0.2525  0.0369  0.0635  126 VAL   B O   
1609 C CB  A VAL   B 117 ? 0.7036 0.7095 0.2240 0.2628  0.0177  0.0410  126 VAL   B CB  
1610 C CB  B VAL   B 117 ? 0.7030 0.7077 0.2255 0.2593  0.0187  0.0418  126 VAL   B CB  
1611 C CB  C VAL   B 117 ? 0.7031 0.7090 0.2234 0.2628  0.0177  0.0410  126 VAL   B CB  
1612 C CB  D VAL   B 117 ? 0.7031 0.7090 0.2234 0.2628  0.0177  0.0410  126 VAL   B CB  
1613 C CG1 A VAL   B 117 ? 0.7068 0.7036 0.2223 0.2640  0.0047  0.0278  126 VAL   B CG1 
1614 C CG1 B VAL   B 117 ? 0.7075 0.7241 0.2257 0.2727  0.0262  0.0482  126 VAL   B CG1 
1615 C CG1 C VAL   B 117 ? 0.7058 0.7027 0.2212 0.2642  0.0047  0.0278  126 VAL   B CG1 
1616 C CG1 D VAL   B 117 ? 0.7058 0.7027 0.2213 0.2642  0.0047  0.0278  126 VAL   B CG1 
1617 C CG2 A VAL   B 117 ? 0.6969 0.6982 0.2285 0.2462  0.0248  0.0460  126 VAL   B CG2 
1618 C CG2 B VAL   B 117 ? 0.7094 0.7046 0.2276 0.2593  0.0062  0.0290  126 VAL   B CG2 
1619 C CG2 C VAL   B 117 ? 0.6973 0.6986 0.2290 0.2461  0.0247  0.0459  126 VAL   B CG2 
1620 C CG2 D VAL   B 117 ? 0.6973 0.6985 0.2290 0.2461  0.0247  0.0459  126 VAL   B CG2 
1621 N N   . ALA   B 118 ? 0.7174 0.7508 0.2364 0.2827  0.0329  0.0602  127 ALA   B N   
1622 C CA  . ALA   B 118 ? 0.7306 0.7774 0.2547 0.2865  0.0448  0.0734  127 ALA   B CA  
1623 C C   . ALA   B 118 ? 0.7586 0.8163 0.2810 0.2952  0.0541  0.0827  127 ALA   B C   
1624 O O   . ALA   B 118 ? 0.7484 0.8206 0.2619 0.3118  0.0572  0.0863  127 ALA   B O   
1625 C CB  . ALA   B 118 ? 0.7314 0.7879 0.2502 0.2991  0.0429  0.0722  127 ALA   B CB  
1626 N N   . LEU   B 119 ? 0.7639 0.8153 0.2947 0.2846  0.0582  0.0862  128 LEU   B N   
1627 C CA  . LEU   B 119 ? 0.7789 0.8380 0.3109 0.2909  0.0661  0.0955  128 LEU   B CA  
1628 C C   . LEU   B 119 ? 0.8189 0.8757 0.3692 0.2769  0.0758  0.1059  128 LEU   B C   
1629 O O   . LEU   B 119 ? 0.8483 0.8929 0.4076 0.2604  0.0731  0.1003  128 LEU   B O   
1630 C CB  . LEU   B 119 ? 0.7884 0.8401 0.3133 0.2926  0.0585  0.0859  128 LEU   B CB  
1631 C CG  . LEU   B 119 ? 0.7933 0.8465 0.3020 0.3059  0.0475  0.0736  128 LEU   B CG  
1632 C CD1 . LEU   B 119 ? 0.7928 0.8374 0.2979 0.3049  0.0393  0.0633  128 LEU   B CD1 
1633 C CD2 . LEU   B 119 ? 0.8244 0.8961 0.3213 0.3261  0.0514  0.0795  128 LEU   B CD2 
1634 N N   . ASP   B 120 ? 0.8970 0.9659 0.4533 0.2831  0.0864  0.1205  129 ASP   B N   
1635 C CA  . ASP   B 120 ? 0.9055 0.9744 0.4821 0.2716  0.0962  0.1317  129 ASP   B CA  
1636 C C   . ASP   B 120 ? 0.8755 0.9420 0.4600 0.2703  0.1004  0.1372  129 ASP   B C   
1637 O O   . ASP   B 120 ? 0.8859 0.9629 0.4649 0.2837  0.1044  0.1462  129 ASP   B O   
1638 C CB  . ASP   B 120 ? 0.9600 1.0445 0.5407 0.2792  0.1050  0.1452  129 ASP   B CB  
1639 C CG  . ASP   B 120 ? 0.9802 1.0628 0.5805 0.2651  0.1105  0.1507  129 ASP   B CG  
1640 O OD1 . ASP   B 120 ? 0.9689 1.0384 0.5768 0.2497  0.1062  0.1420  129 ASP   B OD1 
1641 O OD2 . ASP   B 120 ? 1.0377 1.1333 0.6460 0.2697  0.1191  0.1635  129 ASP   B OD2 
1642 N N   . TYR   B 121 ? 0.8163 0.8702 0.4128 0.2553  0.0991  0.1313  130 TYR   B N   
1643 C CA  . TYR   B 121 ? 0.7918 0.8415 0.3994 0.2521  0.1025  0.1345  130 TYR   B CA  
1644 C C   . TYR   B 121 ? 0.7569 0.7997 0.3871 0.2351  0.1073  0.1355  130 TYR   B C   
1645 O O   . TYR   B 121 ? 0.7259 0.7652 0.3592 0.2248  0.1055  0.1300  130 TYR   B O   
1646 C CB  . TYR   B 121 ? 0.8242 0.8654 0.4218 0.2522  0.0935  0.1213  130 TYR   B CB  
1647 C CG  . TYR   B 121 ? 0.8522 0.9007 0.4316 0.2698  0.0893  0.1212  130 TYR   B CG  
1648 C CD1 . TYR   B 121 ? 0.8716 0.9275 0.4525 0.2800  0.0940  0.1318  130 TYR   B CD1 
1649 C CD2 . TYR   B 121 ? 0.8737 0.9220 0.4351 0.2763  0.0800  0.1100  130 TYR   B CD2 
1650 C CE1 . TYR   B 121 ? 0.9101 0.9745 0.4731 0.2966  0.0897  0.1312  130 TYR   B CE1 
1651 C CE2 . TYR   B 121 ? 0.9091 0.9652 0.4540 0.2930  0.0754  0.1082  130 TYR   B CE2 
1652 C CZ  . TYR   B 121 ? 0.9276 0.9925 0.4725 0.3033  0.0803  0.1186  130 TYR   B CZ  
1653 O OH  . TYR   B 121 ? 0.9948 1.0689 0.5224 0.3200  0.0754  0.1164  130 TYR   B OH  
1654 N N   . PRO   B 122 ? 0.7225 0.7633 0.3695 0.2319  0.1129  0.1418  131 PRO   B N   
1655 C CA  . PRO   B 122 ? 0.6986 0.7338 0.3688 0.2167  0.1174  0.1418  131 PRO   B CA  
1656 C C   . PRO   B 122 ? 0.6738 0.6982 0.3416 0.2031  0.1101  0.1240  131 PRO   B C   
1657 O O   . PRO   B 122 ? 0.6504 0.6707 0.3026 0.2060  0.1027  0.1141  131 PRO   B O   
1658 C CB  . PRO   B 122 ? 0.7135 0.7480 0.4009 0.2184  0.1232  0.1507  131 PRO   B CB  
1659 C CG  . PRO   B 122 ? 0.7257 0.7691 0.3980 0.2365  0.1235  0.1603  131 PRO   B CG  
1660 C CD  . PRO   B 122 ? 0.7371 0.7807 0.3830 0.2425  0.1145  0.1484  131 PRO   B CD  
1661 N N   . ALA   B 123 ? 0.6700 0.6912 0.3527 0.1892  0.1122  0.1209  132 ALA   B N   
1662 C CA  . ALA   B 123 ? 0.6558 0.6693 0.3382 0.1746  0.1066  0.1054  132 ALA   B CA  
1663 C C   . ALA   B 123 ? 0.6499 0.6569 0.3335 0.1718  0.1039  0.0961  132 ALA   B C   
1664 O O   . ALA   B 123 ? 0.6206 0.6229 0.2927 0.1658  0.0969  0.0835  132 ALA   B O   
1665 C CB  . ALA   B 123 ? 0.6590 0.6726 0.3602 0.1614  0.1105  0.1050  132 ALA   B CB  
1666 N N   . GLY   B 124 ? 0.6334 0.6406 0.3301 0.1767  0.1088  0.1025  133 GLY   B N   
1667 C CA  . GLY   B 124 ? 0.6274 0.6293 0.3278 0.1751  0.1066  0.0942  133 GLY   B CA  
1668 C C   . GLY   B 124 ? 0.6087 0.6103 0.2876 0.1856  0.0997  0.0903  133 GLY   B C   
1669 O O   . GLY   B 124 ? 0.6108 0.6086 0.2928 0.1846  0.0974  0.0831  133 GLY   B O   
1670 N N   . THR   B 125 ? 0.5992 0.6048 0.2588 0.1946  0.0961  0.0934  134 THR   B N   
1671 C CA  . THR   B 125 ? 0.6122 0.6174 0.2509 0.2035  0.0876  0.0868  134 THR   B CA  
1672 C C   . THR   B 125 ? 0.6091 0.6080 0.2398 0.1920  0.0802  0.0727  134 THR   B C   
1673 O O   . THR   B 125 ? 0.6099 0.6061 0.2274 0.1956  0.0721  0.0642  134 THR   B O   
1674 C CB  . THR   B 125 ? 0.6489 0.6623 0.2725 0.2196  0.0873  0.0960  134 THR   B CB  
1675 O OG1 . THR   B 125 ? 0.6344 0.6548 0.2684 0.2271  0.0958  0.1111  134 THR   B OG1 
1676 C CG2 . THR   B 125 ? 0.6544 0.6694 0.2605 0.2325  0.0799  0.0913  134 THR   B CG2 
1677 N N   . SER   B 126 ? 0.5949 0.5922 0.2337 0.1786  0.0824  0.0706  135 SER   B N   
1678 C CA  . SER   B 126 ? 0.5985 0.5913 0.2314 0.1662  0.0762  0.0593  135 SER   B CA  
1679 C C   . SER   B 126 ? 0.5817 0.5702 0.2116 0.1643  0.0711  0.0487  135 SER   B C   
1680 O O   . SER   B 126 ? 0.6076 0.5957 0.2503 0.1619  0.0751  0.0468  135 SER   B O   
1681 C CB  . SER   B 126 ? 0.5931 0.5859 0.2389 0.1511  0.0802  0.0571  135 SER   B CB  
1682 O OG  . SER   B 126 ? 0.6042 0.6005 0.2498 0.1512  0.0819  0.0643  135 SER   B OG  
1683 N N   . GLY   B 127 ? 0.5781 0.5638 0.1936 0.1655  0.0626  0.0426  136 GLY   B N   
1684 C CA  . GLY   B 127 ? 0.5750 0.5570 0.1893 0.1610  0.0573  0.0318  136 GLY   B CA  
1685 C C   . GLY   B 127 ? 0.5845 0.5663 0.1902 0.1744  0.0519  0.0304  136 GLY   B C   
1686 O O   . GLY   B 127 ? 0.5669 0.5457 0.1710 0.1707  0.0461  0.0212  136 GLY   B O   
1687 N N   . SER   B 128 ? 0.5827 0.5686 0.1828 0.1895  0.0536  0.0393  137 SER   B N   
1688 C CA  . SER   B 128 ? 0.5889 0.5768 0.1787 0.2046  0.0480  0.0383  137 SER   B CA  
1689 C C   . SER   B 128 ? 0.5800 0.5639 0.1576 0.2047  0.0375  0.0297  137 SER   B C   
1690 O O   . SER   B 128 ? 0.5991 0.5802 0.1738 0.1964  0.0359  0.0297  137 SER   B O   
1691 C CB  . SER   B 128 ? 0.5857 0.5813 0.1709 0.2202  0.0525  0.0501  137 SER   B CB  
1692 O OG  . SER   B 128 ? 0.5932 0.5912 0.1943 0.2168  0.0628  0.0595  137 SER   B OG  
1693 N N   . PRO   B 129 ? 0.5789 0.5614 0.1517 0.2107  0.0298  0.0219  138 PRO   B N   
1694 C CA  . PRO   B 129 ? 0.5764 0.5540 0.1412 0.2098  0.0192  0.0131  138 PRO   B CA  
1695 C C   . PRO   B 129 ? 0.5964 0.5767 0.1477 0.2250  0.0133  0.0137  138 PRO   B C   
1696 O O   . PRO   B 129 ? 0.5975 0.5852 0.1431 0.2403  0.0151  0.0180  138 PRO   B O   
1697 C CB  . PRO   B 129 ? 0.5806 0.5565 0.1483 0.2102  0.0135  0.0043  138 PRO   B CB  
1698 C CG  . PRO   B 129 ? 0.5768 0.5583 0.1504 0.2172  0.0201  0.0092  138 PRO   B CG  
1699 C CD  . PRO   B 129 ? 0.5667 0.5513 0.1461 0.2147  0.0311  0.0204  138 PRO   B CD  
1700 N N   . ILE   B 130 ? 0.6012 0.5759 0.1483 0.2213  0.0054  0.0082  139 ILE   B N   
1701 C CA  . ILE   B 130 ? 0.6236 0.5993 0.1594 0.2346  -0.0024 0.0053  139 ILE   B CA  
1702 C C   . ILE   B 130 ? 0.6451 0.6154 0.1801 0.2359  -0.0143 -0.0066 139 ILE   B C   
1703 O O   . ILE   B 130 ? 0.6322 0.5959 0.1751 0.2220  -0.0168 -0.0109 139 ILE   B O   
1704 C CB  . ILE   B 130 ? 0.6319 0.6052 0.1662 0.2302  -0.0029 0.0084  139 ILE   B CB  
1705 C CG1 . ILE   B 130 ? 0.6337 0.6136 0.1702 0.2299  0.0087  0.0202  139 ILE   B CG1 
1706 C CG2 . ILE   B 130 ? 0.6428 0.6156 0.1680 0.2429  -0.0130 0.0023  139 ILE   B CG2 
1707 C CD1 . ILE   B 130 ? 0.6424 0.6178 0.1848 0.2149  0.0105  0.0230  139 ILE   B CD1 
1708 N N   . LEU   B 131 ? 0.6716 0.6468 0.1982 0.2528  -0.0203 -0.0115 140 LEU   B N   
1709 C CA  . LEU   B 131 ? 0.6983 0.6694 0.2260 0.2551  -0.0319 -0.0236 140 LEU   B CA  
1710 C C   . LEU   B 131 ? 0.7136 0.6830 0.2340 0.2661  -0.0435 -0.0321 140 LEU   B C   
1711 O O   . LEU   B 131 ? 0.7341 0.7100 0.2451 0.2780  -0.0413 -0.0282 140 LEU   B O   
1712 C CB  . LEU   B 131 ? 0.7207 0.7000 0.2454 0.2671  -0.0309 -0.0245 140 LEU   B CB  
1713 C CG  . LEU   B 131 ? 0.7289 0.7119 0.2605 0.2615  -0.0193 -0.0156 140 LEU   B CG  
1714 C CD1 . LEU   B 131 ? 0.7586 0.7497 0.2868 0.2752  -0.0205 -0.0165 140 LEU   B CD1 
1715 C CD2 . LEU   B 131 ? 0.7212 0.6964 0.2664 0.2419  -0.0177 -0.0182 140 LEU   B CD2 
1716 N N   . ASP   B 132 ? 0.7198 0.6817 0.2455 0.2628  -0.0553 -0.0433 141 ASP   B N   
1717 C CA  . ASP   B 132 ? 0.7478 0.7080 0.2690 0.2751  -0.0684 -0.0544 141 ASP   B CA  
1718 C C   . ASP   B 132 ? 0.7650 0.7330 0.2808 0.2904  -0.0740 -0.0627 141 ASP   B C   
1719 O O   . ASP   B 132 ? 0.7315 0.7060 0.2468 0.2914  -0.0670 -0.0581 141 ASP   B O   
1720 C CB  . ASP   B 132 ? 0.7544 0.7014 0.2866 0.2631  -0.0792 -0.0615 141 ASP   B CB  
1721 C CG  . ASP   B 132 ? 0.7632 0.7050 0.3069 0.2519  -0.0834 -0.0668 141 ASP   B CG  
1722 O OD1 . ASP   B 132 ? 0.7582 0.7064 0.3012 0.2563  -0.0810 -0.0685 141 ASP   B OD1 
1723 O OD2 . ASP   B 132 ? 0.7912 0.7230 0.3455 0.2374  -0.0884 -0.0678 141 ASP   B OD2 
1724 N N   . LYS   B 133 ? 0.8139 0.7805 0.3275 0.3011  -0.0872 -0.0754 142 LYS   B N   
1725 C CA  . LYS   B 133 ? 0.8720 0.8490 0.3767 0.3202  -0.0938 -0.0846 142 LYS   B CA  
1726 C C   . LYS   B 133 ? 0.8514 0.8264 0.3650 0.3147  -0.0980 -0.0901 142 LYS   B C   
1727 O O   . LYS   B 133 ? 0.8223 0.8079 0.3287 0.3279  -0.0994 -0.0932 142 LYS   B O   
1728 C CB  . LYS   B 133 ? 0.9312 0.9071 0.4326 0.3328  -0.1073 -0.0983 142 LYS   B CB  
1729 C CG  . LYS   B 133 ? 1.0144 1.0013 0.5012 0.3483  -0.1029 -0.0951 142 LYS   B CG  
1730 C CD  . LYS   B 133 ? 1.0837 1.0644 0.5728 0.3520  -0.1121 -0.1037 142 LYS   B CD  
1731 C CE  . LYS   B 133 ? 1.1367 1.1319 0.6109 0.3698  -0.1074 -0.1019 142 LYS   B CE  
1732 N NZ  . LYS   B 133 ? 1.1590 1.1519 0.6341 0.3801  -0.1196 -0.1159 142 LYS   B NZ  
1733 N N   . CYS   B 134 ? 0.8705 0.8337 0.3992 0.2957  -0.0994 -0.0905 143 CYS   B N   
1734 C CA  . CYS   B 134 ? 0.8661 0.8270 0.4066 0.2874  -0.1028 -0.0955 143 CYS   B CA  
1735 C C   . CYS   B 134 ? 0.8362 0.8008 0.3797 0.2777  -0.0888 -0.0840 143 CYS   B C   
1736 O O   . CYS   B 134 ? 0.8102 0.7736 0.3648 0.2696  -0.0900 -0.0874 143 CYS   B O   
1737 C CB  . CYS   B 134 ? 0.9154 0.8632 0.4718 0.2713  -0.1109 -0.1009 143 CYS   B CB  
1738 S SG  . CYS   B 134 ? 0.9596 0.9010 0.5211 0.2807  -0.1310 -0.1183 143 CYS   B SG  
1739 N N   . GLY   B 135 ? 0.8067 0.7758 0.3427 0.2784  -0.0762 -0.0714 144 GLY   B N   
1740 C CA  . GLY   B 135 ? 0.7730 0.7453 0.3137 0.2698  -0.0631 -0.0610 144 GLY   B CA  
1741 C C   . GLY   B 135 ? 0.7455 0.7094 0.2979 0.2479  -0.0573 -0.0568 144 GLY   B C   
1742 O O   . GLY   B 135 ? 0.7407 0.7068 0.3001 0.2396  -0.0483 -0.0517 144 GLY   B O   
1743 N N   . ARG   B 136 ? 0.7165 0.6721 0.2715 0.2393  -0.0624 -0.0589 145 ARG   B N   
1744 C CA  . ARG   B 136 ? 0.7119 0.6615 0.2764 0.2184  -0.0567 -0.0540 145 ARG   B CA  
1745 C C   . ARG   B 136 ? 0.6867 0.6380 0.2460 0.2152  -0.0458 -0.0427 145 ARG   B C   
1746 O O   . ARG   B 136 ? 0.6895 0.6418 0.2393 0.2255  -0.0471 -0.0403 145 ARG   B O   
1747 C CB  . ARG   B 136 ? 0.7459 0.6863 0.3172 0.2104  -0.0681 -0.0605 145 ARG   B CB  
1748 C CG  . ARG   B 136 ? 0.7960 0.7356 0.3781 0.2074  -0.0754 -0.0699 145 ARG   B CG  
1749 C CD  . ARG   B 136 ? 0.8540 0.7844 0.4446 0.2013  -0.0880 -0.0764 145 ARG   B CD  
1750 N NE  . ARG   B 136 ? 0.9350 0.8623 0.5171 0.2149  -0.0959 -0.0795 145 ARG   B NE  
1751 C CZ  . ARG   B 136 ? 0.9848 0.9032 0.5703 0.2106  -0.1034 -0.0799 145 ARG   B CZ  
1752 N NH1 . ARG   B 136 ? 0.9936 0.9051 0.5903 0.1923  -0.1042 -0.0759 145 ARG   B NH1 
1753 N NH2 . ARG   B 136 ? 1.0386 0.9558 0.6165 0.2253  -0.1102 -0.0843 145 ARG   B NH2 
1754 N N   . VAL   B 137 ? 0.6511 0.6026 0.2177 0.1998  -0.0363 -0.0371 146 VAL   B N   
1755 C CA  . VAL   B 137 ? 0.6300 0.5833 0.1942 0.1945  -0.0259 -0.0270 146 VAL   B CA  
1756 C C   . VAL   B 137 ? 0.6321 0.5785 0.1956 0.1854  -0.0308 -0.0260 146 VAL   B C   
1757 O O   . VAL   B 137 ? 0.6349 0.5773 0.2061 0.1700  -0.0329 -0.0279 146 VAL   B O   
1758 C CB  . VAL   B 137 ? 0.6050 0.5622 0.1776 0.1836  -0.0145 -0.0229 146 VAL   B CB  
1759 C CG1 . VAL   B 137 ? 0.5896 0.5488 0.1610 0.1790  -0.0050 -0.0136 146 VAL   B CG1 
1760 C CG2 . VAL   B 137 ? 0.6092 0.5724 0.1834 0.1946  -0.0111 -0.0234 146 VAL   B CG2 
1761 N N   . ILE   B 138 ? 0.6286 0.5748 0.1840 0.1945  -0.0323 -0.0225 147 ILE   B N   
1762 C CA  . ILE   B 138 ? 0.6333 0.5734 0.1881 0.1883  -0.0372 -0.0204 147 ILE   B CA  
1763 C C   . ILE   B 138 ? 0.6196 0.5622 0.1751 0.1778  -0.0271 -0.0108 147 ILE   B C   
1764 O O   . ILE   B 138 ? 0.6221 0.5603 0.1779 0.1702  -0.0303 -0.0077 147 ILE   B O   
1765 C CB  . ILE   B 138 ? 0.6444 0.5834 0.1915 0.2049  -0.0456 -0.0239 147 ILE   B CB  
1766 C CG1 . ILE   B 138 ? 0.6451 0.5934 0.1833 0.2195  -0.0380 -0.0185 147 ILE   B CG1 
1767 C CG2 . ILE   B 138 ? 0.6507 0.5862 0.1993 0.2124  -0.0573 -0.0351 147 ILE   B CG2 
1768 C CD1 . ILE   B 138 ? 0.6681 0.6172 0.1988 0.2338  -0.0443 -0.0207 147 ILE   B CD1 
1769 N N   . GLY   B 139 ? 0.6113 0.5606 0.1683 0.1772  -0.0160 -0.0063 148 GLY   B N   
1770 C CA  . GLY   B 139 ? 0.5981 0.5501 0.1583 0.1659  -0.0067 0.0010  148 GLY   B CA  
1771 C C   . GLY   B 139 ? 0.5912 0.5503 0.1529 0.1723  0.0037  0.0060  148 GLY   B C   
1772 O O   . GLY   B 139 ? 0.5794 0.5419 0.1388 0.1857  0.0038  0.0045  148 GLY   B O   
1773 N N   A LEU   B 140 ? 0.5807 0.5428 0.1470 0.1636  0.0120  0.0121  149 LEU   B N   
1774 N N   B LEU   B 140 ? 0.5809 0.5429 0.1471 0.1636  0.0120  0.0120  149 LEU   B N   
1775 N N   C LEU   B 140 ? 0.5720 0.5342 0.1375 0.1650  0.0118  0.0125  149 LEU   B N   
1776 N N   D LEU   B 140 ? 0.5721 0.5343 0.1376 0.1649  0.0118  0.0125  149 LEU   B N   
1777 C CA  A LEU   B 140 ? 0.5780 0.5461 0.1503 0.1656  0.0229  0.0176  149 LEU   B CA  
1778 C CA  B LEU   B 140 ? 0.5781 0.5462 0.1504 0.1656  0.0229  0.0176  149 LEU   B CA  
1779 C CA  C LEU   B 140 ? 0.5695 0.5378 0.1413 0.1664  0.0228  0.0180  149 LEU   B CA  
1780 C CA  D LEU   B 140 ? 0.5696 0.5378 0.1414 0.1664  0.0228  0.0180  149 LEU   B CA  
1781 C C   A LEU   B 140 ? 0.5841 0.5559 0.1535 0.1723  0.0268  0.0262  149 LEU   B C   
1782 C C   B LEU   B 140 ? 0.5841 0.5559 0.1535 0.1722  0.0268  0.0262  149 LEU   B C   
1783 C C   C LEU   B 140 ? 0.5817 0.5539 0.1506 0.1736  0.0270  0.0268  149 LEU   B C   
1784 C C   D LEU   B 140 ? 0.5817 0.5539 0.1506 0.1736  0.0269  0.0268  149 LEU   B C   
1785 O O   A LEU   B 140 ? 0.5878 0.5577 0.1540 0.1678  0.0231  0.0276  149 LEU   B O   
1786 O O   B LEU   B 140 ? 0.5878 0.5575 0.1539 0.1677  0.0231  0.0276  149 LEU   B O   
1787 O O   C LEU   B 140 ? 0.5810 0.5506 0.1456 0.1695  0.0220  0.0279  149 LEU   B O   
1788 O O   D LEU   B 140 ? 0.5810 0.5506 0.1456 0.1695  0.0220  0.0279  149 LEU   B O   
1789 C CB  A LEU   B 140 ? 0.5702 0.5394 0.1533 0.1493  0.0292  0.0158  149 LEU   B CB  
1790 C CB  B LEU   B 140 ? 0.5702 0.5394 0.1533 0.1493  0.0292  0.0158  149 LEU   B CB  
1791 C CB  C LEU   B 140 ? 0.5587 0.5277 0.1411 0.1497  0.0288  0.0161  149 LEU   B CB  
1792 C CB  D LEU   B 140 ? 0.5587 0.5278 0.1411 0.1497  0.0288  0.0161  149 LEU   B CB  
1793 C CG  A LEU   B 140 ? 0.5651 0.5330 0.1532 0.1429  0.0274  0.0075  149 LEU   B CG  
1794 C CG  B LEU   B 140 ? 0.5652 0.5332 0.1534 0.1429  0.0274  0.0075  149 LEU   B CG  
1795 C CG  C LEU   B 140 ? 0.5498 0.5177 0.1374 0.1433  0.0272  0.0079  149 LEU   B CG  
1796 C CG  D LEU   B 140 ? 0.5498 0.5177 0.1374 0.1434  0.0272  0.0079  149 LEU   B CG  
1797 C CD1 A LEU   B 140 ? 0.5597 0.5316 0.1598 0.1305  0.0359  0.0059  149 LEU   B CD1 
1798 C CD1 B LEU   B 140 ? 0.5598 0.5316 0.1598 0.1305  0.0359  0.0059  149 LEU   B CD1 
1799 C CD1 C LEU   B 140 ? 0.5433 0.5151 0.1428 0.1313  0.0359  0.0065  149 LEU   B CD1 
1800 C CD1 D LEU   B 140 ? 0.5433 0.5151 0.1428 0.1313  0.0359  0.0065  149 LEU   B CD1 
1801 C CD2 A LEU   B 140 ? 0.5711 0.5395 0.1580 0.1568  0.0252  0.0053  149 LEU   B CD2 
1802 C CD2 B LEU   B 140 ? 0.5711 0.5396 0.1581 0.1568  0.0252  0.0053  149 LEU   B CD2 
1803 C CD2 C LEU   B 140 ? 0.5565 0.5248 0.1428 0.1572  0.0250  0.0056  149 LEU   B CD2 
1804 C CD2 D LEU   B 140 ? 0.5565 0.5249 0.1428 0.1572  0.0250  0.0056  149 LEU   B CD2 
1805 N N   A TYR   B 141 ? 0.5809 0.5587 0.1513 0.1840  0.0333  0.0324  150 TYR   B N   
1806 N N   B TYR   B 141 ? 0.5813 0.5591 0.1517 0.1840  0.0333  0.0324  150 TYR   B N   
1807 N N   C TYR   B 141 ? 0.5782 0.5566 0.1506 0.1826  0.0351  0.0334  150 TYR   B N   
1808 N N   D TYR   B 141 ? 0.5784 0.5567 0.1507 0.1826  0.0351  0.0334  150 TYR   B N   
1809 C CA  A TYR   B 141 ? 0.5913 0.5749 0.1613 0.1907  0.0389  0.0419  150 TYR   B CA  
1810 C CA  B TYR   B 141 ? 0.5914 0.5750 0.1614 0.1907  0.0389  0.0419  150 TYR   B CA  
1811 C CA  C TYR   B 141 ? 0.5966 0.5807 0.1683 0.1895  0.0404  0.0429  150 TYR   B CA  
1812 C CA  D TYR   B 141 ? 0.5967 0.5808 0.1684 0.1896  0.0404  0.0429  150 TYR   B CA  
1813 C C   A TYR   B 141 ? 0.5819 0.5675 0.1653 0.1789  0.0483  0.0469  150 TYR   B C   
1814 C C   B TYR   B 141 ? 0.5821 0.5678 0.1656 0.1789  0.0483  0.0469  150 TYR   B C   
1815 C C   C TYR   B 141 ? 0.5897 0.5762 0.1747 0.1785  0.0498  0.0483  150 TYR   B C   
1816 C C   D TYR   B 141 ? 0.5898 0.5763 0.1748 0.1785  0.0498  0.0483  150 TYR   B C   
1817 O O   A TYR   B 141 ? 0.5918 0.5762 0.1845 0.1715  0.0518  0.0437  150 TYR   B O   
1818 O O   B TYR   B 141 ? 0.5916 0.5760 0.1843 0.1715  0.0518  0.0437  150 TYR   B O   
1819 O O   C TYR   B 141 ? 0.6096 0.5958 0.2051 0.1726  0.0548  0.0470  150 TYR   B O   
1820 O O   D TYR   B 141 ? 0.6094 0.5956 0.2049 0.1727  0.0548  0.0470  150 TYR   B O   
1821 C CB  A TYR   B 141 ? 0.6001 0.5903 0.1642 0.2091  0.0408  0.0466  150 TYR   B CB  
1822 C CB  B TYR   B 141 ? 0.6003 0.5905 0.1644 0.2091  0.0408  0.0465  150 TYR   B CB  
1823 C CB  C TYR   B 141 ? 0.6101 0.6009 0.1767 0.2076  0.0429  0.0481  150 TYR   B CB  
1824 C CB  D TYR   B 141 ? 0.6102 0.6010 0.1768 0.2077  0.0429  0.0481  150 TYR   B CB  
1825 C CG  A TYR   B 141 ? 0.6100 0.6090 0.1759 0.2173  0.0491  0.0583  150 TYR   B CG  
1826 C CG  B TYR   B 141 ? 0.6100 0.6090 0.1759 0.2173  0.0491  0.0583  150 TYR   B CG  
1827 C CG  C TYR   B 141 ? 0.6268 0.6261 0.1958 0.2148  0.0511  0.0598  150 TYR   B CG  
1828 C CG  D TYR   B 141 ? 0.6268 0.6260 0.1958 0.2148  0.0511  0.0598  150 TYR   B CG  
1829 C CD1 A TYR   B 141 ? 0.6105 0.6136 0.1881 0.2161  0.0590  0.0668  150 TYR   B CD1 
1830 C CD1 B TYR   B 141 ? 0.6104 0.6135 0.1880 0.2160  0.0590  0.0667  150 TYR   B CD1 
1831 C CD1 C TYR   B 141 ? 0.6298 0.6324 0.2121 0.2108  0.0611  0.0680  150 TYR   B CD1 
1832 C CD1 D TYR   B 141 ? 0.6297 0.6324 0.2121 0.2108  0.0611  0.0680  150 TYR   B CD1 
1833 C CD2 A TYR   B 141 ? 0.6190 0.6228 0.1762 0.2269  0.0470  0.0611  150 TYR   B CD2 
1834 C CD2 B TYR   B 141 ? 0.6189 0.6227 0.1761 0.2270  0.0470  0.0611  150 TYR   B CD2 
1835 C CD2 C TYR   B 141 ? 0.6436 0.6479 0.2032 0.2254  0.0488  0.0626  150 TYR   B CD2 
1836 C CD2 D TYR   B 141 ? 0.6436 0.6478 0.2032 0.2254  0.0488  0.0626  150 TYR   B CD2 
1837 C CE1 A TYR   B 141 ? 0.6188 0.6307 0.1998 0.2233  0.0669  0.0789  150 TYR   B CE1 
1838 C CE1 B TYR   B 141 ? 0.6186 0.6305 0.1996 0.2233  0.0669  0.0789  150 TYR   B CE1 
1839 C CE1 C TYR   B 141 ? 0.6405 0.6512 0.2272 0.2165  0.0689  0.0798  150 TYR   B CE1 
1840 C CE1 D TYR   B 141 ? 0.6404 0.6512 0.2271 0.2165  0.0688  0.0798  150 TYR   B CE1 
1841 C CE2 A TYR   B 141 ? 0.6259 0.6397 0.1853 0.2349  0.0552  0.0724  150 TYR   B CE2 
1842 C CE2 B TYR   B 141 ? 0.6256 0.6394 0.1850 0.2349  0.0552  0.0724  150 TYR   B CE2 
1843 C CE2 C TYR   B 141 ? 0.6558 0.6696 0.2183 0.2321  0.0569  0.0739  150 TYR   B CE2 
1844 C CE2 D TYR   B 141 ? 0.6557 0.6694 0.2182 0.2321  0.0569  0.0739  150 TYR   B CE2 
1845 C CZ  A TYR   B 141 ? 0.6226 0.6405 0.1939 0.2328  0.0653  0.0819  150 TYR   B CZ  
1846 C CZ  B TYR   B 141 ? 0.6224 0.6403 0.1938 0.2328  0.0653  0.0819  150 TYR   B CZ  
1847 C CZ  C TYR   B 141 ? 0.6553 0.6724 0.2316 0.2273  0.0671  0.0831  150 TYR   B CZ  
1848 C CZ  D TYR   B 141 ? 0.6552 0.6722 0.2315 0.2273  0.0671  0.0831  150 TYR   B CZ  
1849 O OH  A TYR   B 141 ? 0.6285 0.6567 0.2041 0.2395  0.0737  0.0943  150 TYR   B OH  
1850 O OH  B TYR   B 141 ? 0.6282 0.6564 0.2039 0.2395  0.0737  0.0943  150 TYR   B OH  
1851 O OH  C TYR   B 141 ? 0.6633 0.6901 0.2441 0.2333  0.0750  0.0950  150 TYR   B OH  
1852 O OH  D TYR   B 141 ? 0.6631 0.6900 0.2439 0.2333  0.0750  0.0950  150 TYR   B OH  
1853 N N   A GLY   B 142 ? 0.5814 0.5701 0.1671 0.1766  0.0513  0.0530  151 GLY   B N   
1854 N N   B GLY   B 142 ? 0.5817 0.5704 0.1674 0.1766  0.0513  0.0530  151 GLY   B N   
1855 N N   C GLY   B 142 ? 0.5899 0.5791 0.1762 0.1760  0.0519  0.0539  151 GLY   B N   
1856 N N   D GLY   B 142 ? 0.5900 0.5791 0.1763 0.1760  0.0519  0.0539  151 GLY   B N   
1857 C CA  A GLY   B 142 ? 0.5815 0.5736 0.1814 0.1680  0.0603  0.0584  151 GLY   B CA  
1858 C CA  B GLY   B 142 ? 0.5815 0.5736 0.1815 0.1680  0.0603  0.0584  151 GLY   B CA  
1859 C CA  C GLY   B 142 ? 0.5945 0.5874 0.1949 0.1679  0.0608  0.0597  151 GLY   B CA  
1860 C CA  D GLY   B 142 ? 0.5945 0.5874 0.1949 0.1679  0.0608  0.0597  151 GLY   B CA  
1861 C C   A GLY   B 142 ? 0.5804 0.5717 0.1838 0.1543  0.0592  0.0571  151 GLY   B C   
1862 C C   B GLY   B 142 ? 0.5805 0.5719 0.1840 0.1543  0.0592  0.0571  151 GLY   B C   
1863 C C   C GLY   B 142 ? 0.5951 0.5872 0.1983 0.1547  0.0593  0.0585  151 GLY   B C   
1864 C C   D GLY   B 142 ? 0.5951 0.5872 0.1983 0.1547  0.0593  0.0585  151 GLY   B C   
1865 O O   A GLY   B 142 ? 0.5773 0.5719 0.1938 0.1470  0.0662  0.0604  151 GLY   B O   
1866 O O   B GLY   B 142 ? 0.5773 0.5719 0.1939 0.1469  0.0662  0.0604  151 GLY   B O   
1867 O O   C GLY   B 142 ? 0.5929 0.5891 0.2086 0.1487  0.0662  0.0631  151 GLY   B O   
1868 O O   D GLY   B 142 ? 0.5929 0.5891 0.2086 0.1487  0.0662  0.0631  151 GLY   B O   
1869 N N   A ASN   B 143 ? 0.5896 0.5772 0.1830 0.1514  0.0507  0.0532  152 ASN   B N   
1870 N N   B ASN   B 143 ? 0.5896 0.5773 0.1831 0.1514  0.0507  0.0532  152 ASN   B N   
1871 N N   C ASN   B 143 ? 0.6070 0.5946 0.2003 0.1507  0.0504  0.0531  152 ASN   B N   
1872 N N   D ASN   B 143 ? 0.6070 0.5946 0.2003 0.1507  0.0504  0.0531  152 ASN   B N   
1873 C CA  A ASN   B 143 ? 0.5935 0.5817 0.1885 0.1407  0.0486  0.0541  152 ASN   B CA  
1874 C CA  B ASN   B 143 ? 0.5935 0.5818 0.1885 0.1408  0.0486  0.0541  152 ASN   B CA  
1875 C CA  C ASN   B 143 ? 0.6106 0.5981 0.2044 0.1395  0.0474  0.0533  152 ASN   B CA  
1876 C CA  D ASN   B 143 ? 0.6105 0.5981 0.2044 0.1395  0.0474  0.0533  152 ASN   B CA  
1877 C C   A ASN   B 143 ? 0.6053 0.5936 0.1912 0.1501  0.0424  0.0573  152 ASN   B C   
1878 C C   B ASN   B 143 ? 0.6054 0.5937 0.1913 0.1502  0.0424  0.0574  152 ASN   B C   
1879 C C   C ASN   B 143 ? 0.6148 0.6026 0.1999 0.1498  0.0415  0.0570  152 ASN   B C   
1880 C C   D ASN   B 143 ? 0.6148 0.6026 0.2000 0.1498  0.0415  0.0570  152 ASN   B C   
1881 O O   A ASN   B 143 ? 0.6155 0.5973 0.1920 0.1496  0.0323  0.0521  152 ASN   B O   
1882 O O   B ASN   B 143 ? 0.6153 0.5972 0.1918 0.1497  0.0323  0.0521  152 ASN   B O   
1883 O O   C ASN   B 143 ? 0.6292 0.6109 0.2047 0.1512  0.0314  0.0522  152 ASN   B O   
1884 O O   D ASN   B 143 ? 0.6291 0.6108 0.2045 0.1512  0.0314  0.0523  152 ASN   B O   
1885 C CB  A ASN   B 143 ? 0.5897 0.5741 0.1835 0.1247  0.0438  0.0470  152 ASN   B CB  
1886 C CB  B ASN   B 143 ? 0.5896 0.5741 0.1835 0.1247  0.0437  0.0470  152 ASN   B CB  
1887 C CB  C ASN   B 143 ? 0.6158 0.5988 0.2069 0.1249  0.0415  0.0458  152 ASN   B CB  
1888 C CB  D ASN   B 143 ? 0.6157 0.5987 0.2069 0.1250  0.0415  0.0458  152 ASN   B CB  
1889 C CG  A ASN   B 143 ? 0.5816 0.5701 0.1817 0.1123  0.0455  0.0487  152 ASN   B CG  
1890 C CG  B ASN   B 143 ? 0.5817 0.5702 0.1817 0.1123  0.0455  0.0487  152 ASN   B CG  
1891 C CG  C ASN   B 143 ? 0.6153 0.6012 0.2100 0.1122  0.0411  0.0472  152 ASN   B CG  
1892 C CG  D ASN   B 143 ? 0.6153 0.6011 0.2099 0.1122  0.0411  0.0472  152 ASN   B CG  
1893 O OD1 A ASN   B 143 ? 0.5794 0.5732 0.1897 0.1123  0.0525  0.0530  152 ASN   B OD1 
1894 O OD1 B ASN   B 143 ? 0.5795 0.5733 0.1897 0.1123  0.0525  0.0530  152 ASN   B OD1 
1895 O OD1 C ASN   B 143 ? 0.6225 0.6138 0.2260 0.1109  0.0472  0.0515  152 ASN   B OD1 
1896 O OD1 D ASN   B 143 ? 0.6224 0.6137 0.2259 0.1109  0.0472  0.0515  152 ASN   B OD1 
1897 N ND2 A ASN   B 143 ? 0.5756 0.5623 0.1704 0.1013  0.0390  0.0456  152 ASN   B ND2 
1898 N ND2 B ASN   B 143 ? 0.5759 0.5627 0.1707 0.1013  0.0390  0.0456  152 ASN   B ND2 
1899 N ND2 C ASN   B 143 ? 0.6113 0.5943 0.1999 0.1023  0.0338  0.0439  152 ASN   B ND2 
1900 N ND2 D ASN   B 143 ? 0.6114 0.5943 0.2000 0.1023  0.0338  0.0439  152 ASN   B ND2 
1901 N N   . GLY   B 144 ? 0.6070 0.6022 0.2001 0.1513  0.0479  0.0651  153 GLY   B N   
1902 C CA  . GLY   B 144 ? 0.6540 0.6513 0.2411 0.1607  0.0434  0.0685  153 GLY   B CA  
1903 C C   . GLY   B 144 ? 0.6806 0.6858 0.2774 0.1599  0.0494  0.0761  153 GLY   B C   
1904 O O   . GLY   B 144 ? 0.6774 0.6839 0.2838 0.1466  0.0522  0.0764  153 GLY   B O   
1905 N N   A VAL   B 145 ? 0.6969 0.7087 0.2918 0.1739  0.0514  0.0818  154 VAL   B N   
1906 N N   B VAL   B 145 ? 0.6969 0.7087 0.2919 0.1739  0.0514  0.0818  154 VAL   B N   
1907 N N   C VAL   B 145 ? 0.6962 0.7080 0.2911 0.1739  0.0514  0.0818  154 VAL   B N   
1908 N N   D VAL   B 145 ? 0.6790 0.6909 0.2740 0.1742  0.0517  0.0818  154 VAL   B N   
1909 C CA  A VAL   B 145 ? 0.7099 0.7300 0.3135 0.1743  0.0551  0.0889  154 VAL   B CA  
1910 C CA  B VAL   B 145 ? 0.7100 0.7301 0.3136 0.1743  0.0551  0.0889  154 VAL   B CA  
1911 C CA  C VAL   B 145 ? 0.7092 0.7293 0.3128 0.1743  0.0551  0.0889  154 VAL   B CA  
1912 C CA  D VAL   B 145 ? 0.6829 0.7030 0.2853 0.1758  0.0547  0.0887  154 VAL   B CA  
1913 C C   A VAL   B 145 ? 0.7304 0.7612 0.3373 0.1886  0.0640  0.0976  154 VAL   B C   
1914 C C   B VAL   B 145 ? 0.7302 0.7610 0.3371 0.1886  0.0640  0.0976  154 VAL   B C   
1915 C C   C VAL   B 145 ? 0.7312 0.7620 0.3380 0.1886  0.0640  0.0976  154 VAL   B C   
1916 C C   D VAL   B 145 ? 0.7117 0.7424 0.3189 0.1885  0.0646  0.0978  154 VAL   B C   
1917 O O   A VAL   B 145 ? 0.7222 0.7543 0.3191 0.2018  0.0635  0.0969  154 VAL   B O   
1918 O O   B VAL   B 145 ? 0.7226 0.7546 0.3194 0.2018  0.0635  0.0969  154 VAL   B O   
1919 O O   C VAL   B 145 ? 0.7200 0.7520 0.3168 0.2018  0.0635  0.0969  154 VAL   B O   
1920 O O   D VAL   B 145 ? 0.6973 0.7290 0.2965 0.2001  0.0657  0.0976  154 VAL   B O   
1921 C CB  A VAL   B 145 ? 0.7205 0.7383 0.3180 0.1750  0.0454  0.0863  154 VAL   B CB  
1922 C CB  B VAL   B 145 ? 0.7203 0.7382 0.3179 0.1750  0.0454  0.0863  154 VAL   B CB  
1923 C CB  C VAL   B 145 ? 0.7210 0.7388 0.3185 0.1750  0.0454  0.0863  154 VAL   B CB  
1924 C CB  D VAL   B 145 ? 0.6762 0.6939 0.2701 0.1804  0.0447  0.0857  154 VAL   B CB  
1925 C CG1 A VAL   B 145 ? 0.7216 0.7410 0.3087 0.1923  0.0412  0.0849  154 VAL   B CG1 
1926 C CG1 B VAL   B 145 ? 0.7217 0.7412 0.3089 0.1923  0.0412  0.0849  154 VAL   B CG1 
1927 C CG1 C VAL   B 145 ? 0.7202 0.7396 0.3073 0.1923  0.0412  0.0849  154 VAL   B CG1 
1928 C CG1 D VAL   B 145 ? 0.6785 0.7065 0.2773 0.1889  0.0476  0.0923  154 VAL   B CG1 
1929 C CG2 A VAL   B 145 ? 0.7252 0.7497 0.3337 0.1690  0.0474  0.0917  154 VAL   B CG2 
1930 C CG2 B VAL   B 145 ? 0.7248 0.7493 0.3333 0.1690  0.0474  0.0917  154 VAL   B CG2 
1931 C CG2 C VAL   B 145 ? 0.7274 0.7518 0.3358 0.1690  0.0475  0.0917  154 VAL   B CG2 
1932 C CG2 D VAL   B 145 ? 0.6664 0.6761 0.2598 0.1650  0.0364  0.0808  154 VAL   B CG2 
1933 N N   . VAL   B 146 ? 0.7417 0.7808 0.3628 0.1856  0.0716  0.1056  155 VAL   B N   
1934 C CA  . VAL   B 146 ? 0.7701 0.8219 0.3971 0.1977  0.0808  0.1164  155 VAL   B CA  
1935 C C   . VAL   B 146 ? 0.8391 0.8975 0.4613 0.2066  0.0769  0.1171  155 VAL   B C   
1936 O O   . VAL   B 146 ? 0.8305 0.8864 0.4569 0.1975  0.0716  0.1145  155 VAL   B O   
1937 C CB  . VAL   B 146 ? 0.7746 0.8312 0.4225 0.1880  0.0898  0.1239  155 VAL   B CB  
1938 C CG1 . VAL   B 146 ? 0.7850 0.8555 0.4421 0.1984  0.0997  0.1368  155 VAL   B CG1 
1939 C CG2 . VAL   B 146 ? 0.7866 0.8361 0.4410 0.1794  0.0929  0.1216  155 VAL   B CG2 
1940 N N   . ILE   B 147 ? 0.9038 0.9707 0.5170 0.2237  0.0786  0.1198  156 ILE   B N   
1941 C CA  . ILE   B 147 ? 0.9725 1.0442 0.5781 0.2344  0.0726  0.1167  156 ILE   B CA  
1942 C C   . ILE   B 147 ? 1.0311 1.1197 0.6470 0.2418  0.0816  0.1272  156 ILE   B C   
1943 O O   . ILE   B 147 ? 1.0177 1.1138 0.6452 0.2398  0.0923  0.1375  156 ILE   B O   
1944 C CB  . ILE   B 147 ? 0.9682 1.0382 0.5560 0.2489  0.0665  0.1092  156 ILE   B CB  
1945 C CG1 . ILE   B 147 ? 0.9778 1.0567 0.5603 0.2609  0.0748  0.1148  156 ILE   B CG1 
1946 C CG2 . ILE   B 147 ? 0.9442 0.9972 0.5242 0.2405  0.0553  0.0979  156 ILE   B CG2 
1947 C CD1 . ILE   B 147 ? 0.9742 1.0572 0.5399 0.2785  0.0694  0.1077  156 ILE   B CD1 
1948 N N   A LYS   B 148 ? 1.0501 1.1445 0.6632 0.2499  0.0770  0.1247  157 LYS   B N   
1949 N N   B LYS   B 148 ? 1.0501 1.1445 0.6632 0.2499  0.0770  0.1247  157 LYS   B N   
1950 N N   C LYS   B 148 ? 1.0504 1.1450 0.6636 0.2500  0.0771  0.1248  157 LYS   B N   
1951 N N   D LYS   B 148 ? 1.0504 1.1450 0.6636 0.2500  0.0771  0.1248  157 LYS   B N   
1952 C CA  A LYS   B 148 ? 1.0687 1.1809 0.6913 0.2582  0.0845  0.1334  157 LYS   B CA  
1953 C CA  B LYS   B 148 ? 1.0687 1.1809 0.6913 0.2582  0.0845  0.1334  157 LYS   B CA  
1954 C CA  C LYS   B 148 ? 1.0690 1.1812 0.6920 0.2578  0.0847  0.1336  157 LYS   B CA  
1955 C CA  D LYS   B 148 ? 1.0690 1.1812 0.6920 0.2578  0.0847  0.1336  157 LYS   B CA  
1956 C C   A LYS   B 148 ? 1.0804 1.2066 0.7066 0.2661  0.0981  0.1454  157 LYS   B C   
1957 C C   B LYS   B 148 ? 1.0804 1.2066 0.7066 0.2661  0.0981  0.1454  157 LYS   B C   
1958 C C   C LYS   B 148 ? 1.0810 1.2074 0.7072 0.2663  0.0981  0.1454  157 LYS   B C   
1959 C C   D LYS   B 148 ? 1.0810 1.2074 0.7072 0.2663  0.0981  0.1454  157 LYS   B C   
1960 O O   A LYS   B 148 ? 1.0919 1.2298 0.7343 0.2638  0.1073  0.1564  157 LYS   B O   
1961 O O   B LYS   B 148 ? 1.0919 1.2298 0.7343 0.2638  0.1073  0.1564  157 LYS   B O   
1962 O O   C LYS   B 148 ? 1.0938 1.2324 0.7358 0.2645  0.1074  0.1565  157 LYS   B O   
1963 O O   D LYS   B 148 ? 1.0938 1.2324 0.7358 0.2645  0.1074  0.1565  157 LYS   B O   
1964 C CB  A LYS   B 148 ? 1.0853 1.2033 0.6980 0.2732  0.0780  0.1267  157 LYS   B CB  
1965 C CB  B LYS   B 148 ? 1.0853 1.2033 0.6980 0.2732  0.0780  0.1267  157 LYS   B CB  
1966 C CB  C LYS   B 148 ? 1.0862 1.2040 0.7001 0.2722  0.0779  0.1270  157 LYS   B CB  
1967 C CB  D LYS   B 148 ? 1.0862 1.2040 0.7001 0.2722  0.0779  0.1270  157 LYS   B CB  
1968 C CG  A LYS   B 148 ? 1.0845 1.1928 0.6993 0.2666  0.0659  0.1187  157 LYS   B CG  
1969 C CG  B LYS   B 148 ? 1.0845 1.1928 0.6993 0.2666  0.0659  0.1187  157 LYS   B CG  
1970 C CG  C LYS   B 148 ? 1.0899 1.2282 0.7125 0.2826  0.0859  0.1349  157 LYS   B CG  
1971 C CG  D LYS   B 148 ? 1.0899 1.2282 0.7125 0.2826  0.0859  0.1349  157 LYS   B CG  
1972 C CD  A LYS   B 148 ? 1.0934 1.2049 0.6991 0.2821  0.0579  0.1102  157 LYS   B CD  
1973 C CD  B LYS   B 148 ? 1.0934 1.2049 0.6991 0.2821  0.0579  0.1102  157 LYS   B CD  
1974 C CD  C LYS   B 148 ? 1.0858 1.2264 0.7271 0.2709  0.0868  0.1398  157 LYS   B CD  
1975 C CD  D LYS   B 148 ? 1.0858 1.2264 0.7271 0.2709  0.0868  0.1398  157 LYS   B CD  
1976 C CE  A LYS   B 148 ? 1.0966 1.2297 0.7073 0.2966  0.0661  0.1158  157 LYS   B CE  
1977 C CE  B LYS   B 148 ? 1.0966 1.2297 0.7073 0.2966  0.0661  0.1158  157 LYS   B CE  
1978 C CE  C LYS   B 148 ? 1.0848 1.2081 0.7262 0.2576  0.0738  0.1309  157 LYS   B CE  
1979 C CE  D LYS   B 148 ? 1.0848 1.2081 0.7262 0.2576  0.0738  0.1309  157 LYS   B CE  
1980 N NZ  A LYS   B 148 ? 1.0870 1.2258 0.7147 0.2894  0.0671  0.1212  157 LYS   B NZ  
1981 N NZ  B LYS   B 148 ? 1.0870 1.2258 0.7147 0.2894  0.0671  0.1212  157 LYS   B NZ  
1982 N NZ  C LYS   B 148 ? 1.0807 1.2092 0.7382 0.2504  0.0726  0.1342  157 LYS   B NZ  
1983 N NZ  D LYS   B 148 ? 1.0807 1.2092 0.7382 0.2504  0.0726  0.1342  157 LYS   B NZ  
1984 N N   . ASN   B 149 ? 1.0871 1.2120 0.6997 0.2746  0.0987  0.1437  158 ASN   B N   
1985 C CA  . ASN   B 149 ? 1.0886 1.2277 0.7009 0.2850  0.1104  0.1554  158 ASN   B CA  
1986 C C   . ASN   B 149 ? 1.0394 1.1742 0.6659 0.2731  0.1183  0.1650  158 ASN   B C   
1987 O O   . ASN   B 149 ? 1.0573 1.2046 0.6871 0.2808  0.1287  0.1776  158 ASN   B O   
1988 C CB  . ASN   B 149 ? 1.1540 1.2932 0.7454 0.2990  0.1065  0.1490  158 ASN   B CB  
1989 C CG  . ASN   B 149 ? 1.1654 1.2988 0.7423 0.3063  0.0937  0.1335  158 ASN   B CG  
1990 O OD1 . ASN   B 149 ? 1.2236 1.3593 0.8043 0.3069  0.0898  0.1300  158 ASN   B OD1 
1991 N ND2 . ASN   B 149 ? 1.1924 1.3181 0.7540 0.3121  0.0867  0.1242  158 ASN   B ND2 
1992 N N   . GLY   B 150 ? 0.9771 1.0955 0.6111 0.2562  0.1134  0.1592  159 GLY   B N   
1993 C CA  . GLY   B 150 ? 0.8983 1.0109 0.5469 0.2446  0.1196  0.1653  159 GLY   B CA  
1994 C C   . GLY   B 150 ? 0.8641 0.9658 0.5024 0.2445  0.1165  0.1599  159 GLY   B C   
1995 O O   . GLY   B 150 ? 0.8437 0.9376 0.4943 0.2333  0.1193  0.1614  159 GLY   B O   
1996 N N   A SER   B 151 ? 0.8612 0.9632 0.4789 0.2574  0.1109  0.1534  160 SER   B N   
1997 N N   B SER   B 151 ? 0.8697 0.9718 0.4875 0.2574  0.1110  0.1534  160 SER   B N   
1998 N N   C SER   B 151 ? 0.8519 0.9533 0.4696 0.2569  0.1107  0.1530  160 SER   B N   
1999 N N   D SER   B 151 ? 0.8518 0.9532 0.4695 0.2569  0.1107  0.1530  160 SER   B N   
2000 C CA  A SER   B 151 ? 0.8436 0.9354 0.4492 0.2589  0.1057  0.1458  160 SER   B CA  
2001 C CA  B SER   B 151 ? 0.8575 0.9494 0.4629 0.2591  0.1056  0.1457  160 SER   B CA  
2002 C CA  C SER   B 151 ? 0.8249 0.9157 0.4312 0.2577  0.1054  0.1453  160 SER   B CA  
2003 C CA  D SER   B 151 ? 0.8250 0.9157 0.4312 0.2577  0.1054  0.1454  160 SER   B CA  
2004 C C   A SER   B 151 ? 0.8278 0.9022 0.4319 0.2447  0.0955  0.1322  160 SER   B C   
2005 C C   B SER   B 151 ? 0.8368 0.9112 0.4410 0.2446  0.0955  0.1323  160 SER   B C   
2006 C C   C SER   B 151 ? 0.7964 0.8697 0.4030 0.2422  0.0960  0.1325  160 SER   B C   
2007 C C   D SER   B 151 ? 0.7964 0.8697 0.4030 0.2422  0.0960  0.1325  160 SER   B C   
2008 O O   A SER   B 151 ? 0.8208 0.8925 0.4286 0.2372  0.0911  0.1283  160 SER   B O   
2009 O O   B SER   B 151 ? 0.8294 0.9009 0.4375 0.2369  0.0912  0.1284  160 SER   B O   
2010 O O   C SER   B 151 ? 0.7884 0.8591 0.4012 0.2331  0.0929  0.1298  160 SER   B O   
2011 O O   D SER   B 151 ? 0.7884 0.8591 0.4012 0.2331  0.0929  0.1298  160 SER   B O   
2012 C CB  A SER   B 151 ? 0.8527 0.9518 0.4380 0.2773  0.1020  0.1420  160 SER   B CB  
2013 C CB  B SER   B 151 ? 0.8742 0.9733 0.4593 0.2773  0.1017  0.1416  160 SER   B CB  
2014 C CB  C SER   B 151 ? 0.8375 0.9340 0.4231 0.2751  0.1006  0.1402  160 SER   B CB  
2015 C CB  D SER   B 151 ? 0.8375 0.9341 0.4231 0.2751  0.1006  0.1402  160 SER   B CB  
2016 O OG  A SER   B 151 ? 0.8409 0.9327 0.4170 0.2796  0.0983  0.1369  160 SER   B OG  
2017 O OG  B SER   B 151 ? 0.8789 0.9799 0.4573 0.2817  0.0949  0.1341  160 SER   B OG  
2018 O OG  C SER   B 151 ? 0.8364 0.9342 0.4154 0.2790  0.0937  0.1327  160 SER   B OG  
2019 O OG  D SER   B 151 ? 0.8365 0.9343 0.4155 0.2790  0.0937  0.1327  160 SER   B OG  
2020 N N   A TYR   B 152 ? 0.8147 0.8791 0.4137 0.2414  0.0919  0.1259  161 TYR   B N   
2021 N N   B TYR   B 152 ? 0.8180 0.8824 0.4170 0.2414  0.0919  0.1259  161 TYR   B N   
2022 N N   C TYR   B 152 ? 0.7718 0.8349 0.3721 0.2394  0.0918  0.1255  161 TYR   B N   
2023 N N   D TYR   B 152 ? 0.7718 0.8349 0.3721 0.2395  0.0918  0.1255  161 TYR   B N   
2024 C CA  A TYR   B 152 ? 0.7982 0.8473 0.3955 0.2278  0.0831  0.1137  161 TYR   B CA  
2025 C CA  B TYR   B 152 ? 0.7995 0.8486 0.3968 0.2278  0.0831  0.1137  161 TYR   B CA  
2026 C CA  C TYR   B 152 ? 0.7482 0.7962 0.3465 0.2260  0.0829  0.1132  161 TYR   B CA  
2027 C CA  D TYR   B 152 ? 0.7482 0.7962 0.3465 0.2260  0.0829  0.1132  161 TYR   B CA  
2028 C C   A TYR   B 152 ? 0.7715 0.8153 0.3508 0.2358  0.0723  0.1027  161 TYR   B C   
2029 C C   B TYR   B 152 ? 0.7719 0.8157 0.3512 0.2358  0.0724  0.1027  161 TYR   B C   
2030 C C   C TYR   B 152 ? 0.7436 0.7865 0.3237 0.2344  0.0725  0.1025  161 TYR   B C   
2031 C C   D TYR   B 152 ? 0.7436 0.7865 0.3237 0.2344  0.0725  0.1025  161 TYR   B C   
2032 O O   A TYR   B 152 ? 0.7706 0.8195 0.3395 0.2499  0.0724  0.1029  161 TYR   B O   
2033 O O   B TYR   B 152 ? 0.7711 0.8200 0.3400 0.2499  0.0724  0.1029  161 TYR   B O   
2034 O O   C TYR   B 152 ? 0.7413 0.7885 0.3118 0.2475  0.0728  0.1028  161 TYR   B O   
2035 O O   D TYR   B 152 ? 0.7414 0.7886 0.3119 0.2475  0.0728  0.1028  161 TYR   B O   
2036 C CB  A TYR   B 152 ? 0.8139 0.8563 0.4203 0.2183  0.0867  0.1135  161 TYR   B CB  
2037 C CB  B TYR   B 152 ? 0.8144 0.8568 0.4209 0.2183  0.0867  0.1135  161 TYR   B CB  
2038 C CB  C TYR   B 152 ? 0.7366 0.7776 0.3450 0.2150  0.0863  0.1127  161 TYR   B CB  
2039 C CB  D TYR   B 152 ? 0.7366 0.7776 0.3451 0.2151  0.0863  0.1127  161 TYR   B CB  
2040 C CG  A TYR   B 152 ? 0.8285 0.8584 0.4363 0.2025  0.0800  0.1025  161 TYR   B CG  
2041 C CG  B TYR   B 152 ? 0.8285 0.8585 0.4364 0.2025  0.0800  0.1025  161 TYR   B CG  
2042 C CG  C TYR   B 152 ? 0.7240 0.7534 0.3356 0.1981  0.0804  0.1025  161 TYR   B CG  
2043 C CG  D TYR   B 152 ? 0.7241 0.7534 0.3357 0.1981  0.0804  0.1025  161 TYR   B CG  
2044 C CD1 A TYR   B 152 ? 0.8293 0.8572 0.4492 0.1878  0.0810  0.1019  161 TYR   B CD1 
2045 C CD1 B TYR   B 152 ? 0.8292 0.8571 0.4491 0.1878  0.0810  0.1019  161 TYR   B CD1 
2046 C CD1 C TYR   B 152 ? 0.7171 0.7460 0.3418 0.1845  0.0824  0.1032  161 TYR   B CD1 
2047 C CD1 D TYR   B 152 ? 0.7171 0.7460 0.3418 0.1845  0.0824  0.1032  161 TYR   B CD1 
2048 C CD2 A TYR   B 152 ? 0.8411 0.8627 0.4385 0.2022  0.0729  0.0928  161 TYR   B CD2 
2049 C CD2 B TYR   B 152 ? 0.8408 0.8624 0.4383 0.2022  0.0729  0.0928  161 TYR   B CD2 
2050 C CD2 C TYR   B 152 ? 0.7197 0.7399 0.3220 0.1954  0.0733  0.0923  161 TYR   B CD2 
2051 C CD2 D TYR   B 152 ? 0.7197 0.7399 0.3221 0.1954  0.0733  0.0924  161 TYR   B CD2 
2052 C CE1 A TYR   B 152 ? 0.8328 0.8518 0.4529 0.1735  0.0754  0.0922  161 TYR   B CE1 
2053 C CE1 B TYR   B 152 ? 0.8327 0.8516 0.4527 0.1735  0.0754  0.0922  161 TYR   B CE1 
2054 C CE1 C TYR   B 152 ? 0.7072 0.7279 0.3335 0.1692  0.0774  0.0942  161 TYR   B CE1 
2055 C CE1 D TYR   B 152 ? 0.7072 0.7280 0.3336 0.1692  0.0774  0.0942  161 TYR   B CE1 
2056 C CE2 A TYR   B 152 ? 0.8422 0.8544 0.4411 0.1876  0.0676  0.0837  161 TYR   B CE2 
2057 C CE2 B TYR   B 152 ? 0.8419 0.8541 0.4409 0.1876  0.0676  0.0837  161 TYR   B CE2 
2058 C CE2 C TYR   B 152 ? 0.7079 0.7197 0.3130 0.1798  0.0688  0.0840  161 TYR   B CE2 
2059 C CE2 D TYR   B 152 ? 0.7080 0.7198 0.3131 0.1798  0.0688  0.0840  161 TYR   B CE2 
2060 C CZ  A TYR   B 152 ? 0.8372 0.8485 0.4467 0.1732  0.0691  0.0836  161 TYR   B CZ  
2061 C CZ  B TYR   B 152 ? 0.8370 0.8483 0.4464 0.1732  0.0691  0.0836  161 TYR   B CZ  
2062 C CZ  C TYR   B 152 ? 0.7058 0.7183 0.3220 0.1668  0.0709  0.0849  161 TYR   B CZ  
2063 C CZ  D TYR   B 152 ? 0.7058 0.7183 0.3220 0.1668  0.0709  0.0849  161 TYR   B CZ  
2064 O OH  A TYR   B 152 ? 0.8489 0.8532 0.4586 0.1590  0.0644  0.0750  161 TYR   B OH  
2065 O OH  B TYR   B 152 ? 0.8481 0.8525 0.4578 0.1590  0.0644  0.0750  161 TYR   B OH  
2066 O OH  C TYR   B 152 ? 0.6891 0.6958 0.3070 0.1515  0.0668  0.0769  161 TYR   B OH  
2067 O OH  D TYR   B 152 ? 0.6893 0.6960 0.3072 0.1515  0.0668  0.0769  161 TYR   B OH  
2068 N N   . VAL   B 153 ? 0.7352 0.7696 0.3116 0.2272  0.0631  0.0938  162 VAL   B N   
2069 C CA  . VAL   B 153 ? 0.6930 0.7198 0.2559 0.2320  0.0516  0.0826  162 VAL   B CA  
2070 C C   . VAL   B 153 ? 0.6585 0.6725 0.2245 0.2152  0.0465  0.0757  162 VAL   B C   
2071 O O   . VAL   B 153 ? 0.6535 0.6644 0.2268 0.2020  0.0458  0.0762  162 VAL   B O   
2072 C CB  . VAL   B 153 ? 0.6741 0.7021 0.2315 0.2387  0.0443  0.0791  162 VAL   B CB  
2073 C CG1 . VAL   B 153 ? 0.6628 0.6803 0.2104 0.2405  0.0316  0.0671  162 VAL   B CG1 
2074 C CG2 . VAL   B 153 ? 0.6951 0.7383 0.2484 0.2567  0.0498  0.0848  162 VAL   B CG2 
2075 N N   A SER   B 154 ? 0.6597 0.6679 0.2204 0.2159  0.0431  0.0695  163 SER   B N   
2076 N N   B SER   B 154 ? 0.6595 0.6677 0.2202 0.2159  0.0431  0.0695  163 SER   B N   
2077 N N   C SER   B 154 ? 0.6491 0.6569 0.2089 0.2164  0.0422  0.0689  163 SER   B N   
2078 N N   D SER   B 154 ? 0.6490 0.6569 0.2088 0.2164  0.0422  0.0689  163 SER   B N   
2079 C CA  A SER   B 154 ? 0.6439 0.6417 0.2073 0.2008  0.0391  0.0627  163 SER   B CA  
2080 C CA  B SER   B 154 ? 0.6439 0.6417 0.2073 0.2008  0.0391  0.0627  163 SER   B CA  
2081 C CA  C SER   B 154 ? 0.6247 0.6226 0.1877 0.2014  0.0389  0.0626  163 SER   B CA  
2082 C CA  D SER   B 154 ? 0.6247 0.6226 0.1877 0.2014  0.0389  0.0626  163 SER   B CA  
2083 C C   A SER   B 154 ? 0.6406 0.6299 0.1963 0.1994  0.0267  0.0540  163 SER   B C   
2084 C C   B SER   B 154 ? 0.6405 0.6297 0.1962 0.1992  0.0267  0.0540  163 SER   B C   
2085 C C   C SER   B 154 ? 0.6152 0.6044 0.1702 0.2004  0.0265  0.0534  163 SER   B C   
2086 C C   D SER   B 154 ? 0.6152 0.6043 0.1702 0.2004  0.0265  0.0534  163 SER   B C   
2087 O O   A SER   B 154 ? 0.6412 0.6316 0.1889 0.2126  0.0209  0.0512  163 SER   B O   
2088 O O   B SER   B 154 ? 0.6415 0.6318 0.1893 0.2124  0.0209  0.0512  163 SER   B O   
2089 O O   C SER   B 154 ? 0.6147 0.6039 0.1608 0.2138  0.0208  0.0488  163 SER   B O   
2090 O O   D SER   B 154 ? 0.6148 0.6040 0.1609 0.2138  0.0208  0.0488  163 SER   B O   
2091 C CB  A SER   B 154 ? 0.6492 0.6464 0.2136 0.2024  0.0425  0.0611  163 SER   B CB  
2092 C CB  B SER   B 154 ? 0.6490 0.6462 0.2134 0.2024  0.0425  0.0611  163 SER   B CB  
2093 C CB  C SER   B 154 ? 0.6313 0.6295 0.1961 0.2032  0.0434  0.0621  163 SER   B CB  
2094 C CB  D SER   B 154 ? 0.6312 0.6294 0.1960 0.2032  0.0434  0.0621  163 SER   B CB  
2095 O OG  A SER   B 154 ? 0.6400 0.6286 0.2069 0.1884  0.0384  0.0535  163 SER   B OG  
2096 O OG  B SER   B 154 ? 0.6400 0.6286 0.2069 0.1884  0.0384  0.0535  163 SER   B OG  
2097 O OG  C SER   B 154 ? 0.6177 0.6078 0.1866 0.1885  0.0407  0.0554  163 SER   B OG  
2098 O OG  D SER   B 154 ? 0.6177 0.6078 0.1866 0.1885  0.0408  0.0554  163 SER   B OG  
2099 N N   A ALA   B 155 ? 0.6209 0.6025 0.1797 0.1838  0.0228  0.0498  164 ALA   B N   
2100 N N   B ALA   B 155 ? 0.6212 0.6027 0.1800 0.1837  0.0229  0.0498  164 ALA   B N   
2101 N N   C ALA   B 155 ? 0.5924 0.5745 0.1507 0.1850  0.0220  0.0506  164 ALA   B N   
2102 N N   D ALA   B 155 ? 0.5925 0.5746 0.1508 0.1850  0.0220  0.0506  164 ALA   B N   
2103 C CA  A ALA   B 155 ? 0.6226 0.5949 0.1760 0.1811  0.0114  0.0418  164 ALA   B CA  
2104 C CA  B ALA   B 155 ? 0.6226 0.5950 0.1761 0.1809  0.0115  0.0418  164 ALA   B CA  
2105 C CA  C ALA   B 155 ? 0.5866 0.5593 0.1400 0.1815  0.0112  0.0423  164 ALA   B CA  
2106 C CA  D ALA   B 155 ? 0.5867 0.5593 0.1400 0.1815  0.0112  0.0423  164 ALA   B CA  
2107 C C   A ALA   B 155 ? 0.6251 0.5958 0.1755 0.1868  0.0105  0.0359  164 ALA   B C   
2108 C C   B ALA   B 155 ? 0.6251 0.5957 0.1755 0.1867  0.0105  0.0359  164 ALA   B C   
2109 C C   C ALA   B 155 ? 0.5960 0.5675 0.1469 0.1865  0.0114  0.0374  164 ALA   B C   
2110 C C   D ALA   B 155 ? 0.5960 0.5676 0.1469 0.1865  0.0114  0.0374  164 ALA   B C   
2111 O O   A ALA   B 155 ? 0.6357 0.6108 0.1918 0.1836  0.0200  0.0392  164 ALA   B O   
2112 O O   B ALA   B 155 ? 0.6349 0.6098 0.1909 0.1835  0.0199  0.0391  164 ALA   B O   
2113 O O   C ALA   B 155 ? 0.6110 0.5878 0.1666 0.1860  0.0207  0.0415  164 ALA   B O   
2114 O O   D ALA   B 155 ? 0.6108 0.5876 0.1664 0.1860  0.0207  0.0415  164 ALA   B O   
2115 C CB  A ALA   B 155 ? 0.6175 0.5848 0.1756 0.1616  0.0089  0.0411  164 ALA   B CB  
2116 C CB  B ALA   B 155 ? 0.6176 0.5849 0.1758 0.1614  0.0089  0.0412  164 ALA   B CB  
2117 C CB  C ALA   B 155 ? 0.5801 0.5475 0.1384 0.1614  0.0093  0.0412  164 ALA   B CB  
2118 C CB  D ALA   B 155 ? 0.5801 0.5476 0.1384 0.1614  0.0093  0.0413  164 ALA   B CB  
2119 N N   A ILE   B 156 ? 0.6287 0.5907 0.1753 0.1861  -0.0015 0.0279  165 ILE   B N   
2120 N N   B ILE   B 156 ? 0.6287 0.5906 0.1753 0.1860  -0.0015 0.0279  165 ILE   B N   
2121 N N   C ILE   B 156 ? 0.6025 0.5653 0.1483 0.1884  -0.0015 0.0285  165 ILE   B N   
2122 N N   D ILE   B 156 ? 0.6025 0.5653 0.1483 0.1884  -0.0015 0.0285  165 ILE   B N   
2123 C CA  A ILE   B 156 ? 0.6271 0.5850 0.1737 0.1845  -0.0048 0.0208  165 ILE   B CA  
2124 C CA  B ILE   B 156 ? 0.6271 0.5850 0.1737 0.1844  -0.0048 0.0208  165 ILE   B CA  
2125 C CA  C ILE   B 156 ? 0.6018 0.5605 0.1481 0.1855  -0.0043 0.0218  165 ILE   B CA  
2126 C CA  D ILE   B 156 ? 0.6018 0.5605 0.1481 0.1855  -0.0043 0.0218  165 ILE   B CA  
2127 C C   A ILE   B 156 ? 0.6142 0.5671 0.1667 0.1650  -0.0060 0.0196  165 ILE   B C   
2128 C C   B ILE   B 156 ? 0.6143 0.5672 0.1668 0.1650  -0.0060 0.0196  165 ILE   B C   
2129 C C   C ILE   B 156 ? 0.5912 0.5448 0.1433 0.1658  -0.0054 0.0212  165 ILE   B C   
2130 C C   D ILE   B 156 ? 0.5913 0.5449 0.1434 0.1658  -0.0055 0.0212  165 ILE   B C   
2131 O O   A ILE   B 156 ? 0.6162 0.5619 0.1687 0.1595  -0.0155 0.0158  165 ILE   B O   
2132 O O   B ILE   B 156 ? 0.6163 0.5620 0.1688 0.1596  -0.0155 0.0158  165 ILE   B O   
2133 O O   C ILE   B 156 ? 0.5960 0.5433 0.1479 0.1600  -0.0141 0.0199  165 ILE   B O   
2134 O O   D ILE   B 156 ? 0.5961 0.5433 0.1480 0.1600  -0.0141 0.0198  165 ILE   B O   
2135 C CB  A ILE   B 156 ? 0.6404 0.5943 0.1811 0.1972  -0.0159 0.0131  165 ILE   B CB  
2136 C CB  B ILE   B 156 ? 0.6403 0.5942 0.1810 0.1972  -0.0159 0.0131  165 ILE   B CB  
2137 C CB  C ILE   B 156 ? 0.6152 0.5694 0.1558 0.1973  -0.0155 0.0137  165 ILE   B CB  
2138 C CB  D ILE   B 156 ? 0.6152 0.5694 0.1558 0.1973  -0.0155 0.0137  165 ILE   B CB  
2139 C CG1 A ILE   B 156 ? 0.6513 0.6133 0.1849 0.2164  -0.0138 0.0147  165 ILE   B CG1 
2140 C CG1 B ILE   B 156 ? 0.6511 0.6131 0.1847 0.2164  -0.0138 0.0147  165 ILE   B CG1 
2141 C CG1 C ILE   B 156 ? 0.6268 0.5888 0.1601 0.2171  -0.0142 0.0146  165 ILE   B CG1 
2142 C CG1 D ILE   B 156 ? 0.6268 0.5888 0.1601 0.2170  -0.0142 0.0146  165 ILE   B CG1 
2143 C CG2 A ILE   B 156 ? 0.6417 0.5925 0.1837 0.1964  -0.0196 0.0056  165 ILE   B CG2 
2144 C CG2 B ILE   B 156 ? 0.6416 0.5924 0.1836 0.1963  -0.0195 0.0056  165 ILE   B CG2 
2145 C CG2 C ILE   B 156 ? 0.6169 0.5679 0.1592 0.1953  -0.0188 0.0065  165 ILE   B CG2 
2146 C CG2 D ILE   B 156 ? 0.6169 0.5679 0.1592 0.1953  -0.0188 0.0065  165 ILE   B CG2 
2147 C CD1 A ILE   B 156 ? 0.6642 0.6241 0.1918 0.2305  -0.0248 0.0056  165 ILE   B CD1 
2148 C CD1 B ILE   B 156 ? 0.6640 0.6239 0.1916 0.2305  -0.0248 0.0056  165 ILE   B CD1 
2149 C CD1 C ILE   B 156 ? 0.6399 0.5988 0.1679 0.2298  -0.0258 0.0052  165 ILE   B CD1 
2150 C CD1 D ILE   B 156 ? 0.6399 0.5988 0.1678 0.2298  -0.0258 0.0052  165 ILE   B CD1 
2151 N N   A THR   B 157 ? 0.6030 0.5603 0.1611 0.1549  0.0034  0.0230  166 THR   B N   
2152 N N   B THR   B 157 ? 0.6029 0.5602 0.1611 0.1548  0.0034  0.0230  166 THR   B N   
2153 N N   C THR   B 157 ? 0.5851 0.5422 0.1428 0.1565  0.0029  0.0224  166 THR   B N   
2154 N N   D THR   B 157 ? 0.5852 0.5423 0.1429 0.1564  0.0029  0.0224  166 THR   B N   
2155 C CA  A THR   B 157 ? 0.5934 0.5492 0.1566 0.1363  0.0040  0.0215  166 THR   B CA  
2156 C CA  B THR   B 157 ? 0.5935 0.5494 0.1567 0.1362  0.0040  0.0215  166 THR   B CA  
2157 C CA  C THR   B 157 ? 0.5809 0.5365 0.1436 0.1375  0.0036  0.0215  166 THR   B CA  
2158 C CA  D THR   B 157 ? 0.5809 0.5366 0.1436 0.1375  0.0036  0.0215  166 THR   B CA  
2159 C C   A THR   B 157 ? 0.5940 0.5463 0.1585 0.1337  -0.0002 0.0142  166 THR   B C   
2160 C C   B THR   B 157 ? 0.5940 0.5464 0.1586 0.1337  -0.0002 0.0142  166 THR   B C   
2161 C C   C THR   B 157 ? 0.5894 0.5420 0.1540 0.1340  0.0001  0.0142  166 THR   B C   
2162 C C   D THR   B 157 ? 0.5894 0.5420 0.1540 0.1340  0.0001  0.0142  166 THR   B C   
2163 O O   A THR   B 157 ? 0.5937 0.5488 0.1602 0.1407  0.0040  0.0113  166 THR   B O   
2164 O O   B THR   B 157 ? 0.5939 0.5490 0.1604 0.1406  0.0041  0.0113  166 THR   B O   
2165 O O   C THR   B 157 ? 0.5960 0.5521 0.1643 0.1367  0.0061  0.0117  166 THR   B O   
2166 O O   D THR   B 157 ? 0.5959 0.5520 0.1642 0.1367  0.0061  0.0117  166 THR   B O   
2167 C CB  A THR   B 157 ? 0.5884 0.5509 0.1584 0.1280  0.0151  0.0245  166 THR   B CB  
2168 C CB  B THR   B 157 ? 0.5883 0.5508 0.1583 0.1279  0.0151  0.0245  166 THR   B CB  
2169 C CB  C THR   B 157 ? 0.5753 0.5377 0.1445 0.1298  0.0147  0.0253  166 THR   B CB  
2170 C CB  D THR   B 157 ? 0.5753 0.5378 0.1445 0.1298  0.0147  0.0253  166 THR   B CB  
2171 O OG1 A THR   B 157 ? 0.5863 0.5529 0.1562 0.1353  0.0193  0.0318  166 THR   B OG1 
2172 O OG1 B THR   B 157 ? 0.5863 0.5528 0.1560 0.1350  0.0191  0.0318  166 THR   B OG1 
2173 O OG1 C THR   B 157 ? 0.5759 0.5418 0.1441 0.1365  0.0175  0.0326  166 THR   B OG1 
2174 O OG1 D THR   B 157 ? 0.5758 0.5418 0.1441 0.1365  0.0175  0.0326  166 THR   B OG1 
2175 C CG2 A THR   B 157 ? 0.5824 0.5458 0.1560 0.1093  0.0155  0.0221  166 THR   B CG2 
2176 C CG2 B THR   B 157 ? 0.5824 0.5458 0.1560 0.1092  0.0155  0.0221  166 THR   B CG2 
2177 C CG2 C THR   B 157 ? 0.5662 0.5296 0.1395 0.1108  0.0156  0.0227  166 THR   B CG2 
2178 C CG2 D THR   B 157 ? 0.5663 0.5297 0.1396 0.1108  0.0155  0.0227  166 THR   B CG2 
2179 N N   . GLN   B 158 ? 0.5971 0.5439 0.1616 0.1243  -0.0086 0.0120  167 GLN   B N   
2180 C CA  . GLN   B 158 ? 0.5896 0.5339 0.1578 0.1182  -0.0125 0.0057  167 GLN   B CA  
2181 C C   . GLN   B 158 ? 0.5909 0.5373 0.1627 0.0986  -0.0113 0.0074  167 GLN   B C   
2182 O O   . GLN   B 158 ? 0.5805 0.5259 0.1500 0.0921  -0.0138 0.0129  167 GLN   B O   
2183 C CB  . GLN   B 158 ? 0.5953 0.5319 0.1617 0.1273  -0.0245 0.0014  167 GLN   B CB  
2184 C CG  . GLN   B 158 ? 0.5891 0.5232 0.1611 0.1226  -0.0296 -0.0052 167 GLN   B CG  
2185 C CD  . GLN   B 158 ? 0.5929 0.5324 0.1675 0.1270  -0.0231 -0.0099 167 GLN   B CD  
2186 O OE1 . GLN   B 158 ? 0.5785 0.5244 0.1560 0.1204  -0.0132 -0.0082 167 GLN   B OE1 
2187 N NE2 . GLN   B 158 ? 0.5801 0.5175 0.1541 0.1399  -0.0291 -0.0160 167 GLN   B NE2 
2188 N N   . GLY   B 159 ? 0.5897 0.5397 0.1668 0.0904  -0.0081 0.0027  168 GLY   B N   
2189 C CA  . GLY   B 159 ? 0.6133 0.5676 0.1932 0.0721  -0.0069 0.0035  168 GLY   B CA  
2190 C C   . GLY   B 159 ? 0.6531 0.6021 0.2354 0.0668  -0.0164 0.0026  168 GLY   B C   
2191 O O   . GLY   B 159 ? 0.6446 0.5860 0.2271 0.0761  -0.0246 0.0006  168 GLY   B O   
2192 N N   . LYS   B 160 ? 0.6992 0.6528 0.2836 0.0508  -0.0160 0.0048  169 LYS   B N   
2193 C CA  . LYS   B 160 ? 0.7699 0.7192 0.3590 0.0442  -0.0248 0.0054  169 LYS   B CA  
2194 C C   . LYS   B 160 ? 0.8083 0.7645 0.4048 0.0384  -0.0201 -0.0013 169 LYS   B C   
2195 O O   . LYS   B 160 ? 0.7880 0.7551 0.3850 0.0315  -0.0098 -0.0036 169 LYS   B O   
2196 C CB  . LYS   B 160 ? 0.8192 0.7703 0.4059 0.0302  -0.0275 0.0145  169 LYS   B CB  
2197 C CG  . LYS   B 160 ? 0.8739 0.8201 0.4667 0.0221  -0.0369 0.0181  169 LYS   B CG  
2198 C CD  . LYS   B 160 ? 0.9032 0.8541 0.4938 0.0065  -0.0382 0.0285  169 LYS   B CD  
2199 C CE  . LYS   B 160 ? 0.9294 0.8793 0.5287 -0.0041 -0.0444 0.0321  169 LYS   B CE  
2200 N NZ  . LYS   B 160 ? 0.9817 0.9394 0.5782 -0.0205 -0.0441 0.0434  169 LYS   B NZ  
2201 N N   . ARG   B 161 ? 0.8472 0.7983 0.4506 0.0405  -0.0276 -0.0050 170 ARG   B N   
2202 C CA  . ARG   B 161 ? 0.8902 0.8479 0.5029 0.0344  -0.0248 -0.0113 170 ARG   B CA  
2203 C C   . ARG   B 161 ? 0.9568 0.9176 0.5748 0.0179  -0.0283 -0.0058 170 ARG   B C   
2204 O O   . ARG   B 161 ? 0.9724 0.9233 0.5930 0.0183  -0.0391 -0.0014 170 ARG   B O   
2205 C CB  . ARG   B 161 ? 0.9149 0.8658 0.5327 0.0486  -0.0312 -0.0191 170 ARG   B CB  
2206 C CG  . ARG   B 161 ? 0.9194 0.8774 0.5474 0.0452  -0.0281 -0.0267 170 ARG   B CG  
2207 C CD  . ARG   B 161 ? 0.9432 0.8944 0.5773 0.0577  -0.0372 -0.0340 170 ARG   B CD  
2208 N NE  . ARG   B 161 ? 0.9613 0.9196 0.6075 0.0518  -0.0357 -0.0403 170 ARG   B NE  
2209 C CZ  . ARG   B 161 ? 0.9721 0.9348 0.6227 0.0600  -0.0324 -0.0483 170 ARG   B CZ  
2210 N NH1 . ARG   B 161 ? 0.9344 0.8950 0.5779 0.0751  -0.0304 -0.0503 170 ARG   B NH1 
2211 N NH2 . ARG   B 161 ? 1.0106 0.9805 0.6737 0.0530  -0.0314 -0.0536 170 ARG   B NH2 
2212 N N   . GLU   B 162 ? 1.0009 0.9753 0.6208 0.0038  -0.0196 -0.0056 171 GLU   B N   
2213 C CA  . GLU   B 162 ? 1.0519 1.0328 0.6776 -0.0126 -0.0212 0.0000  171 GLU   B CA  
2214 C C   . GLU   B 162 ? 1.0429 1.0258 0.6817 -0.0132 -0.0229 -0.0069 171 GLU   B C   
2215 O O   . GLU   B 162 ? 1.1110 1.0898 0.7585 -0.0189 -0.0310 -0.0029 171 GLU   B O   
2216 C CB  . GLU   B 162 ? 1.0929 1.0902 0.7130 -0.0266 -0.0106 0.0027  171 GLU   B CB  
2217 C CG  . GLU   B 162 ? 1.1361 1.1324 0.7443 -0.0279 -0.0103 0.0104  171 GLU   B CG  
2218 C CD  . GLU   B 162 ? 1.1815 1.1787 0.7871 -0.0403 -0.0161 0.0232  171 GLU   B CD  
2219 O OE1 . GLU   B 162 ? 1.2195 1.2265 0.8165 -0.0488 -0.0115 0.0284  171 GLU   B OE1 
2220 O OE2 . GLU   B 162 ? 1.1994 1.1877 0.8125 -0.0415 -0.0257 0.0281  171 GLU   B OE2 
2221 S S   C DMS   C .   ? 1.3827 1.3799 1.1462 0.2396  0.1025  0.1213  101 DMS   A S   
2222 S S   D DMS   C .   ? 1.3827 1.3799 1.1462 0.2396  0.1025  0.1213  101 DMS   A S   
2223 O O   C DMS   C .   ? 1.3759 1.3798 1.1380 0.2489  0.1082  0.1433  101 DMS   A O   
2224 O O   D DMS   C .   ? 1.3759 1.3798 1.1380 0.2489  0.1082  0.1433  101 DMS   A O   
2225 C C1  C DMS   C .   ? 1.3639 1.3603 1.1399 0.2482  0.0986  0.1222  101 DMS   A C1  
2226 C C1  D DMS   C .   ? 1.3639 1.3603 1.1399 0.2482  0.0986  0.1222  101 DMS   A C1  
2227 C C2  C DMS   C .   ? 1.3394 1.3279 1.1351 0.2218  0.1082  0.1128  101 DMS   A C2  
2228 C C2  D DMS   C .   ? 1.3394 1.3279 1.1351 0.2218  0.1082  0.1128  101 DMS   A C2  
2229 S S   A DMS   D .   ? 0.9246 0.9480 0.5734 0.1860  0.0982  0.1088  201 DMS   B S   
2230 S S   B DMS   D .   ? 0.9249 0.9483 0.5737 0.1861  0.0982  0.1089  201 DMS   B S   
2231 O O   A DMS   D .   ? 0.9354 0.9682 0.5835 0.1934  0.1015  0.1187  201 DMS   B O   
2232 O O   B DMS   D .   ? 0.9354 0.9682 0.5834 0.1934  0.1014  0.1186  201 DMS   B O   
2233 C C1  A DMS   D .   ? 0.9277 0.9437 0.5776 0.1677  0.0919  0.0958  201 DMS   B C1  
2234 C C1  B DMS   D .   ? 0.9275 0.9435 0.5773 0.1677  0.0919  0.0959  201 DMS   B C1  
2235 C C2  A DMS   D .   ? 0.9356 0.9556 0.5604 0.1965  0.0888  0.1005  201 DMS   B C2  
2236 C C2  B DMS   D .   ? 0.9355 0.9555 0.5604 0.1965  0.0888  0.1005  201 DMS   B C2  
2237 S S   A DMS   E .   ? 5.3199 5.3822 5.0649 -0.0028 0.1022  -0.0897 202 DMS   B S   
2238 S S   B DMS   E .   ? 5.3199 5.3822 5.0649 -0.0028 0.1022  -0.0897 202 DMS   B S   
2239 O O   A DMS   E .   ? 5.2640 5.3239 4.9883 -0.0010 0.0986  -0.0826 202 DMS   B O   
2240 O O   B DMS   E .   ? 5.2640 5.3239 4.9883 -0.0010 0.0986  -0.0826 202 DMS   B O   
2241 C C1  A DMS   E .   ? 5.2663 5.3291 5.0364 0.0002  0.1079  -0.1032 202 DMS   B C1  
2242 C C1  B DMS   E .   ? 5.2663 5.3291 5.0364 0.0002  0.1079  -0.1032 202 DMS   B C1  
2243 C C2  A DMS   E .   ? 5.1587 5.2056 4.9140 0.0100  0.1024  -0.0737 202 DMS   B C2  
2244 C C2  B DMS   E .   ? 5.1587 5.2056 4.9140 0.0100  0.1024  -0.0737 202 DMS   B C2  
2245 S S   A DMS   F .   ? 1.5252 1.5343 1.1707 0.1368  0.0791  0.0774  203 DMS   B S   
2246 S S   B DMS   F .   ? 1.5241 1.5333 1.1696 0.1368  0.0791  0.0774  203 DMS   B S   
2247 O O   A DMS   F .   ? 1.4954 1.5054 1.1312 0.1363  0.0725  0.0776  203 DMS   B O   
2248 O O   B DMS   F .   ? 1.4957 1.5056 1.1315 0.1363  0.0725  0.0776  203 DMS   B O   
2249 C C1  A DMS   F .   ? 1.5144 1.5192 1.1643 0.1193  0.0771  0.0652  203 DMS   B C1  
2250 C C1  B DMS   F .   ? 1.5138 1.5186 1.1637 0.1193  0.0771  0.0652  203 DMS   B C1  
2251 C C2  A DMS   F .   ? 1.5155 1.5313 1.1842 0.1335  0.0889  0.0856  203 DMS   B C2  
2252 C C2  B DMS   F .   ? 1.5150 1.5308 1.1837 0.1335  0.0889  0.0855  203 DMS   B C2  
2253 N N1  C A1BG4 G .   ? 0.7960 0.8427 0.5106 0.1599  0.1171  0.1339  204 A1BG4 B N1  
2254 N N1  D A1BG4 G .   ? 0.7959 0.8426 0.5105 0.1599  0.1171  0.1339  204 A1BG4 B N1  
2255 N N3  C A1BG4 G .   ? 0.6924 0.6966 0.3453 0.0999  0.0744  0.0533  204 A1BG4 B N3  
2256 N N3  D A1BG4 G .   ? 0.6924 0.6966 0.3453 0.0999  0.0744  0.0533  204 A1BG4 B N3  
2257 C C4  C A1BG4 G .   ? 0.7782 0.8047 0.4460 0.1605  0.0978  0.1067  204 A1BG4 B C4  
2258 C C4  D A1BG4 G .   ? 0.7780 0.8046 0.4459 0.1605  0.0978  0.1067  204 A1BG4 B C4  
2259 C C5  C A1BG4 G .   ? 0.7672 0.7943 0.4329 0.1713  0.1012  0.1114  204 A1BG4 B C5  
2260 C C5  D A1BG4 G .   ? 0.7672 0.7943 0.4328 0.1713  0.1012  0.1114  204 A1BG4 B C5  
2261 C C6  C A1BG4 G .   ? 0.7522 0.7730 0.4025 0.1756  0.0952  0.1033  204 A1BG4 B C6  
2262 C C6  D A1BG4 G .   ? 0.7521 0.7730 0.4025 0.1756  0.0952  0.1033  204 A1BG4 B C6  
2263 C C7  C A1BG4 G .   ? 0.7529 0.7776 0.3899 0.1917  0.0944  0.1077  204 A1BG4 B C7  
2264 C C7  D A1BG4 G .   ? 0.7529 0.7776 0.3899 0.1917  0.0944  0.1077  204 A1BG4 B C7  
2265 C C8  C A1BG4 G .   ? 0.7517 0.7714 0.3757 0.1964  0.0882  0.0999  204 A1BG4 B C8  
2266 C C8  D A1BG4 G .   ? 0.7517 0.7714 0.3757 0.1965  0.0882  0.0999  204 A1BG4 B C8  
2267 C C10 C A1BG4 G .   ? 0.7327 0.7405 0.3689 0.1690  0.0846  0.0843  204 A1BG4 B C10 
2268 C C10 D A1BG4 G .   ? 0.7327 0.7406 0.3689 0.1690  0.0846  0.0843  204 A1BG4 B C10 
2269 C C13 C A1BG4 G .   ? 0.6958 0.7005 0.3518 0.1228  0.0811  0.0666  204 A1BG4 B C13 
2270 C C13 D A1BG4 G .   ? 0.6958 0.7005 0.3518 0.1228  0.0811  0.0666  204 A1BG4 B C13 
2271 C C15 C A1BG4 G .   ? 0.6823 0.6934 0.3675 0.0859  0.0844  0.0501  204 A1BG4 B C15 
2272 C C15 D A1BG4 G .   ? 0.6823 0.6934 0.3675 0.0859  0.0844  0.0501  204 A1BG4 B C15 
2273 C C17 C A1BG4 G .   ? 0.7881 0.8226 0.4670 0.1780  0.1102  0.1247  204 A1BG4 B C17 
2274 C C17 D A1BG4 G .   ? 0.7879 0.8225 0.4668 0.1780  0.1102  0.1247  204 A1BG4 B C17 
2275 C C1  C A1BG4 G .   ? 0.7975 0.8497 0.5335 0.1622  0.1268  0.1466  204 A1BG4 B C1  
2276 C C1  D A1BG4 G .   ? 0.7974 0.8497 0.5335 0.1622  0.1268  0.1466  204 A1BG4 B C1  
2277 C C2  C A1BG4 G .   ? 0.7868 0.8267 0.4840 0.1637  0.1119  0.1264  204 A1BG4 B C2  
2278 C C2  D A1BG4 G .   ? 0.7868 0.8267 0.4840 0.1637  0.1119  0.1264  204 A1BG4 B C2  
2279 C C3  C A1BG4 G .   ? 0.7853 0.8183 0.4684 0.1567  0.1028  0.1137  204 A1BG4 B C3  
2280 C C3  D A1BG4 G .   ? 0.7852 0.8181 0.4683 0.1567  0.1028  0.1136  204 A1BG4 B C3  
2281 C C9  C A1BG4 G .   ? 0.7380 0.7489 0.3624 0.1849  0.0833  0.0885  204 A1BG4 B C9  
2282 C C9  D A1BG4 G .   ? 0.7381 0.7490 0.3625 0.1849  0.0833  0.0885  204 A1BG4 B C9  
2283 C C11 C A1BG4 G .   ? 0.7308 0.7434 0.3797 0.1643  0.0901  0.0911  204 A1BG4 B C11 
2284 C C11 D A1BG4 G .   ? 0.7308 0.7435 0.3797 0.1643  0.0901  0.0911  204 A1BG4 B C11 
2285 C C12 C A1BG4 G .   ? 0.7131 0.7231 0.3737 0.1472  0.0902  0.0842  204 A1BG4 B C12 
2286 C C12 D A1BG4 G .   ? 0.7132 0.7232 0.3737 0.1472  0.0902  0.0842  204 A1BG4 B C12 
2287 O O1  C A1BG4 G .   ? 0.7007 0.7132 0.3796 0.1418  0.0966  0.0878  204 A1BG4 B O1  
2288 O O1  D A1BG4 G .   ? 0.7009 0.7133 0.3797 0.1418  0.0966  0.0878  204 A1BG4 B O1  
2289 N N2  C A1BG4 G .   ? 0.6991 0.7046 0.3492 0.1385  0.0826  0.0740  204 A1BG4 B N2  
2290 N N2  D A1BG4 G .   ? 0.6993 0.7047 0.3493 0.1385  0.0826  0.0740  204 A1BG4 B N2  
2291 C C14 C A1BG4 G .   ? 0.6943 0.6963 0.3390 0.1139  0.0735  0.0588  204 A1BG4 B C14 
2292 C C14 D A1BG4 G .   ? 0.6944 0.6963 0.3391 0.1139  0.0735  0.0588  204 A1BG4 B C14 
2293 N N4  C A1BG4 G .   ? 0.6853 0.6928 0.3566 0.0996  0.0822  0.0565  204 A1BG4 B N4  
2294 N N4  D A1BG4 G .   ? 0.6854 0.6928 0.3567 0.0996  0.0822  0.0564  204 A1BG4 B N4  
2295 C C16 C A1BG4 G .   ? 0.6964 0.7039 0.3706 0.1130  0.0866  0.0654  204 A1BG4 B C16 
2296 C C16 D A1BG4 G .   ? 0.6964 0.7038 0.3705 0.1130  0.0866  0.0654  204 A1BG4 B C16 
2297 N N5  C A1BG4 G .   ? 0.7935 0.8343 0.4884 0.1743  0.1158  0.1326  204 A1BG4 B N5  
2298 N N5  D A1BG4 G .   ? 0.7934 0.8342 0.4883 0.1743  0.1158  0.1326  204 A1BG4 B N5  
2299 S S   C SO4   H .   ? 1.3889 1.4527 1.1368 -0.0034 0.1032  -0.0934 205 SO4   B S   
2300 S S   D SO4   H .   ? 1.3889 1.4527 1.1368 -0.0034 0.1032  -0.0934 205 SO4   B S   
2301 O O1  C SO4   H .   ? 1.3530 1.4197 1.0782 -0.0064 0.0996  -0.0896 205 SO4   B O1  
2302 O O1  D SO4   H .   ? 1.3530 1.4197 1.0782 -0.0064 0.0996  -0.0896 205 SO4   B O1  
2303 O O2  C SO4   H .   ? 1.3858 1.4427 1.1319 0.0004  0.1010  -0.0808 205 SO4   B O2  
2304 O O2  D SO4   H .   ? 1.3858 1.4427 1.1319 0.0004  0.1010  -0.0808 205 SO4   B O2  
2305 O O3  C SO4   H .   ? 1.3744 1.4297 1.1388 0.0061  0.1063  -0.0933 205 SO4   B O3  
2306 O O3  D SO4   H .   ? 1.3744 1.4297 1.1388 0.0061  0.1063  -0.0933 205 SO4   B O3  
2307 O O4  C SO4   H .   ? 1.4061 1.4837 1.1635 -0.0136 0.1058  -0.1100 205 SO4   B O4  
2308 O O4  D SO4   H .   ? 1.4061 1.4837 1.1635 -0.0136 0.1058  -0.1100 205 SO4   B O4  
2309 S S   C DMS   I .   ? 1.2240 1.2564 0.9951 0.1494  0.1326  0.1377  206 DMS   B S   
2310 S S   D DMS   I .   ? 1.2238 1.2562 0.9949 0.1494  0.1326  0.1377  206 DMS   B S   
2311 O O   C DMS   I .   ? 1.1994 1.2331 0.9406 0.1579  0.1264  0.1346  206 DMS   B O   
2312 O O   D DMS   I .   ? 1.1995 1.2332 0.9408 0.1579  0.1264  0.1346  206 DMS   B O   
2313 C C1  C DMS   I .   ? 1.2042 1.2331 0.9842 0.1308  0.1279  0.1219  206 DMS   B C1  
2314 C C1  D DMS   I .   ? 1.2042 1.2331 0.9842 0.1308  0.1279  0.1219  206 DMS   B C1  
2315 C C2  C DMS   I .   ? 1.2207 1.2642 1.0086 0.1531  0.1403  0.1550  206 DMS   B C2  
2316 C C2  D DMS   I .   ? 1.2206 1.2641 1.0085 0.1531  0.1403  0.1550  206 DMS   B C2  
# 
