data_7IAP
# 
_entry.id   7IAP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7IAP         pdb_00007iap 10.2210/pdb7iap/pdb 
WWPDB D_1001408528 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7IAP 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, X.'              1  ? 
'Marples, P.G.'       2  ? 
'Godoy, A.S.'         3  ? 
'Koekemoer, L.'       4  ? 
'Aschenbrenner, J.C.' 5  ? 
'Balcomb, B.H.'       6  ? 
'Fairhead, M.'        7  ? 
'Lithgo, R.M.'        8  ? 
'Lee, A.'             9  ? 
'Kenton, N.'          10 ? 
'Thompson, W.'        11 ? 
'Tomlinson, C.W.E.'   12 ? 
'Wild, C.'            13 ? 
'Winokan, M.'         14 ? 
'Williams, E.P.'      15 ? 
'Chandran, A.V.'      16 ? 
'Walsh, M.A.'         17 ? 
'Fearon, D.'          18 ? 
'von Delft, F.'       19 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                                                     5067.486  1  
?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                                              18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                               78.133    1  
?                           ?    ? ? 
4 non-polymer syn '6-cyclopropyl-N-(2,3-dihydro-1H-isoindol-5-yl)-1-methyl-1H-pyrazolo[3,4-b]pyridine-4-carboxamide' 333.387   1  
?                           ?    ? ? 
5 water       nat water                                                                                              18.015    66 
?                           ?    ? ? 
# 
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 '6-cyclopropyl-N-(2,3-dihydro-1H-isoindol-5-yl)-1-methyl-1H-pyrazolo[3,4-b]pyridine-4-carboxamide' A1B9A 
5 water                                                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B9A non-polymer         . '6-cyclopropyl-N-(2,3-dihydro-1H-isoindol-5-yl)-1-methyl-1H-pyrazolo[3,4-b]pyridine-4-carboxamide' ? 
'C19 H19 N5 O'   333.387 
ALA   'L-peptide linking' y ALANINE                                                                                            ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                           ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                         ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                    ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                           ? 
'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                               ? 
'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                          ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                    ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                            ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                          ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                              ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                         ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                            ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                             ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                         ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                      ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                            ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                             ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                          ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                         ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                           ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                             ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1B9A 1  202 203 A1B9A LIG B . 
E 5 HOH   1  101 118 HOH   HOH A . 
E 5 HOH   2  102 98  HOH   HOH A . 
E 5 HOH   3  103 34  HOH   HOH A . 
E 5 HOH   4  104 40  HOH   HOH A . 
E 5 HOH   5  105 105 HOH   HOH A . 
E 5 HOH   6  106 29  HOH   HOH A . 
E 5 HOH   7  107 49  HOH   HOH A . 
E 5 HOH   8  108 16  HOH   HOH A . 
E 5 HOH   9  109 110 HOH   HOH A . 
E 5 HOH   10 110 66  HOH   HOH A . 
E 5 HOH   11 111 120 HOH   HOH A . 
E 5 HOH   12 112 83  HOH   HOH A . 
E 5 HOH   13 113 27  HOH   HOH A . 
E 5 HOH   14 114 119 HOH   HOH A . 
E 5 HOH   15 115 124 HOH   HOH A . 
F 5 HOH   1  301 14  HOH   HOH B . 
F 5 HOH   2  302 11  HOH   HOH B . 
F 5 HOH   3  303 56  HOH   HOH B . 
F 5 HOH   4  304 32  HOH   HOH B . 
F 5 HOH   5  305 100 HOH   HOH B . 
F 5 HOH   6  306 1   HOH   HOH B . 
F 5 HOH   7  307 117 HOH   HOH B . 
F 5 HOH   8  308 9   HOH   HOH B . 
F 5 HOH   9  309 63  HOH   HOH B . 
F 5 HOH   10 310 58  HOH   HOH B . 
F 5 HOH   11 311 39  HOH   HOH B . 
F 5 HOH   12 312 4   HOH   HOH B . 
F 5 HOH   13 313 20  HOH   HOH B . 
F 5 HOH   14 314 36  HOH   HOH B . 
F 5 HOH   15 315 5   HOH   HOH B . 
F 5 HOH   16 316 60  HOH   HOH B . 
F 5 HOH   17 317 61  HOH   HOH B . 
F 5 HOH   18 318 67  HOH   HOH B . 
F 5 HOH   19 319 54  HOH   HOH B . 
F 5 HOH   20 320 108 HOH   HOH B . 
F 5 HOH   21 321 10  HOH   HOH B . 
F 5 HOH   22 322 125 HOH   HOH B . 
F 5 HOH   23 323 51  HOH   HOH B . 
F 5 HOH   24 324 69  HOH   HOH B . 
F 5 HOH   25 325 35  HOH   HOH B . 
F 5 HOH   26 326 73  HOH   HOH B . 
F 5 HOH   27 327 2   HOH   HOH B . 
F 5 HOH   28 328 57  HOH   HOH B . 
F 5 HOH   29 329 115 HOH   HOH B . 
F 5 HOH   30 330 103 HOH   HOH B . 
F 5 HOH   31 331 3   HOH   HOH B . 
F 5 HOH   32 332 64  HOH   HOH B . 
F 5 HOH   33 333 123 HOH   HOH B . 
F 5 HOH   34 334 72  HOH   HOH B . 
F 5 HOH   35 335 62  HOH   HOH B . 
F 5 HOH   36 336 50  HOH   HOH B . 
F 5 HOH   37 337 68  HOH   HOH B . 
F 5 HOH   38 338 112 HOH   HOH B . 
F 5 HOH   39 339 17  HOH   HOH B . 
F 5 HOH   40 340 121 HOH   HOH B . 
F 5 HOH   41 341 102 HOH   HOH B . 
F 5 HOH   42 342 87  HOH   HOH B . 
F 5 HOH   43 343 79  HOH   HOH B . 
F 5 HOH   44 344 23  HOH   HOH B . 
F 5 HOH   45 345 116 HOH   HOH B . 
F 5 HOH   46 346 127 HOH   HOH B . 
F 5 HOH   47 347 107 HOH   HOH B . 
F 5 HOH   48 348 44  HOH   HOH B . 
F 5 HOH   49 349 122 HOH   HOH B . 
F 5 HOH   50 350 126 HOH   HOH B . 
F 5 HOH   51 351 109 HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      '2.10.4 (23-JAN-2024)' ?               program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.7.15                 02/11/23        program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 PDB_EXTRACT 3.23                   'SEP. 23, 2016' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
4 XDS         .                      ?               program ?                 ?                                'data reduction'  
?                                                   ?   ? 
5 PHASER      .                      ?               program ?                 ?                                phasing           
?                                                   ?   ? 
# 
_cell.entry_id           7IAP 
_cell.length_a           42.445 
_cell.length_b           42.445 
_cell.length_c           216.754 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7IAP 
_symmetry.Int_Tables_number                95 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.entry_id          7IAP 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.450 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   41.58 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-07-31 
_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   0.92134 
_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        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7IAP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.190 
_reflns.d_resolution_high            2.350 
_reflns.number_obs                   9125 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.485 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        4.700 
_reflns.B_iso_Wilson_estimate        48.350 
_reflns.pdbx_redundancy              18.600 
_reflns.pdbx_Rrim_I_all              0.498 
_reflns.pdbx_Rpim_I_all              0.111 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     169439 
_reflns.pdbx_scaling_rejects         270 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 2.350 2.470  ? 17585 ? ? 4.048 ? ? ? 13.800 ? 0.800  ? 1274 ? ? ? ? 100.000 4.194 1.057 0.634 ? 
1 2 7.420 54.190 ? 6574  ? ? 0.200 ? ? ? 17.400 ? 11.900 ? 378  ? ? ? ? 99.900  0.206 0.048 0.993 ? 
# 
_refine.entry_id                                 7IAP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.3480 
_refine.ls_d_res_low                             54.1900 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5000 
_refine.ls_number_reflns_obs                     9008 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2408 
_refine.ls_R_factor_R_work                       0.2387 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2816 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.7700 
_refine.ls_number_reflns_R_free                  430 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               52.0300 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -3.0744 
_refine.aniso_B[2][2]                            -3.0744 
_refine.aniso_B[3][3]                            6.1488 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9270 
_refine.correlation_coeff_Fo_to_Fc_free          0.9050 
_refine.overall_SU_R_Cruickshank_DPI             0.4370 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2780 
_refine.pdbx_overall_SU_R_Blow_DPI               0.5470 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2900 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      5GPI 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                110.650 
_refine.B_iso_min                                23.250 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7IAP 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.340 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.3480 
_refine_hist.d_res_low                        54.1900 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             66 
_refine_hist.number_atoms_total               1571 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           49.11 
_refine_hist.pdbx_B_iso_mean_solvent          46.18 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        538  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              269  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1567 ?      ? 10.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 194  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1207 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1567 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2135 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.730  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    18.590 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.3500 
_refine_ls_shell.d_res_low                        2.3900 
_refine_ls_shell.pdbx_total_number_of_bins_used   22 
_refine_ls_shell.percent_reflns_obs               93.3300 
_refine_ls_shell.number_reflns_R_work             410 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3419 
_refine_ls_shell.R_factor_R_free                  0.3237 
_refine_ls_shell.percent_reflns_R_free            4.4300 
_refine_ls_shell.number_reflns_R_free             19 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                429 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IAP 
_struct.title                     
;Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0029723-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IAP 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, XChemExplorer, ASAP Discovery Consortium, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7IAP A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IAP 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 7IAP SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IAP MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IAP MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IAP LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4820 ? 
1 MORE         -28  ? 
1 'SSA (A^2)'  9760 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? 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 TYR A 9   ? GLY A 14  ? TYR A 52  GLY A 57  
AA1 2 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 3 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 4 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 5 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 6 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 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
AA4 1 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA4 2 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
# 
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 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 2 3 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 3 4 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 4 5 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 5 6 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O LYS B 98  ? O LYS B 107 N ALA B 90  ? N ALA B 99  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O ILE B 106 ? O ILE B 115 
AA3 3 4 N GLY B 105 ? N GLY B 114 O ALA B 116 ? O ALA B 125 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA4 1 2 N LEU B 49  ? N LEU B 58  O LEU B 56  ? O LEU B 65  
# 
_pdbx_entry_details.entry_id                   7IAP 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU B 30 ? ? -112.73 -159.39 
2 1 LYS B 54 ? ? 59.64   18.47   
3 1 CYS B 80 ? ? 78.85   -17.69  
4 1 LEU B 92 ? ? -131.38 -47.64  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     348 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.5227 -1.5350 -19.2602 -0.0900 -0.0047 -0.3284 0.1875 0.1144 0.1260 4.5193 5.4073 5.8370 
-2.7885 0.8892 1.6460  0.4774 -0.4501 -0.0273 0.5705 0.3611 -0.3608 -0.5387 0.0697 0.5874 
'X-RAY DIFFRACTION' 2 ? refined -18.4424 0.9434  -15.6828 0.0954  0.0801  -0.1815 0.2205 0.0235 0.0262 2.0623 1.3939 2.6632 
-0.9410 0.9058 -0.0983 0.4044 -0.3754 -0.0290 0.2578 0.1601 0.1203  -0.0955 0.1429 0.3646 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 50 A 88  '{ A|* }' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 B 171 '{ B|* }' ? ? ? ? ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B9A N1   N Y N 1   
A1B9A N3   N N N 2   
A1B9A C4   C Y N 3   
A1B9A C5   C N N 4   
A1B9A C6   C Y N 5   
A1B9A C7   C Y N 6   
A1B9A C8   C Y N 7   
A1B9A C10  C Y N 8   
A1B9A C13  C N N 9   
A1B9A C15  C Y N 10  
A1B9A C17  C N N 11  
A1B9A C1   C N N 12  
A1B9A N2   N Y N 13  
A1B9A C2   C Y N 14  
A1B9A C3   C Y N 15  
A1B9A O1   O N N 16  
A1B9A C9   C Y N 17  
A1B9A C11  C Y N 18  
A1B9A C12  C N N 19  
A1B9A N4   N N N 20  
A1B9A C14  C Y N 21  
A1B9A C16  C N N 22  
A1B9A C18  C N N 23  
A1B9A N5   N Y N 24  
A1B9A C19  C Y N 25  
A1B9A H5   H N N 26  
A1B9A H6   H N N 27  
A1B9A H7   H N N 28  
A1B9A H12  H N N 29  
A1B9A H13  H N N 30  
A1B9A H16  H N N 31  
A1B9A H17  H N N 32  
A1B9A H1   H N N 33  
A1B9A H3   H N N 34  
A1B9A H2   H N N 35  
A1B9A H4   H N N 36  
A1B9A H8   H N N 37  
A1B9A H9   H N N 38  
A1B9A H10  H N N 39  
A1B9A H11  H N N 40  
A1B9A H14  H N N 41  
A1B9A H15  H N N 42  
A1B9A H18  H N N 43  
A1B9A H19  H N N 44  
ALA   N    N N N 45  
ALA   CA   C N S 46  
ALA   C    C N N 47  
ALA   O    O N N 48  
ALA   CB   C N N 49  
ALA   OXT  O N N 50  
ALA   H    H N N 51  
ALA   H2   H N N 52  
ALA   HA   H N N 53  
ALA   HB1  H N N 54  
ALA   HB2  H N N 55  
ALA   HB3  H N N 56  
ALA   HXT  H N N 57  
ARG   N    N N N 58  
ARG   CA   C N S 59  
ARG   C    C N N 60  
ARG   O    O N N 61  
ARG   CB   C N N 62  
ARG   CG   C N N 63  
ARG   CD   C N N 64  
ARG   NE   N N N 65  
ARG   CZ   C N N 66  
ARG   NH1  N N N 67  
ARG   NH2  N N N 68  
ARG   OXT  O N N 69  
ARG   H    H N N 70  
ARG   H2   H N N 71  
ARG   HA   H N N 72  
ARG   HB2  H N N 73  
ARG   HB3  H N N 74  
ARG   HG2  H N N 75  
ARG   HG3  H N N 76  
ARG   HD2  H N N 77  
ARG   HD3  H N N 78  
ARG   HE   H N N 79  
ARG   HH11 H N N 80  
ARG   HH12 H N N 81  
ARG   HH21 H N N 82  
ARG   HH22 H N N 83  
ARG   HXT  H N N 84  
ASN   N    N N N 85  
ASN   CA   C N S 86  
ASN   C    C N N 87  
ASN   O    O N N 88  
ASN   CB   C N N 89  
ASN   CG   C N N 90  
ASN   OD1  O N N 91  
ASN   ND2  N N N 92  
ASN   OXT  O N N 93  
ASN   H    H N N 94  
ASN   H2   H N N 95  
ASN   HA   H N N 96  
ASN   HB2  H N N 97  
ASN   HB3  H N N 98  
ASN   HD21 H N N 99  
ASN   HD22 H N N 100 
ASN   HXT  H N N 101 
ASP   N    N N N 102 
ASP   CA   C N S 103 
ASP   C    C N N 104 
ASP   O    O N N 105 
ASP   CB   C N N 106 
ASP   CG   C N N 107 
ASP   OD1  O N N 108 
ASP   OD2  O N N 109 
ASP   OXT  O N N 110 
ASP   H    H N N 111 
ASP   H2   H N N 112 
ASP   HA   H N N 113 
ASP   HB2  H N N 114 
ASP   HB3  H N N 115 
ASP   HD2  H N N 116 
ASP   HXT  H N N 117 
CYS   N    N N N 118 
CYS   CA   C N R 119 
CYS   C    C N N 120 
CYS   O    O N N 121 
CYS   CB   C N N 122 
CYS   SG   S N N 123 
CYS   OXT  O N N 124 
CYS   H    H N N 125 
CYS   H2   H N N 126 
CYS   HA   H N N 127 
CYS   HB2  H N N 128 
CYS   HB3  H N N 129 
CYS   HG   H N N 130 
CYS   HXT  H N N 131 
DMS   S    S N N 132 
DMS   O    O N N 133 
DMS   C1   C N N 134 
DMS   C2   C N N 135 
DMS   H11  H N N 136 
DMS   H12  H N N 137 
DMS   H13  H N N 138 
DMS   H21  H N N 139 
DMS   H22  H N N 140 
DMS   H23  H N N 141 
GLN   N    N N N 142 
GLN   CA   C N S 143 
GLN   C    C N N 144 
GLN   O    O N N 145 
GLN   CB   C N N 146 
GLN   CG   C N N 147 
GLN   CD   C N N 148 
GLN   OE1  O N N 149 
GLN   NE2  N N N 150 
GLN   OXT  O N N 151 
GLN   H    H N N 152 
GLN   H2   H N N 153 
GLN   HA   H N N 154 
GLN   HB2  H N N 155 
GLN   HB3  H N N 156 
GLN   HG2  H N N 157 
GLN   HG3  H N N 158 
GLN   HE21 H N N 159 
GLN   HE22 H N N 160 
GLN   HXT  H N N 161 
GLU   N    N N N 162 
GLU   CA   C N S 163 
GLU   C    C N N 164 
GLU   O    O N N 165 
GLU   CB   C N N 166 
GLU   CG   C N N 167 
GLU   CD   C N N 168 
GLU   OE1  O N N 169 
GLU   OE2  O N N 170 
GLU   OXT  O N N 171 
GLU   H    H N N 172 
GLU   H2   H N N 173 
GLU   HA   H N N 174 
GLU   HB2  H N N 175 
GLU   HB3  H N N 176 
GLU   HG2  H N N 177 
GLU   HG3  H N N 178 
GLU   HE2  H N N 179 
GLU   HXT  H N N 180 
GLY   N    N N N 181 
GLY   CA   C N N 182 
GLY   C    C N N 183 
GLY   O    O N N 184 
GLY   OXT  O N N 185 
GLY   H    H N N 186 
GLY   H2   H N N 187 
GLY   HA2  H N N 188 
GLY   HA3  H N N 189 
GLY   HXT  H N N 190 
HIS   N    N N N 191 
HIS   CA   C N S 192 
HIS   C    C N N 193 
HIS   O    O N N 194 
HIS   CB   C N N 195 
HIS   CG   C Y N 196 
HIS   ND1  N Y N 197 
HIS   CD2  C Y N 198 
HIS   CE1  C Y N 199 
HIS   NE2  N Y N 200 
HIS   OXT  O N N 201 
HIS   H    H N N 202 
HIS   H2   H N N 203 
HIS   HA   H N N 204 
HIS   HB2  H N N 205 
HIS   HB3  H N N 206 
HIS   HD1  H N N 207 
HIS   HD2  H N N 208 
HIS   HE1  H N N 209 
HIS   HE2  H N N 210 
HIS   HXT  H N N 211 
HOH   O    O N N 212 
HOH   H1   H N N 213 
HOH   H2   H N N 214 
ILE   N    N N N 215 
ILE   CA   C N S 216 
ILE   C    C N N 217 
ILE   O    O N N 218 
ILE   CB   C N S 219 
ILE   CG1  C N N 220 
ILE   CG2  C N N 221 
ILE   CD1  C N N 222 
ILE   OXT  O N N 223 
ILE   H    H N N 224 
ILE   H2   H N N 225 
ILE   HA   H N N 226 
ILE   HB   H N N 227 
ILE   HG12 H N N 228 
ILE   HG13 H N N 229 
ILE   HG21 H N N 230 
ILE   HG22 H N N 231 
ILE   HG23 H N N 232 
ILE   HD11 H N N 233 
ILE   HD12 H N N 234 
ILE   HD13 H N N 235 
ILE   HXT  H N N 236 
LEU   N    N N N 237 
LEU   CA   C N S 238 
LEU   C    C N N 239 
LEU   O    O N N 240 
LEU   CB   C N N 241 
LEU   CG   C N N 242 
LEU   CD1  C N N 243 
LEU   CD2  C N N 244 
LEU   OXT  O N N 245 
LEU   H    H N N 246 
LEU   H2   H N N 247 
LEU   HA   H N N 248 
LEU   HB2  H N N 249 
LEU   HB3  H N N 250 
LEU   HG   H N N 251 
LEU   HD11 H N N 252 
LEU   HD12 H N N 253 
LEU   HD13 H N N 254 
LEU   HD21 H N N 255 
LEU   HD22 H N N 256 
LEU   HD23 H N N 257 
LEU   HXT  H N N 258 
LYS   N    N N N 259 
LYS   CA   C N S 260 
LYS   C    C N N 261 
LYS   O    O N N 262 
LYS   CB   C N N 263 
LYS   CG   C N N 264 
LYS   CD   C N N 265 
LYS   CE   C N N 266 
LYS   NZ   N N N 267 
LYS   OXT  O N N 268 
LYS   H    H N N 269 
LYS   H2   H N N 270 
LYS   HA   H N N 271 
LYS   HB2  H N N 272 
LYS   HB3  H N N 273 
LYS   HG2  H N N 274 
LYS   HG3  H N N 275 
LYS   HD2  H N N 276 
LYS   HD3  H N N 277 
LYS   HE2  H N N 278 
LYS   HE3  H N N 279 
LYS   HZ1  H N N 280 
LYS   HZ2  H N N 281 
LYS   HZ3  H N N 282 
LYS   HXT  H N N 283 
MET   N    N N N 284 
MET   CA   C N S 285 
MET   C    C N N 286 
MET   O    O N N 287 
MET   CB   C N N 288 
MET   CG   C N N 289 
MET   SD   S N N 290 
MET   CE   C N N 291 
MET   OXT  O N N 292 
MET   H    H N N 293 
MET   H2   H N N 294 
MET   HA   H N N 295 
MET   HB2  H N N 296 
MET   HB3  H N N 297 
MET   HG2  H N N 298 
MET   HG3  H N N 299 
MET   HE1  H N N 300 
MET   HE2  H N N 301 
MET   HE3  H N N 302 
MET   HXT  H N N 303 
PHE   N    N N N 304 
PHE   CA   C N S 305 
PHE   C    C N N 306 
PHE   O    O N N 307 
PHE   CB   C N N 308 
PHE   CG   C Y N 309 
PHE   CD1  C Y N 310 
PHE   CD2  C Y N 311 
PHE   CE1  C Y N 312 
PHE   CE2  C Y N 313 
PHE   CZ   C Y N 314 
PHE   OXT  O N N 315 
PHE   H    H N N 316 
PHE   H2   H N N 317 
PHE   HA   H N N 318 
PHE   HB2  H N N 319 
PHE   HB3  H N N 320 
PHE   HD1  H N N 321 
PHE   HD2  H N N 322 
PHE   HE1  H N N 323 
PHE   HE2  H N N 324 
PHE   HZ   H N N 325 
PHE   HXT  H N N 326 
PRO   N    N N N 327 
PRO   CA   C N S 328 
PRO   C    C N N 329 
PRO   O    O N N 330 
PRO   CB   C N N 331 
PRO   CG   C N N 332 
PRO   CD   C N N 333 
PRO   OXT  O N N 334 
PRO   H    H N N 335 
PRO   HA   H N N 336 
PRO   HB2  H N N 337 
PRO   HB3  H N N 338 
PRO   HG2  H N N 339 
PRO   HG3  H N N 340 
PRO   HD2  H N N 341 
PRO   HD3  H N N 342 
PRO   HXT  H N N 343 
SER   N    N N N 344 
SER   CA   C N S 345 
SER   C    C N N 346 
SER   O    O N N 347 
SER   CB   C N N 348 
SER   OG   O N N 349 
SER   OXT  O N N 350 
SER   H    H N N 351 
SER   H2   H N N 352 
SER   HA   H N N 353 
SER   HB2  H N N 354 
SER   HB3  H N N 355 
SER   HG   H N N 356 
SER   HXT  H N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1B9A C1  N1   sing N N 1   
A1B9A N1  N2   sing Y N 2   
A1B9A N2  C2   doub Y N 3   
A1B9A C2  C3   sing Y N 4   
A1B9A C3  C4   doub Y N 5   
A1B9A C4  C5   sing N N 6   
A1B9A C5  O1   doub N N 7   
A1B9A C5  N3   sing N N 8   
A1B9A N3  C6   sing N N 9   
A1B9A C6  C7   doub Y N 10  
A1B9A C7  C8   sing Y N 11  
A1B9A C8  C9   doub Y N 12  
A1B9A C9  C10  sing Y N 13  
A1B9A C10 C11  doub Y N 14  
A1B9A C10 C12  sing N N 15  
A1B9A C12 N4   sing N N 16  
A1B9A N4  C13  sing N N 17  
A1B9A C4  C14  sing Y N 18  
A1B9A C14 C15  doub Y N 19  
A1B9A C15 C16  sing N N 20  
A1B9A C16 C17  sing N N 21  
A1B9A C17 C18  sing N N 22  
A1B9A C15 N5   sing Y N 23  
A1B9A N5  C19  doub Y N 24  
A1B9A N1  C19  sing Y N 25  
A1B9A C3  C19  sing Y N 26  
A1B9A C6  C11  sing Y N 27  
A1B9A C16 C18  sing N N 28  
A1B9A C9  C13  sing N N 29  
A1B9A N3  H5   sing N N 30  
A1B9A C7  H6   sing N N 31  
A1B9A C8  H7   sing N N 32  
A1B9A C13 H12  sing N N 33  
A1B9A C13 H13  sing N N 34  
A1B9A C17 H16  sing N N 35  
A1B9A C17 H17  sing N N 36  
A1B9A C1  H1   sing N N 37  
A1B9A C1  H3   sing N N 38  
A1B9A C1  H2   sing N N 39  
A1B9A C2  H4   sing N N 40  
A1B9A C11 H8   sing N N 41  
A1B9A C12 H9   sing N N 42  
A1B9A C12 H10  sing N N 43  
A1B9A N4  H11  sing N N 44  
A1B9A C14 H14  sing N N 45  
A1B9A C16 H15  sing N N 46  
A1B9A C18 H18  sing N N 47  
A1B9A C18 H19  sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
DMS   S   O    doub N N 131 
DMS   S   C1   sing N N 132 
DMS   S   C2   sing N N 133 
DMS   C1  H11  sing N N 134 
DMS   C1  H12  sing N N 135 
DMS   C1  H13  sing N N 136 
DMS   C2  H21  sing N N 137 
DMS   C2  H22  sing N N 138 
DMS   C2  H23  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
PHE   N   CA   sing N N 294 
PHE   N   H    sing N N 295 
PHE   N   H2   sing N N 296 
PHE   CA  C    sing N N 297 
PHE   CA  CB   sing N N 298 
PHE   CA  HA   sing N N 299 
PHE   C   O    doub N N 300 
PHE   C   OXT  sing N N 301 
PHE   CB  CG   sing N N 302 
PHE   CB  HB2  sing N N 303 
PHE   CB  HB3  sing N N 304 
PHE   CG  CD1  doub Y N 305 
PHE   CG  CD2  sing Y N 306 
PHE   CD1 CE1  sing Y N 307 
PHE   CD1 HD1  sing N N 308 
PHE   CD2 CE2  doub Y N 309 
PHE   CD2 HD2  sing N N 310 
PHE   CE1 CZ   doub Y N 311 
PHE   CE1 HE1  sing N N 312 
PHE   CE2 CZ   sing Y N 313 
PHE   CE2 HE2  sing N N 314 
PHE   CZ  HZ   sing N N 315 
PHE   OXT HXT  sing N N 316 
PRO   N   CA   sing N N 317 
PRO   N   CD   sing N N 318 
PRO   N   H    sing N N 319 
PRO   CA  C    sing N N 320 
PRO   CA  CB   sing N N 321 
PRO   CA  HA   sing N N 322 
PRO   C   O    doub N N 323 
PRO   C   OXT  sing N N 324 
PRO   CB  CG   sing N N 325 
PRO   CB  HB2  sing N N 326 
PRO   CB  HB3  sing N N 327 
PRO   CG  CD   sing N N 328 
PRO   CG  HG2  sing N N 329 
PRO   CG  HG3  sing N N 330 
PRO   CD  HD2  sing N N 331 
PRO   CD  HD3  sing N N 332 
PRO   OXT HXT  sing N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002345 
_pdbx_deposit_group.group_description   
;XDomainX of XOrganismX None screened against the XXX Fragment Library by X-ray Crystallography at the XChem facility of Diamond Light Source beamline I04-1
;
_pdbx_deposit_group.group_title         
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7IAP 
_atom_sites.fract_transf_matrix[1][1]   0.023560 
_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]   0.023560 
_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]   0.004614 
_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   ? -21.267 19.418  -7.378  1.00 55.49  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.313 18.396  -7.400  1.00 55.72  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.460 17.720  -8.767  1.00 54.32  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.810 18.372  -9.757  1.00 54.28  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.662 18.967  -6.938  1.00 58.99  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.563 17.913  -6.322  1.00 66.52  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.235 17.421  -5.218  1.00 67.47  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.590 17.570  -6.948  1.00 70.23  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.225 16.396  -8.802  1.00 52.75  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.326 15.587  -10.009 1.00 51.49  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.762 15.379  -10.493 1.00 50.12  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.708 15.421  -9.697  1.00 50.03  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.640 14.239  -9.811  1.00 51.93  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.166 14.360  -9.590  1.00 53.58  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.378 12.760  -9.354  1.00 53.35  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.690 13.278  -9.175  1.00 53.53  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.913 15.148  -11.812 1.00 48.57  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.205 14.957  -12.466 1.00 47.69  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.095 14.014  -13.654 1.00 46.41  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.028 13.920  -14.259 1.00 46.63  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.811 16.303  -12.900 1.00 47.95  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.002 17.050  -13.941 1.00 49.13  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.014 17.953  -13.565 1.00 49.98  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.271 16.905  -15.300 1.00 50.17  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.276 18.651  -14.512 1.00 50.96  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.543 17.602  -16.258 1.00 51.05  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.554 18.486  -15.858 1.00 52.12  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.802 19.160  -16.791 1.00 53.69  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.197 13.330  -14.016 1.00 44.91  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.158 12.383  -15.131 1.00 43.65  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.963 12.840  -16.353 1.00 43.38  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.953 13.570  -16.223 1.00 43.18  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.533 10.945  -14.702 1.00 43.21  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -27.970 10.840  -14.182 1.00 43.02  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.528 10.402  -13.684 1.00 43.68  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.448 9.401   -14.128 1.00 43.29  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.487 12.430  -17.549 1.00 43.08  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.071 12.739  -18.861 1.00 43.42  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.178 11.460  -19.679 1.00 43.28  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.185 10.753  -19.782 1.00 43.18  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.175 13.709  -19.641 1.00 45.74  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.120 15.107  -19.064 1.00 52.06  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.384 16.111  -19.928 1.00 58.80  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.610 15.688  -20.817 1.00 58.94  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.579 17.329  -19.711 1.00 62.22  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.338 11.180  -20.298 1.00 42.87  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.467 9.966   -21.103 1.00 43.09  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.604 9.995   -22.353 1.00 43.52  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.586 11.001  -23.057 1.00 43.41  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.917 9.645   -21.436 1.00 43.75  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.097 8.195   -21.831 1.00 45.35  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.554 7.831   -21.873 1.00 47.50  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.751 6.408   -22.118 1.00 49.84  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.793 5.856   -23.326 1.00 52.77  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.645 6.605   -24.413 1.00 53.20  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.968 4.549   -23.458 1.00 52.69  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.855 8.904   -22.599 1.00 43.99  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.971 8.761   -23.759 1.00 45.52  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.404 7.657   -24.757 1.00 47.37  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.650 7.318   -25.666 1.00 47.19  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.533 8.539   -23.311 1.00 45.52  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.602 7.111   -24.578 1.00 48.83  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -28.137 6.110   -25.486 1.00 50.49  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.546 4.785   -24.883 1.00 52.06  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.416 4.566   -23.681 1.00 51.91  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -29.076 3.898   -25.744 1.00 53.26  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.492 2.539   -25.404 1.00 54.25  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.305 1.621   -25.266 1.00 54.83  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.249 1.882   -25.833 1.00 54.96  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.365 1.966   -26.527 1.00 55.76  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.803 2.382   -26.471 1.00 61.01  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -32.104 3.377   -25.781 1.00 61.57  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.629 1.743   -27.154 1.00 64.07  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.499 0.499   -24.575 1.00 54.99  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.466 -0.505  -24.449 1.00 55.25  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.850 -1.710  -25.293 1.00 55.95  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.706 -2.502  -24.905 1.00 55.48  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.229 -0.849  -22.978 1.00 55.48  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.745 0.398   -22.213 1.00 56.28  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.253 -1.992  -22.866 1.00 55.87  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.486 0.202   -20.703 1.00 57.24  ? 59  ILE   A CD1 1 
ATOM   82   N N   . THR   A 1 17  ? -27.259 -1.797  -26.493 1.00 57.25  ? 60  THR   A N   1 
ATOM   83   C CA  . THR   A 1 17  ? -27.472 -2.881  -27.459 1.00 59.10  ? 60  THR   A CA  1 
ATOM   84   C C   . THR   A 1 17  ? -26.163 -3.317  -28.111 1.00 60.82  ? 60  THR   A C   1 
ATOM   85   O O   . THR   A 1 17  ? -25.258 -2.504  -28.280 1.00 60.80  ? 60  THR   A O   1 
ATOM   86   C CB  . THR   A 1 17  ? -28.368 -2.415  -28.610 1.00 60.21  ? 60  THR   A CB  1 
ATOM   87   O OG1 . THR   A 1 17  ? -27.829 -1.202  -29.147 1.00 60.89  ? 60  THR   A OG1 1 
ATOM   88   C CG2 . THR   A 1 17  ? -29.819 -2.254  -28.200 1.00 60.80  ? 60  THR   A CG2 1 
ATOM   89   N N   . TRP   A 1 18  ? -26.089 -4.577  -28.543 1.00 62.27  ? 61  TRP   A N   1 
ATOM   90   C CA  . TRP   A 1 18  ? -24.935 -5.068  -29.286 1.00 64.69  ? 61  TRP   A CA  1 
ATOM   91   C C   . TRP   A 1 18  ? -25.134 -4.611  -30.731 1.00 67.90  ? 61  TRP   A C   1 
ATOM   92   O O   . TRP   A 1 18  ? -26.218 -4.804  -31.289 1.00 67.95  ? 61  TRP   A O   1 
ATOM   93   C CB  . TRP   A 1 18  ? -24.886 -6.604  -29.220 1.00 64.40  ? 61  TRP   A CB  1 
ATOM   94   C CG  . TRP   A 1 18  ? -23.885 -7.268  -30.119 1.00 64.85  ? 61  TRP   A CG  1 
ATOM   95   C CD1 . TRP   A 1 18  ? -24.084 -7.661  -31.410 1.00 65.82  ? 61  TRP   A CD1 1 
ATOM   96   C CD2 . TRP   A 1 18  ? -22.602 -7.789  -29.736 1.00 64.97  ? 61  TRP   A CD2 1 
ATOM   97   N NE1 . TRP   A 1 18  ? -22.978 -8.335  -31.875 1.00 66.11  ? 61  TRP   A NE1 1 
ATOM   98   C CE2 . TRP   A 1 18  ? -22.059 -8.437  -30.863 1.00 65.77  ? 61  TRP   A CE2 1 
ATOM   99   C CE3 . TRP   A 1 18  ? -21.847 -7.745  -28.559 1.00 65.38  ? 61  TRP   A CE3 1 
ATOM   100  C CZ2 . TRP   A 1 18  ? -20.802 -9.033  -30.844 1.00 66.30  ? 61  TRP   A CZ2 1 
ATOM   101  C CZ3 . TRP   A 1 18  ? -20.599 -8.331  -28.547 1.00 66.09  ? 61  TRP   A CZ3 1 
ATOM   102  C CH2 . TRP   A 1 18  ? -20.078 -8.940  -29.686 1.00 66.25  ? 61  TRP   A CH2 1 
ATOM   103  N N   . GLU   A 1 19  ? -24.114 -3.994  -31.338 1.00 70.32  ? 62  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 19  ? -24.223 -3.549  -32.727 1.00 73.07  ? 62  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 19  ? -23.390 -4.427  -33.660 1.00 75.91  ? 62  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 19  ? -22.171 -4.503  -33.515 1.00 76.21  ? 62  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 19  ? -23.844 -2.068  -32.869 1.00 75.59  ? 62  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 19  ? -24.735 -1.126  -32.069 1.00 81.61  ? 62  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 19  ? -26.186 -1.003  -32.505 1.00 89.29  ? 62  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 19  ? -26.433 -0.675  -33.691 1.00 93.15  ? 62  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 19  ? -27.080 -1.213  -31.654 1.00 90.15  ? 62  GLU   A OE2 1 
ATOM   112  N N   . LYS   A 1 20  ? -24.045 -5.123  -34.588 1.00 77.92  ? 63  LYS   A N   1 
ATOM   113  C CA  . LYS   A 1 20  ? -23.337 -5.955  -35.557 1.00 80.62  ? 63  LYS   A CA  1 
ATOM   114  C C   . LYS   A 1 20  ? -22.556 -5.044  -36.514 1.00 82.67  ? 63  LYS   A C   1 
ATOM   115  O O   . LYS   A 1 20  ? -23.025 -3.945  -36.819 1.00 83.18  ? 63  LYS   A O   1 
ATOM   116  C CB  . LYS   A 1 20  ? -24.324 -6.807  -36.374 1.00 83.68  ? 63  LYS   A CB  1 
ATOM   117  C CG  . LYS   A 1 20  ? -25.423 -7.495  -35.567 1.00 88.85  ? 63  LYS   A CG  1 
ATOM   118  C CD  . LYS   A 1 20  ? -26.400 -8.206  -36.518 1.00 93.95  ? 63  LYS   A CD  1 
ATOM   119  C CE  . LYS   A 1 20  ? -27.754 -8.468  -35.899 1.00 98.28  ? 63  LYS   A CE  1 
ATOM   120  N NZ  . LYS   A 1 20  ? -28.697 -9.072  -36.881 1.00 100.74 ? 63  LYS   A NZ  1 
ATOM   121  N N   . ASP   A 1 21  ? -21.392 -5.502  -37.010 1.00 83.73  ? 64  ASP   A N   1 
ATOM   122  C CA  . ASP   A 1 21  ? -20.554 -4.717  -37.933 1.00 85.14  ? 64  ASP   A CA  1 
ATOM   123  C C   . ASP   A 1 21  ? -19.936 -3.493  -37.248 1.00 85.79  ? 64  ASP   A C   1 
ATOM   124  O O   . ASP   A 1 21  ? -19.799 -2.430  -37.866 1.00 86.03  ? 64  ASP   A O   1 
ATOM   125  C CB  . ASP   A 1 21  ? -21.310 -4.289  -39.211 1.00 87.16  ? 64  ASP   A CB  1 
ATOM   126  C CG  . ASP   A 1 21  ? -21.796 -5.431  -40.074 1.00 92.86  ? 64  ASP   A CG  1 
ATOM   127  O OD1 . ASP   A 1 21  ? -21.053 -6.431  -40.207 1.00 94.47  ? 64  ASP   A OD1 1 
ATOM   128  O OD2 . ASP   A 1 21  ? -22.922 -5.324  -40.624 1.00 94.72  ? 64  ASP   A OD2 1 
ATOM   129  N N   . ALA   A 1 22  ? -19.582 -3.640  -35.968 1.00 85.65  ? 65  ALA   A N   1 
ATOM   130  C CA  . ALA   A 1 22  ? -18.933 -2.579  -35.203 1.00 85.96  ? 65  ALA   A CA  1 
ATOM   131  C C   . ALA   A 1 22  ? -17.403 -2.602  -35.490 1.00 86.58  ? 65  ALA   A C   1 
ATOM   132  O O   . ALA   A 1 22  ? -16.906 -3.547  -36.112 1.00 86.57  ? 65  ALA   A O   1 
ATOM   133  C CB  . ALA   A 1 22  ? -19.208 -2.787  -33.715 1.00 85.85  ? 65  ALA   A CB  1 
ATOM   134  N N   . GLU   A 1 23  ? -16.662 -1.560  -35.070 1.00 86.83  ? 66  GLU   A N   1 
ATOM   135  C CA  . GLU   A 1 23  ? -15.214 -1.525  -35.260 1.00 87.22  ? 66  GLU   A CA  1 
ATOM   136  C C   . GLU   A 1 23  ? -14.591 -2.610  -34.379 1.00 86.27  ? 66  GLU   A C   1 
ATOM   137  O O   . GLU   A 1 23  ? -14.795 -2.583  -33.171 1.00 86.34  ? 66  GLU   A O   1 
ATOM   138  C CB  . GLU   A 1 23  ? -14.668 -0.154  -34.842 1.00 90.88  ? 66  GLU   A CB  1 
ATOM   139  C CG  . GLU   A 1 23  ? -13.222 0.069   -35.244 1.00 98.22  ? 66  GLU   A CG  1 
ATOM   140  C CD  . GLU   A 1 23  ? -12.557 1.255   -34.571 1.00 107.53 ? 66  GLU   A CD  1 
ATOM   141  O OE1 . GLU   A 1 23  ? -13.282 2.132   -34.047 1.00 109.06 ? 66  GLU   A OE1 1 
ATOM   142  O OE2 . GLU   A 1 23  ? -11.304 1.303   -34.567 1.00 110.65 ? 66  GLU   A OE2 1 
ATOM   143  N N   . VAL   A 1 24  ? -13.892 -3.590  -34.984 1.00 85.23  ? 67  VAL   A N   1 
ATOM   144  C CA  . VAL   A 1 24  ? -13.257 -4.701  -34.260 1.00 84.52  ? 67  VAL   A CA  1 
ATOM   145  C C   . VAL   A 1 24  ? -11.774 -4.423  -34.052 1.00 83.40  ? 67  VAL   A C   1 
ATOM   146  O O   . VAL   A 1 24  ? -10.992 -4.564  -34.989 1.00 83.60  ? 67  VAL   A O   1 
ATOM   147  C CB  . VAL   A 1 24  ? -13.451 -6.074  -34.956 1.00 85.28  ? 67  VAL   A CB  1 
ATOM   148  C CG1 . VAL   A 1 24  ? -13.071 -7.204  -34.018 1.00 85.86  ? 67  VAL   A CG1 1 
ATOM   149  C CG2 . VAL   A 1 24  ? -14.880 -6.260  -35.449 1.00 85.89  ? 67  VAL   A CG2 1 
ATOM   150  N N   . THR   A 1 25  ? -11.379 -4.031  -32.836 1.00 82.17  ? 68  THR   A N   1 
ATOM   151  C CA  . THR   A 1 25  ? -9.979  -3.720  -32.546 1.00 81.56  ? 68  THR   A CA  1 
ATOM   152  C C   . THR   A 1 25  ? -9.575  -4.177  -31.115 1.00 80.97  ? 68  THR   A C   1 
ATOM   153  O O   . THR   A 1 25  ? -10.404 -4.706  -30.382 1.00 80.83  ? 68  THR   A O   1 
ATOM   154  C CB  . THR   A 1 25  ? -9.724  -2.226  -32.832 1.00 82.52  ? 68  THR   A CB  1 
ATOM   155  O OG1 . THR   A 1 25  ? -8.319  -1.996  -32.888 1.00 83.32  ? 68  THR   A OG1 1 
ATOM   156  C CG2 . THR   A 1 25  ? -10.353 -1.330  -31.793 1.00 82.80  ? 68  THR   A CG2 1 
ATOM   157  N N   . GLY   A 1 26  ? -8.303  -4.020  -30.751 1.00 80.40  ? 69  GLY   A N   1 
ATOM   158  C CA  . GLY   A 1 26  ? -7.826  -4.400  -29.429 1.00 80.16  ? 69  GLY   A CA  1 
ATOM   159  C C   . GLY   A 1 26  ? -7.274  -5.808  -29.355 1.00 79.59  ? 69  GLY   A C   1 
ATOM   160  O O   . GLY   A 1 26  ? -7.830  -6.736  -29.946 1.00 79.77  ? 69  GLY   A O   1 
ATOM   161  N N   . ASN   A 1 27  ? -6.174  -5.977  -28.618 1.00 78.64  ? 70  ASN   A N   1 
ATOM   162  C CA  . ASN   A 1 27  ? -5.556  -7.287  -28.443 1.00 78.14  ? 70  ASN   A CA  1 
ATOM   163  C C   . ASN   A 1 27  ? -6.051  -7.994  -27.145 1.00 76.68  ? 70  ASN   A C   1 
ATOM   164  O O   . ASN   A 1 27  ? -6.771  -7.381  -26.358 1.00 76.87  ? 70  ASN   A O   1 
ATOM   165  C CB  . ASN   A 1 27  ? -4.020  -7.171  -28.525 1.00 79.84  ? 70  ASN   A CB  1 
ATOM   166  C CG  . ASN   A 1 27  ? -3.374  -6.481  -27.348 1.00 83.82  ? 70  ASN   A CG  1 
ATOM   167  O OD1 . ASN   A 1 27  ? -3.766  -5.385  -26.938 1.00 85.00  ? 70  ASN   A OD1 1 
ATOM   168  N ND2 . ASN   A 1 27  ? -2.352  -7.107  -26.782 1.00 84.82  ? 70  ASN   A ND2 1 
ATOM   169  N N   . SER   A 1 28  ? -5.715  -9.290  -26.952 1.00 75.00  ? 71  SER   A N   1 
ATOM   170  C CA  . SER   A 1 28  ? -6.138  -10.077 -25.779 1.00 73.76  ? 71  SER   A CA  1 
ATOM   171  C C   . SER   A 1 28  ? -4.926  -10.546 -24.967 1.00 72.61  ? 71  SER   A C   1 
ATOM   172  O O   . SER   A 1 28  ? -4.430  -11.652 -25.179 1.00 72.90  ? 71  SER   A O   1 
ATOM   173  C CB  . SER   A 1 28  ? -6.947  -11.301 -26.208 1.00 74.43  ? 71  SER   A CB  1 
ATOM   174  O OG  . SER   A 1 28  ? -7.810  -11.049 -27.302 1.00 76.02  ? 71  SER   A OG  1 
ATOM   175  N N   . PRO   A 1 29  ? -4.452  -9.742  -24.005 1.00 71.30  ? 72  PRO   A N   1 
ATOM   176  C CA  . PRO   A 1 29  ? -3.248  -10.137 -23.253 1.00 70.48  ? 72  PRO   A CA  1 
ATOM   177  C C   . PRO   A 1 29  ? -3.472  -10.860 -21.924 1.00 69.84  ? 72  PRO   A C   1 
ATOM   178  O O   . PRO   A 1 29  ? -4.401  -10.515 -21.194 1.00 70.47  ? 72  PRO   A O   1 
ATOM   179  C CB  . PRO   A 1 29  ? -2.532  -8.804  -23.040 1.00 71.20  ? 72  PRO   A CB  1 
ATOM   180  C CG  . PRO   A 1 29  ? -3.644  -7.755  -23.083 1.00 71.85  ? 72  PRO   A CG  1 
ATOM   181  C CD  . PRO   A 1 29  ? -4.893  -8.377  -23.657 1.00 70.49  ? 72  PRO   A CD  1 
ATOM   182  N N   . ARG   A 1 30  ? -2.592  -11.810 -21.572 1.00 68.66  ? 73  ARG   A N   1 
ATOM   183  C CA  . ARG   A 1 30  ? -2.698  -12.492 -20.277 1.00 68.34  ? 73  ARG   A CA  1 
ATOM   184  C C   . ARG   A 1 30  ? -1.700  -11.874 -19.293 1.00 66.33  ? 73  ARG   A C   1 
ATOM   185  O O   . ARG   A 1 30  ? -0.492  -11.992 -19.476 1.00 65.89  ? 73  ARG   A O   1 
ATOM   186  C CB  . ARG   A 1 30  ? -2.511  -14.005 -20.418 1.00 71.27  ? 73  ARG   A CB  1 
ATOM   187  C CG  . ARG   A 1 30  ? -3.616  -14.639 -21.248 1.00 77.12  ? 73  ARG   A CG  1 
ATOM   188  C CD  . ARG   A 1 30  ? -3.143  -15.893 -21.959 1.00 82.75  ? 73  ARG   A CD  1 
ATOM   189  N NE  . ARG   A 1 30  ? -4.135  -16.383 -22.921 1.00 87.69  ? 73  ARG   A NE  1 
ATOM   190  C CZ  . ARG   A 1 30  ? -5.105  -17.244 -22.623 1.00 91.14  ? 73  ARG   A CZ  1 
ATOM   191  N NH1 . ARG   A 1 30  ? -5.224  -17.724 -21.388 1.00 91.89  ? 73  ARG   A NH1 1 
ATOM   192  N NH2 . ARG   A 1 30  ? -5.964  -17.634 -23.557 1.00 90.70  ? 73  ARG   A NH2 1 
ATOM   193  N N   . LEU   A 1 31  ? -2.212  -11.163 -18.278 1.00 64.75  ? 74  LEU   A N   1 
ATOM   194  C CA  . LEU   A 1 31  ? -1.374  -10.452 -17.325 1.00 63.51  ? 74  LEU   A CA  1 
ATOM   195  C C   . LEU   A 1 31  ? -1.534  -10.938 -15.889 1.00 62.24  ? 74  LEU   A C   1 
ATOM   196  O O   . LEU   A 1 31  ? -2.650  -10.965 -15.378 1.00 62.50  ? 74  LEU   A O   1 
ATOM   197  C CB  . LEU   A 1 31  ? -1.706  -8.951  -17.391 1.00 63.58  ? 74  LEU   A CB  1 
ATOM   198  C CG  . LEU   A 1 31  ? -1.508  -8.308  -18.753 1.00 65.11  ? 74  LEU   A CG  1 
ATOM   199  C CD1 . LEU   A 1 31  ? -2.070  -6.915  -18.793 1.00 65.43  ? 74  LEU   A CD1 1 
ATOM   200  C CD2 . LEU   A 1 31  ? -0.044  -8.309  -19.144 1.00 66.02  ? 74  LEU   A CD2 1 
ATOM   201  N N   . ASP   A 1 32  ? -0.410  -11.252 -15.219 1.00 60.43  ? 75  ASP   A N   1 
ATOM   202  C CA  . ASP   A 1 32  ? -0.401  -11.654 -13.818 1.00 59.18  ? 75  ASP   A CA  1 
ATOM   203  C C   . ASP   A 1 32  ? -0.488  -10.386 -12.996 1.00 57.03  ? 75  ASP   A C   1 
ATOM   204  O O   . ASP   A 1 32  ? 0.460   -9.602  -13.000 1.00 57.29  ? 75  ASP   A O   1 
ATOM   205  C CB  . ASP   A 1 32  ? 0.910   -12.379 -13.478 1.00 61.60  ? 75  ASP   A CB  1 
ATOM   206  C CG  . ASP   A 1 32  ? 1.065   -13.726 -14.151 1.00 66.98  ? 75  ASP   A CG  1 
ATOM   207  O OD1 . ASP   A 1 32  ? 0.032   -14.307 -14.563 1.00 68.02  ? 75  ASP   A OD1 1 
ATOM   208  O OD2 . ASP   A 1 32  ? 2.218   -14.207 -14.260 1.00 69.20  ? 75  ASP   A OD2 1 
ATOM   209  N N   . VAL   A 1 33  ? -1.626  -10.158 -12.317 1.00 54.68  ? 76  VAL   A N   1 
ATOM   210  C CA  . VAL   A 1 33  ? -1.829  -8.939  -11.537 1.00 52.93  ? 76  VAL   A CA  1 
ATOM   211  C C   . VAL   A 1 33  ? -2.127  -9.225  -10.031 1.00 51.67  ? 76  VAL   A C   1 
ATOM   212  O O   . VAL   A 1 33  ? -2.169  -10.390 -9.611  1.00 51.42  ? 76  VAL   A O   1 
ATOM   213  C CB  . VAL   A 1 33  ? -2.911  -8.035  -12.207 1.00 52.97  ? 76  VAL   A CB  1 
ATOM   214  C CG1 . VAL   A 1 33  ? -2.470  -7.561  -13.581 1.00 53.33  ? 76  VAL   A CG1 1 
ATOM   215  C CG2 . VAL   A 1 33  ? -4.260  -8.736  -12.278 1.00 53.07  ? 76  VAL   A CG2 1 
ATOM   216  N N   . ALA   A 1 34  ? -2.248  -8.144  -9.215  1.00 50.34  ? 77  ALA   A N   1 
ATOM   217  C CA  . ALA   A 1 34  ? -2.554  -8.167  -7.791  1.00 49.37  ? 77  ALA   A CA  1 
ATOM   218  C C   . ALA   A 1 34  ? -3.493  -7.004  -7.483  1.00 48.57  ? 77  ALA   A C   1 
ATOM   219  O O   . ALA   A 1 34  ? -3.306  -5.905  -8.005  1.00 48.95  ? 77  ALA   A O   1 
ATOM   220  C CB  . ALA   A 1 34  ? -1.290  -8.016  -6.984  1.00 49.23  ? 77  ALA   A CB  1 
ATOM   221  N N   . LEU   A 1 35  ? -4.501  -7.238  -6.649  1.00 47.19  ? 78  LEU   A N   1 
ATOM   222  C CA  . LEU   A 1 35  ? -5.455  -6.196  -6.283  1.00 46.24  ? 78  LEU   A CA  1 
ATOM   223  C C   . LEU   A 1 35  ? -5.265  -5.801  -4.807  1.00 45.92  ? 78  LEU   A C   1 
ATOM   224  O O   . LEU   A 1 35  ? -5.408  -6.646  -3.918  1.00 45.71  ? 78  LEU   A O   1 
ATOM   225  C CB  . LEU   A 1 35  ? -6.881  -6.687  -6.542  1.00 45.56  ? 78  LEU   A CB  1 
ATOM   226  C CG  . LEU   A 1 35  ? -7.976  -5.666  -6.306  1.00 46.09  ? 78  LEU   A CG  1 
ATOM   227  C CD1 . LEU   A 1 35  ? -7.912  -4.572  -7.327  1.00 46.60  ? 78  LEU   A CD1 1 
ATOM   228  C CD2 . LEU   A 1 35  ? -9.333  -6.316  -6.366  1.00 46.22  ? 78  LEU   A CD2 1 
ATOM   229  N N   . ASP   A 1 36  ? -4.910  -4.533  -4.546  1.00 45.51  ? 79  ASP   A N   1 
ATOM   230  C CA  . ASP   A 1 36  ? -4.713  -4.075  -3.168  1.00 45.40  ? 79  ASP   A CA  1 
ATOM   231  C C   . ASP   A 1 36  ? -6.053  -3.716  -2.484  1.00 45.08  ? 79  ASP   A C   1 
ATOM   232  O O   . ASP   A 1 36  ? -7.096  -3.674  -3.145  1.00 44.80  ? 79  ASP   A O   1 
ATOM   233  C CB  . ASP   A 1 36  ? -3.668  -2.931  -3.086  1.00 46.77  ? 79  ASP   A CB  1 
ATOM   234  C CG  . ASP   A 1 36  ? -4.160  -1.562  -3.507  1.00 50.43  ? 79  ASP   A CG  1 
ATOM   235  O OD1 . ASP   A 1 36  ? -5.320  -1.460  -3.939  1.00 51.28  ? 79  ASP   A OD1 1 
ATOM   236  O OD2 . ASP   A 1 36  ? -3.385  -0.590  -3.392  1.00 51.96  ? 79  ASP   A OD2 1 
ATOM   237  N N   . GLU   A 1 37  ? -6.015  -3.446  -1.169  1.00 44.62  ? 80  GLU   A N   1 
ATOM   238  C CA  . GLU   A 1 37  ? -7.191  -3.098  -0.379  1.00 44.75  ? 80  GLU   A CA  1 
ATOM   239  C C   . GLU   A 1 37  ? -7.936  -1.862  -0.930  1.00 44.71  ? 80  GLU   A C   1 
ATOM   240  O O   . GLU   A 1 37  ? -9.119  -1.705  -0.678  1.00 44.97  ? 80  GLU   A O   1 
ATOM   241  C CB  . GLU   A 1 37  ? -6.771  -2.865  1.082   1.00 47.06  ? 80  GLU   A CB  1 
ATOM   242  C CG  . GLU   A 1 37  ? -7.830  -3.247  2.101   1.00 52.17  ? 80  GLU   A CG  1 
ATOM   243  C CD  . GLU   A 1 37  ? -7.695  -2.538  3.432   1.00 57.22  ? 80  GLU   A CD  1 
ATOM   244  O OE1 . GLU   A 1 37  ? -8.113  -1.361  3.526   1.00 58.87  ? 80  GLU   A OE1 1 
ATOM   245  O OE2 . GLU   A 1 37  ? -7.162  -3.155  4.381   1.00 59.85  ? 80  GLU   A OE2 1 
ATOM   246  N N   . SER   A 1 38  ? -7.251  -0.996  -1.686  1.00 43.93  ? 81  SER   A N   1 
ATOM   247  C CA  . SER   A 1 38  ? -7.850  0.198   -2.275  1.00 43.33  ? 81  SER   A CA  1 
ATOM   248  C C   . SER   A 1 38  ? -8.473  -0.037  -3.657  1.00 42.86  ? 81  SER   A C   1 
ATOM   249  O O   . SER   A 1 38  ? -8.839  0.940   -4.316  1.00 43.46  ? 81  SER   A O   1 
ATOM   250  C CB  . SER   A 1 38  ? -6.807  1.304   -2.397  1.00 44.40  ? 81  SER   A CB  1 
ATOM   251  O OG  . SER   A 1 38  ? -6.191  1.565   -1.147  1.00 47.38  ? 81  SER   A OG  1 
ATOM   252  N N   . GLY   A 1 39  ? -8.566  -1.291  -4.105  1.00 41.52  ? 82  GLY   A N   1 
ATOM   253  C CA  . GLY   A 1 39  ? -9.113  -1.605  -5.420  1.00 40.95  ? 82  GLY   A CA  1 
ATOM   254  C C   . GLY   A 1 39  ? -8.227  -1.158  -6.568  1.00 40.52  ? 82  GLY   A C   1 
ATOM   255  O O   . GLY   A 1 39  ? -8.702  -0.925  -7.677  1.00 40.39  ? 82  GLY   A O   1 
ATOM   256  N N   . ASP   A 1 40  ? -6.929  -1.048  -6.306  1.00 40.17  ? 83  ASP   A N   1 
ATOM   257  C CA  . ASP   A 1 40  ? -5.937  -0.640  -7.276  1.00 40.14  ? 83  ASP   A CA  1 
ATOM   258  C C   . ASP   A 1 40  ? -5.136  -1.856  -7.710  1.00 40.50  ? 83  ASP   A C   1 
ATOM   259  O O   . ASP   A 1 40  ? -4.595  -2.580  -6.864  1.00 40.22  ? 83  ASP   A O   1 
ATOM   260  C CB  . ASP   A 1 40  ? -5.024  0.434   -6.666  1.00 40.48  ? 83  ASP   A CB  1 
ATOM   261  C CG  . ASP   A 1 40  ? -5.746  1.748   -6.492  1.00 41.73  ? 83  ASP   A CG  1 
ATOM   262  O OD1 . ASP   A 1 40  ? -6.499  2.118   -7.388  1.00 41.72  ? 83  ASP   A OD1 1 
ATOM   263  O OD2 . ASP   A 1 40  ? -5.543  2.406   -5.456  1.00 43.37  ? 83  ASP   A OD2 1 
ATOM   264  N N   . PHE   A 1 41  ? -5.089  -2.087  -9.027  1.00 40.67  ? 84  PHE   A N   1 
ATOM   265  C CA  . PHE   A 1 41  ? -4.371  -3.194  -9.636  1.00 41.55  ? 84  PHE   A CA  1 
ATOM   266  C C   . PHE   A 1 41  ? -2.885  -2.869  -9.819  1.00 44.23  ? 84  PHE   A C   1 
ATOM   267  O O   . PHE   A 1 41  ? -2.497  -1.708  -9.942  1.00 44.30  ? 84  PHE   A O   1 
ATOM   268  C CB  . PHE   A 1 41  ? -4.996  -3.553  -10.992 1.00 40.44  ? 84  PHE   A CB  1 
ATOM   269  C CG  . PHE   A 1 41  ? -6.303  -4.302  -10.918 1.00 40.07  ? 84  PHE   A CG  1 
ATOM   270  C CD1 . PHE   A 1 41  ? -6.327  -5.661  -10.669 1.00 40.32  ? 84  PHE   A CD1 1 
ATOM   271  C CD2 . PHE   A 1 41  ? -7.509  -3.648  -11.114 1.00 40.26  ? 84  PHE   A CD2 1 
ATOM   272  C CE1 . PHE   A 1 41  ? -7.532  -6.347  -10.605 1.00 40.67  ? 84  PHE   A CE1 1 
ATOM   273  C CE2 . PHE   A 1 41  ? -8.712  -4.340  -11.055 1.00 40.40  ? 84  PHE   A CE2 1 
ATOM   274  C CZ  . PHE   A 1 41  ? -8.716  -5.683  -10.807 1.00 40.03  ? 84  PHE   A CZ  1 
ATOM   275  N N   . SER   A 1 42  ? -2.059  -3.900  -9.853  1.00 46.51  ? 85  SER   A N   1 
ATOM   276  C CA  . SER   A 1 42  ? -0.621  -3.746  -10.043 1.00 49.43  ? 85  SER   A CA  1 
ATOM   277  C C   . SER   A 1 42  ? -0.076  -4.982  -10.750 1.00 52.71  ? 85  SER   A C   1 
ATOM   278  O O   . SER   A 1 42  ? -0.561  -6.086  -10.482 1.00 53.31  ? 85  SER   A O   1 
ATOM   279  C CB  . SER   A 1 42  ? 0.080   -3.568  -8.698  1.00 50.24  ? 85  SER   A CB  1 
ATOM   280  O OG  . SER   A 1 42  ? -0.130  -4.676  -7.839  1.00 51.82  ? 85  SER   A OG  1 
ATOM   281  N N   . LEU   A 1 43  ? 0.900   -4.813  -11.661 1.00 54.54  ? 86  LEU   A N   1 
ATOM   282  C CA  . LEU   A 1 43  ? 1.469   -5.975  -12.336 1.00 57.12  ? 86  LEU   A CA  1 
ATOM   283  C C   . LEU   A 1 43  ? 2.379   -6.712  -11.378 1.00 60.10  ? 86  LEU   A C   1 
ATOM   284  O O   . LEU   A 1 43  ? 3.178   -6.089  -10.681 1.00 60.32  ? 86  LEU   A O   1 
ATOM   285  C CB  . LEU   A 1 43  ? 2.258   -5.595  -13.591 1.00 57.24  ? 86  LEU   A CB  1 
ATOM   286  C CG  . LEU   A 1 43  ? 1.469   -5.072  -14.780 1.00 59.05  ? 86  LEU   A CG  1 
ATOM   287  C CD1 . LEU   A 1 43  ? 2.393   -4.777  -15.938 1.00 59.62  ? 86  LEU   A CD1 1 
ATOM   288  C CD2 . LEU   A 1 43  ? 0.407   -6.049  -15.226 1.00 59.75  ? 86  LEU   A CD2 1 
ATOM   289  N N   . VAL   A 1 44  ? 2.260   -8.043  -11.349 1.00 62.23  ? 87  VAL   A N   1 
ATOM   290  C CA  . VAL   A 1 44  ? 3.091   -8.942  -10.542 1.00 64.21  ? 87  VAL   A CA  1 
ATOM   291  C C   . VAL   A 1 44  ? 4.196   -9.461  -11.442 1.00 66.77  ? 87  VAL   A C   1 
ATOM   292  O O   . VAL   A 1 44  ? 3.929   -9.820  -12.594 1.00 67.34  ? 87  VAL   A O   1 
ATOM   293  C CB  . VAL   A 1 44  ? 2.239   -10.118 -10.005 1.00 64.69  ? 87  VAL   A CB  1 
ATOM   294  C CG1 . VAL   A 1 44  ? 3.104   -11.244 -9.453  1.00 65.29  ? 87  VAL   A CG1 1 
ATOM   295  C CG2 . VAL   A 1 44  ? 1.252   -9.635  -8.961  1.00 65.07  ? 87  VAL   A CG2 1 
ATOM   296  N N   . GLU   A 1 45  ? 5.435   -9.477  -10.950 1.00 68.25  ? 88  GLU   A N   1 
ATOM   297  C CA  . GLU   A 1 45  ? 6.551   -10.003 -11.731 1.00 70.34  ? 88  GLU   A CA  1 
ATOM   298  C C   . GLU   A 1 45  ? 7.512   -10.779 -10.812 1.00 71.12  ? 88  GLU   A C   1 
ATOM   299  O O   . GLU   A 1 45  ? 7.813   -11.950 -11.057 1.00 71.49  ? 88  GLU   A O   1 
ATOM   300  C CB  . GLU   A 1 45  ? 7.291   -8.884  -12.497 1.00 73.98  ? 88  GLU   A CB  1 
ATOM   301  C CG  . GLU   A 1 45  ? 6.431   -8.020  -13.411 1.00 79.62  ? 88  GLU   A CG  1 
ATOM   302  C CD  . GLU   A 1 45  ? 6.435   -8.404  -14.878 1.00 86.13  ? 88  GLU   A CD  1 
ATOM   303  O OE1 . GLU   A 1 45  ? 7.486   -8.875  -15.376 1.00 87.28  ? 88  GLU   A OE1 1 
ATOM   304  O OE2 . GLU   A 1 45  ? 5.378   -8.231  -15.530 1.00 87.42  ? 88  GLU   A OE2 1 
ATOM   305  N N   . GLY   B 2 7   ? -36.373 12.351  -11.694 1.00 56.68  ? 16  GLY   B N   1 
ATOM   306  C CA  . GLY   B 2 7   ? -35.779 12.701  -12.980 1.00 57.13  ? 16  GLY   B CA  1 
ATOM   307  C C   . GLY   B 2 7   ? -35.914 11.634  -14.055 1.00 57.12  ? 16  GLY   B C   1 
ATOM   308  O O   . GLY   B 2 7   ? -36.999 11.066  -14.237 1.00 57.96  ? 16  GLY   B O   1 
ATOM   309  N N   . GLU   B 2 8   ? -34.823 11.373  -14.803 1.00 55.57  ? 17  GLU   B N   1 
ATOM   310  C CA  . GLU   B 2 8   ? -34.860 10.353  -15.841 1.00 54.53  ? 17  GLU   B CA  1 
ATOM   311  C C   . GLU   B 2 8   ? -34.309 9.037   -15.316 1.00 52.96  ? 17  GLU   B C   1 
ATOM   312  O O   . GLU   B 2 8   ? -33.152 8.971   -14.891 1.00 53.08  ? 17  GLU   B O   1 
ATOM   313  C CB  . GLU   B 2 8   ? -34.092 10.783  -17.089 1.00 57.21  ? 17  GLU   B CB  1 
ATOM   314  C CG  . GLU   B 2 8   ? -34.276 9.805   -18.237 1.00 62.12  ? 17  GLU   B CG  1 
ATOM   315  C CD  . GLU   B 2 8   ? -33.547 10.181  -19.508 1.00 68.92  ? 17  GLU   B CD  1 
ATOM   316  O OE1 . GLU   B 2 8   ? -32.507 10.872  -19.410 1.00 70.35  ? 17  GLU   B OE1 1 
ATOM   317  O OE2 . GLU   B 2 8   ? -34.025 9.802   -20.604 1.00 71.03  ? 17  GLU   B OE2 1 
ATOM   318  N N   A THR   B 2 9   ? -35.129 7.982   -15.339 0.50 52.15  ? 18  THR   B N   1 
ATOM   319  N N   B THR   B 2 9   ? -35.138 7.993   -15.342 0.50 52.15  ? 18  THR   B N   1 
ATOM   320  C CA  A THR   B 2 9   ? -34.686 6.670   -14.855 0.50 51.84  ? 18  THR   B CA  1 
ATOM   321  C CA  B THR   B 2 9   ? -34.765 6.664   -14.860 0.50 51.85  ? 18  THR   B CA  1 
ATOM   322  C C   A THR   B 2 9   ? -34.850 5.578   -15.935 0.50 51.11  ? 18  THR   B C   1 
ATOM   323  C C   B THR   B 2 9   ? -34.862 5.582   -15.937 0.50 51.12  ? 18  THR   B C   1 
ATOM   324  O O   A THR   B 2 9   ? -34.925 4.394   -15.608 0.50 51.28  ? 18  THR   B O   1 
ATOM   325  O O   B THR   B 2 9   ? -34.919 4.402   -15.597 0.50 51.29  ? 18  THR   B O   1 
ATOM   326  C CB  A THR   B 2 9   ? -35.357 6.307   -13.501 0.50 53.40  ? 18  THR   B CB  1 
ATOM   327  C CB  B THR   B 2 9   ? -35.640 6.279   -13.658 0.50 53.39  ? 18  THR   B CB  1 
ATOM   328  O OG1 A THR   B 2 9   ? -35.565 7.484   -12.706 0.50 54.58  ? 18  THR   B OG1 1 
ATOM   329  O OG1 B THR   B 2 9   ? -37.019 6.504   -13.982 0.50 54.45  ? 18  THR   B OG1 1 
ATOM   330  C CG2 A THR   B 2 9   ? -34.537 5.313   -12.687 0.50 53.76  ? 18  THR   B CG2 1 
ATOM   331  C CG2 B THR   B 2 9   ? -35.262 7.042   -12.391 0.50 53.86  ? 18  THR   B CG2 1 
ATOM   332  N N   . THR   B 2 10  ? -34.884 5.969   -17.221 1.00 50.25  ? 19  THR   B N   1 
ATOM   333  C CA  . THR   B 2 10  ? -35.006 5.034   -18.337 1.00 49.09  ? 19  THR   B CA  1 
ATOM   334  C C   . THR   B 2 10  ? -33.737 4.190   -18.445 1.00 47.49  ? 19  THR   B C   1 
ATOM   335  O O   . THR   B 2 10  ? -32.638 4.713   -18.251 1.00 47.42  ? 19  THR   B O   1 
ATOM   336  C CB  . THR   B 2 10  ? -35.241 5.824   -19.649 1.00 50.43  ? 19  THR   B CB  1 
ATOM   337  O OG1 . THR   B 2 10  ? -36.310 6.762   -19.477 1.00 51.93  ? 19  THR   B OG1 1 
ATOM   338  C CG2 . THR   B 2 10  ? -35.537 4.924   -20.835 1.00 50.60  ? 19  THR   B CG2 1 
ATOM   339  N N   . ASP   B 2 11  ? -33.874 2.892   -18.763 1.00 46.04  ? 20  ASP   B N   1 
ATOM   340  C CA  . ASP   B 2 11  ? -32.719 2.012   -18.937 1.00 45.38  ? 20  ASP   B CA  1 
ATOM   341  C C   . ASP   B 2 11  ? -31.799 2.560   -20.048 1.00 44.70  ? 20  ASP   B C   1 
ATOM   342  O O   . ASP   B 2 11  ? -32.288 3.100   -21.044 1.00 44.92  ? 20  ASP   B O   1 
ATOM   343  C CB  . ASP   B 2 11  ? -33.167 0.588   -19.328 1.00 46.95  ? 20  ASP   B CB  1 
ATOM   344  C CG  . ASP   B 2 11  ? -33.700 -0.280  -18.206 1.00 50.85  ? 20  ASP   B CG  1 
ATOM   345  O OD1 . ASP   B 2 11  ? -34.063 0.271   -17.156 1.00 51.64  ? 20  ASP   B OD1 1 
ATOM   346  O OD2 . ASP   B 2 11  ? -33.765 -1.514  -18.390 1.00 52.72  ? 20  ASP   B OD2 1 
ATOM   347  N N   . GLY   B 2 12  ? -30.493 2.437   -19.860 1.00 43.37  ? 21  GLY   B N   1 
ATOM   348  C CA  . GLY   B 2 12  ? -29.536 2.915   -20.844 1.00 42.29  ? 21  GLY   B CA  1 
ATOM   349  C C   . GLY   B 2 12  ? -28.204 3.293   -20.243 1.00 41.26  ? 21  GLY   B C   1 
ATOM   350  O O   . GLY   B 2 12  ? -27.952 3.043   -19.065 1.00 41.42  ? 21  GLY   B O   1 
ATOM   351  N N   . VAL   B 2 13  ? -27.323 3.865   -21.062 1.00 40.09  ? 22  VAL   B N   1 
ATOM   352  C CA  . VAL   B 2 13  ? -25.998 4.286   -20.618 1.00 39.21  ? 22  VAL   B CA  1 
ATOM   353  C C   . VAL   B 2 13  ? -25.987 5.804   -20.423 1.00 38.58  ? 22  VAL   B C   1 
ATOM   354  O O   . VAL   B 2 13  ? -26.649 6.520   -21.164 1.00 39.01  ? 22  VAL   B O   1 
ATOM   355  C CB  . VAL   B 2 13  ? -24.871 3.745   -21.531 1.00 39.42  ? 22  VAL   B CB  1 
ATOM   356  C CG1 . VAL   B 2 13  ? -25.073 4.147   -22.988 1.00 39.94  ? 22  VAL   B CG1 1 
ATOM   357  C CG2 . VAL   B 2 13  ? -23.502 4.158   -21.030 1.00 39.43  ? 22  VAL   B CG2 1 
ATOM   358  N N   . TYR   B 2 14  ? -25.368 6.281   -19.341 1.00 37.74  ? 23  TYR   B N   1 
ATOM   359  C CA  . TYR   B 2 14  ? -25.388 7.697   -18.995 1.00 37.27  ? 23  TYR   B CA  1 
ATOM   360  C C   . TYR   B 2 14  ? -23.997 8.264   -18.734 1.00 37.57  ? 23  TYR   B C   1 
ATOM   361  O O   . TYR   B 2 14  ? -23.125 7.551   -18.267 1.00 38.06  ? 23  TYR   B O   1 
ATOM   362  C CB  . TYR   B 2 14  ? -26.227 7.905   -17.720 1.00 36.31  ? 23  TYR   B CB  1 
ATOM   363  C CG  . TYR   B 2 14  ? -27.718 7.729   -17.900 1.00 35.93  ? 23  TYR   B CG  1 
ATOM   364  C CD1 . TYR   B 2 14  ? -28.266 6.475   -18.120 1.00 36.54  ? 23  TYR   B CD1 1 
ATOM   365  C CD2 . TYR   B 2 14  ? -28.592 8.789   -17.697 1.00 36.47  ? 23  TYR   B CD2 1 
ATOM   366  C CE1 . TYR   B 2 14  ? -29.634 6.302   -18.276 1.00 37.54  ? 23  TYR   B CE1 1 
ATOM   367  C CE2 . TYR   B 2 14  ? -29.969 8.624   -17.811 1.00 37.36  ? 23  TYR   B CE2 1 
ATOM   368  C CZ  . TYR   B 2 14  ? -30.488 7.374   -18.099 1.00 38.50  ? 23  TYR   B CZ  1 
ATOM   369  O OH  . TYR   B 2 14  ? -31.841 7.175   -18.227 1.00 39.67  ? 23  TYR   B OH  1 
ATOM   370  N N   . ARG   B 2 15  ? -23.814 9.561   -18.967 1.00 37.11  ? 24  ARG   B N   1 
ATOM   371  C CA  . ARG   B 2 15  ? -22.564 10.252  -18.672 1.00 37.19  ? 24  ARG   B CA  1 
ATOM   372  C C   . ARG   B 2 15  ? -22.671 10.817  -17.261 1.00 37.63  ? 24  ARG   B C   1 
ATOM   373  O O   . ARG   B 2 15  ? -23.736 11.258  -16.841 1.00 37.69  ? 24  ARG   B O   1 
ATOM   374  C CB  . ARG   B 2 15  ? -22.326 11.426  -19.650 1.00 37.73  ? 24  ARG   B CB  1 
ATOM   375  C CG  . ARG   B 2 15  ? -22.283 11.066  -21.129 1.00 38.05  ? 24  ARG   B CG  1 
ATOM   376  C CD  . ARG   B 2 15  ? -22.124 12.332  -21.961 1.00 39.62  ? 24  ARG   B CD  1 
ATOM   377  N NE  . ARG   B 2 15  ? -22.316 12.096  -23.398 1.00 40.17  ? 24  ARG   B NE  1 
ATOM   378  C CZ  . ARG   B 2 15  ? -21.337 11.792  -24.246 1.00 41.44  ? 24  ARG   B CZ  1 
ATOM   379  N NH1 . ARG   B 2 15  ? -20.084 11.687  -23.817 1.00 41.18  ? 24  ARG   B NH1 1 
ATOM   380  N NH2 . ARG   B 2 15  ? -21.604 11.579  -25.530 1.00 40.63  ? 24  ARG   B NH2 1 
ATOM   381  N N   . VAL   B 2 16  ? -21.571 10.809  -16.536 1.00 37.73  ? 25  VAL   B N   1 
ATOM   382  C CA  . VAL   B 2 16  ? -21.475 11.348  -15.187 1.00 38.18  ? 25  VAL   B CA  1 
ATOM   383  C C   . VAL   B 2 16  ? -20.635 12.615  -15.325 1.00 38.98  ? 25  VAL   B C   1 
ATOM   384  O O   . VAL   B 2 16  ? -19.449 12.553  -15.667 1.00 38.59  ? 25  VAL   B O   1 
ATOM   385  C CB  . VAL   B 2 16  ? -20.838 10.334  -14.185 1.00 38.28  ? 25  VAL   B CB  1 
ATOM   386  C CG1 . VAL   B 2 16  ? -20.828 10.902  -12.772 1.00 38.39  ? 25  VAL   B CG1 1 
ATOM   387  C CG2 . VAL   B 2 16  ? -21.552 8.978   -14.226 1.00 38.27  ? 25  VAL   B CG2 1 
ATOM   388  N N   . MET   B 2 17  ? -21.268 13.769  -15.135 1.00 39.98  ? 26  MET   B N   1 
ATOM   389  C CA  . MET   B 2 17  ? -20.594 15.050  -15.304 1.00 41.61  ? 26  MET   B CA  1 
ATOM   390  C C   . MET   B 2 17  ? -20.443 15.809  -13.977 1.00 44.22  ? 26  MET   B C   1 
ATOM   391  O O   . MET   B 2 17  ? -21.091 15.478  -12.993 1.00 44.64  ? 26  MET   B O   1 
ATOM   392  C CB  . MET   B 2 17  ? -21.391 15.931  -16.281 1.00 41.68  ? 26  MET   B CB  1 
ATOM   393  C CG  . MET   B 2 17  ? -21.988 15.217  -17.453 1.00 42.66  ? 26  MET   B CG  1 
ATOM   394  S SD  . MET   B 2 17  ? -20.755 14.940  -18.719 1.00 44.20  ? 26  MET   B SD  1 
ATOM   395  C CE  . MET   B 2 17  ? -20.276 16.667  -19.087 1.00 40.61  ? 26  MET   B CE  1 
ATOM   396  N N   . THR   B 2 18  ? -19.617 16.855  -13.965 1.00 46.07  ? 27  THR   B N   1 
ATOM   397  C CA  . THR   B 2 18  ? -19.439 17.713  -12.805 1.00 48.34  ? 27  THR   B CA  1 
ATOM   398  C C   . THR   B 2 18  ? -19.197 19.162  -13.261 1.00 50.86  ? 27  THR   B C   1 
ATOM   399  O O   . THR   B 2 18  ? -18.502 19.399  -14.251 1.00 50.77  ? 27  THR   B O   1 
ATOM   400  C CB  . THR   B 2 18  ? -18.343 17.172  -11.856 1.00 49.22  ? 27  THR   B CB  1 
ATOM   401  O OG1 . THR   B 2 18  ? -18.135 18.107  -10.792 1.00 50.18  ? 27  THR   B OG1 1 
ATOM   402  C CG2 . THR   B 2 18  ? -17.029 16.905  -12.565 1.00 49.24  ? 27  THR   B CG2 1 
ATOM   403  N N   . ARG   B 2 19  ? -19.800 20.124  -12.562 1.00 52.92  ? 28  ARG   B N   1 
ATOM   404  C CA  . ARG   B 2 19  ? -19.580 21.541  -12.870 1.00 55.44  ? 28  ARG   B CA  1 
ATOM   405  C C   . ARG   B 2 19  ? -18.623 22.236  -11.852 1.00 57.15  ? 28  ARG   B C   1 
ATOM   406  O O   . ARG   B 2 19  ? -18.500 23.462  -11.846 1.00 57.15  ? 28  ARG   B O   1 
ATOM   407  C CB  . ARG   B 2 19  ? -20.915 22.293  -12.992 1.00 57.43  ? 28  ARG   B CB  1 
ATOM   408  C CG  . ARG   B 2 19  ? -21.693 21.956  -14.260 1.00 61.30  ? 28  ARG   B CG  1 
ATOM   409  C CD  . ARG   B 2 19  ? -22.653 23.072  -14.624 1.00 65.70  ? 28  ARG   B CD  1 
ATOM   410  N NE  . ARG   B 2 19  ? -23.754 22.614  -15.474 1.00 69.96  ? 28  ARG   B NE  1 
ATOM   411  C CZ  . ARG   B 2 19  ? -24.929 22.189  -15.017 1.00 72.94  ? 28  ARG   B CZ  1 
ATOM   412  N NH1 . ARG   B 2 19  ? -25.166 22.147  -13.709 1.00 73.06  ? 28  ARG   B NH1 1 
ATOM   413  N NH2 . ARG   B 2 19  ? -25.874 21.793  -15.863 1.00 72.83  ? 28  ARG   B NH2 1 
ATOM   414  N N   . ARG   B 2 20  ? -17.939 21.434  -11.016 1.00 58.46  ? 29  ARG   B N   1 
ATOM   415  C CA  . ARG   B 2 20  ? -16.997 21.857  -9.974  1.00 60.01  ? 29  ARG   B CA  1 
ATOM   416  C C   . ARG   B 2 20  ? -15.714 22.495  -10.563 1.00 60.21  ? 29  ARG   B C   1 
ATOM   417  O O   . ARG   B 2 20  ? -15.034 23.264  -9.883  1.00 60.23  ? 29  ARG   B O   1 
ATOM   418  C CB  . ARG   B 2 20  ? -16.676 20.638  -9.076  1.00 62.45  ? 29  ARG   B CB  1 
ATOM   419  C CG  . ARG   B 2 20  ? -15.863 20.918  -7.813  1.00 67.27  ? 29  ARG   B CG  1 
ATOM   420  C CD  . ARG   B 2 20  ? -15.491 19.635  -7.069  1.00 71.83  ? 29  ARG   B CD  1 
ATOM   421  N NE  . ARG   B 2 20  ? -14.855 18.634  -7.935  1.00 75.82  ? 29  ARG   B NE  1 
ATOM   422  C CZ  . ARG   B 2 20  ? -13.541 18.512  -8.104  1.00 78.78  ? 29  ARG   B CZ  1 
ATOM   423  N NH1 . ARG   B 2 20  ? -12.703 19.323  -7.470  1.00 79.02  ? 29  ARG   B NH1 1 
ATOM   424  N NH2 . ARG   B 2 20  ? -13.056 17.584  -8.921  1.00 78.45  ? 29  ARG   B NH2 1 
ATOM   425  N N   . LEU   B 2 21  ? -15.404 22.196  -11.832 1.00 60.14  ? 30  LEU   B N   1 
ATOM   426  C CA  . LEU   B 2 21  ? -14.238 22.755  -12.499 1.00 60.41  ? 30  LEU   B CA  1 
ATOM   427  C C   . LEU   B 2 21  ? -14.639 23.721  -13.647 1.00 59.88  ? 30  LEU   B C   1 
ATOM   428  O O   . LEU   B 2 21  ? -15.739 24.286  -13.623 1.00 60.11  ? 30  LEU   B O   1 
ATOM   429  C CB  . LEU   B 2 21  ? -13.300 21.624  -12.960 1.00 60.95  ? 30  LEU   B CB  1 
ATOM   430  C CG  . LEU   B 2 21  ? -12.105 21.408  -12.057 1.00 62.80  ? 30  LEU   B CG  1 
ATOM   431  C CD1 . LEU   B 2 21  ? -12.270 20.149  -11.239 1.00 63.31  ? 30  LEU   B CD1 1 
ATOM   432  C CD2 . LEU   B 2 21  ? -10.817 21.395  -12.861 1.00 63.63  ? 30  LEU   B CD2 1 
ATOM   433  N N   . LEU   B 2 22  ? -13.724 23.971  -14.597 1.00 58.73  ? 31  LEU   B N   1 
ATOM   434  C CA  . LEU   B 2 22  ? -13.959 24.845  -15.730 1.00 57.87  ? 31  LEU   B CA  1 
ATOM   435  C C   . LEU   B 2 22  ? -14.922 24.154  -16.677 1.00 57.39  ? 31  LEU   B C   1 
ATOM   436  O O   . LEU   B 2 22  ? -14.655 23.037  -17.127 1.00 57.53  ? 31  LEU   B O   1 
ATOM   437  C CB  . LEU   B 2 22  ? -12.638 25.083  -16.432 1.00 57.50  ? 31  LEU   B CB  1 
ATOM   438  C CG  . LEU   B 2 22  ? -12.673 26.157  -17.454 1.00 57.97  ? 31  LEU   B CG  1 
ATOM   439  C CD1 . LEU   B 2 22  ? -12.185 27.441  -16.868 1.00 58.19  ? 31  LEU   B CD1 1 
ATOM   440  C CD2 . LEU   B 2 22  ? -11.865 25.754  -18.636 1.00 58.43  ? 31  LEU   B CD2 1 
ATOM   441  N N   . GLY   B 2 23  ? -16.054 24.795  -16.926 1.00 56.55  ? 32  GLY   B N   1 
ATOM   442  C CA  . GLY   B 2 23  ? -17.099 24.233  -17.765 1.00 56.02  ? 32  GLY   B CA  1 
ATOM   443  C C   . GLY   B 2 23  ? -17.698 22.979  -17.170 1.00 55.13  ? 32  GLY   B C   1 
ATOM   444  O O   . GLY   B 2 23  ? -17.652 22.778  -15.953 1.00 55.42  ? 32  GLY   B O   1 
ATOM   445  N N   . SER   B 2 24  ? -18.250 22.120  -18.025 1.00 53.92  ? 33  SER   B N   1 
ATOM   446  C CA  . SER   B 2 24  ? -18.830 20.862  -17.571 1.00 53.33  ? 33  SER   B CA  1 
ATOM   447  C C   . SER   B 2 24  ? -17.856 19.766  -17.921 1.00 52.10  ? 33  SER   B C   1 
ATOM   448  O O   . SER   B 2 24  ? -17.544 19.600  -19.093 1.00 52.22  ? 33  SER   B O   1 
ATOM   449  C CB  . SER   B 2 24  ? -20.168 20.611  -18.257 1.00 54.81  ? 33  SER   B CB  1 
ATOM   450  O OG  . SER   B 2 24  ? -21.204 21.373  -17.656 1.00 57.09  ? 33  SER   B OG  1 
ATOM   451  N N   . THR   B 2 25  ? -17.341 19.045  -16.921 1.00 50.79  ? 34  THR   B N   1 
ATOM   452  C CA  . THR   B 2 25  ? -16.356 17.996  -17.181 1.00 50.01  ? 34  THR   B CA  1 
ATOM   453  C C   . THR   B 2 25  ? -16.919 16.604  -16.949 1.00 48.57  ? 34  THR   B C   1 
ATOM   454  O O   . THR   B 2 25  ? -17.563 16.369  -15.933 1.00 48.44  ? 34  THR   B O   1 
ATOM   455  C CB  . THR   B 2 25  ? -15.080 18.251  -16.362 1.00 50.96  ? 34  THR   B CB  1 
ATOM   456  O OG1 . THR   B 2 25  ? -14.541 19.523  -16.727 1.00 52.25  ? 34  THR   B OG1 1 
ATOM   457  C CG2 . THR   B 2 25  ? -14.035 17.181  -16.565 1.00 50.86  ? 34  THR   B CG2 1 
ATOM   458  N N   . GLN   B 2 26  ? -16.691 15.687  -17.893 1.00 47.32  ? 35  GLN   B N   1 
ATOM   459  C CA  . GLN   B 2 26  ? -17.144 14.314  -17.730 1.00 46.59  ? 35  GLN   B CA  1 
ATOM   460  C C   . GLN   B 2 26  ? -16.148 13.514  -16.879 1.00 46.45  ? 35  GLN   B C   1 
ATOM   461  O O   . GLN   B 2 26  ? -14.997 13.321  -17.285 1.00 46.67  ? 35  GLN   B O   1 
ATOM   462  C CB  . GLN   B 2 26  ? -17.370 13.623  -19.082 1.00 46.50  ? 35  GLN   B CB  1 
ATOM   463  C CG  . GLN   B 2 26  ? -17.998 12.256  -18.906 1.00 47.38  ? 35  GLN   B CG  1 
ATOM   464  C CD  . GLN   B 2 26  ? -18.192 11.529  -20.196 1.00 50.07  ? 35  GLN   B CD  1 
ATOM   465  O OE1 . GLN   B 2 26  ? -18.800 12.048  -21.143 1.00 51.92  ? 35  GLN   B OE1 1 
ATOM   466  N NE2 . GLN   B 2 26  ? -17.702 10.297  -20.254 1.00 49.21  ? 35  GLN   B NE2 1 
ATOM   467  N N   . VAL   B 2 27  ? -16.591 13.047  -15.707 1.00 45.57  ? 36  VAL   B N   1 
ATOM   468  C CA  . VAL   B 2 27  ? -15.750 12.227  -14.832 1.00 45.20  ? 36  VAL   B CA  1 
ATOM   469  C C   . VAL   B 2 27  ? -15.942 10.714  -15.032 1.00 44.54  ? 36  VAL   B C   1 
ATOM   470  O O   . VAL   B 2 27  ? -15.175 9.928   -14.467 1.00 44.77  ? 36  VAL   B O   1 
ATOM   471  C CB  . VAL   B 2 27  ? -15.907 12.592  -13.333 1.00 45.91  ? 36  VAL   B CB  1 
ATOM   472  C CG1 . VAL   B 2 27  ? -15.109 13.834  -12.982 1.00 46.61  ? 36  VAL   B CG1 1 
ATOM   473  C CG2 . VAL   B 2 27  ? -17.371 12.751  -12.941 1.00 46.17  ? 36  VAL   B CG2 1 
ATOM   474  N N   . GLY   B 2 28  ? -16.973 10.314  -15.773 1.00 43.31  ? 37  GLY   B N   1 
ATOM   475  C CA  . GLY   B 2 28  ? -17.265 8.906   -15.965 1.00 42.67  ? 37  GLY   B CA  1 
ATOM   476  C C   . GLY   B 2 28  ? -18.584 8.619   -16.644 1.00 42.13  ? 37  GLY   B C   1 
ATOM   477  O O   . GLY   B 2 28  ? -19.210 9.509   -17.212 1.00 42.52  ? 37  GLY   B O   1 
ATOM   478  N N   . VAL   B 2 29  ? -18.990 7.351   -16.611 1.00 41.29  ? 38  VAL   B N   1 
ATOM   479  C CA  . VAL   B 2 29  ? -20.159 6.764   -17.262 1.00 41.20  ? 38  VAL   B CA  1 
ATOM   480  C C   . VAL   B 2 29  ? -20.835 5.733   -16.310 1.00 40.61  ? 38  VAL   B C   1 
ATOM   481  O O   . VAL   B 2 29  ? -20.227 5.285   -15.332 1.00 40.50  ? 38  VAL   B O   1 
ATOM   482  C CB  . VAL   B 2 29  ? -19.695 6.085   -18.592 1.00 42.28  ? 38  VAL   B CB  1 
ATOM   483  C CG1 . VAL   B 2 29  ? -20.852 5.472   -19.357 1.00 42.81  ? 38  VAL   B CG1 1 
ATOM   484  C CG2 . VAL   B 2 29  ? -18.932 7.053   -19.489 1.00 42.99  ? 38  VAL   B CG2 1 
ATOM   485  N N   . GLY   B 2 30  ? -22.080 5.369   -16.598 1.00 39.82  ? 39  GLY   B N   1 
ATOM   486  C CA  . GLY   B 2 30  ? -22.811 4.407   -15.786 1.00 39.45  ? 39  GLY   B CA  1 
ATOM   487  C C   . GLY   B 2 30  ? -23.980 3.763   -16.501 1.00 39.03  ? 39  GLY   B C   1 
ATOM   488  O O   . GLY   B 2 30  ? -24.376 4.205   -17.578 1.00 39.73  ? 39  GLY   B O   1 
ATOM   489  N N   . VAL   B 2 31  ? -24.540 2.704   -15.915 1.00 37.90  ? 40  VAL   B N   1 
ATOM   490  C CA  . VAL   B 2 31  ? -25.654 1.963   -16.500 1.00 37.23  ? 40  VAL   B CA  1 
ATOM   491  C C   . VAL   B 2 31  ? -26.909 2.128   -15.661 1.00 37.23  ? 40  VAL   B C   1 
ATOM   492  O O   . VAL   B 2 31  ? -26.883 1.830   -14.472 1.00 37.97  ? 40  VAL   B O   1 
ATOM   493  C CB  . VAL   B 2 31  ? -25.296 0.457   -16.618 1.00 36.97  ? 40  VAL   B CB  1 
ATOM   494  C CG1 . VAL   B 2 31  ? -26.499 -0.384  -17.037 1.00 36.83  ? 40  VAL   B CG1 1 
ATOM   495  C CG2 . VAL   B 2 31  ? -24.121 0.246   -17.561 1.00 37.33  ? 40  VAL   B CG2 1 
ATOM   496  N N   . MET   B 2 32  ? -28.011 2.560   -16.269 1.00 36.19  ? 41  MET   B N   1 
ATOM   497  C CA  . MET   B 2 32  ? -29.280 2.596   -15.574 1.00 35.84  ? 41  MET   B CA  1 
ATOM   498  C C   . MET   B 2 32  ? -30.004 1.322   -16.015 1.00 36.32  ? 41  MET   B C   1 
ATOM   499  O O   . MET   B 2 32  ? -30.153 1.085   -17.210 1.00 36.21  ? 41  MET   B O   1 
ATOM   500  C CB  . MET   B 2 32  ? -30.084 3.836   -15.934 1.00 35.49  ? 41  MET   B CB  1 
ATOM   501  C CG  . MET   B 2 32  ? -31.328 3.980   -15.115 1.00 36.45  ? 41  MET   B CG  1 
ATOM   502  S SD  . MET   B 2 32  ? -30.989 4.597   -13.446 1.00 39.80  ? 41  MET   B SD  1 
ATOM   503  C CE  . MET   B 2 32  ? -30.453 6.256   -13.843 1.00 36.77  ? 41  MET   B CE  1 
ATOM   504  N N   . GLN   B 2 33  ? -30.358 0.460   -15.066 1.00 36.65  ? 42  GLN   B N   1 
ATOM   505  C CA  . GLN   B 2 33  ? -31.066 -0.786  -15.351 1.00 37.23  ? 42  GLN   B CA  1 
ATOM   506  C C   . GLN   B 2 33  ? -31.984 -1.086  -14.154 1.00 37.25  ? 42  GLN   B C   1 
ATOM   507  O O   . GLN   B 2 33  ? -31.503 -1.074  -13.028 1.00 37.71  ? 42  GLN   B O   1 
ATOM   508  C CB  . GLN   B 2 33  ? -30.067 -1.937  -15.596 1.00 39.28  ? 42  GLN   B CB  1 
ATOM   509  C CG  . GLN   B 2 33  ? -30.709 -3.326  -15.497 1.00 44.21  ? 42  GLN   B CG  1 
ATOM   510  C CD  . GLN   B 2 33  ? -30.104 -4.370  -16.400 1.00 49.23  ? 42  GLN   B CD  1 
ATOM   511  O OE1 . GLN   B 2 33  ? -29.927 -5.537  -16.005 1.00 50.48  ? 42  GLN   B OE1 1 
ATOM   512  N NE2 . GLN   B 2 33  ? -29.767 -3.979  -17.626 1.00 50.24  ? 42  GLN   B NE2 1 
ATOM   513  N N   . GLU   B 2 34  ? -33.291 -1.297  -14.391 1.00 36.60  ? 43  GLU   B N   1 
ATOM   514  C CA  . GLU   B 2 34  ? -34.282 -1.596  -13.356 1.00 36.81  ? 43  GLU   B CA  1 
ATOM   515  C C   . GLU   B 2 34  ? -34.326 -0.562  -12.197 1.00 36.97  ? 43  GLU   B C   1 
ATOM   516  O O   . GLU   B 2 34  ? -34.426 -0.936  -11.020 1.00 37.14  ? 43  GLU   B O   1 
ATOM   517  C CB  . GLU   B 2 34  ? -34.109 -3.024  -12.817 1.00 39.14  ? 43  GLU   B CB  1 
ATOM   518  C CG  . GLU   B 2 34  ? -34.043 -4.092  -13.894 1.00 43.68  ? 43  GLU   B CG  1 
ATOM   519  C CD  . GLU   B 2 34  ? -33.352 -5.377  -13.477 1.00 51.37  ? 43  GLU   B CD  1 
ATOM   520  O OE1 . GLU   B 2 34  ? -33.566 -5.828  -12.328 1.00 52.38  ? 43  GLU   B OE1 1 
ATOM   521  O OE2 . GLU   B 2 34  ? -32.591 -5.936  -14.301 1.00 55.17  ? 43  GLU   B OE2 1 
ATOM   522  N N   . GLY   B 2 35  ? -34.248 0.723   -12.546 1.00 36.35  ? 44  GLY   B N   1 
ATOM   523  C CA  . GLY   B 2 35  ? -34.303 1.813   -11.576 1.00 35.89  ? 44  GLY   B CA  1 
ATOM   524  C C   . GLY   B 2 35  ? -33.046 2.006   -10.745 1.00 35.12  ? 44  GLY   B C   1 
ATOM   525  O O   . GLY   B 2 35  ? -33.048 2.800   -9.800  1.00 34.71  ? 44  GLY   B O   1 
ATOM   526  N N   . VAL   B 2 36  ? -31.962 1.278   -11.078 1.00 34.29  ? 45  VAL   B N   1 
ATOM   527  C CA  . VAL   B 2 36  ? -30.700 1.359   -10.350 1.00 33.95  ? 45  VAL   B CA  1 
ATOM   528  C C   . VAL   B 2 36  ? -29.607 1.848   -11.295 1.00 33.02  ? 45  VAL   B C   1 
ATOM   529  O O   . VAL   B 2 36  ? -29.519 1.390   -12.436 1.00 33.13  ? 45  VAL   B O   1 
ATOM   530  C CB  . VAL   B 2 36  ? -30.350 0.011   -9.645  1.00 35.03  ? 45  VAL   B CB  1 
ATOM   531  C CG1 . VAL   B 2 36  ? -28.949 0.020   -9.033  1.00 35.62  ? 45  VAL   B CG1 1 
ATOM   532  C CG2 . VAL   B 2 36  ? -31.381 -0.322  -8.576  1.00 35.53  ? 45  VAL   B CG2 1 
ATOM   533  N N   . PHE   B 2 37  ? -28.837 2.843   -10.849 1.00 32.05  ? 46  PHE   B N   1 
ATOM   534  C CA  . PHE   B 2 37  ? -27.744 3.399   -11.626 1.00 31.80  ? 46  PHE   B CA  1 
ATOM   535  C C   . PHE   B 2 37  ? -26.458 2.800   -11.081 1.00 31.39  ? 46  PHE   B C   1 
ATOM   536  O O   . PHE   B 2 37  ? -26.159 2.933   -9.897  1.00 31.08  ? 46  PHE   B O   1 
ATOM   537  C CB  . PHE   B 2 37  ? -27.726 4.916   -11.494 1.00 31.84  ? 46  PHE   B CB  1 
ATOM   538  C CG  . PHE   B 2 37  ? -26.686 5.567   -12.357 1.00 32.44  ? 46  PHE   B CG  1 
ATOM   539  C CD1 . PHE   B 2 37  ? -26.819 5.585   -13.737 1.00 32.83  ? 46  PHE   B CD1 1 
ATOM   540  C CD2 . PHE   B 2 37  ? -25.591 6.197   -11.794 1.00 32.96  ? 46  PHE   B CD2 1 
ATOM   541  C CE1 . PHE   B 2 37  ? -25.868 6.202   -14.532 1.00 33.01  ? 46  PHE   B CE1 1 
ATOM   542  C CE2 . PHE   B 2 37  ? -24.641 6.813   -12.596 1.00 33.42  ? 46  PHE   B CE2 1 
ATOM   543  C CZ  . PHE   B 2 37  ? -24.795 6.823   -13.958 1.00 32.88  ? 46  PHE   B CZ  1 
ATOM   544  N N   . HIS   B 2 38  ? -25.736 2.081   -11.938 1.00 30.96  ? 47  HIS   B N   1 
ATOM   545  C CA  . HIS   B 2 38  ? -24.521 1.368   -11.592 1.00 30.90  ? 47  HIS   B CA  1 
ATOM   546  C C   . HIS   B 2 38  ? -23.321 2.096   -12.187 1.00 31.64  ? 47  HIS   B C   1 
ATOM   547  O O   . HIS   B 2 38  ? -23.290 2.306   -13.392 1.00 31.52  ? 47  HIS   B O   1 
ATOM   548  C CB  . HIS   B 2 38  ? -24.572 -0.041  -12.206 1.00 30.71  ? 47  HIS   B CB  1 
ATOM   549  C CG  . HIS   B 2 38  ? -25.829 -0.805  -11.923 1.00 31.45  ? 47  HIS   B CG  1 
ATOM   550  N ND1 . HIS   B 2 38  ? -27.033 -0.457  -12.509 1.00 32.70  ? 47  HIS   B ND1 1 
ATOM   551  C CD2 . HIS   B 2 38  ? -26.013 -1.920  -11.177 1.00 32.14  ? 47  HIS   B CD2 1 
ATOM   552  C CE1 . HIS   B 2 38  ? -27.915 -1.341  -12.072 1.00 33.08  ? 47  HIS   B CE1 1 
ATOM   553  N NE2 . HIS   B 2 38  ? -27.347 -2.235  -11.259 1.00 33.10  ? 47  HIS   B NE2 1 
ATOM   554  N N   . THR   B 2 39  ? -22.306 2.422   -11.373 1.00 31.82  ? 48  THR   B N   1 
ATOM   555  C CA  . THR   B 2 39  ? -21.100 3.064   -11.908 1.00 32.67  ? 48  THR   B CA  1 
ATOM   556  C C   . THR   B 2 39  ? -19.829 2.516   -11.161 1.00 33.39  ? 48  THR   B C   1 
ATOM   557  O O   . THR   B 2 39  ? -19.926 1.551   -10.397 1.00 33.12  ? 48  THR   B O   1 
ATOM   558  C CB  . THR   B 2 39  ? -21.280 4.624   -11.932 1.00 33.19  ? 48  THR   B CB  1 
ATOM   559  O OG1 . THR   B 2 39  ? -20.251 5.202   -12.740 1.00 33.90  ? 48  THR   B OG1 1 
ATOM   560  C CG2 . THR   B 2 39  ? -21.250 5.251   -10.541 1.00 32.82  ? 48  THR   B CG2 1 
ATOM   561  N N   . MET   B 2 40  ? -18.648 3.095   -11.421 1.00 33.90  ? 49  MET   B N   1 
ATOM   562  C CA  . MET   B 2 40  ? -17.437 2.700   -10.723 1.00 34.74  ? 49  MET   B CA  1 
ATOM   563  C C   . MET   B 2 40  ? -17.251 3.643   -9.543  1.00 35.72  ? 49  MET   B C   1 
ATOM   564  O O   . MET   B 2 40  ? -17.505 4.844   -9.665  1.00 36.71  ? 49  MET   B O   1 
ATOM   565  C CB  . MET   B 2 40  ? -16.245 2.712   -11.677 1.00 35.76  ? 49  MET   B CB  1 
ATOM   566  C CG  . MET   B 2 40  ? -16.458 1.818   -12.893 1.00 37.59  ? 49  MET   B CG  1 
ATOM   567  S SD  . MET   B 2 40  ? -14.989 0.866   -13.385 1.00 42.68  ? 49  MET   B SD  1 
ATOM   568  C CE  . MET   B 2 40  ? -15.027 -0.474  -12.197 1.00 39.68  ? 49  MET   B CE  1 
ATOM   569  N N   . TRP   B 2 41  ? -16.837 3.108   -8.389  1.00 35.36  ? 50  TRP   B N   1 
ATOM   570  C CA  A TRP   B 2 41  ? -16.646 3.912   -7.191  0.50 35.93  ? 50  TRP   B CA  1 
ATOM   571  C CA  B TRP   B 2 41  ? -16.633 3.893   -7.184  0.50 35.57  ? 50  TRP   B CA  1 
ATOM   572  C C   . TRP   B 2 41  ? -15.697 5.086   -7.385  1.00 36.25  ? 50  TRP   B C   1 
ATOM   573  O O   . TRP   B 2 41  ? -15.955 6.155   -6.840  1.00 36.22  ? 50  TRP   B O   1 
ATOM   574  C CB  A TRP   B 2 41  ? -16.197 3.053   -6.000  0.50 36.18  ? 50  TRP   B CB  1 
ATOM   575  C CB  B TRP   B 2 41  ? -16.131 3.002   -6.039  0.50 35.30  ? 50  TRP   B CB  1 
ATOM   576  C CG  A TRP   B 2 41  ? -16.422 3.714   -4.672  0.50 36.82  ? 50  TRP   B CG  1 
ATOM   577  C CG  B TRP   B 2 41  ? -15.934 3.742   -4.752  0.50 35.23  ? 50  TRP   B CG  1 
ATOM   578  C CD1 A TRP   B 2 41  ? -17.537 3.624   -3.895  0.50 37.86  ? 50  TRP   B CD1 1 
ATOM   579  C CD1 B TRP   B 2 41  ? -14.832 4.447   -4.369  0.50 35.93  ? 50  TRP   B CD1 1 
ATOM   580  C CD2 A TRP   B 2 41  ? -15.520 4.594   -3.981  0.50 37.10  ? 50  TRP   B CD2 1 
ATOM   581  C CD2 B TRP   B 2 41  ? -16.897 3.904   -3.711  0.50 35.14  ? 50  TRP   B CD2 1 
ATOM   582  N NE1 A TRP   B 2 41  ? -17.379 4.374   -2.750  0.50 38.36  ? 50  TRP   B NE1 1 
ATOM   583  N NE1 B TRP   B 2 41  ? -15.056 5.051   -3.157  0.50 36.24  ? 50  TRP   B NE1 1 
ATOM   584  C CE2 A TRP   B 2 41  ? -16.155 4.991   -2.786  0.50 38.05  ? 50  TRP   B CE2 1 
ATOM   585  C CE2 B TRP   B 2 41  ? -16.311 4.716   -2.718  0.50 35.83  ? 50  TRP   B CE2 1 
ATOM   586  C CE3 A TRP   B 2 41  ? -14.227 5.062   -4.243  0.50 37.66  ? 50  TRP   B CE3 1 
ATOM   587  C CE3 B TRP   B 2 41  ? -18.195 3.428   -3.510  0.50 35.55  ? 50  TRP   B CE3 1 
ATOM   588  C CZ2 A TRP   B 2 41  ? -15.550 5.849   -1.869  0.50 38.65  ? 50  TRP   B CZ2 1 
ATOM   589  C CZ2 B TRP   B 2 41  ? -16.977 5.057   -1.544  0.50 35.93  ? 50  TRP   B CZ2 1 
ATOM   590  C CZ3 A TRP   B 2 41  ? -13.639 5.929   -3.342  0.50 38.64  ? 50  TRP   B CZ3 1 
ATOM   591  C CZ3 B TRP   B 2 41  ? -18.847 3.763   -2.341  0.50 36.12  ? 50  TRP   B CZ3 1 
ATOM   592  C CH2 A TRP   B 2 41  ? -14.287 6.292   -2.158  0.50 38.85  ? 50  TRP   B CH2 1 
ATOM   593  C CH2 B TRP   B 2 41  ? -18.240 4.569   -1.375  0.50 35.92  ? 50  TRP   B CH2 1 
ATOM   594  N N   . HIS   B 2 42  ? -14.590 4.902   -8.127  1.00 36.75  ? 51  HIS   B N   1 
ATOM   595  C CA  . HIS   B 2 42  ? -13.639 6.009   -8.313  1.00 37.62  ? 51  HIS   B CA  1 
ATOM   596  C C   . HIS   B 2 42  ? -14.208 7.182   -9.134  1.00 38.63  ? 51  HIS   B C   1 
ATOM   597  O O   . HIS   B 2 42  ? -13.599 8.247   -9.166  1.00 38.84  ? 51  HIS   B O   1 
ATOM   598  C CB  . HIS   B 2 42  ? -12.298 5.523   -8.874  1.00 38.19  ? 51  HIS   B CB  1 
ATOM   599  C CG  . HIS   B 2 42  ? -12.288 5.281   -10.349 1.00 39.98  ? 51  HIS   B CG  1 
ATOM   600  N ND1 . HIS   B 2 42  ? -12.448 4.015   -10.873 1.00 41.79  ? 51  HIS   B ND1 1 
ATOM   601  C CD2 . HIS   B 2 42  ? -12.107 6.152   -11.362 1.00 41.04  ? 51  HIS   B CD2 1 
ATOM   602  C CE1 . HIS   B 2 42  ? -12.400 4.162   -12.180 1.00 42.29  ? 51  HIS   B CE1 1 
ATOM   603  N NE2 . HIS   B 2 42  ? -12.208 5.434   -12.520 1.00 42.41  ? 51  HIS   B NE2 1 
ATOM   604  N N   . VAL   B 2 43  ? -15.363 6.993   -9.791  1.00 39.03  ? 52  VAL   B N   1 
ATOM   605  C CA  . VAL   B 2 43  ? -15.973 8.048   -10.582 1.00 39.88  ? 52  VAL   B CA  1 
ATOM   606  C C   . VAL   B 2 43  ? -16.668 9.060   -9.674  1.00 40.20  ? 52  VAL   B C   1 
ATOM   607  O O   . VAL   B 2 43  ? -16.317 10.235  -9.694  1.00 40.20  ? 52  VAL   B O   1 
ATOM   608  C CB  . VAL   B 2 43  ? -16.935 7.459   -11.648 1.00 41.27  ? 52  VAL   B CB  1 
ATOM   609  C CG1 . VAL   B 2 43  ? -17.762 8.555   -12.322 1.00 41.97  ? 52  VAL   B CG1 1 
ATOM   610  C CG2 . VAL   B 2 43  ? -16.173 6.628   -12.675 1.00 41.97  ? 52  VAL   B CG2 1 
ATOM   611  N N   . THR   B 2 44  ? -17.585 8.578   -8.809  1.00 40.07  ? 53  THR   B N   1 
ATOM   612  C CA  . THR   B 2 44  ? -18.401 9.414   -7.950  1.00 40.07  ? 53  THR   B CA  1 
ATOM   613  C C   . THR   B 2 44  ? -17.945 9.510   -6.506  1.00 40.24  ? 53  THR   B C   1 
ATOM   614  O O   . THR   B 2 44  ? -18.446 10.375  -5.783  1.00 40.81  ? 53  THR   B O   1 
ATOM   615  C CB  . THR   B 2 44  ? -19.862 8.945   -8.004  1.00 41.26  ? 53  THR   B CB  1 
ATOM   616  O OG1 . THR   B 2 44  ? -20.014 7.753   -7.233  1.00 42.38  ? 53  THR   B OG1 1 
ATOM   617  C CG2 . THR   B 2 44  ? -20.372 8.715   -9.432  1.00 41.32  ? 53  THR   B CG2 1 
ATOM   618  N N   . LYS   B 2 45  ? -17.059 8.611   -6.061  1.00 39.38  ? 54  LYS   B N   1 
ATOM   619  C CA  . LYS   B 2 45  ? -16.569 8.537   -4.671  1.00 39.44  ? 54  LYS   B CA  1 
ATOM   620  C C   . LYS   B 2 45  ? -17.686 8.304   -3.630  1.00 38.78  ? 54  LYS   B C   1 
ATOM   621  O O   . LYS   B 2 45  ? -17.490 8.563   -2.446  1.00 38.23  ? 54  LYS   B O   1 
ATOM   622  C CB  . LYS   B 2 45  ? -15.741 9.773   -4.288  1.00 41.29  ? 54  LYS   B CB  1 
ATOM   623  C CG  . LYS   B 2 45  ? -14.721 10.191  -5.327  1.00 45.25  ? 54  LYS   B CG  1 
ATOM   624  C CD  . LYS   B 2 45  ? -13.351 9.663   -5.016  1.00 49.79  ? 54  LYS   B CD  1 
ATOM   625  C CE  . LYS   B 2 45  ? -12.305 10.672  -5.430  1.00 54.45  ? 54  LYS   B CE  1 
ATOM   626  N NZ  . LYS   B 2 45  ? -12.464 11.083  -6.857  1.00 57.73  ? 54  LYS   B NZ  1 
ATOM   627  N N   . GLY   B 2 46  ? -18.841 7.830   -4.079  1.00 38.66  ? 55  GLY   B N   1 
ATOM   628  C CA  . GLY   B 2 46  ? -19.985 7.621   -3.205  1.00 39.06  ? 55  GLY   B CA  1 
ATOM   629  C C   . GLY   B 2 46  ? -20.845 8.859   -2.998  1.00 39.46  ? 55  GLY   B C   1 
ATOM   630  O O   . GLY   B 2 46  ? -21.779 8.822   -2.204  1.00 39.58  ? 55  GLY   B O   1 
ATOM   631  N N   . ALA   B 2 47  ? -20.555 9.964   -3.695  1.00 39.74  ? 56  ALA   B N   1 
ATOM   632  C CA  . ALA   B 2 47  ? -21.349 11.184  -3.581  1.00 40.58  ? 56  ALA   B CA  1 
ATOM   633  C C   . ALA   B 2 47  ? -22.708 11.028  -4.272  1.00 41.42  ? 56  ALA   B C   1 
ATOM   634  O O   . ALA   B 2 47  ? -22.814 10.306  -5.259  1.00 41.79  ? 56  ALA   B O   1 
ATOM   635  C CB  . ALA   B 2 47  ? -20.599 12.346  -4.203  1.00 40.78  ? 56  ALA   B CB  1 
ATOM   636  N N   . ALA   B 2 48  ? -23.734 11.733  -3.783  1.00 41.46  ? 57  ALA   B N   1 
ATOM   637  C CA  . ALA   B 2 48  ? -25.057 11.683  -4.394  1.00 41.95  ? 57  ALA   B CA  1 
ATOM   638  C C   . ALA   B 2 48  ? -25.012 12.262  -5.813  1.00 42.44  ? 57  ALA   B C   1 
ATOM   639  O O   . ALA   B 2 48  ? -24.184 13.117  -6.102  1.00 43.00  ? 57  ALA   B O   1 
ATOM   640  C CB  . ALA   B 2 48  ? -26.065 12.450  -3.541  1.00 41.73  ? 57  ALA   B CB  1 
ATOM   641  N N   . LEU   B 2 49  ? -25.865 11.765  -6.708  1.00 42.29  ? 58  LEU   B N   1 
ATOM   642  C CA  . LEU   B 2 49  ? -25.915 12.259  -8.083  1.00 42.53  ? 58  LEU   B CA  1 
ATOM   643  C C   . LEU   B 2 49  ? -27.231 12.998  -8.340  1.00 43.87  ? 58  LEU   B C   1 
ATOM   644  O O   . LEU   B 2 49  ? -28.182 12.870  -7.571  1.00 44.25  ? 58  LEU   B O   1 
ATOM   645  C CB  . LEU   B 2 49  ? -25.719 11.113  -9.084  1.00 41.82  ? 58  LEU   B CB  1 
ATOM   646  C CG  . LEU   B 2 49  ? -24.467 10.279  -8.878  1.00 42.20  ? 58  LEU   B CG  1 
ATOM   647  C CD1 . LEU   B 2 49  ? -24.472 9.061   -9.754  1.00 42.17  ? 58  LEU   B CD1 1 
ATOM   648  C CD2 . LEU   B 2 49  ? -23.225 11.092  -9.097  1.00 42.60  ? 58  LEU   B CD2 1 
ATOM   649  N N   . ARG   B 2 50  ? -27.280 13.792  -9.396  1.00 44.61  ? 59  ARG   B N   1 
ATOM   650  C CA  . ARG   B 2 50  ? -28.480 14.552  -9.727  1.00 46.09  ? 59  ARG   B CA  1 
ATOM   651  C C   . ARG   B 2 50  ? -28.959 14.177  -11.134 1.00 47.21  ? 59  ARG   B C   1 
ATOM   652  O O   . ARG   B 2 50  ? -28.141 13.870  -11.993 1.00 47.41  ? 59  ARG   B O   1 
ATOM   653  C CB  . ARG   B 2 50  ? -28.172 16.055  -9.575  1.00 47.83  ? 59  ARG   B CB  1 
ATOM   654  C CG  . ARG   B 2 50  ? -29.124 16.985  -10.290 1.00 52.33  ? 59  ARG   B CG  1 
ATOM   655  C CD  . ARG   B 2 50  ? -28.869 18.449  -9.984  1.00 57.02  ? 59  ARG   B CD  1 
ATOM   656  N NE  . ARG   B 2 50  ? -27.514 18.898  -10.319 1.00 61.05  ? 59  ARG   B NE  1 
ATOM   657  C CZ  . ARG   B 2 50  ? -27.136 19.320  -11.523 1.00 64.66  ? 59  ARG   B CZ  1 
ATOM   658  N NH1 . ARG   B 2 50  ? -27.987 19.291  -12.545 1.00 64.26  ? 59  ARG   B NH1 1 
ATOM   659  N NH2 . ARG   B 2 50  ? -25.891 19.736  -11.726 1.00 65.61  ? 59  ARG   B NH2 1 
ATOM   660  N N   . SER   B 2 51  ? -30.269 14.134  -11.358 1.00 47.90  ? 60  SER   B N   1 
ATOM   661  C CA  . SER   B 2 51  ? -30.817 13.857  -12.690 1.00 49.35  ? 60  SER   B CA  1 
ATOM   662  C C   . SER   B 2 51  ? -31.953 14.855  -12.907 1.00 51.16  ? 60  SER   B C   1 
ATOM   663  O O   . SER   B 2 51  ? -33.113 14.551  -12.636 1.00 51.05  ? 60  SER   B O   1 
ATOM   664  C CB  . SER   B 2 51  ? -31.332 12.426  -12.784 1.00 50.43  ? 60  SER   B CB  1 
ATOM   665  O OG  . SER   B 2 51  ? -31.734 12.127  -14.110 1.00 52.91  ? 60  SER   B OG  1 
ATOM   666  N N   . GLY   B 2 52  ? -31.600 16.062  -13.333 1.00 52.32  ? 61  GLY   B N   1 
ATOM   667  C CA  . GLY   B 2 52  ? -32.575 17.127  -13.489 1.00 53.72  ? 61  GLY   B CA  1 
ATOM   668  C C   . GLY   B 2 52  ? -32.918 17.630  -12.107 1.00 55.30  ? 61  GLY   B C   1 
ATOM   669  O O   . GLY   B 2 52  ? -32.013 17.872  -11.304 1.00 56.01  ? 61  GLY   B O   1 
ATOM   670  N N   . GLU   B 2 53  ? -34.211 17.718  -11.782 1.00 55.53  ? 62  GLU   B N   1 
ATOM   671  C CA  . GLU   B 2 53  ? -34.629 18.119  -10.440 1.00 56.29  ? 62  GLU   B CA  1 
ATOM   672  C C   . GLU   B 2 53  ? -34.491 16.985  -9.394  1.00 56.25  ? 62  GLU   B C   1 
ATOM   673  O O   . GLU   B 2 53  ? -34.494 17.264  -8.190  1.00 56.33  ? 62  GLU   B O   1 
ATOM   674  C CB  . GLU   B 2 53  ? -36.073 18.632  -10.464 1.00 59.74  ? 62  GLU   B CB  1 
ATOM   675  C CG  . GLU   B 2 53  ? -36.191 20.133  -10.651 1.00 66.56  ? 62  GLU   B CG  1 
ATOM   676  C CD  . GLU   B 2 53  ? -37.614 20.600  -10.892 1.00 75.55  ? 62  GLU   B CD  1 
ATOM   677  O OE1 . GLU   B 2 53  ? -38.419 19.801  -11.425 1.00 77.10  ? 62  GLU   B OE1 1 
ATOM   678  O OE2 . GLU   B 2 53  ? -37.923 21.768  -10.557 1.00 78.61  ? 62  GLU   B OE2 1 
ATOM   679  N N   . GLY   B 2 54  ? -34.383 15.735  -9.859  1.00 55.88  ? 63  GLY   B N   1 
ATOM   680  C CA  . GLY   B 2 54  ? -34.294 14.555  -9.007  1.00 55.82  ? 63  GLY   B CA  1 
ATOM   681  C C   . GLY   B 2 54  ? -32.924 14.232  -8.442  1.00 55.33  ? 63  GLY   B C   1 
ATOM   682  O O   . GLY   B 2 54  ? -31.900 14.628  -9.002  1.00 55.90  ? 63  GLY   B O   1 
ATOM   683  N N   . ARG   B 2 55  ? -32.903 13.473  -7.331  1.00 53.77  ? 64  ARG   B N   1 
ATOM   684  C CA  . ARG   B 2 55  ? -31.677 13.058  -6.654  1.00 52.47  ? 64  ARG   B CA  1 
ATOM   685  C C   . ARG   B 2 55  ? -31.498 11.522  -6.692  1.00 50.86  ? 64  ARG   B C   1 
ATOM   686  O O   . ARG   B 2 55  ? -32.475 10.773  -6.668  1.00 50.87  ? 64  ARG   B O   1 
ATOM   687  C CB  . ARG   B 2 55  ? -31.714 13.547  -5.195  1.00 53.33  ? 64  ARG   B CB  1 
ATOM   688  C CG  . ARG   B 2 55  ? -30.371 13.545  -4.489  1.00 55.86  ? 64  ARG   B CG  1 
ATOM   689  C CD  . ARG   B 2 55  ? -30.530 13.958  -3.039  1.00 58.97  ? 64  ARG   B CD  1 
ATOM   690  N NE  . ARG   B 2 55  ? -29.298 13.781  -2.262  1.00 61.82  ? 64  ARG   B NE  1 
ATOM   691  C CZ  . ARG   B 2 55  ? -28.689 14.758  -1.590  1.00 63.90  ? 64  ARG   B CZ  1 
ATOM   692  N NH1 . ARG   B 2 55  ? -29.186 15.991  -1.600  1.00 63.60  ? 64  ARG   B NH1 1 
ATOM   693  N NH2 . ARG   B 2 55  ? -27.586 14.508  -0.896  1.00 63.26  ? 64  ARG   B NH2 1 
ATOM   694  N N   . LEU   B 2 56  ? -30.248 11.063  -6.745  1.00 49.23  ? 65  LEU   B N   1 
ATOM   695  C CA  . LEU   B 2 56  ? -29.915 9.644   -6.732  1.00 48.05  ? 65  LEU   B CA  1 
ATOM   696  C C   . LEU   B 2 56  ? -28.975 9.444   -5.555  1.00 47.17  ? 65  LEU   B C   1 
ATOM   697  O O   . LEU   B 2 56  ? -27.867 9.976   -5.562  1.00 47.32  ? 65  LEU   B O   1 
ATOM   698  C CB  . LEU   B 2 56  ? -29.189 9.227   -8.021  1.00 47.99  ? 65  LEU   B CB  1 
ATOM   699  C CG  . LEU   B 2 56  ? -29.808 9.605   -9.353  1.00 49.25  ? 65  LEU   B CG  1 
ATOM   700  C CD1 . LEU   B 2 56  ? -28.983 9.063   -10.474 1.00 49.80  ? 65  LEU   B CD1 1 
ATOM   701  C CD2 . LEU   B 2 56  ? -31.215 9.079   -9.483  1.00 49.85  ? 65  LEU   B CD2 1 
ATOM   702  N N   . ASP   B 2 57  ? -29.410 8.714   -4.536  1.00 46.20  ? 66  ASP   B N   1 
ATOM   703  C CA  . ASP   B 2 57  ? -28.589 8.484   -3.349  1.00 45.59  ? 66  ASP   B CA  1 
ATOM   704  C C   . ASP   B 2 57  ? -27.905 7.117   -3.404  1.00 44.21  ? 66  ASP   B C   1 
ATOM   705  O O   . ASP   B 2 57  ? -28.498 6.147   -3.878  1.00 44.29  ? 66  ASP   B O   1 
ATOM   706  C CB  . ASP   B 2 57  ? -29.458 8.598   -2.098  1.00 47.96  ? 66  ASP   B CB  1 
ATOM   707  C CG  . ASP   B 2 57  ? -30.092 9.962   -1.938  1.00 54.64  ? 66  ASP   B CG  1 
ATOM   708  O OD1 . ASP   B 2 57  ? -29.402 10.972  -2.210  1.00 55.88  ? 66  ASP   B OD1 1 
ATOM   709  O OD2 . ASP   B 2 57  ? -31.275 10.023  -1.523  1.00 57.49  ? 66  ASP   B OD2 1 
ATOM   710  N N   . PRO   B 2 58  ? -26.654 7.017   -2.924  1.00 42.69  ? 67  PRO   B N   1 
ATOM   711  C CA  . PRO   B 2 58  ? -25.963 5.720   -2.949  1.00 41.76  ? 67  PRO   B CA  1 
ATOM   712  C C   . PRO   B 2 58  ? -26.692 4.638   -2.150  1.00 41.15  ? 67  PRO   B C   1 
ATOM   713  O O   . PRO   B 2 58  ? -27.391 4.947   -1.193  1.00 41.58  ? 67  PRO   B O   1 
ATOM   714  C CB  . PRO   B 2 58  ? -24.589 6.040   -2.346  1.00 42.45  ? 67  PRO   B CB  1 
ATOM   715  C CG  . PRO   B 2 58  ? -24.792 7.304   -1.570  1.00 43.07  ? 67  PRO   B CG  1 
ATOM   716  C CD  . PRO   B 2 58  ? -25.812 8.074   -2.331  1.00 41.85  ? 67  PRO   B CD  1 
ATOM   717  N N   . TYR   B 2 59  ? -26.566 3.373   -2.564  1.00 39.95  ? 68  TYR   B N   1 
ATOM   718  C CA  . TYR   B 2 59  ? -27.232 2.277   -1.871  1.00 38.69  ? 68  TYR   B CA  1 
ATOM   719  C C   . TYR   B 2 59  ? -26.208 1.249   -1.422  1.00 38.10  ? 68  TYR   B C   1 
ATOM   720  O O   . TYR   B 2 59  ? -26.252 0.783   -0.288  1.00 38.03  ? 68  TYR   B O   1 
ATOM   721  C CB  . TYR   B 2 59  ? -28.304 1.656   -2.776  1.00 37.77  ? 68  TYR   B CB  1 
ATOM   722  C CG  . TYR   B 2 59  ? -29.066 0.507   -2.151  1.00 37.17  ? 68  TYR   B CG  1 
ATOM   723  C CD1 . TYR   B 2 59  ? -28.504 -0.762  -2.066  1.00 37.75  ? 68  TYR   B CD1 1 
ATOM   724  C CD2 . TYR   B 2 59  ? -30.385 0.656   -1.758  1.00 36.94  ? 68  TYR   B CD2 1 
ATOM   725  C CE1 . TYR   B 2 59  ? -29.196 -1.821  -1.496  1.00 38.10  ? 68  TYR   B CE1 1 
ATOM   726  C CE2 . TYR   B 2 59  ? -31.102 -0.405  -1.229  1.00 37.47  ? 68  TYR   B CE2 1 
ATOM   727  C CZ  . TYR   B 2 59  ? -30.505 -1.645  -1.102  1.00 38.20  ? 68  TYR   B CZ  1 
ATOM   728  O OH  . TYR   B 2 59  ? -31.206 -2.696  -0.569  1.00 38.61  ? 68  TYR   B OH  1 
ATOM   729  N N   . TRP   B 2 60  ? -25.311 0.868   -2.322  1.00 37.57  ? 69  TRP   B N   1 
ATOM   730  C CA  . TRP   B 2 60  ? -24.252 -0.089  -2.041  1.00 37.75  ? 69  TRP   B CA  1 
ATOM   731  C C   . TRP   B 2 60  ? -22.955 0.402   -2.696  1.00 37.91  ? 69  TRP   B C   1 
ATOM   732  O O   . TRP   B 2 60  ? -22.987 1.051   -3.729  1.00 37.88  ? 69  TRP   B O   1 
ATOM   733  C CB  . TRP   B 2 60  ? -24.630 -1.506  -2.539  1.00 37.84  ? 69  TRP   B CB  1 
ATOM   734  C CG  . TRP   B 2 60  ? -23.475 -2.476  -2.522  1.00 38.36  ? 69  TRP   B CG  1 
ATOM   735  C CD1 . TRP   B 2 60  ? -22.993 -3.159  -1.444  1.00 39.28  ? 69  TRP   B CD1 1 
ATOM   736  C CD2 . TRP   B 2 60  ? -22.575 -2.754  -3.609  1.00 38.11  ? 69  TRP   B CD2 1 
ATOM   737  N NE1 . TRP   B 2 60  ? -21.870 -3.873  -1.801  1.00 39.59  ? 69  TRP   B NE1 1 
ATOM   738  C CE2 . TRP   B 2 60  ? -21.581 -3.624  -3.118  1.00 39.03  ? 69  TRP   B CE2 1 
ATOM   739  C CE3 . TRP   B 2 60  ? -22.499 -2.327  -4.941  1.00 38.08  ? 69  TRP   B CE3 1 
ATOM   740  C CZ2 . TRP   B 2 60  ? -20.537 -4.091  -3.919  1.00 39.39  ? 69  TRP   B CZ2 1 
ATOM   741  C CZ3 . TRP   B 2 60  ? -21.475 -2.798  -5.734  1.00 38.76  ? 69  TRP   B CZ3 1 
ATOM   742  C CH2 . TRP   B 2 60  ? -20.520 -3.687  -5.231  1.00 39.06  ? 69  TRP   B CH2 1 
ATOM   743  N N   . GLY   B 2 61  ? -21.824 0.058   -2.106  1.00 38.10  ? 70  GLY   B N   1 
ATOM   744  C CA  . GLY   B 2 61  ? -20.518 0.420   -2.637  1.00 38.55  ? 70  GLY   B CA  1 
ATOM   745  C C   . GLY   B 2 61  ? -19.406 -0.370  -1.985  1.00 38.70  ? 70  GLY   B C   1 
ATOM   746  O O   . GLY   B 2 61  ? -19.575 -0.856  -0.870  1.00 39.00  ? 70  GLY   B O   1 
ATOM   747  N N   . ASP   B 2 62  ? -18.271 -0.523  -2.675  1.00 38.47  ? 71  ASP   B N   1 
ATOM   748  C CA  . ASP   B 2 62  ? -17.111 -1.261  -2.172  1.00 38.64  ? 71  ASP   B CA  1 
ATOM   749  C C   . ASP   B 2 62  ? -15.898 -0.737  -2.937  1.00 38.29  ? 71  ASP   B C   1 
ATOM   750  O O   . ASP   B 2 62  ? -15.877 -0.814  -4.158  1.00 38.04  ? 71  ASP   B O   1 
ATOM   751  C CB  . ASP   B 2 62  ? -17.289 -2.772  -2.426  1.00 40.84  ? 71  ASP   B CB  1 
ATOM   752  C CG  . ASP   B 2 62  ? -16.235 -3.682  -1.803  1.00 46.12  ? 71  ASP   B CG  1 
ATOM   753  O OD1 . ASP   B 2 62  ? -15.086 -3.678  -2.282  1.00 46.76  ? 71  ASP   B OD1 1 
ATOM   754  O OD2 . ASP   B 2 62  ? -16.577 -4.433  -0.876  1.00 49.50  ? 71  ASP   B OD2 1 
ATOM   755  N N   . VAL   B 2 63  ? -14.893 -0.210  -2.221  1.00 37.94  ? 72  VAL   B N   1 
ATOM   756  C CA  . VAL   B 2 63  ? -13.673 0.363   -2.796  1.00 37.68  ? 72  VAL   B CA  1 
ATOM   757  C C   . VAL   B 2 63  ? -12.778 -0.712  -3.444  1.00 37.73  ? 72  VAL   B C   1 
ATOM   758  O O   . VAL   B 2 63  ? -12.194 -0.439  -4.490  1.00 38.44  ? 72  VAL   B O   1 
ATOM   759  C CB  . VAL   B 2 63  ? -12.937 1.231   -1.736  1.00 38.12  ? 72  VAL   B CB  1 
ATOM   760  C CG1 . VAL   B 2 63  ? -11.470 1.459   -2.076  1.00 38.59  ? 72  VAL   B CG1 1 
ATOM   761  C CG2 . VAL   B 2 63  ? -13.659 2.560   -1.510  1.00 38.15  ? 72  VAL   B CG2 1 
ATOM   762  N N   . LYS   B 2 64  ? -12.735 -1.943  -2.902  1.00 37.05  ? 73  LYS   B N   1 
ATOM   763  C CA  . LYS   B 2 64  ? -11.921 -3.005  -3.502  1.00 36.88  ? 73  LYS   B CA  1 
ATOM   764  C C   . LYS   B 2 64  ? -12.531 -3.472  -4.824  1.00 36.75  ? 73  LYS   B C   1 
ATOM   765  O O   . LYS   B 2 64  ? -11.826 -3.550  -5.829  1.00 36.33  ? 73  LYS   B O   1 
ATOM   766  C CB  . LYS   B 2 64  ? -11.721 -4.173  -2.530  1.00 38.82  ? 73  LYS   B CB  1 
ATOM   767  C CG  . LYS   B 2 64  ? -10.564 -5.100  -2.907  1.00 42.61  ? 73  LYS   B CG  1 
ATOM   768  C CD  . LYS   B 2 64  ? -10.216 -5.968  -1.705  1.00 47.87  ? 73  LYS   B CD  1 
ATOM   769  C CE  . LYS   B 2 64  ? -8.925  -6.732  -1.837  1.00 52.79  ? 73  LYS   B CE  1 
ATOM   770  N NZ  . LYS   B 2 64  ? -9.131  -8.053  -2.487  1.00 56.15  ? 73  LYS   B NZ  1 
ATOM   771  N N   . GLN   B 2 65  ? -13.846 -3.752  -4.840  1.00 36.75  ? 74  GLN   B N   1 
ATOM   772  C CA  . GLN   B 2 65  ? -14.518 -4.118  -6.093  1.00 36.71  ? 74  GLN   B CA  1 
ATOM   773  C C   . GLN   B 2 65  ? -14.498 -2.928  -7.074  1.00 36.48  ? 74  GLN   B C   1 
ATOM   774  O O   . GLN   B 2 65  ? -14.455 -3.130  -8.288  1.00 36.69  ? 74  GLN   B O   1 
ATOM   775  C CB  . GLN   B 2 65  ? -15.980 -4.558  -5.838  1.00 38.26  ? 74  GLN   B CB  1 
ATOM   776  C CG  . GLN   B 2 65  ? -16.133 -5.809  -4.964  1.00 41.15  ? 74  GLN   B CG  1 
ATOM   777  C CD  . GLN   B 2 65  ? -17.567 -6.336  -4.915  1.00 45.46  ? 74  GLN   B CD  1 
ATOM   778  O OE1 . GLN   B 2 65  ? -18.300 -6.362  -5.924  1.00 46.12  ? 74  GLN   B OE1 1 
ATOM   779  N NE2 . GLN   B 2 65  ? -17.995 -6.801  -3.732  1.00 46.16  ? 74  GLN   B NE2 1 
ATOM   780  N N   . ASP   B 2 66  ? -14.514 -1.690  -6.531  1.00 36.09  ? 75  ASP   B N   1 
ATOM   781  C CA  . ASP   B 2 66  ? -14.561 -0.402  -7.225  1.00 36.07  ? 75  ASP   B CA  1 
ATOM   782  C C   . ASP   B 2 66  ? -15.895 -0.253  -7.924  1.00 35.71  ? 75  ASP   B C   1 
ATOM   783  O O   . ASP   B 2 66  ? -15.950 0.233   -9.042  1.00 36.07  ? 75  ASP   B O   1 
ATOM   784  C CB  . ASP   B 2 66  ? -13.373 -0.178  -8.182  1.00 37.51  ? 75  ASP   B CB  1 
ATOM   785  C CG  . ASP   B 2 66  ? -13.330 1.229   -8.725  1.00 41.65  ? 75  ASP   B CG  1 
ATOM   786  O OD1 . ASP   B 2 66  ? -13.587 2.158   -7.960  1.00 42.17  ? 75  ASP   B OD1 1 
ATOM   787  O OD2 . ASP   B 2 66  ? -13.087 1.391   -9.934  1.00 45.17  ? 75  ASP   B OD2 1 
ATOM   788  N N   . LEU   B 2 67  ? -16.986 -0.641  -7.254  1.00 34.91  ? 76  LEU   B N   1 
ATOM   789  C CA  . LEU   B 2 67  ? -18.319 -0.523  -7.827  1.00 34.50  ? 76  LEU   B CA  1 
ATOM   790  C C   . LEU   B 2 67  ? -19.269 0.188   -6.867  1.00 33.91  ? 76  LEU   B C   1 
ATOM   791  O O   . LEU   B 2 67  ? -19.079 0.137   -5.648  1.00 33.63  ? 76  LEU   B O   1 
ATOM   792  C CB  . LEU   B 2 67  ? -18.879 -1.910  -8.161  1.00 34.59  ? 76  LEU   B CB  1 
ATOM   793  C CG  . LEU   B 2 67  ? -18.120 -2.721  -9.179  1.00 35.70  ? 76  LEU   B CG  1 
ATOM   794  C CD1 . LEU   B 2 67  ? -18.687 -4.089  -9.256  1.00 35.89  ? 76  LEU   B CD1 1 
ATOM   795  C CD2 . LEU   B 2 67  ? -18.150 -2.050  -10.579 1.00 36.51  ? 76  LEU   B CD2 1 
ATOM   796  N N   . VAL   B 2 68  ? -20.300 0.858   -7.415  1.00 33.14  ? 77  VAL   B N   1 
ATOM   797  C CA  . VAL   B 2 68  ? -21.287 1.548   -6.577  1.00 32.63  ? 77  VAL   B CA  1 
ATOM   798  C C   . VAL   B 2 68  ? -22.664 1.526   -7.247  1.00 32.21  ? 77  VAL   B C   1 
ATOM   799  O O   . VAL   B 2 68  ? -22.748 1.595   -8.467  1.00 32.35  ? 77  VAL   B O   1 
ATOM   800  C CB  . VAL   B 2 68  ? -20.815 2.976   -6.191  1.00 32.89  ? 77  VAL   B CB  1 
ATOM   801  C CG1 . VAL   B 2 68  ? -20.433 3.780   -7.414  1.00 33.26  ? 77  VAL   B CG1 1 
ATOM   802  C CG2 . VAL   B 2 68  ? -21.843 3.719   -5.346  1.00 33.01  ? 77  VAL   B CG2 1 
ATOM   803  N N   . SER   B 2 69  ? -23.729 1.327   -6.471  1.00 31.63  ? 78  SER   B N   1 
ATOM   804  C CA  . SER   B 2 69  ? -25.088 1.347   -7.017  1.00 31.49  ? 78  SER   B CA  1 
ATOM   805  C C   . SER   B 2 69  ? -25.892 2.483   -6.362  1.00 31.32  ? 78  SER   B C   1 
ATOM   806  O O   . SER   B 2 69  ? -25.591 2.902   -5.246  1.00 31.24  ? 78  SER   B O   1 
ATOM   807  C CB  . SER   B 2 69  ? -25.779 -0.012  -6.877  1.00 31.46  ? 78  SER   B CB  1 
ATOM   808  O OG  . SER   B 2 69  ? -26.050 -0.345  -5.526  1.00 31.24  ? 78  SER   B OG  1 
ATOM   809  N N   . TYR   B 2 70  ? -26.855 3.028   -7.095  1.00 31.41  ? 79  TYR   B N   1 
ATOM   810  C CA  . TYR   B 2 70  ? -27.683 4.141   -6.650  1.00 32.11  ? 79  TYR   B CA  1 
ATOM   811  C C   . TYR   B 2 70  ? -29.148 3.750   -6.769  1.00 33.35  ? 79  TYR   B C   1 
ATOM   812  O O   . TYR   B 2 70  ? -29.538 3.116   -7.759  1.00 34.04  ? 79  TYR   B O   1 
ATOM   813  C CB  . TYR   B 2 70  ? -27.418 5.386   -7.518  1.00 31.91  ? 79  TYR   B CB  1 
ATOM   814  C CG  . TYR   B 2 70  ? -26.110 6.072   -7.205  1.00 32.36  ? 79  TYR   B CG  1 
ATOM   815  C CD1 . TYR   B 2 70  ? -24.921 5.644   -7.781  1.00 33.28  ? 79  TYR   B CD1 1 
ATOM   816  C CD2 . TYR   B 2 70  ? -26.065 7.167   -6.356  1.00 33.04  ? 79  TYR   B CD2 1 
ATOM   817  C CE1 . TYR   B 2 70  ? -23.710 6.249   -7.469  1.00 34.08  ? 79  TYR   B CE1 1 
ATOM   818  C CE2 . TYR   B 2 70  ? -24.864 7.790   -6.047  1.00 33.85  ? 79  TYR   B CE2 1 
ATOM   819  C CZ  . TYR   B 2 70  ? -23.686 7.322   -6.599  1.00 35.00  ? 79  TYR   B CZ  1 
ATOM   820  O OH  . TYR   B 2 70  ? -22.501 7.953   -6.312  1.00 36.60  ? 79  TYR   B OH  1 
ATOM   821  N N   . CYS   B 2 71  ? -29.949 4.098   -5.753  1.00 33.21  ? 80  CYS   B N   1 
ATOM   822  C CA  . CYS   B 2 71  ? -31.390 3.854   -5.705  1.00 33.49  ? 80  CYS   B CA  1 
ATOM   823  C C   . CYS   B 2 71  ? -31.777 2.418   -5.334  1.00 33.12  ? 80  CYS   B C   1 
ATOM   824  O O   . CYS   B 2 71  ? -32.924 2.185   -4.946  1.00 33.19  ? 80  CYS   B O   1 
ATOM   825  C CB  . CYS   B 2 71  ? -32.066 4.293   -6.999  1.00 34.85  ? 80  CYS   B CB  1 
ATOM   826  S SG  . CYS   B 2 71  ? -31.865 6.056   -7.386  1.00 40.73  ? 80  CYS   B SG  1 
ATOM   827  N N   . GLY   B 2 72  ? -30.848 1.474   -5.446  1.00 32.49  ? 81  GLY   B N   1 
ATOM   828  C CA  . GLY   B 2 72  ? -31.141 0.090   -5.110  1.00 32.86  ? 81  GLY   B CA  1 
ATOM   829  C C   . GLY   B 2 72  ? -29.933 -0.806  -5.195  1.00 33.48  ? 81  GLY   B C   1 
ATOM   830  O O   . GLY   B 2 72  ? -28.819 -0.349  -5.468  1.00 33.25  ? 81  GLY   B O   1 
ATOM   831  N N   . PRO   B 2 73  ? -30.125 -2.102  -4.914  1.00 34.11  ? 82  PRO   B N   1 
ATOM   832  C CA  . PRO   B 2 73  ? -28.996 -3.030  -4.979  1.00 34.58  ? 82  PRO   B CA  1 
ATOM   833  C C   . PRO   B 2 73  ? -28.544 -3.311  -6.412  1.00 35.54  ? 82  PRO   B C   1 
ATOM   834  O O   . PRO   B 2 73  ? -29.315 -3.100  -7.356  1.00 35.77  ? 82  PRO   B O   1 
ATOM   835  C CB  . PRO   B 2 73  ? -29.539 -4.281  -4.283  1.00 34.83  ? 82  PRO   B CB  1 
ATOM   836  C CG  . PRO   B 2 73  ? -30.975 -4.228  -4.489  1.00 34.88  ? 82  PRO   B CG  1 
ATOM   837  C CD  . PRO   B 2 73  ? -31.367 -2.788  -4.511  1.00 33.47  ? 82  PRO   B CD  1 
ATOM   838  N N   . TRP   B 2 74  ? -27.291 -3.799  -6.567  1.00 35.83  ? 83  TRP   B N   1 
ATOM   839  C CA  . TRP   B 2 74  ? -26.683 -4.123  -7.856  1.00 36.59  ? 83  TRP   B CA  1 
ATOM   840  C C   . TRP   B 2 74  ? -27.540 -5.147  -8.616  1.00 37.72  ? 83  TRP   B C   1 
ATOM   841  O O   . TRP   B 2 74  ? -27.906 -6.178  -8.049  1.00 37.79  ? 83  TRP   B O   1 
ATOM   842  C CB  . TRP   B 2 74  ? -25.239 -4.603  -7.641  1.00 36.49  ? 83  TRP   B CB  1 
ATOM   843  C CG  . TRP   B 2 74  ? -24.443 -4.744  -8.899  1.00 36.95  ? 83  TRP   B CG  1 
ATOM   844  C CD1 . TRP   B 2 74  ? -24.365 -5.844  -9.697  1.00 37.71  ? 83  TRP   B CD1 1 
ATOM   845  C CD2 . TRP   B 2 74  ? -23.587 -3.753  -9.493  1.00 37.30  ? 83  TRP   B CD2 1 
ATOM   846  N NE1 . TRP   B 2 74  ? -23.546 -5.588  -10.776 1.00 38.17  ? 83  TRP   B NE1 1 
ATOM   847  C CE2 . TRP   B 2 74  ? -23.056 -4.311  -10.675 1.00 37.81  ? 83  TRP   B CE2 1 
ATOM   848  C CE3 . TRP   B 2 74  ? -23.235 -2.439  -9.152  1.00 37.79  ? 83  TRP   B CE3 1 
ATOM   849  C CZ2 . TRP   B 2 74  ? -22.218 -3.595  -11.525 1.00 38.25  ? 83  TRP   B CZ2 1 
ATOM   850  C CZ3 . TRP   B 2 74  ? -22.381 -1.741  -9.985  1.00 38.32  ? 83  TRP   B CZ3 1 
ATOM   851  C CH2 . TRP   B 2 74  ? -21.901 -2.310  -11.166 1.00 38.41  ? 83  TRP   B CH2 1 
ATOM   852  N N   . LYS   B 2 75  ? -27.925 -4.818  -9.874  1.00 38.50  ? 84  LYS   B N   1 
ATOM   853  C CA  . LYS   B 2 75  ? -28.828 -5.614  -10.715 1.00 39.60  ? 84  LYS   B CA  1 
ATOM   854  C C   . LYS   B 2 75  ? -28.123 -6.376  -11.842 1.00 41.54  ? 84  LYS   B C   1 
ATOM   855  O O   . LYS   B 2 75  ? -28.697 -7.311  -12.403 1.00 41.74  ? 84  LYS   B O   1 
ATOM   856  C CB  . LYS   B 2 75  ? -29.884 -4.706  -11.371 1.00 40.64  ? 84  LYS   B CB  1 
ATOM   857  C CG  . LYS   B 2 75  ? -30.678 -3.825  -10.441 1.00 43.86  ? 84  LYS   B CG  1 
ATOM   858  C CD  . LYS   B 2 75  ? -31.616 -4.628  -9.560  1.00 47.95  ? 84  LYS   B CD  1 
ATOM   859  C CE  . LYS   B 2 75  ? -32.814 -3.803  -9.166  1.00 51.37  ? 84  LYS   B CE  1 
ATOM   860  N NZ  . LYS   B 2 75  ? -33.600 -4.445  -8.080  1.00 53.87  ? 84  LYS   B NZ  1 
ATOM   861  N N   . LEU   B 2 76  ? -26.936 -5.930  -12.239 1.00 42.49  ? 85  LEU   B N   1 
ATOM   862  C CA  . LEU   B 2 76  ? -26.207 -6.551  -13.337 1.00 43.67  ? 85  LEU   B CA  1 
ATOM   863  C C   . LEU   B 2 76  ? -25.550 -7.855  -12.882 1.00 45.35  ? 85  LEU   B C   1 
ATOM   864  O O   . LEU   B 2 76  ? -24.622 -7.827  -12.088 1.00 45.48  ? 85  LEU   B O   1 
ATOM   865  C CB  . LEU   B 2 76  ? -25.166 -5.574  -13.901 1.00 43.58  ? 85  LEU   B CB  1 
ATOM   866  C CG  . LEU   B 2 76  ? -25.640 -4.138  -14.136 1.00 44.40  ? 85  LEU   B CG  1 
ATOM   867  C CD1 . LEU   B 2 76  ? -24.505 -3.266  -14.578 1.00 44.94  ? 85  LEU   B CD1 1 
ATOM   868  C CD2 . LEU   B 2 76  ? -26.770 -4.081  -15.135 1.00 44.69  ? 85  LEU   B CD2 1 
ATOM   869  N N   . ASP   B 2 77  ? -26.017 -8.997  -13.395 1.00 46.80  ? 86  ASP   B N   1 
ATOM   870  C CA  . ASP   B 2 77  ? -25.487 -10.298 -12.989 1.00 48.72  ? 86  ASP   B CA  1 
ATOM   871  C C   . ASP   B 2 77  ? -24.892 -11.160 -14.117 1.00 49.98  ? 86  ASP   B C   1 
ATOM   872  O O   . ASP   B 2 77  ? -24.448 -12.272 -13.837 1.00 50.71  ? 86  ASP   B O   1 
ATOM   873  C CB  . ASP   B 2 77  ? -26.545 -11.102 -12.220 1.00 51.18  ? 86  ASP   B CB  1 
ATOM   874  C CG  . ASP   B 2 77  ? -27.865 -11.303 -12.939 1.00 57.62  ? 86  ASP   B CG  1 
ATOM   875  O OD1 . ASP   B 2 77  ? -28.036 -10.741 -14.051 1.00 58.52  ? 86  ASP   B OD1 1 
ATOM   876  O OD2 . ASP   B 2 77  ? -28.733 -12.016 -12.392 1.00 60.66  ? 86  ASP   B OD2 1 
ATOM   877  N N   . ALA   B 2 78  ? -24.854 -10.666 -15.361 1.00 50.07  ? 87  ALA   B N   1 
ATOM   878  C CA  . ALA   B 2 78  ? -24.281 -11.433 -16.473 1.00 50.67  ? 87  ALA   B CA  1 
ATOM   879  C C   . ALA   B 2 78  ? -22.737 -11.486 -16.407 1.00 51.24  ? 87  ALA   B C   1 
ATOM   880  O O   . ALA   B 2 78  ? -22.116 -10.619 -15.800 1.00 51.19  ? 87  ALA   B O   1 
ATOM   881  C CB  . ALA   B 2 78  ? -24.726 -10.837 -17.803 1.00 50.70  ? 87  ALA   B CB  1 
ATOM   882  N N   . ALA   B 2 79  ? -22.117 -12.487 -17.051 1.00 51.53  ? 88  ALA   B N   1 
ATOM   883  C CA  . ALA   B 2 79  ? -20.660 -12.612 -17.047 1.00 52.10  ? 88  ALA   B CA  1 
ATOM   884  C C   . ALA   B 2 79  ? -20.074 -13.100 -18.378 1.00 52.54  ? 88  ALA   B C   1 
ATOM   885  O O   . ALA   B 2 79  ? -20.745 -13.799 -19.131 1.00 52.28  ? 88  ALA   B O   1 
ATOM   886  C CB  . ALA   B 2 79  ? -20.224 -13.534 -15.920 1.00 52.36  ? 88  ALA   B CB  1 
ATOM   887  N N   . TRP   B 2 80  ? -18.803 -12.758 -18.642 1.00 53.03  ? 89  TRP   B N   1 
ATOM   888  C CA  . TRP   B 2 80  ? -18.088 -13.203 -19.830 1.00 53.96  ? 89  TRP   B CA  1 
ATOM   889  C C   . TRP   B 2 80  ? -17.932 -14.710 -19.780 1.00 54.39  ? 89  TRP   B C   1 
ATOM   890  O O   . TRP   B 2 80  ? -17.683 -15.271 -18.710 1.00 54.27  ? 89  TRP   B O   1 
ATOM   891  C CB  . TRP   B 2 80  ? -16.702 -12.549 -19.911 1.00 54.34  ? 89  TRP   B CB  1 
ATOM   892  C CG  . TRP   B 2 80  ? -15.926 -12.894 -21.152 1.00 55.10  ? 89  TRP   B CG  1 
ATOM   893  C CD1 . TRP   B 2 80  ? -16.375 -12.862 -22.439 1.00 56.23  ? 89  TRP   B CD1 1 
ATOM   894  C CD2 . TRP   B 2 80  ? -14.537 -13.228 -21.220 1.00 55.27  ? 89  TRP   B CD2 1 
ATOM   895  N NE1 . TRP   B 2 80  ? -15.363 -13.216 -23.302 1.00 56.69  ? 89  TRP   B NE1 1 
ATOM   896  C CE2 . TRP   B 2 80  ? -14.217 -13.427 -22.578 1.00 56.37  ? 89  TRP   B CE2 1 
ATOM   897  C CE3 . TRP   B 2 80  ? -13.531 -13.382 -20.266 1.00 55.74  ? 89  TRP   B CE3 1 
ATOM   898  C CZ2 . TRP   B 2 80  ? -12.940 -13.799 -22.994 1.00 57.07  ? 89  TRP   B CZ2 1 
ATOM   899  C CZ3 . TRP   B 2 80  ? -12.266 -13.737 -20.684 1.00 56.67  ? 89  TRP   B CZ3 1 
ATOM   900  C CH2 . TRP   B 2 80  ? -11.981 -13.948 -22.029 1.00 56.90  ? 89  TRP   B CH2 1 
ATOM   901  N N   . ASP   B 2 81  ? -18.121 -15.367 -20.929 1.00 54.47  ? 90  ASP   B N   1 
ATOM   902  C CA  . ASP   B 2 81  ? -18.022 -16.813 -21.013 1.00 55.15  ? 90  ASP   B CA  1 
ATOM   903  C C   . ASP   B 2 81  ? -16.579 -17.338 -21.129 1.00 56.09  ? 90  ASP   B C   1 
ATOM   904  O O   . ASP   B 2 81  ? -16.378 -18.549 -21.095 1.00 55.97  ? 90  ASP   B O   1 
ATOM   905  C CB  . ASP   B 2 81  ? -18.908 -17.360 -22.154 1.00 56.49  ? 90  ASP   B CB  1 
ATOM   906  C CG  . ASP   B 2 81  ? -18.533 -16.924 -23.563 1.00 60.07  ? 90  ASP   B CG  1 
ATOM   907  O OD1 . ASP   B 2 81  ? -17.544 -16.182 -23.715 1.00 61.65  ? 90  ASP   B OD1 1 
ATOM   908  O OD2 . ASP   B 2 81  ? -19.233 -17.319 -24.513 1.00 60.85  ? 90  ASP   B OD2 1 
ATOM   909  N N   . GLY   B 2 82  ? -15.605 -16.439 -21.258 1.00 56.75  ? 91  GLY   B N   1 
ATOM   910  C CA  . GLY   B 2 82  ? -14.208 -16.808 -21.424 1.00 58.02  ? 91  GLY   B CA  1 
ATOM   911  C C   . GLY   B 2 82  ? -13.866 -17.241 -22.841 1.00 59.54  ? 91  GLY   B C   1 
ATOM   912  O O   . GLY   B 2 82  ? -12.770 -17.747 -23.080 1.00 59.76  ? 91  GLY   B O   1 
ATOM   913  N N   . LEU   B 2 83  ? -14.788 -17.041 -23.804 1.00 59.90  ? 92  LEU   B N   1 
ATOM   914  C CA  . LEU   B 2 83  ? -14.571 -17.481 -25.167 1.00 60.93  ? 92  LEU   B CA  1 
ATOM   915  C C   . LEU   B 2 83  ? -14.855 -16.446 -26.215 1.00 62.10  ? 92  LEU   B C   1 
ATOM   916  O O   . LEU   B 2 83  ? -14.087 -16.324 -27.162 1.00 62.89  ? 92  LEU   B O   1 
ATOM   917  C CB  . LEU   B 2 83  ? -15.463 -18.699 -25.469 1.00 61.43  ? 92  LEU   B CB  1 
ATOM   918  C CG  . LEU   B 2 83  ? -15.031 -20.080 -24.985 1.00 63.61  ? 92  LEU   B CG  1 
ATOM   919  C CD1 . LEU   B 2 83  ? -15.870 -21.145 -25.667 1.00 64.31  ? 92  LEU   B CD1 1 
ATOM   920  C CD2 . LEU   B 2 83  ? -13.576 -20.353 -25.299 1.00 64.05  ? 92  LEU   B CD2 1 
ATOM   921  N N   . SER   B 2 84  ? -16.009 -15.772 -26.116 1.00 62.11  ? 93  SER   B N   1 
ATOM   922  C CA  . SER   B 2 84  ? -16.503 -14.870 -27.142 1.00 62.20  ? 93  SER   B CA  1 
ATOM   923  C C   . SER   B 2 84  ? -15.976 -13.450 -27.072 1.00 61.47  ? 93  SER   B C   1 
ATOM   924  O O   . SER   B 2 84  ? -15.466 -13.004 -26.039 1.00 61.72  ? 93  SER   B O   1 
ATOM   925  C CB  . SER   B 2 84  ? -18.032 -14.848 -27.130 1.00 64.21  ? 93  SER   B CB  1 
ATOM   926  O OG  . SER   B 2 84  ? -18.606 -16.107 -26.820 1.00 67.22  ? 93  SER   B OG  1 
ATOM   927  N N   . GLU   B 2 85  ? -16.100 -12.747 -28.196 1.00 60.46  ? 94  GLU   B N   1 
ATOM   928  C CA  . GLU   B 2 85  ? -15.754 -11.348 -28.307 1.00 60.19  ? 94  GLU   B CA  1 
ATOM   929  C C   . GLU   B 2 85  ? -16.896 -10.538 -27.664 1.00 58.98  ? 94  GLU   B C   1 
ATOM   930  O O   . GLU   B 2 85  ? -18.076 -10.872 -27.782 1.00 59.26  ? 94  GLU   B O   1 
ATOM   931  C CB  . GLU   B 2 85  ? -15.553 -10.936 -29.789 1.00 62.85  ? 94  GLU   B CB  1 
ATOM   932  C CG  . GLU   B 2 85  ? -14.300 -11.508 -30.438 1.00 67.60  ? 94  GLU   B CG  1 
ATOM   933  C CD  . GLU   B 2 85  ? -13.843 -10.813 -31.708 1.00 74.69  ? 94  GLU   B CD  1 
ATOM   934  O OE1 . GLU   B 2 85  ? -14.663 -10.104 -32.338 1.00 75.14  ? 94  GLU   B OE1 1 
ATOM   935  O OE2 . GLU   B 2 85  ? -12.659 -10.984 -32.080 1.00 76.84  ? 94  GLU   B OE2 1 
ATOM   936  N N   . VAL   B 2 86  ? -16.531 -9.499  -26.954 1.00 57.48  ? 95  VAL   B N   1 
ATOM   937  C CA  . VAL   B 2 86  ? -17.470 -8.638  -26.247 1.00 56.13  ? 95  VAL   B CA  1 
ATOM   938  C C   . VAL   B 2 86  ? -17.553 -7.263  -26.953 1.00 55.48  ? 95  VAL   B C   1 
ATOM   939  O O   . VAL   B 2 86  ? -16.843 -7.031  -27.933 1.00 55.68  ? 95  VAL   B O   1 
ATOM   940  C CB  . VAL   B 2 86  ? -16.976 -8.498  -24.781 1.00 55.66  ? 95  VAL   B CB  1 
ATOM   941  C CG1 . VAL   B 2 86  ? -16.852 -9.859  -24.110 1.00 55.81  ? 95  VAL   B CG1 1 
ATOM   942  C CG2 . VAL   B 2 86  ? -15.653 -7.743  -24.737 1.00 55.74  ? 95  VAL   B CG2 1 
ATOM   943  N N   . GLN   B 2 87  ? -18.412 -6.353  -26.466 1.00 54.71  ? 96  GLN   B N   1 
ATOM   944  C CA  . GLN   B 2 87  ? -18.487 -5.016  -27.028 1.00 54.27  ? 96  GLN   B CA  1 
ATOM   945  C C   . GLN   B 2 87  ? -18.412 -3.968  -25.951 1.00 53.42  ? 96  GLN   B C   1 
ATOM   946  O O   . GLN   B 2 87  ? -19.270 -3.936  -25.074 1.00 53.50  ? 96  GLN   B O   1 
ATOM   947  C CB  . GLN   B 2 87  ? -19.726 -4.826  -27.913 1.00 55.71  ? 96  GLN   B CB  1 
ATOM   948  C CG  . GLN   B 2 87  ? -19.359 -4.917  -29.389 1.00 59.19  ? 96  GLN   B CG  1 
ATOM   949  C CD  . GLN   B 2 87  ? -20.520 -4.734  -30.325 1.00 62.73  ? 96  GLN   B CD  1 
ATOM   950  O OE1 . GLN   B 2 87  ? -21.500 -4.040  -30.035 1.00 63.08  ? 96  GLN   B OE1 1 
ATOM   951  N NE2 . GLN   B 2 87  ? -20.417 -5.357  -31.488 1.00 64.10  ? 96  GLN   B NE2 1 
ATOM   952  N N   . LEU   B 2 88  ? -17.376 -3.127  -25.989 1.00 52.15  ? 97  LEU   B N   1 
ATOM   953  C CA  . LEU   B 2 88  ? -17.292 -2.019  -25.051 1.00 51.09  ? 97  LEU   B CA  1 
ATOM   954  C C   . LEU   B 2 88  ? -18.160 -0.916  -25.687 1.00 50.31  ? 97  LEU   B C   1 
ATOM   955  O O   . LEU   B 2 88  ? -17.894 -0.513  -26.815 1.00 50.39  ? 97  LEU   B O   1 
ATOM   956  C CB  . LEU   B 2 88  ? -15.831 -1.539  -24.867 1.00 50.72  ? 97  LEU   B CB  1 
ATOM   957  C CG  . LEU   B 2 88  ? -15.648 -0.143  -24.244 1.00 51.15  ? 97  LEU   B CG  1 
ATOM   958  C CD1 . LEU   B 2 88  ? -16.256 -0.068  -22.879 1.00 51.41  ? 97  LEU   B CD1 1 
ATOM   959  C CD2 . LEU   B 2 88  ? -14.201 0.259   -24.195 1.00 51.29  ? 97  LEU   B CD2 1 
ATOM   960  N N   . LEU   B 2 89  ? -19.233 -0.497  -25.008 1.00 49.19  ? 98  LEU   B N   1 
ATOM   961  C CA  . LEU   B 2 89  ? -20.063 0.596   -25.493 1.00 48.36  ? 98  LEU   B CA  1 
ATOM   962  C C   . LEU   B 2 89  ? -19.387 1.824   -24.886 1.00 47.61  ? 98  LEU   B C   1 
ATOM   963  O O   . LEU   B 2 89  ? -19.672 2.197   -23.752 1.00 47.03  ? 98  LEU   B O   1 
ATOM   964  C CB  . LEU   B 2 89  ? -21.520 0.413   -25.007 1.00 48.34  ? 98  LEU   B CB  1 
ATOM   965  C CG  . LEU   B 2 89  ? -22.576 1.557   -25.140 1.00 49.11  ? 98  LEU   B CG  1 
ATOM   966  C CD1 . LEU   B 2 89  ? -22.330 2.476   -26.322 1.00 49.85  ? 98  LEU   B CD1 1 
ATOM   967  C CD2 . LEU   B 2 89  ? -23.979 0.990   -25.207 1.00 49.25  ? 98  LEU   B CD2 1 
ATOM   968  N N   . ALA   B 2 90  ? -18.402 2.376   -25.605 1.00 47.38  ? 99  ALA   B N   1 
ATOM   969  C CA  . ALA   B 2 90  ? -17.615 3.483   -25.083 1.00 47.73  ? 99  ALA   B CA  1 
ATOM   970  C C   . ALA   B 2 90  ? -18.323 4.804   -25.178 1.00 47.75  ? 99  ALA   B C   1 
ATOM   971  O O   . ALA   B 2 90  ? -18.783 5.176   -26.246 1.00 48.03  ? 99  ALA   B O   1 
ATOM   972  C CB  . ALA   B 2 90  ? -16.274 3.564   -25.783 1.00 47.78  ? 99  ALA   B CB  1 
ATOM   973  N N   . VAL   B 2 91  ? -18.400 5.527   -24.060 1.00 47.05  ? 100 VAL   B N   1 
ATOM   974  C CA  . VAL   B 2 91  ? -19.027 6.842   -24.024 1.00 46.82  ? 100 VAL   B CA  1 
ATOM   975  C C   . VAL   B 2 91  ? -17.918 7.843   -23.660 1.00 47.64  ? 100 VAL   B C   1 
ATOM   976  O O   . VAL   B 2 91  ? -17.685 8.119   -22.484 1.00 48.01  ? 100 VAL   B O   1 
ATOM   977  C CB  . VAL   B 2 91  ? -20.195 6.848   -23.014 1.00 46.03  ? 100 VAL   B CB  1 
ATOM   978  C CG1 . VAL   B 2 91  ? -20.899 8.197   -23.000 1.00 46.43  ? 100 VAL   B CG1 1 
ATOM   979  C CG2 . VAL   B 2 91  ? -21.180 5.729   -23.322 1.00 45.59  ? 100 VAL   B CG2 1 
ATOM   980  N N   . PRO   B 2 92  ? -17.176 8.346   -24.663 1.00 47.58  ? 101 PRO   B N   1 
ATOM   981  C CA  . PRO   B 2 92  ? -16.025 9.210   -24.363 1.00 47.87  ? 101 PRO   B CA  1 
ATOM   982  C C   . PRO   B 2 92  ? -16.377 10.670  -24.154 1.00 48.88  ? 101 PRO   B C   1 
ATOM   983  O O   . PRO   B 2 92  ? -17.352 11.142  -24.723 1.00 49.37  ? 101 PRO   B O   1 
ATOM   984  C CB  . PRO   B 2 92  ? -15.111 9.023   -25.584 1.00 48.30  ? 101 PRO   B CB  1 
ATOM   985  C CG  . PRO   B 2 92  ? -15.858 8.105   -26.539 1.00 48.58  ? 101 PRO   B CG  1 
ATOM   986  C CD  . PRO   B 2 92  ? -17.281 8.077   -26.106 1.00 47.05  ? 101 PRO   B CD  1 
ATOM   987  N N   . PRO   B 2 93  ? -15.579 11.412  -23.372 1.00 49.16  ? 102 PRO   B N   1 
ATOM   988  C CA  . PRO   B 2 93  ? -15.906 12.825  -23.138 1.00 49.40  ? 102 PRO   B CA  1 
ATOM   989  C C   . PRO   B 2 93  ? -16.020 13.650  -24.418 1.00 50.15  ? 102 PRO   B C   1 
ATOM   990  O O   . PRO   B 2 93  ? -15.126 13.619  -25.268 1.00 50.32  ? 102 PRO   B O   1 
ATOM   991  C CB  . PRO   B 2 93  ? -14.785 13.305  -22.214 1.00 50.10  ? 102 PRO   B CB  1 
ATOM   992  C CG  . PRO   B 2 93  ? -14.299 12.046  -21.526 1.00 50.53  ? 102 PRO   B CG  1 
ATOM   993  C CD  . PRO   B 2 93  ? -14.399 10.986  -22.591 1.00 48.83  ? 102 PRO   B CD  1 
ATOM   994  N N   . GLY   B 2 94  ? -17.172 14.310  -24.575 1.00 50.07  ? 103 GLY   B N   1 
ATOM   995  C CA  . GLY   B 2 94  ? -17.487 15.140  -25.734 1.00 50.36  ? 103 GLY   B CA  1 
ATOM   996  C C   . GLY   B 2 94  ? -17.771 14.394  -27.025 1.00 50.61  ? 103 GLY   B C   1 
ATOM   997  O O   . GLY   B 2 94  ? -18.006 15.013  -28.060 1.00 50.56  ? 103 GLY   B O   1 
ATOM   998  N N   . GLU   B 2 95  ? -17.714 13.067  -26.992 1.00 50.87  ? 104 GLU   B N   1 
ATOM   999  C CA  . GLU   B 2 95  ? -17.912 12.251  -28.179 1.00 51.67  ? 104 GLU   B CA  1 
ATOM   1000 C C   . GLU   B 2 95  ? -19.096 11.324  -28.016 1.00 52.32  ? 104 GLU   B C   1 
ATOM   1001 O O   . GLU   B 2 95  ? -19.410 10.906  -26.906 1.00 52.68  ? 104 GLU   B O   1 
ATOM   1002 C CB  . GLU   B 2 95  ? -16.651 11.432  -28.473 1.00 54.32  ? 104 GLU   B CB  1 
ATOM   1003 C CG  . GLU   B 2 95  ? -15.378 12.258  -28.518 1.00 60.14  ? 104 GLU   B CG  1 
ATOM   1004 C CD  . GLU   B 2 95  ? -14.117 11.478  -28.835 1.00 69.05  ? 104 GLU   B CD  1 
ATOM   1005 O OE1 . GLU   B 2 95  ? -14.207 10.242  -29.019 1.00 71.50  ? 104 GLU   B OE1 1 
ATOM   1006 O OE2 . GLU   B 2 95  ? -13.036 12.107  -28.907 1.00 71.56  ? 104 GLU   B OE2 1 
ATOM   1007 N N   . ARG   B 2 96  ? -19.726 10.970  -29.128 1.00 52.49  ? 105 ARG   B N   1 
ATOM   1008 C CA  . ARG   B 2 96  ? -20.892 10.099  -29.171 1.00 53.57  ? 105 ARG   B CA  1 
ATOM   1009 C C   . ARG   B 2 96  ? -20.561 8.650   -28.768 1.00 54.41  ? 105 ARG   B C   1 
ATOM   1010 O O   . ARG   B 2 96  ? -19.438 8.180   -28.998 1.00 54.72  ? 105 ARG   B O   1 
ATOM   1011 C CB  . ARG   B 2 96  ? -21.475 10.161  -30.591 1.00 55.28  ? 105 ARG   B CB  1 
ATOM   1012 C CG  . ARG   B 2 96  ? -22.848 9.543   -30.781 1.00 58.73  ? 105 ARG   B CG  1 
ATOM   1013 C CD  . ARG   B 2 96  ? -23.489 9.988   -32.085 1.00 63.18  ? 105 ARG   B CD  1 
ATOM   1014 N NE  . ARG   B 2 96  ? -22.667 9.705   -33.266 1.00 67.57  ? 105 ARG   B NE  1 
ATOM   1015 C CZ  . ARG   B 2 96  ? -22.129 10.640  -34.048 1.00 70.80  ? 105 ARG   B CZ  1 
ATOM   1016 N NH1 . ARG   B 2 96  ? -22.305 11.928  -33.774 1.00 70.56  ? 105 ARG   B NH1 1 
ATOM   1017 N NH2 . ARG   B 2 96  ? -21.397 10.293  -35.098 1.00 70.99  ? 105 ARG   B NH2 1 
ATOM   1018 N N   . ALA   B 2 97  ? -21.540 7.947   -28.152 1.00 54.42  ? 106 ALA   B N   1 
ATOM   1019 C CA  . ALA   B 2 97  ? -21.411 6.548   -27.734 1.00 54.94  ? 106 ALA   B CA  1 
ATOM   1020 C C   . ALA   B 2 97  ? -21.055 5.680   -28.940 1.00 55.61  ? 106 ALA   B C   1 
ATOM   1021 O O   . ALA   B 2 97  ? -21.606 5.874   -30.021 1.00 55.93  ? 106 ALA   B O   1 
ATOM   1022 C CB  . ALA   B 2 97  ? -22.706 6.065   -27.106 1.00 54.87  ? 106 ALA   B CB  1 
ATOM   1023 N N   . LYS   B 2 98  ? -20.094 4.771   -28.772 1.00 55.72  ? 107 LYS   B N   1 
ATOM   1024 C CA  . LYS   B 2 98  ? -19.596 3.956   -29.871 1.00 56.27  ? 107 LYS   B CA  1 
ATOM   1025 C C   . LYS   B 2 98  ? -19.264 2.535   -29.424 1.00 55.73  ? 107 LYS   B C   1 
ATOM   1026 O O   . LYS   B 2 98  ? -18.538 2.356   -28.458 1.00 56.02  ? 107 LYS   B O   1 
ATOM   1027 C CB  . LYS   B 2 98  ? -18.355 4.659   -30.429 1.00 59.31  ? 107 LYS   B CB  1 
ATOM   1028 C CG  . LYS   B 2 98  ? -17.624 3.970   -31.565 1.00 64.63  ? 107 LYS   B CG  1 
ATOM   1029 C CD  . LYS   B 2 98  ? -16.322 4.729   -31.897 1.00 69.77  ? 107 LYS   B CD  1 
ATOM   1030 C CE  . LYS   B 2 98  ? -15.504 5.059   -30.654 1.00 73.47  ? 107 LYS   B CE  1 
ATOM   1031 N NZ  . LYS   B 2 98  ? -14.088 5.397   -30.969 1.00 76.02  ? 107 LYS   B NZ  1 
ATOM   1032 N N   . ASN   B 2 99  ? -19.804 1.525   -30.111 1.00 55.15  ? 108 ASN   B N   1 
ATOM   1033 C CA  . ASN   B 2 99  ? -19.551 0.130   -29.763 1.00 55.40  ? 108 ASN   B CA  1 
ATOM   1034 C C   . ASN   B 2 99  ? -18.270 -0.364  -30.408 1.00 55.77  ? 108 ASN   B C   1 
ATOM   1035 O O   . ASN   B 2 99  ? -18.103 -0.223  -31.615 1.00 56.42  ? 108 ASN   B O   1 
ATOM   1036 C CB  . ASN   B 2 99  ? -20.691 -0.765  -30.228 1.00 56.24  ? 108 ASN   B CB  1 
ATOM   1037 C CG  . ASN   B 2 99  ? -22.015 -0.481  -29.588 1.00 59.50  ? 108 ASN   B CG  1 
ATOM   1038 O OD1 . ASN   B 2 99  ? -22.619 0.576   -29.795 1.00 61.16  ? 108 ASN   B OD1 1 
ATOM   1039 N ND2 . ASN   B 2 99  ? -22.516 -1.437  -28.824 1.00 59.78  ? 108 ASN   B ND2 1 
ATOM   1040 N N   . ILE   B 2 100 ? -17.378 -0.958  -29.625 1.00 55.27  ? 109 ILE   B N   1 
ATOM   1041 C CA  . ILE   B 2 100 ? -16.130 -1.492  -30.150 1.00 55.69  ? 109 ILE   B CA  1 
ATOM   1042 C C   . ILE   B 2 100 ? -16.033 -2.965  -29.811 1.00 56.25  ? 109 ILE   B C   1 
ATOM   1043 O O   . ILE   B 2 100 ? -15.813 -3.300  -28.655 1.00 56.52  ? 109 ILE   B O   1 
ATOM   1044 C CB  . ILE   B 2 100 ? -14.913 -0.765  -29.556 1.00 56.26  ? 109 ILE   B CB  1 
ATOM   1045 C CG1 . ILE   B 2 100 ? -15.055 0.765   -29.609 1.00 57.16  ? 109 ILE   B CG1 1 
ATOM   1046 C CG2 . ILE   B 2 100 ? -13.623 -1.256  -30.209 1.00 56.70  ? 109 ILE   B CG2 1 
ATOM   1047 C CD1 . ILE   B 2 100 ? -14.959 1.371   -30.971 1.00 58.32  ? 109 ILE   B CD1 1 
ATOM   1048 N N   . GLN   B 2 101 ? -16.161 -3.843  -30.801 1.00 56.54  ? 110 GLN   B N   1 
ATOM   1049 C CA  . GLN   B 2 101 ? -16.040 -5.280  -30.576 1.00 57.16  ? 110 GLN   B CA  1 
ATOM   1050 C C   . GLN   B 2 101 ? -14.574 -5.648  -30.362 1.00 58.00  ? 110 GLN   B C   1 
ATOM   1051 O O   . GLN   B 2 101 ? -13.711 -5.199  -31.108 1.00 58.36  ? 110 GLN   B O   1 
ATOM   1052 C CB  . GLN   B 2 101 ? -16.592 -6.046  -31.781 1.00 58.23  ? 110 GLN   B CB  1 
ATOM   1053 C CG  . GLN   B 2 101 ? -16.768 -7.541  -31.558 1.00 59.79  ? 110 GLN   B CG  1 
ATOM   1054 C CD  . GLN   B 2 101 ? -17.784 -8.071  -32.537 1.00 62.39  ? 110 GLN   B CD  1 
ATOM   1055 O OE1 . GLN   B 2 101 ? -18.815 -7.435  -32.800 1.00 63.93  ? 110 GLN   B OE1 1 
ATOM   1056 N NE2 . GLN   B 2 101 ? -17.517 -9.232  -33.110 1.00 61.71  ? 110 GLN   B NE2 1 
ATOM   1057 N N   . THR   B 2 102 ? -14.285 -6.455  -29.336 1.00 58.00  ? 111 THR   B N   1 
ATOM   1058 C CA  . THR   B 2 102 ? -12.922 -6.877  -29.033 1.00 58.41  ? 111 THR   B CA  1 
ATOM   1059 C C   . THR   B 2 102 ? -12.928 -8.255  -28.365 1.00 58.50  ? 111 THR   B C   1 
ATOM   1060 O O   . THR   B 2 102 ? -13.969 -8.655  -27.850 1.00 58.81  ? 111 THR   B O   1 
ATOM   1061 C CB  . THR   B 2 102 ? -12.269 -5.844  -28.093 1.00 60.13  ? 111 THR   B CB  1 
ATOM   1062 O OG1 . THR   B 2 102 ? -10.942 -6.273  -27.776 1.00 61.52  ? 111 THR   B OG1 1 
ATOM   1063 C CG2 . THR   B 2 102 ? -13.076 -5.608  -26.819 1.00 60.32  ? 111 THR   B CG2 1 
ATOM   1064 N N   . LEU   B 2 103 ? -11.784 -8.983  -28.359 1.00 58.05  ? 112 LEU   B N   1 
ATOM   1065 C CA  . LEU   B 2 103 ? -11.722 -10.247 -27.633 1.00 58.55  ? 112 LEU   B CA  1 
ATOM   1066 C C   . LEU   B 2 103 ? -10.900 -9.973  -26.394 1.00 59.57  ? 112 LEU   B C   1 
ATOM   1067 O O   . LEU   B 2 103 ? -9.744  -9.547  -26.498 1.00 60.20  ? 112 LEU   B O   1 
ATOM   1068 C CB  . LEU   B 2 103 ? -11.096 -11.412 -28.396 1.00 58.68  ? 112 LEU   B CB  1 
ATOM   1069 C CG  . LEU   B 2 103 ? -11.129 -12.718 -27.583 1.00 60.15  ? 112 LEU   B CG  1 
ATOM   1070 C CD1 . LEU   B 2 103 ? -12.361 -13.505 -27.876 1.00 60.87  ? 112 LEU   B CD1 1 
ATOM   1071 C CD2 . LEU   B 2 103 ? -9.899  -13.542 -27.771 1.00 60.83  ? 112 LEU   B CD2 1 
ATOM   1072 N N   . PRO   B 2 104 ? -11.467 -10.215 -25.208 1.00 59.11  ? 113 PRO   B N   1 
ATOM   1073 C CA  . PRO   B 2 104 ? -10.722 -9.916  -23.987 1.00 58.98  ? 113 PRO   B CA  1 
ATOM   1074 C C   . PRO   B 2 104 ? -9.612  -10.906 -23.683 1.00 59.33  ? 113 PRO   B C   1 
ATOM   1075 O O   . PRO   B 2 104 ? -9.653  -12.067 -24.100 1.00 59.67  ? 113 PRO   B O   1 
ATOM   1076 C CB  . PRO   B 2 104 ? -11.788 -9.929  -22.887 1.00 59.37  ? 113 PRO   B CB  1 
ATOM   1077 C CG  . PRO   B 2 104 ? -13.080 -10.195 -23.555 1.00 59.95  ? 113 PRO   B CG  1 
ATOM   1078 C CD  . PRO   B 2 104 ? -12.820 -10.720 -24.921 1.00 58.42  ? 113 PRO   B CD  1 
ATOM   1079 N N   . GLY   B 2 105 ? -8.626  -10.411 -22.946 1.00 58.54  ? 114 GLY   B N   1 
ATOM   1080 C CA  . GLY   B 2 105 ? -7.520  -11.189 -22.426 1.00 57.98  ? 114 GLY   B CA  1 
ATOM   1081 C C   . GLY   B 2 105 ? -7.889  -11.667 -21.034 1.00 57.44  ? 114 GLY   B C   1 
ATOM   1082 O O   . GLY   B 2 105 ? -9.075  -11.826 -20.723 1.00 57.75  ? 114 GLY   B O   1 
ATOM   1083 N N   . ILE   B 2 106 ? -6.892  -11.898 -20.180 1.00 56.46  ? 115 ILE   B N   1 
ATOM   1084 C CA  . ILE   B 2 106 ? -7.136  -12.417 -18.841 1.00 56.74  ? 115 ILE   B CA  1 
ATOM   1085 C C   . ILE   B 2 106 ? -6.236  -11.735 -17.814 1.00 56.78  ? 115 ILE   B C   1 
ATOM   1086 O O   . ILE   B 2 106 ? -5.027  -11.647 -18.019 1.00 57.29  ? 115 ILE   B O   1 
ATOM   1087 C CB  . ILE   B 2 106 ? -6.833  -13.944 -18.793 1.00 57.65  ? 115 ILE   B CB  1 
ATOM   1088 C CG1 . ILE   B 2 106 ? -7.647  -14.778 -19.793 1.00 58.99  ? 115 ILE   B CG1 1 
ATOM   1089 C CG2 . ILE   B 2 106 ? -6.981  -14.491 -17.395 1.00 58.61  ? 115 ILE   B CG2 1 
ATOM   1090 C CD1 . ILE   B 2 106 ? -9.053  -14.949 -19.480 1.00 60.52  ? 115 ILE   B CD1 1 
ATOM   1091 N N   . PHE   B 2 107 ? -6.803  -11.354 -16.673 1.00 56.07  ? 116 PHE   B N   1 
ATOM   1092 C CA  . PHE   B 2 107 ? -6.054  -10.864 -15.532 1.00 56.09  ? 116 PHE   B CA  1 
ATOM   1093 C C   . PHE   B 2 107 ? -5.953  -12.090 -14.653 1.00 56.47  ? 116 PHE   B C   1 
ATOM   1094 O O   . PHE   B 2 107 ? -6.981  -12.546 -14.161 1.00 56.81  ? 116 PHE   B O   1 
ATOM   1095 C CB  . PHE   B 2 107 ? -6.874  -9.823  -14.758 1.00 55.75  ? 116 PHE   B CB  1 
ATOM   1096 C CG  . PHE   B 2 107 ? -6.638  -8.374  -15.097 1.00 56.14  ? 116 PHE   B CG  1 
ATOM   1097 C CD1 . PHE   B 2 107 ? -6.013  -8.014  -16.279 1.00 56.88  ? 116 PHE   B CD1 1 
ATOM   1098 C CD2 . PHE   B 2 107 ? -7.082  -7.369  -14.254 1.00 56.84  ? 116 PHE   B CD2 1 
ATOM   1099 C CE1 . PHE   B 2 107 ? -5.843  -6.677  -16.613 1.00 57.56  ? 116 PHE   B CE1 1 
ATOM   1100 C CE2 . PHE   B 2 107 ? -6.880  -6.033  -14.575 1.00 57.54  ? 116 PHE   B CE2 1 
ATOM   1101 C CZ  . PHE   B 2 107 ? -6.279  -5.695  -15.761 1.00 57.38  ? 116 PHE   B CZ  1 
ATOM   1102 N N   . LYS   B 2 108 ? -4.758  -12.660 -14.484 1.00 56.35  ? 117 LYS   B N   1 
ATOM   1103 C CA  . LYS   B 2 108 ? -4.578  -13.823 -13.620 1.00 56.66  ? 117 LYS   B CA  1 
ATOM   1104 C C   . LYS   B 2 108 ? -4.181  -13.302 -12.245 1.00 55.68  ? 117 LYS   B C   1 
ATOM   1105 O O   . LYS   B 2 108 ? -3.192  -12.585 -12.143 1.00 55.15  ? 117 LYS   B O   1 
ATOM   1106 C CB  . LYS   B 2 108 ? -3.489  -14.765 -14.186 1.00 59.91  ? 117 LYS   B CB  1 
ATOM   1107 C CG  . LYS   B 2 108 ? -3.870  -15.400 -15.519 1.00 66.51  ? 117 LYS   B CG  1 
ATOM   1108 C CD  . LYS   B 2 108 ? -2.700  -16.131 -16.199 1.00 73.59  ? 117 LYS   B CD  1 
ATOM   1109 C CE  . LYS   B 2 108 ? -3.033  -16.546 -17.631 1.00 79.08  ? 117 LYS   B CE  1 
ATOM   1110 N NZ  . LYS   B 2 108 ? -1.864  -17.123 -18.378 1.00 81.34  ? 117 LYS   B NZ  1 
ATOM   1111 N N   . THR   B 2 109 ? -4.982  -13.601 -11.202 1.00 55.57  ? 118 THR   B N   1 
ATOM   1112 C CA  . THR   B 2 109 ? -4.753  -13.152 -9.805  1.00 55.47  ? 118 THR   B CA  1 
ATOM   1113 C C   . THR   B 2 109 ? -4.649  -14.361 -8.834  1.00 55.04  ? 118 THR   B C   1 
ATOM   1114 O O   . THR   B 2 109 ? -4.874  -15.497 -9.248  1.00 55.00  ? 118 THR   B O   1 
ATOM   1115 C CB  . THR   B 2 109 ? -5.878  -12.153 -9.332  1.00 56.87  ? 118 THR   B CB  1 
ATOM   1116 O OG1 . THR   B 2 109 ? -7.070  -12.869 -8.999  1.00 58.09  ? 118 THR   B OG1 1 
ATOM   1117 C CG2 . THR   B 2 109 ? -6.174  -11.045 -10.325 1.00 57.11  ? 118 THR   B CG2 1 
ATOM   1118 N N   . LYS   B 2 110 ? -4.335  -14.118 -7.541  1.00 54.76  ? 119 LYS   B N   1 
ATOM   1119 C CA  . LYS   B 2 110 ? -4.290  -15.176 -6.523  1.00 54.95  ? 119 LYS   B CA  1 
ATOM   1120 C C   . LYS   B 2 110 ? -5.699  -15.678 -6.126  1.00 55.75  ? 119 LYS   B C   1 
ATOM   1121 O O   . LYS   B 2 110 ? -5.806  -16.719 -5.478  1.00 55.81  ? 119 LYS   B O   1 
ATOM   1122 C CB  . LYS   B 2 110 ? -3.525  -14.708 -5.276  1.00 55.25  ? 119 LYS   B CB  1 
ATOM   1123 C CG  . LYS   B 2 110 ? -4.237  -13.621 -4.510  1.00 58.29  ? 119 LYS   B CG  1 
ATOM   1124 C CD  . LYS   B 2 110 ? -3.449  -13.185 -3.290  1.00 62.34  ? 119 LYS   B CD  1 
ATOM   1125 C CE  . LYS   B 2 110 ? -4.337  -12.930 -2.094  1.00 65.60  ? 119 LYS   B CE  1 
ATOM   1126 N NZ  . LYS   B 2 110 ? -5.255  -11.781 -2.312  1.00 67.39  ? 119 LYS   B NZ  1 
ATOM   1127 N N   . ASP   B 2 111 ? -6.767  -14.945 -6.516  1.00 56.11  ? 120 ASP   B N   1 
ATOM   1128 C CA  . ASP   B 2 111 ? -8.153  -15.288 -6.221  1.00 56.91  ? 120 ASP   B CA  1 
ATOM   1129 C C   . ASP   B 2 111 ? -8.967  -15.660 -7.459  1.00 57.73  ? 120 ASP   B C   1 
ATOM   1130 O O   . ASP   B 2 111 ? -10.194 -15.605 -7.400  1.00 58.38  ? 120 ASP   B O   1 
ATOM   1131 C CB  . ASP   B 2 111 ? -8.840  -14.109 -5.533  1.00 58.96  ? 120 ASP   B CB  1 
ATOM   1132 C CG  . ASP   B 2 111 ? -8.358  -13.861 -4.128  1.00 63.99  ? 120 ASP   B CG  1 
ATOM   1133 O OD1 . ASP   B 2 111 ? -8.341  -14.824 -3.329  1.00 64.50  ? 120 ASP   B OD1 1 
ATOM   1134 O OD2 . ASP   B 2 111 ? -8.012  -12.700 -3.818  1.00 66.50  ? 120 ASP   B OD2 1 
ATOM   1135 N N   . GLY   B 2 112 ? -8.315  -16.005 -8.564  1.00 57.51  ? 121 GLY   B N   1 
ATOM   1136 C CA  . GLY   B 2 112 ? -9.021  -16.387 -9.779  1.00 57.72  ? 121 GLY   B CA  1 
ATOM   1137 C C   . GLY   B 2 112 ? -8.818  -15.436 -10.935 1.00 57.88  ? 121 GLY   B C   1 
ATOM   1138 O O   . GLY   B 2 112 ? -8.386  -14.300 -10.737 1.00 58.34  ? 121 GLY   B O   1 
ATOM   1139 N N   . ASP   B 2 113 ? -9.146  -15.886 -12.151 1.00 57.44  ? 122 ASP   B N   1 
ATOM   1140 C CA  . ASP   B 2 113 ? -8.993  -15.086 -13.360 1.00 57.60  ? 122 ASP   B CA  1 
ATOM   1141 C C   . ASP   B 2 113 ? -10.205 -14.227 -13.699 1.00 57.65  ? 122 ASP   B C   1 
ATOM   1142 O O   . ASP   B 2 113 ? -11.349 -14.633 -13.496 1.00 58.10  ? 122 ASP   B O   1 
ATOM   1143 C CB  . ASP   B 2 113 ? -8.633  -15.975 -14.556 1.00 59.16  ? 122 ASP   B CB  1 
ATOM   1144 C CG  . ASP   B 2 113 ? -7.297  -16.681 -14.432 1.00 64.71  ? 122 ASP   B CG  1 
ATOM   1145 O OD1 . ASP   B 2 113 ? -6.700  -16.651 -13.316 1.00 65.36  ? 122 ASP   B OD1 1 
ATOM   1146 O OD2 . ASP   B 2 113 ? -6.851  -17.289 -15.440 1.00 67.07  ? 122 ASP   B OD2 1 
ATOM   1147 N N   . ILE   B 2 114 ? -9.937  -13.038 -14.243 1.00 56.72  ? 123 ILE   B N   1 
ATOM   1148 C CA  . ILE   B 2 114 ? -10.945 -12.056 -14.632 1.00 56.50  ? 123 ILE   B CA  1 
ATOM   1149 C C   . ILE   B 2 114 ? -10.715 -11.687 -16.108 1.00 55.74  ? 123 ILE   B C   1 
ATOM   1150 O O   . ILE   B 2 114 ? -9.606  -11.849 -16.619 1.00 55.79  ? 123 ILE   B O   1 
ATOM   1151 C CB  . ILE   B 2 114 ? -10.797 -10.793 -13.723 1.00 57.21  ? 123 ILE   B CB  1 
ATOM   1152 C CG1 . ILE   B 2 114 ? -10.801 -11.150 -12.230 1.00 58.65  ? 123 ILE   B CG1 1 
ATOM   1153 C CG2 . ILE   B 2 114 ? -11.840 -9.739  -14.013 1.00 57.42  ? 123 ILE   B CG2 1 
ATOM   1154 C CD1 . ILE   B 2 114 ? -10.263 -10.080 -11.368 1.00 60.21  ? 123 ILE   B CD1 1 
ATOM   1155 N N   . GLY   B 2 115 ? -11.747 -11.183 -16.774 1.00 54.53  ? 124 GLY   B N   1 
ATOM   1156 C CA  . GLY   B 2 115 ? -11.600 -10.718 -18.147 1.00 54.43  ? 124 GLY   B CA  1 
ATOM   1157 C C   . GLY   B 2 115 ? -10.803 -9.426  -18.202 1.00 53.84  ? 124 GLY   B C   1 
ATOM   1158 O O   . GLY   B 2 115 ? -10.582 -8.779  -17.169 1.00 53.51  ? 124 GLY   B O   1 
ATOM   1159 N N   . ALA   B 2 116 ? -10.364 -9.028  -19.409 1.00 53.35  ? 125 ALA   B N   1 
ATOM   1160 C CA  . ALA   B 2 116 ? -9.601  -7.787  -19.559 1.00 53.45  ? 125 ALA   B CA  1 
ATOM   1161 C C   . ALA   B 2 116 ? -9.665  -7.215  -20.969 1.00 53.55  ? 125 ALA   B C   1 
ATOM   1162 O O   . ALA   B 2 116 ? -9.221  -7.861  -21.910 1.00 53.99  ? 125 ALA   B O   1 
ATOM   1163 C CB  . ALA   B 2 116 ? -8.146  -7.995  -19.154 1.00 53.44  ? 125 ALA   B CB  1 
ATOM   1164 N N   . VAL   B 2 117 ? -10.181 -5.997  -21.114 1.00 53.07  ? 126 VAL   B N   1 
ATOM   1165 C CA  A VAL   B 2 117 ? -10.254 -5.357  -22.425 0.50 53.46  ? 126 VAL   B CA  1 
ATOM   1166 C CA  B VAL   B 2 117 ? -10.284 -5.331  -22.404 0.50 53.46  ? 126 VAL   B CA  1 
ATOM   1167 C C   . VAL   B 2 117 ? -9.090  -4.378  -22.620 1.00 53.95  ? 126 VAL   B C   1 
ATOM   1168 O O   . VAL   B 2 117 ? -8.796  -3.556  -21.746 1.00 53.97  ? 126 VAL   B O   1 
ATOM   1169 C CB  A VAL   B 2 117 ? -11.635 -4.733  -22.735 0.50 53.89  ? 126 VAL   B CB  1 
ATOM   1170 C CB  B VAL   B 2 117 ? -11.643 -4.598  -22.493 0.50 53.89  ? 126 VAL   B CB  1 
ATOM   1171 C CG1 A VAL   B 2 117 ? -12.681 -5.818  -22.963 0.50 54.31  ? 126 VAL   B CG1 1 
ATOM   1172 C CG1 B VAL   B 2 117 ? -11.786 -3.867  -23.814 0.50 54.42  ? 126 VAL   B CG1 1 
ATOM   1173 C CG2 A VAL   B 2 117 ? -12.074 -3.784  -21.632 0.50 54.28  ? 126 VAL   B CG2 1 
ATOM   1174 C CG2 B VAL   B 2 117 ? -12.796 -5.573  -22.293 0.50 54.25  ? 126 VAL   B CG2 1 
ATOM   1175 N N   . ALA   B 2 118 ? -8.393  -4.497  -23.768 1.00 54.19  ? 127 ALA   B N   1 
ATOM   1176 C CA  . ALA   B 2 118 ? -7.247  -3.645  -24.087 1.00 54.92  ? 127 ALA   B CA  1 
ATOM   1177 C C   . ALA   B 2 118 ? -7.609  -2.621  -25.154 1.00 55.98  ? 127 ALA   B C   1 
ATOM   1178 O O   . ALA   B 2 118 ? -7.358  -2.815  -26.339 1.00 56.55  ? 127 ALA   B O   1 
ATOM   1179 C CB  . ALA   B 2 118 ? -6.063  -4.483  -24.537 1.00 54.75  ? 127 ALA   B CB  1 
ATOM   1180 N N   . LEU   B 2 119 ? -8.256  -1.556  -24.734 1.00 56.23  ? 128 LEU   B N   1 
ATOM   1181 C CA  . LEU   B 2 119 ? -8.641  -0.469  -25.608 1.00 57.12  ? 128 LEU   B CA  1 
ATOM   1182 C C   . LEU   B 2 119 ? -8.174  0.839   -24.973 1.00 58.20  ? 128 LEU   B C   1 
ATOM   1183 O O   . LEU   B 2 119 ? -8.085  0.946   -23.750 1.00 59.00  ? 128 LEU   B O   1 
ATOM   1184 C CB  . LEU   B 2 119 ? -10.151 -0.465  -25.853 1.00 57.51  ? 128 LEU   B CB  1 
ATOM   1185 C CG  . LEU   B 2 119 ? -10.699 -1.659  -26.630 1.00 59.32  ? 128 LEU   B CG  1 
ATOM   1186 C CD1 . LEU   B 2 119 ? -12.214 -1.663  -26.613 1.00 59.89  ? 128 LEU   B CD1 1 
ATOM   1187 C CD2 . LEU   B 2 119 ? -10.189 -1.672  -28.072 1.00 60.06  ? 128 LEU   B CD2 1 
ATOM   1188 N N   . ASP   B 2 120 ? -7.866  1.832   -25.796 1.00 58.45  ? 129 ASP   B N   1 
ATOM   1189 C CA  . ASP   B 2 120 ? -7.319  3.095   -25.316 1.00 58.82  ? 129 ASP   B CA  1 
ATOM   1190 C C   . ASP   B 2 120 ? -8.300  4.262   -25.317 1.00 58.22  ? 129 ASP   B C   1 
ATOM   1191 O O   . ASP   B 2 120 ? -8.619  4.815   -26.370 1.00 58.04  ? 129 ASP   B O   1 
ATOM   1192 C CB  . ASP   B 2 120 ? -6.062  3.439   -26.118 1.00 61.06  ? 129 ASP   B CB  1 
ATOM   1193 C CG  . ASP   B 2 120 ? -5.049  2.316   -26.063 1.00 66.59  ? 129 ASP   B CG  1 
ATOM   1194 O OD1 . ASP   B 2 120 ? -4.778  1.816   -24.941 1.00 67.34  ? 129 ASP   B OD1 1 
ATOM   1195 O OD2 . ASP   B 2 120 ? -4.554  1.908   -27.145 1.00 69.05  ? 129 ASP   B OD2 1 
ATOM   1196 N N   . TYR   B 2 121 ? -8.744  4.659   -24.124 1.00 57.63  ? 130 TYR   B N   1 
ATOM   1197 C CA  . TYR   B 2 121 ? -9.686  5.765   -23.951 1.00 57.82  ? 130 TYR   B CA  1 
ATOM   1198 C C   . TYR   B 2 121 ? -9.281  6.656   -22.770 1.00 56.63  ? 130 TYR   B C   1 
ATOM   1199 O O   . TYR   B 2 121 ? -8.605  6.184   -21.850 1.00 57.05  ? 130 TYR   B O   1 
ATOM   1200 C CB  . TYR   B 2 121 ? -11.109 5.215   -23.725 1.00 58.64  ? 130 TYR   B CB  1 
ATOM   1201 C CG  . TYR   B 2 121 ? -11.758 4.750   -25.003 1.00 60.29  ? 130 TYR   B CG  1 
ATOM   1202 C CD1 . TYR   B 2 121 ? -12.565 5.600   -25.746 1.00 61.73  ? 130 TYR   B CD1 1 
ATOM   1203 C CD2 . TYR   B 2 121 ? -11.558 3.462   -25.477 1.00 61.73  ? 130 TYR   B CD2 1 
ATOM   1204 C CE1 . TYR   B 2 121 ? -13.124 5.191   -26.951 1.00 63.13  ? 130 TYR   B CE1 1 
ATOM   1205 C CE2 . TYR   B 2 121 ? -12.094 3.048   -26.689 1.00 62.97  ? 130 TYR   B CE2 1 
ATOM   1206 C CZ  . TYR   B 2 121 ? -12.878 3.914   -27.423 1.00 64.18  ? 130 TYR   B CZ  1 
ATOM   1207 O OH  . TYR   B 2 121 ? -13.419 3.489   -28.608 1.00 66.11  ? 130 TYR   B OH  1 
ATOM   1208 N N   . PRO   B 2 122 ? -9.713  7.937   -22.749 1.00 54.82  ? 131 PRO   B N   1 
ATOM   1209 C CA  . PRO   B 2 122 ? -9.397  8.787   -21.585 1.00 53.41  ? 131 PRO   B CA  1 
ATOM   1210 C C   . PRO   B 2 122 ? -10.029 8.242   -20.297 1.00 51.76  ? 131 PRO   B C   1 
ATOM   1211 O O   . PRO   B 2 122 ? -11.043 7.543   -20.363 1.00 52.22  ? 131 PRO   B O   1 
ATOM   1212 C CB  . PRO   B 2 122 ? -9.986  10.155  -21.959 1.00 54.12  ? 131 PRO   B CB  1 
ATOM   1213 C CG  . PRO   B 2 122 ? -10.291 10.085  -23.422 1.00 54.84  ? 131 PRO   B CG  1 
ATOM   1214 C CD  . PRO   B 2 122 ? -10.542 8.652   -23.739 1.00 53.82  ? 131 PRO   B CD  1 
ATOM   1215 N N   . ALA   B 2 123 ? -9.444  8.558   -19.128 1.00 49.64  ? 132 ALA   B N   1 
ATOM   1216 C CA  . ALA   B 2 123 ? -9.947  8.082   -17.835 1.00 48.22  ? 132 ALA   B CA  1 
ATOM   1217 C C   . ALA   B 2 123 ? -11.432 8.393   -17.595 1.00 47.04  ? 132 ALA   B C   1 
ATOM   1218 O O   . ALA   B 2 123 ? -12.101 7.641   -16.883 1.00 46.99  ? 132 ALA   B O   1 
ATOM   1219 C CB  . ALA   B 2 123 ? -9.099  8.630   -16.702 1.00 47.94  ? 132 ALA   B CB  1 
ATOM   1220 N N   . GLY   B 2 124 ? -11.938 9.454   -18.235 1.00 45.73  ? 133 GLY   B N   1 
ATOM   1221 C CA  . GLY   B 2 124 ? -13.337 9.866   -18.159 1.00 44.77  ? 133 GLY   B CA  1 
ATOM   1222 C C   . GLY   B 2 124 ? -14.320 8.920   -18.832 1.00 43.71  ? 133 GLY   B C   1 
ATOM   1223 O O   . GLY   B 2 124 ? -15.535 9.122   -18.745 1.00 43.56  ? 133 GLY   B O   1 
ATOM   1224 N N   . THR   B 2 125 ? -13.810 7.884   -19.535 1.00 42.80  ? 134 THR   B N   1 
ATOM   1225 C CA  . THR   B 2 125 ? -14.651 6.862   -20.168 1.00 42.33  ? 134 THR   B CA  1 
ATOM   1226 C C   . THR   B 2 125 ? -15.093 5.774   -19.140 1.00 41.35  ? 134 THR   B C   1 
ATOM   1227 O O   . THR   B 2 125 ? -15.977 4.976   -19.451 1.00 41.27  ? 134 THR   B O   1 
ATOM   1228 C CB  . THR   B 2 125 ? -13.951 6.300   -21.429 1.00 43.92  ? 134 THR   B CB  1 
ATOM   1229 O OG1 . THR   B 2 125 ? -13.535 7.387   -22.262 1.00 44.58  ? 134 THR   B OG1 1 
ATOM   1230 C CG2 . THR   B 2 125 ? -14.849 5.378   -22.249 1.00 44.47  ? 134 THR   B CG2 1 
ATOM   1231 N N   . SER   B 2 126 ? -14.492 5.776   -17.912 1.00 40.54  ? 135 SER   B N   1 
ATOM   1232 C CA  . SER   B 2 126 ? -14.718 4.860   -16.784 1.00 40.48  ? 135 SER   B CA  1 
ATOM   1233 C C   . SER   B 2 126 ? -16.182 4.688   -16.425 1.00 40.18  ? 135 SER   B C   1 
ATOM   1234 O O   . SER   B 2 126 ? -16.832 5.651   -16.072 1.00 40.12  ? 135 SER   B O   1 
ATOM   1235 C CB  . SER   B 2 126 ? -13.991 5.366   -15.541 1.00 41.77  ? 135 SER   B CB  1 
ATOM   1236 O OG  . SER   B 2 126 ? -12.582 5.434   -15.697 1.00 44.25  ? 135 SER   B OG  1 
ATOM   1237 N N   . GLY   B 2 127 ? -16.654 3.455   -16.422 1.00 39.72  ? 136 GLY   B N   1 
ATOM   1238 C CA  . GLY   B 2 127 ? -18.035 3.132   -16.109 1.00 40.02  ? 136 GLY   B CA  1 
ATOM   1239 C C   . GLY   B 2 127 ? -18.814 2.615   -17.303 1.00 40.61  ? 136 GLY   B C   1 
ATOM   1240 O O   . GLY   B 2 127 ? -19.907 2.071   -17.134 1.00 40.95  ? 136 GLY   B O   1 
ATOM   1241 N N   . SER   B 2 128 ? -18.266 2.788   -18.524 1.00 40.35  ? 137 SER   B N   1 
ATOM   1242 C CA  . SER   B 2 128 ? -18.873 2.320   -19.757 1.00 40.76  ? 137 SER   B CA  1 
ATOM   1243 C C   . SER   B 2 128 ? -19.036 0.805   -19.720 1.00 41.53  ? 137 SER   B C   1 
ATOM   1244 O O   . SER   B 2 128 ? -18.111 0.073   -19.363 1.00 41.14  ? 137 SER   B O   1 
ATOM   1245 C CB  . SER   B 2 128 ? -18.026 2.725   -20.961 1.00 41.31  ? 137 SER   B CB  1 
ATOM   1246 O OG  . SER   B 2 128 ? -18.033 4.130   -21.137 1.00 42.17  ? 137 SER   B OG  1 
ATOM   1247 N N   . PRO   B 2 129 ? -20.231 0.318   -20.078 1.00 42.23  ? 138 PRO   B N   1 
ATOM   1248 C CA  . PRO   B 2 129 ? -20.467 -1.129  -20.017 1.00 42.50  ? 138 PRO   B CA  1 
ATOM   1249 C C   . PRO   B 2 129 ? -19.807 -1.947  -21.109 1.00 43.21  ? 138 PRO   B C   1 
ATOM   1250 O O   . PRO   B 2 129 ? -19.613 -1.497  -22.239 1.00 43.34  ? 138 PRO   B O   1 
ATOM   1251 C CB  . PRO   B 2 129 ? -21.985 -1.239  -20.133 1.00 43.16  ? 138 PRO   B CB  1 
ATOM   1252 C CG  . PRO   B 2 129 ? -22.384 -0.025  -20.915 1.00 43.74  ? 138 PRO   B CG  1 
ATOM   1253 C CD  . PRO   B 2 129 ? -21.441 1.060   -20.492 1.00 41.95  ? 138 PRO   B CD  1 
ATOM   1254 N N   . ILE   B 2 130 ? -19.509 -3.186  -20.758 1.00 43.26  ? 139 ILE   B N   1 
ATOM   1255 C CA  . ILE   B 2 130 ? -18.991 -4.193  -21.658 1.00 43.38  ? 139 ILE   B CA  1 
ATOM   1256 C C   . ILE   B 2 130 ? -20.162 -5.151  -21.872 1.00 44.34  ? 139 ILE   B C   1 
ATOM   1257 O O   . ILE   B 2 130 ? -20.851 -5.522  -20.921 1.00 44.11  ? 139 ILE   B O   1 
ATOM   1258 C CB  . ILE   B 2 130 ? -17.770 -4.859  -21.033 1.00 43.47  ? 139 ILE   B CB  1 
ATOM   1259 C CG1 . ILE   B 2 130 ? -16.633 -3.845  -20.892 1.00 44.20  ? 139 ILE   B CG1 1 
ATOM   1260 C CG2 . ILE   B 2 130 ? -17.344 -6.067  -21.839 1.00 43.81  ? 139 ILE   B CG2 1 
ATOM   1261 C CD1 . ILE   B 2 130 ? -15.663 -4.224  -19.821 1.00 45.49  ? 139 ILE   B CD1 1 
ATOM   1262 N N   . LEU   B 2 131 ? -20.457 -5.469  -23.129 1.00 45.24  ? 140 LEU   B N   1 
ATOM   1263 C CA  . LEU   B 2 131 ? -21.622 -6.269  -23.473 1.00 46.49  ? 140 LEU   B CA  1 
ATOM   1264 C C   . LEU   B 2 131 ? -21.339 -7.629  -24.065 1.00 48.01  ? 140 LEU   B C   1 
ATOM   1265 O O   . LEU   B 2 131 ? -20.318 -7.839  -24.724 1.00 48.17  ? 140 LEU   B O   1 
ATOM   1266 C CB  . LEU   B 2 131 ? -22.472 -5.495  -24.487 1.00 46.74  ? 140 LEU   B CB  1 
ATOM   1267 C CG  . LEU   B 2 131 ? -22.822 -4.058  -24.168 1.00 47.93  ? 140 LEU   B CG  1 
ATOM   1268 C CD1 . LEU   B 2 131 ? -23.726 -3.497  -25.238 1.00 48.33  ? 140 LEU   B CD1 1 
ATOM   1269 C CD2 . LEU   B 2 131 ? -23.448 -3.936  -22.780 1.00 48.27  ? 140 LEU   B CD2 1 
ATOM   1270 N N   . ASP   B 2 132 ? -22.284 -8.549  -23.871 1.00 48.80  ? 141 ASP   B N   1 
ATOM   1271 C CA  . ASP   B 2 132 ? -22.212 -9.838  -24.533 1.00 50.18  ? 141 ASP   B CA  1 
ATOM   1272 C C   . ASP   B 2 132 ? -23.070 -9.741  -25.826 1.00 51.81  ? 141 ASP   B C   1 
ATOM   1273 O O   . ASP   B 2 132 ? -23.686 -8.693  -26.070 1.00 51.61  ? 141 ASP   B O   1 
ATOM   1274 C CB  . ASP   B 2 132 ? -22.617 -10.988 -23.593 1.00 51.57  ? 141 ASP   B CB  1 
ATOM   1275 C CG  . ASP   B 2 132 ? -24.069 -11.065 -23.184 1.00 56.17  ? 141 ASP   B CG  1 
ATOM   1276 O OD1 . ASP   B 2 132 ? -24.883 -10.286 -23.722 1.00 56.84  ? 141 ASP   B OD1 1 
ATOM   1277 O OD2 . ASP   B 2 132 ? -24.394 -11.915 -22.328 1.00 58.58  ? 141 ASP   B OD2 1 
ATOM   1278 N N   . LYS   B 2 133 ? -23.116 -10.813 -26.640 1.00 52.94  ? 142 LYS   B N   1 
ATOM   1279 C CA  . LYS   B 2 133 ? -23.868 -10.854 -27.892 1.00 54.48  ? 142 LYS   B CA  1 
ATOM   1280 C C   . LYS   B 2 133 ? -25.373 -10.565 -27.713 1.00 55.20  ? 142 LYS   B C   1 
ATOM   1281 O O   . LYS   B 2 133 ? -26.009 -10.033 -28.630 1.00 55.33  ? 142 LYS   B O   1 
ATOM   1282 C CB  . LYS   B 2 133 ? -23.618 -12.180 -28.623 1.00 57.38  ? 142 LYS   B CB  1 
ATOM   1283 C CG  . LYS   B 2 133 ? -22.316 -12.168 -29.418 1.00 63.52  ? 142 LYS   B CG  1 
ATOM   1284 C CD  . LYS   B 2 133 ? -21.250 -13.132 -28.891 1.00 70.14  ? 142 LYS   B CD  1 
ATOM   1285 C CE  . LYS   B 2 133 ? -20.216 -13.406 -29.969 1.00 75.12  ? 142 LYS   B CE  1 
ATOM   1286 N NZ  . LYS   B 2 133 ? -19.279 -14.509 -29.606 1.00 78.30  ? 142 LYS   B NZ  1 
ATOM   1287 N N   . CYS   B 2 134 ? -25.923 -10.844 -26.520 1.00 55.26  ? 143 CYS   B N   1 
ATOM   1288 C CA  . CYS   B 2 134 ? -27.324 -10.525 -26.235 1.00 56.01  ? 143 CYS   B CA  1 
ATOM   1289 C C   . CYS   B 2 134 ? -27.547 -9.049  -25.798 1.00 55.42  ? 143 CYS   B C   1 
ATOM   1290 O O   . CYS   B 2 134 ? -28.693 -8.628  -25.634 1.00 55.74  ? 143 CYS   B O   1 
ATOM   1291 C CB  . CYS   B 2 134 ? -27.896 -11.493 -25.206 1.00 58.23  ? 143 CYS   B CB  1 
ATOM   1292 S SG  . CYS   B 2 134 ? -27.829 -13.230 -25.709 1.00 66.36  ? 143 CYS   B SG  1 
ATOM   1293 N N   . GLY   B 2 135 ? -26.468 -8.289  -25.622 1.00 54.12  ? 144 GLY   B N   1 
ATOM   1294 C CA  . GLY   B 2 135 ? -26.528 -6.908  -25.167 1.00 53.65  ? 144 GLY   B CA  1 
ATOM   1295 C C   . GLY   B 2 135 ? -26.550 -6.771  -23.653 1.00 52.75  ? 144 GLY   B C   1 
ATOM   1296 O O   . GLY   B 2 135 ? -26.773 -5.670  -23.133 1.00 52.74  ? 144 GLY   B O   1 
ATOM   1297 N N   . ARG   B 2 136 ? -26.313 -7.895  -22.932 1.00 51.73  ? 145 ARG   B N   1 
ATOM   1298 C CA  . ARG   B 2 136 ? -26.299 -7.953  -21.474 1.00 51.20  ? 145 ARG   B CA  1 
ATOM   1299 C C   . ARG   B 2 136 ? -25.007 -7.407  -20.926 1.00 49.89  ? 145 ARG   B C   1 
ATOM   1300 O O   . ARG   B 2 136 ? -23.935 -7.673  -21.473 1.00 50.10  ? 145 ARG   B O   1 
ATOM   1301 C CB  . ARG   B 2 136 ? -26.551 -9.381  -20.974 1.00 52.88  ? 145 ARG   B CB  1 
ATOM   1302 C CG  . ARG   B 2 136 ? -28.021 -9.759  -21.033 1.00 56.67  ? 145 ARG   B CG  1 
ATOM   1303 C CD  . ARG   B 2 136 ? -28.230 -11.198 -20.659 1.00 60.53  ? 145 ARG   B CD  1 
ATOM   1304 N NE  . ARG   B 2 136 ? -27.771 -12.088 -21.721 1.00 64.34  ? 145 ARG   B NE  1 
ATOM   1305 C CZ  . ARG   B 2 136 ? -27.264 -13.300 -21.520 1.00 67.80  ? 145 ARG   B CZ  1 
ATOM   1306 N NH1 . ARG   B 2 136 ? -27.112 -13.769 -20.284 1.00 67.82  ? 145 ARG   B NH1 1 
ATOM   1307 N NH2 . ARG   B 2 136 ? -26.877 -14.042 -22.550 1.00 68.36  ? 145 ARG   B NH2 1 
ATOM   1308 N N   . VAL   B 2 137 ? -25.109 -6.607  -19.867 1.00 48.49  ? 146 VAL   B N   1 
ATOM   1309 C CA  . VAL   B 2 137 ? -23.936 -6.001  -19.269 1.00 47.60  ? 146 VAL   B CA  1 
ATOM   1310 C C   . VAL   B 2 137 ? -23.170 -7.024  -18.455 1.00 46.47  ? 146 VAL   B C   1 
ATOM   1311 O O   . VAL   B 2 137 ? -23.651 -7.505  -17.429 1.00 46.70  ? 146 VAL   B O   1 
ATOM   1312 C CB  . VAL   B 2 137 ? -24.283 -4.749  -18.457 1.00 48.39  ? 146 VAL   B CB  1 
ATOM   1313 C CG1 . VAL   B 2 137 ? -23.015 -4.087  -17.935 1.00 49.13  ? 146 VAL   B CG1 1 
ATOM   1314 C CG2 . VAL   B 2 137 ? -25.114 -3.775  -19.293 1.00 48.54  ? 146 VAL   B CG2 1 
ATOM   1315 N N   . ILE   B 2 138 ? -22.004 -7.406  -18.959 1.00 44.88  ? 147 ILE   B N   1 
ATOM   1316 C CA  . ILE   B 2 138 ? -21.163 -8.377  -18.287 1.00 43.62  ? 147 ILE   B CA  1 
ATOM   1317 C C   . ILE   B 2 138 ? -20.065 -7.729  -17.414 1.00 42.52  ? 147 ILE   B C   1 
ATOM   1318 O O   . ILE   B 2 138 ? -19.248 -8.446  -16.840 1.00 42.46  ? 147 ILE   B O   1 
ATOM   1319 C CB  . ILE   B 2 138 ? -20.586 -9.392  -19.309 1.00 43.62  ? 147 ILE   B CB  1 
ATOM   1320 C CG1 . ILE   B 2 138 ? -19.771 -8.686  -20.404 1.00 44.03  ? 147 ILE   B CG1 1 
ATOM   1321 C CG2 . ILE   B 2 138 ? -21.698 -10.232 -19.915 1.00 43.91  ? 147 ILE   B CG2 1 
ATOM   1322 C CD1 . ILE   B 2 138 ? -18.733 -9.543  -20.986 1.00 44.57  ? 147 ILE   B CD1 1 
ATOM   1323 N N   . GLY   B 2 139 ? -20.067 -6.403  -17.294 1.00 41.22  ? 148 GLY   B N   1 
ATOM   1324 C CA  . GLY   B 2 139 ? -19.082 -5.710  -16.479 1.00 40.58  ? 148 GLY   B CA  1 
ATOM   1325 C C   . GLY   B 2 139 ? -18.857 -4.275  -16.891 1.00 39.96  ? 148 GLY   B C   1 
ATOM   1326 O O   . GLY   B 2 139 ? -19.352 -3.837  -17.931 1.00 40.15  ? 148 GLY   B O   1 
ATOM   1327 N N   . LEU   B 2 140 ? -18.106 -3.530  -16.079 1.00 39.32  ? 149 LEU   B N   1 
ATOM   1328 C CA  . LEU   B 2 140 ? -17.789 -2.138  -16.372 1.00 39.33  ? 149 LEU   B CA  1 
ATOM   1329 C C   . LEU   B 2 140 ? -16.303 -1.963  -16.650 1.00 40.12  ? 149 LEU   B C   1 
ATOM   1330 O O   . LEU   B 2 140 ? -15.456 -2.674  -16.094 1.00 40.62  ? 149 LEU   B O   1 
ATOM   1331 C CB  . LEU   B 2 140 ? -18.240 -1.180  -15.253 1.00 38.87  ? 149 LEU   B CB  1 
ATOM   1332 C CG  . LEU   B 2 140 ? -19.705 -1.224  -14.833 1.00 39.44  ? 149 LEU   B CG  1 
ATOM   1333 C CD1 . LEU   B 2 140 ? -20.008 -0.145  -13.803 1.00 39.78  ? 149 LEU   B CD1 1 
ATOM   1334 C CD2 . LEU   B 2 140 ? -20.661 -1.130  -16.034 1.00 39.19  ? 149 LEU   B CD2 1 
ATOM   1335 N N   . TYR   B 2 141 ? -16.006 -1.004  -17.516 1.00 40.03  ? 150 TYR   B N   1 
ATOM   1336 C CA  . TYR   B 2 141 ? -14.677 -0.665  -17.991 1.00 40.71  ? 150 TYR   B CA  1 
ATOM   1337 C C   . TYR   B 2 141 ? -14.133 0.544   -17.217 1.00 40.86  ? 150 TYR   B C   1 
ATOM   1338 O O   . TYR   B 2 141 ? -14.890 1.461   -16.967 1.00 41.07  ? 150 TYR   B O   1 
ATOM   1339 C CB  . TYR   B 2 141 ? -14.826 -0.373  -19.501 1.00 41.32  ? 150 TYR   B CB  1 
ATOM   1340 C CG  . TYR   B 2 141 ? -13.678 0.332   -20.183 1.00 43.00  ? 150 TYR   B CG  1 
ATOM   1341 C CD1 . TYR   B 2 141 ? -13.782 1.663   -20.560 1.00 44.44  ? 150 TYR   B CD1 1 
ATOM   1342 C CD2 . TYR   B 2 141 ? -12.528 -0.357  -20.544 1.00 44.49  ? 150 TYR   B CD2 1 
ATOM   1343 C CE1 . TYR   B 2 141 ? -12.761 2.299   -21.258 1.00 46.11  ? 150 TYR   B CE1 1 
ATOM   1344 C CE2 . TYR   B 2 141 ? -11.492 0.270   -21.228 1.00 45.88  ? 150 TYR   B CE2 1 
ATOM   1345 C CZ  . TYR   B 2 141 ? -11.616 1.597   -21.596 1.00 47.42  ? 150 TYR   B CZ  1 
ATOM   1346 O OH  . TYR   B 2 141 ? -10.582 2.234   -22.252 1.00 49.52  ? 150 TYR   B OH  1 
ATOM   1347 N N   . GLY   B 2 142 ? -12.863 0.532   -16.808 1.00 41.00  ? 151 GLY   B N   1 
ATOM   1348 C CA  . GLY   B 2 142 ? -12.288 1.661   -16.074 1.00 42.04  ? 151 GLY   B CA  1 
ATOM   1349 C C   . GLY   B 2 142 ? -11.340 1.366   -14.916 1.00 42.93  ? 151 GLY   B C   1 
ATOM   1350 O O   . GLY   B 2 142 ? -10.800 2.305   -14.314 1.00 42.91  ? 151 GLY   B O   1 
ATOM   1351 N N   . ASN   B 2 143 ? -11.140 0.083   -14.562 1.00 43.22  ? 152 ASN   B N   1 
ATOM   1352 C CA  . ASN   B 2 143 ? -10.206 -0.258  -13.481 1.00 44.53  ? 152 ASN   B CA  1 
ATOM   1353 C C   . ASN   B 2 143 ? -9.289  -1.380  -13.902 1.00 45.57  ? 152 ASN   B C   1 
ATOM   1354 O O   . ASN   B 2 143 ? -9.727  -2.518  -14.052 1.00 45.62  ? 152 ASN   B O   1 
ATOM   1355 C CB  . ASN   B 2 143 ? -10.911 -0.608  -12.165 1.00 45.45  ? 152 ASN   B CB  1 
ATOM   1356 C CG  . ASN   B 2 143 ? -9.954  -0.775  -10.996 1.00 48.28  ? 152 ASN   B CG  1 
ATOM   1357 O OD1 . ASN   B 2 143 ? -8.842  -0.235  -10.987 1.00 48.83  ? 152 ASN   B OD1 1 
ATOM   1358 N ND2 . ASN   B 2 143 ? -10.369 -1.514  -9.961  1.00 49.21  ? 152 ASN   B ND2 1 
ATOM   1359 N N   . GLY   B 2 144 ? -8.023  -1.056  -14.073 1.00 46.27  ? 153 GLY   B N   1 
ATOM   1360 C CA  . GLY   B 2 144 ? -7.047  -2.048  -14.481 1.00 47.92  ? 153 GLY   B CA  1 
ATOM   1361 C C   . GLY   B 2 144 ? -5.615  -1.650  -14.227 1.00 49.53  ? 153 GLY   B C   1 
ATOM   1362 O O   . GLY   B 2 144 ? -5.277  -1.169  -13.142 1.00 49.63  ? 153 GLY   B O   1 
ATOM   1363 N N   . VAL   B 2 145 ? -4.764  -1.834  -15.239 1.00 50.48  ? 154 VAL   B N   1 
ATOM   1364 C CA  . VAL   B 2 145 ? -3.337  -1.607  -15.079 1.00 52.12  ? 154 VAL   B CA  1 
ATOM   1365 C C   . VAL   B 2 145 ? -2.648  -0.912  -16.283 1.00 53.56  ? 154 VAL   B C   1 
ATOM   1366 O O   . VAL   B 2 145 ? -3.207  -0.818  -17.375 1.00 53.27  ? 154 VAL   B O   1 
ATOM   1367 C CB  . VAL   B 2 145 ? -2.692  -2.978  -14.756 1.00 52.71  ? 154 VAL   B CB  1 
ATOM   1368 C CG1 . VAL   B 2 145 ? -2.487  -3.810  -16.017 1.00 52.64  ? 154 VAL   B CG1 1 
ATOM   1369 C CG2 . VAL   B 2 145 ? -1.394  -2.812  -13.986 1.00 53.92  ? 154 VAL   B CG2 1 
ATOM   1370 N N   . VAL   B 2 146 ? -1.443  -0.386  -16.044 1.00 54.73  ? 155 VAL   B N   1 
ATOM   1371 C CA  . VAL   B 2 146 ? -0.603  0.241   -17.057 1.00 56.30  ? 155 VAL   B CA  1 
ATOM   1372 C C   . VAL   B 2 146 ? 0.455   -0.800  -17.439 1.00 57.93  ? 155 VAL   B C   1 
ATOM   1373 O O   . VAL   B 2 146 ? 1.063   -1.402  -16.553 1.00 58.00  ? 155 VAL   B O   1 
ATOM   1374 C CB  . VAL   B 2 146 ? 0.021   1.548   -16.518 1.00 57.01  ? 155 VAL   B CB  1 
ATOM   1375 C CG1 . VAL   B 2 146 ? 1.196   1.998   -17.367 1.00 57.66  ? 155 VAL   B CG1 1 
ATOM   1376 C CG2 . VAL   B 2 146 ? -1.025  2.649   -16.427 1.00 57.61  ? 155 VAL   B CG2 1 
ATOM   1377 N N   . ILE   B 2 147 ? 0.622   -1.069  -18.738 1.00 59.38  ? 156 ILE   B N   1 
ATOM   1378 C CA  . ILE   B 2 147 ? 1.582   -2.073  -19.193 1.00 61.55  ? 156 ILE   B CA  1 
ATOM   1379 C C   . ILE   B 2 147 ? 2.922   -1.432  -19.661 1.00 64.14  ? 156 ILE   B C   1 
ATOM   1380 O O   . ILE   B 2 147 ? 3.051   -0.211  -19.592 1.00 64.54  ? 156 ILE   B O   1 
ATOM   1381 C CB  . ILE   B 2 147 ? 0.908   -2.993  -20.247 1.00 61.85  ? 156 ILE   B CB  1 
ATOM   1382 C CG1 . ILE   B 2 147 ? 0.537   -2.225  -21.531 1.00 62.97  ? 156 ILE   B CG1 1 
ATOM   1383 C CG2 . ILE   B 2 147 ? -0.314  -3.681  -19.628 1.00 62.24  ? 156 ILE   B CG2 1 
ATOM   1384 C CD1 . ILE   B 2 147 ? -0.103  -3.091  -22.635 1.00 63.81  ? 156 ILE   B CD1 1 
ATOM   1385 N N   . LYS   B 2 148 ? 3.935   -2.249  -20.063 1.00 65.72  ? 157 LYS   B N   1 
ATOM   1386 C CA  . LYS   B 2 148 ? 5.262   -1.786  -20.523 1.00 67.68  ? 157 LYS   B CA  1 
ATOM   1387 C C   . LYS   B 2 148 ? 5.274   -0.582  -21.492 1.00 68.66  ? 157 LYS   B C   1 
ATOM   1388 O O   . LYS   B 2 148 ? 6.183   0.247   -21.411 1.00 69.04  ? 157 LYS   B O   1 
ATOM   1389 C CB  . LYS   B 2 148 ? 6.056   -2.936  -21.168 1.00 70.79  ? 157 LYS   B CB  1 
ATOM   1390 C CG  . LYS   B 2 148 ? 6.333   -4.108  -20.235 1.00 76.78  ? 157 LYS   B CG  1 
ATOM   1391 C CD  . LYS   B 2 148 ? 7.184   -5.188  -20.925 1.00 82.50  ? 157 LYS   B CD  1 
ATOM   1392 C CE  . LYS   B 2 148 ? 8.629   -4.778  -21.144 1.00 86.92  ? 157 LYS   B CE  1 
ATOM   1393 N NZ  . LYS   B 2 148 ? 9.479   -5.002  -19.936 1.00 88.84  ? 157 LYS   B NZ  1 
ATOM   1394 N N   . ASN   B 2 149 ? 4.312   -0.502  -22.427 1.00 68.69  ? 158 ASN   B N   1 
ATOM   1395 C CA  . ASN   B 2 149 ? 4.290   0.612   -23.381 1.00 69.43  ? 158 ASN   B CA  1 
ATOM   1396 C C   . ASN   B 2 149 ? 3.507   1.854   -22.898 1.00 68.80  ? 158 ASN   B C   1 
ATOM   1397 O O   . ASN   B 2 149 ? 3.266   2.770   -23.691 1.00 69.04  ? 158 ASN   B O   1 
ATOM   1398 C CB  . ASN   B 2 149 ? 3.801   0.168   -24.769 1.00 71.98  ? 158 ASN   B CB  1 
ATOM   1399 C CG  . ASN   B 2 149 ? 2.600   -0.751  -24.765 1.00 76.72  ? 158 ASN   B CG  1 
ATOM   1400 O OD1 . ASN   B 2 149 ? 2.636   -1.865  -24.221 1.00 78.60  ? 158 ASN   B OD1 1 
ATOM   1401 N ND2 . ASN   B 2 149 ? 1.523   -0.314  -25.403 1.00 77.35  ? 158 ASN   B ND2 1 
ATOM   1402 N N   . GLY   B 2 150 ? 3.134   1.881   -21.617 1.00 67.52  ? 159 GLY   B N   1 
ATOM   1403 C CA  . GLY   B 2 150 ? 2.402   2.997   -21.029 1.00 66.70  ? 159 GLY   B CA  1 
ATOM   1404 C C   . GLY   B 2 150 ? 0.899   2.945   -21.221 1.00 65.72  ? 159 GLY   B C   1 
ATOM   1405 O O   . GLY   B 2 150 ? 0.167   3.724   -20.600 1.00 65.87  ? 159 GLY   B O   1 
ATOM   1406 N N   . SER   B 2 151 ? 0.421   2.022   -22.085 1.00 64.29  ? 160 SER   B N   1 
ATOM   1407 C CA  A SER   B 2 151 ? -0.997  1.807   -22.385 0.50 63.85  ? 160 SER   B CA  1 
ATOM   1408 C CA  B SER   B 2 151 ? -1.010  1.920   -22.339 0.50 63.84  ? 160 SER   B CA  1 
ATOM   1409 C C   . SER   B 2 151 ? -1.775  1.289   -21.161 1.00 62.83  ? 160 SER   B C   1 
ATOM   1410 O O   . SER   B 2 151 ? -1.173  0.744   -20.231 1.00 62.40  ? 160 SER   B O   1 
ATOM   1411 C CB  A SER   B 2 151 ? -1.130  0.816   -23.540 0.50 65.34  ? 160 SER   B CB  1 
ATOM   1412 C CB  B SER   B 2 151 ? -1.287  1.213   -23.664 0.50 65.22  ? 160 SER   B CB  1 
ATOM   1413 O OG  A SER   B 2 151 ? -2.470  0.426   -23.793 0.50 67.84  ? 160 SER   B OG  1 
ATOM   1414 O OG  B SER   B 2 151 ? -1.059  -0.180  -23.578 0.50 67.41  ? 160 SER   B OG  1 
ATOM   1415 N N   . TYR   B 2 152 ? -3.108  1.435   -21.169 1.00 60.93  ? 161 TYR   B N   1 
ATOM   1416 C CA  . TYR   B 2 152 ? -3.961  0.948   -20.089 1.00 59.17  ? 161 TYR   B CA  1 
ATOM   1417 C C   . TYR   B 2 152 ? -4.773  -0.276  -20.545 1.00 57.55  ? 161 TYR   B C   1 
ATOM   1418 O O   . TYR   B 2 152 ? -5.327  -0.301  -21.655 1.00 57.86  ? 161 TYR   B O   1 
ATOM   1419 C CB  . TYR   B 2 152 ? -4.896  2.079   -19.610 1.00 58.54  ? 161 TYR   B CB  1 
ATOM   1420 C CG  . TYR   B 2 152 ? -5.356  1.974   -18.172 1.00 58.55  ? 161 TYR   B CG  1 
ATOM   1421 C CD1 . TYR   B 2 152 ? -4.595  2.499   -17.140 1.00 59.32  ? 161 TYR   B CD1 1 
ATOM   1422 C CD2 . TYR   B 2 152 ? -6.592  1.431   -17.854 1.00 58.78  ? 161 TYR   B CD2 1 
ATOM   1423 C CE1 . TYR   B 2 152 ? -5.028  2.439   -15.818 1.00 59.70  ? 161 TYR   B CE1 1 
ATOM   1424 C CE2 . TYR   B 2 152 ? -7.031  1.356   -16.536 1.00 59.14  ? 161 TYR   B CE2 1 
ATOM   1425 C CZ  . TYR   B 2 152 ? -6.251  1.874   -15.521 1.00 59.94  ? 161 TYR   B CZ  1 
ATOM   1426 O OH  . TYR   B 2 152 ? -6.674  1.818   -14.214 1.00 61.12  ? 161 TYR   B OH  1 
ATOM   1427 N N   . VAL   B 2 153 ? -4.798  -1.305  -19.694 1.00 55.34  ? 162 VAL   B N   1 
ATOM   1428 C CA  . VAL   B 2 153 ? -5.563  -2.524  -19.910 1.00 53.63  ? 162 VAL   B CA  1 
ATOM   1429 C C   . VAL   B 2 153 ? -6.530  -2.605  -18.742 1.00 51.60  ? 162 VAL   B C   1 
ATOM   1430 O O   . VAL   B 2 153 ? -6.106  -2.684  -17.593 1.00 51.20  ? 162 VAL   B O   1 
ATOM   1431 C CB  . VAL   B 2 153 ? -4.668  -3.781  -20.032 1.00 54.03  ? 162 VAL   B CB  1 
ATOM   1432 C CG1 . VAL   B 2 153 ? -5.490  -5.063  -19.879 1.00 54.20  ? 162 VAL   B CG1 1 
ATOM   1433 C CG2 . VAL   B 2 153 ? -3.915  -3.776  -21.361 1.00 54.49  ? 162 VAL   B CG2 1 
ATOM   1434 N N   . SER   B 2 154 ? -7.821  -2.502  -19.025 1.00 50.12  ? 163 SER   B N   1 
ATOM   1435 C CA  . SER   B 2 154 ? -8.828  -2.504  -17.974 1.00 49.03  ? 163 SER   B CA  1 
ATOM   1436 C C   . SER   B 2 154 ? -9.418  -3.888  -17.751 1.00 48.23  ? 163 SER   B C   1 
ATOM   1437 O O   . SER   B 2 154 ? -9.611  -4.626  -18.703 1.00 48.79  ? 163 SER   B O   1 
ATOM   1438 C CB  . SER   B 2 154 ? -9.923  -1.491  -18.304 1.00 48.91  ? 163 SER   B CB  1 
ATOM   1439 O OG  . SER   B 2 154 ? -11.180 -1.803  -17.727 1.00 50.12  ? 163 SER   B OG  1 
ATOM   1440 N N   . ALA   B 2 155 ? -9.781  -4.198  -16.517 1.00 46.73  ? 164 ALA   B N   1 
ATOM   1441 C CA  . ALA   B 2 155 ? -10.463 -5.445  -16.201 1.00 46.07  ? 164 ALA   B CA  1 
ATOM   1442 C C   . ALA   B 2 155 ? -11.969 -5.335  -16.587 1.00 45.23  ? 164 ALA   B C   1 
ATOM   1443 O O   . ALA   B 2 155 ? -12.490 -4.239  -16.812 1.00 45.10  ? 164 ALA   B O   1 
ATOM   1444 C CB  . ALA   B 2 155 ? -10.339 -5.717  -14.700 1.00 46.22  ? 164 ALA   B CB  1 
ATOM   1445 N N   . ILE   B 2 156 ? -12.664 -6.473  -16.655 1.00 44.53  ? 165 ILE   B N   1 
ATOM   1446 C CA  . ILE   B 2 156 ? -14.098 -6.497  -16.853 1.00 44.35  ? 165 ILE   B CA  1 
ATOM   1447 C C   . ILE   B 2 156 ? -14.631 -6.661  -15.432 1.00 44.30  ? 165 ILE   B C   1 
ATOM   1448 O O   . ILE   B 2 156 ? -14.511 -7.754  -14.867 1.00 44.33  ? 165 ILE   B O   1 
ATOM   1449 C CB  . ILE   B 2 156 ? -14.518 -7.678  -17.754 1.00 44.80  ? 165 ILE   B CB  1 
ATOM   1450 C CG1 . ILE   B 2 156 ? -13.929 -7.513  -19.182 1.00 45.99  ? 165 ILE   B CG1 1 
ATOM   1451 C CG2 . ILE   B 2 156 ? -16.050 -7.809  -17.778 1.00 44.86  ? 165 ILE   B CG2 1 
ATOM   1452 C CD1 . ILE   B 2 156 ? -14.237 -8.633  -20.139 1.00 46.93  ? 165 ILE   B CD1 1 
ATOM   1453 N N   . THR   B 2 157 ? -15.132 -5.563  -14.818 1.00 43.81  ? 166 THR   B N   1 
ATOM   1454 C CA  . THR   B 2 157 ? -15.605 -5.607  -13.427 1.00 43.36  ? 166 THR   B CA  1 
ATOM   1455 C C   . THR   B 2 157 ? -17.110 -5.784  -13.275 1.00 43.15  ? 166 THR   B C   1 
ATOM   1456 O O   . THR   B 2 157 ? -17.862 -4.887  -13.627 1.00 42.61  ? 166 THR   B O   1 
ATOM   1457 C CB  . THR   B 2 157 ? -15.214 -4.348  -12.662 1.00 43.97  ? 166 THR   B CB  1 
ATOM   1458 O OG1 . THR   B 2 157 ? -13.862 -3.992  -12.932 1.00 44.92  ? 166 THR   B OG1 1 
ATOM   1459 C CG2 . THR   B 2 157 ? -15.419 -4.513  -11.187 1.00 44.19  ? 166 THR   B CG2 1 
ATOM   1460 N N   . GLN   B 2 158 ? -17.541 -6.896  -12.673 1.00 43.35  ? 167 GLN   B N   1 
ATOM   1461 C CA  . GLN   B 2 158 ? -18.952 -7.160  -12.427 1.00 43.91  ? 167 GLN   B CA  1 
ATOM   1462 C C   . GLN   B 2 158 ? -19.247 -7.216  -10.914 1.00 45.95  ? 167 GLN   B C   1 
ATOM   1463 O O   . GLN   B 2 158 ? -18.378 -7.542  -10.107 1.00 45.88  ? 167 GLN   B O   1 
ATOM   1464 C CB  . GLN   B 2 158 ? -19.386 -8.457  -13.145 1.00 44.07  ? 167 GLN   B CB  1 
ATOM   1465 C CG  . GLN   B 2 158 ? -20.889 -8.787  -13.115 1.00 45.44  ? 167 GLN   B CG  1 
ATOM   1466 C CD  . GLN   B 2 158 ? -21.793 -7.712  -13.698 1.00 46.67  ? 167 GLN   B CD  1 
ATOM   1467 O OE1 . GLN   B 2 158 ? -21.871 -6.586  -13.190 1.00 47.01  ? 167 GLN   B OE1 1 
ATOM   1468 N NE2 . GLN   B 2 158 ? -22.537 -8.049  -14.734 1.00 45.65  ? 167 GLN   B NE2 1 
ATOM   1469 N N   . GLY   B 2 159 ? -20.458 -6.835  -10.544 1.00 47.43  ? 168 GLY   B N   1 
ATOM   1470 C CA  . GLY   B 2 159 ? -20.907 -6.866  -9.168  1.00 49.25  ? 168 GLY   B CA  1 
ATOM   1471 C C   . GLY   B 2 159 ? -21.668 -8.132  -8.842  1.00 51.87  ? 168 GLY   B C   1 
ATOM   1472 O O   . GLY   B 2 159 ? -21.873 -8.996  -9.699  1.00 51.68  ? 168 GLY   B O   1 
ATOM   1473 N N   . LYS   B 2 160 ? -22.086 -8.257  -7.580  1.00 54.13  ? 169 LYS   B N   1 
ATOM   1474 C CA  . LYS   B 2 160 ? -22.837 -9.423  -7.144  1.00 56.36  ? 169 LYS   B CA  1 
ATOM   1475 C C   . LYS   B 2 160 ? -24.317 -9.067  -7.010  1.00 58.07  ? 169 LYS   B C   1 
ATOM   1476 O O   . LYS   B 2 160 ? -24.652 -7.994  -6.515  1.00 58.38  ? 169 LYS   B O   1 
ATOM   1477 C CB  . LYS   B 2 160 ? -22.264 -9.983  -5.832  1.00 58.68  ? 169 LYS   B CB  1 
ATOM   1478 C CG  . LYS   B 2 160 ? -22.475 -11.482 -5.681  1.00 63.52  ? 169 LYS   B CG  1 
ATOM   1479 C CD  . LYS   B 2 160 ? -23.393 -11.802 -4.506  1.00 68.49  ? 169 LYS   B CD  1 
ATOM   1480 C CE  . LYS   B 2 160 ? -23.702 -13.276 -4.400  1.00 72.23  ? 169 LYS   B CE  1 
ATOM   1481 N NZ  . LYS   B 2 160 ? -24.504 -13.578 -3.183  1.00 74.75  ? 169 LYS   B NZ  1 
ATOM   1482 N N   . ARG   B 2 161 ? -25.195 -9.940  -7.513  1.00 59.07  ? 170 ARG   B N   1 
ATOM   1483 C CA  . ARG   B 2 161 ? -26.641 -9.766  -7.424  1.00 60.21  ? 170 ARG   B CA  1 
ATOM   1484 C C   . ARG   B 2 161 ? -27.134 -10.697 -6.307  1.00 61.74  ? 170 ARG   B C   1 
ATOM   1485 O O   . ARG   B 2 161 ? -26.771 -11.875 -6.290  1.00 62.16  ? 170 ARG   B O   1 
ATOM   1486 C CB  . ARG   B 2 161 ? -27.316 -10.088 -8.778  1.00 60.67  ? 170 ARG   B CB  1 
ATOM   1487 C CG  . ARG   B 2 161 ? -28.838 -10.191 -8.715  1.00 62.18  ? 170 ARG   B CG  1 
ATOM   1488 C CD  . ARG   B 2 161 ? -29.549 -9.832  -10.010 1.00 64.14  ? 170 ARG   B CD  1 
ATOM   1489 N NE  . ARG   B 2 161 ? -30.887 -9.298  -9.734  1.00 66.56  ? 170 ARG   B NE  1 
ATOM   1490 C CZ  . ARG   B 2 161 ? -31.664 -8.699  -10.631 1.00 68.21  ? 170 ARG   B CZ  1 
ATOM   1491 N NH1 . ARG   B 2 161 ? -31.253 -8.557  -11.885 1.00 68.18  ? 170 ARG   B NH1 1 
ATOM   1492 N NH2 . ARG   B 2 161 ? -32.845 -8.213  -10.275 1.00 67.54  ? 170 ARG   B NH2 1 
ATOM   1493 N N   . GLU   B 2 162 ? -27.909 -10.170 -5.355  1.00 62.60  ? 171 GLU   B N   1 
ATOM   1494 C CA  . GLU   B 2 162 ? -28.403 -10.976 -4.237  1.00 64.10  ? 171 GLU   B CA  1 
ATOM   1495 C C   . GLU   B 2 162 ? -29.898 -11.282 -4.343  1.00 64.78  ? 171 GLU   B C   1 
ATOM   1496 O O   . GLU   B 2 162 ? -30.304 -12.441 -4.240  1.00 65.13  ? 171 GLU   B O   1 
ATOM   1497 C CB  . GLU   B 2 162 ? -28.085 -10.295 -2.899  1.00 67.27  ? 171 GLU   B CB  1 
ATOM   1498 C CG  . GLU   B 2 162 ? -26.595 -10.164 -2.622  1.00 74.39  ? 171 GLU   B CG  1 
ATOM   1499 C CD  . GLU   B 2 162 ? -25.997 -11.274 -1.776  1.00 83.55  ? 171 GLU   B CD  1 
ATOM   1500 O OE1 . GLU   B 2 162 ? -24.972 -11.017 -1.102  1.00 85.74  ? 171 GLU   B OE1 1 
ATOM   1501 O OE2 . GLU   B 2 162 ? -26.555 -12.397 -1.775  1.00 85.88  ? 171 GLU   B OE2 1 
HETATM 1502 S S   . DMS   C 3 .   ? -18.494 12.027  -0.425  1.00 75.73  ? 201 DMS   B S   1 
HETATM 1503 O O   . DMS   C 3 .   ? -19.342 10.789  -0.354  1.00 75.64  ? 201 DMS   B O   1 
HETATM 1504 C C1  . DMS   C 3 .   ? -19.572 13.422  -0.841  1.00 75.80  ? 201 DMS   B C1  1 
HETATM 1505 C C2  . DMS   C 3 .   ? -17.592 12.031  -1.999  1.00 75.53  ? 201 DMS   B C2  1 
HETATM 1506 N N1  . A1B9A D 4 .   ? -5.770  5.860   -17.981 1.00 47.12  ? 202 A1B9A B N1  1 
HETATM 1507 N N3  . A1B9A D 4 .   ? -8.695  4.533   -13.003 1.00 44.58  ? 202 A1B9A B N3  1 
HETATM 1508 C C4  . A1B9A D 4 .   ? -7.849  5.135   -15.194 1.00 45.97  ? 202 A1B9A B C4  1 
HETATM 1509 C C5  . A1B9A D 4 .   ? -7.838  5.308   -13.708 1.00 45.50  ? 202 A1B9A B C5  1 
HETATM 1510 C C6  . A1B9A D 4 .   ? -8.850  4.480   -11.596 1.00 43.43  ? 202 A1B9A B C6  1 
HETATM 1511 C C7  . A1B9A D 4 .   ? -8.552  5.592   -10.811 1.00 43.13  ? 202 A1B9A B C7  1 
HETATM 1512 C C8  . A1B9A D 4 .   ? -8.687  5.533   -9.432  1.00 42.78  ? 202 A1B9A B C8  1 
HETATM 1513 C C10 . A1B9A D 4 .   ? -9.315  3.209   -9.621  1.00 42.64  ? 202 A1B9A B C10 1 
HETATM 1514 C C13 . A1B9A D 4 .   ? -9.266  3.994   -7.396  1.00 42.47  ? 202 A1B9A B C13 1 
HETATM 1515 C C15 . A1B9A D 4 .   ? -9.022  4.564   -17.246 1.00 45.80  ? 202 A1B9A B C15 1 
HETATM 1516 C C17 . A1B9A D 4 .   ? -10.475 4.348   -19.374 1.00 44.88  ? 202 A1B9A B C17 1 
HETATM 1517 C C1  . A1B9A D 4 .   ? -5.414  5.901   -19.390 1.00 47.29  ? 202 A1B9A B C1  1 
HETATM 1518 N N2  . A1B9A D 4 .   ? -4.889  6.276   -17.025 1.00 47.46  ? 202 A1B9A B N2  1 
HETATM 1519 C C2  . A1B9A D 4 .   ? -5.461  6.077   -15.855 1.00 47.16  ? 202 A1B9A B C2  1 
HETATM 1520 C C3  . A1B9A D 4 .   ? -6.767  5.555   -16.026 1.00 46.69  ? 202 A1B9A B C3  1 
HETATM 1521 O O1  . A1B9A D 4 .   ? -7.043  6.089   -13.190 1.00 45.97  ? 202 A1B9A B O1  1 
HETATM 1522 C C9  . A1B9A D 4 .   ? -9.035  4.325   -8.843  1.00 42.57  ? 202 A1B9A B C9  1 
HETATM 1523 C C11 . A1B9A D 4 .   ? -9.195  3.258   -11.004 1.00 42.96  ? 202 A1B9A B C11 1 
HETATM 1524 C C12 . A1B9A D 4 .   ? -9.705  2.066   -8.730  1.00 42.26  ? 202 A1B9A B C12 1 
HETATM 1525 N N4  . A1B9A D 4 .   ? -9.202  2.526   -7.428  1.00 42.37  ? 202 A1B9A B N4  1 
HETATM 1526 C C14 . A1B9A D 4 .   ? -8.986  4.668   -15.836 1.00 45.77  ? 202 A1B9A B C14 1 
HETATM 1527 C C16 . A1B9A D 4 .   ? -10.214 4.020   -17.940 1.00 45.24  ? 202 A1B9A B C16 1 
HETATM 1528 C C18 . A1B9A D 4 .   ? -10.039 2.994   -19.008 1.00 44.82  ? 202 A1B9A B C18 1 
HETATM 1529 N N5  . A1B9A D 4 .   ? -7.998  4.921   -18.016 1.00 46.04  ? 202 A1B9A B N5  1 
HETATM 1530 C C19 . A1B9A D 4 .   ? -6.913  5.424   -17.416 1.00 46.52  ? 202 A1B9A B C19 1 
HETATM 1531 O O   . HOH   E 5 .   ? -4.050  -13.931 -25.510 1.00 34.75  ? 101 HOH   A O   1 
HETATM 1532 O O   . HOH   E 5 .   ? -23.483 18.951  -19.379 1.00 23.55  ? 102 HOH   A O   1 
HETATM 1533 O O   . HOH   E 5 .   ? -2.191  -4.008  -6.031  1.00 38.67  ? 103 HOH   A O   1 
HETATM 1534 O O   . HOH   E 5 .   ? -5.392  1.866   -10.019 1.00 36.51  ? 104 HOH   A O   1 
HETATM 1535 O O   . HOH   E 5 .   ? -28.378 -6.304  -28.160 1.00 65.12  ? 105 HOH   A O   1 
HETATM 1536 O O   . HOH   E 5 .   ? -4.721  -10.078 -5.552  1.00 37.81  ? 106 HOH   A O   1 
HETATM 1537 O O   . HOH   E 5 .   ? -8.231  -1.552  6.750   1.00 43.13  ? 107 HOH   A O   1 
HETATM 1538 O O   . HOH   E 5 .   ? -29.143 16.246  -15.237 1.00 43.85  ? 108 HOH   A O   1 
HETATM 1539 O O   . HOH   E 5 .   ? -3.424  -3.875  0.595   1.00 54.28  ? 109 HOH   A O   1 
HETATM 1540 O O   . HOH   E 5 .   ? -25.765 13.933  -23.430 1.00 45.79  ? 110 HOH   A O   1 
HETATM 1541 O O   . HOH   E 5 .   ? -21.661 -8.741  -34.991 1.00 44.43  ? 111 HOH   A O   1 
HETATM 1542 O O   . HOH   E 5 .   ? -8.349  4.278   -3.789  1.00 44.29  ? 112 HOH   A O   1 
HETATM 1543 O O   . HOH   E 5 .   ? -2.534  -8.417  -3.360  1.00 46.68  ? 113 HOH   A O   1 
HETATM 1544 O O   . HOH   E 5 .   ? -3.725  -0.429  0.273   1.00 47.53  ? 114 HOH   A O   1 
HETATM 1545 O O   . HOH   E 5 .   ? -5.452  5.827   -8.183  1.00 57.43  ? 115 HOH   A O   1 
HETATM 1546 O O   . HOH   F 5 .   ? -6.431  -0.396  -10.919 1.00 48.34  ? 301 HOH   B O   1 
HETATM 1547 O O   . HOH   F 5 .   ? -33.749 1.729   -15.236 1.00 46.36  ? 302 HOH   B O   1 
HETATM 1548 O O   . HOH   F 5 .   ? -17.000 -14.810 -16.344 1.00 60.70  ? 303 HOH   B O   1 
HETATM 1549 O O   . HOH   F 5 .   ? -12.603 -3.380  -10.055 1.00 26.79  ? 304 HOH   B O   1 
HETATM 1550 O O   . HOH   F 5 .   ? -35.139 4.066   -8.952  1.00 44.14  ? 305 HOH   B O   1 
HETATM 1551 O O   . HOH   F 5 .   ? -12.869 -2.266  -14.627 1.00 36.51  ? 306 HOH   B O   1 
HETATM 1552 O O   . HOH   F 5 .   ? -9.205  -6.310  -25.816 1.00 45.01  ? 307 HOH   B O   1 
HETATM 1553 O O   . HOH   F 5 .   ? -15.361 -4.815  1.460   1.00 36.27  ? 308 HOH   B O   1 
HETATM 1554 O O   . HOH   F 5 .   ? -28.133 -7.103  -5.564  1.00 54.27  ? 309 HOH   B O   1 
HETATM 1555 O O   . HOH   F 5 .   ? -17.490 12.865  -5.701  1.00 41.98  ? 310 HOH   B O   1 
HETATM 1556 O O   . HOH   F 5 .   ? -21.625 7.164   -0.090  0.50 23.25  ? 311 HOH   B O   1 
HETATM 1557 O O   . HOH   F 5 .   ? -17.859 -10.708 -16.295 1.00 49.84  ? 312 HOH   B O   1 
HETATM 1558 O O   . HOH   F 5 .   ? -6.762  -9.098  -3.296  1.00 33.64  ? 313 HOH   B O   1 
HETATM 1559 O O   . HOH   F 5 .   ? -31.143 12.684  -16.728 1.00 44.42  ? 314 HOH   B O   1 
HETATM 1560 O O   . HOH   F 5 .   ? -26.294 -7.865  -16.694 1.00 37.94  ? 315 HOH   B O   1 
HETATM 1561 O O   . HOH   F 5 .   ? -21.880 5.482   -32.817 1.00 47.41  ? 316 HOH   B O   1 
HETATM 1562 O O   . HOH   F 5 .   ? -29.847 -5.188  -0.804  1.00 55.92  ? 317 HOH   B O   1 
HETATM 1563 O O   . HOH   F 5 .   ? -23.576 -14.624 -18.277 1.00 53.46  ? 318 HOH   B O   1 
HETATM 1564 O O   . HOH   F 5 .   ? 8.199   -4.613  -17.399 1.00 59.42  ? 319 HOH   B O   1 
HETATM 1565 O O   . HOH   F 5 .   ? -21.781 -12.145 -12.721 1.00 59.63  ? 320 HOH   B O   1 
HETATM 1566 O O   . HOH   F 5 .   ? -18.067 15.443  -22.065 1.00 30.44  ? 321 HOH   B O   1 
HETATM 1567 O O   . HOH   F 5 .   ? -5.403  3.424   -12.151 1.00 55.38  ? 322 HOH   B O   1 
HETATM 1568 O O   . HOH   F 5 .   ? -13.082 -12.000 -34.789 1.00 51.50  ? 323 HOH   B O   1 
HETATM 1569 O O   . HOH   F 5 .   ? -7.073  -10.572 -5.728  1.00 45.13  ? 324 HOH   B O   1 
HETATM 1570 O O   . HOH   F 5 .   ? -16.615 -14.101 -30.957 1.00 50.79  ? 325 HOH   B O   1 
HETATM 1571 O O   . HOH   F 5 .   ? -10.888 7.867   -13.776 1.00 41.57  ? 326 HOH   B O   1 
HETATM 1572 O O   . HOH   F 5 .   ? -27.894 -6.292  -18.382 1.00 42.56  ? 327 HOH   B O   1 
HETATM 1573 O O   . HOH   F 5 .   ? -18.118 26.208  -13.907 1.00 50.29  ? 328 HOH   B O   1 
HETATM 1574 O O   . HOH   F 5 .   ? -15.297 9.659   -0.567  1.00 36.25  ? 329 HOH   B O   1 
HETATM 1575 O O   . HOH   F 5 .   ? -21.283 2.443   -32.677 1.00 43.54  ? 330 HOH   B O   1 
HETATM 1576 O O   . HOH   F 5 .   ? -26.041 -4.711  -3.859  1.00 38.91  ? 331 HOH   B O   1 
HETATM 1577 O O   . HOH   F 5 .   ? -19.307 -6.000  -0.724  1.00 56.73  ? 332 HOH   B O   1 
HETATM 1578 O O   . HOH   F 5 .   ? -22.472 -13.798 -25.594 1.00 34.92  ? 333 HOH   B O   1 
HETATM 1579 O O   . HOH   F 5 .   ? -17.593 14.181  -31.162 1.00 28.10  ? 334 HOH   B O   1 
HETATM 1580 O O   . HOH   F 5 .   ? -14.407 -6.849  -1.867  1.00 54.92  ? 335 HOH   B O   1 
HETATM 1581 O O   . HOH   F 5 .   ? -31.352 0.510   -22.865 1.00 44.84  ? 336 HOH   B O   1 
HETATM 1582 O O   . HOH   F 5 .   ? -20.924 -14.163 -22.434 1.00 45.50  ? 337 HOH   B O   1 
HETATM 1583 O O   . HOH   F 5 .   ? -30.503 -8.057  -5.377  1.00 59.83  ? 338 HOH   B O   1 
HETATM 1584 O O   . HOH   F 5 .   ? -0.525  0.715   -12.948 1.00 41.37  ? 339 HOH   B O   1 
HETATM 1585 O O   . HOH   F 5 .   ? -5.271  9.671   -16.619 1.00 34.73  ? 340 HOH   B O   1 
HETATM 1586 O O   . HOH   F 5 .   ? -30.889 4.103   -2.114  1.00 35.21  ? 341 HOH   B O   1 
HETATM 1587 O O   . HOH   F 5 .   ? -1.070  -15.249 -10.546 1.00 51.39  ? 342 HOH   B O   1 
HETATM 1588 O O   . HOH   F 5 .   ? -23.933 -7.548  -2.158  1.00 49.37  ? 343 HOH   B O   1 
HETATM 1589 O O   . HOH   F 5 .   ? -32.363 6.574   -3.546  1.00 69.43  ? 344 HOH   B O   1 
HETATM 1590 O O   . HOH   F 5 .   ? -15.067 -12.931 -16.013 1.00 35.67  ? 345 HOH   B O   1 
HETATM 1591 O O   . HOH   F 5 .   ? -5.868  8.106   -23.887 1.00 45.58  ? 346 HOH   B O   1 
HETATM 1592 O O   . HOH   F 5 .   ? -10.235 -10.847 -7.870  1.00 50.20  ? 347 HOH   B O   1 
HETATM 1593 O O   . HOH   F 5 .   ? -21.222 3.438   -0.000  0.50 71.47  ? 348 HOH   B O   1 
HETATM 1594 O O   . HOH   F 5 .   ? 0.075   -20.634 -19.165 1.00 61.06  ? 349 HOH   B O   1 
HETATM 1595 O O   . HOH   F 5 .   ? -9.856  9.010   -10.651 1.00 49.11  ? 350 HOH   B O   1 
HETATM 1596 O O   . HOH   F 5 .   ? -13.945 -7.022  1.599   1.00 73.87  ? 351 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 0.8961 0.4489 0.7633 0.1997  -0.1082 -0.1352 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.8801 0.5074 0.7294 0.2231  -0.0917 -0.1381 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.8574 0.5017 0.7049 0.2166  -0.0698 -0.0995 50  ASP   A C   
4    O O   . ASP   A 7   ? 0.8781 0.4737 0.7107 0.2309  -0.0726 -0.0831 50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.9298 0.5570 0.7545 0.2697  -0.1052 -0.1718 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.9967 0.7151 0.8155 0.2868  -0.0885 -0.1875 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 0.9969 0.7529 0.8138 0.2809  -0.0856 -0.2051 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.0334 0.7853 0.8497 0.3056  -0.0783 -0.1816 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.8125 0.5225 0.6694 0.1991  -0.0499 -0.0865 51  MET   A N   
10   C CA  . MET   A 8   ? 0.7899 0.5227 0.6439 0.1942  -0.0310 -0.0552 51  MET   A CA  
11   C C   . MET   A 8   ? 0.7686 0.5297 0.6062 0.2280  -0.0304 -0.0635 51  MET   A C   
12   O O   . MET   A 8   ? 0.7571 0.5506 0.5931 0.2504  -0.0360 -0.0941 51  MET   A O   
13   C CB  . MET   A 8   ? 0.7722 0.5608 0.6401 0.1683  -0.0142 -0.0439 51  MET   A CB  
14   C CG  . MET   A 8   ? 0.7917 0.5615 0.6825 0.1364  -0.0147 -0.0328 51  MET   A CG  
15   S SD  . MET   A 8   ? 0.7639 0.5974 0.6657 0.1148  0.0009  -0.0227 51  MET   A SD  
16   C CE  . MET   A 8   ? 0.7613 0.5716 0.7008 0.0828  -0.0058 -0.0161 51  MET   A CE  
17   N N   . TYR   A 9   ? 0.7553 0.5084 0.5819 0.2333  -0.0235 -0.0377 52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.7390 0.5192 0.5539 0.2664  -0.0276 -0.0461 52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.7177 0.5195 0.5262 0.2608  -0.0155 -0.0204 52  TYR   A C   
20   O O   . TYR   A 9   ? 0.7324 0.5048 0.5344 0.2397  -0.0048 0.0100  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.7712 0.4890 0.5618 0.3023  -0.0477 -0.0520 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.8226 0.4566 0.5877 0.2964  -0.0472 -0.0153 52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.8544 0.4211 0.6235 0.2740  -0.0497 -0.0059 52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.8502 0.4701 0.5859 0.3150  -0.0447 0.0091  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.8994 0.3883 0.6486 0.2639  -0.0436 0.0314  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.8983 0.4385 0.6028 0.3110  -0.0388 0.0472  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.9311 0.4052 0.6441 0.2834  -0.0360 0.0602  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.9858 0.3815 0.6728 0.2734  -0.0243 0.1018  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.6794 0.5348 0.4923 0.2805  -0.0177 -0.0347 53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.6589 0.5354 0.4644 0.2787  -0.0111 -0.0169 53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.6714 0.5278 0.4491 0.3187  -0.0274 -0.0154 53  ILE   A C   
32   O O   . ILE   A 10  ? 0.6697 0.5249 0.4460 0.3512  -0.0449 -0.0384 53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.6184 0.5702 0.4531 0.2616  -0.0007 -0.0312 53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.5888 0.5968 0.4491 0.2809  -0.0081 -0.0666 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.6174 0.5774 0.4648 0.2258  0.0149  -0.0253 53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.5605 0.6348 0.4497 0.2637  0.0023  -0.0759 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.6825 0.5213 0.4331 0.3202  -0.0224 0.0116  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.7082 0.5227 0.4188 0.3608  -0.0377 0.0181  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.6916 0.5517 0.4009 0.3614  -0.0363 0.0184  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.6892 0.5524 0.3989 0.3329  -0.0175 0.0387  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.7834 0.5098 0.4445 0.3657  -0.0304 0.0584  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.8874 0.5490 0.5415 0.3708  -0.0375 0.0588  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.0215 0.5875 0.6251 0.3764  -0.0298 0.1006  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.0352 0.5905 0.6139 0.3667  -0.0105 0.1343  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.0926 0.5915 0.6800 0.3907  -0.0418 0.1002  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.6755 0.5697 0.3835 0.3960  -0.0587 -0.0060 55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.6654 0.5989 0.3728 0.3980  -0.0626 -0.0108 55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.7087 0.5908 0.3539 0.4113  -0.0558 0.0252  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.7444 0.5677 0.3373 0.4432  -0.0620 0.0443  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.6476 0.6365 0.3783 0.4299  -0.0916 -0.0511 55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.6420 0.6840 0.3972 0.4165  -0.0952 -0.0665 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.6297 0.7415 0.4338 0.4350  -0.1215 -0.1127 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.6322 0.7918 0.4698 0.4145  -0.1252 -0.1303 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.6811 0.8358 0.4884 0.4385  -0.1459 -0.1352 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.7263 0.8319 0.4632 0.4857  -0.1619 -0.1204 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.6555 0.8488 0.4976 0.4169  -0.1510 -0.1546 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.7079 0.6087 0.3550 0.3879  -0.0408 0.0362  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.7584 0.6227 0.3485 0.4001  -0.0293 0.0691  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.7772 0.6738 0.3489 0.4245  -0.0468 0.0516  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.7972 0.6737 0.3221 0.4351  -0.0359 0.0748  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.7585 0.6121 0.3591 0.3587  0.0035  0.0984  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.7653 0.7136 0.3764 0.4332  -0.0736 0.0094  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.7790 0.7581 0.3812 0.4564  -0.0975 -0.0153 57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.7569 0.7958 0.4251 0.4238  -0.1029 -0.0479 57  GLY   A C   
65   O O   . GLY   A 14  ? 0.7314 0.7907 0.4503 0.3820  -0.0848 -0.0494 57  GLY   A O   
66   N N   . ASP   A 15  ? 0.7656 0.8287 0.4295 0.4450  -0.1297 -0.0752 58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.7432 0.8533 0.4650 0.4161  -0.1387 -0.1069 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.7617 0.8520 0.4696 0.3875  -0.1150 -0.0850 58  ASP   A C   
69   O O   . ASP   A 15  ? 0.7963 0.8465 0.4453 0.4010  -0.0987 -0.0520 58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.7569 0.8899 0.4719 0.4532  -0.1803 -0.1448 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.7903 0.9725 0.5553 0.4709  -0.2107 -0.1850 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.7910 0.9767 0.5718 0.4710  -0.2010 -0.1782 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.8092 1.0274 0.5978 0.4882  -0.2467 -0.2261 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.7364 0.8550 0.4981 0.3499  -0.1132 -0.1039 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.7505 0.8496 0.4992 0.3275  -0.0967 -0.0888 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.7575 0.8639 0.5045 0.3402  -0.1255 -0.1197 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.7223 0.8583 0.5275 0.3168  -0.1399 -0.1514 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.7343 0.8431 0.5307 0.2776  -0.0713 -0.0807 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.7506 0.8468 0.5408 0.2706  -0.0471 -0.0527 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.7507 0.8387 0.5337 0.2595  -0.0605 -0.0703 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.7479 0.8521 0.5748 0.2281  -0.0233 -0.0448 59  ILE   A CD1 
82   N N   . THR   A 17  ? 0.8054 0.8848 0.4849 0.3793  -0.1342 -0.1118 60  THR   A N   
83   C CA  . THR   A 17  ? 0.8354 0.9133 0.4970 0.4017  -0.1650 -0.1422 60  THR   A CA  
84   C C   . THR   A 17  ? 0.8910 0.9344 0.4855 0.4209  -0.1509 -0.1189 60  THR   A C   
85   O O   . THR   A 17  ? 0.9125 0.9368 0.4610 0.4339  -0.1231 -0.0802 60  THR   A O   
86   C CB  . THR   A 17  ? 0.8557 0.9437 0.4883 0.4533  -0.2025 -0.1683 60  THR   A CB  
87   O OG1 . THR   A 17  ? 0.8962 0.9568 0.4605 0.4886  -0.1869 -0.1325 60  THR   A OG1 
88   C CG2 . THR   A 17  ? 0.8223 0.9579 0.5299 0.4421  -0.2284 -0.2072 60  THR   A CG2 
89   N N   . TRP   A 18  ? 0.9133 0.9496 0.5029 0.4253  -0.1709 -0.1444 61  TRP   A N   
90   C CA  . TRP   A 18  ? 0.9750 0.9844 0.4985 0.4530  -0.1622 -0.1301 61  TRP   A CA  
91   C C   . TRP   A 18  ? 1.0423 1.0452 0.4926 0.5154  -0.1833 -0.1372 61  TRP   A C   
92   O O   . TRP   A 18  ? 1.0360 1.0514 0.4944 0.5368  -0.2247 -0.1774 61  TRP   A O   
93   C CB  . TRP   A 18  ? 0.9690 0.9666 0.5115 0.4392  -0.1819 -0.1605 61  TRP   A CB  
94   C CG  . TRP   A 18  ? 1.0056 0.9787 0.4795 0.4771  -0.1828 -0.1586 61  TRP   A CG  
95   C CD1 . TRP   A 18  ? 1.0393 1.0035 0.4581 0.5286  -0.2151 -0.1868 61  TRP   A CD1 
96   C CD2 . TRP   A 18  ? 1.0178 0.9751 0.4755 0.4678  -0.1545 -0.1342 61  TRP   A CD2 
97   N NE1 . TRP   A 18  ? 1.0675 1.0116 0.4328 0.5536  -0.2047 -0.1791 61  TRP   A NE1 
98   C CE2 . TRP   A 18  ? 1.0552 0.9969 0.4468 0.5166  -0.1678 -0.1473 61  TRP   A CE2 
99   C CE3 . TRP   A 18  ? 1.0122 0.9698 0.5023 0.4278  -0.1206 -0.1041 61  TRP   A CE3 
100  C CZ2 . TRP   A 18  ? 1.0753 1.0059 0.4380 0.5258  -0.1470 -0.1317 61  TRP   A CZ2 
101  C CZ3 . TRP   A 18  ? 1.0343 0.9803 0.4964 0.4369  -0.1030 -0.0893 61  TRP   A CZ3 
102  C CH2 . TRP   A 18  ? 1.0604 0.9955 0.4614 0.4855  -0.1147 -0.1023 61  TRP   A CH2 
103  N N   . GLU   A 19  ? 1.1023 1.0876 0.4822 0.5451  -0.1547 -0.0986 62  GLU   A N   
104  C CA  . GLU   A 19  ? 1.1696 1.1419 0.4647 0.6083  -0.1691 -0.0985 62  GLU   A CA  
105  C C   . GLU   A 19  ? 1.2324 1.1912 0.4607 0.6459  -0.1694 -0.1026 62  GLU   A C   
106  O O   . GLU   A 19  ? 1.2432 1.1979 0.4546 0.6377  -0.1307 -0.0699 62  GLU   A O   
107  C CB  . GLU   A 19  ? 1.2199 1.1773 0.4747 0.6202  -0.1357 -0.0499 62  GLU   A CB  
108  C CG  . GLU   A 19  ? 1.2750 1.2413 0.5846 0.5948  -0.1406 -0.0503 62  GLU   A CG  
109  C CD  . GLU   A 19  ? 1.3648 1.3455 0.6821 0.6242  -0.1898 -0.0930 62  GLU   A CD  
110  O OE1 . GLU   A 19  ? 1.4451 1.4089 0.6852 0.6832  -0.2101 -0.0969 62  GLU   A OE1 
111  O OE2 . GLU   A 19  ? 1.3377 1.3494 0.7382 0.5899  -0.2075 -0.1228 62  GLU   A OE2 
112  N N   . LYS   A 20  ? 1.2699 1.2258 0.4648 0.6882  -0.2152 -0.1470 63  LYS   A N   
113  C CA  . LYS   A 20  ? 1.3328 1.2745 0.4557 0.7332  -0.2208 -0.1573 63  LYS   A CA  
114  C C   . LYS   A 20  ? 1.3964 1.3259 0.4189 0.7835  -0.1872 -0.1134 63  LYS   A C   
115  O O   . LYS   A 20  ? 1.4149 1.3375 0.4081 0.8020  -0.1853 -0.0950 63  LYS   A O   
116  C CB  . LYS   A 20  ? 1.3769 1.3161 0.4864 0.7698  -0.2842 -0.2208 63  LYS   A CB  
117  C CG  . LYS   A 20  ? 1.4027 1.3565 0.6167 0.7205  -0.3212 -0.2665 63  LYS   A CG  
118  C CD  . LYS   A 20  ? 1.4713 1.4257 0.6729 0.7606  -0.3871 -0.3315 63  LYS   A CD  
119  C CE  . LYS   A 20  ? 1.4812 1.4627 0.7904 0.7165  -0.4240 -0.3754 63  LYS   A CE  
120  N NZ  . LYS   A 20  ? 1.5125 1.4999 0.8154 0.7567  -0.4916 -0.4421 63  LYS   A NZ  
121  N N   . ASP   A 21  ? 1.4293 1.3551 0.3969 0.8080  -0.1605 -0.0968 64  ASP   A N   
122  C CA  . ASP   A 21  ? 1.4815 1.3995 0.3539 0.8533  -0.1198 -0.0512 64  ASP   A CA  
123  C C   . ASP   A 21  ? 1.4797 1.4000 0.3799 0.8123  -0.0639 0.0097  64  ASP   A C   
124  O O   . ASP   A 21  ? 1.5097 1.4124 0.3467 0.8390  -0.0394 0.0481  64  ASP   A O   
125  C CB  . ASP   A 21  ? 1.5455 1.4440 0.3222 0.9237  -0.1510 -0.0651 64  ASP   A CB  
126  C CG  . ASP   A 21  ? 1.6321 1.5272 0.3689 0.9733  -0.2075 -0.1269 64  ASP   A CG  
127  O OD1 . ASP   A 21  ? 1.6547 1.5540 0.3806 0.9817  -0.2029 -0.1406 64  ASP   A OD1 
128  O OD2 . ASP   A 21  ? 1.6648 1.5528 0.3813 1.0066  -0.2592 -0.1645 64  ASP   A OD2 
129  N N   . ALA   A 22  ? 1.4418 1.3785 0.4341 0.7484  -0.0461 0.0175  65  ALA   A N   
130  C CA  . ALA   A 22  ? 1.4314 1.3721 0.4626 0.7043  0.0021  0.0679  65  ALA   A CA  
131  C C   . ALA   A 22  ? 1.4418 1.4000 0.4478 0.7090  0.0551  0.1061  65  ALA   A C   
132  O O   . ALA   A 22  ? 1.4505 1.4203 0.4185 0.7427  0.0516  0.0889  65  ALA   A O   
133  C CB  . ALA   A 22  ? 1.3909 1.3441 0.5268 0.6396  -0.0063 0.0543  65  ALA   A CB  
134  N N   . GLU   A 23  ? 1.4362 1.3982 0.4649 0.6772  0.1032  0.1555  66  GLU   A N   
135  C CA  . GLU   A 23  ? 1.4338 1.4236 0.4565 0.6749  0.1559  0.1911  66  GLU   A CA  
136  C C   . GLU   A 23  ? 1.3877 1.4114 0.4790 0.6460  0.1509  0.1672  66  GLU   A C   
137  O O   . GLU   A 23  ? 1.3618 1.3878 0.5308 0.5962  0.1403  0.1589  66  GLU   A O   
138  C CB  . GLU   A 23  ? 1.4722 1.4567 0.5241 0.6361  0.2024  0.2438  66  GLU   A CB  
139  C CG  . GLU   A 23  ? 1.5570 1.5739 0.6008 0.6358  0.2623  0.2853  66  GLU   A CG  
140  C CD  . GLU   A 23  ? 1.6537 1.6727 0.7591 0.5811  0.3042  0.3288  66  GLU   A CD  
141  O OE1 . GLU   A 23  ? 1.6809 1.6599 0.8028 0.5575  0.2915  0.3365  66  GLU   A OE1 
142  O OE2 . GLU   A 23  ? 1.6669 1.7295 0.8076 0.5627  0.3481  0.3523  66  GLU   A OE2 
143  N N   . VAL   A 24  ? 1.3787 1.4247 0.4349 0.6821  0.1555  0.1538  67  VAL   A N   
144  C CA  . VAL   A 24  ? 1.3437 1.4154 0.4521 0.6653  0.1480  0.1300  67  VAL   A CA  
145  C C   . VAL   A 24  ? 1.3033 1.4229 0.4424 0.6508  0.2015  0.1650  67  VAL   A C   
146  O O   . VAL   A 24  ? 1.3143 1.4600 0.4023 0.6915  0.2310  0.1781  67  VAL   A O   
147  C CB  . VAL   A 24  ? 1.3730 1.4359 0.4314 0.7149  0.1108  0.0842  67  VAL   A CB  
148  C CG1 . VAL   A 24  ? 1.3587 1.4287 0.4749 0.6913  0.0929  0.0570  67  VAL   A CG1 
149  C CG2 . VAL   A 24  ? 1.4066 1.4290 0.4278 0.7376  0.0593  0.0490  67  VAL   A CG2 
150  N N   . THR   A 25  ? 1.2542 1.3901 0.4778 0.5948  0.2142  0.1782  68  THR   A N   
151  C CA  . THR   A 25  ? 1.2136 1.4023 0.4829 0.5757  0.2612  0.2071  68  THR   A CA  
152  C C   . THR   A 25  ? 1.1712 1.3789 0.5263 0.5330  0.2474  0.1906  68  THR   A C   
153  O O   . THR   A 25  ? 1.1749 1.3494 0.5469 0.5175  0.2064  0.1620  68  THR   A O   
154  C CB  . THR   A 25  ? 1.2251 1.4143 0.4961 0.5549  0.3062  0.2570  68  THR   A CB  
155  O OG1 . THR   A 25  ? 1.2038 1.4522 0.5099 0.5458  0.3568  0.2846  68  THR   A OG1 
156  C CG2 . THR   A 25  ? 1.2195 1.3790 0.5473 0.5018  0.2941  0.2640  68  THR   A CG2 
157  N N   . GLY   A 26  ? 1.1284 1.3910 0.5352 0.5172  0.2812  0.2074  69  GLY   A N   
158  C CA  . GLY   A 26  ? 1.0938 1.3765 0.5754 0.4832  0.2676  0.1925  69  GLY   A CA  
159  C C   . GLY   A 26  ? 1.0827 1.3842 0.5572 0.5154  0.2484  0.1609  69  GLY   A C   
160  O O   . GLY   A 26  ? 1.1156 1.3849 0.5305 0.5542  0.2210  0.1351  69  GLY   A O   
161  N N   . ASN   A 27  ? 1.0336 1.3848 0.5695 0.5013  0.2591  0.1602  70  ASN   A N   
162  C CA  . ASN   A 27  ? 1.0232 1.3912 0.5546 0.5343  0.2397  0.1305  70  ASN   A CA  
163  C C   . ASN   A 27  ? 1.0124 1.3352 0.5658 0.5124  0.1954  0.1053  70  ASN   A C   
164  O O   . ASN   A 27  ? 1.0162 1.3082 0.5963 0.4697  0.1854  0.1122  70  ASN   A O   
165  C CB  . ASN   A 27  ? 0.9994 1.4562 0.5779 0.5443  0.2772  0.1414  70  ASN   A CB  
166  C CG  . ASN   A 27  ? 1.0057 1.5029 0.6760 0.4952  0.2873  0.1526  70  ASN   A CG  
167  O OD1 . ASN   A 27  ? 1.0155 1.4972 0.7171 0.4499  0.2969  0.1739  70  ASN   A OD1 
168  N ND2 . ASN   A 27  ? 0.9861 1.5358 0.7007 0.5069  0.2825  0.1357  70  ASN   A ND2 
169  N N   . SER   A 28  ? 1.0009 1.3134 0.5356 0.5446  0.1693  0.0767  71  SER   A N   
170  C CA  . SER   A 28  ? 0.9995 1.2604 0.5425 0.5289  0.1300  0.0560  71  SER   A CA  
171  C C   . SER   A 28  ? 0.9576 1.2607 0.5406 0.5376  0.1282  0.0484  71  SER   A C   
172  O O   . SER   A 28  ? 0.9720 1.2713 0.5265 0.5808  0.1120  0.0264  71  SER   A O   
173  C CB  . SER   A 28  ? 1.0524 1.2438 0.5317 0.5593  0.0934  0.0270  71  SER   A CB  
174  O OG  . SER   A 28  ? 1.0948 1.2634 0.5301 0.5706  0.0933  0.0265  71  SER   A OG  
175  N N   . PRO   A 29  ? 0.9070 1.2475 0.5547 0.5001  0.1399  0.0627  72  PRO   A N   
176  C CA  . PRO   A 29  ? 0.8661 1.2558 0.5559 0.5123  0.1350  0.0521  72  PRO   A CA  
177  C C   . PRO   A 29  ? 0.8780 1.2136 0.5620 0.5047  0.0964  0.0366  72  PRO   A C   
178  O O   . PRO   A 29  ? 0.9041 1.1878 0.5857 0.4672  0.0848  0.0431  72  PRO   A O   
179  C CB  . PRO   A 29  ? 0.8244 1.2898 0.5911 0.4770  0.1687  0.0740  72  PRO   A CB  
180  C CG  . PRO   A 29  ? 0.8486 1.2712 0.6102 0.4342  0.1776  0.0949  72  PRO   A CG  
181  C CD  . PRO   A 29  ? 0.8818 1.2278 0.5687 0.4500  0.1579  0.0868  72  PRO   A CD  
182  N N   . ARG   A 30  ? 0.8593 1.2092 0.5404 0.5417  0.0783  0.0174  73  ARG   A N   
183  C CA  . ARG   A 30  ? 0.8780 1.1731 0.5456 0.5391  0.0431  0.0062  73  ARG   A CA  
184  C C   . ARG   A 30  ? 0.8073 1.1703 0.5425 0.5259  0.0450  0.0070  73  ARG   A C   
185  O O   . ARG   A 30  ? 0.7640 1.2038 0.5357 0.5557  0.0511  -0.0035 73  ARG   A O   
186  C CB  . ARG   A 30  ? 0.9519 1.1962 0.5599 0.5909  0.0137  -0.0168 73  ARG   A CB  
187  C CG  . ARG   A 30  ? 1.0733 1.2391 0.6177 0.5981  0.0039  -0.0225 73  ARG   A CG  
188  C CD  . ARG   A 30  ? 1.1690 1.3125 0.6628 0.6591  -0.0149 -0.0475 73  ARG   A CD  
189  N NE  . ARG   A 30  ? 1.2707 1.3506 0.7106 0.6673  -0.0243 -0.0572 73  ARG   A NE  
190  C CZ  . ARG   A 30  ? 1.3638 1.3397 0.7593 0.6580  -0.0550 -0.0672 73  ARG   A CZ  
191  N NH1 . ARG   A 30  ? 1.3946 1.3125 0.7843 0.6412  -0.0752 -0.0639 73  ARG   A NH1 
192  N NH2 . ARG   A 30  ? 1.3871 1.3158 0.7434 0.6655  -0.0657 -0.0807 73  ARG   A NH2 
193  N N   . LEU   A 31  ? 0.7879 1.1286 0.5437 0.4817  0.0399  0.0172  74  LEU   A N   
194  C CA  . LEU   A 31  ? 0.7299 1.1318 0.5512 0.4655  0.0381  0.0149  74  LEU   A CA  
195  C C   . LEU   A 31  ? 0.7408 1.0884 0.5354 0.4662  0.0029  0.0060  74  LEU   A C   
196  O O   . LEU   A 31  ? 0.7837 1.0541 0.5370 0.4418  -0.0051 0.0149  74  LEU   A O   
197  C CB  . LEU   A 31  ? 0.7030 1.1354 0.5773 0.4139  0.0650  0.0339  74  LEU   A CB  
198  C CG  . LEU   A 31  ? 0.6985 1.1800 0.5954 0.4099  0.1042  0.0493  74  LEU   A CG  
199  C CD1 . LEU   A 31  ? 0.6904 1.1735 0.6220 0.3600  0.1262  0.0704  74  LEU   A CD1 
200  C CD2 . LEU   A 31  ? 0.6577 1.2401 0.6106 0.4353  0.1214  0.0417  74  LEU   A CD2 
201  N N   . ASP   A 32  ? 0.6941 1.0875 0.5146 0.4944  -0.0166 -0.0115 75  ASP   A N   
202  C CA  . ASP   A 32  ? 0.7033 1.0511 0.4944 0.5017  -0.0508 -0.0198 75  ASP   A CA  
203  C C   . ASP   A 32  ? 0.6485 1.0264 0.4921 0.4574  -0.0469 -0.0152 75  ASP   A C   
204  O O   . ASP   A 32  ? 0.5941 1.0644 0.5184 0.4501  -0.0400 -0.0243 75  ASP   A O   
205  C CB  . ASP   A 32  ? 0.7144 1.1092 0.5169 0.5546  -0.0763 -0.0437 75  ASP   A CB  
206  C CG  . ASP   A 32  ? 0.8159 1.1709 0.5582 0.6070  -0.0875 -0.0528 75  ASP   A CG  
207  O OD1 . ASP   A 32  ? 0.8819 1.1455 0.5572 0.6019  -0.0858 -0.0417 75  ASP   A OD1 
208  O OD2 . ASP   A 32  ? 0.8161 1.2323 0.5809 0.6542  -0.0998 -0.0738 75  ASP   A OD2 
209  N N   . VAL   A 33  ? 0.6571 0.9606 0.4598 0.4268  -0.0502 -0.0026 76  VAL   A N   
210  C CA  . VAL   A 33  ? 0.6149 0.9374 0.4587 0.3871  -0.0479 -0.0003 76  VAL   A CA  
211  C C   . VAL   A 33  ? 0.6350 0.8999 0.4281 0.3924  -0.0771 -0.0052 76  VAL   A C   
212  O O   . VAL   A 33  ? 0.6745 0.8804 0.3988 0.4254  -0.0971 -0.0066 76  VAL   A O   
213  C CB  . VAL   A 33  ? 0.6177 0.9229 0.4718 0.3430  -0.0178 0.0194  76  VAL   A CB  
214  C CG1 . VAL   A 33  ? 0.5852 0.9525 0.4886 0.3391  0.0120  0.0261  76  VAL   A CG1 
215  C CG2 . VAL   A 33  ? 0.6753 0.8877 0.4535 0.3386  -0.0172 0.0317  76  VAL   A CG2 
216  N N   . ALA   A 34  ? 0.6017 0.8838 0.4271 0.3631  -0.0803 -0.0086 77  ALA   A N   
217  C CA  . ALA   A 34  ? 0.6203 0.8564 0.3991 0.3666  -0.1039 -0.0133 77  ALA   A CA  
218  C C   . ALA   A 34  ? 0.6094 0.8329 0.4033 0.3223  -0.0891 -0.0056 77  ALA   A C   
219  O O   . ALA   A 34  ? 0.5722 0.8494 0.4384 0.2940  -0.0745 -0.0078 77  ALA   A O   
220  C CB  . ALA   A 34  ? 0.5875 0.8816 0.4012 0.3932  -0.1359 -0.0399 77  ALA   A CB  
221  N N   . LEU   A 35  ? 0.6388 0.7904 0.3640 0.3168  -0.0911 0.0041  78  LEU   A N   
222  C CA  . LEU   A 35  ? 0.6285 0.7669 0.3613 0.2811  -0.0782 0.0090  78  LEU   A CA  
223  C C   . LEU   A 35  ? 0.6331 0.7668 0.3450 0.2907  -0.1033 -0.0068 78  LEU   A C   
224  O O   . LEU   A 35  ? 0.6724 0.7556 0.3088 0.3167  -0.1175 -0.0039 78  LEU   A O   
225  C CB  . LEU   A 35  ? 0.6613 0.7310 0.3386 0.2655  -0.0565 0.0307  78  LEU   A CB  
226  C CG  . LEU   A 35  ? 0.6684 0.7281 0.3546 0.2319  -0.0404 0.0353  78  LEU   A CG  
227  C CD1 . LEU   A 35  ? 0.6351 0.7423 0.3931 0.2075  -0.0254 0.0346  78  LEU   A CD1 
228  C CD2 . LEU   A 35  ? 0.7081 0.7066 0.3416 0.2203  -0.0223 0.0530  78  LEU   A CD2 
229  N N   . ASP   A 36  ? 0.5907 0.7729 0.3657 0.2718  -0.1101 -0.0240 79  ASP   A N   
230  C CA  . ASP   A 36  ? 0.5961 0.7764 0.3524 0.2834  -0.1380 -0.0447 79  ASP   A CA  
231  C C   . ASP   A 36  ? 0.6295 0.7539 0.3296 0.2683  -0.1249 -0.0348 79  ASP   A C   
232  O O   . ASP   A 36  ? 0.6369 0.7350 0.3304 0.2440  -0.0948 -0.0143 79  ASP   A O   
233  C CB  . ASP   A 36  ? 0.5570 0.8122 0.4079 0.2723  -0.1576 -0.0737 79  ASP   A CB  
234  C CG  . ASP   A 36  ? 0.5794 0.8473 0.4893 0.2291  -0.1394 -0.0730 79  ASP   A CG  
235  O OD1 . ASP   A 36  ? 0.6143 0.8398 0.4944 0.2102  -0.1117 -0.0510 79  ASP   A OD1 
236  O OD2 . ASP   A 36  ? 0.5562 0.8747 0.5433 0.2147  -0.1546 -0.0958 79  ASP   A OD2 
237  N N   . GLU   A 37  ? 0.6410 0.7525 0.3019 0.2856  -0.1483 -0.0517 80  GLU   A N   
238  C CA  . GLU   A 37  ? 0.6764 0.7430 0.2807 0.2779  -0.1362 -0.0457 80  GLU   A CA  
239  C C   . GLU   A 37  ? 0.6522 0.7339 0.3127 0.2393  -0.1159 -0.0465 80  GLU   A C   
240  O O   . GLU   A 37  ? 0.6794 0.7273 0.3018 0.2285  -0.0950 -0.0353 80  GLU   A O   
241  C CB  . GLU   A 37  ? 0.7223 0.7845 0.2815 0.3091  -0.1701 -0.0703 80  GLU   A CB  
242  C CG  . GLU   A 37  ? 0.8413 0.8421 0.2986 0.3216  -0.1561 -0.0555 80  GLU   A CG  
243  C CD  . GLU   A 37  ? 0.9168 0.9189 0.3382 0.3454  -0.1841 -0.0837 80  GLU   A CD  
244  O OE1 . GLU   A 37  ? 0.9190 0.9394 0.3784 0.3260  -0.1831 -0.1010 80  GLU   A OE1 
245  O OE2 . GLU   A 37  ? 0.9807 0.9621 0.3313 0.3871  -0.2095 -0.0899 80  GLU   A OE2 
246  N N   . SER   A 38  ? 0.5959 0.7273 0.3462 0.2193  -0.1206 -0.0588 81  SER   A N   
247  C CA  . SER   A 38  ? 0.5690 0.7072 0.3703 0.1855  -0.1036 -0.0580 81  SER   A CA  
248  C C   . SER   A 38  ? 0.5599 0.6912 0.3772 0.1649  -0.0697 -0.0302 81  SER   A C   
249  O O   . SER   A 38  ? 0.5508 0.6884 0.4121 0.1401  -0.0564 -0.0273 81  SER   A O   
250  C CB  . SER   A 38  ? 0.5370 0.7238 0.4261 0.1710  -0.1235 -0.0822 81  SER   A CB  
251  O OG  . SER   A 38  ? 0.5743 0.7710 0.4547 0.1910  -0.1609 -0.1143 81  SER   A OG  
252  N N   . GLY   A 39  ? 0.5606 0.6758 0.3411 0.1773  -0.0586 -0.0116 82  GLY   A N   
253  C CA  . GLY   A 39  ? 0.5520 0.6608 0.3432 0.1631  -0.0318 0.0101  82  GLY   A CA  
254  C C   . GLY   A 39  ? 0.5077 0.6628 0.3690 0.1530  -0.0263 0.0115  82  GLY   A C   
255  O O   . GLY   A 39  ? 0.5010 0.6549 0.3790 0.1385  -0.0045 0.0266  82  GLY   A O   
256  N N   . ASP   A 40  ? 0.4751 0.6739 0.3774 0.1622  -0.0455 -0.0045 83  ASP   A N   
257  C CA  . ASP   A 40  ? 0.4319 0.6851 0.4080 0.1519  -0.0376 -0.0038 83  ASP   A CA  
258  C C   . ASP   A 40  ? 0.4315 0.7080 0.3992 0.1795  -0.0401 -0.0014 83  ASP   A C   
259  O O   . ASP   A 40  ? 0.4363 0.7143 0.3775 0.2073  -0.0652 -0.0155 83  ASP   A O   
260  C CB  . ASP   A 40  ? 0.3993 0.6950 0.4439 0.1389  -0.0576 -0.0279 83  ASP   A CB  
261  C CG  . ASP   A 40  ? 0.4176 0.6887 0.4793 0.1104  -0.0528 -0.0297 83  ASP   A CG  
262  O OD1 . ASP   A 40  ? 0.4252 0.6747 0.4851 0.0937  -0.0265 -0.0086 83  ASP   A OD1 
263  O OD2 . ASP   A 40  ? 0.4338 0.7057 0.5082 0.1086  -0.0783 -0.0545 83  ASP   A OD2 
264  N N   . PHE   A 41  ? 0.4238 0.7146 0.4069 0.1765  -0.0153 0.0157  84  PHE   A N   
265  C CA  . PHE   A 41  ? 0.4297 0.7435 0.4055 0.2052  -0.0146 0.0173  84  PHE   A CA  
266  C C   . PHE   A 41  ? 0.4094 0.8062 0.4651 0.2087  -0.0188 0.0032  84  PHE   A C   
267  O O   . PHE   A 41  ? 0.3739 0.8097 0.4996 0.1795  -0.0102 0.0008  84  PHE   A O   
268  C CB  . PHE   A 41  ? 0.4291 0.7242 0.3831 0.2042  0.0131  0.0386  84  PHE   A CB  
269  C CG  . PHE   A 41  ? 0.4737 0.6960 0.3529 0.2083  0.0137  0.0481  84  PHE   A CG  
270  C CD1 . PHE   A 41  ? 0.5074 0.6941 0.3305 0.2365  0.0004  0.0460  84  PHE   A CD1 
271  C CD2 . PHE   A 41  ? 0.4906 0.6799 0.3590 0.1836  0.0274  0.0584  84  PHE   A CD2 
272  C CE1 . PHE   A 41  ? 0.5540 0.6739 0.3174 0.2339  0.0030  0.0551  84  PHE   A CE1 
273  C CE2 . PHE   A 41  ? 0.5300 0.6627 0.3423 0.1842  0.0288  0.0646  84  PHE   A CE2 
274  C CZ  . PHE   A 41  ? 0.5531 0.6517 0.3162 0.2063  0.0179  0.0635  84  PHE   A CZ  
275  N N   . SER   A 42  ? 0.4316 0.8554 0.4800 0.2443  -0.0316 -0.0066 85  SER   A N   
276  C CA  . SER   A 42  ? 0.4116 0.9261 0.5405 0.2528  -0.0356 -0.0231 85  SER   A CA  
277  C C   . SER   A 42  ? 0.4545 0.9878 0.5604 0.2942  -0.0330 -0.0229 85  SER   A C   
278  O O   . SER   A 42  ? 0.5103 0.9809 0.5343 0.3239  -0.0479 -0.0212 85  SER   A O   
279  C CB  . SER   A 42  ? 0.4045 0.9456 0.5588 0.2628  -0.0750 -0.0532 85  SER   A CB  
280  O OG  . SER   A 42  ? 0.4700 0.9590 0.5400 0.3026  -0.1042 -0.0606 85  SER   A OG  
281  N N   . LEU   A 43  ? 0.4270 1.0428 0.6025 0.2963  -0.0124 -0.0239 86  LEU   A N   
282  C CA  . LEU   A 43  ? 0.4590 1.0982 0.6130 0.3414  -0.0107 -0.0278 86  LEU   A CA  
283  C C   . LEU   A 43  ? 0.4870 1.1539 0.6426 0.3828  -0.0514 -0.0573 86  LEU   A C   
284  O O   . LEU   A 43  ? 0.4459 1.1744 0.6718 0.3740  -0.0695 -0.0786 86  LEU   A O   
285  C CB  . LEU   A 43  ? 0.4076 1.1339 0.6331 0.3356  0.0273  -0.0201 86  LEU   A CB  
286  C CG  . LEU   A 43  ? 0.4456 1.1443 0.6537 0.3094  0.0692  0.0111  86  LEU   A CG  
287  C CD1 . LEU   A 43  ? 0.4009 1.1901 0.6741 0.3095  0.1085  0.0196  86  LEU   A CD1 
288  C CD2 . LEU   A 43  ? 0.5176 1.1296 0.6228 0.3341  0.0664  0.0214  86  LEU   A CD2 
289  N N   . VAL   A 44  ? 0.5564 1.1743 0.6336 0.4297  -0.0687 -0.0603 87  VAL   A N   
290  C CA  . VAL   A 44  ? 0.5835 1.2135 0.6425 0.4808  -0.1094 -0.0862 87  VAL   A CA  
291  C C   . VAL   A 44  ? 0.5749 1.2866 0.6755 0.5191  -0.1009 -0.0990 87  VAL   A C   
292  O O   . VAL   A 44  ? 0.5958 1.2930 0.6699 0.5264  -0.0736 -0.0841 87  VAL   A O   
293  C CB  . VAL   A 44  ? 0.6712 1.1791 0.6076 0.5085  -0.1321 -0.0776 87  VAL   A CB  
294  C CG1 . VAL   A 44  ? 0.6912 1.1979 0.5917 0.5716  -0.1715 -0.1000 87  VAL   A CG1 
295  C CG2 . VAL   A 44  ? 0.7122 1.1509 0.6091 0.4758  -0.1401 -0.0675 87  VAL   A CG2 
296  N N   . GLU   A 45  ? 0.5408 1.3438 0.7086 0.5458  -0.1243 -0.1291 88  GLU   A N   
297  C CA  . GLU   A 45  ? 0.5224 1.4151 0.7350 0.5880  -0.1170 -0.1454 88  GLU   A CA  
298  C C   . GLU   A 45  ? 0.5210 1.4469 0.7343 0.6468  -0.1676 -0.1814 88  GLU   A C   
299  O O   . GLU   A 45  ? 0.5539 1.4544 0.7079 0.7060  -0.1849 -0.1907 88  GLU   A O   
300  C CB  . GLU   A 45  ? 0.4846 1.5028 0.8235 0.5503  -0.0749 -0.1439 88  GLU   A CB  
301  C CG  . GLU   A 45  ? 0.5670 1.5529 0.9054 0.4941  -0.0263 -0.1075 88  GLU   A CG  
302  C CD  . GLU   A 45  ? 0.6381 1.6580 0.9764 0.5052  0.0192  -0.0905 88  GLU   A CD  
303  O OE1 . GLU   A 45  ? 0.6097 1.7180 0.9886 0.5460  0.0237  -0.1087 88  GLU   A OE1 
304  O OE2 . GLU   A 45  ? 0.6880 1.6490 0.9845 0.4762  0.0498  -0.0605 88  GLU   A OE2 
305  N N   . GLY   B 7   ? 0.7502 0.7356 0.6678 0.2329  0.0760  -0.0965 16  GLY   B N   
306  C CA  . GLY   B 7   ? 0.7653 0.7301 0.6752 0.2430  0.0680  -0.0871 16  GLY   B CA  
307  C C   . GLY   B 7   ? 0.7595 0.7365 0.6742 0.2444  0.0599  -0.0812 16  GLY   B C   
308  O O   . GLY   B 7   ? 0.7563 0.7583 0.6875 0.2472  0.0569  -0.0877 16  GLY   B O   
309  N N   . GLU   B 8   ? 0.7500 0.7107 0.6507 0.2432  0.0554  -0.0693 17  GLU   B N   
310  C CA  . GLU   B 8   ? 0.7336 0.7032 0.6349 0.2468  0.0464  -0.0649 17  GLU   B CA  
311  C C   . GLU   B 8   ? 0.7129 0.6885 0.6110 0.2298  0.0463  -0.0627 17  GLU   B C   
312  O O   . GLU   B 8   ? 0.7232 0.6860 0.6077 0.2202  0.0501  -0.0558 17  GLU   B O   
313  C CB  . GLU   B 8   ? 0.7783 0.7306 0.6650 0.2593  0.0412  -0.0533 17  GLU   B CB  
314  C CG  . GLU   B 8   ? 0.8375 0.7999 0.7231 0.2679  0.0304  -0.0515 17  GLU   B CG  
315  C CD  . GLU   B 8   ? 0.9334 0.8830 0.8024 0.2822  0.0262  -0.0392 17  GLU   B CD  
316  O OE1 . GLU   B 8   ? 0.9607 0.8941 0.8180 0.2785  0.0325  -0.0284 17  GLU   B OE1 
317  O OE2 . GLU   B 8   ? 0.9578 0.9151 0.8258 0.2970  0.0164  -0.0401 17  GLU   B OE2 
318  N N   A THR   B 9   ? 0.6920 0.6866 0.6028 0.2257  0.0411  -0.0681 18  THR   B N   
319  N N   B THR   B 9   ? 0.6919 0.6866 0.6028 0.2258  0.0411  -0.0682 18  THR   B N   
320  C CA  A THR   B 9   ? 0.6886 0.6855 0.5958 0.2097  0.0395  -0.0656 18  THR   B CA  
321  C CA  B THR   B 9   ? 0.6879 0.6859 0.5962 0.2099  0.0393  -0.0661 18  THR   B CA  
322  C C   A THR   B 9   ? 0.6785 0.6778 0.5857 0.2147  0.0255  -0.0649 18  THR   B C   
323  C C   B THR   B 9   ? 0.6786 0.6780 0.5859 0.2148  0.0255  -0.0649 18  THR   B C   
324  O O   A THR   B 9   ? 0.6788 0.6816 0.5881 0.2026  0.0211  -0.0654 18  THR   B O   
325  O O   B THR   B 9   ? 0.6791 0.6815 0.5880 0.2025  0.0213  -0.0653 18  THR   B O   
326  C CB  A THR   B 9   ? 0.6984 0.7121 0.6186 0.1938  0.0474  -0.0715 18  THR   B CB  
327  C CB  B THR   B 9   ? 0.6954 0.7132 0.6199 0.1959  0.0458  -0.0729 18  THR   B CB  
328  O OG1 A THR   B 9   ? 0.7116 0.7275 0.6347 0.1964  0.0580  -0.0765 18  THR   B OG1 
329  O OG1 B THR   B 9   ? 0.6945 0.7337 0.6406 0.2039  0.0428  -0.0810 18  THR   B OG1 
330  C CG2 A THR   B 9   ? 0.7090 0.7161 0.6176 0.1765  0.0498  -0.0660 18  THR   B CG2 
331  C CG2 B THR   B 9   ? 0.7043 0.7187 0.6234 0.1889  0.0589  -0.0743 18  THR   B CG2 
332  N N   . THR   B 10  ? 0.6703 0.6657 0.5732 0.2333  0.0177  -0.0636 19  THR   B N   
333  C CA  . THR   B 10  ? 0.6563 0.6527 0.5560 0.2419  0.0029  -0.0646 19  THR   B CA  
334  C C   . THR   B 10  ? 0.6478 0.6298 0.5267 0.2381  -0.0001 -0.0572 19  THR   B C   
335  O O   . THR   B 10  ? 0.6554 0.6266 0.5197 0.2377  0.0079  -0.0487 19  THR   B O   
336  C CB  . THR   B 10  ? 0.6752 0.6705 0.5706 0.2651  -0.0030 -0.0637 19  THR   B CB  
337  O OG1 . THR   B 10  ? 0.6846 0.6913 0.5971 0.2708  0.0008  -0.0700 19  THR   B OG1 
338  C CG2 . THR   B 10  ? 0.6771 0.6758 0.5695 0.2770  -0.0199 -0.0675 19  THR   B CG2 
339  N N   . ASP   B 11  ? 0.6300 0.6116 0.5077 0.2356  -0.0126 -0.0608 20  ASP   B N   
340  C CA  . ASP   B 11  ? 0.6332 0.6010 0.4899 0.2355  -0.0176 -0.0554 20  ASP   B CA  
341  C C   . ASP   B 11  ? 0.6331 0.5952 0.4699 0.2557  -0.0184 -0.0479 20  ASP   B C   
342  O O   . ASP   B 11  ? 0.6339 0.6009 0.4720 0.2723  -0.0229 -0.0492 20  ASP   B O   
343  C CB  . ASP   B 11  ? 0.6538 0.6185 0.5117 0.2339  -0.0346 -0.0624 20  ASP   B CB  
344  C CG  . ASP   B 11  ? 0.6978 0.6642 0.5702 0.2110  -0.0345 -0.0654 20  ASP   B CG  
345  O OD1 . ASP   B 11  ? 0.7000 0.6765 0.5857 0.1978  -0.0211 -0.0643 20  ASP   B OD1 
346  O OD2 . ASP   B 11  ? 0.7256 0.6824 0.5951 0.2067  -0.0484 -0.0686 20  ASP   B OD2 
347  N N   . GLY   B 12  ? 0.6246 0.5792 0.4439 0.2544  -0.0139 -0.0394 21  GLY   B N   
348  C CA  . GLY   B 12  ? 0.6173 0.5710 0.4187 0.2716  -0.0129 -0.0300 21  GLY   B CA  
349  C C   . GLY   B 12  ? 0.6082 0.5594 0.3999 0.2637  -0.0014 -0.0190 21  GLY   B C   
350  O O   . GLY   B 12  ? 0.6101 0.5582 0.4056 0.2462  0.0040  -0.0200 21  GLY   B O   
351  N N   . VAL   B 13  ? 0.5967 0.5510 0.3757 0.2766  0.0021  -0.0079 22  VAL   B N   
352  C CA  . VAL   B 13  ? 0.5873 0.5431 0.3594 0.2693  0.0124  0.0037  22  VAL   B CA  
353  C C   . VAL   B 13  ? 0.5773 0.5302 0.3583 0.2639  0.0237  0.0115  22  VAL   B C   
354  O O   . VAL   B 13  ? 0.5822 0.5338 0.3663 0.2750  0.0230  0.0127  22  VAL   B O   
355  C CB  . VAL   B 13  ? 0.5936 0.5580 0.3461 0.2849  0.0088  0.0121  22  VAL   B CB  
356  C CG1 . VAL   B 13  ? 0.6011 0.5717 0.3449 0.3075  0.0054  0.0173  22  VAL   B CG1 
357  C CG2 . VAL   B 13  ? 0.5927 0.5636 0.3418 0.2759  0.0192  0.0243  22  VAL   B CG2 
358  N N   . TYR   B 14  ? 0.5661 0.5157 0.3520 0.2466  0.0328  0.0148  23  TYR   B N   
359  C CA  . TYR   B 14  ? 0.5599 0.5017 0.3546 0.2395  0.0415  0.0198  23  TYR   B CA  
360  C C   . TYR   B 14  ? 0.5644 0.5077 0.3555 0.2306  0.0489  0.0330  23  TYR   B C   
361  O O   . TYR   B 14  ? 0.5698 0.5206 0.3556 0.2240  0.0489  0.0343  23  TYR   B O   
362  C CB  . TYR   B 14  ? 0.5458 0.4805 0.3533 0.2251  0.0445  0.0074  23  TYR   B CB  
363  C CG  . TYR   B 14  ? 0.5373 0.4733 0.3546 0.2318  0.0395  -0.0044 23  TYR   B CG  
364  C CD1 . TYR   B 14  ? 0.5426 0.4859 0.3599 0.2351  0.0308  -0.0120 23  TYR   B CD1 
365  C CD2 . TYR   B 14  ? 0.5425 0.4726 0.3706 0.2333  0.0430  -0.0090 23  TYR   B CD2 
366  C CE1 . TYR   B 14  ? 0.5495 0.4977 0.3793 0.2394  0.0256  -0.0225 23  TYR   B CE1 
367  C CE2 . TYR   B 14  ? 0.5478 0.4844 0.3874 0.2395  0.0386  -0.0202 23  TYR   B CE2 
368  C CZ  . TYR   B 14  ? 0.5579 0.5052 0.3997 0.2416  0.0301  -0.0266 23  TYR   B CZ  
369  O OH  . TYR   B 14  ? 0.5646 0.5218 0.4210 0.2460  0.0250  -0.0372 23  TYR   B OH  
370  N N   . ARG   B 15  ? 0.5599 0.4950 0.3551 0.2291  0.0544  0.0424  24  ARG   B N   
371  C CA  . ARG   B 15  ? 0.5604 0.4961 0.3566 0.2172  0.0608  0.0554  24  ARG   B CA  
372  C C   . ARG   B 15  ? 0.5672 0.4895 0.3729 0.1985  0.0638  0.0464  24  ARG   B C   
373  O O   . ARG   B 15  ? 0.5702 0.4796 0.3821 0.1983  0.0634  0.0355  24  ARG   B O   
374  C CB  . ARG   B 15  ? 0.5692 0.4993 0.3651 0.2236  0.0643  0.0718  24  ARG   B CB  
375  C CG  . ARG   B 15  ? 0.5726 0.5163 0.3568 0.2448  0.0620  0.0821  24  ARG   B CG  
376  C CD  . ARG   B 15  ? 0.5954 0.5308 0.3790 0.2491  0.0665  0.0998  24  ARG   B CD  
377  N NE  . ARG   B 15  ? 0.6030 0.5498 0.3734 0.2723  0.0641  0.1085  24  ARG   B NE  
378  C CZ  . ARG   B 15  ? 0.6154 0.5839 0.3753 0.2808  0.0674  0.1243  24  ARG   B CZ  
379  N NH1 . ARG   B 15  ? 0.6059 0.5891 0.3696 0.2674  0.0731  0.1337  24  ARG   B NH1 
380  N NH2 . ARG   B 15  ? 0.6067 0.5851 0.3522 0.3041  0.0646  0.1304  24  ARG   B NH2 
381  N N   . VAL   B 16  ? 0.5666 0.4939 0.3732 0.1843  0.0665  0.0505  25  VAL   B N   
382  C CA  . VAL   B 16  ? 0.5740 0.4895 0.3871 0.1670  0.0684  0.0422  25  VAL   B CA  
383  C C   . VAL   B 16  ? 0.5851 0.4918 0.4042 0.1578  0.0712  0.0552  25  VAL   B C   
384  O O   . VAL   B 16  ? 0.5753 0.4966 0.3945 0.1535  0.0728  0.0692  25  VAL   B O   
385  C CB  . VAL   B 16  ? 0.5727 0.5000 0.3818 0.1571  0.0675  0.0360  25  VAL   B CB  
386  C CG1 . VAL   B 16  ? 0.5766 0.4920 0.3901 0.1414  0.0690  0.0258  25  VAL   B CG1 
387  C CG2 . VAL   B 16  ? 0.5723 0.5070 0.3748 0.1659  0.0637  0.0268  25  VAL   B CG2 
388  N N   . MET   B 17  ? 0.6038 0.4870 0.4282 0.1558  0.0713  0.0516  26  MET   B N   
389  C CA  . MET   B 17  ? 0.6276 0.4956 0.4580 0.1463  0.0722  0.0643  26  MET   B CA  
390  C C   . MET   B 17  ? 0.6651 0.5140 0.5010 0.1296  0.0703  0.0532  26  MET   B C   
391  O O   . MET   B 17  ? 0.6720 0.5183 0.5058 0.1288  0.0694  0.0352  26  MET   B O   
392  C CB  . MET   B 17  ? 0.6347 0.4844 0.4644 0.1593  0.0719  0.0706  26  MET   B CB  
393  C CG  . MET   B 17  ? 0.6448 0.5090 0.4671 0.1796  0.0717  0.0744  26  MET   B CG  
394  S SD  . MET   B 17  ? 0.6579 0.5464 0.4751 0.1840  0.0752  0.0994  26  MET   B SD  
395  C CE  . MET   B 17  ? 0.6182 0.4827 0.4420 0.1736  0.0777  0.1194  26  MET   B CE  
396  N N   . THR   B 18  ? 0.6910 0.5259 0.5337 0.1165  0.0692  0.0641  27  THR   B N   
397  C CA  . THR   B 18  ? 0.7257 0.5380 0.5730 0.1014  0.0650  0.0534  27  THR   B CA  
398  C C   . THR   B 18  ? 0.7654 0.5481 0.6189 0.0948  0.0620  0.0657  27  THR   B C   
399  O O   . THR   B 18  ? 0.7604 0.5503 0.6182 0.0925  0.0645  0.0878  27  THR   B O   
400  C CB  . THR   B 18  ? 0.7298 0.5605 0.5798 0.0853  0.0638  0.0507  27  THR   B CB  
401  O OG1 . THR   B 18  ? 0.7487 0.5554 0.6024 0.0711  0.0580  0.0399  27  THR   B OG1 
402  C CG2 . THR   B 18  ? 0.7196 0.5752 0.5763 0.0779  0.0660  0.0720  27  THR   B CG2 
403  N N   . ARG   B 19  ? 0.8030 0.5519 0.6559 0.0928  0.0567  0.0518  28  ARG   B N   
404  C CA  . ARG   B 19  ? 0.8450 0.5585 0.7028 0.0854  0.0516  0.0619  28  ARG   B CA  
405  C C   . ARG   B 19  ? 0.8694 0.5667 0.7351 0.0619  0.0441  0.0580  28  ARG   B C   
406  O O   . ARG   B 19  ? 0.8802 0.5414 0.7498 0.0534  0.0372  0.0622  28  ARG   B O   
407  C CB  . ARG   B 19  ? 0.8834 0.5645 0.7342 0.1025  0.0486  0.0508  28  ARG   B CB  
408  C CG  . ARG   B 19  ? 0.9306 0.6223 0.7763 0.1234  0.0536  0.0606  28  ARG   B CG  
409  C CD  . ARG   B 19  ? 1.0003 0.6544 0.8415 0.1369  0.0489  0.0588  28  ARG   B CD  
410  N NE  . ARG   B 19  ? 1.0521 0.7187 0.8873 0.1607  0.0521  0.0577  28  ARG   B NE  
411  C CZ  . ARG   B 19  ? 1.0884 0.7619 0.9209 0.1757  0.0521  0.0365  28  ARG   B CZ  
412  N NH1 . ARG   B 19  ? 1.0908 0.7610 0.9240 0.1706  0.0505  0.0151  28  ARG   B NH1 
413  N NH2 . ARG   B 19  ? 1.0837 0.7702 0.9132 0.1960  0.0536  0.0368  28  ARG   B NH2 
414  N N   . ARG   B 20  ? 0.8768 0.6001 0.7443 0.0518  0.0444  0.0501  29  ARG   B N   
415  C CA  . ARG   B 20  ? 0.8964 0.6128 0.7710 0.0305  0.0366  0.0439  29  ARG   B CA  
416  C C   . ARG   B 20  ? 0.8926 0.6116 0.7835 0.0102  0.0344  0.0685  29  ARG   B C   
417  O O   . ARG   B 20  ? 0.8959 0.5968 0.7958 -0.0092 0.0251  0.0658  29  ARG   B O   
418  C CB  . ARG   B 20  ? 0.9177 0.6674 0.7876 0.0294  0.0388  0.0310  29  ARG   B CB  
419  C CG  . ARG   B 20  ? 0.9787 0.7250 0.8523 0.0110  0.0300  0.0197  29  ARG   B CG  
420  C CD  . ARG   B 20  ? 1.0267 0.8085 0.8941 0.0118  0.0329  0.0111  29  ARG   B CD  
421  N NE  . ARG   B 20  ? 1.0630 0.8830 0.9349 0.0141  0.0402  0.0296  29  ARG   B NE  
422  C CZ  . ARG   B 20  ? 1.0882 0.9324 0.9726 0.0000  0.0388  0.0439  29  ARG   B CZ  
423  N NH1 . ARG   B 20  ? 1.0908 0.9251 0.9866 -0.0200 0.0297  0.0424  29  ARG   B NH1 
424  N NH2 . ARG   B 20  ? 1.0718 0.9512 0.9578 0.0063  0.0457  0.0592  29  ARG   B NH2 
425  N N   . LEU   B 21  ? 0.8827 0.6247 0.7777 0.0145  0.0426  0.0926  30  LEU   B N   
426  C CA  . LEU   B 21  ? 0.8777 0.6288 0.7890 -0.0037 0.0430  0.1192  30  LEU   B CA  
427  C C   . LEU   B 21  ? 0.8803 0.6031 0.7918 0.0004  0.0444  0.1391  30  LEU   B C   
428  O O   . LEU   B 21  ? 0.8992 0.5844 0.8002 0.0130  0.0407  0.1279  30  LEU   B O   
429  C CB  . LEU   B 21  ? 0.8645 0.6706 0.7806 -0.0033 0.0515  0.1331  30  LEU   B CB  
430  C CG  . LEU   B 21  ? 0.8754 0.7059 0.8048 -0.0237 0.0470  0.1310  30  LEU   B CG  
431  C CD1 . LEU   B 21  ? 0.8860 0.7148 0.8047 -0.0198 0.0421  0.1020  30  LEU   B CD1 
432  C CD2 . LEU   B 21  ? 0.8659 0.7493 0.8026 -0.0231 0.0554  0.1506  30  LEU   B CD2 
433  N N   . LEU   B 22  ? 0.8557 0.5965 0.7793 -0.0103 0.0493  0.1689  31  LEU   B N   
434  C CA  . LEU   B 22  ? 0.8529 0.5701 0.7758 -0.0075 0.0515  0.1918  31  LEU   B CA  
435  C C   . LEU   B 22  ? 0.8486 0.5779 0.7540 0.0224  0.0600  0.1931  31  LEU   B C   
436  O O   . LEU   B 22  ? 0.8367 0.6106 0.7387 0.0330  0.0683  0.1975  31  LEU   B O   
437  C CB  . LEU   B 22  ? 0.8334 0.5772 0.7743 -0.0272 0.0565  0.2243  31  LEU   B CB  
438  C CG  . LEU   B 22  ? 0.8479 0.5644 0.7901 -0.0303 0.0579  0.2515  31  LEU   B CG  
439  C CD1 . LEU   B 22  ? 0.8597 0.5338 0.8174 -0.0587 0.0459  0.2561  31  LEU   B CD1 
440  C CD2 . LEU   B 22  ? 0.8363 0.5999 0.7838 -0.0293 0.0709  0.2836  31  LEU   B CD2 
441  N N   . GLY   B 23  ? 0.8551 0.5445 0.7490 0.0369  0.0564  0.1870  32  GLY   B N   
442  C CA  . GLY   B 23  ? 0.8511 0.5483 0.7290 0.0657  0.0620  0.1852  32  GLY   B CA  
443  C C   . GLY   B 23  ? 0.8341 0.5565 0.7042 0.0803  0.0637  0.1598  32  GLY   B C   
444  O O   . GLY   B 23  ? 0.8375 0.5576 0.7107 0.0714  0.0592  0.1387  32  GLY   B O   
445  N N   . SER   B 24  ? 0.8142 0.5608 0.6738 0.1024  0.0697  0.1621  33  SER   B N   
446  C CA  . SER   B 24  ? 0.8010 0.5714 0.6539 0.1155  0.0708  0.1405  33  SER   B CA  
447  C C   . SER   B 24  ? 0.7699 0.5857 0.6241 0.1137  0.0768  0.1509  33  SER   B C   
448  O O   . SER   B 24  ? 0.7664 0.6012 0.6165 0.1232  0.0820  0.1707  33  SER   B O   
449  C CB  . SER   B 24  ? 0.8253 0.5908 0.6663 0.1415  0.0710  0.1336  33  SER   B CB  
450  O OG  . SER   B 24  ? 0.8665 0.5970 0.7058 0.1464  0.0651  0.1158  33  SER   B OG  
451  N N   . THR   B 25  ? 0.7459 0.5793 0.6045 0.1029  0.0757  0.1383  34  THR   B N   
452  C CA  . THR   B 25  ? 0.7216 0.5976 0.5810 0.1023  0.0802  0.1470  34  THR   B CA  
453  C C   . THR   B 25  ? 0.7008 0.5955 0.5493 0.1175  0.0800  0.1293  34  THR   B C   
454  O O   . THR   B 25  ? 0.7040 0.5859 0.5506 0.1159  0.0763  0.1081  34  THR   B O   
455  C CB  . THR   B 25  ? 0.7256 0.6113 0.5993 0.0777  0.0785  0.1509  34  THR   B CB  
456  O OG1 . THR   B 25  ? 0.7435 0.6127 0.6290 0.0624  0.0783  0.1704  34  THR   B OG1 
457  C CG2 . THR   B 25  ? 0.7087 0.6402 0.5836 0.0784  0.0826  0.1585  34  THR   B CG2 
458  N N   . GLN   B 26  ? 0.6777 0.6020 0.5183 0.1326  0.0836  0.1383  35  GLN   B N   
459  C CA  . GLN   B 26  ? 0.6668 0.6065 0.4969 0.1460  0.0817  0.1228  35  GLN   B CA  
460  C C   . GLN   B 26  ? 0.6566 0.6189 0.4893 0.1354  0.0810  0.1187  35  GLN   B C   
461  O O   . GLN   B 26  ? 0.6493 0.6390 0.4851 0.1331  0.0841  0.1338  35  GLN   B O   
462  C CB  . GLN   B 26  ? 0.6636 0.6217 0.4816 0.1692  0.0832  0.1311  35  GLN   B CB  
463  C CG  . GLN   B 26  ? 0.6757 0.6414 0.4832 0.1825  0.0786  0.1132  35  GLN   B CG  
464  C CD  . GLN   B 26  ? 0.7085 0.6911 0.5028 0.2058  0.0777  0.1190  35  GLN   B CD  
465  O OE1 . GLN   B 26  ? 0.7359 0.7109 0.5259 0.2184  0.0781  0.1257  35  GLN   B OE1 
466  N NE2 . GLN   B 26  ? 0.6932 0.6978 0.4789 0.2136  0.0753  0.1155  35  GLN   B NE2 
467  N N   . VAL   B 27  ? 0.6491 0.6022 0.4800 0.1300  0.0772  0.0988  36  VAL   B N   
468  C CA  . VAL   B 27  ? 0.6383 0.6101 0.4689 0.1217  0.0754  0.0932  36  VAL   B CA  
469  C C   . VAL   B 27  ? 0.6292 0.6172 0.4461 0.1373  0.0734  0.0860  36  VAL   B C   
470  O O   . VAL   B 27  ? 0.6275 0.6320 0.4415 0.1339  0.0715  0.0832  36  VAL   B O   
471  C CB  . VAL   B 27  ? 0.6521 0.6055 0.4869 0.1053  0.0722  0.0775  36  VAL   B CB  
472  C CG1 . VAL   B 27  ? 0.6593 0.6034 0.5081 0.0864  0.0714  0.0855  36  VAL   B CG1 
473  C CG2 . VAL   B 27  ? 0.6655 0.5936 0.4953 0.1112  0.0710  0.0608  36  VAL   B CG2 
474  N N   . GLY   B 28  ? 0.6184 0.5999 0.4271 0.1541  0.0723  0.0821  37  GLY   B N   
475  C CA  . GLY   B 28  ? 0.6114 0.6023 0.4075 0.1680  0.0681  0.0740  37  GLY   B CA  
476  C C   . GLY   B 28  ? 0.6103 0.5898 0.4008 0.1832  0.0652  0.0670  37  GLY   B C   
477  O O   . GLY   B 28  ? 0.6176 0.5857 0.4124 0.1869  0.0671  0.0708  37  GLY   B O   
478  N N   . VAL   B 29  ? 0.6019 0.5842 0.3827 0.1922  0.0595  0.0571  38  VAL   B N   
479  C CA  . VAL   B 29  ? 0.6048 0.5803 0.3803 0.2068  0.0539  0.0490  38  VAL   B CA  
480  C C   . VAL   B 29  ? 0.6008 0.5680 0.3743 0.2010  0.0488  0.0337  38  VAL   B C   
481  O O   . VAL   B 29  ? 0.5994 0.5688 0.3705 0.1903  0.0491  0.0313  38  VAL   B O   
482  C CB  . VAL   B 29  ? 0.6175 0.6091 0.3800 0.2275  0.0500  0.0567  38  VAL   B CB  
483  C CG1 . VAL   B 29  ? 0.6285 0.6131 0.3851 0.2435  0.0419  0.0477  38  VAL   B CG1 
484  C CG2 . VAL   B 29  ? 0.6217 0.6259 0.3857 0.2321  0.0567  0.0749  38  VAL   B CG2 
485  N N   . GLY   B 30  ? 0.5930 0.5520 0.3680 0.2076  0.0440  0.0244  39  GLY   B N   
486  C CA  . GLY   B 30  ? 0.5904 0.5429 0.3656 0.2010  0.0394  0.0123  39  GLY   B CA  
487  C C   . GLY   B 30  ? 0.5860 0.5352 0.3619 0.2119  0.0310  0.0046  39  GLY   B C   
488  O O   . GLY   B 30  ? 0.5939 0.5450 0.3706 0.2255  0.0289  0.0068  39  GLY   B O   
489  N N   . VAL   B 31  ? 0.5734 0.5175 0.3492 0.2056  0.0254  -0.0040 40  VAL   B N   
490  C CA  . VAL   B 31  ? 0.5649 0.5058 0.3439 0.2127  0.0154  -0.0121 40  VAL   B CA  
491  C C   . VAL   B 31  ? 0.5596 0.4995 0.3553 0.1996  0.0185  -0.0203 40  VAL   B C   
492  O O   . VAL   B 31  ? 0.5692 0.5071 0.3663 0.1843  0.0230  -0.0218 40  VAL   B O   
493  C CB  . VAL   B 31  ? 0.5682 0.5032 0.3332 0.2167  0.0036  -0.0145 40  VAL   B CB  
494  C CG1 . VAL   B 31  ? 0.5667 0.4954 0.3375 0.2193  -0.0086 -0.0239 40  VAL   B CG1 
495  C CG2 . VAL   B 31  ? 0.5767 0.5171 0.3244 0.2342  -0.0001 -0.0077 40  VAL   B CG2 
496  N N   . MET   B 32  ? 0.5413 0.4848 0.3491 0.2065  0.0161  -0.0253 41  MET   B N   
497  C CA  . MET   B 32  ? 0.5294 0.4774 0.3549 0.1960  0.0182  -0.0334 41  MET   B CA  
498  C C   . MET   B 32  ? 0.5346 0.4821 0.3634 0.1971  0.0048  -0.0394 41  MET   B C   
499  O O   . MET   B 32  ? 0.5346 0.4815 0.3597 0.2124  -0.0058 -0.0412 41  MET   B O   
500  C CB  . MET   B 32  ? 0.5187 0.4726 0.3571 0.2034  0.0230  -0.0361 41  MET   B CB  
501  C CG  . MET   B 32  ? 0.5213 0.4851 0.3786 0.1938  0.0274  -0.0444 41  MET   B CG  
502  S SD  . MET   B 32  ? 0.5638 0.5272 0.4212 0.1772  0.0422  -0.0445 41  MET   B SD  
503  C CE  . MET   B 32  ? 0.5298 0.4841 0.3831 0.1877  0.0482  -0.0407 41  MET   B CE  
504  N N   . GLN   B 33  ? 0.5375 0.4838 0.3712 0.1808  0.0042  -0.0417 42  GLN   B N   
505  C CA  . GLN   B 33  ? 0.5443 0.4871 0.3832 0.1775  -0.0095 -0.0466 42  GLN   B CA  
506  C C   . GLN   B 33  ? 0.5360 0.4872 0.3920 0.1566  -0.0034 -0.0482 42  GLN   B C   
507  O O   . GLN   B 33  ? 0.5443 0.4940 0.3944 0.1446  0.0066  -0.0437 42  GLN   B O   
508  C CB  . GLN   B 33  ? 0.5833 0.5087 0.4006 0.1810  -0.0204 -0.0437 42  GLN   B CB  
509  C CG  . GLN   B 33  ? 0.6476 0.5628 0.4693 0.1728  -0.0352 -0.0482 42  GLN   B CG  
510  C CD  . GLN   B 33  ? 0.7245 0.6209 0.5252 0.1862  -0.0521 -0.0499 42  GLN   B CD  
511  O OE1 . GLN   B 33  ? 0.7490 0.6278 0.5411 0.1778  -0.0610 -0.0493 42  GLN   B OE1 
512  N NE2 . GLN   B 33  ? 0.7399 0.6388 0.5302 0.2085  -0.0569 -0.0517 42  GLN   B NE2 
513  N N   . GLU   B 34  ? 0.5166 0.4798 0.3942 0.1531  -0.0089 -0.0542 43  GLU   B N   
514  C CA  . GLU   B 34  ? 0.5079 0.4855 0.4053 0.1335  -0.0028 -0.0547 43  GLU   B CA  
515  C C   . GLU   B 34  ? 0.5039 0.4956 0.4053 0.1272  0.0167  -0.0531 43  GLU   B C   
516  O O   . GLU   B 34  ? 0.5042 0.5004 0.4066 0.1108  0.0249  -0.0492 43  GLU   B O   
517  C CB  . GLU   B 34  ? 0.5443 0.5074 0.4354 0.1173  -0.0103 -0.0499 43  GLU   B CB  
518  C CG  . GLU   B 34  ? 0.6103 0.5547 0.4948 0.1242  -0.0316 -0.0531 43  GLU   B CG  
519  C CD  . GLU   B 34  ? 0.7222 0.6411 0.5887 0.1148  -0.0403 -0.0476 43  GLU   B CD  
520  O OE1 . GLU   B 34  ? 0.7331 0.6527 0.6044 0.0946  -0.0339 -0.0412 43  GLU   B OE1 
521  O OE2 . GLU   B 34  ? 0.7840 0.6822 0.6300 0.1291  -0.0535 -0.0494 43  GLU   B OE2 
522  N N   . GLY   B 35  ? 0.4943 0.4910 0.3959 0.1411  0.0231  -0.0561 44  GLY   B N   
523  C CA  . GLY   B 35  ? 0.4844 0.4908 0.3884 0.1387  0.0390  -0.0572 44  GLY   B CA  
524  C C   . GLY   B 35  ? 0.4863 0.4788 0.3692 0.1334  0.0467  -0.0517 44  GLY   B C   
525  O O   . GLY   B 35  ? 0.4791 0.4778 0.3618 0.1298  0.0587  -0.0535 44  GLY   B O   
526  N N   . VAL   B 36  ? 0.4877 0.4626 0.3524 0.1342  0.0392  -0.0458 45  VAL   B N   
527  C CA  . VAL   B 36  ? 0.4935 0.4575 0.3389 0.1297  0.0446  -0.0405 45  VAL   B CA  
528  C C   . VAL   B 36  ? 0.4895 0.4429 0.3222 0.1435  0.0407  -0.0370 45  VAL   B C   
529  O O   . VAL   B 36  ? 0.4934 0.4421 0.3231 0.1544  0.0302  -0.0361 45  VAL   B O   
530  C CB  . VAL   B 36  ? 0.5134 0.4695 0.3482 0.1167  0.0408  -0.0355 45  VAL   B CB  
531  C CG1 . VAL   B 36  ? 0.5315 0.4769 0.3451 0.1150  0.0436  -0.0302 45  VAL   B CG1 
532  C CG2 . VAL   B 36  ? 0.5111 0.4807 0.3583 0.1011  0.0480  -0.0361 45  VAL   B CG2 
533  N N   . PHE   B 37  ? 0.4801 0.4312 0.3064 0.1434  0.0490  -0.0352 46  PHE   B N   
534  C CA  . PHE   B 37  ? 0.4824 0.4268 0.2989 0.1534  0.0474  -0.0294 46  PHE   B CA  
535  C C   . PHE   B 37  ? 0.4844 0.4237 0.2846 0.1475  0.0466  -0.0237 46  PHE   B C   
536  O O   . PHE   B 37  ? 0.4816 0.4210 0.2781 0.1364  0.0530  -0.0245 46  PHE   B O   
537  C CB  . PHE   B 37  ? 0.4813 0.4250 0.3033 0.1555  0.0555  -0.0306 46  PHE   B CB  
538  C CG  . PHE   B 37  ? 0.4930 0.4312 0.3082 0.1643  0.0542  -0.0224 46  PHE   B CG  
539  C CD1 . PHE   B 37  ? 0.4978 0.4367 0.3130 0.1790  0.0482  -0.0187 46  PHE   B CD1 
540  C CD2 . PHE   B 37  ? 0.5030 0.4371 0.3122 0.1576  0.0590  -0.0179 46  PHE   B CD2 
541  C CE1 . PHE   B 37  ? 0.5028 0.4397 0.3117 0.1869  0.0487  -0.0089 46  PHE   B CE1 
542  C CE2 . PHE   B 37  ? 0.5106 0.4428 0.3163 0.1637  0.0586  -0.0083 46  PHE   B CE2 
543  C CZ  . PHE   B 37  ? 0.5033 0.4374 0.3087 0.1782  0.0543  -0.0030 46  PHE   B CZ  
544  N N   . HIS   B 38  ? 0.4836 0.4197 0.2732 0.1567  0.0381  -0.0188 47  HIS   B N   
545  C CA  . HIS   B 38  ? 0.4891 0.4222 0.2628 0.1550  0.0352  -0.0136 47  HIS   B CA  
546  C C   . HIS   B 38  ? 0.4984 0.4368 0.2670 0.1630  0.0373  -0.0064 47  HIS   B C   
547  O O   . HIS   B 38  ? 0.4957 0.4371 0.2647 0.1765  0.0341  -0.0033 47  HIS   B O   
548  C CB  . HIS   B 38  ? 0.4921 0.4183 0.2565 0.1626  0.0226  -0.0140 47  HIS   B CB  
549  C CG  . HIS   B 38  ? 0.5004 0.4214 0.2730 0.1547  0.0182  -0.0196 47  HIS   B CG  
550  N ND1 . HIS   B 38  ? 0.5093 0.4352 0.2981 0.1575  0.0171  -0.0248 47  HIS   B ND1 
551  C CD2 . HIS   B 38  ? 0.5140 0.4262 0.2811 0.1441  0.0140  -0.0195 47  HIS   B CD2 
552  C CE1 . HIS   B 38  ? 0.5129 0.4358 0.3082 0.1471  0.0129  -0.0278 47  HIS   B CE1 
553  N NE2 . HIS   B 38  ? 0.5207 0.4339 0.3030 0.1380  0.0112  -0.0240 47  HIS   B NE2 
554  N N   . THR   B 39  ? 0.5014 0.4428 0.2650 0.1550  0.0421  -0.0029 48  THR   B N   
555  C CA  . THR   B 39  ? 0.5098 0.4599 0.2714 0.1602  0.0439  0.0056  48  THR   B CA  
556  C C   . THR   B 39  ? 0.5206 0.4767 0.2712 0.1553  0.0426  0.0090  48  THR   B C   
557  O O   . THR   B 39  ? 0.5222 0.4725 0.2639 0.1508  0.0391  0.0053  48  THR   B O   
558  C CB  . THR   B 39  ? 0.5124 0.4616 0.2869 0.1556  0.0516  0.0069  48  THR   B CB  
559  O OG1 . THR   B 39  ? 0.5183 0.4766 0.2930 0.1613  0.0527  0.0178  48  THR   B OG1 
560  C CG2 . THR   B 39  ? 0.5081 0.4528 0.2861 0.1401  0.0572  0.0014  48  THR   B CG2 
561  N N   . MET   B 40  ? 0.5226 0.4912 0.2741 0.1565  0.0448  0.0171  49  MET   B N   
562  C CA  . MET   B 40  ? 0.5326 0.5109 0.2765 0.1522  0.0434  0.0200  49  MET   B CA  
563  C C   . MET   B 40  ? 0.5431 0.5196 0.2944 0.1352  0.0489  0.0168  49  MET   B C   
564  O O   . MET   B 40  ? 0.5528 0.5259 0.3162 0.1298  0.0538  0.0172  49  MET   B O   
565  C CB  . MET   B 40  ? 0.5392 0.5376 0.2819 0.1633  0.0423  0.0306  49  MET   B CB  
566  C CG  . MET   B 40  ? 0.5653 0.5652 0.2980 0.1833  0.0361  0.0321  49  MET   B CG  
567  S SD  . MET   B 40  ? 0.6272 0.6490 0.3455 0.1997  0.0303  0.0385  49  MET   B SD  
568  C CE  . MET   B 40  ? 0.6000 0.6050 0.3026 0.1961  0.0219  0.0293  49  MET   B CE  
569  N N   . TRP   B 41  ? 0.5416 0.5181 0.2839 0.1279  0.0470  0.0131  50  TRP   B N   
570  C CA  A TRP   B 41  ? 0.5482 0.5227 0.2942 0.1133  0.0505  0.0080  50  TRP   B CA  
571  C CA  B TRP   B 41  ? 0.5437 0.5183 0.2894 0.1134  0.0504  0.0081  50  TRP   B CA  
572  C C   . TRP   B 41  ? 0.5447 0.5296 0.3031 0.1073  0.0523  0.0134  50  TRP   B C   
573  O O   . TRP   B 41  ? 0.5445 0.5207 0.3110 0.0971  0.0552  0.0084  50  TRP   B O   
574  C CB  A TRP   B 41  ? 0.5561 0.5312 0.2874 0.1089  0.0471  0.0045  50  TRP   B CB  
575  C CB  B TRP   B 41  ? 0.5447 0.5208 0.2757 0.1094  0.0468  0.0050  50  TRP   B CB  
576  C CG  A TRP   B 41  ? 0.5662 0.5357 0.2972 0.0960  0.0505  -0.0038 50  TRP   B CG  
577  C CG  B TRP   B 41  ? 0.5441 0.5188 0.2755 0.0962  0.0491  -0.0016 50  TRP   B CG  
578  C CD1 A TRP   B 41  ? 0.5845 0.5426 0.3113 0.0914  0.0545  -0.0115 50  TRP   B CD1 
579  C CD1 B TRP   B 41  ? 0.5476 0.5334 0.2841 0.0892  0.0473  -0.0006 50  TRP   B CD1 
580  C CD2 A TRP   B 41  ? 0.5660 0.5424 0.3010 0.0867  0.0498  -0.0058 50  TRP   B CD2 
581  C CD2 B TRP   B 41  ? 0.5484 0.5113 0.2754 0.0891  0.0531  -0.0109 50  TRP   B CD2 
582  N NE1 A TRP   B 41  ? 0.5918 0.5490 0.3169 0.0820  0.0566  -0.0189 50  TRP   B NE1 
583  N NE1 B TRP   B 41  ? 0.5549 0.5333 0.2889 0.0788  0.0487  -0.0102 50  TRP   B NE1 
584  C CE2 A TRP   B 41  ? 0.5830 0.5494 0.3133 0.0785  0.0527  -0.0163 50  TRP   B CE2 
585  C CE2 B TRP   B 41  ? 0.5563 0.5217 0.2832 0.0796  0.0529  -0.0166 50  TRP   B CE2 
586  C CE3 A TRP   B 41  ? 0.5653 0.5574 0.3082 0.0842  0.0465  0.0002  50  TRP   B CE3 
587  C CE3 B TRP   B 41  ? 0.5581 0.5110 0.2818 0.0898  0.0567  -0.0149 50  TRP   B CE3 
588  C CZ2 A TRP   B 41  ? 0.5898 0.5577 0.3211 0.0691  0.0509  -0.0226 50  TRP   B CZ2 
589  C CZ2 B TRP   B 41  ? 0.5624 0.5199 0.2829 0.0733  0.0565  -0.0268 50  TRP   B CZ2 
590  C CZ3 A TRP   B 41  ? 0.5755 0.5699 0.3228 0.0724  0.0447  -0.0050 50  TRP   B CZ3 
591  C CZ3 B TRP   B 41  ? 0.5680 0.5166 0.2876 0.0824  0.0616  -0.0234 50  TRP   B CZ3 
592  C CH2 A TRP   B 41  ? 0.5850 0.5658 0.3252 0.0655  0.0460  -0.0171 50  TRP   B CH2 
593  C CH2 B TRP   B 41  ? 0.5659 0.5165 0.2824 0.0755  0.0617  -0.0296 50  TRP   B CH2 
594  N N   . HIS   B 42  ? 0.5441 0.5479 0.3044 0.1133  0.0501  0.0237  51  HIS   B N   
595  C CA  . HIS   B 42  ? 0.5460 0.5624 0.3210 0.1048  0.0518  0.0312  51  HIS   B CA  
596  C C   . HIS   B 42  ? 0.5577 0.5642 0.3459 0.1034  0.0565  0.0357  51  HIS   B C   
597  O O   . HIS   B 42  ? 0.5548 0.5646 0.3563 0.0929  0.0577  0.0416  51  HIS   B O   
598  C CB  . HIS   B 42  ? 0.5435 0.5886 0.3189 0.1115  0.0494  0.0421  51  HIS   B CB  
599  C CG  . HIS   B 42  ? 0.5625 0.6186 0.3379 0.1273  0.0512  0.0525  51  HIS   B CG  
600  N ND1 . HIS   B 42  ? 0.5898 0.6484 0.3496 0.1451  0.0471  0.0513  51  HIS   B ND1 
601  C CD2 . HIS   B 42  ? 0.5691 0.6335 0.3567 0.1283  0.0560  0.0640  51  HIS   B CD2 
602  C CE1 . HIS   B 42  ? 0.5918 0.6610 0.3540 0.1575  0.0495  0.0606  51  HIS   B CE1 
603  N NE2 . HIS   B 42  ? 0.5863 0.6602 0.3648 0.1479  0.0556  0.0694  51  HIS   B NE2 
604  N N   . VAL   B 43  ? 0.5681 0.5617 0.3531 0.1135  0.0582  0.0334  52  VAL   B N   
605  C CA  . VAL   B 43  ? 0.5791 0.5618 0.3742 0.1148  0.0619  0.0374  52  VAL   B CA  
606  C C   . VAL   B 43  ? 0.5884 0.5497 0.3893 0.1033  0.0634  0.0269  52  VAL   B C   
607  O O   . VAL   B 43  ? 0.5872 0.5418 0.3986 0.0944  0.0642  0.0310  52  VAL   B O   
608  C CB  . VAL   B 43  ? 0.5998 0.5790 0.3893 0.1316  0.0617  0.0378  52  VAL   B CB  
609  C CG1 . VAL   B 43  ? 0.6105 0.5756 0.4087 0.1340  0.0648  0.0398  52  VAL   B CG1 
610  C CG2 . VAL   B 43  ? 0.6041 0.6039 0.3866 0.1456  0.0595  0.0480  52  VAL   B CG2 
611  N N   . THR   B 44  ? 0.5926 0.5438 0.3859 0.1030  0.0633  0.0136  53  THR   B N   
612  C CA  . THR   B 44  ? 0.5976 0.5311 0.3937 0.0963  0.0652  0.0017  53  THR   B CA  
613  C C   . THR   B 44  ? 0.6019 0.5341 0.3928 0.0845  0.0636  -0.0075 53  THR   B C   
614  O O   . THR   B 44  ? 0.6135 0.5312 0.4060 0.0795  0.0643  -0.0177 53  THR   B O   
615  C CB  . THR   B 44  ? 0.6158 0.5428 0.4091 0.1049  0.0675  -0.0065 53  THR   B CB  
616  O OG1 . THR   B 44  ? 0.6313 0.5647 0.4140 0.1035  0.0669  -0.0117 53  THR   B OG1 
617  C CG2 . THR   B 44  ? 0.6146 0.5439 0.4113 0.1183  0.0672  0.0009  53  THR   B CG2 
618  N N   . LYS   B 45  ? 0.5888 0.5357 0.3717 0.0821  0.0607  -0.0052 54  LYS   B N   
619  C CA  . LYS   B 45  ? 0.5918 0.5401 0.3666 0.0726  0.0582  -0.0137 54  LYS   B CA  
620  C C   . LYS   B 45  ? 0.5902 0.5285 0.3546 0.0729  0.0614  -0.0267 54  LYS   B C   
621  O O   . LYS   B 45  ? 0.5864 0.5223 0.3438 0.0661  0.0602  -0.0359 54  LYS   B O   
622  C CB  . LYS   B 45  ? 0.6133 0.5578 0.3977 0.0607  0.0547  -0.0151 54  LYS   B CB  
623  C CG  . LYS   B 45  ? 0.6550 0.6108 0.4534 0.0580  0.0530  -0.0002 54  LYS   B CG  
624  C CD  . LYS   B 45  ? 0.7049 0.6843 0.5027 0.0536  0.0485  0.0054  54  LYS   B CD  
625  C CE  . LYS   B 45  ? 0.7549 0.7428 0.5711 0.0420  0.0457  0.0151  54  LYS   B CE  
626  N NZ  . LYS   B 45  ? 0.7927 0.7807 0.6200 0.0468  0.0504  0.0294  54  LYS   B NZ  
627  N N   . GLY   B 46  ? 0.5899 0.5250 0.3540 0.0808  0.0654  -0.0273 55  GLY   B N   
628  C CA  . GLY   B 46  ? 0.5985 0.5293 0.3562 0.0809  0.0700  -0.0376 55  GLY   B CA  
629  C C   . GLY   B 46  ? 0.6050 0.5242 0.3700 0.0817  0.0735  -0.0476 55  GLY   B C   
630  O O   . GLY   B 46  ? 0.6081 0.5274 0.3683 0.0826  0.0782  -0.0570 55  GLY   B O   
631  N N   . ALA   B 47  ? 0.6082 0.5175 0.3841 0.0819  0.0713  -0.0453 56  ALA   B N   
632  C CA  . ALA   B 47  ? 0.6221 0.5160 0.4038 0.0847  0.0729  -0.0548 56  ALA   B CA  
633  C C   . ALA   B 47  ? 0.6303 0.5250 0.4184 0.0957  0.0775  -0.0557 56  ALA   B C   
634  O O   . ALA   B 47  ? 0.6312 0.5337 0.4232 0.1007  0.0773  -0.0461 56  ALA   B O   
635  C CB  . ALA   B 47  ? 0.6261 0.5062 0.4174 0.0807  0.0681  -0.0495 56  ALA   B CB  
636  N N   . ALA   B 48  ? 0.6327 0.5207 0.4220 0.1009  0.0808  -0.0679 57  ALA   B N   
637  C CA  . ALA   B 48  ? 0.6348 0.5268 0.4324 0.1118  0.0846  -0.0699 57  ALA   B CA  
638  C C   . ALA   B 48  ? 0.6410 0.5227 0.4486 0.1188  0.0813  -0.0609 57  ALA   B C   
639  O O   . ALA   B 48  ? 0.6529 0.5193 0.4618 0.1153  0.0773  -0.0565 57  ALA   B O   
640  C CB  . ALA   B 48  ? 0.6334 0.5223 0.4300 0.1177  0.0887  -0.0856 57  ALA   B CB  
641  N N   . LEU   B 49  ? 0.6339 0.5245 0.4485 0.1280  0.0823  -0.0574 58  LEU   B N   
642  C CA  . LEU   B 49  ? 0.6373 0.5198 0.4590 0.1370  0.0793  -0.0486 58  LEU   B CA  
643  C C   . LEU   B 49  ? 0.6533 0.5308 0.4826 0.1496  0.0805  -0.0572 58  LEU   B C   
644  O O   . LEU   B 49  ? 0.6544 0.5414 0.4855 0.1520  0.0845  -0.0690 58  LEU   B O   
645  C CB  . LEU   B 49  ? 0.6238 0.5197 0.4457 0.1403  0.0770  -0.0376 58  LEU   B CB  
646  C CG  . LEU   B 49  ? 0.6288 0.5320 0.4425 0.1311  0.0752  -0.0298 58  LEU   B CG  
647  C CD1 . LEU   B 49  ? 0.6252 0.5401 0.4368 0.1373  0.0719  -0.0226 58  LEU   B CD1 
648  C CD2 . LEU   B 49  ? 0.6371 0.5316 0.4501 0.1254  0.0734  -0.0212 58  LEU   B CD2 
649  N N   . ARG   B 50  ? 0.6658 0.5300 0.4992 0.1585  0.0774  -0.0507 59  ARG   B N   
650  C CA  . ARG   B 50  ? 0.6845 0.5425 0.5243 0.1729  0.0773  -0.0583 59  ARG   B CA  
651  C C   . ARG   B 50  ? 0.6943 0.5601 0.5394 0.1850  0.0745  -0.0497 59  ARG   B C   
652  O O   . ARG   B 50  ? 0.6980 0.5635 0.5397 0.1836  0.0720  -0.0360 59  ARG   B O   
653  C CB  . ARG   B 50  ? 0.7174 0.5455 0.5543 0.1741  0.0746  -0.0603 59  ARG   B CB  
654  C CG  . ARG   B 50  ? 0.7774 0.5921 0.6187 0.1913  0.0722  -0.0631 59  ARG   B CG  
655  C CD  . ARG   B 50  ? 0.8499 0.6301 0.6866 0.1921  0.0681  -0.0668 59  ARG   B CD  
656  N NE  . ARG   B 50  ? 0.9084 0.6693 0.7420 0.1789  0.0645  -0.0519 59  ARG   B NE  
657  C CZ  . ARG   B 50  ? 0.9579 0.7065 0.7925 0.1819  0.0618  -0.0348 59  ARG   B CZ  
658  N NH1 . ARG   B 50  ? 0.9507 0.7035 0.7875 0.1989  0.0615  -0.0310 59  ARG   B NH1 
659  N NH2 . ARG   B 50  ? 0.9746 0.7098 0.8085 0.1678  0.0596  -0.0206 59  ARG   B NH2 
660  N N   . SER   B 51  ? 0.6967 0.5731 0.5502 0.1974  0.0746  -0.0580 60  SER   B N   
661  C CA  . SER   B 51  ? 0.7110 0.5947 0.5695 0.2107  0.0702  -0.0520 60  SER   B CA  
662  C C   . SER   B 51  ? 0.7337 0.6113 0.5988 0.2269  0.0691  -0.0605 60  SER   B C   
663  O O   . SER   B 51  ? 0.7223 0.6195 0.5978 0.2331  0.0704  -0.0717 60  SER   B O   
664  C CB  . SER   B 51  ? 0.7140 0.6238 0.5784 0.2085  0.0693  -0.0542 60  SER   B CB  
665  O OG  . SER   B 51  ? 0.7423 0.6580 0.6099 0.2215  0.0630  -0.0493 60  SER   B OG  
666  N N   . GLY   B 52  ? 0.7593 0.6099 0.6186 0.2332  0.0667  -0.0550 61  GLY   B N   
667  C CA  . GLY   B 52  ? 0.7800 0.6188 0.6426 0.2500  0.0645  -0.0631 61  GLY   B CA  
668  C C   . GLY   B 52  ? 0.8010 0.6362 0.6640 0.2473  0.0683  -0.0793 61  GLY   B C   
669  O O   . GLY   B 52  ? 0.8176 0.6379 0.6728 0.2337  0.0698  -0.0794 61  GLY   B O   
670  N N   . GLU   B 53  ? 0.7951 0.6475 0.6671 0.2602  0.0699  -0.0936 62  GLU   B N   
671  C CA  . GLU   B 53  ? 0.8041 0.6593 0.6753 0.2604  0.0746  -0.1101 62  GLU   B CA  
672  C C   . GLU   B 53  ? 0.7937 0.6768 0.6669 0.2439  0.0819  -0.1140 62  GLU   B C   
673  O O   . GLU   B 53  ? 0.7965 0.6797 0.6642 0.2406  0.0863  -0.1252 62  GLU   B O   
674  C CB  . GLU   B 53  ? 0.8404 0.7085 0.7210 0.2822  0.0744  -0.1237 62  GLU   B CB  
675  C CG  . GLU   B 53  ? 0.9419 0.7733 0.8139 0.2985  0.0684  -0.1286 62  GLU   B CG  
676  C CD  . GLU   B 53  ? 1.0480 0.8935 0.9292 0.3235  0.0670  -0.1409 62  GLU   B CD  
677  O OE1 . GLU   B 53  ? 1.0508 0.9316 0.9471 0.3286  0.0680  -0.1402 62  GLU   B OE1 
678  O OE2 . GLU   B 53  ? 1.0974 0.9185 0.9709 0.3385  0.0637  -0.1518 62  GLU   B OE2 
679  N N   . GLY   B 54  ? 0.7797 0.6843 0.6590 0.2350  0.0824  -0.1048 63  GLY   B N   
680  C CA  . GLY   B 54  ? 0.7704 0.6993 0.6513 0.2196  0.0882  -0.1058 63  GLY   B CA  
681  C C   . GLY   B 54  ? 0.7732 0.6886 0.6403 0.2021  0.0890  -0.0990 63  GLY   B C   
682  O O   . GLY   B 54  ? 0.7907 0.6831 0.6502 0.1991  0.0844  -0.0893 63  GLY   B O   
683  N N   . ARG   B 55  ? 0.7485 0.6812 0.6132 0.1906  0.0951  -0.1032 64  ARG   B N   
684  C CA  . ARG   B 55  ? 0.7392 0.6637 0.5907 0.1748  0.0957  -0.0982 64  ARG   B CA  
685  C C   . ARG   B 55  ? 0.7122 0.6555 0.5648 0.1633  0.0965  -0.0895 64  ARG   B C   
686  O O   . ARG   B 55  ? 0.7012 0.6675 0.5643 0.1638  0.0992  -0.0913 64  ARG   B O   
687  C CB  . ARG   B 55  ? 0.7533 0.6776 0.5956 0.1725  0.1011  -0.1109 64  ARG   B CB  
688  C CG  . ARG   B 55  ? 0.7950 0.7052 0.6224 0.1589  0.0995  -0.1082 64  ARG   B CG  
689  C CD  . ARG   B 55  ? 0.8372 0.7496 0.6540 0.1588  0.1041  -0.1224 64  ARG   B CD  
690  N NE  . ARG   B 55  ? 0.8810 0.7842 0.6835 0.1456  0.1019  -0.1206 64  ARG   B NE  
691  C CZ  . ARG   B 55  ? 0.9179 0.8001 0.7097 0.1450  0.0976  -0.1298 64  ARG   B CZ  
692  N NH1 . ARG   B 55  ? 0.9199 0.7843 0.7122 0.1572  0.0949  -0.1414 64  ARG   B NH1 
693  N NH2 . ARG   B 55  ? 0.9152 0.7930 0.6954 0.1327  0.0947  -0.1283 64  ARG   B NH2 
694  N N   . LEU   B 56  ? 0.6984 0.6316 0.5405 0.1530  0.0934  -0.0802 65  LEU   B N   
695  C CA  . LEU   B 56  ? 0.6805 0.6255 0.5198 0.1432  0.0924  -0.0723 65  LEU   B CA  
696  C C   . LEU   B 56  ? 0.6753 0.6169 0.5001 0.1312  0.0949  -0.0725 65  LEU   B C   
697  O O   . LEU   B 56  ? 0.6848 0.6113 0.5018 0.1281  0.0917  -0.0693 65  LEU   B O   
698  C CB  . LEU   B 56  ? 0.6826 0.6200 0.5208 0.1457  0.0849  -0.0604 65  LEU   B CB  
699  C CG  . LEU   B 56  ? 0.6958 0.6315 0.5438 0.1595  0.0805  -0.0585 65  LEU   B CG  
700  C CD1 . LEU   B 56  ? 0.7062 0.6373 0.5489 0.1622  0.0740  -0.0468 65  LEU   B CD1 
701  C CD2 . LEU   B 56  ? 0.6926 0.6472 0.5544 0.1641  0.0809  -0.0647 65  LEU   B CD2 
702  N N   . ASP   B 57  ? 0.6588 0.6158 0.4806 0.1243  0.1005  -0.0757 66  ASP   B N   
703  C CA  . ASP   B 57  ? 0.6571 0.6123 0.4630 0.1144  0.1026  -0.0763 66  ASP   B CA  
704  C C   . ASP   B 57  ? 0.6413 0.5989 0.4395 0.1055  0.0991  -0.0653 66  ASP   B C   
705  O O   . ASP   B 57  ? 0.6372 0.6034 0.4422 0.1045  0.0978  -0.0602 66  ASP   B O   
706  C CB  . ASP   B 57  ? 0.6828 0.6534 0.4862 0.1138  0.1117  -0.0860 66  ASP   B CB  
707  C CG  . ASP   B 57  ? 0.7671 0.7341 0.5750 0.1252  0.1143  -0.0990 66  ASP   B CG  
708  O OD1 . ASP   B 57  ? 0.7911 0.7362 0.5960 0.1289  0.1088  -0.1017 66  ASP   B OD1 
709  O OD2 . ASP   B 57  ? 0.7944 0.7808 0.6089 0.1305  0.1217  -0.1063 66  ASP   B OD2 
710  N N   . PRO   B 58  ? 0.6296 0.5789 0.4137 0.0994  0.0961  -0.0621 67  PRO   B N   
711  C CA  . PRO   B 58  ? 0.6206 0.5708 0.3953 0.0934  0.0918  -0.0523 67  PRO   B CA  
712  C C   . PRO   B 58  ? 0.6106 0.5720 0.3808 0.0866  0.0963  -0.0507 67  PRO   B C   
713  O O   . PRO   B 58  ? 0.6131 0.5845 0.3824 0.0846  0.1043  -0.0572 67  PRO   B O   
714  C CB  . PRO   B 58  ? 0.6361 0.5793 0.3974 0.0889  0.0888  -0.0518 67  PRO   B CB  
715  C CG  . PRO   B 58  ? 0.6452 0.5853 0.4061 0.0894  0.0929  -0.0634 67  PRO   B CG  
716  C CD  . PRO   B 58  ? 0.6250 0.5635 0.4014 0.0980  0.0952  -0.0679 67  PRO   B CD  
717  N N   . TYR   B 59  ? 0.5969 0.5567 0.3642 0.0835  0.0910  -0.0416 68  TYR   B N   
718  C CA  . TYR   B 59  ? 0.5796 0.5469 0.3435 0.0750  0.0941  -0.0373 68  TYR   B CA  
719  C C   . TYR   B 59  ? 0.5819 0.5396 0.3260 0.0698  0.0887  -0.0291 68  TYR   B C   
720  O O   . TYR   B 59  ? 0.5840 0.5455 0.3156 0.0623  0.0933  -0.0266 68  TYR   B O   
721  C CB  . TYR   B 59  ? 0.5608 0.5325 0.3417 0.0754  0.0911  -0.0346 68  TYR   B CB  
722  C CG  . TYR   B 59  ? 0.5506 0.5297 0.3319 0.0639  0.0935  -0.0283 68  TYR   B CG  
723  C CD1 . TYR   B 59  ? 0.5670 0.5326 0.3346 0.0578  0.0860  -0.0187 68  TYR   B CD1 
724  C CD2 . TYR   B 59  ? 0.5356 0.5351 0.3327 0.0596  0.1023  -0.0308 68  TYR   B CD2 
725  C CE1 . TYR   B 59  ? 0.5703 0.5391 0.3382 0.0454  0.0875  -0.0109 68  TYR   B CE1 
726  C CE2 . TYR   B 59  ? 0.5385 0.5467 0.3387 0.0469  0.1048  -0.0226 68  TYR   B CE2 
727  C CZ  . TYR   B 59  ? 0.5584 0.5492 0.3438 0.0388  0.0972  -0.0120 68  TYR   B CZ  
728  O OH  . TYR   B 59  ? 0.5610 0.5570 0.3492 0.0244  0.0990  -0.0020 68  TYR   B OH  
729  N N   . TRP   B 60  ? 0.5803 0.5268 0.3206 0.0752  0.0788  -0.0246 69  TRP   B N   
730  C CA  . TRP   B 60  ? 0.5918 0.5292 0.3133 0.0739  0.0719  -0.0175 69  TRP   B CA  
731  C C   . TRP   B 60  ? 0.5958 0.5303 0.3144 0.0821  0.0659  -0.0174 69  TRP   B C   
732  O O   . TRP   B 60  ? 0.5910 0.5264 0.3220 0.0891  0.0646  -0.0190 69  TRP   B O   
733  C CB  . TRP   B 60  ? 0.5970 0.5245 0.3164 0.0726  0.0639  -0.0102 69  TRP   B CB  
734  C CG  . TRP   B 60  ? 0.6145 0.5292 0.3141 0.0759  0.0542  -0.0037 69  TRP   B CG  
735  C CD1 . TRP   B 60  ? 0.6343 0.5437 0.3145 0.0702  0.0539  0.0014  69  TRP   B CD1 
736  C CD2 . TRP   B 60  ? 0.6147 0.5227 0.3106 0.0880  0.0438  -0.0021 69  TRP   B CD2 
737  N NE1 . TRP   B 60  ? 0.6468 0.5454 0.3121 0.0784  0.0430  0.0055  69  TRP   B NE1 
738  C CE2 . TRP   B 60  ? 0.6363 0.5355 0.3111 0.0897  0.0371  0.0032  69  TRP   B CE2 
739  C CE3 . TRP   B 60  ? 0.6099 0.5201 0.3169 0.0989  0.0398  -0.0044 69  TRP   B CE3 
740  C CZ2 . TRP   B 60  ? 0.6454 0.5399 0.3113 0.1027  0.0267  0.0053  69  TRP   B CZ2 
741  C CZ3 . TRP   B 60  ? 0.6231 0.5292 0.3205 0.1111  0.0303  -0.0013 69  TRP   B CZ3 
742  C CH2 . TRP   B 60  ? 0.6358 0.5348 0.3133 0.1133  0.0238  0.0030  69  TRP   B CH2 
743  N N   . GLY   B 61  ? 0.6042 0.5368 0.3064 0.0814  0.0624  -0.0144 70  GLY   B N   
744  C CA  . GLY   B 61  ? 0.6098 0.5449 0.3102 0.0879  0.0569  -0.0128 70  GLY   B CA  
745  C C   . GLY   B 61  ? 0.6183 0.5525 0.2995 0.0881  0.0511  -0.0084 70  GLY   B C   
746  O O   . GLY   B 61  ? 0.6275 0.5590 0.2954 0.0818  0.0530  -0.0081 70  GLY   B O   
747  N N   . ASP   B 62  ? 0.6146 0.5532 0.2938 0.0965  0.0440  -0.0045 71  ASP   B N   
748  C CA  . ASP   B 62  ? 0.6219 0.5625 0.2837 0.0999  0.0371  -0.0007 71  ASP   B CA  
749  C C   . ASP   B 62  ? 0.6098 0.5658 0.2792 0.1071  0.0336  0.0015  71  ASP   B C   
750  O O   . ASP   B 62  ? 0.6035 0.5617 0.2803 0.1164  0.0313  0.0048  71  ASP   B O   
751  C CB  . ASP   B 62  ? 0.6596 0.5855 0.3068 0.1064  0.0292  0.0048  71  ASP   B CB  
752  C CG  . ASP   B 62  ? 0.7342 0.6581 0.3600 0.1115  0.0211  0.0088  71  ASP   B CG  
753  O OD1 . ASP   B 62  ? 0.7385 0.6749 0.3634 0.1213  0.0158  0.0102  71  ASP   B OD1 
754  O OD2 . ASP   B 62  ? 0.7867 0.6974 0.3966 0.1066  0.0200  0.0115  71  ASP   B OD2 
755  N N   . VAL   B 63  ? 0.6017 0.5702 0.2696 0.1029  0.0330  0.0001  72  VAL   B N   
756  C CA  . VAL   B 63  ? 0.5886 0.5766 0.2667 0.1064  0.0303  0.0033  72  VAL   B CA  
757  C C   . VAL   B 63  ? 0.5897 0.5861 0.2580 0.1212  0.0222  0.0099  72  VAL   B C   
758  O O   . VAL   B 63  ? 0.5899 0.6019 0.2688 0.1288  0.0216  0.0149  72  VAL   B O   
759  C CB  . VAL   B 63  ? 0.5897 0.5883 0.2702 0.0957  0.0304  -0.0015 72  VAL   B CB  
760  C CG1 . VAL   B 63  ? 0.5849 0.6079 0.2733 0.0985  0.0252  0.0034  72  VAL   B CG1 
761  C CG2 . VAL   B 63  ? 0.5878 0.5796 0.2822 0.0846  0.0372  -0.0084 72  VAL   B CG2 
762  N N   . LYS   B 64  ? 0.5918 0.5770 0.2391 0.1267  0.0161  0.0106  73  LYS   B N   
763  C CA  . LYS   B 64  ? 0.5920 0.5820 0.2274 0.1435  0.0069  0.0153  73  LYS   B CA  
764  C C   . LYS   B 64  ? 0.5930 0.5732 0.2301 0.1551  0.0048  0.0172  73  LYS   B C   
765  O O   . LYS   B 64  ? 0.5813 0.5774 0.2214 0.1691  0.0017  0.0206  73  LYS   B O   
766  C CB  . LYS   B 64  ? 0.6293 0.6058 0.2399 0.1467  -0.0005 0.0158  73  LYS   B CB  
767  C CG  . LYS   B 64  ? 0.6779 0.6649 0.2762 0.1654  -0.0109 0.0192  73  LYS   B CG  
768  C CD  . LYS   B 64  ? 0.7571 0.7313 0.3304 0.1681  -0.0185 0.0200  73  LYS   B CD  
769  C CE  . LYS   B 64  ? 0.8185 0.8071 0.3803 0.1880  -0.0290 0.0223  73  LYS   B CE  
770  N NZ  . LYS   B 64  ? 0.8805 0.8396 0.4134 0.1988  -0.0399 0.0243  73  LYS   B NZ  
771  N N   . GLN   B 65  ? 0.6011 0.5580 0.2372 0.1498  0.0065  0.0149  74  GLN   B N   
772  C CA  . GLN   B 65  ? 0.6027 0.5501 0.2421 0.1599  0.0034  0.0150  74  GLN   B CA  
773  C C   . GLN   B 65  ? 0.5869 0.5524 0.2468 0.1612  0.0103  0.0160  74  GLN   B C   
774  O O   . GLN   B 65  ? 0.5880 0.5571 0.2489 0.1754  0.0069  0.0177  74  GLN   B O   
775  C CB  . GLN   B 65  ? 0.6307 0.5534 0.2696 0.1508  0.0039  0.0123  74  GLN   B CB  
776  C CG  . GLN   B 65  ? 0.6813 0.5824 0.2998 0.1479  -0.0029 0.0140  74  GLN   B CG  
777  C CD  . GLN   B 65  ? 0.7422 0.6217 0.3633 0.1386  -0.0032 0.0134  74  GLN   B CD  
778  O OE1 . GLN   B 65  ? 0.7487 0.6234 0.3804 0.1426  -0.0055 0.0110  74  GLN   B OE1 
779  N NE2 . GLN   B 65  ? 0.7583 0.6257 0.3698 0.1260  -0.0012 0.0163  74  GLN   B NE2 
780  N N   . ASP   B 66  ? 0.5738 0.5490 0.2483 0.1472  0.0194  0.0150  75  ASP   B N   
781  C CA  . ASP   B 66  ? 0.5630 0.5503 0.2571 0.1442  0.0265  0.0167  75  ASP   B CA  
782  C C   . ASP   B 66  ? 0.5607 0.5339 0.2621 0.1454  0.0290  0.0140  75  ASP   B C   
783  O O   . ASP   B 66  ? 0.5600 0.5400 0.2703 0.1532  0.0304  0.0174  75  ASP   B O   
784  C CB  . ASP   B 66  ? 0.5713 0.5833 0.2704 0.1555  0.0253  0.0244  75  ASP   B CB  
785  C CG  . ASP   B 66  ? 0.6134 0.6366 0.3326 0.1489  0.0331  0.0287  75  ASP   B CG  
786  O OD1 . ASP   B 66  ? 0.6186 0.6363 0.3473 0.1336  0.0378  0.0252  75  ASP   B OD1 
787  O OD2 . ASP   B 66  ? 0.6522 0.6879 0.3761 0.1602  0.0339  0.0357  75  ASP   B OD2 
788  N N   . LEU   B 67  ? 0.5575 0.5133 0.2556 0.1376  0.0297  0.0086  76  LEU   B N   
789  C CA  . LEU   B 67  ? 0.5526 0.4981 0.2600 0.1378  0.0314  0.0053  76  LEU   B CA  
790  C C   . LEU   B 67  ? 0.5439 0.4847 0.2599 0.1234  0.0397  -0.0004 76  LEU   B C   
791  O O   . LEU   B 67  ? 0.5430 0.4830 0.2518 0.1139  0.0422  -0.0023 76  LEU   B O   
792  C CB  . LEU   B 67  ? 0.5624 0.4929 0.2589 0.1446  0.0223  0.0045  76  LEU   B CB  
793  C CG  . LEU   B 67  ? 0.5798 0.5116 0.2650 0.1626  0.0123  0.0075  76  LEU   B CG  
794  C CD1 . LEU   B 67  ? 0.5933 0.5042 0.2662 0.1664  0.0015  0.0052  76  LEU   B CD1 
795  C CD2 . LEU   B 67  ? 0.5831 0.5259 0.2781 0.1747  0.0134  0.0092  76  LEU   B CD2 
796  N N   . VAL   B 68  ? 0.5300 0.4689 0.2601 0.1236  0.0438  -0.0035 77  VAL   B N   
797  C CA  . VAL   B 68  ? 0.5214 0.4584 0.2601 0.1131  0.0518  -0.0100 77  VAL   B CA  
798  C C   . VAL   B 68  ? 0.5130 0.4471 0.2637 0.1163  0.0522  -0.0133 77  VAL   B C   
799  O O   . VAL   B 68  ? 0.5129 0.4473 0.2689 0.1268  0.0482  -0.0114 77  VAL   B O   
800  C CB  . VAL   B 68  ? 0.5208 0.4625 0.2665 0.1082  0.0579  -0.0124 77  VAL   B CB  
801  C CG1 . VAL   B 68  ? 0.5211 0.4661 0.2767 0.1161  0.0572  -0.0076 77  VAL   B CG1 
802  C CG2 . VAL   B 68  ? 0.5208 0.4601 0.2732 0.1010  0.0654  -0.0210 77  VAL   B CG2 
803  N N   . SER   B 69  ? 0.5046 0.4382 0.2591 0.1079  0.0566  -0.0178 78  SER   B N   
804  C CA  . SER   B 69  ? 0.4972 0.4328 0.2665 0.1097  0.0572  -0.0215 78  SER   B CA  
805  C C   . SER   B 69  ? 0.4888 0.4318 0.2693 0.1054  0.0674  -0.0286 78  SER   B C   
806  O O   . SER   B 69  ? 0.4894 0.4342 0.2635 0.0985  0.0735  -0.0312 78  SER   B O   
807  C CB  . SER   B 69  ? 0.4988 0.4304 0.2663 0.1044  0.0521  -0.0198 78  SER   B CB  
808  O OG  . SER   B 69  ? 0.4969 0.4310 0.2592 0.0917  0.0584  -0.0193 78  SER   B OG  
809  N N   . TYR   B 70  ? 0.4835 0.4306 0.2794 0.1117  0.0682  -0.0326 79  TYR   B N   
810  C CA  . TYR   B 70  ? 0.4864 0.4403 0.2933 0.1119  0.0765  -0.0404 79  TYR   B CA  
811  C C   . TYR   B 70  ? 0.4930 0.4588 0.3152 0.1115  0.0777  -0.0441 79  TYR   B C   
812  O O   . TYR   B 70  ? 0.4996 0.4652 0.3285 0.1160  0.0699  -0.0418 79  TYR   B O   
813  C CB  . TYR   B 70  ? 0.4842 0.4318 0.2964 0.1223  0.0758  -0.0413 79  TYR   B CB  
814  C CG  . TYR   B 70  ? 0.4961 0.4350 0.2984 0.1197  0.0764  -0.0386 79  TYR   B CG  
815  C CD1 . TYR   B 70  ? 0.5116 0.4474 0.3055 0.1211  0.0708  -0.0297 79  TYR   B CD1 
816  C CD2 . TYR   B 70  ? 0.5060 0.4411 0.3081 0.1165  0.0817  -0.0454 79  TYR   B CD2 
817  C CE1 . TYR   B 70  ? 0.5248 0.4570 0.3129 0.1171  0.0711  -0.0266 79  TYR   B CE1 
818  C CE2 . TYR   B 70  ? 0.5213 0.4483 0.3164 0.1122  0.0806  -0.0434 79  TYR   B CE2 
819  C CZ  . TYR   B 70  ? 0.5377 0.4649 0.3273 0.1114  0.0755  -0.0333 79  TYR   B CZ  
820  O OH  . TYR   B 70  ? 0.5604 0.4837 0.3466 0.1058  0.0741  -0.0307 79  TYR   B OH  
821  N N   . CYS   B 71  ? 0.4852 0.4635 0.3130 0.1064  0.0869  -0.0500 80  CYS   B N   
822  C CA  . CYS   B 71  ? 0.4766 0.4735 0.3223 0.1049  0.0902  -0.0535 80  CYS   B CA  
823  C C   . CYS   B 71  ? 0.4695 0.4727 0.3163 0.0921  0.0883  -0.0469 80  CYS   B C   
824  O O   . CYS   B 71  ? 0.4588 0.4818 0.3206 0.0864  0.0935  -0.0483 80  CYS   B O   
825  C CB  . CYS   B 71  ? 0.4878 0.4870 0.3495 0.1173  0.0845  -0.0568 80  CYS   B CB  
826  S SG  . CYS   B 71  ? 0.5652 0.5553 0.4270 0.1320  0.0872  -0.0635 80  CYS   B SG  
827  N N   . GLY   B 72  ? 0.4719 0.4591 0.3036 0.0875  0.0808  -0.0393 81  GLY   B N   
828  C CA  . GLY   B 72  ? 0.4773 0.4637 0.3075 0.0752  0.0771  -0.0320 81  GLY   B CA  
829  C C   . GLY   B 72  ? 0.4993 0.4643 0.3085 0.0740  0.0682  -0.0249 81  GLY   B C   
830  O O   . GLY   B 72  ? 0.5040 0.4588 0.3006 0.0823  0.0658  -0.0253 81  GLY   B O   
831  N N   . PRO   B 73  ? 0.5109 0.4690 0.3161 0.0632  0.0629  -0.0177 82  PRO   B N   
832  C CA  . PRO   B 73  ? 0.5316 0.4674 0.3150 0.0642  0.0530  -0.0114 82  PRO   B CA  
833  C C   . PRO   B 73  ? 0.5489 0.4709 0.3307 0.0778  0.0388  -0.0134 82  PRO   B C   
834  O O   . PRO   B 73  ? 0.5442 0.4719 0.3429 0.0834  0.0347  -0.0182 82  PRO   B O   
835  C CB  . PRO   B 73  ? 0.5372 0.4677 0.3186 0.0484  0.0511  -0.0029 82  PRO   B CB  
836  C CG  . PRO   B 73  ? 0.5231 0.4715 0.3308 0.0413  0.0540  -0.0050 82  PRO   B CG  
837  C CD  . PRO   B 73  ? 0.4935 0.4637 0.3143 0.0495  0.0652  -0.0142 82  PRO   B CD  
838  N N   . TRP   B 74  ? 0.5648 0.4708 0.3257 0.0846  0.0312  -0.0099 83  TRP   B N   
839  C CA  . TRP   B 74  ? 0.5803 0.4751 0.3349 0.1002  0.0183  -0.0113 83  TRP   B CA  
840  C C   . TRP   B 74  ? 0.5958 0.4796 0.3578 0.0997  0.0049  -0.0127 83  TRP   B C   
841  O O   . TRP   B 74  ? 0.6016 0.4735 0.3606 0.0874  0.0001  -0.0083 83  TRP   B O   
842  C CB  . TRP   B 74  ? 0.5908 0.4743 0.3214 0.1066  0.0135  -0.0069 83  TRP   B CB  
843  C CG  . TRP   B 74  ? 0.6009 0.4795 0.3234 0.1254  0.0031  -0.0082 83  TRP   B CG  
844  C CD1 . TRP   B 74  ? 0.6194 0.4813 0.3322 0.1349  -0.0124 -0.0091 83  TRP   B CD1 
845  C CD2 . TRP   B 74  ? 0.6012 0.4926 0.3234 0.1376  0.0074  -0.0085 83  TRP   B CD2 
846  N NE1 . TRP   B 74  ? 0.6260 0.4925 0.3319 0.1543  -0.0171 -0.0105 83  TRP   B NE1 
847  C CE2 . TRP   B 74  ? 0.6128 0.4985 0.3253 0.1552  -0.0044 -0.0089 83  TRP   B CE2 
848  C CE3 . TRP   B 74  ? 0.6000 0.5064 0.3293 0.1351  0.0196  -0.0082 83  TRP   B CE3 
849  C CZ2 . TRP   B 74  ? 0.6147 0.5133 0.3253 0.1697  -0.0025 -0.0072 83  TRP   B CZ2 
850  C CZ3 . TRP   B 74  ? 0.6039 0.5194 0.3326 0.1474  0.0202  -0.0062 83  TRP   B CZ3 
851  C CH2 . TRP   B 74  ? 0.6086 0.5222 0.3286 0.1642  0.0102  -0.0048 83  TRP   B CH2 
852  N N   . LYS   B 75  ? 0.6009 0.4886 0.3734 0.1121  -0.0014 -0.0187 84  LYS   B N   
853  C CA  . LYS   B 75  ? 0.6142 0.4940 0.3966 0.1131  -0.0156 -0.0227 84  LYS   B CA  
854  C C   . LYS   B 75  ? 0.6507 0.5119 0.4159 0.1308  -0.0328 -0.0254 84  LYS   B C   
855  O O   . LYS   B 75  ? 0.6572 0.5041 0.4246 0.1309  -0.0483 -0.0290 84  LYS   B O   
856  C CB  . LYS   B 75  ? 0.6128 0.5122 0.4191 0.1168  -0.0120 -0.0293 84  LYS   B CB  
857  C CG  . LYS   B 75  ? 0.6405 0.5615 0.4646 0.1044  0.0046  -0.0292 84  LYS   B CG  
858  C CD  . LYS   B 75  ? 0.6872 0.6115 0.5231 0.0839  0.0057  -0.0256 84  LYS   B CD  
859  C CE  . LYS   B 75  ? 0.7128 0.6654 0.5738 0.0770  0.0181  -0.0288 84  LYS   B CE  
860  N NZ  . LYS   B 75  ? 0.7380 0.7001 0.6089 0.0557  0.0242  -0.0224 84  LYS   B NZ  
861  N N   . LEU   B 76  ? 0.6672 0.5306 0.4168 0.1466  -0.0307 -0.0242 85  LEU   B N   
862  C CA  . LEU   B 76  ? 0.6920 0.5433 0.4238 0.1671  -0.0454 -0.0269 85  LEU   B CA  
863  C C   . LEU   B 76  ? 0.7283 0.5557 0.4390 0.1661  -0.0563 -0.0243 85  LEU   B C   
864  O O   . LEU   B 76  ? 0.7339 0.5620 0.4323 0.1634  -0.0494 -0.0184 85  LEU   B O   
865  C CB  . LEU   B 76  ? 0.6881 0.5553 0.4126 0.1834  -0.0375 -0.0245 85  LEU   B CB  
866  C CG  . LEU   B 76  ? 0.6855 0.5732 0.4283 0.1829  -0.0245 -0.0247 85  LEU   B CG  
867  C CD1 . LEU   B 76  ? 0.6908 0.5912 0.4257 0.1953  -0.0171 -0.0194 85  LEU   B CD1 
868  C CD2 . LEU   B 76  ? 0.6842 0.5737 0.4399 0.1899  -0.0323 -0.0316 85  LEU   B CD2 
869  N N   . ASP   B 77  ? 0.7559 0.5607 0.4618 0.1690  -0.0748 -0.0290 86  ASP   B N   
870  C CA  . ASP   B 77  ? 0.7969 0.5730 0.4815 0.1685  -0.0877 -0.0267 86  ASP   B CA  
871  C C   . ASP   B 77  ? 0.8266 0.5829 0.4896 0.1930  -0.1082 -0.0341 86  ASP   B C   
872  O O   . ASP   B 77  ? 0.8516 0.5801 0.4951 0.1951  -0.1211 -0.0333 86  ASP   B O   
873  C CB  . ASP   B 77  ? 0.8301 0.5889 0.5257 0.1440  -0.0923 -0.0235 86  ASP   B CB  
874  C CG  . ASP   B 77  ? 0.9053 0.6618 0.6221 0.1382  -0.1030 -0.0305 86  ASP   B CG  
875  O OD1 . ASP   B 77  ? 0.9106 0.6796 0.6334 0.1543  -0.1064 -0.0388 86  ASP   B OD1 
876  O OD2 . ASP   B 77  ? 0.9444 0.6880 0.6723 0.1172  -0.1081 -0.0270 86  ASP   B OD2 
877  N N   . ALA   B 78  ? 0.8230 0.5923 0.4871 0.2130  -0.1116 -0.0410 87  ALA   B N   
878  C CA  . ALA   B 78  ? 0.8434 0.5973 0.4847 0.2398  -0.1306 -0.0492 87  ALA   B CA  
879  C C   . ALA   B 78  ? 0.8569 0.6164 0.4735 0.2582  -0.1275 -0.0451 87  ALA   B C   
880  O O   . ALA   B 78  ? 0.8471 0.6298 0.4681 0.2526  -0.1094 -0.0367 87  ALA   B O   
881  C CB  . ALA   B 78  ? 0.8360 0.6061 0.4844 0.2566  -0.1336 -0.0568 87  ALA   B CB  
882  N N   . ALA   B 79  ? 0.8757 0.6153 0.4668 0.2811  -0.1461 -0.0519 88  ALA   B N   
883  C CA  . ALA   B 79  ? 0.8877 0.6360 0.4558 0.3012  -0.1444 -0.0488 88  ALA   B CA  
884  C C   . ALA   B 79  ? 0.9013 0.6486 0.4463 0.3365  -0.1595 -0.0583 88  ALA   B C   
885  O O   . ALA   B 79  ? 0.9081 0.6315 0.4468 0.3455  -0.1787 -0.0695 88  ALA   B O   
886  C CB  . ALA   B 79  ? 0.9043 0.6265 0.4584 0.2916  -0.1499 -0.0445 88  ALA   B CB  
887  N N   . TRP   B 80  ? 0.9028 0.6773 0.4349 0.3568  -0.1514 -0.0541 89  TRP   B N   
888  C CA  . TRP   B 80  ? 0.9207 0.7010 0.4284 0.3932  -0.1631 -0.0617 89  TRP   B CA  
889  C C   . TRP   B 80  ? 0.9490 0.6873 0.4303 0.4065  -0.1877 -0.0718 89  TRP   B C   
890  O O   . TRP   B 80  ? 0.9558 0.6739 0.4321 0.3934  -0.1896 -0.0674 89  TRP   B O   
891  C CB  . TRP   B 80  ? 0.9133 0.7356 0.4159 0.4082  -0.1473 -0.0524 89  TRP   B CB  
892  C CG  . TRP   B 80  ? 0.9258 0.7633 0.4043 0.4472  -0.1561 -0.0586 89  TRP   B CG  
893  C CD1 . TRP   B 80  ? 0.9415 0.7819 0.4130 0.4678  -0.1643 -0.0670 89  TRP   B CD1 
894  C CD2 . TRP   B 80  ? 0.9277 0.7858 0.3866 0.4715  -0.1557 -0.0564 89  TRP   B CD2 
895  N NE1 . TRP   B 80  ? 0.9493 0.8090 0.3956 0.5043  -0.1694 -0.0704 89  TRP   B NE1 
896  C CE2 . TRP   B 80  ? 0.9432 0.8160 0.3827 0.5072  -0.1637 -0.0637 89  TRP   B CE2 
897  C CE3 . TRP   B 80  ? 0.9315 0.7993 0.3870 0.4679  -0.1499 -0.0492 89  TRP   B CE3 
898  C CZ2 . TRP   B 80  ? 0.9510 0.8488 0.3684 0.5393  -0.1653 -0.0639 89  TRP   B CZ2 
899  C CZ3 . TRP   B 80  ? 0.9418 0.8344 0.3772 0.4989  -0.1521 -0.0495 89  TRP   B CZ3 
900  C CH2 . TRP   B 80  ? 0.9455 0.8538 0.3625 0.5343  -0.1593 -0.0567 89  TRP   B CH2 
901  N N   . ASP   B 81  ? 0.9614 0.6838 0.4245 0.4325  -0.2077 -0.0855 90  ASP   B N   
902  C CA  . ASP   B 81  ? 0.9943 0.6713 0.4300 0.4478  -0.2345 -0.0973 90  ASP   B CA  
903  C C   . ASP   B 81  ? 1.0134 0.6987 0.4191 0.4797  -0.2386 -0.0986 90  ASP   B C   
904  O O   . ASP   B 81  ? 1.0336 0.6790 0.4140 0.4939  -0.2609 -0.1079 90  ASP   B O   
905  C CB  . ASP   B 81  ? 1.0221 0.6742 0.4501 0.4623  -0.2575 -0.1140 90  ASP   B CB  
906  C CG  . ASP   B 81  ? 1.0606 0.7453 0.4765 0.4967  -0.2568 -0.1208 90  ASP   B CG  
907  O OD1 . ASP   B 81  ? 1.0661 0.7954 0.4810 0.5091  -0.2371 -0.1110 90  ASP   B OD1 
908  O OD2 . ASP   B 81  ? 1.0793 0.7458 0.4870 0.5109  -0.2760 -0.1354 90  ASP   B OD2 
909  N N   . GLY   B 82  ? 1.0035 0.7398 0.4129 0.4904  -0.2180 -0.0891 91  GLY   B N   
910  C CA  . GLY   B 82  ? 1.0212 0.7771 0.4063 0.5217  -0.2193 -0.0893 91  GLY   B CA  
911  C C   . GLY   B 82  ? 1.0471 0.8094 0.4057 0.5644  -0.2336 -0.1028 91  GLY   B C   
912  O O   . GLY   B 82  ? 1.0539 0.8286 0.3882 0.5956  -0.2389 -0.1061 91  GLY   B O   
913  N N   . LEU   B 83  ? 1.0524 0.8089 0.4146 0.5682  -0.2403 -0.1111 92  LEU   B N   
914  C CA  . LEU   B 83  ? 1.0736 0.8334 0.4082 0.6097  -0.2558 -0.1256 92  LEU   B CA  
915  C C   . LEU   B 83  ? 1.0716 0.8717 0.4162 0.6180  -0.2427 -0.1224 92  LEU   B C   
916  O O   . LEU   B 83  ? 1.0767 0.9108 0.4023 0.6532  -0.2403 -0.1240 92  LEU   B O   
917  C CB  . LEU   B 83  ? 1.1065 0.8039 0.4239 0.6149  -0.2885 -0.1454 92  LEU   B CB  
918  C CG  . LEU   B 83  ? 1.1593 0.8086 0.4488 0.6275  -0.3123 -0.1553 92  LEU   B CG  
919  C CD1 . LEU   B 83  ? 1.1931 0.7872 0.4633 0.6403  -0.3460 -0.1768 92  LEU   B CD1 
920  C CD2 . LEU   B 83  ? 1.1649 0.8427 0.4260 0.6676  -0.3108 -0.1566 92  LEU   B CD2 
921  N N   . SER   B 84  ? 1.0642 0.8592 0.4364 0.5885  -0.2362 -0.1187 93  SER   B N   
922  C CA  . SER   B 84  ? 1.0531 0.8764 0.4338 0.5955  -0.2279 -0.1173 93  SER   B CA  
923  C C   . SER   B 84  ? 1.0188 0.8962 0.4205 0.5856  -0.1967 -0.0966 93  SER   B C   
924  O O   . SER   B 84  ? 1.0120 0.9029 0.4303 0.5633  -0.1799 -0.0830 93  SER   B O   
925  C CB  . SER   B 84  ? 1.0826 0.8743 0.4827 0.5708  -0.2381 -0.1246 93  SER   B CB  
926  O OG  . SER   B 84  ? 1.1421 0.8793 0.5327 0.5657  -0.2648 -0.1395 93  SER   B OG  
927  N N   . GLU   B 85  ? 0.9969 0.9037 0.3965 0.6028  -0.1901 -0.0944 94  GLU   B N   
928  C CA  . GLU   B 85  ? 0.9713 0.9252 0.3906 0.5934  -0.1624 -0.0744 94  GLU   B CA  
929  C C   . GLU   B 85  ? 0.9491 0.8900 0.4019 0.5544  -0.1534 -0.0686 94  GLU   B C   
930  O O   . GLU   B 85  ? 0.9615 0.8708 0.4193 0.5460  -0.1682 -0.0807 94  GLU   B O   
931  C CB  . GLU   B 85  ? 0.9996 0.9867 0.4016 0.6273  -0.1598 -0.0732 94  GLU   B CB  
932  C CG  . GLU   B 85  ? 1.0609 1.0755 0.4322 0.6671  -0.1622 -0.0748 94  GLU   B CG  
933  C CD  . GLU   B 85  ? 1.1392 1.2009 0.4978 0.6962  -0.1506 -0.0656 94  GLU   B CD  
934  O OE1 . GLU   B 85  ? 1.1419 1.2053 0.5076 0.6928  -0.1478 -0.0633 94  GLU   B OE1 
935  O OE2 . GLU   B 85  ? 1.1599 1.2588 0.5010 0.7235  -0.1442 -0.0602 94  GLU   B OE2 
936  N N   . VAL   B 86  ? 0.9139 0.8798 0.3902 0.5307  -0.1301 -0.0509 95  VAL   B N   
937  C CA  . VAL   B 86  ? 0.8892 0.8470 0.3966 0.4954  -0.1192 -0.0447 95  VAL   B CA  
938  C C   . VAL   B 86  ? 0.8658 0.8570 0.3852 0.4963  -0.1011 -0.0308 95  VAL   B C   
939  O O   . VAL   B 86  ? 0.8634 0.8848 0.3674 0.5226  -0.0962 -0.0246 95  VAL   B O   
940  C CB  . VAL   B 86  ? 0.8787 0.8344 0.4019 0.4669  -0.1079 -0.0361 95  VAL   B CB  
941  C CG1 . VAL   B 86  ? 0.8970 0.8183 0.4054 0.4674  -0.1258 -0.0477 95  VAL   B CG1 
942  C CG2 . VAL   B 86  ? 0.8649 0.8630 0.3901 0.4713  -0.0889 -0.0197 95  VAL   B CG2 
943  N N   . GLN   B 87  ? 0.8489 0.8350 0.3948 0.4690  -0.0911 -0.0255 96  GLN   B N   
944  C CA  . GLN   B 87  ? 0.8308 0.8431 0.3882 0.4680  -0.0745 -0.0114 96  GLN   B CA  
945  C C   . GLN   B 87  ? 0.8089 0.8272 0.3935 0.4358  -0.0558 0.0017  96  GLN   B C   
946  O O   . GLN   B 87  ? 0.8118 0.8075 0.4136 0.4117  -0.0573 -0.0041 96  GLN   B O   
947  C CB  . GLN   B 87  ? 0.8524 0.8538 0.4103 0.4762  -0.0838 -0.0197 96  GLN   B CB  
948  C CG  . GLN   B 87  ? 0.8984 0.9198 0.4306 0.5131  -0.0886 -0.0195 96  GLN   B CG  
949  C CD  . GLN   B 87  ? 0.9474 0.9590 0.4772 0.5243  -0.0998 -0.0287 96  GLN   B CD  
950  O OE1 . GLN   B 87  ? 0.9475 0.9499 0.4995 0.5047  -0.0962 -0.0280 96  GLN   B OE1 
951  N NE2 . GLN   B 87  ? 0.9729 0.9881 0.4746 0.5584  -0.1143 -0.0384 96  GLN   B NE2 
952  N N   . LEU   B 88  ? 0.7810 0.8306 0.3698 0.4351  -0.0385 0.0191  97  LEU   B N   
953  C CA  . LEU   B 88  ? 0.7577 0.8119 0.3717 0.4054  -0.0220 0.0311  97  LEU   B CA  
954  C C   . LEU   B 88  ? 0.7442 0.7983 0.3689 0.4032  -0.0158 0.0368  97  LEU   B C   
955  O O   . LEU   B 88  ? 0.7420 0.8160 0.3565 0.4229  -0.0120 0.0460  97  LEU   B O   
956  C CB  . LEU   B 88  ? 0.7410 0.8287 0.3574 0.4040  -0.0077 0.0478  97  LEU   B CB  
957  C CG  . LEU   B 88  ? 0.7352 0.8316 0.3765 0.3772  0.0095  0.0628  97  LEU   B CG  
958  C CD1 . LEU   B 88  ? 0.7420 0.8121 0.3994 0.3492  0.0088  0.0545  97  LEU   B CD1 
959  C CD2 . LEU   B 88  ? 0.7239 0.8561 0.3688 0.3766  0.0214  0.0792  97  LEU   B CD2 
960  N N   . LEU   B 89  ? 0.7313 0.7633 0.3744 0.3818  -0.0157 0.0309  98  LEU   B N   
961  C CA  . LEU   B 89  ? 0.7175 0.7481 0.3716 0.3795  -0.0100 0.0359  98  LEU   B CA  
962  C C   . LEU   B 89  ? 0.6989 0.7411 0.3691 0.3600  0.0078  0.0527  98  LEU   B C   
963  O O   . LEU   B 89  ? 0.6900 0.7194 0.3773 0.3359  0.0125  0.0502  98  LEU   B O   
964  C CB  . LEU   B 89  ? 0.7215 0.7263 0.3887 0.3669  -0.0188 0.0208  98  LEU   B CB  
965  C CG  . LEU   B 89  ? 0.7277 0.7271 0.4111 0.3602  -0.0136 0.0227  98  LEU   B CG  
966  C CD1 . LEU   B 89  ? 0.7347 0.7496 0.4096 0.3783  -0.0075 0.0363  98  LEU   B CD1 
967  C CD2 . LEU   B 89  ? 0.7331 0.7158 0.4224 0.3607  -0.0277 0.0055  98  LEU   B CD2 
968  N N   . ALA   B 90  ? 0.6895 0.7575 0.3533 0.3706  0.0174  0.0698  99  ALA   B N   
969  C CA  . ALA   B 90  ? 0.6846 0.7649 0.3640 0.3515  0.0328  0.0868  99  ALA   B CA  
970  C C   . ALA   B 90  ? 0.6842 0.7526 0.3775 0.3408  0.0399  0.0944  99  ALA   B C   
971  O O   . ALA   B 90  ? 0.6898 0.7599 0.3752 0.3572  0.0391  0.0993  99  ALA   B O   
972  C CB  . ALA   B 90  ? 0.6766 0.7920 0.3470 0.3647  0.0406  0.1041  99  ALA   B CB  
973  N N   . VAL   B 91  ? 0.6734 0.7288 0.3856 0.3148  0.0461  0.0949  100 VAL   B N   
974  C CA  . VAL   B 91  ? 0.6711 0.7115 0.3964 0.3040  0.0522  0.1012  100 VAL   B CA  
975  C C   . VAL   B 91  ? 0.6739 0.7251 0.4109 0.2867  0.0642  0.1196  100 VAL   B C   
976  O O   . VAL   B 91  ? 0.6770 0.7197 0.4273 0.2648  0.0666  0.1158  100 VAL   B O   
977  C CB  . VAL   B 91  ? 0.6659 0.6799 0.4032 0.2897  0.0476  0.0835  100 VAL   B CB  
978  C CG1 . VAL   B 91  ? 0.6725 0.6700 0.4215 0.2823  0.0526  0.0880  100 VAL   B CG1 
979  C CG2 . VAL   B 91  ? 0.6655 0.6725 0.3942 0.3037  0.0349  0.0662  100 VAL   B CG2 
980  N N   . PRO   B 92  ? 0.6679 0.7400 0.3999 0.2962  0.0713  0.1400  101 PRO   B N   
981  C CA  . PRO   B 92  ? 0.6625 0.7488 0.4077 0.2782  0.0819  0.1592  101 PRO   B CA  
982  C C   . PRO   B 92  ? 0.6781 0.7413 0.4377 0.2610  0.0871  0.1687  101 PRO   B C   
983  O O   . PRO   B 92  ? 0.6921 0.7366 0.4472 0.2704  0.0851  0.1678  101 PRO   B O   
984  C CB  . PRO   B 92  ? 0.6600 0.7823 0.3930 0.2973  0.0876  0.1780  101 PRO   B CB  
985  C CG  . PRO   B 92  ? 0.6709 0.7935 0.3813 0.3273  0.0787  0.1666  101 PRO   B CG  
986  C CD  . PRO   B 92  ? 0.6625 0.7495 0.3758 0.3241  0.0697  0.1470  101 PRO   B CD  
987  N N   . PRO   B 93  ? 0.6759 0.7394 0.4525 0.2366  0.0926  0.1776  102 PRO   B N   
988  C CA  . PRO   B 93  ? 0.6838 0.7200 0.4731 0.2201  0.0956  0.1856  102 PRO   B CA  
989  C C   . PRO   B 93  ? 0.6954 0.7314 0.4785 0.2314  0.1007  0.2071  102 PRO   B C   
990  O O   . PRO   B 93  ? 0.6888 0.7553 0.4678 0.2382  0.1076  0.2276  102 PRO   B O   
991  C CB  . PRO   B 93  ? 0.6842 0.7281 0.4914 0.1938  0.0993  0.1932  102 PRO   B CB  
992  C CG  . PRO   B 93  ? 0.6838 0.7482 0.4881 0.1949  0.0958  0.1790  102 PRO   B CG  
993  C CD  . PRO   B 93  ? 0.6613 0.7475 0.4464 0.2231  0.0945  0.1786  102 PRO   B CD  
994  N N   . GLY   B 94  ? 0.7060 0.7096 0.4867 0.2360  0.0972  0.2017  103 GLY   B N   
995  C CA  . GLY   B 94  ? 0.7149 0.7112 0.4876 0.2482  0.1004  0.2203  103 GLY   B CA  
996  C C   . GLY   B 94  ? 0.7179 0.7359 0.4693 0.2786  0.0994  0.2232  103 GLY   B C   
997  O O   . GLY   B 94  ? 0.7213 0.7368 0.4628 0.2916  0.1023  0.2399  103 GLY   B O   
998  N N   . GLU   B 95  ? 0.7171 0.7556 0.4600 0.2910  0.0946  0.2076  104 GLU   B N   
999  C CA  . GLU   B 95  ? 0.7276 0.7867 0.4488 0.3210  0.0915  0.2074  104 GLU   B CA  
1000 C C   . GLU   B 95  ? 0.7428 0.7880 0.4570 0.3342  0.0787  0.1795  104 GLU   B C   
1001 O O   . GLU   B 95  ? 0.7481 0.7805 0.4732 0.3201  0.0740  0.1609  104 GLU   B O   
1002 C CB  . GLU   B 95  ? 0.7499 0.8496 0.4644 0.3275  0.0962  0.2160  104 GLU   B CB  
1003 C CG  . GLU   B 95  ? 0.8127 0.9333 0.5389 0.3111  0.1092  0.2439  104 GLU   B CG  
1004 C CD  . GLU   B 95  ? 0.9118 1.0787 0.6330 0.3192  0.1147  0.2530  104 GLU   B CD  
1005 O OE1 . GLU   B 95  ? 0.9437 1.1229 0.6503 0.3384  0.1073  0.2358  104 GLU   B OE1 
1006 O OE2 . GLU   B 95  ? 0.9318 1.1230 0.6642 0.3065  0.1259  0.2776  104 GLU   B OE2 
1007 N N   . ARG   B 96  ? 0.7496 0.7993 0.4455 0.3610  0.0729  0.1772  105 ARG   B N   
1008 C CA  . ARG   B 96  ? 0.7689 0.8077 0.4586 0.3750  0.0592  0.1522  105 ARG   B CA  
1009 C C   . ARG   B 96  ? 0.7770 0.8285 0.4617 0.3781  0.0519  0.1355  105 ARG   B C   
1010 O O   . ARG   B 96  ? 0.7754 0.8520 0.4518 0.3832  0.0562  0.1445  105 ARG   B O   
1011 C CB  . ARG   B 96  ? 0.7956 0.8393 0.4653 0.4043  0.0544  0.1568  105 ARG   B CB  
1012 C CG  . ARG   B 96  ? 0.8450 0.8755 0.5111 0.4186  0.0391  0.1329  105 ARG   B CG  
1013 C CD  . ARG   B 96  ? 0.9067 0.9375 0.5563 0.4443  0.0352  0.1398  105 ARG   B CD  
1014 N NE  . ARG   B 96  ? 0.9615 1.0191 0.5867 0.4674  0.0384  0.1550  105 ARG   B NE  
1015 C CZ  . ARG   B 96  ? 1.0026 1.0695 0.6181 0.4740  0.0495  0.1818  105 ARG   B CZ  
1016 N NH1 . ARG   B 96  ? 1.0020 1.0489 0.6301 0.4585  0.0574  0.1963  105 ARG   B NH1 
1017 N NH2 . ARG   B 96  ? 1.0031 1.0989 0.5954 0.4965  0.0529  0.1948  105 ARG   B NH2 
1018 N N   . ALA   B 97  ? 0.7809 0.8154 0.4712 0.3751  0.0407  0.1117  106 ALA   B N   
1019 C CA  . ALA   B 97  ? 0.7878 0.8265 0.4730 0.3774  0.0313  0.0947  106 ALA   B CA  
1020 C C   . ALA   B 97  ? 0.7980 0.8562 0.4585 0.4067  0.0245  0.0950  106 ALA   B C   
1021 O O   . ALA   B 97  ? 0.8056 0.8659 0.4537 0.4276  0.0203  0.0970  106 ALA   B O   
1022 C CB  . ALA   B 97  ? 0.7908 0.8083 0.4858 0.3713  0.0202  0.0724  106 ALA   B CB  
1023 N N   . LYS   B 98  ? 0.7974 0.8706 0.4492 0.4101  0.0234  0.0934  107 LYS   B N   
1024 C CA  . LYS   B 98  ? 0.8060 0.8999 0.4323 0.4398  0.0175  0.0937  107 LYS   B CA  
1025 C C   . LYS   B 98  ? 0.8026 0.8948 0.4202 0.4442  0.0061  0.0769  107 LYS   B C   
1026 O O   . LYS   B 98  ? 0.8021 0.8975 0.4289 0.4273  0.0113  0.0787  107 LYS   B O   
1027 C CB  . LYS   B 98  ? 0.8355 0.9607 0.4573 0.4442  0.0334  0.1195  107 LYS   B CB  
1028 C CG  . LYS   B 98  ? 0.9019 1.0570 0.4967 0.4765  0.0315  0.1243  107 LYS   B CG  
1029 C CD  . LYS   B 98  ? 0.9544 1.1453 0.5510 0.4747  0.0501  0.1528  107 LYS   B CD  
1030 C CE  . LYS   B 98  ? 0.9920 1.1870 0.6127 0.4439  0.0598  0.1597  107 LYS   B CE  
1031 N NZ  . LYS   B 98  ? 1.0098 1.2467 0.6319 0.4447  0.0748  0.1843  107 LYS   B NZ  
1032 N N   . ASN   B 99  ? 0.8037 0.8889 0.4029 0.4671  -0.0108 0.0602  108 ASN   B N   
1033 C CA  . ASN   B 99  ? 0.8131 0.8906 0.4013 0.4732  -0.0243 0.0436  108 ASN   B CA  
1034 C C   . ASN   B 99  ? 0.8156 0.9222 0.3814 0.4973  -0.0221 0.0508  108 ASN   B C   
1035 O O   . ASN   B 99  ? 0.8241 0.9492 0.3706 0.5243  -0.0223 0.0564  108 ASN   B O   
1036 C CB  . ASN   B 99  ? 0.8345 0.8895 0.4130 0.4870  -0.0457 0.0216  108 ASN   B CB  
1037 C CG  . ASN   B 99  ? 0.8762 0.9067 0.4777 0.4652  -0.0498 0.0123  108 ASN   B CG  
1038 O OD1 . ASN   B 99  ? 0.8930 0.9249 0.5061 0.4600  -0.0420 0.0201  108 ASN   B OD1 
1039 N ND2 . ASN   B 99  ? 0.8851 0.8930 0.4930 0.4530  -0.0624 -0.0043 108 ASN   B ND2 
1040 N N   . ILE   B 100 ? 0.8069 0.9193 0.3740 0.4895  -0.0201 0.0507  109 ILE   B N   
1041 C CA  . ILE   B 100 ? 0.8087 0.9517 0.3556 0.5133  -0.0182 0.0563  109 ILE   B CA  
1042 C C   . ILE   B 100 ? 0.8268 0.9520 0.3583 0.5240  -0.0363 0.0360  109 ILE   B C   
1043 O O   . ILE   B 100 ? 0.8307 0.9427 0.3739 0.5032  -0.0367 0.0322  109 ILE   B O   
1044 C CB  . ILE   B 100 ? 0.8006 0.9736 0.3633 0.4965  0.0014  0.0773  109 ILE   B CB  
1045 C CG1 . ILE   B 100 ? 0.8025 0.9839 0.3852 0.4779  0.0185  0.0978  109 ILE   B CG1 
1046 C CG2 . ILE   B 100 ? 0.7994 1.0121 0.3426 0.5236  0.0045  0.0844  109 ILE   B CG2 
1047 C CD1 . ILE   B 100 ? 0.8138 1.0194 0.3825 0.5008  0.0251  0.1125  109 ILE   B CD1 
1048 N N   . GLN   B 101 ? 0.8404 0.9638 0.3440 0.5570  -0.0519 0.0231  110 GLN   B N   
1049 C CA  . GLN   B 101 ? 0.8614 0.9636 0.3467 0.5704  -0.0716 0.0032  110 GLN   B CA  
1050 C C   . GLN   B 101 ? 0.8656 0.9971 0.3409 0.5822  -0.0649 0.0105  110 GLN   B C   
1051 O O   . GLN   B 101 ? 0.8592 1.0324 0.3258 0.6009  -0.0525 0.0249  110 GLN   B O   
1052 C CB  . GLN   B 101 ? 0.8882 0.9793 0.3451 0.6044  -0.0918 -0.0138 110 GLN   B CB  
1053 C CG  . GLN   B 101 ? 0.9254 0.9821 0.3644 0.6157  -0.1169 -0.0374 110 GLN   B CG  
1054 C CD  . GLN   B 101 ? 0.9716 1.0057 0.3933 0.6367  -0.1390 -0.0563 110 GLN   B CD  
1055 O OE1 . GLN   B 101 ? 0.9888 1.0158 0.4243 0.6261  -0.1387 -0.0561 110 GLN   B OE1 
1056 N NE2 . GLN   B 101 ? 0.9773 0.9995 0.3681 0.6679  -0.1597 -0.0738 110 GLN   B NE2 
1057 N N   . THR   B 102 ? 0.8719 0.9835 0.3484 0.5716  -0.0728 0.0014  111 THR   B N   
1058 C CA  . THR   B 102 ? 0.8713 1.0090 0.3390 0.5830  -0.0686 0.0063  111 THR   B CA  
1059 C C   . THR   B 102 ? 0.8895 0.9906 0.3428 0.5870  -0.0892 -0.0128 111 THR   B C   
1060 O O   . THR   B 102 ? 0.9059 0.9632 0.3652 0.5695  -0.1017 -0.0250 111 THR   B O   
1061 C CB  . THR   B 102 ? 0.8751 1.0376 0.3721 0.5521  -0.0467 0.0263  111 THR   B CB  
1062 O OG1 . THR   B 102 ? 0.8855 1.0762 0.3758 0.5630  -0.0436 0.0305  111 THR   B OG1 
1063 C CG2 . THR   B 102 ? 0.8814 1.0080 0.4026 0.5133  -0.0466 0.0230  111 THR   B CG2 
1064 N N   . LEU   B 103 ? 0.8840 1.0031 0.3188 0.6098  -0.0927 -0.0147 112 LEU   B N   
1065 C CA  . LEU   B 103 ? 0.9072 0.9891 0.3282 0.6124  -0.1118 -0.0307 112 LEU   B CA  
1066 C C   . LEU   B 103 ? 0.9090 1.0061 0.3484 0.5891  -0.0988 -0.0188 112 LEU   B C   
1067 O O   . LEU   B 103 ? 0.9000 1.0452 0.3422 0.5984  -0.0846 -0.0057 112 LEU   B O   
1068 C CB  . LEU   B 103 ? 0.9209 1.0038 0.3048 0.6567  -0.1295 -0.0451 112 LEU   B CB  
1069 C CG  . LEU   B 103 ? 0.9602 0.9957 0.3296 0.6569  -0.1511 -0.0612 112 LEU   B CG  
1070 C CD1 . LEU   B 103 ? 0.9920 0.9717 0.3492 0.6585  -0.1756 -0.0808 112 LEU   B CD1 
1071 C CD2 . LEU   B 103 ? 0.9717 1.0257 0.3140 0.6925  -0.1582 -0.0663 112 LEU   B CD2 
1072 N N   . PRO   B 104 ? 0.9113 0.9706 0.3638 0.5588  -0.1033 -0.0228 113 PRO   B N   
1073 C CA  . PRO   B 104 ? 0.8994 0.9728 0.3686 0.5365  -0.0915 -0.0121 113 PRO   B CA  
1074 C C   . PRO   B 104 ? 0.9085 0.9884 0.3573 0.5583  -0.1007 -0.0170 113 PRO   B C   
1075 O O   . PRO   B 104 ? 0.9306 0.9858 0.3507 0.5858  -0.1207 -0.0322 113 PRO   B O   
1076 C CB  . PRO   B 104 ? 0.9134 0.9431 0.3990 0.5007  -0.0947 -0.0160 113 PRO   B CB  
1077 C CG  . PRO   B 104 ? 0.9337 0.9298 0.4144 0.5031  -0.1075 -0.0277 113 PRO   B CG  
1078 C CD  . PRO   B 104 ? 0.9200 0.9257 0.3741 0.5428  -0.1187 -0.0361 113 PRO   B CD  
1079 N N   . GLY   B 105 ? 0.8826 0.9953 0.3465 0.5460  -0.0867 -0.0044 114 GLY   B N   
1080 C CA  . GLY   B 105 ? 0.8764 0.9999 0.3266 0.5615  -0.0929 -0.0067 114 GLY   B CA  
1081 C C   . GLY   B 105 ? 0.8829 0.9633 0.3362 0.5361  -0.1008 -0.0114 114 GLY   B C   
1082 O O   . GLY   B 105 ? 0.9011 0.9359 0.3573 0.5169  -0.1079 -0.0178 114 GLY   B O   
1083 N N   . ILE   B 106 ? 0.8652 0.9617 0.3181 0.5359  -0.0995 -0.0076 115 ILE   B N   
1084 C CA  . ILE   B 106 ? 0.8823 0.9398 0.3337 0.5153  -0.1074 -0.0111 115 ILE   B CA  
1085 C C   . ILE   B 106 ? 0.8644 0.9570 0.3360 0.4962  -0.0933 0.0009  115 ILE   B C   
1086 O O   . ILE   B 106 ? 0.8554 0.9945 0.3267 0.5142  -0.0886 0.0061  115 ILE   B O   
1087 C CB  . ILE   B 106 ? 0.9166 0.9411 0.3329 0.5445  -0.1306 -0.0246 115 ILE   B CB  
1088 C CG1 . ILE   B 106 ? 0.9549 0.9381 0.3483 0.5646  -0.1493 -0.0393 115 ILE   B CG1 
1089 C CG2 . ILE   B 106 ? 0.9422 0.9304 0.3546 0.5253  -0.1379 -0.0252 115 ILE   B CG2 
1090 C CD1 . ILE   B 106 ? 0.9895 0.9205 0.3894 0.5375  -0.1560 -0.0438 115 ILE   B CD1 
1091 N N   . PHE   B 107 ? 0.8577 0.9278 0.3449 0.4617  -0.0884 0.0041  116 PHE   B N   
1092 C CA  . PHE   B 107 ? 0.8453 0.9384 0.3477 0.4428  -0.0793 0.0123  116 PHE   B CA  
1093 C C   . PHE   B 107 ? 0.8705 0.9263 0.3487 0.4492  -0.0958 0.0047  116 PHE   B C   
1094 O O   . PHE   B 107 ? 0.8938 0.8998 0.3649 0.4346  -0.1035 -0.0003 116 PHE   B O   
1095 C CB  . PHE   B 107 ? 0.8360 0.9183 0.3640 0.4037  -0.0667 0.0179  116 PHE   B CB  
1096 C CG  . PHE   B 107 ? 0.8172 0.9416 0.3744 0.3890  -0.0481 0.0293  116 PHE   B CG  
1097 C CD1 . PHE   B 107 ? 0.8115 0.9773 0.3722 0.4089  -0.0420 0.0354  116 PHE   B CD1 
1098 C CD2 . PHE   B 107 ? 0.8196 0.9404 0.3996 0.3559  -0.0372 0.0341  116 PHE   B CD2 
1099 C CE1 . PHE   B 107 ? 0.7998 1.0003 0.3871 0.3937  -0.0253 0.0479  116 PHE   B CE1 
1100 C CE2 . PHE   B 107 ? 0.8089 0.9627 0.4148 0.3421  -0.0219 0.0446  116 PHE   B CE2 
1101 C CZ  . PHE   B 107 ? 0.7927 0.9847 0.4026 0.3600  -0.0161 0.0522  116 PHE   B CZ  
1102 N N   . LYS   B 108 ? 0.8657 0.9447 0.3307 0.4718  -0.1018 0.0042  117 LYS   B N   
1103 C CA  . LYS   B 108 ? 0.8900 0.9330 0.3299 0.4797  -0.1181 -0.0020 117 LYS   B CA  
1104 C C   . LYS   B 108 ? 0.8686 0.9236 0.3233 0.4535  -0.1099 0.0055  117 LYS   B C   
1105 O O   . LYS   B 108 ? 0.8384 0.9460 0.3110 0.4524  -0.0993 0.0124  117 LYS   B O   
1106 C CB  . LYS   B 108 ? 0.9333 0.9947 0.3484 0.5219  -0.1307 -0.0078 117 LYS   B CB  
1107 C CG  . LYS   B 108 ? 1.0301 1.0731 0.4240 0.5519  -0.1425 -0.0181 117 LYS   B CG  
1108 C CD  . LYS   B 108 ? 1.1159 1.1916 0.4886 0.5969  -0.1511 -0.0235 117 LYS   B CD  
1109 C CE  . LYS   B 108 ? 1.1950 1.2610 0.5486 0.6273  -0.1603 -0.0338 117 LYS   B CE  
1110 N NZ  . LYS   B 108 ? 1.2170 1.3228 0.5507 0.6736  -0.1663 -0.0390 117 LYS   B NZ  
1111 N N   . THR   B 109 ? 0.8846 0.8931 0.3335 0.4309  -0.1142 0.0046  118 THR   B N   
1112 C CA  . THR   B 109 ? 0.8783 0.8922 0.3372 0.4058  -0.1074 0.0104  118 THR   B CA  
1113 C C   . THR   B 109 ? 0.8962 0.8694 0.3256 0.4121  -0.1232 0.0078  118 THR   B C   
1114 O O   . THR   B 109 ? 0.9170 0.8523 0.3203 0.4323  -0.1393 0.0016  118 THR   B O   
1115 C CB  . THR   B 109 ? 0.8921 0.8943 0.3745 0.3688  -0.0936 0.0142  118 THR   B CB  
1116 O OG1 . THR   B 109 ? 0.9309 0.8772 0.3993 0.3580  -0.1014 0.0110  118 THR   B OG1 
1117 C CG2 . THR   B 109 ? 0.8778 0.9072 0.3850 0.3633  -0.0805 0.0167  118 THR   B CG2 
1118 N N   . LYS   B 110 ? 0.8901 0.8682 0.3224 0.3948  -0.1195 0.0124  119 LYS   B N   
1119 C CA  . LYS   B 110 ? 0.9150 0.8539 0.3189 0.3981  -0.1330 0.0123  119 LYS   B CA  
1120 C C   . LYS   B 110 ? 0.9486 0.8274 0.3423 0.3784  -0.1368 0.0130  119 LYS   B C   
1121 O O   . LYS   B 110 ? 0.9721 0.8094 0.3390 0.3829  -0.1500 0.0140  119 LYS   B O   
1122 C CB  . LYS   B 110 ? 0.9078 0.8739 0.3174 0.3866  -0.1278 0.0169  119 LYS   B CB  
1123 C CG  . LYS   B 110 ? 0.9382 0.9069 0.3698 0.3505  -0.1126 0.0210  119 LYS   B CG  
1124 C CD  . LYS   B 110 ? 0.9795 0.9747 0.4144 0.3414  -0.1098 0.0236  119 LYS   B CD  
1125 C CE  . LYS   B 110 ? 1.0306 0.9984 0.4633 0.3132  -0.1039 0.0265  119 LYS   B CE  
1126 N NZ  . LYS   B 110 ? 1.0423 1.0158 0.5026 0.2877  -0.0884 0.0265  119 LYS   B NZ  
1127 N N   . ASP   B 111 ? 0.9472 0.8223 0.3626 0.3567  -0.1254 0.0135  120 ASP   B N   
1128 C CA  . ASP   B 111 ? 0.9743 0.8016 0.3865 0.3361  -0.1270 0.0147  120 ASP   B CA  
1129 C C   . ASP   B 111 ? 0.9925 0.7963 0.4047 0.3441  -0.1341 0.0087  120 ASP   B C   
1130 O O   . ASP   B 111 ? 1.0072 0.7837 0.4273 0.3235  -0.1318 0.0096  120 ASP   B O   
1131 C CB  . ASP   B 111 ? 0.9869 0.8288 0.4246 0.3033  -0.1086 0.0192  120 ASP   B CB  
1132 C CG  . ASP   B 111 ? 1.0485 0.9005 0.4822 0.2911  -0.1037 0.0242  120 ASP   B CG  
1133 O OD1 . ASP   B 111 ? 1.0740 0.8945 0.4821 0.2939  -0.1140 0.0275  120 ASP   B OD1 
1134 O OD2 . ASP   B 111 ? 1.0607 0.9503 0.5157 0.2789  -0.0905 0.0250  120 ASP   B OD2 
1135 N N   . GLY   B 112 ? 0.9881 0.8050 0.3921 0.3740  -0.1425 0.0023  121 GLY   B N   
1136 C CA  . GLY   B 112 ? 0.9988 0.7945 0.3999 0.3853  -0.1512 -0.0052 121 GLY   B CA  
1137 C C   . GLY   B 112 ? 0.9795 0.8198 0.3999 0.3953  -0.1406 -0.0075 121 GLY   B C   
1138 O O   . GLY   B 112 ? 0.9630 0.8481 0.4056 0.3849  -0.1237 -0.0015 121 GLY   B O   
1139 N N   . ASP   B 113 ? 0.9812 0.8084 0.3929 0.4151  -0.1510 -0.0157 122 ASP   B N   
1140 C CA  . ASP   B 113 ? 0.9652 0.8324 0.3910 0.4276  -0.1419 -0.0172 122 ASP   B CA  
1141 C C   . ASP   B 113 ? 0.9583 0.8236 0.4084 0.4042  -0.1311 -0.0159 122 ASP   B C   
1142 O O   . ASP   B 113 ? 0.9779 0.8021 0.4275 0.3892  -0.1382 -0.0192 122 ASP   B O   
1143 C CB  . ASP   B 113 ? 0.9958 0.8556 0.3965 0.4664  -0.1589 -0.0278 122 ASP   B CB  
1144 C CG  . ASP   B 113 ? 1.0687 0.9430 0.4468 0.4965  -0.1679 -0.0298 122 ASP   B CG  
1145 O OD1 . ASP   B 113 ? 1.0733 0.9570 0.4531 0.4863  -0.1635 -0.0231 122 ASP   B OD1 
1146 O OD2 . ASP   B 113 ? 1.1048 0.9813 0.4621 0.5320  -0.1803 -0.0389 122 ASP   B OD2 
1147 N N   . ILE   B 114 ? 0.9241 0.8352 0.3959 0.4017  -0.1144 -0.0105 123 ILE   B N   
1148 C CA  . ILE   B 114 ? 0.9119 0.8276 0.4074 0.3826  -0.1027 -0.0085 123 ILE   B CA  
1149 C C   . ILE   B 114 ? 0.8929 0.8365 0.3886 0.4064  -0.1010 -0.0101 123 ILE   B C   
1150 O O   . ILE   B 114 ? 0.8872 0.8605 0.3720 0.4322  -0.1022 -0.0093 123 ILE   B O   
1151 C CB  . ILE   B 114 ? 0.9028 0.8462 0.4247 0.3543  -0.0830 0.0016  123 ILE   B CB  
1152 C CG1 . ILE   B 114 ? 0.9291 0.8527 0.4467 0.3355  -0.0841 0.0036  123 ILE   B CG1 
1153 C CG2 . ILE   B 114 ? 0.8971 0.8420 0.4426 0.3344  -0.0713 0.0035  123 ILE   B CG2 
1154 C CD1 . ILE   B 114 ? 0.9319 0.8869 0.4689 0.3164  -0.0685 0.0113  123 ILE   B CD1 
1155 N N   . GLY   B 115 ? 0.8758 0.8125 0.3836 0.3988  -0.0978 -0.0119 124 GLY   B N   
1156 C CA  . GLY   B 115 ? 0.8653 0.8295 0.3734 0.4197  -0.0945 -0.0117 124 GLY   B CA  
1157 C C   . GLY   B 115 ? 0.8340 0.8491 0.3626 0.4134  -0.0739 0.0019  124 GLY   B C   
1158 O O   . GLY   B 115 ? 0.8208 0.8452 0.3669 0.3887  -0.0627 0.0093  124 GLY   B O   
1159 N N   . ALA   B 116 ? 0.8173 0.8658 0.3438 0.4353  -0.0692 0.0056  125 ALA   B N   
1160 C CA  . ALA   B 116 ? 0.7955 0.8929 0.3426 0.4283  -0.0498 0.0208  125 ALA   B CA  
1161 C C   . ALA   B 116 ? 0.7881 0.9112 0.3354 0.4456  -0.0435 0.0261  125 ALA   B C   
1162 O O   . ALA   B 116 ? 0.7962 0.9326 0.3224 0.4780  -0.0509 0.0221  125 ALA   B O   
1163 C CB  . ALA   B 116 ? 0.7846 0.9171 0.3287 0.4384  -0.0473 0.0264  125 ALA   B CB  
1164 N N   . VAL   B 117 ? 0.7722 0.9027 0.3415 0.4258  -0.0300 0.0354  126 VAL   B N   
1165 C CA  A VAL   B 117 ? 0.7690 0.9236 0.3386 0.4406  -0.0228 0.0430  126 VAL   B CA  
1166 C CA  B VAL   B 117 ? 0.7691 0.9230 0.3392 0.4398  -0.0227 0.0431  126 VAL   B CA  
1167 C C   . VAL   B 117 ? 0.7524 0.9598 0.3376 0.4382  -0.0051 0.0624  126 VAL   B C   
1168 O O   . VAL   B 117 ? 0.7419 0.9582 0.3503 0.4106  0.0055  0.0716  126 VAL   B O   
1169 C CB  A VAL   B 117 ? 0.7799 0.9079 0.3596 0.4265  -0.0216 0.0409  126 VAL   B CB  
1170 C CB  B VAL   B 117 ? 0.7790 0.9058 0.3626 0.4208  -0.0201 0.0417  126 VAL   B CB  
1171 C CG1 A VAL   B 117 ? 0.8051 0.8920 0.3664 0.4386  -0.0408 0.0225  126 VAL   B CG1 
1172 C CG1 B VAL   B 117 ? 0.7777 0.9278 0.3623 0.4337  -0.0116 0.0517  126 VAL   B CG1 
1173 C CG2 A VAL   B 117 ? 0.7807 0.8954 0.3863 0.3896  -0.0120 0.0453  126 VAL   B CG2 
1174 C CG2 B VAL   B 117 ? 0.8036 0.8835 0.3743 0.4232  -0.0380 0.0235  126 VAL   B CG2 
1175 N N   . ALA   B 118 ? 0.7476 0.9917 0.3198 0.4676  -0.0025 0.0686  127 ALA   B N   
1176 C CA  . ALA   B 118 ? 0.7333 1.0331 0.3204 0.4672  0.0145  0.0890  127 ALA   B CA  
1177 C C   . ALA   B 118 ? 0.7391 1.0553 0.3325 0.4688  0.0263  0.1032  127 ALA   B C   
1178 O O   . ALA   B 118 ? 0.7435 1.0856 0.3195 0.4985  0.0272  0.1070  127 ALA   B O   
1179 C CB  . ALA   B 118 ? 0.7241 1.0627 0.2936 0.4992  0.0112  0.0886  127 ALA   B CB  
1180 N N   . LEU   B 119 ? 0.7406 1.0394 0.3564 0.4385  0.0345  0.1104  128 LEU   B N   
1181 C CA  . LEU   B 119 ? 0.7460 1.0546 0.3697 0.4356  0.0458  0.1254  128 LEU   B CA  
1182 C C   . LEU   B 119 ? 0.7440 1.0678 0.3994 0.4021  0.0609  0.1438  128 LEU   B C   
1183 O O   . LEU   B 119 ? 0.7542 1.0628 0.4247 0.3775  0.0594  0.1387  128 LEU   B O   
1184 C CB  . LEU   B 119 ? 0.7687 1.0310 0.3855 0.4344  0.0372  0.1129  128 LEU   B CB  
1185 C CG  . LEU   B 119 ? 0.8076 1.0517 0.3945 0.4660  0.0202  0.0944  128 LEU   B CG  
1186 C CD1 . LEU   B 119 ? 0.8301 1.0286 0.4170 0.4580  0.0107  0.0810  128 LEU   B CD1 
1187 C CD2 . LEU   B 119 ? 0.8115 1.0921 0.3783 0.5003  0.0234  0.1028  128 LEU   B CD2 
1188 N N   . ASP   B 120 ? 0.7344 1.0872 0.3991 0.4011  0.0746  0.1654  129 ASP   B N   
1189 C CA  . ASP   B 120 ? 0.7241 1.0919 0.4190 0.3697  0.0878  0.1845  129 ASP   B CA  
1190 C C   . ASP   B 120 ? 0.7234 1.0579 0.4308 0.3487  0.0921  0.1902  129 ASP   B C   
1191 O O   . ASP   B 120 ? 0.7212 1.0610 0.4229 0.3590  0.0982  0.2028  129 ASP   B O   
1192 C CB  . ASP   B 120 ? 0.7300 1.1587 0.4312 0.3787  0.1012  0.2086  129 ASP   B CB  
1193 C CG  . ASP   B 120 ? 0.7917 1.2568 0.4818 0.4007  0.0970  0.2024  129 ASP   B CG  
1194 O OD1 . ASP   B 120 ? 0.8032 1.2570 0.4985 0.3900  0.0891  0.1890  129 ASP   B OD1 
1195 O OD2 . ASP   B 120 ? 0.8150 1.3196 0.4890 0.4308  0.1011  0.2102  129 ASP   B OD2 
1196 N N   . TYR   B 121 ? 0.7218 1.0227 0.4452 0.3206  0.0890  0.1812  130 TYR   B N   
1197 C CA  . TYR   B 121 ? 0.7317 0.9979 0.4673 0.3006  0.0917  0.1837  130 TYR   B CA  
1198 C C   . TYR   B 121 ? 0.7100 0.9695 0.4722 0.2661  0.0957  0.1881  130 TYR   B C   
1199 O O   . TYR   B 121 ? 0.7101 0.9794 0.4781 0.2575  0.0924  0.1810  130 TYR   B O   
1200 C CB  . TYR   B 121 ? 0.7613 0.9826 0.4840 0.3066  0.0801  0.1610  130 TYR   B CB  
1201 C CG  . TYR   B 121 ? 0.7900 1.0104 0.4902 0.3364  0.0758  0.1584  130 TYR   B CG  
1202 C CD1 . TYR   B 121 ? 0.8128 1.0196 0.5129 0.3385  0.0792  0.1660  130 TYR   B CD1 
1203 C CD2 . TYR   B 121 ? 0.8117 1.0442 0.4894 0.3638  0.0670  0.1478  130 TYR   B CD2 
1204 C CE1 . TYR   B 121 ? 0.8372 1.0458 0.5156 0.3673  0.0746  0.1638  130 TYR   B CE1 
1205 C CE2 . TYR   B 121 ? 0.8346 1.0678 0.4903 0.3927  0.0618  0.1447  130 TYR   B CE2 
1206 C CZ  . TYR   B 121 ? 0.8532 1.0756 0.5096 0.3942  0.0657  0.1527  130 TYR   B CZ  
1207 O OH  . TYR   B 121 ? 0.8850 1.1083 0.5184 0.4238  0.0592  0.1485  130 TYR   B OH  
1208 N N   . PRO   B 122 ? 0.6887 0.9285 0.4658 0.2468  0.1012  0.1982  131 PRO   B N   
1209 C CA  . PRO   B 122 ? 0.6669 0.8948 0.4675 0.2146  0.1024  0.1992  131 PRO   B CA  
1210 C C   . PRO   B 122 ? 0.6574 0.8537 0.4557 0.2059  0.0927  0.1743  131 PRO   B C   
1211 O O   . PRO   B 122 ? 0.6763 0.8491 0.4585 0.2197  0.0861  0.1583  131 PRO   B O   
1212 C CB  . PRO   B 122 ? 0.6807 0.8843 0.4911 0.2020  0.1075  0.2116  131 PRO   B CB  
1213 C CG  . PRO   B 122 ? 0.6912 0.9068 0.4857 0.2268  0.1120  0.2238  131 PRO   B CG  
1214 C CD  . PRO   B 122 ? 0.6831 0.9071 0.4546 0.2546  0.1049  0.2075  131 PRO   B CD  
1215 N N   . ALA   B 123 ? 0.6251 0.8216 0.4393 0.1827  0.0916  0.1715  132 ALA   B N   
1216 C CA  . ALA   B 123 ? 0.6171 0.7869 0.4281 0.1738  0.0836  0.1497  132 ALA   B CA  
1217 C C   . ALA   B 123 ? 0.6185 0.7442 0.4247 0.1715  0.0805  0.1363  132 ALA   B C   
1218 O O   . ALA   B 123 ? 0.6273 0.7341 0.4241 0.1735  0.0742  0.1183  132 ALA   B O   
1219 C CB  . ALA   B 123 ? 0.6051 0.7817 0.4346 0.1487  0.0830  0.1505  132 ALA   B CB  
1220 N N   . GLY   B 124 ? 0.6044 0.7162 0.4167 0.1688  0.0851  0.1461  133 GLY   B N   
1221 C CA  . GLY   B 124 ? 0.6059 0.6802 0.4150 0.1693  0.0827  0.1351  133 GLY   B CA  
1222 C C   . GLY   B 124 ? 0.6006 0.6684 0.3919 0.1926  0.0783  0.1249  133 GLY   B C   
1223 O O   . GLY   B 124 ? 0.6082 0.6491 0.3979 0.1943  0.0756  0.1143  133 GLY   B O   
1224 N N   . THR   B 125 ? 0.5850 0.6780 0.3633 0.2116  0.0766  0.1275  134 THR   B N   
1225 C CA  . THR   B 125 ? 0.5872 0.6734 0.3477 0.2340  0.0696  0.1164  134 THR   B CA  
1226 C C   . THR   B 125 ? 0.5819 0.6530 0.3362 0.2312  0.0611  0.0964  134 THR   B C   
1227 O O   . THR   B 125 ? 0.5890 0.6473 0.3319 0.2444  0.0537  0.0849  134 THR   B O   
1228 C CB  . THR   B 125 ? 0.6017 0.7186 0.3483 0.2581  0.0705  0.1274  134 THR   B CB  
1229 O OG1 . THR   B 125 ? 0.6026 0.7348 0.3564 0.2571  0.0801  0.1487  134 THR   B OG1 
1230 C CG2 . THR   B 125 ? 0.6182 0.7255 0.3458 0.2826  0.0618  0.1162  134 THR   B CG2 
1231 N N   . SER   B 126 ? 0.5688 0.6408 0.3308 0.2131  0.0617  0.0930  135 SER   B N   
1232 C CA  . SER   B 126 ? 0.5741 0.6337 0.3304 0.2074  0.0553  0.0777  135 SER   B CA  
1233 C C   . SER   B 126 ? 0.5805 0.6109 0.3355 0.2051  0.0514  0.0635  135 SER   B C   
1234 O O   . SER   B 126 ? 0.5809 0.5964 0.3470 0.1934  0.0554  0.0617  135 SER   B O   
1235 C CB  . SER   B 126 ? 0.5857 0.6483 0.3532 0.1859  0.0581  0.0780  135 SER   B CB  
1236 O OG  . SER   B 126 ? 0.6053 0.6987 0.3773 0.1854  0.0610  0.0904  135 SER   B OG  
1237 N N   . GLY   B 127 ? 0.5814 0.6041 0.3237 0.2152  0.0431  0.0532  136 GLY   B N   
1238 C CA  . GLY   B 127 ? 0.5927 0.5924 0.3354 0.2126  0.0388  0.0406  136 GLY   B CA  
1239 C C   . GLY   B 127 ? 0.6040 0.5997 0.3391 0.2316  0.0319  0.0374  136 GLY   B C   
1240 O O   . GLY   B 127 ? 0.6135 0.5935 0.3489 0.2309  0.0258  0.0265  136 GLY   B O   
1241 N N   . SER   B 128 ? 0.5975 0.6093 0.3262 0.2486  0.0325  0.0470  137 SER   B N   
1242 C CA  . SER   B 128 ? 0.6065 0.6171 0.3250 0.2699  0.0250  0.0440  137 SER   B CA  
1243 C C   . SER   B 128 ? 0.6242 0.6258 0.3281 0.2797  0.0118  0.0322  137 SER   B C   
1244 O O   . SER   B 128 ? 0.6204 0.6285 0.3144 0.2821  0.0091  0.0328  137 SER   B O   
1245 C CB  . SER   B 128 ? 0.6082 0.6421 0.3194 0.2869  0.0293  0.0582  137 SER   B CB  
1246 O OG  . SER   B 128 ? 0.6136 0.6508 0.3378 0.2782  0.0400  0.0703  137 SER   B OG  
1247 N N   . PRO   B 129 ? 0.6387 0.6242 0.3416 0.2851  0.0023  0.0212  138 PRO   B N   
1248 C CA  . PRO   B 129 ? 0.6511 0.6225 0.3412 0.2919  -0.0123 0.0098  138 PRO   B CA  
1249 C C   . PRO   B 129 ? 0.6648 0.6442 0.3330 0.3188  -0.0221 0.0092  138 PRO   B C   
1250 O O   . PRO   B 129 ? 0.6634 0.6580 0.3256 0.3367  -0.0203 0.0150  138 PRO   B O   
1251 C CB  . PRO   B 129 ? 0.6616 0.6166 0.3616 0.2879  -0.0193 -0.0007 138 PRO   B CB  
1252 C CG  . PRO   B 129 ? 0.6628 0.6280 0.3713 0.2940  -0.0120 0.0051  138 PRO   B CG  
1253 C CD  . PRO   B 129 ? 0.6336 0.6120 0.3483 0.2842  0.0033  0.0184  138 PRO   B CD  
1254 N N   . ILE   B 130 ? 0.6738 0.6414 0.3284 0.3228  -0.0333 0.0019  139 ILE   B N   
1255 C CA  . ILE   B 130 ? 0.6829 0.6515 0.3138 0.3496  -0.0463 -0.0029 139 ILE   B CA  
1256 C C   . ILE   B 130 ? 0.7060 0.6456 0.3331 0.3519  -0.0643 -0.0180 139 ILE   B C   
1257 O O   . ILE   B 130 ? 0.7065 0.6256 0.3439 0.3312  -0.0674 -0.0232 139 ILE   B O   
1258 C CB  . ILE   B 130 ? 0.6865 0.6599 0.3053 0.3519  -0.0471 -0.0005 139 ILE   B CB  
1259 C CG1 . ILE   B 130 ? 0.6822 0.6881 0.3090 0.3476  -0.0299 0.0147  139 ILE   B CG1 
1260 C CG2 . ILE   B 130 ? 0.7012 0.6701 0.2934 0.3810  -0.0634 -0.0087 139 ILE   B CG2 
1261 C CD1 . ILE   B 130 ? 0.6983 0.7076 0.3226 0.3387  -0.0283 0.0169  139 ILE   B CD1 
1262 N N   . LEU   B 131 ? 0.7218 0.6613 0.3358 0.3759  -0.0757 -0.0246 140 LEU   B N   
1263 C CA  . LEU   B 131 ? 0.7466 0.6604 0.3596 0.3780  -0.0943 -0.0394 140 LEU   B CA  
1264 C C   . LEU   B 131 ? 0.7802 0.6768 0.3671 0.4010  -0.1155 -0.0514 140 LEU   B C   
1265 O O   . LEU   B 131 ? 0.7845 0.6959 0.3499 0.4261  -0.1165 -0.0493 140 LEU   B O   
1266 C CB  . LEU   B 131 ? 0.7439 0.6674 0.3646 0.3867  -0.0938 -0.0406 140 LEU   B CB  
1267 C CG  . LEU   B 131 ? 0.7463 0.6850 0.3900 0.3698  -0.0748 -0.0298 140 LEU   B CG  
1268 C CD1 . LEU   B 131 ? 0.7483 0.6924 0.3957 0.3822  -0.0784 -0.0328 140 LEU   B CD1 
1269 C CD2 . LEU   B 131 ? 0.7474 0.6735 0.4133 0.3382  -0.0690 -0.0307 140 LEU   B CD2 
1270 N N   . ASP   B 132 ? 0.7999 0.6655 0.3889 0.3931  -0.1334 -0.0641 141 ASP   B N   
1271 C CA  . ASP   B 132 ? 0.8333 0.6758 0.3976 0.4152  -0.1576 -0.0781 141 ASP   B CA  
1272 C C   . ASP   B 132 ? 0.8544 0.6979 0.4161 0.4333  -0.1702 -0.0887 141 ASP   B C   
1273 O O   . ASP   B 132 ? 0.8398 0.7016 0.4197 0.4265  -0.1589 -0.0835 141 ASP   B O   
1274 C CB  . ASP   B 132 ? 0.8631 0.6678 0.4285 0.3967  -0.1721 -0.0851 141 ASP   B CB  
1275 C CG  . ASP   B 132 ? 0.9187 0.7060 0.5095 0.3702  -0.1779 -0.0899 141 ASP   B CG  
1276 O OD1 . ASP   B 132 ? 0.9167 0.7193 0.5239 0.3690  -0.1741 -0.0913 141 ASP   B OD1 
1277 O OD2 . ASP   B 132 ? 0.9573 0.7169 0.5518 0.3510  -0.1863 -0.0916 141 ASP   B OD2 
1278 N N   . LYS   B 133 ? 0.8834 0.7063 0.4216 0.4570  -0.1946 -0.1041 142 LYS   B N   
1279 C CA  . LYS   B 133 ? 0.9052 0.7277 0.4369 0.4772  -0.2099 -0.1164 142 LYS   B CA  
1280 C C   . LYS   B 133 ? 0.9071 0.7212 0.4690 0.4533  -0.2144 -0.1213 142 LYS   B C   
1281 O O   . LYS   B 133 ? 0.9034 0.7306 0.4683 0.4655  -0.2176 -0.1256 142 LYS   B O   
1282 C CB  . LYS   B 133 ? 0.9614 0.7578 0.4611 0.5058  -0.2379 -0.1341 142 LYS   B CB  
1283 C CG  . LYS   B 133 ? 1.0419 0.8617 0.5097 0.5421  -0.2331 -0.1310 142 LYS   B CG  
1284 C CD  . LYS   B 133 ? 1.1404 0.9400 0.5844 0.5533  -0.2435 -0.1357 142 LYS   B CD  
1285 C CE  . LYS   B 133 ? 1.2076 1.0300 0.6167 0.5969  -0.2455 -0.1384 142 LYS   B CE  
1286 N NZ  . LYS   B 133 ? 1.2638 1.0649 0.6465 0.6136  -0.2594 -0.1463 142 LYS   B NZ  
1287 N N   . CYS   B 134 ? 0.9060 0.7028 0.4907 0.4198  -0.2127 -0.1192 143 CYS   B N   
1288 C CA  . CYS   B 134 ? 0.9053 0.7010 0.5220 0.3955  -0.2139 -0.1220 143 CYS   B CA  
1289 C C   . CYS   B 134 ? 0.8792 0.7060 0.5204 0.3801  -0.1867 -0.1078 143 CYS   B C   
1290 O O   . CYS   B 134 ? 0.8725 0.7048 0.5403 0.3637  -0.1855 -0.1098 143 CYS   B O   
1291 C CB  . CYS   B 134 ? 0.9389 0.7042 0.5694 0.3672  -0.2250 -0.1257 143 CYS   B CB  
1292 S SG  . CYS   B 134 ? 1.0659 0.7862 0.6692 0.3827  -0.2604 -0.1432 143 CYS   B SG  
1293 N N   . GLY   B 135 ? 0.8590 0.7057 0.4916 0.3858  -0.1663 -0.0941 144 GLY   B N   
1294 C CA  . GLY   B 135 ? 0.8383 0.7093 0.4907 0.3719  -0.1419 -0.0807 144 GLY   B CA  
1295 C C   . GLY   B 135 ? 0.8221 0.6889 0.4931 0.3404  -0.1284 -0.0731 144 GLY   B C   
1296 O O   . GLY   B 135 ? 0.8104 0.6931 0.5002 0.3261  -0.1102 -0.0646 144 GLY   B O   
1297 N N   . ARG   B 136 ? 0.8193 0.6631 0.4833 0.3305  -0.1379 -0.0764 145 ARG   B N   
1298 C CA  . ARG   B 136 ? 0.8102 0.6480 0.4873 0.3022  -0.1270 -0.0694 145 ARG   B CA  
1299 C C   . ARG   B 136 ? 0.7921 0.6439 0.4597 0.3031  -0.1095 -0.0573 145 ARG   B C   
1300 O O   . ARG   B 136 ? 0.8011 0.6565 0.4460 0.3244  -0.1125 -0.0560 145 ARG   B O   
1301 C CB  . ARG   B 136 ? 0.8440 0.6497 0.5154 0.2920  -0.1449 -0.0760 145 ARG   B CB  
1302 C CG  . ARG   B 136 ? 0.8882 0.6836 0.5815 0.2768  -0.1573 -0.0845 145 ARG   B CG  
1303 C CD  . ARG   B 136 ? 0.9509 0.7114 0.6376 0.2670  -0.1772 -0.0899 145 ARG   B CD  
1304 N NE  . ARG   B 136 ? 1.0151 0.7547 0.6748 0.2942  -0.2002 -0.1014 145 ARG   B NE  
1305 C CZ  . ARG   B 136 ? 1.0771 0.7835 0.7156 0.2978  -0.2167 -0.1049 145 ARG   B CZ  
1306 N NH1 . ARG   B 136 ? 1.0818 0.7724 0.7227 0.2752  -0.2118 -0.0961 145 ARG   B NH1 
1307 N NH2 . ARG   B 136 ? 1.0988 0.7872 0.7114 0.3258  -0.2383 -0.1174 145 ARG   B NH2 
1308 N N   . VAL   B 137 ? 0.7650 0.6271 0.4503 0.2809  -0.0915 -0.0490 146 VAL   B N   
1309 C CA  . VAL   B 137 ? 0.7508 0.6270 0.4306 0.2786  -0.0755 -0.0381 146 VAL   B CA  
1310 C C   . VAL   B 137 ? 0.7470 0.6072 0.4114 0.2743  -0.0809 -0.0370 146 VAL   B C   
1311 O O   . VAL   B 137 ? 0.7525 0.5979 0.4240 0.2538  -0.0815 -0.0372 146 VAL   B O   
1312 C CB  . VAL   B 137 ? 0.7486 0.6393 0.4505 0.2587  -0.0563 -0.0314 146 VAL   B CB  
1313 C CG1 . VAL   B 137 ? 0.7549 0.6601 0.4516 0.2569  -0.0420 -0.0209 146 VAL   B CG1 
1314 C CG2 . VAL   B 137 ? 0.7418 0.6449 0.4577 0.2648  -0.0530 -0.0329 146 VAL   B CG2 
1315 N N   . ILE   B 138 ? 0.7330 0.5970 0.3754 0.2955  -0.0855 -0.0358 147 ILE   B N   
1316 C CA  . ILE   B 138 ? 0.7277 0.5774 0.3524 0.2963  -0.0918 -0.0350 147 ILE   B CA  
1317 C C   . ILE   B 138 ? 0.7067 0.5764 0.3325 0.2885  -0.0751 -0.0241 147 ILE   B C   
1318 O O   . ILE   B 138 ? 0.7135 0.5755 0.3243 0.2907  -0.0793 -0.0227 147 ILE   B O   
1319 C CB  . ILE   B 138 ? 0.7400 0.5795 0.3380 0.3261  -0.1100 -0.0427 147 ILE   B CB  
1320 C CG1 . ILE   B 138 ? 0.7374 0.6084 0.3274 0.3509  -0.1031 -0.0387 147 ILE   B CG1 
1321 C CG2 . ILE   B 138 ? 0.7533 0.5654 0.3497 0.3295  -0.1303 -0.0553 147 ILE   B CG2 
1322 C CD1 . ILE   B 138 ? 0.7535 0.6244 0.3156 0.3794  -0.1145 -0.0425 147 ILE   B CD1 
1323 N N   . GLY   B 139 ? 0.6766 0.5698 0.3198 0.2794  -0.0579 -0.0170 148 GLY   B N   
1324 C CA  . GLY   B 139 ? 0.6610 0.5728 0.3079 0.2702  -0.0436 -0.0077 148 GLY   B CA  
1325 C C   . GLY   B 139 ? 0.6398 0.5777 0.3009 0.2694  -0.0288 0.0000  148 GLY   B C   
1326 O O   . GLY   B 139 ? 0.6391 0.5824 0.3040 0.2799  -0.0292 -0.0007 148 GLY   B O   
1327 N N   . LEU   B 140 ? 0.6243 0.5770 0.2927 0.2569  -0.0165 0.0077  149 LEU   B N   
1328 C CA  . LEU   B 140 ? 0.6125 0.5869 0.2949 0.2535  -0.0031 0.0165  149 LEU   B CA  
1329 C C   . LEU   B 140 ? 0.6157 0.6166 0.2922 0.2635  0.0010  0.0260  149 LEU   B C   
1330 O O   . LEU   B 140 ? 0.6243 0.6285 0.2905 0.2654  -0.0028 0.0259  149 LEU   B O   
1331 C CB  . LEU   B 140 ? 0.6021 0.5727 0.3022 0.2288  0.0077  0.0171  149 LEU   B CB  
1332 C CG  . LEU   B 140 ? 0.6126 0.5640 0.3221 0.2171  0.0064  0.0087  149 LEU   B CG  
1333 C CD1 . LEU   B 140 ? 0.6115 0.5638 0.3363 0.1971  0.0181  0.0093  149 LEU   B CD1 
1334 C CD2 . LEU   B 140 ? 0.6092 0.5575 0.3224 0.2294  0.0016  0.0053  149 LEU   B CD2 
1335 N N   . TYR   B 141 ? 0.6055 0.6265 0.2890 0.2699  0.0089  0.0352  150 TYR   B N   
1336 C CA  . TYR   B 141 ? 0.6039 0.6567 0.2860 0.2793  0.0148  0.0471  150 TYR   B CA  
1337 C C   . TYR   B 141 ? 0.5952 0.6607 0.2967 0.2572  0.0271  0.0564  150 TYR   B C   
1338 O O   . TYR   B 141 ? 0.5975 0.6506 0.3125 0.2426  0.0327  0.0564  150 TYR   B O   
1339 C CB  . TYR   B 141 ? 0.6092 0.6745 0.2864 0.2996  0.0157  0.0527  150 TYR   B CB  
1340 C CG  . TYR   B 141 ? 0.6172 0.7189 0.2979 0.3070  0.0257  0.0691  150 TYR   B CG  
1341 C CD1 . TYR   B 141 ? 0.6275 0.7375 0.3236 0.2976  0.0369  0.0815  150 TYR   B CD1 
1342 C CD2 . TYR   B 141 ? 0.6314 0.7597 0.2993 0.3255  0.0235  0.0729  150 TYR   B CD2 
1343 C CE1 . TYR   B 141 ? 0.6359 0.7801 0.3360 0.3033  0.0464  0.0991  150 TYR   B CE1 
1344 C CE2 . TYR   B 141 ? 0.6345 0.8018 0.3071 0.3327  0.0336  0.0895  150 TYR   B CE2 
1345 C CZ  . TYR   B 141 ? 0.6457 0.8210 0.3349 0.3205  0.0454  0.1035  150 TYR   B CZ  
1346 O OH  . TYR   B 141 ? 0.6570 0.8718 0.3527 0.3248  0.0562  0.1226  150 TYR   B OH  
1347 N N   . GLY   B 142 ? 0.5887 0.6778 0.2914 0.2551  0.0298  0.0630  151 GLY   B N   
1348 C CA  . GLY   B 142 ? 0.5915 0.6925 0.3134 0.2333  0.0392  0.0711  151 GLY   B CA  
1349 C C   . GLY   B 142 ? 0.5990 0.7101 0.3221 0.2229  0.0376  0.0696  151 GLY   B C   
1350 O O   . GLY   B 142 ? 0.5896 0.7117 0.3291 0.2049  0.0437  0.0754  151 GLY   B O   
1351 N N   . ASN   B 143 ? 0.6105 0.7158 0.3161 0.2337  0.0283  0.0614  152 ASN   B N   
1352 C CA  . ASN   B 143 ? 0.6240 0.7398 0.3282 0.2266  0.0257  0.0601  152 ASN   B CA  
1353 C C   . ASN   B 143 ? 0.6364 0.7713 0.3238 0.2502  0.0184  0.0607  152 ASN   B C   
1354 O O   . ASN   B 143 ? 0.6506 0.7647 0.3180 0.2652  0.0085  0.0522  152 ASN   B O   
1355 C CB  . ASN   B 143 ? 0.6477 0.7326 0.3465 0.2118  0.0217  0.0491  152 ASN   B CB  
1356 C CG  . ASN   B 143 ? 0.6800 0.7765 0.3778 0.2034  0.0196  0.0484  152 ASN   B CG  
1357 O OD1 . ASN   B 143 ? 0.6727 0.8004 0.3821 0.2005  0.0229  0.0560  152 ASN   B OD1 
1358 N ND2 . ASN   B 143 ? 0.7042 0.7770 0.3887 0.1985  0.0138  0.0400  152 ASN   B ND2 
1359 N N   . GLY   B 144 ? 0.6290 0.8036 0.3254 0.2534  0.0226  0.0705  153 GLY   B N   
1360 C CA  . GLY   B 144 ? 0.6466 0.8460 0.3282 0.2781  0.0164  0.0713  153 GLY   B CA  
1361 C C   . GLY   B 144 ? 0.6469 0.8922 0.3427 0.2750  0.0208  0.0809  153 GLY   B C   
1362 O O   . GLY   B 144 ? 0.6434 0.8908 0.3517 0.2541  0.0218  0.0805  153 GLY   B O   
1363 N N   . VAL   B 145 ? 0.6462 0.9312 0.3407 0.2963  0.0233  0.0896  154 VAL   B N   
1364 C CA  . VAL   B 145 ? 0.6452 0.9811 0.3539 0.2964  0.0268  0.0991  154 VAL   B CA  
1365 C C   . VAL   B 145 ? 0.6421 1.0271 0.3659 0.3040  0.0383  0.1166  154 VAL   B C   
1366 O O   . VAL   B 145 ? 0.6424 1.0226 0.3590 0.3164  0.0423  0.1204  154 VAL   B O   
1367 C CB  . VAL   B 145 ? 0.6585 0.9998 0.3444 0.3205  0.0147  0.0898  154 VAL   B CB  
1368 C CG1 . VAL   B 145 ? 0.6591 1.0165 0.3246 0.3568  0.0115  0.0896  154 VAL   B CG1 
1369 C CG2 . VAL   B 145 ? 0.6554 1.0370 0.3563 0.3131  0.0147  0.0942  154 VAL   B CG2 
1370 N N   . VAL   B 146 ? 0.6334 1.0667 0.3794 0.2948  0.0438  0.1280  155 VAL   B N   
1371 C CA  . VAL   B 146 ? 0.6293 1.1173 0.3925 0.2999  0.0555  0.1473  155 VAL   B CA  
1372 C C   . VAL   B 146 ? 0.6396 1.1721 0.3896 0.3323  0.0515  0.1467  155 VAL   B C   
1373 O O   . VAL   B 146 ? 0.6387 1.1789 0.3860 0.3345  0.0430  0.1385  155 VAL   B O   
1374 C CB  . VAL   B 146 ? 0.6176 1.1307 0.4178 0.2656  0.0635  0.1611  155 VAL   B CB  
1375 C CG1 . VAL   B 146 ? 0.5962 1.1780 0.4167 0.2706  0.0742  0.1822  155 VAL   B CG1 
1376 C CG2 . VAL   B 146 ? 0.6354 1.1073 0.4464 0.2397  0.0685  0.1638  155 VAL   B CG2 
1377 N N   . ILE   B 147 ? 0.6529 1.2120 0.3911 0.3601  0.0565  0.1538  156 ILE   B N   
1378 C CA  . ILE   B 147 ? 0.6714 1.2731 0.3941 0.3955  0.0526  0.1519  156 ILE   B CA  
1379 C C   . ILE   B 147 ? 0.6685 1.3497 0.4189 0.3945  0.0659  0.1734  156 ILE   B C   
1380 O O   . ILE   B 147 ? 0.6579 1.3547 0.4395 0.3638  0.0770  0.1897  156 ILE   B O   
1381 C CB  . ILE   B 147 ? 0.6948 1.2738 0.3816 0.4317  0.0465  0.1421  156 ILE   B CB  
1382 C CG1 . ILE   B 147 ? 0.7022 1.2974 0.3929 0.4355  0.0597  0.1573  156 ILE   B CG1 
1383 C CG2 . ILE   B 147 ? 0.7322 1.2361 0.3966 0.4283  0.0322  0.1216  156 ILE   B CG2 
1384 C CD1 . ILE   B 147 ? 0.7315 1.3069 0.3863 0.4727  0.0527  0.1468  156 ILE   B CD1 
1385 N N   . LYS   B 148 ? 0.6751 1.4067 0.4155 0.4271  0.0640  0.1733  157 LYS   B N   
1386 C CA  . LYS   B 148 ? 0.6632 1.4784 0.4297 0.4300  0.0764  0.1934  157 LYS   B CA  
1387 C C   . LYS   B 148 ? 0.6574 1.5047 0.4464 0.4156  0.0952  0.2188  157 LYS   B C   
1388 O O   . LYS   B 148 ? 0.6320 1.5345 0.4565 0.3952  0.1060  0.2385  157 LYS   B O   
1389 C CB  . LYS   B 148 ? 0.6960 1.5549 0.4388 0.4773  0.0722  0.1877  157 LYS   B CB  
1390 C CG  . LYS   B 148 ? 0.7881 1.6209 0.5082 0.4946  0.0533  0.1652  157 LYS   B CG  
1391 C CD  . LYS   B 148 ? 0.8545 1.7304 0.5498 0.5445  0.0484  0.1591  157 LYS   B CD  
1392 C CE  . LYS   B 148 ? 0.8689 1.8403 0.5933 0.5499  0.0606  0.1772  157 LYS   B CE  
1393 N NZ  . LYS   B 148 ? 0.8796 1.8731 0.6226 0.5381  0.0528  0.1730  157 LYS   B NZ  
1394 N N   . ASN   B 149 ? 0.6754 1.4903 0.4442 0.4264  0.0984  0.2193  158 ASN   B N   
1395 C CA  . ASN   B 149 ? 0.6701 1.5119 0.4562 0.4149  0.1158  0.2444  158 ASN   B CA  
1396 C C   . ASN   B 149 ? 0.6694 1.4666 0.4782 0.3711  0.1197  0.2518  158 ASN   B C   
1397 O O   . ASN   B 149 ? 0.6670 1.4710 0.4850 0.3618  0.1321  0.2711  158 ASN   B O   
1398 C CB  . ASN   B 149 ? 0.7135 1.5549 0.4666 0.4523  0.1188  0.2445  158 ASN   B CB  
1399 C CG  . ASN   B 149 ? 0.8094 1.5821 0.5237 0.4735  0.1022  0.2174  158 ASN   B CG  
1400 O OD1 . ASN   B 149 ? 0.8450 1.6020 0.5396 0.4925  0.0875  0.1968  158 ASN   B OD1 
1401 N ND2 . ASN   B 149 ? 0.8349 1.5663 0.5376 0.4713  0.1036  0.2176  158 ASN   B ND2 
1402 N N   . GLY   B 150 ? 0.6655 1.4183 0.4817 0.3462  0.1091  0.2369  159 GLY   B N   
1403 C CA  . GLY   B 150 ? 0.6635 1.3718 0.4992 0.3068  0.1107  0.2401  159 GLY   B CA  
1404 C C   . GLY   B 150 ? 0.6819 1.3209 0.4942 0.3094  0.1057  0.2273  159 GLY   B C   
1405 O O   . GLY   B 150 ? 0.6946 1.2897 0.5184 0.2804  0.1045  0.2247  159 GLY   B O   
1406 N N   . SER   B 151 ? 0.6780 1.3076 0.4572 0.3451  0.1020  0.2182  160 SER   B N   
1407 C CA  A SER   B 151 ? 0.7005 1.2696 0.4561 0.3523  0.0957  0.2047  160 SER   B CA  
1408 C CA  B SER   B 151 ? 0.6997 1.2680 0.4577 0.3491  0.0963  0.2057  160 SER   B CA  
1409 C C   . SER   B 151 ? 0.7096 1.2211 0.4567 0.3405  0.0816  0.1812  160 SER   B C   
1410 O O   . SER   B 151 ? 0.7011 1.2198 0.4502 0.3380  0.0745  0.1724  160 SER   B O   
1411 C CB  A SER   B 151 ? 0.7271 1.3061 0.4496 0.3951  0.0925  0.1990  160 SER   B CB  
1412 C CB  B SER   B 151 ? 0.7245 1.3013 0.4522 0.3885  0.0959  0.2039  160 SER   B CB  
1413 O OG  A SER   B 151 ? 0.7854 1.3074 0.4848 0.4038  0.0835  0.1834  160 SER   B OG  
1414 O OG  B SER   B 151 ? 0.7644 1.3328 0.4643 0.4180  0.0821  0.1835  160 SER   B OG  
1415 N N   . TYR   B 152 ? 0.7070 1.1637 0.4442 0.3345  0.0775  0.1714  161 TYR   B N   
1416 C CA  . TYR   B 152 ? 0.7053 1.1088 0.4340 0.3238  0.0656  0.1508  161 TYR   B CA  
1417 C C   . TYR   B 152 ? 0.7063 1.0783 0.4022 0.3523  0.0535  0.1333  161 TYR   B C   
1418 O O   . TYR   B 152 ? 0.7158 1.0840 0.3987 0.3703  0.0546  0.1351  161 TYR   B O   
1419 C CB  . TYR   B 152 ? 0.7044 1.0700 0.4497 0.2928  0.0695  0.1520  161 TYR   B CB  
1420 C CG  . TYR   B 152 ? 0.7160 1.0440 0.4645 0.2716  0.0617  0.1367  161 TYR   B CG  
1421 C CD1 . TYR   B 152 ? 0.7142 1.0566 0.4832 0.2482  0.0631  0.1398  161 TYR   B CD1 
1422 C CD2 . TYR   B 152 ? 0.7407 1.0199 0.4730 0.2736  0.0534  0.1200  161 TYR   B CD2 
1423 C CE1 . TYR   B 152 ? 0.7300 1.0388 0.4994 0.2302  0.0564  0.1259  161 TYR   B CE1 
1424 C CE2 . TYR   B 152 ? 0.7549 1.0027 0.4893 0.2545  0.0479  0.1076  161 TYR   B CE2 
1425 C CZ  . TYR   B 152 ? 0.7546 1.0169 0.5061 0.2337  0.0497  0.1105  161 TYR   B CZ  
1426 O OH  . TYR   B 152 ? 0.7795 1.0123 0.5306 0.2166  0.0445  0.0983  161 TYR   B OH  
1427 N N   . VAL   B 153 ? 0.6904 1.0401 0.3724 0.3567  0.0410  0.1169  162 VAL   B N   
1428 C CA  . VAL   B 153 ? 0.6907 1.0038 0.3433 0.3790  0.0269  0.0994  162 VAL   B CA  
1429 C C   . VAL   B 153 ? 0.6814 0.9435 0.3357 0.3555  0.0202  0.0870  162 VAL   B C   
1430 O O   . VAL   B 153 ? 0.6750 0.9349 0.3357 0.3406  0.0181  0.0841  162 VAL   B O   
1431 C CB  . VAL   B 153 ? 0.6964 1.0293 0.3273 0.4096  0.0170  0.0925  162 VAL   B CB  
1432 C CG1 . VAL   B 153 ? 0.7248 1.0075 0.3272 0.4248  -0.0008 0.0726  162 VAL   B CG1 
1433 C CG2 . VAL   B 153 ? 0.6879 1.0701 0.3124 0.4385  0.0235  0.1030  162 VAL   B CG2 
1434 N N   . SER   B 154 ? 0.6762 0.9012 0.3267 0.3513  0.0179  0.0807  163 SER   B N   
1435 C CA  . SER   B 154 ? 0.6760 0.8569 0.3301 0.3288  0.0135  0.0702  163 SER   B CA  
1436 C C   . SER   B 154 ? 0.6858 0.8310 0.3159 0.3420  -0.0024 0.0544  163 SER   B C   
1437 O O   . SER   B 154 ? 0.7004 0.8416 0.3117 0.3676  -0.0108 0.0490  163 SER   B O   
1438 C CB  . SER   B 154 ? 0.6761 0.8390 0.3433 0.3143  0.0204  0.0729  163 SER   B CB  
1439 O OG  . SER   B 154 ? 0.7066 0.8268 0.3709 0.3030  0.0138  0.0602  163 SER   B OG  
1440 N N   . ALA   B 155 ? 0.6760 0.7930 0.3065 0.3240  -0.0068 0.0471  164 ALA   B N   
1441 C CA  . ALA   B 155 ? 0.6874 0.7654 0.2976 0.3309  -0.0216 0.0340  164 ALA   B CA  
1442 C C   . ALA   B 155 ? 0.6867 0.7322 0.2996 0.3240  -0.0241 0.0276  164 ALA   B C   
1443 O O   . ALA   B 155 ? 0.6772 0.7280 0.3082 0.3107  -0.0136 0.0326  164 ALA   B O   
1444 C CB  . ALA   B 155 ? 0.6944 0.7573 0.3046 0.3126  -0.0236 0.0313  164 ALA   B CB  
1445 N N   . ILE   B 156 ? 0.6949 0.7066 0.2904 0.3328  -0.0388 0.0166  165 ILE   B N   
1446 C CA  . ILE   B 156 ? 0.7011 0.6828 0.3012 0.3239  -0.0430 0.0096  165 ILE   B CA  
1447 C C   . ILE   B 156 ? 0.7064 0.6641 0.3127 0.2980  -0.0423 0.0075  165 ILE   B C   
1448 O O   . ILE   B 156 ? 0.7194 0.6551 0.3098 0.3002  -0.0535 0.0029  165 ILE   B O   
1449 C CB  . ILE   B 156 ? 0.7215 0.6804 0.3003 0.3472  -0.0611 -0.0011 165 ILE   B CB  
1450 C CG1 . ILE   B 156 ? 0.7305 0.7172 0.2996 0.3766  -0.0612 0.0008  165 ILE   B CG1 
1451 C CG2 . ILE   B 156 ? 0.7299 0.6578 0.3167 0.3341  -0.0670 -0.0087 165 ILE   B CG2 
1452 C CD1 . ILE   B 156 ? 0.7573 0.7232 0.3027 0.4034  -0.0804 -0.0116 165 ILE   B CD1 
1453 N N   . THR   B 157 ? 0.6914 0.6541 0.3189 0.2746  -0.0292 0.0115  166 THR   B N   
1454 C CA  . THR   B 157 ? 0.6897 0.6352 0.3226 0.2509  -0.0264 0.0101  166 THR   B CA  
1455 C C   . THR   B 157 ? 0.6933 0.6129 0.3334 0.2383  -0.0291 0.0041  166 THR   B C   
1456 O O   . THR   B 157 ? 0.6791 0.6041 0.3357 0.2317  -0.0217 0.0040  166 THR   B O   
1457 C CB  . THR   B 157 ? 0.6850 0.6507 0.3352 0.2331  -0.0116 0.0164  166 THR   B CB  
1458 O OG1 . THR   B 157 ? 0.6871 0.6828 0.3368 0.2426  -0.0080 0.0233  166 THR   B OG1 
1459 C CG2 . THR   B 157 ? 0.6924 0.6446 0.3422 0.2136  -0.0095 0.0147  166 THR   B CG2 
1460 N N   . GLN   B 158 ? 0.7085 0.6011 0.3374 0.2336  -0.0392 0.0001  167 GLN   B N   
1461 C CA  . GLN   B 158 ? 0.7199 0.5909 0.3577 0.2191  -0.0418 -0.0043 167 GLN   B CA  
1462 C C   . GLN   B 158 ? 0.7477 0.6101 0.3882 0.1962  -0.0353 -0.0013 167 GLN   B C   
1463 O O   . GLN   B 158 ? 0.7510 0.6133 0.3787 0.1952  -0.0353 0.0023  167 GLN   B O   
1464 C CB  . GLN   B 158 ? 0.7353 0.5798 0.3593 0.2316  -0.0606 -0.0108 167 GLN   B CB  
1465 C CG  . GLN   B 158 ? 0.7550 0.5798 0.3915 0.2172  -0.0657 -0.0153 167 GLN   B CG  
1466 C CD  . GLN   B 158 ? 0.7576 0.5989 0.4168 0.2133  -0.0573 -0.0176 167 GLN   B CD  
1467 O OE1 . GLN   B 158 ? 0.7508 0.6105 0.4251 0.2016  -0.0415 -0.0138 167 GLN   B OE1 
1468 N NE2 . GLN   B 158 ? 0.7466 0.5798 0.4080 0.2232  -0.0688 -0.0246 167 GLN   B NE2 
1469 N N   . GLY   B 159 ? 0.7620 0.6209 0.4191 0.1793  -0.0292 -0.0028 168 GLY   B N   
1470 C CA  . GLY   B 159 ? 0.7860 0.6394 0.4458 0.1585  -0.0221 0.0000  168 GLY   B CA  
1471 C C   . GLY   B 159 ? 0.8304 0.6569 0.4834 0.1505  -0.0327 0.0005  168 GLY   B C   
1472 O O   . GLY   B 159 ? 0.8362 0.6450 0.4823 0.1611  -0.0476 -0.0029 168 GLY   B O   
1473 N N   . LYS   B 160 ? 0.8599 0.6827 0.5140 0.1317  -0.0256 0.0050  169 LYS   B N   
1474 C CA  . LYS   B 160 ? 0.8980 0.6960 0.5473 0.1201  -0.0341 0.0086  169 LYS   B CA  
1475 C C   . LYS   B 160 ? 0.9089 0.7150 0.5827 0.1029  -0.0267 0.0078  169 LYS   B C   
1476 O O   . LYS   B 160 ? 0.9007 0.7295 0.5882 0.0950  -0.0112 0.0072  169 LYS   B O   
1477 C CB  . LYS   B 160 ? 0.9373 0.7251 0.5671 0.1121  -0.0322 0.0167  169 LYS   B CB  
1478 C CG  . LYS   B 160 ? 1.0155 0.7684 0.6297 0.1084  -0.0475 0.0219  169 LYS   B CG  
1479 C CD  . LYS   B 160 ? 1.0790 0.8268 0.6966 0.0844  -0.0398 0.0313  169 LYS   B CD  
1480 C CE  . LYS   B 160 ? 1.1430 0.8531 0.7483 0.0778  -0.0556 0.0381  169 LYS   B CE  
1481 N NZ  . LYS   B 160 ? 1.1755 0.8829 0.7819 0.0540  -0.0466 0.0507  169 LYS   B NZ  
1482 N N   . ARG   B 161 ? 0.9252 0.7137 0.6055 0.0984  -0.0389 0.0068  170 ARG   B N   
1483 C CA  . ARG   B 161 ? 0.9279 0.7262 0.6338 0.0817  -0.0339 0.0066  170 ARG   B CA  
1484 C C   . ARG   B 161 ? 0.9533 0.7372 0.6555 0.0607  -0.0337 0.0172  170 ARG   B C   
1485 O O   . ARG   B 161 ? 0.9748 0.7279 0.6589 0.0612  -0.0482 0.0215  170 ARG   B O   
1486 C CB  . ARG   B 161 ? 0.9319 0.7229 0.6502 0.0895  -0.0487 -0.0016 170 ARG   B CB  
1487 C CG  . ARG   B 161 ? 0.9390 0.7387 0.6850 0.0712  -0.0476 -0.0015 170 ARG   B CG  
1488 C CD  . ARG   B 161 ? 0.9546 0.7633 0.7190 0.0813  -0.0556 -0.0121 170 ARG   B CD  
1489 N NE  . ARG   B 161 ? 0.9667 0.8006 0.7619 0.0658  -0.0460 -0.0125 170 ARG   B NE  
1490 C CZ  . ARG   B 161 ? 0.9749 0.8260 0.7908 0.0726  -0.0480 -0.0211 170 ARG   B CZ  
1491 N NH1 . ARG   B 161 ? 0.9794 0.8239 0.7874 0.0942  -0.0593 -0.0295 170 ARG   B NH1 
1492 N NH2 . ARG   B 161 ? 0.9485 0.8255 0.7923 0.0592  -0.0385 -0.0212 170 ARG   B NH2 
1493 N N   . GLU   B 162 ? 0.9519 0.7575 0.6691 0.0435  -0.0173 0.0219  171 GLU   B N   
1494 C CA  . GLU   B 162 ? 0.9749 0.7719 0.6887 0.0227  -0.0142 0.0344  171 GLU   B CA  
1495 C C   . GLU   B 162 ? 0.9710 0.7769 0.7134 0.0043  -0.0144 0.0370  171 GLU   B C   
1496 O O   . GLU   B 162 ? 0.9835 0.7663 0.7250 -0.0092 -0.0255 0.0453  171 GLU   B O   
1497 C CB  . GLU   B 162 ? 1.0114 0.8280 0.7164 0.0170  0.0049  0.0398  171 GLU   B CB  
1498 C CG  . GLU   B 162 ? 1.1138 0.9216 0.7911 0.0318  0.0035  0.0389  171 GLU   B CG  
1499 C CD  . GLU   B 162 ? 1.2473 1.0298 0.8974 0.0267  -0.0023 0.0507  171 GLU   B CD  
1500 O OE1 . GLU   B 162 ? 1.2800 1.0669 0.9107 0.0326  0.0034  0.0522  171 GLU   B OE1 
1501 O OE2 . GLU   B 162 ? 1.2858 1.0433 0.9340 0.0166  -0.0133 0.0586  171 GLU   B OE2 
1502 S S   . DMS   C .   ? 1.0756 0.9668 0.8350 0.0561  0.0574  -0.0731 201 DMS   B S   
1503 O O   . DMS   C .   ? 1.0730 0.9771 0.8239 0.0636  0.0649  -0.0709 201 DMS   B O   
1504 C C1  . DMS   C .   ? 1.0818 0.9482 0.8502 0.0623  0.0587  -0.0816 201 DMS   B C1  
1505 C C2  . DMS   C .   ? 1.0653 0.9621 0.8423 0.0533  0.0549  -0.0532 201 DMS   B C2  
1506 N N1  . A1B9A D .   ? 0.5554 0.8675 0.3674 0.2010  0.0840  0.1687  202 A1B9A B N1  
1507 N N3  . A1B9A D .   ? 0.5818 0.7465 0.3654 0.1610  0.0541  0.0928  202 A1B9A B N3  
1508 C C4  . A1B9A D .   ? 0.5803 0.7918 0.3746 0.1779  0.0650  0.1206  202 A1B9A B C4  
1509 C C5  . A1B9A D .   ? 0.5780 0.7728 0.3780 0.1575  0.0604  0.1092  202 A1B9A B C5  
1510 C C6  . A1B9A D .   ? 0.5738 0.7205 0.3559 0.1464  0.0496  0.0805  202 A1B9A B C6  
1511 C C7  . A1B9A D .   ? 0.5648 0.7098 0.3643 0.1236  0.0511  0.0809  202 A1B9A B C7  
1512 C C8  . A1B9A D .   ? 0.5669 0.6961 0.3623 0.1115  0.0463  0.0681  202 A1B9A B C8  
1513 C C10 . A1B9A D .   ? 0.5814 0.6985 0.3402 0.1422  0.0392  0.0583  202 A1B9A B C10 
1514 C C13 . A1B9A D .   ? 0.5829 0.6838 0.3468 0.1128  0.0364  0.0448  202 A1B9A B C13 
1515 C C15 . A1B9A D .   ? 0.5892 0.7909 0.3601 0.2140  0.0666  0.1236  202 A1B9A B C15 
1516 C C17 . A1B9A D .   ? 0.5902 0.7759 0.3390 0.2481  0.0669  0.1257  202 A1B9A B C17 
1517 C C1  . A1B9A D .   ? 0.5480 0.8927 0.3561 0.2200  0.0919  0.1858  202 A1B9A B C1  
1518 N N2  . A1B9A D .   ? 0.5476 0.8761 0.3794 0.1793  0.0833  0.1710  202 A1B9A B N2  
1519 C C2  . A1B9A D .   ? 0.5571 0.8503 0.3843 0.1684  0.0755  0.1528  202 A1B9A B C2  
1520 C C3  . A1B9A D .   ? 0.5711 0.8251 0.3777 0.1810  0.0718  0.1396  202 A1B9A B C3  
1521 O O1  . A1B9A D .   ? 0.5726 0.7828 0.3912 0.1391  0.0619  0.1152  202 A1B9A B O1  
1522 C C9  . A1B9A D .   ? 0.5750 0.6927 0.3497 0.1214  0.0411  0.0576  202 A1B9A B C9  
1523 C C11 . A1B9A D .   ? 0.5793 0.7116 0.3413 0.1557  0.0427  0.0687  202 A1B9A B C11 
1524 C C12 . A1B9A D .   ? 0.5896 0.6880 0.3279 0.1466  0.0325  0.0472  202 A1B9A B C12 
1525 N N4  . A1B9A D .   ? 0.5884 0.6899 0.3314 0.1301  0.0310  0.0426  202 A1B9A B N4  
1526 C C14 . A1B9A D .   ? 0.5915 0.7780 0.3695 0.1936  0.0631  0.1138  202 A1B9A B C14 
1527 C C16 . A1B9A D .   ? 0.5964 0.7725 0.3499 0.2314  0.0623  0.1148  202 A1B9A B C16 
1528 C C18 . A1B9A D .   ? 0.5926 0.7846 0.3259 0.2615  0.0581  0.1144  202 A1B9A B C18 
1529 N N5  . A1B9A D .   ? 0.5763 0.8176 0.3554 0.2189  0.0735  0.1413  202 A1B9A B N5  
1530 C C19 . A1B9A D .   ? 0.5675 0.8347 0.3653 0.2017  0.0766  0.1497  202 A1B9A B C19 
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