data_7HB8
# 
_entry.id   7HB8 
# 
_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   7HB8         pdb_00007hb8 10.2210/pdb7hb8/pdb 
WWPDB D_1001407255 ?            ?                   
# 
_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       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HB8 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_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.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
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 'Heat shock protein HSP 90-alpha'                                             26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-[(1R,2R,4S)-bicyclo[2.2.1]hept-5-en-2-yl]-N-methylthiophene-2-carboxamide' 233.329   1   ?        ? ? ? 
3 water       nat water                                                                         18.015    225 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-[(1R,2R,4S)-bicyclo[2.2.1]hept-5-en-2-yl]-N-methylthiophene-2-carboxamide' A1AXS 
3 water                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLN n 
1 4   PRO n 
1 5   MET n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   GLU n 
1 10  VAL n 
1 11  GLU n 
1 12  THR n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  GLN n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLN n 
1 22  LEU n 
1 23  MET n 
1 24  SER n 
1 25  LEU n 
1 26  ILE n 
1 27  ILE n 
1 28  ASN n 
1 29  THR n 
1 30  PHE n 
1 31  TYR n 
1 32  SER n 
1 33  ASN n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLU n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  ASN n 
1 45  SER n 
1 46  SER n 
1 47  ASP n 
1 48  ALA n 
1 49  LEU n 
1 50  ASP n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  TYR n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ASP n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  LEU n 
1 64  ASP n 
1 65  SER n 
1 66  GLY n 
1 67  LYS n 
1 68  GLU n 
1 69  LEU n 
1 70  HIS n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ILE n 
1 75  PRO n 
1 76  ASN n 
1 77  LYS n 
1 78  GLN n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  THR n 
1 84  ILE n 
1 85  VAL n 
1 86  ASP n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  GLY n 
1 91  MET n 
1 92  THR n 
1 93  LYS n 
1 94  ALA n 
1 95  ASP n 
1 96  LEU n 
1 97  ILE n 
1 98  ASN n 
1 99  ASN n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ILE n 
1 104 ALA n 
1 105 LYS n 
1 106 SER n 
1 107 GLY n 
1 108 THR n 
1 109 LYS n 
1 110 ALA n 
1 111 PHE n 
1 112 MET n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 GLN n 
1 117 ALA n 
1 118 GLY n 
1 119 ALA n 
1 120 ASP n 
1 121 ILE n 
1 122 SER n 
1 123 MET n 
1 124 ILE n 
1 125 GLY n 
1 126 GLN n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 GLY n 
1 131 PHE n 
1 132 TYR n 
1 133 SER n 
1 134 ALA n 
1 135 TYR n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 GLU n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 HIS n 
1 148 ASN n 
1 149 ASP n 
1 150 ASP n 
1 151 GLU n 
1 152 GLN n 
1 153 TYR n 
1 154 ALA n 
1 155 TRP n 
1 156 GLU n 
1 157 SER n 
1 158 SER n 
1 159 ALA n 
1 160 GLY n 
1 161 GLY n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 VAL n 
1 166 ARG n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 GLY n 
1 171 GLU n 
1 172 PRO n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 LEU n 
1 182 HIS n 
1 183 LEU n 
1 184 LYS n 
1 185 GLU n 
1 186 ASP n 
1 187 GLN n 
1 188 THR n 
1 189 GLU n 
1 190 TYR n 
1 191 LEU n 
1 192 GLU n 
1 193 GLU n 
1 194 ARG n 
1 195 ARG n 
1 196 ILE n 
1 197 LYS n 
1 198 GLU n 
1 199 ILE n 
1 200 VAL n 
1 201 LYS n 
1 202 LYS n 
1 203 HIS n 
1 204 SER n 
1 205 GLN n 
1 206 PHE n 
1 207 ILE n 
1 208 GLY n 
1 209 TYR n 
1 210 PRO n 
1 211 ILE n 
1 212 THR n 
1 213 LEU n 
1 214 PHE n 
1 215 VAL n 
1 216 GLU n 
1 217 LYS n 
1 218 GLU n 
1 219 ARG n 
1 220 ASP n 
1 221 LYS n 
1 222 GLU n 
1 223 VAL n 
1 224 SER n 
1 225 ASP n 
1 226 ASP n 
1 227 GLU n 
1 228 ALA n 
1 229 GLU n 
1 230 LEU n 
1 231 GLU n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   237 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90AA1, HSP90A, HSPC1, HSPCA' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1AXS non-polymer         . 'N-[(1R,2R,4S)-bicyclo[2.2.1]hept-5-en-2-yl]-N-methylthiophene-2-carboxamide' ? 'C13 H15 N O S'  
233.329 
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 
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   MET 1   8   ?   ?   ?   A . n 
A 1 2   ASP 2   9   ?   ?   ?   A . n 
A 1 3   GLN 3   10  ?   ?   ?   A . n 
A 1 4   PRO 4   11  ?   ?   ?   A . n 
A 1 5   MET 5   12  ?   ?   ?   A . n 
A 1 6   GLU 6   13  ?   ?   ?   A . n 
A 1 7   GLU 7   14  ?   ?   ?   A . n 
A 1 8   GLU 8   15  ?   ?   ?   A . n 
A 1 9   GLU 9   16  16  GLU GLU A . n 
A 1 10  VAL 10  17  17  VAL VAL A . n 
A 1 11  GLU 11  18  18  GLU GLU A . n 
A 1 12  THR 12  19  19  THR THR A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  ALA 14  21  21  ALA ALA A . n 
A 1 15  PHE 15  22  22  PHE PHE A . n 
A 1 16  GLN 16  23  23  GLN GLN A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  GLU 18  25  25  GLU GLU A . n 
A 1 19  ILE 19  26  26  ILE ILE A . n 
A 1 20  ALA 20  27  27  ALA ALA A . n 
A 1 21  GLN 21  28  28  GLN GLN A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  SER 24  31  31  SER SER A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  ILE 27  34  34  ILE ILE A . n 
A 1 28  ASN 28  35  35  ASN ASN A . n 
A 1 29  THR 29  36  36  THR THR A . n 
A 1 30  PHE 30  37  37  PHE PHE A . n 
A 1 31  TYR 31  38  38  TYR TYR A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ASN 33  40  40  ASN ASN A . n 
A 1 34  LYS 34  41  41  LYS LYS A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  PHE 37  44  44  PHE PHE A . n 
A 1 38  LEU 38  45  45  LEU LEU A . n 
A 1 39  ARG 39  46  46  ARG ARG A . n 
A 1 40  GLU 40  47  47  GLU GLU A . n 
A 1 41  LEU 41  48  48  LEU LEU A . n 
A 1 42  ILE 42  49  49  ILE ILE A . n 
A 1 43  SER 43  50  50  SER SER A . n 
A 1 44  ASN 44  51  51  ASN ASN A . n 
A 1 45  SER 45  52  52  SER SER A . n 
A 1 46  SER 46  53  53  SER SER A . n 
A 1 47  ASP 47  54  54  ASP ASP A . n 
A 1 48  ALA 48  55  55  ALA ALA A . n 
A 1 49  LEU 49  56  56  LEU LEU A . n 
A 1 50  ASP 50  57  57  ASP ASP A . n 
A 1 51  LYS 51  58  58  LYS LYS A . n 
A 1 52  ILE 52  59  59  ILE ILE A . n 
A 1 53  ARG 53  60  60  ARG ARG A . n 
A 1 54  TYR 54  61  61  TYR TYR A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  SER 56  63  63  SER SER A . n 
A 1 57  LEU 57  64  64  LEU LEU A . n 
A 1 58  THR 58  65  65  THR THR A . n 
A 1 59  ASP 59  66  66  ASP ASP A . n 
A 1 60  PRO 60  67  67  PRO PRO A . n 
A 1 61  SER 61  68  68  SER SER A . n 
A 1 62  LYS 62  69  69  LYS LYS A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ASP 64  71  71  ASP ASP A . n 
A 1 65  SER 65  72  72  SER SER A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  LYS 67  74  74  LYS LYS A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  LEU 69  76  76  LEU LEU A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  ILE 71  78  78  ILE ILE A . n 
A 1 72  ASN 72  79  79  ASN ASN A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  ILE 74  81  81  ILE ILE A . n 
A 1 75  PRO 75  82  82  PRO PRO A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  LYS 77  84  84  LYS LYS A . n 
A 1 78  GLN 78  85  85  GLN GLN A . n 
A 1 79  ASP 79  86  86  ASP ASP A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  THR 81  88  88  THR THR A . n 
A 1 82  LEU 82  89  89  LEU LEU A . n 
A 1 83  THR 83  90  90  THR THR A . n 
A 1 84  ILE 84  91  91  ILE ILE A . n 
A 1 85  VAL 85  92  92  VAL VAL A . n 
A 1 86  ASP 86  93  93  ASP ASP A . n 
A 1 87  THR 87  94  94  THR THR A . n 
A 1 88  GLY 88  95  95  GLY GLY A . n 
A 1 89  ILE 89  96  96  ILE ILE A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  MET 91  98  98  MET MET A . n 
A 1 92  THR 92  99  99  THR THR A . n 
A 1 93  LYS 93  100 100 LYS LYS A . n 
A 1 94  ALA 94  101 101 ALA ALA A . n 
A 1 95  ASP 95  102 102 ASP ASP A . n 
A 1 96  LEU 96  103 103 LEU LEU A . n 
A 1 97  ILE 97  104 104 ILE ILE A . n 
A 1 98  ASN 98  105 105 ASN ASN A . n 
A 1 99  ASN 99  106 106 ASN ASN A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 GLY 101 108 108 GLY GLY A . n 
A 1 102 THR 102 109 109 THR THR A . n 
A 1 103 ILE 103 110 110 ILE ILE A . n 
A 1 104 ALA 104 111 111 ALA ALA A . n 
A 1 105 LYS 105 112 112 LYS LYS A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 THR 108 115 115 THR THR A . n 
A 1 109 LYS 109 116 116 LYS LYS A . n 
A 1 110 ALA 110 117 117 ALA ALA A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 MET 112 119 119 MET MET A . n 
A 1 113 GLU 113 120 120 GLU GLU A . n 
A 1 114 ALA 114 121 121 ALA ALA A . n 
A 1 115 LEU 115 122 122 LEU LEU A . n 
A 1 116 GLN 116 123 123 GLN GLN A . n 
A 1 117 ALA 117 124 124 ALA ALA A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 ALA 119 126 126 ALA ALA A . n 
A 1 120 ASP 120 127 127 ASP ASP A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 SER 122 129 129 SER SER A . n 
A 1 123 MET 123 130 130 MET MET A . n 
A 1 124 ILE 124 131 131 ILE ILE A . n 
A 1 125 GLY 125 132 132 GLY GLY A . n 
A 1 126 GLN 126 133 133 GLN GLN A . n 
A 1 127 PHE 127 134 134 PHE PHE A . n 
A 1 128 GLY 128 135 135 GLY GLY A . n 
A 1 129 VAL 129 136 136 VAL VAL A . n 
A 1 130 GLY 130 137 137 GLY GLY A . n 
A 1 131 PHE 131 138 138 PHE PHE A . n 
A 1 132 TYR 132 139 139 TYR TYR A . n 
A 1 133 SER 133 140 140 SER SER A . n 
A 1 134 ALA 134 141 141 ALA ALA A . n 
A 1 135 TYR 135 142 142 TYR TYR A . n 
A 1 136 LEU 136 143 143 LEU LEU A . n 
A 1 137 VAL 137 144 144 VAL VAL A . n 
A 1 138 ALA 138 145 145 ALA ALA A . n 
A 1 139 GLU 139 146 146 GLU GLU A . n 
A 1 140 LYS 140 147 147 LYS LYS A . n 
A 1 141 VAL 141 148 148 VAL VAL A . n 
A 1 142 THR 142 149 149 THR THR A . n 
A 1 143 VAL 143 150 150 VAL VAL A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 THR 145 152 152 THR THR A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 HIS 147 154 154 HIS HIS A . n 
A 1 148 ASN 148 155 155 ASN ASN A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 ASP 150 157 157 ASP ASP A . n 
A 1 151 GLU 151 158 158 GLU GLU A . n 
A 1 152 GLN 152 159 159 GLN GLN A . n 
A 1 153 TYR 153 160 160 TYR TYR A . n 
A 1 154 ALA 154 161 161 ALA ALA A . n 
A 1 155 TRP 155 162 162 TRP TRP A . n 
A 1 156 GLU 156 163 163 GLU GLU A . n 
A 1 157 SER 157 164 164 SER SER A . n 
A 1 158 SER 158 165 165 SER SER A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 GLY 160 167 167 GLY GLY A . n 
A 1 161 GLY 161 168 168 GLY GLY A . n 
A 1 162 SER 162 169 169 SER SER A . n 
A 1 163 PHE 163 170 170 PHE PHE A . n 
A 1 164 THR 164 171 171 THR THR A . n 
A 1 165 VAL 165 172 172 VAL VAL A . n 
A 1 166 ARG 166 173 173 ARG ARG A . n 
A 1 167 THR 167 174 174 THR THR A . n 
A 1 168 ASP 168 175 175 ASP ASP A . n 
A 1 169 THR 169 176 176 THR THR A . n 
A 1 170 GLY 170 177 177 GLY GLY A . n 
A 1 171 GLU 171 178 178 GLU GLU A . n 
A 1 172 PRO 172 179 179 PRO PRO A . n 
A 1 173 MET 173 180 180 MET MET A . n 
A 1 174 GLY 174 181 181 GLY GLY A . n 
A 1 175 ARG 175 182 182 ARG ARG A . n 
A 1 176 GLY 176 183 183 GLY GLY A . n 
A 1 177 THR 177 184 184 THR THR A . n 
A 1 178 LYS 178 185 185 LYS LYS A . n 
A 1 179 VAL 179 186 186 VAL VAL A . n 
A 1 180 ILE 180 187 187 ILE ILE A . n 
A 1 181 LEU 181 188 188 LEU LEU A . n 
A 1 182 HIS 182 189 189 HIS HIS A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 GLU 185 192 192 GLU GLU A . n 
A 1 186 ASP 186 193 193 ASP ASP A . n 
A 1 187 GLN 187 194 194 GLN GLN A . n 
A 1 188 THR 188 195 195 THR THR A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 TYR 190 197 197 TYR TYR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLU 192 199 199 GLU GLU A . n 
A 1 193 GLU 193 200 200 GLU GLU A . n 
A 1 194 ARG 194 201 201 ARG ARG A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 ILE 196 203 203 ILE ILE A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 GLU 198 205 205 GLU GLU A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 VAL 200 207 207 VAL VAL A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 LYS 202 209 209 LYS LYS A . n 
A 1 203 HIS 203 210 210 HIS HIS A . n 
A 1 204 SER 204 211 211 SER SER A . n 
A 1 205 GLN 205 212 212 GLN GLN A . n 
A 1 206 PHE 206 213 213 PHE PHE A . n 
A 1 207 ILE 207 214 214 ILE ILE A . n 
A 1 208 GLY 208 215 215 GLY GLY A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 PRO 210 217 217 PRO PRO A . n 
A 1 211 ILE 211 218 218 ILE ILE A . n 
A 1 212 THR 212 219 219 THR THR A . n 
A 1 213 LEU 213 220 220 LEU LEU A . n 
A 1 214 PHE 214 221 221 PHE PHE A . n 
A 1 215 VAL 215 222 222 VAL VAL A . n 
A 1 216 GLU 216 223 223 GLU GLU A . n 
A 1 217 LYS 217 224 224 LYS LYS A . n 
A 1 218 GLU 218 225 225 GLU GLU A . n 
A 1 219 ARG 219 226 ?   ?   ?   A . n 
A 1 220 ASP 220 227 ?   ?   ?   A . n 
A 1 221 LYS 221 228 ?   ?   ?   A . n 
A 1 222 GLU 222 229 ?   ?   ?   A . n 
A 1 223 VAL 223 230 ?   ?   ?   A . n 
A 1 224 SER 224 231 ?   ?   ?   A . n 
A 1 225 ASP 225 232 ?   ?   ?   A . n 
A 1 226 ASP 226 233 ?   ?   ?   A . n 
A 1 227 GLU 227 234 ?   ?   ?   A . n 
A 1 228 ALA 228 235 ?   ?   ?   A . n 
A 1 229 GLU 229 236 ?   ?   ?   A . n 
A 1 230 LEU 230 237 ?   ?   ?   A . n 
A 1 231 GLU 231 238 ?   ?   ?   A . n 
A 1 232 HIS 232 239 ?   ?   ?   A . n 
A 1 233 HIS 233 240 ?   ?   ?   A . n 
A 1 234 HIS 234 241 ?   ?   ?   A . n 
A 1 235 HIS 235 242 ?   ?   ?   A . n 
A 1 236 HIS 236 243 ?   ?   ?   A . n 
A 1 237 HIS 237 244 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AXS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AXS 1   301 301 A1AXS B2G A . 
C 3 HOH   1   401 210 HOH   HOH A . 
C 3 HOH   2   402 113 HOH   HOH A . 
C 3 HOH   3   403 78  HOH   HOH A . 
C 3 HOH   4   404 40  HOH   HOH A . 
C 3 HOH   5   405 71  HOH   HOH A . 
C 3 HOH   6   406 80  HOH   HOH A . 
C 3 HOH   7   407 181 HOH   HOH A . 
C 3 HOH   8   408 56  HOH   HOH A . 
C 3 HOH   9   409 178 HOH   HOH A . 
C 3 HOH   10  410 35  HOH   HOH A . 
C 3 HOH   11  411 48  HOH   HOH A . 
C 3 HOH   12  412 38  HOH   HOH A . 
C 3 HOH   13  413 21  HOH   HOH A . 
C 3 HOH   14  414 69  HOH   HOH A . 
C 3 HOH   15  415 165 HOH   HOH A . 
C 3 HOH   16  416 100 HOH   HOH A . 
C 3 HOH   17  417 39  HOH   HOH A . 
C 3 HOH   18  418 67  HOH   HOH A . 
C 3 HOH   19  419 1   HOH   HOH A . 
C 3 HOH   20  420 27  HOH   HOH A . 
C 3 HOH   21  421 79  HOH   HOH A . 
C 3 HOH   22  422 45  HOH   HOH A . 
C 3 HOH   23  423 14  HOH   HOH A . 
C 3 HOH   24  424 32  HOH   HOH A . 
C 3 HOH   25  425 96  HOH   HOH A . 
C 3 HOH   26  426 98  HOH   HOH A . 
C 3 HOH   27  427 9   HOH   HOH A . 
C 3 HOH   28  428 47  HOH   HOH A . 
C 3 HOH   29  429 88  HOH   HOH A . 
C 3 HOH   30  430 163 HOH   HOH A . 
C 3 HOH   31  431 75  HOH   HOH A . 
C 3 HOH   32  432 42  HOH   HOH A . 
C 3 HOH   33  433 120 HOH   HOH A . 
C 3 HOH   34  434 123 HOH   HOH A . 
C 3 HOH   35  435 87  HOH   HOH A . 
C 3 HOH   36  436 214 HOH   HOH A . 
C 3 HOH   37  437 22  HOH   HOH A . 
C 3 HOH   38  438 187 HOH   HOH A . 
C 3 HOH   39  439 4   HOH   HOH A . 
C 3 HOH   40  440 3   HOH   HOH A . 
C 3 HOH   41  441 68  HOH   HOH A . 
C 3 HOH   42  442 25  HOH   HOH A . 
C 3 HOH   43  443 73  HOH   HOH A . 
C 3 HOH   44  444 58  HOH   HOH A . 
C 3 HOH   45  445 20  HOH   HOH A . 
C 3 HOH   46  446 218 HOH   HOH A . 
C 3 HOH   47  447 29  HOH   HOH A . 
C 3 HOH   48  448 136 HOH   HOH A . 
C 3 HOH   49  449 23  HOH   HOH A . 
C 3 HOH   50  450 139 HOH   HOH A . 
C 3 HOH   51  451 59  HOH   HOH A . 
C 3 HOH   52  452 41  HOH   HOH A . 
C 3 HOH   53  453 6   HOH   HOH A . 
C 3 HOH   54  454 202 HOH   HOH A . 
C 3 HOH   55  455 65  HOH   HOH A . 
C 3 HOH   56  456 7   HOH   HOH A . 
C 3 HOH   57  457 37  HOH   HOH A . 
C 3 HOH   58  458 171 HOH   HOH A . 
C 3 HOH   59  459 143 HOH   HOH A . 
C 3 HOH   60  460 154 HOH   HOH A . 
C 3 HOH   61  461 111 HOH   HOH A . 
C 3 HOH   62  462 18  HOH   HOH A . 
C 3 HOH   63  463 109 HOH   HOH A . 
C 3 HOH   64  464 194 HOH   HOH A . 
C 3 HOH   65  465 30  HOH   HOH A . 
C 3 HOH   66  466 197 HOH   HOH A . 
C 3 HOH   67  467 196 HOH   HOH A . 
C 3 HOH   68  468 13  HOH   HOH A . 
C 3 HOH   69  469 134 HOH   HOH A . 
C 3 HOH   70  470 156 HOH   HOH A . 
C 3 HOH   71  471 121 HOH   HOH A . 
C 3 HOH   72  472 76  HOH   HOH A . 
C 3 HOH   73  473 26  HOH   HOH A . 
C 3 HOH   74  474 220 HOH   HOH A . 
C 3 HOH   75  475 103 HOH   HOH A . 
C 3 HOH   76  476 24  HOH   HOH A . 
C 3 HOH   77  477 43  HOH   HOH A . 
C 3 HOH   78  478 12  HOH   HOH A . 
C 3 HOH   79  479 215 HOH   HOH A . 
C 3 HOH   80  480 62  HOH   HOH A . 
C 3 HOH   81  481 36  HOH   HOH A . 
C 3 HOH   82  482 91  HOH   HOH A . 
C 3 HOH   83  483 212 HOH   HOH A . 
C 3 HOH   84  484 90  HOH   HOH A . 
C 3 HOH   85  485 5   HOH   HOH A . 
C 3 HOH   86  486 112 HOH   HOH A . 
C 3 HOH   87  487 168 HOH   HOH A . 
C 3 HOH   88  488 176 HOH   HOH A . 
C 3 HOH   89  489 201 HOH   HOH A . 
C 3 HOH   90  490 15  HOH   HOH A . 
C 3 HOH   91  491 85  HOH   HOH A . 
C 3 HOH   92  492 19  HOH   HOH A . 
C 3 HOH   93  493 140 HOH   HOH A . 
C 3 HOH   94  494 55  HOH   HOH A . 
C 3 HOH   95  495 179 HOH   HOH A . 
C 3 HOH   96  496 157 HOH   HOH A . 
C 3 HOH   97  497 102 HOH   HOH A . 
C 3 HOH   98  498 101 HOH   HOH A . 
C 3 HOH   99  499 200 HOH   HOH A . 
C 3 HOH   100 500 8   HOH   HOH A . 
C 3 HOH   101 501 77  HOH   HOH A . 
C 3 HOH   102 502 225 HOH   HOH A . 
C 3 HOH   103 503 57  HOH   HOH A . 
C 3 HOH   104 504 132 HOH   HOH A . 
C 3 HOH   105 505 53  HOH   HOH A . 
C 3 HOH   106 506 105 HOH   HOH A . 
C 3 HOH   107 507 31  HOH   HOH A . 
C 3 HOH   108 508 106 HOH   HOH A . 
C 3 HOH   109 509 74  HOH   HOH A . 
C 3 HOH   110 510 97  HOH   HOH A . 
C 3 HOH   111 511 50  HOH   HOH A . 
C 3 HOH   112 512 60  HOH   HOH A . 
C 3 HOH   113 513 49  HOH   HOH A . 
C 3 HOH   114 514 44  HOH   HOH A . 
C 3 HOH   115 515 54  HOH   HOH A . 
C 3 HOH   116 516 137 HOH   HOH A . 
C 3 HOH   117 517 148 HOH   HOH A . 
C 3 HOH   118 518 211 HOH   HOH A . 
C 3 HOH   119 519 129 HOH   HOH A . 
C 3 HOH   120 520 33  HOH   HOH A . 
C 3 HOH   121 521 28  HOH   HOH A . 
C 3 HOH   122 522 155 HOH   HOH A . 
C 3 HOH   123 523 66  HOH   HOH A . 
C 3 HOH   124 524 117 HOH   HOH A . 
C 3 HOH   125 525 209 HOH   HOH A . 
C 3 HOH   126 526 70  HOH   HOH A . 
C 3 HOH   127 527 124 HOH   HOH A . 
C 3 HOH   128 528 16  HOH   HOH A . 
C 3 HOH   129 529 17  HOH   HOH A . 
C 3 HOH   130 530 191 HOH   HOH A . 
C 3 HOH   131 531 86  HOH   HOH A . 
C 3 HOH   132 532 72  HOH   HOH A . 
C 3 HOH   133 533 217 HOH   HOH A . 
C 3 HOH   134 534 127 HOH   HOH A . 
C 3 HOH   135 535 95  HOH   HOH A . 
C 3 HOH   136 536 162 HOH   HOH A . 
C 3 HOH   137 537 63  HOH   HOH A . 
C 3 HOH   138 538 216 HOH   HOH A . 
C 3 HOH   139 539 84  HOH   HOH A . 
C 3 HOH   140 540 206 HOH   HOH A . 
C 3 HOH   141 541 51  HOH   HOH A . 
C 3 HOH   142 542 183 HOH   HOH A . 
C 3 HOH   143 543 195 HOH   HOH A . 
C 3 HOH   144 544 34  HOH   HOH A . 
C 3 HOH   145 545 167 HOH   HOH A . 
C 3 HOH   146 546 81  HOH   HOH A . 
C 3 HOH   147 547 159 HOH   HOH A . 
C 3 HOH   148 548 170 HOH   HOH A . 
C 3 HOH   149 549 158 HOH   HOH A . 
C 3 HOH   150 550 208 HOH   HOH A . 
C 3 HOH   151 551 146 HOH   HOH A . 
C 3 HOH   152 552 61  HOH   HOH A . 
C 3 HOH   153 553 221 HOH   HOH A . 
C 3 HOH   154 554 207 HOH   HOH A . 
C 3 HOH   155 555 89  HOH   HOH A . 
C 3 HOH   156 556 107 HOH   HOH A . 
C 3 HOH   157 557 10  HOH   HOH A . 
C 3 HOH   158 558 160 HOH   HOH A . 
C 3 HOH   159 559 94  HOH   HOH A . 
C 3 HOH   160 560 223 HOH   HOH A . 
C 3 HOH   161 561 130 HOH   HOH A . 
C 3 HOH   162 562 110 HOH   HOH A . 
C 3 HOH   163 563 2   HOH   HOH A . 
C 3 HOH   164 564 11  HOH   HOH A . 
C 3 HOH   165 565 205 HOH   HOH A . 
C 3 HOH   166 566 182 HOH   HOH A . 
C 3 HOH   167 567 119 HOH   HOH A . 
C 3 HOH   168 568 46  HOH   HOH A . 
C 3 HOH   169 569 114 HOH   HOH A . 
C 3 HOH   170 570 108 HOH   HOH A . 
C 3 HOH   171 571 161 HOH   HOH A . 
C 3 HOH   172 572 83  HOH   HOH A . 
C 3 HOH   173 573 116 HOH   HOH A . 
C 3 HOH   174 574 125 HOH   HOH A . 
C 3 HOH   175 575 133 HOH   HOH A . 
C 3 HOH   176 576 135 HOH   HOH A . 
C 3 HOH   177 577 219 HOH   HOH A . 
C 3 HOH   178 578 172 HOH   HOH A . 
C 3 HOH   179 579 203 HOH   HOH A . 
C 3 HOH   180 580 147 HOH   HOH A . 
C 3 HOH   181 581 122 HOH   HOH A . 
C 3 HOH   182 582 204 HOH   HOH A . 
C 3 HOH   183 583 198 HOH   HOH A . 
C 3 HOH   184 584 145 HOH   HOH A . 
C 3 HOH   185 585 99  HOH   HOH A . 
C 3 HOH   186 586 190 HOH   HOH A . 
C 3 HOH   187 587 174 HOH   HOH A . 
C 3 HOH   188 588 64  HOH   HOH A . 
C 3 HOH   189 589 52  HOH   HOH A . 
C 3 HOH   190 590 173 HOH   HOH A . 
C 3 HOH   191 591 128 HOH   HOH A . 
C 3 HOH   192 592 138 HOH   HOH A . 
C 3 HOH   193 593 93  HOH   HOH A . 
C 3 HOH   194 594 177 HOH   HOH A . 
C 3 HOH   195 595 151 HOH   HOH A . 
C 3 HOH   196 596 150 HOH   HOH A . 
C 3 HOH   197 597 192 HOH   HOH A . 
C 3 HOH   198 598 175 HOH   HOH A . 
C 3 HOH   199 599 82  HOH   HOH A . 
C 3 HOH   200 600 186 HOH   HOH A . 
C 3 HOH   201 601 115 HOH   HOH A . 
C 3 HOH   202 602 184 HOH   HOH A . 
C 3 HOH   203 603 213 HOH   HOH A . 
C 3 HOH   204 604 104 HOH   HOH A . 
C 3 HOH   205 605 149 HOH   HOH A . 
C 3 HOH   206 606 126 HOH   HOH A . 
C 3 HOH   207 607 118 HOH   HOH A . 
C 3 HOH   208 608 199 HOH   HOH A . 
C 3 HOH   209 609 185 HOH   HOH A . 
C 3 HOH   210 610 92  HOH   HOH A . 
C 3 HOH   211 611 193 HOH   HOH A . 
C 3 HOH   212 612 188 HOH   HOH A . 
C 3 HOH   213 613 169 HOH   HOH A . 
C 3 HOH   214 614 141 HOH   HOH A . 
C 3 HOH   215 615 152 HOH   HOH A . 
C 3 HOH   216 616 164 HOH   HOH A . 
C 3 HOH   217 617 180 HOH   HOH A . 
C 3 HOH   218 618 131 HOH   HOH A . 
C 3 HOH   219 619 189 HOH   HOH A . 
C 3 HOH   220 620 144 HOH   HOH A . 
C 3 HOH   221 621 224 HOH   HOH A . 
C 3 HOH   222 622 166 HOH   HOH A . 
C 3 HOH   223 623 222 HOH   HOH A . 
C 3 HOH   224 624 142 HOH   HOH A . 
C 3 HOH   225 625 153 HOH   HOH A . 
# 
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 XDS         .           ?               package 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/     ?   ? 
2 Aimless     0.7.7       23/04/21        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 DIMPLE      .           ?               program 'Marcin Wojdyr'   wojdyr@gmail.com                        phasing           
http://ccp4.github.io/dimple/                       ?   ? 
4 PHENIX      1.20.1_4487 ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                       C++ ? 
5 PDB_EXTRACT 3.28        'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.volume             606820.246 
_cell.length_a           68.190 
_cell.length_b           90.180 
_cell.length_c           98.680 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HB8 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.entry_id                         7HB8 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HB8 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HB8 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             45.090 
_reflns.d_resolution_high            1.850 
_reflns.number_obs                   26332 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.097 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.500 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.900 
_reflns.pdbx_Rrim_I_all              0.101 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     340703 
_reflns.pdbx_scaling_rejects         19 
_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                      ? 
# 
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 
1 1 1.850 1.900  ? 25676 1925 ? 1.420 ? ? ? 13.300 ? 2.300  ? ? ? ? ? ? 100.000 1.476 0.401 0.817 
1 2 8.270 45.090 ? 3010  330  ? 0.031 ? ? ? 9.100  ? 45.700 ? ? ? ? ? ? 97.700  0.033 0.010 0.999 
# 
_refine.entry_id                                 7HB8 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.pdbx_overall_phase_error                 19.3752 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.1715 
_refine.B_iso_mean                               38.32 
_refine.ls_number_reflns_R_free                  1289 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_R_factor_R_work                       0.1706 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.85 
_refine.ls_number_reflns_obs                     26312 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  25023 
_refine.ls_d_res_low                             33.28 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1880 
_refine.overall_SU_ML                            0.1718 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1653 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.number_atoms_solvent             225 
_refine_hist.number_atoms_total               1894 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        33.28 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1697 0.0113 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2289 1.2316 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     263  0.0697 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      292  0.0079 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 237  6.5533 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.85 1.92  2752 0.2356 99.86  0.2476 143 . . . . . 
'X-RAY DIFFRACTION' 1.92 2.01  2723 0.2172 99.86  0.2367 153 . . . . . 
'X-RAY DIFFRACTION' 2.01 2.12  2693 0.1897 99.97  0.2273 173 . . . . . 
'X-RAY DIFFRACTION' 2.12 2.25  2780 0.1815 100.00 0.2059 124 . . . . . 
'X-RAY DIFFRACTION' 2.25 2.42  2797 0.1788 99.97  0.2136 122 . . . . . 
'X-RAY DIFFRACTION' 2.42 2.67  2761 0.1882 99.93  0.2171 148 . . . . . 
'X-RAY DIFFRACTION' 2.67 3.05  2787 0.1827 99.97  0.2122 142 . . . . . 
'X-RAY DIFFRACTION' 3.05 3.85  2818 0.1611 99.97  0.1634 132 . . . . . 
'X-RAY DIFFRACTION' 3.85 33.28 2912 0.1489 99.22  0.1595 152 . . . . . 
# 
_struct.entry_id                  7HB8 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13480' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HB8 
_struct_keywords.pdbx_keywords   CHAPERONE 
_struct_keywords.text            
'Crystallographic Fragment Screening; Fragment-Based Drug Discovery (FBDD); Heat shock protein 90 (HSP90), CHAPERONE' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HS90A_HUMAN 
_struct_ref.pdbx_db_accession          P07900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRT
LTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGG
SFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HB8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 229 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07900 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  236 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       236 
# 
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 7HB8 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HB8 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HB8 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HB8 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HB8 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HB8 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HB8 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HB8 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HB8 HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
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 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 GLN A 152 ? SER A 157 ? GLN A 159 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
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 PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HB8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  A HOH 586 ? ? O A HOH 611 ? ? 1.88 
2 1 O  A HOH 467 ? ? O A HOH 597 ? ? 1.96 
3 1 O  A HOH 551 ? ? O A HOH 562 ? ? 2.03 
4 1 O  A HOH 455 ? ? O A HOH 570 ? ? 2.07 
5 1 O  A HOH 539 ? ? O A HOH 596 ? ? 2.07 
6 1 NE A ARG 201 ? ? O A HOH 401 ? ? 2.14 
7 1 O  A HOH 540 ? ? O A HOH 587 ? ? 2.17 
# 
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 TYR A 38  ? ? -160.60 107.01  
2 1 THR A 94  ? ? -102.31 41.03   
3 1 ASN A 105 ? ? -134.66 -46.78  
4 1 ALA A 166 ? ? 62.41   -147.59 
5 1 ARG A 182 ? ? -173.18 136.69  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 13.4671267161   -17.7801994689 -17.9965649957 0.240390401111 0.263005626177 0.250560318824 
0.0281524222702    -0.0491118533055 -0.0137686410943 2.1617249648  1.88451827389 5.26922060631 -0.689898749438 -1.4842172145   
0.66891434374   -0.0126882604873 -0.188020176245 -0.0448185616313 0.0874752004199  0.0279359178513  -0.110432697415 0.127735035593 
0.473174834886  -0.0165616339616 
2 ? 'X-RAY DIFFRACTION' refined -6.60255656592  -6.62917783985 -25.6298809705 0.207599479072 0.207278426793 0.221723021096 
0.00715979660782   -0.0251808411896 -0.0090148535013 1.61031272998 2.41591180678 3.92691976619 -0.729611851039 0.552295556025  
-1.21819151291  -0.0413522692309 0.238978994043  0.157327432509   -0.0704009737996 -0.0677808822748 0.110956554633  
-0.305052368386  -0.078806732996 0.0289374984336  
3 ? 'X-RAY DIFFRACTION' refined -3.50847846251  -18.4025314606 -23.6506942469 0.260228566538 0.204115607983 0.210024469135 
-0.0174319223876   -0.0540087723135 -0.0568324919125 2.36162120434 3.14778253966 3.12699847022 -1.04458236718  -0.97146321451  
-0.650040424373 -0.0241293751186 0.081188011925  -0.0686746179758 0.0204051828377  0.117695748443   0.0888859862725 0.279958880503 
-0.153837601783 -0.0266474682425 
4 ? 'X-RAY DIFFRACTION' refined 12.7204907524   -6.07624406596 -14.9225910449 0.236578546234 0.298934685459 0.343996408701 
-0.000771413922108 -0.0466152618492 -0.0388546196173 3.65373399664 4.14302470144 9.05534449042 0.0451903681621 -2.40825431885  
0.210770623255  0.180461840948   -0.619817680191 0.388464839155   0.525566633085   -0.101624854891  -0.307753709148 
0.00342959210477 0.557185272171  0.0145214935252  
5 ? 'X-RAY DIFFRACTION' refined -0.412634811084 -19.8624953391 -20.8616418466 0.233444550469 0.174096123204 0.240007565067 
-0.0118270139851   -0.0215270904075 -0.0101320265532 2.46331984721 1.25407776933 2.41495318676 -0.348664728635 -0.510492676299 
0.121794317617  -0.0347646738817 0.0289941281449 -0.194016638068  -0.0446134969545 -0.0306823968462 0.0459119572762 0.310433914149 
-0.044484843308 0.0386570692163  
6 ? 'X-RAY DIFFRACTION' refined -13.4123169558  -14.8755150906 -15.5906083982 0.229234703878 0.328490510957 0.26687837473  
0.00410374801351   0.0223445084827  0.0460745831736  4.06341441866 4.66178150605 3.27353433505 1.07229057958   -0.108133440931 
0.339157594746  0.0941800156938  -0.447573370451 -0.235669062889  0.627925439094   -0.0488065467713 0.0744739214803 
-0.167922928207  -0.214483755593 -0.0295012970771 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4 4 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 210 A 195 . 
;chain 'A' and (resid 137 through 210 )
;
6 6 'X-RAY DIFFRACTION' A 211 A 196 A 225 A 210 . 
;chain 'A' and (resid 211 through 225 )
;
# 
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 MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A ARG 226 ? A ARG 219 
10 1 Y 1 A ASP 227 ? A ASP 220 
11 1 Y 1 A LYS 228 ? A LYS 221 
12 1 Y 1 A GLU 229 ? A GLU 222 
13 1 Y 1 A VAL 230 ? A VAL 223 
14 1 Y 1 A SER 231 ? A SER 224 
15 1 Y 1 A ASP 232 ? A ASP 225 
16 1 Y 1 A ASP 233 ? A ASP 226 
17 1 Y 1 A GLU 234 ? A GLU 227 
18 1 Y 1 A ALA 235 ? A ALA 228 
19 1 Y 1 A GLU 236 ? A GLU 229 
20 1 Y 1 A LEU 237 ? A LEU 230 
21 1 Y 1 A GLU 238 ? A GLU 231 
22 1 Y 1 A HIS 239 ? A HIS 232 
23 1 Y 1 A HIS 240 ? A HIS 233 
24 1 Y 1 A HIS 241 ? A HIS 234 
25 1 Y 1 A HIS 242 ? A HIS 235 
26 1 Y 1 A HIS 243 ? A HIS 236 
27 1 Y 1 A HIS 244 ? A HIS 237 
# 
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 
A1AXS C1   C N N 1   
A1AXS C10  C N N 2   
A1AXS C11  C N N 3   
A1AXS C12  C N R 4   
A1AXS C13  C N N 5   
A1AXS C2   C N N 6   
A1AXS C3   C Y N 7   
A1AXS C4   C Y N 8   
A1AXS C5   C Y N 9   
A1AXS C6   C Y N 10  
A1AXS C7   C N R 11  
A1AXS C8   C N N 12  
A1AXS C9   C N R 13  
A1AXS N1   N N N 14  
A1AXS O1   O N N 15  
A1AXS S1   S Y N 16  
A1AXS H13  H N N 17  
A1AXS H14  H N N 18  
A1AXS H15  H N N 19  
A1AXS H10  H N N 20  
A1AXS H11  H N N 21  
A1AXS H12  H N N 22  
A1AXS H132 H N N 23  
A1AXS H133 H N N 24  
A1AXS H4   H N N 25  
A1AXS H5   H N N 26  
A1AXS H6   H N N 27  
A1AXS H7   H N N 28  
A1AXS H82  H N N 29  
A1AXS H83  H N N 30  
A1AXS H9   H N N 31  
ALA   N    N N N 32  
ALA   CA   C N S 33  
ALA   C    C N N 34  
ALA   O    O N N 35  
ALA   CB   C N N 36  
ALA   OXT  O N N 37  
ALA   H    H N N 38  
ALA   H2   H N N 39  
ALA   HA   H N N 40  
ALA   HB1  H N N 41  
ALA   HB2  H N N 42  
ALA   HB3  H N N 43  
ALA   HXT  H N N 44  
ARG   N    N N N 45  
ARG   CA   C N S 46  
ARG   C    C N N 47  
ARG   O    O N N 48  
ARG   CB   C N N 49  
ARG   CG   C N N 50  
ARG   CD   C N N 51  
ARG   NE   N N N 52  
ARG   CZ   C N N 53  
ARG   NH1  N N N 54  
ARG   NH2  N N N 55  
ARG   OXT  O N N 56  
ARG   H    H N N 57  
ARG   H2   H N N 58  
ARG   HA   H N N 59  
ARG   HB2  H N N 60  
ARG   HB3  H N N 61  
ARG   HG2  H N N 62  
ARG   HG3  H N N 63  
ARG   HD2  H N N 64  
ARG   HD3  H N N 65  
ARG   HE   H N N 66  
ARG   HH11 H N N 67  
ARG   HH12 H N N 68  
ARG   HH21 H N N 69  
ARG   HH22 H N N 70  
ARG   HXT  H N N 71  
ASN   N    N N N 72  
ASN   CA   C N S 73  
ASN   C    C N N 74  
ASN   O    O N N 75  
ASN   CB   C N N 76  
ASN   CG   C N N 77  
ASN   OD1  O N N 78  
ASN   ND2  N N N 79  
ASN   OXT  O N N 80  
ASN   H    H N N 81  
ASN   H2   H N N 82  
ASN   HA   H N N 83  
ASN   HB2  H N N 84  
ASN   HB3  H N N 85  
ASN   HD21 H N N 86  
ASN   HD22 H N N 87  
ASN   HXT  H N N 88  
ASP   N    N N N 89  
ASP   CA   C N S 90  
ASP   C    C N N 91  
ASP   O    O N N 92  
ASP   CB   C N N 93  
ASP   CG   C N N 94  
ASP   OD1  O N N 95  
ASP   OD2  O N N 96  
ASP   OXT  O N N 97  
ASP   H    H N N 98  
ASP   H2   H N N 99  
ASP   HA   H N N 100 
ASP   HB2  H N N 101 
ASP   HB3  H N N 102 
ASP   HD2  H N N 103 
ASP   HXT  H N N 104 
GLN   N    N N N 105 
GLN   CA   C N S 106 
GLN   C    C N N 107 
GLN   O    O N N 108 
GLN   CB   C N N 109 
GLN   CG   C N N 110 
GLN   CD   C N N 111 
GLN   OE1  O N N 112 
GLN   NE2  N N N 113 
GLN   OXT  O N N 114 
GLN   H    H N N 115 
GLN   H2   H N N 116 
GLN   HA   H N N 117 
GLN   HB2  H N N 118 
GLN   HB3  H N N 119 
GLN   HG2  H N N 120 
GLN   HG3  H N N 121 
GLN   HE21 H N N 122 
GLN   HE22 H N N 123 
GLN   HXT  H N N 124 
GLU   N    N N N 125 
GLU   CA   C N S 126 
GLU   C    C N N 127 
GLU   O    O N N 128 
GLU   CB   C N N 129 
GLU   CG   C N N 130 
GLU   CD   C N N 131 
GLU   OE1  O N N 132 
GLU   OE2  O N N 133 
GLU   OXT  O N N 134 
GLU   H    H N N 135 
GLU   H2   H N N 136 
GLU   HA   H N N 137 
GLU   HB2  H N N 138 
GLU   HB3  H N N 139 
GLU   HG2  H N N 140 
GLU   HG3  H N N 141 
GLU   HE2  H N N 142 
GLU   HXT  H N N 143 
GLY   N    N N N 144 
GLY   CA   C N N 145 
GLY   C    C N N 146 
GLY   O    O N N 147 
GLY   OXT  O N N 148 
GLY   H    H N N 149 
GLY   H2   H N N 150 
GLY   HA2  H N N 151 
GLY   HA3  H N N 152 
GLY   HXT  H N N 153 
HIS   N    N N N 154 
HIS   CA   C N S 155 
HIS   C    C N N 156 
HIS   O    O N N 157 
HIS   CB   C N N 158 
HIS   CG   C Y N 159 
HIS   ND1  N Y N 160 
HIS   CD2  C Y N 161 
HIS   CE1  C Y N 162 
HIS   NE2  N Y N 163 
HIS   OXT  O N N 164 
HIS   H    H N N 165 
HIS   H2   H N N 166 
HIS   HA   H N N 167 
HIS   HB2  H N N 168 
HIS   HB3  H N N 169 
HIS   HD1  H N N 170 
HIS   HD2  H N N 171 
HIS   HE1  H N N 172 
HIS   HE2  H N N 173 
HIS   HXT  H N N 174 
HOH   O    O N N 175 
HOH   H1   H N N 176 
HOH   H2   H N N 177 
ILE   N    N N N 178 
ILE   CA   C N S 179 
ILE   C    C N N 180 
ILE   O    O N N 181 
ILE   CB   C N S 182 
ILE   CG1  C N N 183 
ILE   CG2  C N N 184 
ILE   CD1  C N N 185 
ILE   OXT  O N N 186 
ILE   H    H N N 187 
ILE   H2   H N N 188 
ILE   HA   H N N 189 
ILE   HB   H N N 190 
ILE   HG12 H N N 191 
ILE   HG13 H N N 192 
ILE   HG21 H N N 193 
ILE   HG22 H N N 194 
ILE   HG23 H N N 195 
ILE   HD11 H N N 196 
ILE   HD12 H N N 197 
ILE   HD13 H N N 198 
ILE   HXT  H N N 199 
LEU   N    N N N 200 
LEU   CA   C N S 201 
LEU   C    C N N 202 
LEU   O    O N N 203 
LEU   CB   C N N 204 
LEU   CG   C N N 205 
LEU   CD1  C N N 206 
LEU   CD2  C N N 207 
LEU   OXT  O N N 208 
LEU   H    H N N 209 
LEU   H2   H N N 210 
LEU   HA   H N N 211 
LEU   HB2  H N N 212 
LEU   HB3  H N N 213 
LEU   HG   H N N 214 
LEU   HD11 H N N 215 
LEU   HD12 H N N 216 
LEU   HD13 H N N 217 
LEU   HD21 H N N 218 
LEU   HD22 H N N 219 
LEU   HD23 H N N 220 
LEU   HXT  H N N 221 
LYS   N    N N N 222 
LYS   CA   C N S 223 
LYS   C    C N N 224 
LYS   O    O N N 225 
LYS   CB   C N N 226 
LYS   CG   C N N 227 
LYS   CD   C N N 228 
LYS   CE   C N N 229 
LYS   NZ   N N N 230 
LYS   OXT  O N N 231 
LYS   H    H N N 232 
LYS   H2   H N N 233 
LYS   HA   H N N 234 
LYS   HB2  H N N 235 
LYS   HB3  H N N 236 
LYS   HG2  H N N 237 
LYS   HG3  H N N 238 
LYS   HD2  H N N 239 
LYS   HD3  H N N 240 
LYS   HE2  H N N 241 
LYS   HE3  H N N 242 
LYS   HZ1  H N N 243 
LYS   HZ2  H N N 244 
LYS   HZ3  H N N 245 
LYS   HXT  H N N 246 
MET   N    N N N 247 
MET   CA   C N S 248 
MET   C    C N N 249 
MET   O    O N N 250 
MET   CB   C N N 251 
MET   CG   C N N 252 
MET   SD   S N N 253 
MET   CE   C N N 254 
MET   OXT  O N N 255 
MET   H    H N N 256 
MET   H2   H N N 257 
MET   HA   H N N 258 
MET   HB2  H N N 259 
MET   HB3  H N N 260 
MET   HG2  H N N 261 
MET   HG3  H N N 262 
MET   HE1  H N N 263 
MET   HE2  H N N 264 
MET   HE3  H N N 265 
MET   HXT  H N N 266 
PHE   N    N N N 267 
PHE   CA   C N S 268 
PHE   C    C N N 269 
PHE   O    O N N 270 
PHE   CB   C N N 271 
PHE   CG   C Y N 272 
PHE   CD1  C Y N 273 
PHE   CD2  C Y N 274 
PHE   CE1  C Y N 275 
PHE   CE2  C Y N 276 
PHE   CZ   C Y N 277 
PHE   OXT  O N N 278 
PHE   H    H N N 279 
PHE   H2   H N N 280 
PHE   HA   H N N 281 
PHE   HB2  H N N 282 
PHE   HB3  H N N 283 
PHE   HD1  H N N 284 
PHE   HD2  H N N 285 
PHE   HE1  H N N 286 
PHE   HE2  H N N 287 
PHE   HZ   H N N 288 
PHE   HXT  H N N 289 
PRO   N    N N N 290 
PRO   CA   C N S 291 
PRO   C    C N N 292 
PRO   O    O N N 293 
PRO   CB   C N N 294 
PRO   CG   C N N 295 
PRO   CD   C N N 296 
PRO   OXT  O N N 297 
PRO   H    H N N 298 
PRO   HA   H N N 299 
PRO   HB2  H N N 300 
PRO   HB3  H N N 301 
PRO   HG2  H N N 302 
PRO   HG3  H N N 303 
PRO   HD2  H N N 304 
PRO   HD3  H N N 305 
PRO   HXT  H N N 306 
SER   N    N N N 307 
SER   CA   C N S 308 
SER   C    C N N 309 
SER   O    O N N 310 
SER   CB   C N N 311 
SER   OG   O N N 312 
SER   OXT  O N N 313 
SER   H    H N N 314 
SER   H2   H N N 315 
SER   HA   H N N 316 
SER   HB2  H N N 317 
SER   HB3  H N N 318 
SER   HG   H N N 319 
SER   HXT  H N N 320 
THR   N    N N N 321 
THR   CA   C N S 322 
THR   C    C N N 323 
THR   O    O N N 324 
THR   CB   C N R 325 
THR   OG1  O N N 326 
THR   CG2  C N N 327 
THR   OXT  O N N 328 
THR   H    H N N 329 
THR   H2   H N N 330 
THR   HA   H N N 331 
THR   HB   H N N 332 
THR   HG1  H N N 333 
THR   HG21 H N N 334 
THR   HG22 H N N 335 
THR   HG23 H N N 336 
THR   HXT  H N N 337 
TRP   N    N N N 338 
TRP   CA   C N S 339 
TRP   C    C N N 340 
TRP   O    O N N 341 
TRP   CB   C N N 342 
TRP   CG   C Y N 343 
TRP   CD1  C Y N 344 
TRP   CD2  C Y N 345 
TRP   NE1  N Y N 346 
TRP   CE2  C Y N 347 
TRP   CE3  C Y N 348 
TRP   CZ2  C Y N 349 
TRP   CZ3  C Y N 350 
TRP   CH2  C Y N 351 
TRP   OXT  O N N 352 
TRP   H    H N N 353 
TRP   H2   H N N 354 
TRP   HA   H N N 355 
TRP   HB2  H N N 356 
TRP   HB3  H N N 357 
TRP   HD1  H N N 358 
TRP   HE1  H N N 359 
TRP   HE3  H N N 360 
TRP   HZ2  H N N 361 
TRP   HZ3  H N N 362 
TRP   HH2  H N N 363 
TRP   HXT  H N N 364 
TYR   N    N N N 365 
TYR   CA   C N S 366 
TYR   C    C N N 367 
TYR   O    O N N 368 
TYR   CB   C N N 369 
TYR   CG   C Y N 370 
TYR   CD1  C Y N 371 
TYR   CD2  C Y N 372 
TYR   CE1  C Y N 373 
TYR   CE2  C Y N 374 
TYR   CZ   C Y N 375 
TYR   OH   O N N 376 
TYR   OXT  O N N 377 
TYR   H    H N N 378 
TYR   H2   H N N 379 
TYR   HA   H N N 380 
TYR   HB2  H N N 381 
TYR   HB3  H N N 382 
TYR   HD1  H N N 383 
TYR   HD2  H N N 384 
TYR   HE1  H N N 385 
TYR   HE2  H N N 386 
TYR   HH   H N N 387 
TYR   HXT  H N N 388 
VAL   N    N N N 389 
VAL   CA   C N S 390 
VAL   C    C N N 391 
VAL   O    O N N 392 
VAL   CB   C N N 393 
VAL   CG1  C N N 394 
VAL   CG2  C N N 395 
VAL   OXT  O N N 396 
VAL   H    H N N 397 
VAL   H2   H N N 398 
VAL   HA   H N N 399 
VAL   HB   H N N 400 
VAL   HG11 H N N 401 
VAL   HG12 H N N 402 
VAL   HG13 H N N 403 
VAL   HG21 H N N 404 
VAL   HG22 H N N 405 
VAL   HG23 H N N 406 
VAL   HXT  H N N 407 
# 
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 
A1AXS C1  N1   sing N N 1   
A1AXS N1  C2   sing N N 2   
A1AXS N1  C7   sing N N 3   
A1AXS C2  O1   doub N N 4   
A1AXS C2  C3   sing N N 5   
A1AXS C3  C4   doub Y N 6   
A1AXS C3  S1   sing Y N 7   
A1AXS C4  C5   sing Y N 8   
A1AXS C5  C6   doub Y N 9   
A1AXS C6  S1   sing Y N 10  
A1AXS C7  C8   sing N N 11  
A1AXS C7  C12  sing N N 12  
A1AXS C8  C9   sing N N 13  
A1AXS C9  C10  sing N N 14  
A1AXS C9  C13  sing N N 15  
A1AXS C10 C11  doub N N 16  
A1AXS C11 C12  sing N N 17  
A1AXS C12 C13  sing N N 18  
A1AXS C1  H13  sing N N 19  
A1AXS C1  H14  sing N N 20  
A1AXS C1  H15  sing N N 21  
A1AXS C10 H10  sing N N 22  
A1AXS C11 H11  sing N N 23  
A1AXS C12 H12  sing N N 24  
A1AXS C13 H132 sing N N 25  
A1AXS C13 H133 sing N N 26  
A1AXS C4  H4   sing N N 27  
A1AXS C5  H5   sing N N 28  
A1AXS C6  H6   sing N N 29  
A1AXS C7  H7   sing N N 30  
A1AXS C8  H82  sing N N 31  
A1AXS C8  H83  sing N N 32  
A1AXS C9  H9   sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
GLN   N   CA   sing N N 103 
GLN   N   H    sing N N 104 
GLN   N   H2   sing N N 105 
GLN   CA  C    sing N N 106 
GLN   CA  CB   sing N N 107 
GLN   CA  HA   sing N N 108 
GLN   C   O    doub N N 109 
GLN   C   OXT  sing N N 110 
GLN   CB  CG   sing N N 111 
GLN   CB  HB2  sing N N 112 
GLN   CB  HB3  sing N N 113 
GLN   CG  CD   sing N N 114 
GLN   CG  HG2  sing N N 115 
GLN   CG  HG3  sing N N 116 
GLN   CD  OE1  doub N N 117 
GLN   CD  NE2  sing N N 118 
GLN   NE2 HE21 sing N N 119 
GLN   NE2 HE22 sing N N 120 
GLN   OXT HXT  sing N N 121 
GLU   N   CA   sing N N 122 
GLU   N   H    sing N N 123 
GLU   N   H2   sing N N 124 
GLU   CA  C    sing N N 125 
GLU   CA  CB   sing N N 126 
GLU   CA  HA   sing N N 127 
GLU   C   O    doub N N 128 
GLU   C   OXT  sing N N 129 
GLU   CB  CG   sing N N 130 
GLU   CB  HB2  sing N N 131 
GLU   CB  HB3  sing N N 132 
GLU   CG  CD   sing N N 133 
GLU   CG  HG2  sing N N 134 
GLU   CG  HG3  sing N N 135 
GLU   CD  OE1  doub N N 136 
GLU   CD  OE2  sing N N 137 
GLU   OE2 HE2  sing N N 138 
GLU   OXT HXT  sing N N 139 
GLY   N   CA   sing N N 140 
GLY   N   H    sing N N 141 
GLY   N   H2   sing N N 142 
GLY   CA  C    sing N N 143 
GLY   CA  HA2  sing N N 144 
GLY   CA  HA3  sing N N 145 
GLY   C   O    doub N N 146 
GLY   C   OXT  sing N N 147 
GLY   OXT HXT  sing N N 148 
HIS   N   CA   sing N N 149 
HIS   N   H    sing N N 150 
HIS   N   H2   sing N N 151 
HIS   CA  C    sing N N 152 
HIS   CA  CB   sing N N 153 
HIS   CA  HA   sing N N 154 
HIS   C   O    doub N N 155 
HIS   C   OXT  sing N N 156 
HIS   CB  CG   sing N N 157 
HIS   CB  HB2  sing N N 158 
HIS   CB  HB3  sing N N 159 
HIS   CG  ND1  sing Y N 160 
HIS   CG  CD2  doub Y N 161 
HIS   ND1 CE1  doub Y N 162 
HIS   ND1 HD1  sing N N 163 
HIS   CD2 NE2  sing Y N 164 
HIS   CD2 HD2  sing N N 165 
HIS   CE1 NE2  sing Y N 166 
HIS   CE1 HE1  sing N N 167 
HIS   NE2 HE2  sing N N 168 
HIS   OXT HXT  sing N N 169 
HOH   O   H1   sing N N 170 
HOH   O   H2   sing N N 171 
ILE   N   CA   sing N N 172 
ILE   N   H    sing N N 173 
ILE   N   H2   sing N N 174 
ILE   CA  C    sing N N 175 
ILE   CA  CB   sing N N 176 
ILE   CA  HA   sing N N 177 
ILE   C   O    doub N N 178 
ILE   C   OXT  sing N N 179 
ILE   CB  CG1  sing N N 180 
ILE   CB  CG2  sing N N 181 
ILE   CB  HB   sing N N 182 
ILE   CG1 CD1  sing N N 183 
ILE   CG1 HG12 sing N N 184 
ILE   CG1 HG13 sing N N 185 
ILE   CG2 HG21 sing N N 186 
ILE   CG2 HG22 sing N N 187 
ILE   CG2 HG23 sing N N 188 
ILE   CD1 HD11 sing N N 189 
ILE   CD1 HD12 sing N N 190 
ILE   CD1 HD13 sing N N 191 
ILE   OXT HXT  sing N N 192 
LEU   N   CA   sing N N 193 
LEU   N   H    sing N N 194 
LEU   N   H2   sing N N 195 
LEU   CA  C    sing N N 196 
LEU   CA  CB   sing N N 197 
LEU   CA  HA   sing N N 198 
LEU   C   O    doub N N 199 
LEU   C   OXT  sing N N 200 
LEU   CB  CG   sing N N 201 
LEU   CB  HB2  sing N N 202 
LEU   CB  HB3  sing N N 203 
LEU   CG  CD1  sing N N 204 
LEU   CG  CD2  sing N N 205 
LEU   CG  HG   sing N N 206 
LEU   CD1 HD11 sing N N 207 
LEU   CD1 HD12 sing N N 208 
LEU   CD1 HD13 sing N N 209 
LEU   CD2 HD21 sing N N 210 
LEU   CD2 HD22 sing N N 211 
LEU   CD2 HD23 sing N N 212 
LEU   OXT HXT  sing N N 213 
LYS   N   CA   sing N N 214 
LYS   N   H    sing N N 215 
LYS   N   H2   sing N N 216 
LYS   CA  C    sing N N 217 
LYS   CA  CB   sing N N 218 
LYS   CA  HA   sing N N 219 
LYS   C   O    doub N N 220 
LYS   C   OXT  sing N N 221 
LYS   CB  CG   sing N N 222 
LYS   CB  HB2  sing N N 223 
LYS   CB  HB3  sing N N 224 
LYS   CG  CD   sing N N 225 
LYS   CG  HG2  sing N N 226 
LYS   CG  HG3  sing N N 227 
LYS   CD  CE   sing N N 228 
LYS   CD  HD2  sing N N 229 
LYS   CD  HD3  sing N N 230 
LYS   CE  NZ   sing N N 231 
LYS   CE  HE2  sing N N 232 
LYS   CE  HE3  sing N N 233 
LYS   NZ  HZ1  sing N N 234 
LYS   NZ  HZ2  sing N N 235 
LYS   NZ  HZ3  sing N N 236 
LYS   OXT HXT  sing N N 237 
MET   N   CA   sing N N 238 
MET   N   H    sing N N 239 
MET   N   H2   sing N N 240 
MET   CA  C    sing N N 241 
MET   CA  CB   sing N N 242 
MET   CA  HA   sing N N 243 
MET   C   O    doub N N 244 
MET   C   OXT  sing N N 245 
MET   CB  CG   sing N N 246 
MET   CB  HB2  sing N N 247 
MET   CB  HB3  sing N N 248 
MET   CG  SD   sing N N 249 
MET   CG  HG2  sing N N 250 
MET   CG  HG3  sing N N 251 
MET   SD  CE   sing N N 252 
MET   CE  HE1  sing N N 253 
MET   CE  HE2  sing N N 254 
MET   CE  HE3  sing N N 255 
MET   OXT HXT  sing N N 256 
PHE   N   CA   sing N N 257 
PHE   N   H    sing N N 258 
PHE   N   H2   sing N N 259 
PHE   CA  C    sing N N 260 
PHE   CA  CB   sing N N 261 
PHE   CA  HA   sing N N 262 
PHE   C   O    doub N N 263 
PHE   C   OXT  sing N N 264 
PHE   CB  CG   sing N N 265 
PHE   CB  HB2  sing N N 266 
PHE   CB  HB3  sing N N 267 
PHE   CG  CD1  doub Y N 268 
PHE   CG  CD2  sing Y N 269 
PHE   CD1 CE1  sing Y N 270 
PHE   CD1 HD1  sing N N 271 
PHE   CD2 CE2  doub Y N 272 
PHE   CD2 HD2  sing N N 273 
PHE   CE1 CZ   doub Y N 274 
PHE   CE1 HE1  sing N N 275 
PHE   CE2 CZ   sing Y N 276 
PHE   CE2 HE2  sing N N 277 
PHE   CZ  HZ   sing N N 278 
PHE   OXT HXT  sing N N 279 
PRO   N   CA   sing N N 280 
PRO   N   CD   sing N N 281 
PRO   N   H    sing N N 282 
PRO   CA  C    sing N N 283 
PRO   CA  CB   sing N N 284 
PRO   CA  HA   sing N N 285 
PRO   C   O    doub N N 286 
PRO   C   OXT  sing N N 287 
PRO   CB  CG   sing N N 288 
PRO   CB  HB2  sing N N 289 
PRO   CB  HB3  sing N N 290 
PRO   CG  CD   sing N N 291 
PRO   CG  HG2  sing N N 292 
PRO   CG  HG3  sing N N 293 
PRO   CD  HD2  sing N N 294 
PRO   CD  HD3  sing N N 295 
PRO   OXT HXT  sing N N 296 
SER   N   CA   sing N N 297 
SER   N   H    sing N N 298 
SER   N   H2   sing N N 299 
SER   CA  C    sing N N 300 
SER   CA  CB   sing N N 301 
SER   CA  HA   sing N N 302 
SER   C   O    doub N N 303 
SER   C   OXT  sing N N 304 
SER   CB  OG   sing N N 305 
SER   CB  HB2  sing N N 306 
SER   CB  HB3  sing N N 307 
SER   OG  HG   sing N N 308 
SER   OXT HXT  sing N N 309 
THR   N   CA   sing N N 310 
THR   N   H    sing N N 311 
THR   N   H2   sing N N 312 
THR   CA  C    sing N N 313 
THR   CA  CB   sing N N 314 
THR   CA  HA   sing N N 315 
THR   C   O    doub N N 316 
THR   C   OXT  sing N N 317 
THR   CB  OG1  sing N N 318 
THR   CB  CG2  sing N N 319 
THR   CB  HB   sing N N 320 
THR   OG1 HG1  sing N N 321 
THR   CG2 HG21 sing N N 322 
THR   CG2 HG22 sing N N 323 
THR   CG2 HG23 sing N N 324 
THR   OXT HXT  sing N N 325 
TRP   N   CA   sing N N 326 
TRP   N   H    sing N N 327 
TRP   N   H2   sing N N 328 
TRP   CA  C    sing N N 329 
TRP   CA  CB   sing N N 330 
TRP   CA  HA   sing N N 331 
TRP   C   O    doub N N 332 
TRP   C   OXT  sing N N 333 
TRP   CB  CG   sing N N 334 
TRP   CB  HB2  sing N N 335 
TRP   CB  HB3  sing N N 336 
TRP   CG  CD1  doub Y N 337 
TRP   CG  CD2  sing Y N 338 
TRP   CD1 NE1  sing Y N 339 
TRP   CD1 HD1  sing N N 340 
TRP   CD2 CE2  doub Y N 341 
TRP   CD2 CE3  sing Y N 342 
TRP   NE1 CE2  sing Y N 343 
TRP   NE1 HE1  sing N N 344 
TRP   CE2 CZ2  sing Y N 345 
TRP   CE3 CZ3  doub Y N 346 
TRP   CE3 HE3  sing N N 347 
TRP   CZ2 CH2  doub Y N 348 
TRP   CZ2 HZ2  sing N N 349 
TRP   CZ3 CH2  sing Y N 350 
TRP   CZ3 HZ3  sing N N 351 
TRP   CH2 HH2  sing N N 352 
TRP   OXT HXT  sing N N 353 
TYR   N   CA   sing N N 354 
TYR   N   H    sing N N 355 
TYR   N   H2   sing N N 356 
TYR   CA  C    sing N N 357 
TYR   CA  CB   sing N N 358 
TYR   CA  HA   sing N N 359 
TYR   C   O    doub N N 360 
TYR   C   OXT  sing N N 361 
TYR   CB  CG   sing N N 362 
TYR   CB  HB2  sing N N 363 
TYR   CB  HB3  sing N N 364 
TYR   CG  CD1  doub Y N 365 
TYR   CG  CD2  sing Y N 366 
TYR   CD1 CE1  sing Y N 367 
TYR   CD1 HD1  sing N N 368 
TYR   CD2 CE2  doub Y N 369 
TYR   CD2 HD2  sing N N 370 
TYR   CE1 CZ   doub Y N 371 
TYR   CE1 HE1  sing N N 372 
TYR   CE2 CZ   sing Y N 373 
TYR   CE2 HE2  sing N N 374 
TYR   CZ  OH   sing N N 375 
TYR   OH  HH   sing N N 376 
TYR   OXT HXT  sing N N 377 
VAL   N   CA   sing N N 378 
VAL   N   H    sing N N 379 
VAL   N   H2   sing N N 380 
VAL   CA  C    sing N N 381 
VAL   CA  CB   sing N N 382 
VAL   CA  HA   sing N N 383 
VAL   C   O    doub N N 384 
VAL   C   OXT  sing N N 385 
VAL   CB  CG1  sing N N 386 
VAL   CB  CG2  sing N N 387 
VAL   CB  HB   sing N N 388 
VAL   CG1 HG11 sing N N 389 
VAL   CG1 HG12 sing N N 390 
VAL   CG1 HG13 sing N N 391 
VAL   CG2 HG21 sing N N 392 
VAL   CG2 HG22 sing N N 393 
VAL   CG2 HG23 sing N N 394 
VAL   OXT HXT  sing N N 395 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HB8 
_atom_sites.fract_transf_matrix[1][1]   0.014665 
_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]   0.011089 
_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]   0.010134 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLU   A 1 9   ? 6.84801   -29.13001 -38.34017 1.000 65.38758  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 8.12229   -28.42273 -38.32439 1.000 59.43425  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 8.21323   -27.50853 -37.10264 1.000 58.89304  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 7.49448   -26.51221 -37.00121 1.000 61.69461  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 8.31030   -27.60170 -39.60111 1.000 70.71154  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 9.33654   -26.47789 -39.45447 1.000 90.39565  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 10.33861  -26.41707 -40.58553 1.000 115.67975 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 10.13040  -27.11312 -41.60581 1.000 115.34904 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 11.32864  -25.65679 -40.45194 1.000 103.61944 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 9.11393   -27.84434 -36.18831 1.000 43.05368  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 9.30568   -27.09130 -34.95368 1.000 44.10364  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 10.66551  -26.41459 -35.02086 1.000 41.54798  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 11.67181  -27.07077 -35.31335 1.000 42.01236  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 9.21171   -28.02375 -33.73812 1.000 48.84384  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 9.28065   -27.20921 -32.42574 1.000 41.57074  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 7.96204   -28.90589 -33.86116 1.000 51.01253  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 10.70311  -25.11111 -34.76761 1.000 33.44619  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 11.97016  -24.40165 -34.67239 1.000 34.23637  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 12.30260  -24.14579 -33.21193 1.000 31.83538  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 11.43676  -23.75365 -32.42351 1.000 29.47312  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 11.95651  -23.07929 -35.43570 1.000 29.52341  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 11.80036  -23.28182 -36.94819 1.000 35.41649  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 11.72483  -21.95304 -37.65870 1.000 55.13971  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 10.69948  -21.25605 -37.50656 1.000 44.43197  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 12.68190  -21.63648 -38.39683 1.000 59.59014  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 13.56369  -24.35452 -32.85985 1.000 27.79512  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 14.00792  -24.15631 -31.48004 1.000 26.32264  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 14.96236  -22.97476 -31.41340 1.000 29.01351  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 15.88443  -22.86922 -32.22113 1.000 28.79083  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 14.70457  -25.41304 -30.95722 1.000 28.34346  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 13.84440  -26.55409 -31.11763 1.000 31.87148  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 15.08160  -25.25057 -29.49471 1.000 26.61200  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 14.76922  -22.11285 -30.41993 1.000 26.74818  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 15.50518  -20.86301 -30.29568 1.000 28.17377  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 16.07266  -20.75731 -28.88973 1.000 30.32357  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 15.47297  -21.25953 -27.93327 1.000 30.58134  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 14.60311  -19.64559 -30.49964 1.000 26.64720  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 13.89717  -19.62853 -31.80584 1.000 27.77793  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 12.70331  -20.31034 -31.97133 1.000 30.69825  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 14.42485  -18.94585 -32.87399 1.000 27.62335  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 12.03626  -20.30059 -33.21005 1.000 28.63552  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 13.74444  -18.90718 -34.10524 1.000 29.32306  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 12.57094  -19.60246 -34.27034 1.000 32.80565  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 17.22487  -20.10911 -28.77109 1.000 25.24099  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 17.73990  -19.74206 -27.43827 1.000 32.20637  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 17.09906  -18.44728 -26.97266 1.000 32.14772  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 16.94030  -17.51318 -27.75280 1.000 33.16402  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 19.26591  -19.56657 -27.46642 1.000 31.05116  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 16.73451  -18.37504 -25.69192 1.000 29.37252  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 16.37459  -17.07523 -25.14147 1.000 31.76114  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 17.59367  -16.16371 -25.16740 1.000 31.14638  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 18.73334  -16.62341 -25.05581 1.000 32.43507  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 15.89884  -17.22012 -23.69471 1.000 28.74855  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 14.50122  -17.74080 -23.54887 1.000 28.74585  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 13.40587  -16.94565 -23.87993 1.000 28.84818  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 14.29097  -19.01184 -23.04038 1.000 26.78165  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 12.10579  -17.42539 -23.70376 1.000 28.52764  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 13.01284  -19.51365 -22.88474 1.000 30.17417  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 11.91830  -18.73531 -23.20655 1.000 27.10291  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.37158  -14.85950 -25.30854 1.000 34.46708  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.46096  -13.95489 -24.95220 1.000 42.90781  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 18.96272  -14.24390 -23.53704 1.000 41.91433  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.20288  -14.66134 -22.65597 1.000 39.25569  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 18.02326  -12.50904 -25.05866 1.000 50.29242  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.71392  -12.12265 -26.45718 1.000 55.23431  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 17.24527  -10.72816 -26.51601 1.000 56.96792  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 17.97819  -9.82908  -26.93289 1.000 68.09805  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.01366  -10.50976 -26.07168 1.000 62.28571  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.25943  -14.00720 -23.31673 1.000 42.21698  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 20.87580  -14.42807 -22.06200 1.000 45.96507  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.20983  -13.76465 -20.85709 1.000 44.55205  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 20.01361  -14.40964 -19.81834 1.000 38.53718  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.37517  -14.13202 -22.09224 1.000 49.88212  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.83861  -12.48309 -20.98696 1.000 34.92580  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.21415  -11.75610 -19.88599 1.000 39.42003  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 17.87276  -12.36688 -19.51713 1.000 33.29164  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.50578  -12.41001 -18.33350 1.000 32.28047  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 19.01685  -10.28288 -20.25926 1.000 47.54827  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.27162  -9.45532  -20.55526 1.000 54.61694  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 21.00546  -9.86690  -21.82965 1.000 69.56188  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.33689  -10.33348 -22.77813 1.000 66.17760  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 22.24550  -9.66441  -21.89398 1.000 64.38503  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.10733  -12.79994 -20.52133 1.000 33.42417  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.78234  -13.34971 -20.26054 1.000 34.30080  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 15.91850  -14.72903 -19.63299 1.000 33.38019  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.18547  -15.07913 -18.69357 1.000 30.41464  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 14.93656  -13.40079 -21.56104 1.000 33.61529  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.46366  -12.01464 -22.01786 1.000 39.06271  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.69791  -14.22506 -21.35021 1.000 32.39625  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 15.54120  -11.08788 -22.47070 1.000 49.89729  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 16.86845  -15.53156 -20.13175 1.000 29.01002  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 17.16079  -16.81652 -19.48239 1.000 32.82404  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.57196  -16.62207 -18.01909 1.000 27.20511  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 17.15367  -17.39198 -17.14060 1.000 29.61554  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 18.24965  -17.56704 -20.24538 1.000 33.68768  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.38877  -15.60768 -17.73312 1.000 30.82194  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.73468  -15.34299 -16.33016 1.000 32.43839  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.50918  -14.94150 -15.53057 1.000 34.32711  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.36195  -15.31399 -14.35032 1.000 28.43346  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.78314  -14.24073 -16.21598 1.000 35.05673  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 21.08230  -14.50065 -16.89401 1.000 44.80873  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 21.93369  -13.25056 -16.96463 1.000 63.92428  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.58067  -12.21297 -16.39171 1.000 55.92754  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 23.02823  -13.32073 -17.71829 1.000 63.99960  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.63148  -14.14723 -16.13916 1.000 30.61450  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.40711  -13.74489 -15.44600 1.000 33.16889  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.52636  -14.94817 -15.16110 1.000 32.78771  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.96972  -15.07369 -14.06438 1.000 33.19082  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.63514  -12.72804 -16.28335 1.000 32.56832  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.26185  -12.39867 -15.70625 1.000 35.82741  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.38367  -11.68104 -14.37698 1.000 41.62383  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.42785  -11.59217 -16.72242 1.000 35.87514  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.35997  -15.84834 -16.13883 1.000 26.77794  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.47947  -16.96514 -15.82933 1.000 30.41113  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 14.10177  -17.89405 -14.79740 1.000 29.01608  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.38077  -18.45247 -13.96531 1.000 31.27642  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.00028  -17.79049 -17.03993 1.000 29.12244  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.25900  -17.01533 -18.13400 1.000 29.47451  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.56798  -17.65944 -19.82921 1.000 31.66028  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 11.51244  -19.06842 -19.55186 1.000 33.59937  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.42194  -18.00723 -14.76262 1.000 26.50414  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 16.00574  -18.86668 -13.73801 1.000 31.80937  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.86190  -18.22572 -12.35945 1.000 31.61898  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 15.63217  -18.92572 -11.36374 1.000 32.34648  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.45820  -19.16699 -14.09461 1.000 35.95968  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 18.21627  -19.31266 -12.91938 1.000 52.76175  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.95175  -16.89272 -12.28083 1.000 32.63348  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.71972  -16.21939 -11.00192 1.000 29.15647  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.28148  -16.42674 -10.53884 1.000 29.07050  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 14.02804  -16.59921 -9.34314  1.000 33.09316  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 16.04904  -14.72869 -11.13320 1.000 32.55041  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.84064  -13.77066 -9.96303  1.000 49.53723  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.70759  -12.51296 -10.14676 1.000 47.82905  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 14.35879  -13.39053 -9.81905  1.000 41.21420  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.32398  -16.38766 -11.46677 1.000 27.14010  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.91291  -16.55850 -11.11527 1.000 29.18967  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.64140  -17.98894 -10.64281 1.000 34.97313  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.87439  -18.22209 -9.69295  1.000 30.33994  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 11.02805  -16.17978 -12.32021 1.000 30.36078  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.99860  -14.65878 -12.47978 1.000 28.82486  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.59155   -16.75832 -12.18500 1.000 30.84102  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.43378  -14.18965 -13.80546 1.000 32.99883  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.29192  -18.96478 -11.27036 1.000 30.52020  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 12.07654  -20.35898 -10.91303 1.000 30.96889  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.79823  -20.71710 -9.62110  1.000 36.11012  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 12.27332  -21.46021 -8.78244  1.000 40.18767  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.52846  -21.24085 -12.08668 1.000 36.57546  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.53864  -21.08359 -13.24329 1.000 35.10492  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 12.67949  -22.71521 -11.63474 1.000 39.07123  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 12.11985  -21.46322 -14.57357 1.000 38.31511  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.99267  -20.17316 -9.40517  1.000 35.81954  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.79853  -20.60846 -8.27194  1.000 35.51807  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.66902  -19.76672 -7.01086  1.000 36.16032  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 15.05691  -20.24744 -5.93496  1.000 39.85584  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.26529  -20.66511 -8.68180  1.000 39.30967  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.49795  -21.64239 -9.78692  1.000 46.38583  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.79942  -22.65611 -9.88791  1.000 47.07105  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 17.44772  -21.33456 -10.65266 1.000 51.85476  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.15096  -18.54912 -7.07783  1.000 36.34600  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 14.09221  -17.72376 -5.87015  1.000 37.99262  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.94136  -18.17838 -4.96246  1.000 38.18298  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.83443  -18.47135 -5.41926  1.000 37.79501  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.93657  -16.24372 -6.24328  1.000 36.98009  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 15.06569  -15.84199 -7.03168  1.000 38.25645  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.89119  -15.36157 -4.98992  1.000 38.77300  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 13.20262  -18.24295 -3.66567  1.000 33.56712  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 12.11091  -18.51868 -2.74880  1.000 35.04431  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.25255  -17.26853 -2.60282  1.000 38.24815  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.74376  -16.20084 -2.20991  1.000 34.74320  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.64138  -18.96453 -1.39888  1.000 38.25073  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.55573  -19.22355 -0.39724  1.000 37.40136  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.82540  -20.40883 -0.44417  1.000 43.50188  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.26467  -18.29676 0.58873   1.000 40.39311  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.82307   -20.66954 0.49449   1.000 45.28584  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.25343  -18.54627 1.52659   1.000 41.16707  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.53460   -19.73552 1.47245   1.000 39.98187  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.97250   -17.39991 -2.92223  1.000 33.20456  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 9.07332   -16.24901 -2.96276  1.000 30.99721  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.65163   -16.79330 -2.87367  1.000 31.39598  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 7.16717   -17.38559 -3.83872  1.000 31.22526  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.28623   -15.43628 -4.24837  1.000 32.31016  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.37007   -14.24509 -4.28365  1.000 33.23631  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.67737   -13.13614 -3.52261  1.000 35.59296  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.23692   -14.19638 -5.10701  1.000 34.94126  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.88571   -12.04347 -3.49155  1.000 46.02756  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.41354   -13.05583 -5.07832  1.000 37.61451  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.77254   -11.98848 -4.26463  1.000 41.40160  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 6.03398   -10.82667 -4.17046  1.000 56.40294  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.99518   -16.61651 -1.72259  1.000 35.66735  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.71796   -17.28136 -1.49640  1.000 35.50594  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.53473   -16.62890 -2.20921  1.000 34.38993  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.52449   -17.31098 -2.42237  1.000 36.37060  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.42619   -17.35041 0.00507   1.000 32.05072  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.40971   -18.13632 0.67880   1.000 36.54415  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.61571   -15.34006 -2.56111  1.000 33.73061  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.46750   -14.59452 -3.09226  1.000 36.10659  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.28394   -14.85057 -4.59720  1.000 29.39188  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.27640   -13.94794 -5.43445  1.000 30.30780  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.63019   -13.11139 -2.77574  1.000 34.09226  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.47185   -12.26358 -3.26715  1.000 35.06059  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.30093   -12.64577 -3.15369  1.000 36.27875  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.79056   -11.05385 -3.72586  1.000 38.51139  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 3.08701   -16.12515 -4.92473  1.000 27.16382  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 3.07168   -16.53587 -6.32538  1.000 28.73687  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.83681   -16.06619 -7.07855  1.000 26.36160  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.86924   -16.01338 -8.31906  1.000 27.29203  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.17413   -18.05309 -6.41136  1.000 30.03780  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.58076   -18.59379 -6.06906  1.000 30.92326  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.57592   -20.08874 -6.05946  1.000 31.37913  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.94521   -20.68296 -5.67577  1.000 38.75374  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.86442   -20.67627 -6.85563  1.000 31.22286  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.75816   -15.71338 -6.37519  1.000 29.77777  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.51208  -15.45280 -7.05747  1.000 30.31426  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.45903  -14.27081 -8.01399  1.000 32.87240  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.37575  -14.12120 -8.84049  1.000 29.34652  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.60921  -15.19385 -6.04353  1.000 29.26664  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.39605  -13.88616 -5.25094  1.000 30.84493  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.36756  -13.74639 -4.08679  1.000 43.86469  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.63559  -14.76294 -3.41749  1.000 42.39737  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -2.88351  -12.62876 -3.86112  1.000 55.90971  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.55008   -13.40020 -7.89297  1.000 27.40912  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.64470   -12.23280 -8.76159  1.000 28.16377  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.82519   -12.61542 -10.21858 1.000 31.70278  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.67418   -11.75577 -11.09879 1.000 27.39383  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.78275   -11.28910 -8.30733  1.000 30.76973  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 3.15694   -11.95565 -8.41652  1.000 32.15409  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.55169   -10.81468 -6.86862  1.000 35.69992  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.87493   -11.63115 -9.68693  1.000 36.31151  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 1.12888   -13.88287 -10.51441 1.000 25.90969  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.25104   -14.25360 -11.92011 1.000 25.85828  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.04058  -13.95428 -12.67250 1.000 26.81511  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.00854  -13.61401 -13.85059 1.000 25.68295  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.59546   -15.74833 -12.08983 1.000 26.80085  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.39964   -16.65924 -11.97146 1.000 28.89835  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? 0.00279   -17.13151 -10.72623 1.000 25.92159  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -0.36109  -17.01115 -13.08979 1.000 27.21466  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.11863  -17.93675 -10.58829 1.000 30.36635  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -1.48808  -17.82751 -12.95743 1.000 27.90224  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -1.85290  -18.29946 -11.69573 1.000 27.49437  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.19221  -14.14221 -12.02622 1.000 27.72286  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.46023  -14.02960 -12.74916 1.000 28.11470  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.75539  -12.58324 -13.12064 1.000 29.71739  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.21067  -12.29618 -14.24085 1.000 27.11528  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.59842  -14.63772 -11.90110 1.000 27.32980  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -4.94238  -14.72592 -12.65798 1.000 28.56020  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -4.76997  -15.52888 -13.91397 1.000 26.04898  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.09432  -15.24657 -11.78156 1.000 33.98423  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.49628  -11.65993 -12.18759 1.000 25.48680  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.57845  -10.22948 -12.46325 1.000 28.84525  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.73342  -9.83049  -13.66474 1.000 25.40878  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.15708  -9.00854  -14.50199 1.000 27.48126  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.10232  -9.45097  -11.22903 1.000 28.55136  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.03343  -7.95000  -11.41783 1.000 36.29502  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.36455  -7.22090  -10.24135 1.000 39.65404  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? 0.04674   -7.56023  -10.10288 1.000 40.56766  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.74657   -7.46180  -8.97867  1.000 49.64398  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? 0.18360   -7.09419  -7.83672  1.000 41.38098  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 2.05606   -7.69193  -9.00964  1.000 45.51347  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.52222  -10.37558 -13.76667 1.000 25.70062  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.35794   -9.97474  -14.87217 1.000 21.31478  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.18266  -10.45318 -16.20349 1.000 26.31875  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.10623  -9.72799  -17.20872 1.000 28.66991  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.77628   -10.50426 -14.65718 1.000 22.93594  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.42903   -9.96729  -13.31400 1.000 26.16678  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.33991   -8.42167  -13.20204 1.000 41.97442  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.48184   -7.74523  -14.24768 1.000 37.44426  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 2.14192   -7.87638  -12.08301 1.000 39.06517  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.68066  -11.69539 -16.24737 1.000 24.57994  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.17019  -12.22197 -17.51218 1.000 26.66767  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.46718  -11.53000 -17.91887 1.000 26.76291  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.70880  -11.29790 -19.10979 1.000 26.05392  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.35930  -13.73493 -17.40851 1.000 24.10898  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -0.05558  -14.51973 -17.15939 1.000 22.35709  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.37649  -16.03550 -16.99464 1.000 25.18033  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 0.95584   -14.34845 -18.30536 1.000 27.94480  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.35001  -11.26859 -16.95265 1.000 23.34825  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.55972  -10.51527 -17.25744 1.000 26.19487  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.20386  -9.10009  -17.71468 1.000 27.59294  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -4.82902  -8.54445  -18.63745 1.000 26.36999  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.50399  -10.52314 -16.03567 1.000 25.15059  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.08764  -11.95332 -15.88486 1.000 25.56425  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.60551  -9.46666  -16.22391 1.000 26.94655  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -6.99925  -12.14879 -14.61977 1.000 25.31887  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.19532  -8.48796  -17.08406 1.000 24.86106  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -2.76624  -7.16750  -17.53418 1.000 27.98115  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.28687  -7.21651  -18.98411 1.000 28.90423  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.60350  -6.31964  -19.78262 1.000 26.08242  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -1.67129  -6.63594  -16.60093 1.000 29.76691  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.11604  -5.42621  -17.08907 1.000 38.57593  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.53215  -8.27312  -19.34365 1.000 24.95089  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.08906  -8.42726  -20.72579 1.000 28.68147  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.27369  -8.57996  -21.66318 1.000 27.17476  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.27475  -8.01080  -22.75771 1.000 25.22538  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.14004  -9.62164  -20.87322 1.000 27.80242  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.28106   -9.30761  -20.40955 1.000 36.32667  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.59075   -8.18226  -20.03636 1.000 33.95277  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 2.15381   -10.29914 -20.47026 1.000 35.81583  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.28267  -9.35661  -21.25675 1.000 25.16779  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.45136  -9.54527  -22.11691 1.000 26.68411  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.18029  -8.23227  -22.30173 1.000 26.60878  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.61434  -7.89686  -23.40766 1.000 26.46870  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.40223  -10.56760 -21.52126 1.000 28.77060  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -4.82705  -11.86510 -21.50957 1.000 30.34843  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.33423  -7.47785  -21.21773 1.000 23.86554  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -5.98687  -6.18697  -21.31210 1.000 24.56330  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.24612  -5.26364  -22.27543 1.000 26.22183  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -5.87836  -4.54169  -23.05911 1.000 27.27338  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.06753  -5.56536  -19.90964 1.000 26.55525  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -6.71704  -4.31286  -19.95503 1.000 31.01991  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -3.90395  -5.25277  -22.22467 1.000 25.43088  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.15864  -4.39386  -23.14920 1.000 26.34589  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.44528  -4.81459  -24.59627 1.000 24.89361  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.61798  -3.96934  -25.49392 1.000 24.97129  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.66201  -4.51062  -22.87684 1.000 25.85459  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.20919  -3.81971  -21.58523 1.000 38.96514  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.00532  -3.11564  -20.94268 1.000 32.23743  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.03328  -4.01921  -21.19617 1.000 33.00291  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.49920  -6.13138  -24.83697 1.000 25.35590  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.72756  -6.64101  -26.19674 1.000 23.86002  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -5.11727  -6.26673  -26.69208 1.000 21.56799  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.31517  -5.96047  -27.88530 1.000 25.14052  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.56234  -8.16660  -26.22371 1.000 22.86903  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -6.09484  -6.31764  -25.79457 1.000 22.97447  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.45024  -5.90715  -26.12194 1.000 23.35806  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.51697  -4.40452  -26.39108 1.000 28.60579  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.17108  -3.97362  -27.34779 1.000 27.68811  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.38432  -6.31267  -24.96823 1.000 23.21481  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.61981  -7.83309  -24.91579 1.000 25.79262  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.15381  -8.24867  -23.51447 1.000 26.24539  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.55506  -8.29966  -26.04451 1.000 22.59831  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.84559  -3.59597  -25.56004 1.000 26.52184  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.72862  -2.16399  -25.82499 1.000 25.22777  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.22430  -1.90637  -27.23777 1.000 24.47475  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.70231  -0.99997  -27.92904 1.000 26.21833  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -5.75348  -1.53340  -24.84330 1.000 28.20290  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.35566  -1.30408  -23.48487 1.000 35.25446  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -7.59284  -1.44006  -23.32685 1.000 29.99021  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -5.56803  -0.98723  -22.56934 1.000 34.34545  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.23310  -2.68819  -27.66422 1.000 25.66241  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.57515  -2.41927  -28.93718 1.000 25.37752  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.50984  -2.68641  -30.10299 1.000 27.23162  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.58495  -1.88192  -31.03469 1.000 26.79610  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.30521  -3.26480  -29.05264 1.000 31.91535  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.14256  -2.73081  -28.18457 1.000 50.06468  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.84042  -3.57522  -28.26747 1.000 65.93745  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? 0.00567   -3.50341  -26.97431 1.000 54.24719  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 1.10171   -4.50418  -26.96598 1.000 63.75761  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.21511  -3.82028  -30.08604 1.000 26.48738  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -7.13103  -4.09174  -31.19683 1.000 26.57514  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.33610  -3.15688  -31.14061 1.000 29.75613  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.85146  -2.75051  -32.19059 1.000 31.88372  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.56121  -5.57579  -31.24401 1.000 25.71322  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -8.32519  -5.90967  -32.54652 1.000 28.72936  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -8.38841  -5.98617  -30.03809 1.000 23.06795  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.53813  -5.60469  -33.78326 1.000 29.77095  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.81226  -2.79757  -29.93857 1.000 27.49336  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.89323  -1.81242  -29.84988 1.000 29.77458  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.50350  -0.49018  -30.51082 1.000 29.20136  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.29327 0.09682   -31.25951 1.000 31.24953  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.30314 -1.56771  -28.38883 1.000 30.41759  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.67075 -0.84612  -28.30745 1.000 38.35639  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.02486 -0.39957  -26.89984 1.000 47.62925  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -10.86010 0.01416   -26.12807 1.000 66.42793  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -10.87535 0.22955   -24.81874 1.000 61.07763  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -11.97584 0.04148   -24.10821 1.000 53.62088  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -9.75458  0.63587   -24.20801 1.000 42.05718  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.29680  0.00634   -30.22466 1.000 27.24155  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.86533  1.28411   -30.81265 1.000 27.22329  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.73726  1.16557   -32.32162 1.000 30.39236  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.25861  2.00251   -33.07304 1.000 29.99444  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.53416  1.71832   -30.18384 1.000 28.86672  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -5.87696  2.91213   -30.82485 1.000 31.49178  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.31176  4.20858   -30.56464 1.000 31.52248  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -4.84930  2.73231   -31.75293 1.000 34.51679  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -5.71056  5.31553   -31.20162 1.000 30.63473  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.25609  3.80783   -32.39691 1.000 38.82674  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.67697  5.10549   -32.10350 1.000 40.49510  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.07740  6.17896   -32.74737 1.000 41.14659  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.07582  0.10165   -32.79010 1.000 29.78905  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.85729  -0.02329  -34.23415 1.000 29.35300  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.17840  -0.14152  -34.97916 1.000 33.88547  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.31954  0.37744   -36.10133 1.000 33.91629  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -5.95262  -1.23436  -34.50549 1.000 34.53473  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.46563  -0.96565  -34.13483 1.000 39.94594  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.48221  -1.95828  -34.75688 1.000 56.48178  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -3.91754  -2.83142  -35.54928 1.000 46.09756  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.27041  -1.86899  -34.43642 1.000 56.41239  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.17403  -0.77772  -34.35974 1.000 33.27652  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.44989 -0.97325  -35.05198 1.000 35.81917  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.22901 0.32631   -35.18769 1.000 38.26351  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.16918 0.39186   -35.98695 1.000 42.36788  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.30411 -2.00576  -34.30351 1.000 35.59294  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.67787 -1.48149  -33.04747 1.000 44.03520  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.85791 1.37455   -34.44467 1.000 35.42233  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.52881 2.66585   -34.61425 1.000 37.46560  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.23150 3.26972   -35.97914 1.000 46.65884  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.07913 3.95636   -36.56434 1.000 48.73662  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.07622 3.63379   -33.52536 1.000 42.46555  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.54529 3.21800   -32.13857 1.000 40.85243  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.06065 4.23929   -31.12761 1.000 50.79287  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.04062 3.06445   -32.09136 1.000 51.01559  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.01816 3.07759   -36.49028 1.000 39.85432  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.71032  3.63417   -37.80069 1.000 43.84192  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.79255  2.60634   -38.91719 1.000 45.33362  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.76920  2.99535   -40.08422 1.000 43.50563  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.33004  4.30301   -37.80467 1.000 47.69242  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.31718  3.30917   -37.65348 1.000 52.75101  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.20733  5.27530   -36.67369 1.000 44.02225  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -9.90552  1.31507   -38.60085 1.000 41.95738  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.10779 0.28297   -39.62380 1.000 41.53687  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -11.03286 -0.76811  -39.03351 1.000 38.59312  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.57701 -1.77302  -38.45408 1.000 36.76177  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.77391  -0.31543  -40.08403 1.000 41.63968  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -8.94663  -1.41154  -41.13334 1.000 47.47598  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -10.09679 -1.74488  -41.48440 1.000 56.24118  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -7.91821  -1.89828  -41.64489 1.000 53.06173  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.35225 -0.57660  -39.13087 1.000 49.14271  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.29917 -1.51946  -38.51375 1.000 39.31366  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -13.11948 -2.95176  -39.00037 1.000 44.44283  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.48947 -3.90013  -38.29800 1.000 43.12162  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.67127 -0.98240  -38.94608 1.000 46.22735  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.46133 0.45380   -39.27667 1.000 54.21627  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -12.97877 0.73603   -39.39582 1.000 49.02128  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.55733 -3.13363  -40.18854 1.000 41.83070  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -12.39438 -4.47138  -40.73705 1.000 42.59467  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -11.44318 -5.33162  -39.90082 1.000 44.36892  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -11.51412 -6.56093  -39.98320 1.000 36.17530  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -11.96730 -4.33004  -42.20732 1.000 44.47466  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -10.56638 -4.27202  -42.35265 1.000 48.12857  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.60994 -4.72224  -39.04138 1.000 35.50142  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.76507  -5.48556  -38.12639 1.000 36.68177  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -10.55560 -6.34944  -37.15459 1.000 34.57523  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -9.98250  -7.26106  -36.56247 1.000 34.07425  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.84643  -4.53660  -37.35701 1.000 33.62135  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -7.89321  -3.86644  -38.32406 1.000 40.05763  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.63389  -3.38749  -37.69391 1.000 41.07107  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.76215  -2.68891  -38.75510 1.000 40.96973  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -4.51141  -2.24024  -38.08721 1.000 48.78396  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.84786 -6.09062  -36.96773 1.000 34.56671  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.67726 -6.93530  -36.11747 1.000 33.60601  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -13.40703 -8.02724  -36.90869 1.000 38.02858  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -14.27028 -8.71100  -36.34838 1.000 34.99531  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.68197 -6.06973  -35.36314 1.000 34.11561  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -13.05312 -5.16053  -34.28125 1.000 33.30135  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -14.11356 -4.35731  -33.52937 1.000 43.43739  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -12.18167 -5.97055  -33.30902 1.000 32.55774  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -13.10204 -8.18447  -38.20321 1.000 36.05088  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -13.73547 -9.24422  -38.99150 1.000 38.98997  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -13.42491 -10.62110 -38.41514 1.000 39.76609  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -14.23124 -11.55071 -38.54007 1.000 38.75900  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -13.28043 -9.16116  -40.45128 1.000 35.99880  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -13.90905 -7.99066  -41.17980 1.000 51.63136  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.86390 -7.38907  -40.62933 1.000 48.81819  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -13.44358 -7.66692  -42.29382 1.000 61.91422  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -12.28446 -10.75619 -37.75539 1.000 39.78938  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -11.84641 -11.98609 -37.10749 1.000 36.34649  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -12.44033 -12.17019 -35.70376 1.000 40.89620  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -11.99371 -13.05197 -34.95756 1.000 38.50058  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -10.31746 -11.98424 -37.03417 1.000 35.48321  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -9.81604  -10.75371 -36.47922 1.000 38.07078  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -13.39447 -11.33062 -35.30710 1.000 40.49103  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -14.06157 -11.49942 -34.03540 1.000 34.89936  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -14.34944 -10.16186 -33.38859 1.000 40.68018  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -13.42242 -9.39541  -33.11344 1.000 36.82390  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.62312 -9.85773  -33.15007 1.000 37.07199  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -15.97770 -8.55457  -32.60692 1.000 40.52373  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -15.90127 -8.51378  -31.08366 1.000 40.39858  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.70568 -7.43989  -30.51429 1.000 36.69284  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -17.38408 -8.17022  -33.07949 1.000 52.01046  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.40814 -7.30930  -34.35946 1.000 54.95888  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -18.66467 -6.43540  -34.44584 1.000 82.04693  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -18.35551 -4.94637  -34.23678 1.000 78.66970  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -17.70200 -4.31582  -35.42586 1.000 75.59013  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -16.01360 -9.64760  -30.40403 1.000 38.05763  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -16.06586 -9.62318  -28.94655 1.000 37.93529  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.67729 -9.45739  -28.35923 1.000 31.26139  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.71865 -10.10572 -28.78872 1.000 35.22877  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.72443 -10.88933 -28.40740 1.000 42.37053  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -18.10338 -11.09372 -28.97275 1.000 46.95884  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -18.10151 -12.10618 -30.09938 1.000 77.55351  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -17.29512 -11.94422 -31.04696 1.000 75.39898  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -18.89297 -13.07007 -30.03304 1.000 104.51422 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.57368 -8.58204  -27.35872 1.000 31.40802  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.31741 -8.27163  -26.69067 1.000 26.27116  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.46010 -8.74427  -25.24370 1.000 28.27293  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -14.16131 -8.10162  -24.44049 1.000 26.78986  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -13.04249 -6.76672  -26.75660 1.000 28.87158  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -12.90260 -6.16227  -28.16126 1.000 28.46150  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.45246 -4.70872  -28.02280 1.000 32.72349  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -11.91454 -6.95892  -28.99600 1.000 29.75164  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.81114 -9.86294  -24.91024 1.000 26.24203  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -13.02416 -10.43740 -23.58917 1.000 24.69346  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -11.82792 -11.28107 -23.17586 1.000 25.52639  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -10.91814 -11.54658 -23.96679 1.000 24.22200  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -14.31345 -11.26119 -23.55115 1.000 27.86690  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -14.30893 -12.41814 -24.50368 1.000 31.25888  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -15.19957 -12.52285 -25.55178 1.000 36.85770  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -13.52085 -13.51764 -24.56818 1.000 34.91606  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -14.97157 -13.64894 -26.20964 1.000 38.42313  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -13.95105 -14.26395 -25.64159 1.000 33.80597  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -11.87475 -11.72024 -21.91254 1.000 24.55947  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -10.87048 -12.57549 -21.28595 1.000 25.70645  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.57814 -13.75759 -20.62425 1.000 27.23659  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.52063 -13.56497 -19.84614 1.000 28.21846  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -10.03628 -11.79468 -20.23907 1.000 22.73424  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.33239  -10.60335 -20.86801 1.000 26.34063  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.05042  -12.74120 -19.55546 1.000 26.47515  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.71735  -9.64899  -19.86853 1.000 27.94338  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -11.12343 -14.98228 -20.91532 1.000 24.75351  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.66988 -16.17340 -20.27416 1.000 25.57076  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -10.58782 -16.86319 -19.45994 1.000 27.10536  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -9.45868  -17.00593 -19.92792 1.000 27.12505  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -12.21885 -17.16104 -21.29896 1.000 26.60711  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -13.38140 -16.59614 -22.08892 1.000 26.09721  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -14.12948 -15.74611 -21.60336 1.000 28.05987  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -13.58202 -17.11700 -23.29230 1.000 28.20241  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -10.94468 -17.30281 -18.24599 1.000 23.84422  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -10.05506 -18.08160 -17.38291 1.000 25.30170  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -10.59818 -19.50092 -17.31690 1.000 27.56010  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -11.74118 -19.69887 -16.90772 1.000 26.29411  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -9.99115  -17.47660 -15.97951 1.000 23.43683  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.62699  -16.00639 -15.95573 1.000 25.82087  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.63111  -15.50309 -14.50022 1.000 28.67509  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -8.26842  -15.72247 -16.63276 1.000 25.83676  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -9.79628  -20.47715 -17.74362 1.000 26.47316  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -10.25752 -21.85207 -17.91198 1.000 26.10216  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -9.35627  -22.82951 -17.17199 1.000 29.68239  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -8.32725  -23.26168 -17.71136 1.000 32.80295  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -10.31231 -22.22483 -19.39663 1.000 28.16614  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -11.06275 -21.14960 -20.16018 1.000 28.33858  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -10.96967 -23.60837 -19.53893 1.000 29.60341  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -11.19347 -21.45026 -21.70247 1.000 36.37452  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -9.67627  -23.16862 -15.93461 1.000 29.48406  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -8.91993  -24.20466 -15.22685 1.000 31.35106  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -9.33793  -25.58685 -15.68922 1.000 36.41664  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -10.49005 -25.82644 -16.05487 1.000 36.93006  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -9.31756  -23.97571 -13.76557 1.000 37.35237  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -10.72769 -23.48193 -13.88116 1.000 34.73126  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -10.79721 -22.64919 -15.13264 1.000 30.87754  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -8.37854  -26.51132 -15.65503 1.000 38.18370  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -8.62128  -27.89731 -16.05136 1.000 38.62660  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -7.86629  -28.79844 -15.08384 1.000 40.79012  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -6.65781  -28.98930 -15.23063 1.000 40.06086  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -8.17163  -28.14278 -17.48592 1.000 39.13646  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -8.61625  -29.49555 -18.01339 1.000 46.05217  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -8.55098  -30.52461 -17.31969 1.000 45.36634  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -9.06064  -29.50337 -19.26314 1.000 48.24406  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -8.58688  -29.38773 -14.12555 1.000 38.96039  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -7.93093  -30.21736 -13.12914 1.000 40.17162  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -7.39206  -31.51398 -13.72130 1.000 46.21996  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -6.40277  -32.04651 -13.21040 1.000 48.55078  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -8.88630  -30.52135 -11.97737 1.000 40.23685  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -8.99262  -29.36735 -10.95518 1.000 50.85778  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.12528 -29.58514 -9.95010  1.000 59.13600  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -10.30067 -28.36084 -9.04839  1.000 61.66126  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.45915 -28.48885 -8.11828  1.000 64.05563  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -8.01927  -32.03793 -14.77759 1.000 52.02635  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -7.54942  -33.29143 -15.37650 1.000 52.41745  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -6.19910  -33.11489 -16.06222 1.000 53.00273  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -5.28799  -33.92834 -15.87138 1.000 49.44045  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -8.57402  -33.83703 -16.37363 1.000 59.21886  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -9.63034  -34.78187 -15.79843 1.000 77.81162  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -10.69540 -34.06912 -14.99422 1.000 96.74249  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.43526 -33.23468 -15.52093 1.000 110.35595 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -10.81124 -34.42758 -13.72030 1.000 87.05739  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -6.05560  -32.06785 -16.87995 1.000 43.60620  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -4.77961  -31.77463 -17.52542 1.000 47.35421  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -3.84371  -30.97377 -16.63518 1.000 44.25446  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -2.68166  -30.77160 -17.01031 1.000 36.62353  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -4.98402  -30.99244 -18.82327 1.000 48.20871  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -5.87116  -31.71619 -19.80745 1.000 62.86663  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -6.31847  -31.06224 -20.77145 1.000 65.53547  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -6.10668  -32.93027 -19.62529 1.000 64.35475  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -4.32942  -30.51208 -15.48427 1.000 39.40713  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -3.56265  -29.64798 -14.59914 1.000 35.58372  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -3.08371  -28.39533 -15.33511 1.000 33.02915  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -1.91820  -28.00260 -15.25769 1.000 34.37066  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -2.38155  -30.37493 -13.97611 1.000 38.57430  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.05283  -29.73052 -12.66763 1.000 42.29423  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -0.62319  -29.86652 -12.36401 1.000 51.21446  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.36623  -31.19035 -11.85171 1.000 45.82686  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 0.78026   -31.84064 -11.99216 1.000 60.34915  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 1.81723   -31.29506 -12.61123 1.000 49.09471  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.89138   -33.06444 -11.49263 1.000 57.64700  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -3.99990  -27.75108 -16.02950 1.000 32.06318  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -3.65824  -26.53925 -16.76020 1.000 32.57663  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -4.60946  -25.42115 -16.37942 1.000 31.58732  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -5.77107  -25.64547 -16.02401 1.000 31.52097  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -3.69647  -26.71963 -18.28873 1.000 36.08768  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -5.01027  -27.11774 -18.69919 1.000 37.01725  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -2.66006  -27.72849 -18.75462 1.000 37.18259  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -4.08186  -24.20564 -16.42166 1.000 26.79710  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -4.87634  -22.99517 -16.31932 1.000 27.48420  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -4.64240  -22.19153 -17.58779 1.000 32.24769  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -3.50119  -21.86730 -17.91965 1.000 30.95942  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -4.50755  -22.17945 -15.07667 1.000 26.78719  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -5.18363  -20.79732 -14.98510 1.000 30.25010  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -6.67137  -20.96560 -14.80132 1.000 32.45321  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -4.59856  -19.98582 -13.77916 1.000 30.26623  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -5.71361  -21.90547 -18.30813 1.000 28.57500  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -5.61665  -21.22056 -19.58446 1.000 27.61074  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -6.21015  -19.83158 -19.45583 1.000 27.30741  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -7.32856  -19.67589 -18.95006 1.000 31.61593  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -6.34627  -21.98835 -20.67570 1.000 28.55758  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -5.74475  -23.27231 -20.86770 1.000 33.40619  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -6.22682  -21.21436 -21.97486 1.000 32.42442  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -5.47894  -18.83309 -19.94782 1.000 26.14084  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -5.93661  -17.45151 -19.99749 1.000 24.30128  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -6.10411  -17.10098 -21.47288 1.000 29.58922  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -5.12113  -17.10448 -22.23085 1.000 28.08556  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -4.96653  -16.48325 -19.31659 1.000 27.28835  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -4.83446  -16.78479 -17.81083 1.000 33.49900  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.45027  -15.03329 -19.50749 1.000 30.17160  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -3.71571  -17.73338 -17.44920 1.000 35.40916  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -7.33965  -16.84958 -21.89290 1.000 24.18807  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -7.63224  -16.61184 -23.30701 1.000 23.48166  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -8.12043  -15.17749 -23.45219 1.000 31.25025  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -9.00939  -14.74967 -22.70319 1.000 29.03211  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -8.72080  -17.54663 -23.85077 1.000 27.80532  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -9.02891  -17.19109 -25.32968 1.000 28.52121  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -8.40064  -19.00431 -23.65390 1.000 40.21535  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.59601  -14.44671 -24.44981 1.000 26.29222  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -8.12920  -13.12335 -24.74256 1.000 24.14947  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -8.36518  -13.04803 -26.24542 1.000 26.08502  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -7.79537  -13.82325 -27.01911 1.000 26.32022  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -7.18853  -12.01271 -24.24387 1.000 25.19633  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -5.86541  -11.92178 -25.04590 1.000 29.63857  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -5.87454  -11.62956 -26.28020 1.000 32.20812  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -4.80648  -12.25183 -24.46011 1.000 27.81860  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -9.25345  -12.14808 -26.64673 1.000 23.39504  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -9.47448  -11.85953 -28.06450 1.000 24.83892  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.78977  -10.55749 -28.47589 1.000 23.96537  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -9.33520  -9.75815  -29.24700 1.000 26.60725  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -10.96988 -11.82369 -28.36004 1.000 29.03921  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.61834 -11.01455 -27.36811 1.000 26.97929  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -11.54459 -13.23659 -28.30969 1.000 29.90792  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.57021  -10.32432 -27.98708 1.000 24.49580  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.86867  -9.08045  -28.28016 1.000 26.08301  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -6.22569  -9.12125  -29.65401 1.000 24.38041  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.55770  -9.95545  -30.49433 1.000 25.91482  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -5.22748  -8.25967  -29.84775 1.000 25.53508  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.59957  -8.12709  -31.17102 1.000 25.47125  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.78288  -9.33789  -31.60699 1.000 26.53034  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.54984  -9.51454  -32.81337 1.000 27.61031  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.74156  -6.84733  -31.17406 1.000 25.30224  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -3.38367  -6.44117  -32.62330 1.000 28.29642  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.50244  -7.00094  -30.24111 1.000 25.51013  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -2.88441  -5.00776  -32.75340 1.000 39.44687  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -3.33483  -10.19538 -30.68807 1.000 27.41278  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -2.55086  -11.34245 -31.10585 1.000 28.60008  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -1.10009  -10.96051 -31.36099 1.000 27.81643  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.68350  -9.80887  -31.23895 1.000 30.22754  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -0.32225  -11.94916 -31.74972 1.000 24.53703  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 1.11707   -11.78645 -31.88759 1.000 28.57823  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 1.55821   -12.41858 -33.19136 1.000 24.99946  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 1.13049   -13.53616 -33.53968 1.000 26.02096  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 1.75138   -12.46351 -30.68529 1.000 26.42332  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 1.49759   -11.72046 -29.39216 1.000 27.69534  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 2.66411   -12.25223 -28.12945 1.000 32.67454  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 1.55225   -13.53941 -27.59230 1.000 29.09045  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 2.41841   -11.70641 -33.91637 1.000 24.91784  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 2.93493   -12.26686 -35.15385 1.000 28.55223  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 4.08136   -13.24436 -34.86776 1.000 30.82352  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 4.62473   -13.31362 -33.77138 1.000 29.38548  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 3.45674   -11.15545 -36.04945 1.000 33.61371  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 4.58087   -10.55602 -35.38449 1.000 31.31291  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.38338   -10.10101 -36.26745 1.000 30.86103  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 4.49569   -13.97198 -35.89413 1.000 25.07195  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 5.67503   -14.81200 -35.74022 1.000 31.25233  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 6.89588   -14.00254 -35.28404 1.000 29.52157  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 7.64139   -14.45003 -34.39799 1.000 31.32967  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 5.97872   -15.53770 -37.05615 1.000 30.64663  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 6.98408   -16.68503 -36.85359 1.000 35.12198  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 7.37955   -17.35756 -38.18389 1.000 37.62043  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 8.33958   -18.53430 -37.94592 1.000 49.93965  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 8.98256   -19.03441 -39.20504 1.000 52.86594  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 7.11457   -12.81779 -35.86840 1.000 30.89203  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 8.27159   -12.00803 -35.48675 1.000 33.33473  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 8.14859   -11.49078 -34.05292 1.000 31.08072  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 9.15792   -11.34509 -33.34774 1.000 32.64188  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 8.44236   -10.84999 -36.45346 1.000 32.81187  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 6.92840   -11.19815 -33.60604 1.000 31.17164  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 6.73151   -10.86547 -32.19351 1.000 29.24493  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 7.26144   -11.98287 -31.30579 1.000 33.11039  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 7.98133   -11.72317 -30.32896 1.000 32.09678  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.25028   -10.66753 -31.87229 1.000 28.57717  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 4.68705   -9.33252  -32.34368 1.000 33.25070  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.44296   -8.34544  -32.51490 1.000 33.87081  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 3.44860   -9.29647  -32.51765 1.000 32.65089  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 6.84901   -13.23634 -31.60686 1.000 26.59540  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 7.19460   -14.40477 -30.79813 1.000 27.44250  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 8.68280   -14.66683 -30.79779 1.000 32.31133  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 9.25712   -15.02994 -29.76564 1.000 32.89283  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 6.45900   -15.66107 -31.30135 1.000 27.60346  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 4.93160   -15.61312 -31.18366 1.000 28.69593  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 4.27752   -16.83786 -31.86264 1.000 27.95933  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 4.49569   -15.50045 -29.70158 1.000 29.90927  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 9.32308   -14.54239 -31.94862 1.000 30.94963  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 10.70792  -14.97204 -32.04660 1.000 33.36874  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 11.67363  -13.87266 -31.64872 1.000 36.50495  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 12.71739  -14.15425 -31.04951 1.000 39.09181  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 10.98735  -15.48243 -33.46614 1.000 35.59021  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 10.23270  -16.79238 -33.68684 1.000 32.10167  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 12.47073  -15.64541 -33.70951 1.000 40.08428  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 10.19968  -17.17201 -35.18096 1.000 41.87782  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 11.36927  -12.62298 -31.99270 1.000 31.61103  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 12.36709  -11.57282 -31.81044 1.000 39.65777  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 11.84404  -10.27543 -31.17335 1.000 39.87571  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.49511  -9.73659  -30.27836 1.000 42.50193  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 13.00960  -11.23855 -33.15123 1.000 46.49464  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 14.25958  -10.40208 -32.99518 1.000 67.36966  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 14.98321  -10.52850 -32.00592 1.000 80.93826  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 14.52144  -9.54151  -33.96675 1.000 72.52165  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 10.70886  -9.73305  -31.62716 1.000 39.12670  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.35222  -8.35139  -31.25319 1.000 36.47127  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 10.14412  -8.20576  -29.75084 1.000 38.81996  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.73480  -7.32411  -29.11814 1.000 51.11607  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.08281   -7.87195  -31.97018 1.000 33.79497  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 9.18077   -7.87133  -33.49381 1.000 41.84236  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 10.26243  -7.82271  -34.07195 1.000 46.15766  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 8.00847   -7.86119  -34.15028 1.000 44.89657  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.26768   -9.03169  -29.17370 1.000 33.53320  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 8.88466   -8.83101  -27.77868 1.000 34.01682  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.02918  -9.16453  -26.83170 1.000 37.78164  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.15676  -8.53676  -25.76520 1.000 35.31620  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 7.64181   -9.66241  -27.45208 1.000 34.28189  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.39998   -9.20289  -28.22524 1.000 33.72397  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.17789   -9.95171  -27.74712 1.000 36.92822  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 6.16558   -7.68343  -28.11794 1.000 34.18053  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 10.86865  -10.13309 -27.20331 1.000 35.77063  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.04093  -10.44526 -26.40402 1.000 36.66154  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.07920  -9.33969  -26.47035 1.000 43.59137  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 13.70923  -9.01020  -25.46666 1.000 38.61492  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.27577  -8.75409  -27.65493 1.000 35.31164  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.16297  -7.60843  -27.76333 1.000 33.62927  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.70535  -6.47084  -26.85378 1.000 38.28742  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.51459  -5.86708  -26.14196 1.000 39.96839  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 14.21876  -7.12599  -29.20254 1.000 40.36317  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.89286  -8.10644  -29.99221 1.000 47.65804  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 14.95964  -5.83219  -29.25302 1.000 40.44046  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.40908  -6.14884  -26.88192 1.000 32.51604  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.87973  -5.12143  -25.98486 1.000 37.68492  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 12.10459  -5.50987  -24.53008 1.000 43.33839  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 12.42433  -4.66308  -23.68712 1.000 47.38711  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.38873  -4.86053  -26.27192 1.000 40.30738  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 10.16829  -4.46721  -27.73410 1.000 47.71940  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.80747   -3.84846  -25.29083 1.000 45.49617  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.49176  -3.01528  -27.98011 1.000 50.19933  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.95317  -6.79423  -24.21551 1.000 35.57830  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 12.03925  -7.25162  -22.82816 1.000 38.99630  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.45582  -7.17358  -22.27152 1.000 42.06872  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.63341  -7.25106  -21.05252 1.000 41.71056  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.51691  -8.68358  -22.71925 1.000 40.48926  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.46716  -7.01225  -23.12954 1.000 38.08989  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.84573  -6.99721  -22.65157 1.000 37.36339  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 16.08788  -5.82652  -21.69358 1.000 39.62409  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.68177  -5.99891  -20.61869 1.000 37.53082  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.79635  -6.95022  -23.85006 1.000 42.56138  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.12065  -7.63082  -23.67475 1.000 48.77993  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.92398  -7.62173  -24.99273 1.000 58.26902  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 20.41115  -7.92544  -24.77014 1.000 68.76369  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 21.34619  -6.81185  -25.14626 1.000 63.77171  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.62684  -4.62418  -22.04883 1.000 38.96497  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.92048  -3.48222  -21.18529 1.000 35.80731  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 15.14713  -3.58258  -19.87465 1.000 37.42791  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.68570  -3.27145  -18.80193 1.000 36.45241  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.58585  -2.15290  -21.87498 1.000 45.03220  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.20147  -2.03924  -22.14882 1.000 47.64297  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.88119  -3.99695  -19.95324 1.000 37.88369  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 13.08302  -4.14798  -18.75373 1.000 36.65120  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.62116  -5.23363  -17.84322 1.000 34.65138  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.60376  -5.08976  -16.62264 1.000 31.91146  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 14.11660  -6.32907  -18.42405 1.000 33.79797  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.74043  -7.38005  -17.62086 1.000 34.26690  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.95367  -6.86014  -16.86410 1.000 34.44086  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 16.09850  -7.10598  -15.66213 1.000 36.87051  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 15.14251  -8.56826  -18.51555 1.000 32.46614  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.95989  -9.13324  -19.08308 1.000 40.27325  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.90240  -9.59530  -17.70946 1.000 36.76713  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.84891  -6.15354  -17.56367 1.000 33.03812  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 18.02039  -5.56918  -16.92171 1.000 35.78531  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.63230  -4.60978  -15.80689 1.000 36.72012  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 18.27933  -4.58490  -14.75755 1.000 36.21162  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.87660  -4.83311  -17.94770 1.000 40.30609  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 20.05025  -4.08520  -17.33706 1.000 47.71363  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 21.04674  -3.64433  -18.40134 1.000 50.17931  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 22.13215  -2.74365  -17.81442 1.000 66.73065  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.73168  -1.87370  -18.86358 1.000 72.39501  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.59680  -3.79404  -16.02426 1.000 35.87117  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 16.19299  -2.84550  -14.98908 1.000 38.72514  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.58167  -3.56401  -13.79165 1.000 35.10121  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.85378  -3.19940  -12.63645 1.000 37.31487  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 15.20659  -1.82438  -15.55881 1.000 34.55252  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.75822  -4.58392  -14.05026 1.000 31.99715  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 14.11954  -5.33301  -12.97402 1.000 36.23926  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 15.15982  -6.03771  -12.10843 1.000 38.25623  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 15.11744  -5.95669  -10.86704 1.000 36.07786  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 13.12620  -6.32386  -13.58992 1.000 32.56977  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.40040  -7.18189  -12.58963 1.000 32.39528  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.79554  -6.63046  -11.46324 1.000 33.24753  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 12.32196  -8.54978  -12.77665 1.000 36.01771  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 11.12448  -7.44784  -10.53635 1.000 31.71594  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.65737  -9.35715  -11.86055 1.000 37.36757  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 11.05860  -8.80789  -10.74052 1.000 33.56306  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 16.13912  -6.68894  -12.74256 1.000 33.43310  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 17.17975  -7.34687  -11.96661 1.000 41.21951  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 18.02915  -6.37413  -11.16498 1.000 40.38412  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.48298  -6.71980  -10.06608 1.000 48.65402  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 18.04347  -8.20959  -12.87847 1.000 41.82358  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.38841  -9.52412  -13.12902 1.000 49.15226  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.02566  -10.40244 -14.53323 1.000 61.32923  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.61644  -11.97821 -13.88475 1.000 58.34374  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 18.28145  -5.17918  -11.68848 1.000 42.71896  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.96617  -4.17128  -10.88527 1.000 47.89175  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 18.11348  -3.77910  -9.68582  1.000 46.81522  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.61739  -3.66295  -8.55978  1.000 50.60387  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 19.28917  -2.95531  -11.75557 1.000 48.79409  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 20.49235  -3.18178  -12.69157 1.000 59.65362  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 21.01594  -1.90336  -13.32153 1.000 81.99259  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.46627  -1.50405  -14.37204 1.000 92.03135  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 21.96712  -1.29626  -12.77179 1.000 86.47165  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.80766  -3.60448  -9.90637  1.000 41.18616  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.91008  -3.20679  -8.82456  1.000 44.98604  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.84480  -4.27327  -7.74225  1.000 44.84359  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.81031  -3.95274  -6.54674  1.000 48.33040  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 14.51173  -2.92974  -9.38177  1.000 36.82805  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.81802  -5.54913  -8.14767  1.000 44.48172  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.76948  -6.64890  -7.18909  1.000 45.81206  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.98738  -6.63277  -6.27871  1.000 54.18319  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.88250  -6.94701  -5.08791  1.000 52.43182  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.66527  -7.99258  -7.91053  1.000 40.11451  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 14.32056  -8.33979  -8.55811  1.000 46.06236  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.44213  -9.56992  -9.47465  1.000 44.30912  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 13.19739  -8.53957  -7.52671  1.000 40.99032  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 18.15226  -6.25989  -6.81975  1.000 53.71624  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 19.33312  -6.07399  -5.97603  1.000 57.54775  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 19.17528  -4.88915  -5.03233  1.000 55.88332  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.75111  -4.88458  -3.93578  1.000 62.38824  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.57616  -5.87675  -6.84478  1.000 63.36890  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.89564  -7.04348  -7.74092  1.000 64.48105  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.93289  -8.34944  -6.96835  1.000 84.37196  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 21.71936  -8.50576  -6.02634  1.000 74.82103  ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 20.07762  -9.29790  -7.36133  1.000 79.97429  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 18.42396  -3.87213  -5.44180  1.000 56.78312  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 18.26090  -2.66348  -4.64752  1.000 63.90573  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 17.11486  -2.76501  -3.64692  1.000 64.82611  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 16.77718  -1.76113  -3.01885  1.000 67.09078  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 18.04596  -1.45235  -5.56355  1.000 62.54816  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 16.49495  -3.93925  -3.49795  1.000 58.88467  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 15.44907  -4.12588  -2.50783  1.000 61.64896  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 14.04999  -4.30745  -3.05877  1.000 59.85587  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 13.11619  -4.51658  -2.27275  1.000 55.86323  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.86277  -4.22117  -4.37145  1.000 46.52080  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.56088  -4.50641  -4.94737  1.000 48.58261  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 12.21946  -5.98399  -4.75718  1.000 52.12219  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 13.03221  -6.78939  -4.29103  1.000 48.28885  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 12.52926  -4.12258  -6.42742  1.000 43.81733  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.98919  -6.34441  -5.09118  1.000 44.69442  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.60014  -7.73618  -4.96391  1.000 49.31175  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.87289   -8.16222  -6.22729  1.000 44.29603  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.45631   -7.33502  -7.04441  1.000 40.63071  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.72062   -7.99126  -3.73557  1.000 51.01657  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.36784   -7.33186  -3.84183  1.000 62.79653  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.30789   -6.08741  -3.77193  1.000 66.43330  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.36347   -8.07405  -3.98312  1.000 62.40412  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.71323   -9.48116  -6.34795  1.000 45.78426  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.21498   -10.08500 -7.58219  1.000 36.60910  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.84066   -9.53127  -7.94736  1.000 37.76375  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.52857   -9.37951  -9.13636  1.000 36.70034  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.25677   -11.62644 -7.42969  1.000 39.07868  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.70579  -12.10584 -7.62875  1.000 41.02773  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.31943   -12.37849 -8.42254  1.000 36.44729  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.05730  -13.43005 -6.98445  1.000 46.17621  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 7.03192   -9.12951  -6.94684  1.000 39.37251  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.68947   -8.63020  -7.24644  1.000 37.40360  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.71268   -7.35917  -8.10318  1.000 40.83762  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.68614   -6.99255  -8.68619  1.000 41.10609  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.91466   -8.35744  -5.96271  1.000 42.96458  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 5.30530   -7.11057  -5.39037  1.000 45.58759  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.85286   -6.68776  -8.21653  1.000 33.87033  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.93868   -5.43538  -8.96204  1.000 35.97685  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 7.27615   -5.65358  -10.43787 1.000 36.81289  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.48081   -4.67954  -11.18020 1.000 34.44227  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.97065   -4.53261  -8.30162  1.000 39.74718  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.41315   -3.90843  -7.03304  1.000 48.49656  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.71851   -3.44521  -5.89188  1.000 56.42018  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 9.49973   -2.18493  -6.88413  1.000 49.57083  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 7.28785   -6.90973  -10.88132 1.000 31.18566  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.81525   -7.25681  -12.20023 1.000 27.09763  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 7.05830   -6.53665  -13.31389 1.000 29.10195  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.64466   -6.18488  -14.34703 1.000 31.56189  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.79156   -8.79030  -12.35736 1.000 30.00803  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.43483   -9.21769  -13.68079 1.000 28.43525  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 6.35434   -9.33721  -12.21793 1.000 30.71688  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.57994   -10.76933 -13.80978 1.000 25.72488  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.76674   -6.25962  -13.11145 1.000 30.78076  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.98317   -5.62565  -14.16197 1.000 37.46431  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 5.38004   -4.18410  -14.40996 1.000 39.45763  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 5.18290   -3.66169  -15.51055 1.000 39.71120  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.96378   -3.52484  -13.40946 1.000 35.90280  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 6.40167   -2.15383  -13.65126 1.000 39.64932  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.57560   -2.07624  -14.59849 1.000 39.85364  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.97987   -0.96997  -14.95944 1.000 45.57828  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.75479   -1.43506  -12.34507 1.000 38.37696  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.70871   -1.58119  -11.25892 1.000 45.17764  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 6.16733   -1.04124  -9.91666  1.000 67.77016  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.83956   -0.00478  -9.84483  1.000 79.12827  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.78964   -1.73787  -8.83631  1.000 58.78704  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 8.12283   -3.21434  -15.00704 1.000 32.76995  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 9.22909   -3.29518  -15.95138 1.000 28.15401  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.83992   -3.90348  -17.28852 1.000 31.65084  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.70817   -4.10297  -18.14761 1.000 32.23856  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.37172  -4.08144  -15.29860 1.000 30.48574  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.81107  -3.46528  -13.98560 1.000 31.86831  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 11.78620  -2.47007  -13.96844 1.000 32.12286  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 10.21755  -3.84314  -12.78524 1.000 31.66828  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 12.17720  -1.87270  -12.78423 1.000 32.72071  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.62251  -3.23919  -11.56630 1.000 31.36229  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.59790  -2.26193  -11.57848 1.000 36.94062  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.56704   -4.20372  -17.49019 1.000 34.77035  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 7.13753   -4.73992  -18.77111 1.000 34.40474  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.48012   -6.18349  -19.04671 1.000 38.21955  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.34350   -6.62301  -20.18943 1.000 36.11192  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.91570   -6.95285  -18.04734 1.000 34.55937  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.27885   -8.34354  -18.30072 1.000 27.60302  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.44027   -9.26033  -17.40643 1.000 27.18671  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.88137   -10.36300 -17.03716 1.000 25.26950  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.79111   -8.57147  -18.10351 1.000 27.99511  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.55093  -7.83111  -19.16596 1.000 36.16760  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 10.24592  -8.04531  -16.74563 1.000 28.32803  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.21155   -8.82497  -17.09262 1.000 26.49288  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.32343   -9.61094  -16.24770 1.000 25.98397  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.99243   -11.00144 -16.77886 1.000 27.11227  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.67964   -11.90781 -15.99584 1.000 28.55912  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 5.04415   -11.20101 -18.10422 1.000 25.52851  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.70911   -12.51255 -18.64050 1.000 23.22894  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.49859   -13.62537 -17.94496 1.000 25.33725  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 4.95891   -14.70520 -17.66426 1.000 26.62276  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 5.01696   -12.58550 -20.13477 1.000 26.73421  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 4.97306   -13.98927 -20.66963 1.000 29.16505  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.75325   -14.62242 -20.88949 1.000 28.69207  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 6.15037   -14.69174 -20.91876 1.000 28.57878  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 3.70569   -15.94895 -21.38082 1.000 27.08201  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 6.10797   -16.01993 -21.40385 1.000 27.12103  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 4.88495   -16.62939 -21.63969 1.000 27.16329  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.79145   -13.38727 -17.69454 1.000 25.55097  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.66829   -14.44268 -17.19725 1.000 24.59750  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.33648   -14.84588 -15.76634 1.000 26.37373  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 7.80243   -15.90105 -15.31877 1.000 26.30366  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 9.13322   -13.99950 -17.32840 1.000 27.77961  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.51220   -13.66912 -18.78162 1.000 28.86011  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.79597   -14.68246 -19.72281 1.000 29.13808  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.52950   -12.36475 -19.21412 1.000 29.95676  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.10617  -14.35594 -21.06530 1.000 27.90349  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 9.82968   -12.04691 -20.53093 1.000 35.58631  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.12619  -13.02545 -21.44331 1.000 33.98152  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.44188  -12.63806 -22.74250 1.000 38.51562  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.50846   -14.06122 -15.05640 1.000 23.22988  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 6.01382   -14.51306 -13.76207 1.000 27.20746  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 5.14213   -15.75441 -13.88337 1.000 26.83915  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.87010   -16.38943 -12.86046 1.000 25.82701  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.24151   -13.36753 -13.05976 1.000 23.90286  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.99303   -13.20117 -13.74599 1.000 27.46922  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.68523   -16.12077 -15.09947 1.000 26.22807  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 4.04837   -17.42042 -15.30097 1.000 24.17632  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 4.87416   -18.56814 -14.73179 1.000 23.91493  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 4.29749   -19.55216 -14.25732 1.000 25.40347  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 3.79446   -17.67327 -16.80445 1.000 22.50081  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 6.21752   -18.46618 -14.75831 1.000 22.71579  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 7.07558   -19.54577 -14.25395 1.000 26.93284  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 7.16482   -19.58634 -12.73029 1.000 28.29102  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.86346   -20.45507 -12.18996 1.000 28.13443  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.47078   -19.44039 -14.89680 1.000 21.01573  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 8.33312   -19.76157 -16.38980 1.000 25.18592  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 8.36760   -21.07515 -16.83149 1.000 24.49704  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 8.07972   -18.75229 -17.31994 1.000 25.88963  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 8.20252   -21.40789 -18.17663 1.000 26.13073  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 7.88542   -19.06540 -18.69933 1.000 27.60318  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 7.94305   -20.40724 -19.10260 1.000 26.51877  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 7.75567   -20.75439 -20.43140 1.000 27.37450  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.43183   -18.71569 -12.03531 1.000 24.12736  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 6.22917   -18.90338 -10.60463 1.000 27.42651  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.39142   -20.13942 -10.34389 1.000 29.34849  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 5.58010   -20.81854 -9.32448  1.000 29.00994  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.51822   -17.68607 -10.01159 1.000 24.35002  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.29936   -16.37500 -9.93217  1.000 27.30447  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.34262   -15.28696 -9.45601  1.000 25.41243  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.52207   -16.53047 -8.98490  1.000 27.11092  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.39402   -20.39031 -11.20055 1.000 24.57653  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.46526   -21.48835 -10.97389 1.000 24.64743  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 3.53207   -22.57114 -12.04051 1.000 28.99257  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.99058   -23.65897 -11.80552 1.000 28.35256  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 2.01087   -21.00290 -10.83640 1.000 25.85981  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.86201   -20.04620 -9.59517  1.000 27.68770  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 1.50308   -20.33972 -12.12486 1.000 25.54883  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 4.13215   -22.33135 -13.20206 1.000 27.08404  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 4.05301   -23.27444 -14.31659 1.000 26.55776  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 5.41193   -23.90144 -14.61274 1.000 30.80063  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 6.43779   -23.21480 -14.59571 1.000 32.41896  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 3.53402   -22.57421 -15.58326 1.000 26.48429  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 5.42085   -25.21675 -14.87075 1.000 30.40560  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 6.64136   -25.87541 -15.31857 1.000 35.43988  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 6.82419   -25.73462 -16.82593 1.000 37.91250  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 7.94513   -25.86855 -17.33130 1.000 33.42224  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 6.63629   -27.35393 -14.92750 1.000 39.29736  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 5.55808   -28.17757 -15.57819 1.000 42.40996  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 5.38775   -29.55881 -14.91607 1.000 75.65929  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 6.22220   -29.93936 -14.05801 1.000 72.33674  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 4.42764   -30.27562 -15.28168 1.000 76.08456  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 5.75353   -25.43905 -17.54607 1.000 30.02521  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 5.82253   -25.27708 -18.99160 1.000 27.21162  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 4.71212   -24.31459 -19.34948 1.000 31.44181  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 3.64506   -24.34243 -18.72894 1.000 27.46633  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 5.62987   -26.62314 -19.71925 1.000 28.69293  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 5.51012   -26.50889 -21.23916 1.000 31.99893  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 5.56236   -27.94412 -21.80353 1.000 35.19014  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 4.31641   -28.31004 -22.57220 1.000 45.76967  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 4.18197   -29.82080 -22.58665 1.000 48.66795  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 4.96574   -23.45101 -20.32097 1.000 25.76253  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 3.94764   -22.51588 -20.77647 1.000 25.98377  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 3.82490   -22.67433 -22.28473 1.000 28.18515  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 4.83480   -22.66843 -22.99610 1.000 26.74436  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 4.27057   -21.06057 -20.41179 1.000 25.20369  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 3.15698   -20.14471 -20.92512 1.000 24.73306  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 4.40649   -20.88012 -18.85832 1.000 25.49455  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 2.60366   -22.85764 -22.75839 1.000 29.81990  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 2.30424   -22.88147 -24.19040 1.000 27.47125  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 1.49099   -21.63410 -24.52130 1.000 29.27127  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? 0.53892   -21.30000 -23.80656 1.000 30.16702  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 1.50594   -24.12802 -24.54914 1.000 27.49972  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 2.19569   -25.27479 -24.07543 1.000 32.42811  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 1.34209   -24.25376 -26.10734 1.000 30.88124  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 1.85273   -20.94259 -25.59530 1.000 24.50587  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 1.13656   -19.74229 -26.01059 1.000 24.02410  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 0.66359   -19.96403 -27.44196 1.000 30.94507  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 1.49223   -20.17271 -28.33617 1.000 30.43610  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 2.02111   -18.49479 -25.91821 1.000 23.72775  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 1.27226   -17.28801 -26.46779 1.000 26.67646  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 2.36807   -18.17111 -24.45277 1.000 24.58827  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -0.65798  -19.92574 -27.65911 1.000 24.70942  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -1.25974  -20.04189 -28.99199 1.000 23.61041  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -1.73219  -18.64251 -29.35722 1.000 26.93219  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -2.39228  -17.97717 -28.55050 1.000 28.00964  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -2.43802  -21.02932 -28.99970 1.000 28.08267  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -2.11187  -22.33350 -28.25515 1.000 34.99374  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -2.90193  -21.32958 -30.41216 1.000 27.45798  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -1.04093  -23.11665 -28.89263 1.000 31.27292  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -1.40375  -18.17708 -30.55021 1.000 26.47716  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -1.71517  -16.79048 -30.82793 1.000 25.99327  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -2.00546  -16.64106 -32.30963 1.000 29.75372  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -1.45413  -17.36963 -33.13377 1.000 30.64198  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -0.57305  -15.86408 -30.38217 1.000 27.30885  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -0.99358  -14.49344 -30.46021 1.000 26.27492  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 0.64153   -16.06431 -31.25348 1.000 28.06384  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -2.87532  -15.68746 -32.62530 1.000 25.86730  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -3.26389  -15.39483 -34.00605 1.000 24.76610  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -3.41224  -13.88917 -34.14736 1.000 29.74030  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -4.24331  -13.28736 -33.45865 1.000 26.58193  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -4.57579  -16.10687 -34.37439 1.000 26.08167  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -5.13718  -15.72353 -35.74395 1.000 31.52124  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -4.26342  -16.28903 -36.86986 1.000 29.83879  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -4.87052  -16.05080 -38.26192 1.000 34.96273  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -5.01505  -14.60681 -38.66120 1.000 31.19380  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -2.60399  -13.29444 -35.01837 1.000 24.75361  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -2.68476  -11.88321 -35.38945 1.000 30.35339  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -3.34137  -11.80027 -36.76072 1.000 29.87778  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -3.14564  -12.69065 -37.59395 1.000 30.15694  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -1.26902  -11.27451 -35.40705 1.000 30.62778  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -1.21024  -9.78700  -35.58963 1.000 31.73011  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -1.37477  -9.16397  -36.81088 1.000 33.18874  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -0.95532  -8.79562  -34.69192 1.000 27.44717  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -1.25010  -7.85619  -36.65887 1.000 33.50503  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -0.99161  -7.60366  -35.38437 1.000 29.57019  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -4.11677  -10.72075 -37.00091 1.000 28.00290  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -4.81571  -10.55860 -38.28046 1.000 31.01729  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -3.85758  -10.64639 -39.46781 1.000 35.53601  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -4.27105  -11.00653 -40.58124 1.000 36.48401  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -5.54381  -9.20020  -38.35071 1.000 35.10697  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.87313  -9.16429  -37.57663 1.000 38.52598  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -7.53620  -10.17637 -37.38821 1.000 36.81138  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -7.26118  -7.97431  -37.13339 1.000 36.57731  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -2.58552  -10.30460 -39.27253 1.000 31.57930  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -1.64154  -10.21746 -40.38807 1.000 40.38399  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -0.75605  -11.45589 -40.52633 1.000 38.33038  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 0.17735   -11.44496 -41.33036 1.000 37.92176  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -0.74234  -8.98040  -40.23483 1.000 35.79517  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -1.50306  -7.67154  -40.35579 1.000 40.59320  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -2.64856  -7.66398  -40.86706 1.000 44.20020  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -0.93180  -6.64098  -39.94065 1.000 41.57198  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -0.99627  -12.51021 -39.74908 1.000 33.26557  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -0.12035  -13.67229 -39.77901 1.000 37.09391  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -0.94842  -14.92928 -39.52789 1.000 39.82731  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -2.15927  -14.86016 -39.30074 1.000 35.07975  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 1.00239   -13.50304 -38.75589 1.000 31.50113  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 2.27749   -14.24169 -39.12974 1.000 44.01254  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 2.23637   -15.08743 -40.04136 1.000 37.23225  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 3.32765   -13.95308 -38.50930 1.000 37.29543  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -0.28336  -16.08518 -39.58012 1.000 35.40534  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -0.91762  -17.36978 -39.30853 1.000 36.87890  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -0.98759  -17.63693 -37.80952 1.000 37.67253  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -0.44226  -16.88818 -36.98346 1.000 33.11356  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -0.14258  -18.50459 -39.97316 1.000 35.67535  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -0.00492  -18.38183 -41.46956 1.000 48.64668  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? 0.99582   -19.40114 -42.00115 1.000 81.42101  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? 0.91016   -20.58596 -41.60735 1.000 79.99068  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? 1.89118   -19.01356 -42.78348 1.000 92.09787  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -1.63891  -18.74905 -37.45523 1.000 27.07894  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -1.75261  -19.11688 -36.04408 1.000 30.24221  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -0.50400  -19.89991 -35.63416 1.000 33.49676  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -0.12486  -20.86844 -36.31676 1.000 33.82166  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -3.00467  -19.95893 -35.80239 1.000 31.72210  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -3.30890  -20.25928 -34.30550 1.000 32.68504  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -4.72185  -20.78064 -34.15225 1.000 40.40014  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -5.68122  -20.14090 -34.60052 1.000 38.45611  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -4.86342  -21.95114 -33.54779 1.000 39.67006  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? 0.12879   -19.48157 -34.52264 1.000 30.15667  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 1.37420   -20.07849 -34.05198 1.000 29.63683  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 1.24254   -20.60707 -32.63849 1.000 30.78895  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? 0.47997   -20.05936 -31.83326 1.000 30.86409  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 2.53070   -19.07670 -34.05202 1.000 24.89453  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 2.92268   -18.69003 -35.45102 1.000 34.01064  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.77679   -19.49591 -36.20041 1.000 33.60932  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 2.44200   -17.52673 -36.01924 1.000 39.70856  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 4.13538   -19.14820 -37.48641 1.000 37.53994  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.78999   -17.16685 -37.29396 1.000 40.48446  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 3.63225   -17.97931 -38.02860 1.000 44.26415  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 3.97903   -17.60300 -39.30168 1.000 57.84036  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 2.07625   -21.60655 -32.32648 1.000 28.19063  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 2.27789   -22.08777 -30.95631 1.000 29.51364  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 3.70926   -21.82095 -30.51491 1.000 31.70998  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 4.65552   -22.32592 -31.12577 1.000 31.15497  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 1.96011   -23.57261 -30.83795 1.000 32.36129  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 3.85805   -21.05003 -29.43675 1.000 25.12525  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 5.12675   -20.84023 -28.73900 1.000 26.58111  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 5.11106   -21.69978 -27.47674 1.000 27.77118  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 4.06075   -21.88301 -26.85916 1.000 27.57323  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 5.27810   -19.34756 -28.38823 1.000 27.21771  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 6.48361   -18.90157 -27.58885 1.000 25.52489  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 7.57589   -18.22101 -28.06585 1.000 27.07733  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 6.67360   -19.01800 -26.15611 1.000 27.30292  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 8.44187   -17.91685 -27.01580 1.000 26.95656  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 7.91093   -18.40064 -25.84333 1.000 29.19007  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 5.91481   -19.58507 -25.11284 1.000 27.26293  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 8.42581   -18.36136 -24.53544 1.000 29.66447  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 6.43454   -19.53825 -23.78924 1.000 23.32264  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 7.66657   -18.91130 -23.52554 1.000 26.87011  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 6.26065   -22.24409 -27.09429 1.000 25.54082  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 6.26522   -23.08813 -25.91065 1.000 28.86934  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 7.62467   -23.03308 -25.24991 1.000 29.36394  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 8.65118   -23.05779 -25.93856 1.000 28.58762  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 5.99476   -24.53715 -26.25886 1.000 31.59826  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 5.57852   -25.42690 -25.13388 1.000 34.89592  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 4.87392   -26.67222 -25.67559 1.000 48.93437  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 5.57692   -27.45377 -26.34914 1.000 51.23516  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 3.64334   -26.85875 -25.47986 1.000 41.82573  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 7.63380   -23.08944 -23.91279 1.000 28.52137  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 8.92320   -23.20234 -23.24280 1.000 27.71257  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 8.75444   -23.81506 -21.86027 1.000 24.20960  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 7.84533   -23.43146 -21.10835 1.000 27.52027  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 9.61004   -21.83561 -23.07950 1.000 23.82711  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 10.89394  -22.02935 -22.45945 1.000 28.09045  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 9.69238   -24.69112 -21.52258 1.000 26.55804  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 9.87752   -25.21840 -20.17752 1.000 30.74119  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 11.08013  -24.58146 -19.49288 1.000 28.26359  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 11.64639  -25.16331 -18.55373 1.000 31.50395  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 10.02177  -26.73742 -20.23070 1.000 37.55251  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 8.81423   -27.32884 -20.68540 1.000 34.75455  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 11.44605  -23.37752 -19.92467 1.000 29.27488  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 12.64843  -22.68041 -19.46440 1.000 35.51715  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 13.86555  -23.52453 -19.86206 1.000 37.27048  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 13.86931  -24.20156 -20.90238 1.000 37.00964  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 12.52130  -22.36133 -17.97068 1.000 33.72488  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 14.92550  -23.50084 -19.06603 1.000 36.28347  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 16.10959  -24.20670 -19.49894 1.000 36.03019  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 16.88979  -23.51991 -20.59687 1.000 37.72707  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 17.84414  -24.10959 -21.11512 1.000 38.43144  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 16.51024  -22.29520 -20.97486 1.000 32.32664  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 17.26427  -21.52432 -21.94232 1.000 34.92260  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 16.76309  -21.57716 -23.37248 1.000 32.05289  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 17.36270  -20.93288 -24.23807 1.000 33.23982  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 15.67980  -22.28967 -23.65226 1.000 28.27576  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 15.22281  -22.41110 -25.03346 1.000 31.16809  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 13.70359  -22.36475 -25.09956 1.000 28.06823  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 13.00131  -22.60585 -24.11894 1.000 26.45494  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 15.79187  -23.69410 -25.68064 1.000 27.90327  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 15.17545  -24.86931 -25.15362 1.000 33.03569  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 13.20052  -22.05395 -26.28745 1.000 23.89006  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 11.77450  -22.04459 -26.54468 1.000 26.16899  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 11.59265  -22.52871 -27.97380 1.000 27.75109  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 12.54651  -22.53447 -28.75477 1.000 29.08426  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 11.12979  -20.65485 -26.33518 1.000 25.92544  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 11.60499  -19.57483 -27.26714 1.000 28.02352  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 12.71750  -18.79531 -26.95661 1.000 27.09533  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 10.90780  -19.30010 -28.44500 1.000 28.64367  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 13.15701  -17.78229 -27.80132 1.000 31.46668  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 11.33531  -18.26585 -29.30223 1.000 31.10797  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 12.46024  -17.49443 -28.97755 1.000 25.91044  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 10.38312  -22.98146 -28.28252 1.000 26.32717  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 10.05941  -23.46167 -29.63136 1.000 24.63672  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 8.91873   -22.63699 -30.21712 1.000 28.19388  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 8.08199   -22.10265 -29.49346 1.000 27.66444  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 9.68308   -24.94740 -29.64334 1.000 31.32204  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 8.45054   -25.15361 -28.93300 1.000 32.28383  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 10.80845  -25.80902 -29.08105 1.000 32.21794  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 8.89054   -22.54646 -31.55127 1.000 29.91262  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 7.77613   -21.93988 -32.25877 1.000 27.16502  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 7.41067   -22.86414 -33.41527 1.000 33.44144  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 8.29396   -23.34431 -34.13985 1.000 30.20569  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 8.11167   -20.51496 -32.76750 1.000 28.25641  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 6.98168   -19.99634 -33.62374 1.000 31.29039  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 8.35205   -19.56315 -31.60516 1.000 30.95787  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 6.12018   -23.14222 -33.56537 1.000 29.20267  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 5.63541   -23.89162 -34.72903 1.000 33.99272  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 4.31680   -23.29531 -35.19469 1.000 33.64154  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 3.62078   -22.61041 -34.43862 1.000 33.27367  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 5.44688   -25.38399 -34.41007 1.000 36.29709  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 4.32353   -25.68355 -33.38649 1.000 41.38346  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 4.49258   -27.08871 -32.78418 1.000 45.19788  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 5.52646   -27.10670 -31.74507 1.000 58.47420  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 5.93059   -28.18277 -31.06955 1.000 67.70833  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 5.45866   -29.39301 -31.33450 1.000 58.43592  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 6.86817   -28.04787 -30.13185 1.000 52.94320  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 3.98044   -23.55801 -36.46348 1.000 34.38367  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 2.62868   -23.29509 -36.91376 1.000 34.80921  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 1.67378   -24.19314 -36.13416 1.000 39.86999  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 1.96671   -25.36835 -35.88981 1.000 41.62981  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 2.52092   -23.55700 -38.42507 1.000 43.35095  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 3.20952   -22.51947 -39.13431 1.000 45.03784  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 1.06621   -23.54905 -38.87152 1.000 56.06502  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? 0.53611   -23.63767 -35.71291 1.000 41.78878  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -0.41718  -24.39188 -34.90758 1.000 41.86410  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -1.44814  -25.09198 -35.78007 1.000 59.75213  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -2.05363  -24.47152 -36.65880 1.000 58.36683  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -1.15098  -23.51150 -33.89912 1.000 41.03806  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -2.00030  -24.33649 -32.96208 1.000 42.82917  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -1.53438  -25.43374 -32.56745 1.000 59.03995  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -3.12401  -23.91995 -32.62398 1.000 47.19088  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -1.68322  -26.36905 -35.47915 1.000 65.05424  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -2.66296  -27.19697 -36.16720 1.000 82.25548  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -3.92387  -27.45752 -35.35067 1.000 68.30836  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -4.82517  -28.14837 -35.83851 1.000 68.59338  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -2.01660  -28.52770 -36.57285 1.000 79.68031  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -1.47527  -29.17630 -35.40782 1.000 70.77918  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -0.92625  -28.27974 -37.60567 1.000 67.87784  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -4.01866  -26.92235 -34.13592 1.000 61.17068  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -5.22635  -27.03919 -33.33405 1.000 62.70074  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -6.42738  -26.27210 -33.86332 1.000 66.04556  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -6.46772  -25.88850 -35.03950 1.000 58.62762  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -7.41808  -26.05413 -33.00207 1.000 64.29155  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -8.61739  -25.32747 -33.40214 1.000 70.39497  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -8.24019  -23.90699 -33.81505 1.000 56.47434  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -7.43396  -23.25921 -33.12807 1.000 49.11686  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -9.62961  -25.29810 -32.24555 1.000 71.86229  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -11.06986 -24.78868 -32.55298 1.000 78.85538  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -11.94067 -25.74712 -33.39869 1.000 101.82592 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -11.42019 -26.41149 -34.32479 1.000 98.98761  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.16847 -25.83864 -33.13062 1.000 83.15330  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -8.75789  -23.39714 -34.93373 1.000 55.21752  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -8.57495  -21.98408 -35.26867 1.000 48.82327  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -9.15704  -21.09008 -34.18017 1.000 53.52908  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -10.25095 -21.33853 -33.66970 1.000 52.63640  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -9.33221  -21.82666 -36.59185 1.000 47.84198  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -9.40984  -23.19771 -37.15480 1.000 50.21030  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -9.45507  -24.14088 -35.99883 1.000 48.66604  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -8.40453  -20.03555 -33.84493 1.000 41.41563  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -8.66585  -19.11769 -32.75175 1.000 50.47980  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -9.42243  -17.86288 -33.17660 1.000 46.20459  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -10.04278 -17.20965 -32.32929 1.000 53.58174  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -7.31224  -18.70525 -32.18408 1.000 42.51430  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -6.81720  -19.57655 -31.10863 1.000 56.23509  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -5.43007  -18.68854 -30.43995 1.000 51.83310  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -6.26491  -17.26404 -29.74749 1.000 36.98680  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -9.32932  -17.47832 -34.44094 1.000 41.18853  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -9.93147  -16.23911 -34.90717 1.000 40.76228  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -8.94756  -15.09123 -34.81699 1.000 37.69445  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -8.42067  -14.62020 -35.82905 1.000 37.91503  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -8.65172  -14.68608 -33.58747 1.000 32.91106  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -7.71065  -13.61664 -33.29522 1.000 27.36297  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -7.53170  -13.58473 -31.78393 1.000 28.08322  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -8.50966  -13.70131 -31.04919 1.000 29.23050  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -8.20521  -12.24541 -33.81652 1.000 28.22739  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -7.16314  -11.11417 -33.61535 1.000 28.70335  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -7.80419  -9.70688  -33.58428 1.000 29.78874  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -8.74762  -9.54790  -32.48287 1.000 30.80615  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -10.06720 -9.49247  -32.61549 1.000 29.05222  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.65400 -9.55435  -33.80983 1.000 30.07747  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -10.82401 -9.37820  -31.51723 1.000 28.81346  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -6.29511  -13.44096 -31.32613 1.000 26.67974  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -6.08059  -13.26152 -29.90402 1.000 26.10260  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -4.95488  -14.13904 -29.41743 1.000 31.98276  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -4.13120  -14.62149 -30.19872 1.000 28.70626  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -4.91092  -14.34981 -28.11087 1.000 25.43960  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -3.82588  -15.09187 -27.49045 1.000 25.24870  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -4.41308  -16.00926 -26.43161 1.000 29.33695  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -5.33691  -15.61734 -25.70000 1.000 27.85726  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -2.79792  -14.13740 -26.89099 1.000 27.27970  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -2.18200  -13.39423 -27.94494 1.000 28.53923  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -1.71239  -14.90337 -26.13353 1.000 30.02621  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -3.89702  -17.23459 -26.38254 1.000 25.22313  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -4.23465  -18.20984 -25.35381 1.000 27.18597  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -2.94484  -18.61143 -24.64795 1.000 29.67598  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -2.02690  -19.13596 -25.28936 1.000 27.05227  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -4.92356  -19.41996 -26.01316 1.000 30.00302  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -5.08575  -20.65431 -25.14848 1.000 39.31644  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -6.12975  -21.65324 -25.72558 1.000 47.40905  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -6.39380  -21.45014 -27.20949 1.000 47.66943  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -7.27384  -22.53544 -27.78207 1.000 54.95874  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -2.86636  -18.37062 -23.33378 1.000 25.75269  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -1.72206  -18.77641 -22.52214 1.000 26.13440  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -2.13257  -19.98840 -21.70214 1.000 29.39758  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -3.02719  -19.89351 -20.85412 1.000 27.68661  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -1.23783  -17.64930 -21.60719 1.000 22.82270  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -0.06371  -18.14165 -20.69838 1.000 23.99806  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -0.82312  -16.43371 -22.42499 1.000 27.60374  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -1.47241  -21.10631 -21.93946 1.000 23.05961  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -1.75794  -22.37012 -21.26618 1.000 27.22061  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -0.65589  -22.58118 -20.24249 1.000 26.90059  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 0.50595   -22.77382 -20.61307 1.000 27.93128  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -1.83642  -23.53597 -22.25705 1.000 28.33663  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -2.86217  -23.22824 -23.34870 1.000 31.77572  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -2.16892  -24.86186 -21.51295 1.000 26.62146  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -2.71915  -24.09741 -24.54936 1.000 38.40194  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -1.00799  -22.50924 -18.94954 1.000 24.42273  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -0.06204  -22.74095 -17.86305 1.000 27.09606  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -0.13324  -24.20269 -17.44682 1.000 25.49236  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -1.16553  -24.64515 -16.92682 1.000 30.75378  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -0.40198  -21.85350 -16.66314 1.000 23.66420  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -0.40571  -20.37980 -17.02302 1.000 25.42096  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -0.81988  -19.58307 -15.76819 1.000 29.15274  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 0.96475   -19.94957 -17.49294 1.000 27.33038  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 0.94230   -24.96182 -17.69751 1.000 28.13174  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 1.05825   -26.34220 -17.21793 1.000 31.17126  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 1.61684   -26.26331 -15.79674 1.000 31.11465  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 2.81148   -26.03706 -15.59559 1.000 31.21527  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 1.95183   -27.17131 -18.14080 1.000 30.43583  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 1.52313   -27.16027 -19.58431 1.000 30.85193  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 0.74946   -28.16035 -20.13105 1.000 36.35400  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 1.74030   -26.26219 -20.58261 1.000 33.10620  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? 0.51644   -27.88936 -21.40570 1.000 37.00589  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 1.10639   -26.74389 -21.70418 1.000 35.44867  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 0.75261   -26.43274 -14.80491 1.000 28.10745  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 1.09354   -26.03199 -13.44771 1.000 29.99671  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 2.04149   -27.03319 -12.79353 1.000 34.97703  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 1.96524   -28.25041 -13.02642 1.000 34.79209  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -0.18436  -25.91631 -12.61313 1.000 27.99961  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -1.12012  -24.75419 -12.99549 1.000 26.51522  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -2.22201  -24.62964 -11.95647 1.000 31.08491  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -0.37500  -23.43599 -13.12693 1.000 29.19552  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 2.93065   -26.50643 -11.94550 1.000 30.51142  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 3.75285   -27.35397 -11.09814 1.000 33.58609  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 2.84262   -28.15775 -10.18450 1.000 34.98511  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 1.72099   -27.73861 -9.86991  1.000 32.31014  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 4.71492   -26.49450 -10.26637 1.000 37.76079  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 5.74484   -25.67946 -11.08933 1.000 38.40101  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 6.46868   -24.64118 -10.19620 1.000 39.95546  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 7.41961   -23.73794 -10.99264 1.000 47.03100  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 8.02320   -22.55332 -10.24178 1.000 39.83905  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 3.34972   -29.31350 -9.72042  1.000 36.61730  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 2.52568   -30.22881 -8.93537  1.000 39.72058  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.99588   -29.59233 -7.64963  1.000 43.35034  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.87497   -29.89246 -7.23594  1.000 40.05769  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 3.31953   -31.49999 -8.61470  1.000 47.52891  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.44014   -32.70044 -8.29644  1.000 67.10040  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 3.23110   -33.98735 -8.08649  1.000 83.24700  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 4.09540   -34.31717 -8.93380  1.000 75.24392  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.97357   -34.67455 -7.07778  1.000 88.72502  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.75810   -28.71049 -7.00701  1.000 37.29465  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 2.29191   -28.11362 -5.75929  1.000 41.12063  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.60211   -26.76260 -5.94748  1.000 39.38313  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.41082   -26.03252 -4.96333  1.000 35.72509  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 3.44611   -27.97709 -4.76177  1.000 45.82187  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.56171   -27.07335 -5.25720  1.000 50.51991  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.54995   -26.67509 -6.44456  1.000 49.94888  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.45843   -26.75333 -4.44501  1.000 63.86648  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 1.20144   -26.41483 -7.17045  1.000 34.54641  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 0.53887   -25.14413 -7.41134  1.000 34.45870  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -0.89758  -25.33131 -7.90257  1.000 32.54348  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -1.42931  -24.48079 -8.63317  1.000 32.38184  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 1.36360   -24.30448 -8.39499  1.000 32.04903  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.81420   -24.10386 -7.90576  1.000 30.40190  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.86547   -23.34905 -6.59239  1.000 36.68400  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 2.02624   -22.48885 -6.35011  1.000 34.66049  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.86351   -23.64207 -5.75747  1.000 33.00861  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -1.54320  -26.43402 -7.51634  1.000 36.39507  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -2.86657  -26.70237 -8.07181  1.000 34.87555  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -3.97572  -25.91851 -7.37664  1.000 37.61321  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.13782  -26.03381 -7.77909  1.000 34.15112  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.18018  -28.20061 -8.03034  1.000 38.46551  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.16568  -28.67135 -6.67771  1.000 36.42478  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.10899  -28.96070 -8.81477  1.000 42.81380  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -3.65474  -25.10399 -6.36681  1.000 33.48090  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.66827  -24.20693 -5.81940  1.000 38.61604  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.18164  -23.24258 -6.87492  1.000 29.73073  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.31545  -22.76164 -6.78003  1.000 32.60122  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.10643  -23.41986 -4.62677  1.000 36.55259  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.01162  -22.46246 -5.01970  1.000 31.14027  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.29998  -21.87541 -3.80475  1.000 40.92380  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.31204  -22.49509 -3.36174  1.000 42.58022  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.73501  -20.81845 -3.29352  1.000 39.36706  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.37445  -22.94451 -7.89075  1.000 28.61378  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -4.78680  -21.99457 -8.92421  1.000 31.75700  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -5.73664  -22.61312 -9.94101  1.000 32.47867  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.08975  -21.96276 -10.93122 1.000 31.61414  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.54348  -21.38910 -9.58246  1.000 26.49330  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.68027  -20.69602 -8.53508  1.000 25.52147  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.16247  -19.58542 -7.87576  1.000 31.05224  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.42584  -21.20054 -8.16865  1.000 28.62113  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.41120  -18.96353 -6.87215  1.000 29.95641  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.67228  -20.59617 -7.18199  1.000 30.92436  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.17529  -19.46889 -6.54803  1.000 35.07525  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.45531  -18.83878 -5.57135  1.000 32.48864  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.15473  -23.85469 -9.71199  1.000 29.64165  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -7.24386  -24.45610 -10.46724 1.000 31.46719  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -8.56892  -24.36779 -9.72465  1.000 35.35858  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -9.58830  -24.79685 -10.26162 1.000 39.52013  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -6.94173  -25.93469 -10.76983 1.000 31.62182  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -5.66601  -26.15732 -11.58911 1.000 32.06181  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -5.43612  -27.63814 -11.85756 1.000 41.48980  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -5.74915  -25.39181 -12.89024 1.000 34.85337  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -8.57742  -23.86614 -8.49009  1.000 34.59980  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -9.79207  -23.87563 -7.68176  1.000 36.73618  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.56556 -22.59944 -7.94132  1.000 34.23595  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -9.99404  -21.50567 -7.91035  1.000 29.83560  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.50255  -23.98709 -6.18179  1.000 41.36491  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -8.56851  -25.10219 -5.77331  1.000 50.54995  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -9.27434  -26.44626 -5.73369  1.000 71.73910  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -10.51709 -26.45511 -5.57829  1.000 72.72098  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.58834  -27.48920 -5.84212  1.000 76.99789  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -11.87313 -22.74700 -8.14570  1.000 37.44407  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.70890 -21.60811 -8.50541  1.000 37.13867  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.64081 -20.50914 -7.43809  1.000 30.89713  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.48923 -19.33005 -7.75535  1.000 32.34432  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.14668 -22.08676 -8.69880  1.000 40.67319  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.17999 -20.97099 -8.65721  1.000 52.89092  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.55266 -21.43269 -9.13056  1.000 70.17296  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -16.85975 -22.64585 -8.99706  1.000 61.15809  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.30691 -20.58744 -9.66587  1.000 73.73877  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.74467 -20.87552 -6.16108  1.000 30.84223  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.78096 -19.81613 -5.15804  1.000 30.45393  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.43292 -19.12730 -5.04381  1.000 27.19062  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.37544 -17.93692 -4.73602  1.000 32.17293  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.24201 -20.37733 -3.81478  1.000 37.58558  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.35896 -21.45962 -3.30049  1.000 42.35883  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.01647 -22.09464 -2.07778  1.000 51.36619  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.07386 -22.92451 -1.34399  1.000 62.90281  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.32473 -23.44369 -0.15110  1.000 69.47546  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.46897 -23.20633 0.47696   1.000 54.26677  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.39504 -24.19196 0.43721   1.000 66.39870  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.34196 -19.84166 -5.32759  1.000 30.25084  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.02187  -19.22094 -5.28471  1.000 26.01230  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.84590  -18.25696 -6.45514  1.000 29.68995  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.32047  -17.15576 -6.29034  1.000 26.60116  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -7.93838  -20.30420 -5.30011  1.000 33.30584  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.52141  -19.76625 -5.27722  1.000 29.31339  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.22712  -19.12451 -3.86425  1.000 33.99572  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.80305  -18.84302 -3.73436  1.000 30.93652  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.28954  -17.64056 -3.52599  1.000 34.04366  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.06431  -16.58053 -3.33056  1.000 28.34019  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -2.96618  -17.49661 -3.52411  1.000 32.32135  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.27711  -18.65360 -7.64372  1.000 27.29445  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.15934  -17.74214 -8.78388  1.000 26.93133  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.03079 -16.51185 -8.57354  1.000 24.64560  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.60455  -15.38291 -8.84771  1.000 28.93462  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.48571  -18.46362 -10.10371 1.000 26.66836  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.43646  -19.54065 -10.36722 1.000 30.07568  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.46403  -17.45506 -11.27162 1.000 23.81318  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -8.91075  -20.65767 -11.37289 1.000 35.31583  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.25827 -16.70325 -8.08592  1.000 25.55291  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.12548 -15.55712 -7.84146  1.000 29.29340  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.45969 -14.59756 -6.87715  1.000 30.30423  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.46666 -13.38807 -7.08519  1.000 28.14389  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.47853 -15.98762 -7.26997  1.000 32.96419  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.41553 -16.64073 -8.22675  1.000 43.18632  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.72006 -16.97728 -7.52239  1.000 47.12816  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.75333 -17.48245 -8.52530  1.000 60.25836  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.79863 -18.31525 -7.87365  1.000 62.81292  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.86043 -15.13265 -5.81353  1.000 26.88463  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.21616 -14.27865 -4.81720  1.000 29.03969  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.09876  -13.44142 -5.44376  1.000 27.76263  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -8.96595  -12.23973 -5.16271  1.000 27.99859  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.68936  -15.17194 -3.69228  1.000 28.91829  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.97795  -14.45046 -2.56823  1.000 30.59271  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.25690  -15.43312 -1.63030  1.000 33.77865  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.70663  -16.43951 -2.12548  1.000 32.88685  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.27239  -15.20896 -0.39265  1.000 31.78015  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.30259  -14.05955 -6.31177  1.000 24.53156  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.15389  -13.37095 -6.90151  1.000 26.27688  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.60975  -12.29733 -7.87904  1.000 29.58396  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.03480  -11.20154 -7.93398  1.000 29.19989  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.24287  -14.40711 -7.57173  1.000 28.22556  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.65330  -15.32898 -6.49925  1.000 30.09129  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.12968  -13.73491 -8.36234  1.000 26.32580  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.02860  -16.55276 -7.12096  1.000 29.44082  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.61533  -12.60914 -8.69646  1.000 27.37033  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.10722  -11.62183 -9.65435  1.000 27.88356  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -9.67675  -10.41711 -8.90794  1.000 30.92145  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.32134  -9.27148  -9.18572  1.000 31.85879  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.14586 -12.25810 -10.58957 1.000 25.69274  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -10.87081 -11.15771 -11.41004 1.000 27.75458  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.47188  -13.28291 -11.53267 1.000 27.53907  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.52937 -10.66771 -7.90434  1.000 28.52501  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.05340 -9.56185  -7.09407  1.000 33.53295  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -9.94655  -8.75391  -6.44041  1.000 31.81170  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.04761 -7.52830  -6.35549  1.000 34.93735  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.03400 -10.05127 -6.01377  1.000 31.84552  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.11370 -11.07964 -6.45446  1.000 48.49558  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.49260 -11.02808 -7.97942  1.000 68.68142  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -13.80857 -12.41953 -8.54782  1.000 44.29713  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -14.33576 -12.45405 -9.93317  1.000 72.13521  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -8.87821  -9.40186  -5.98503  1.000 34.87873  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -7.87020  -8.65255  -5.23161  1.000 32.69553  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.00445  -7.79035  -6.15569  1.000 33.30185  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.68519  -6.64248  -5.82822  1.000 34.57313  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.01314  -9.62392  -4.40976  1.000 36.75089  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -5.81658  -9.00235  -3.67510  1.000 44.54192  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.16749  -10.06245 -2.78236  1.000 47.63741  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -3.98723  -9.51216  -1.99730  1.000 62.06863  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.31190  -10.58298 -1.17647  1.000 62.44014  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -6.63540  -8.31168  -7.32323  1.000 31.50217  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -5.62308  -7.68976  -8.16458  1.000 35.13767  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.12446  -7.18977  -9.50671  1.000 36.53642  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.40206  -6.42602  -10.16422 1.000 35.06712  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.48231  -8.67784  -8.45226  1.000 30.83428  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -3.71294  -9.07449  -7.23532  1.000 39.71336  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -2.96819  -8.17693  -6.50335  1.000 40.83474  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.57319  -10.27363 -6.62106  1.000 38.92769  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.40203  -8.80558  -5.48665  1.000 44.57380  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.75112  -10.07883 -5.53608  1.000 38.80204  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.29088  -7.62495  -9.96112  1.000 33.89714  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -7.70302  -7.33528  -11.32938 1.000 31.50824  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.13422  -6.80043  -11.38283 1.000 31.72951  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -9.81491  -6.93128  -12.40821 1.000 35.10570  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.55223  -8.58519  -12.20796 1.000 35.12373  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.18913  -9.02918  -12.22945 1.000 34.00496  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.59871  -6.16664  -10.30291 1.000 36.38128  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.02416 -5.85798  -10.21116 1.000 40.57466  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.47288 -4.74342  -11.15403 1.000 40.70678  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.67656 -4.60085  -11.37402 1.000 43.21310  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.38784 -5.49769  -8.77547  1.000 45.79466  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.92604 -4.14044  -8.36019  1.000 48.16522  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -11.16906 -3.88708  -6.88817  1.000 68.16166  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -12.30743 -3.97427  -6.41223  1.000 66.88680  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -10.09555 -3.57927  -6.15179  1.000 62.98782  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.55880 -3.96524  -11.72704 1.000 39.48328  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -10.95314 -2.82808  -12.55904 1.000 34.75161  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.56744 -2.98794  -14.01923 1.000 36.89428  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.63501 -2.00831  -14.77338 1.000 39.09205  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.37068 -1.53528  -12.00048 1.000 34.63140  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.93253 -1.17390  -10.66147 1.000 37.26541  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.30833 -1.12790  -10.46607 1.000 38.01487  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.09498 -0.88347  -9.60443  1.000 42.32115  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.84694 -0.78757  -9.22994  1.000 40.86744  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.62389 -0.55026  -8.36328  1.000 51.64222  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -12.00342 -0.50532  -8.18093  1.000 46.47472  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.18477 -4.19705  -14.43323 1.000 33.93773  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -9.91107  -4.47347  -15.84423 1.000 32.82501  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.14584 -4.18292  -16.68343 1.000 32.62602  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.26801 -4.55763  -16.32146 1.000 35.66575  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.44227  -5.92460  -16.00908 1.000 27.05497  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.12407  -6.13096  -15.25335 1.000 32.47007  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.38208  -6.32486  -17.50104 1.000 31.61208  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -6.92913  -5.50582  -15.91137 1.000 35.54248  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -10.94423 -3.49710  -17.80830 1.000 33.23472  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.06105 -2.92019  -18.54053 1.000 30.58394  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.64414 -3.82705  -19.60927 1.000 34.39840  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.16909 -3.34236  -20.61549 1.000 33.93894  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.55926 -5.13609  -19.39918 1.000 29.99068  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.09309 -6.14437  -20.30312 1.000 28.13076  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.71176 -7.24010  -19.45438 1.000 30.09531  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.23542 -7.50105  -18.34026 1.000 30.34479  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -11.99368 -6.73896  -21.19654 1.000 28.43586  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.36617 -5.69151  -22.05999 1.000 31.26405  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -11.99324 -5.26284  -23.22590 1.000 29.55028  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.17372 -5.07114  -21.66959 1.000 26.97617  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.43408 -4.24333  -23.99779 1.000 33.24925  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.60307  -4.06217  -22.44447 1.000 26.78115  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.24884 -3.65246  -23.59810 1.000 28.67407  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.69339  -2.65165  -24.36528 1.000 32.89694  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.77079 -7.88520  -19.93525 1.000 32.34818  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.37371 -8.97953  -19.16373 1.000 29.86639  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.40186 -10.13434 -18.98000 1.000 29.15877  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.79614 -10.62237 -19.93428 1.000 31.75894  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.59197 -9.39630  -19.99910 1.000 31.99800  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.45308 -8.72875  -21.30670 1.000 35.79888  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.45046 -7.63021  -21.21678 1.000 28.46291  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.26504 -10.56966 -17.73642 1.000 26.33360  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.43220 -11.70740 -17.36064 1.000 28.29525  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.37367 -12.81713 -16.90522 1.000 33.39756  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.05553 -12.69782 -15.87604 1.000 31.46489  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.42712 -11.34781 -16.25379 1.000 33.45976  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.46145 -10.24927 -16.70482 1.000 30.00849  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.66983 -12.59488 -15.74178 1.000 29.68333  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.57628 -9.72407  -15.55664 1.000 33.34880  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.42391 -13.90127 -17.66462 1.000 27.70105  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -15.31349 -15.00728 -17.34078 1.000 28.77417  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.46696 -16.15981 -16.84080 1.000 25.96229  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.56550 -16.63511 -17.54840 1.000 27.20209  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -16.13566 -15.43635 -18.56262 1.000 29.18189  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -16.88026 -14.31802 -19.05812 1.000 29.09534  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.11045 -16.57614 -18.20699 1.000 28.95314  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.75166 -16.60272 -15.62863 1.000 27.54303  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.08031 -17.75347 -15.05199 1.000 30.10480  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -14.95480 -18.97707 -15.33463 1.000 30.59136  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.07081 -19.07952 -14.81374 1.000 33.13693  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -13.86477 -17.53671 -13.55970 1.000 30.05832  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.39367 -18.74430 -12.73608 1.000 33.64617  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.06472 -19.32474 -13.24149 1.000 29.20945  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.33646 -18.46805 -11.20688 1.000 32.76730  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -14.46230 -19.87996 -16.18807 1.000 30.19180  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -15.19496 -21.09727 -16.51738 1.000 32.75343  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -15.14196 -22.06240 -15.33722 1.000 33.92116  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -14.12082 -22.17490 -14.66516 1.000 40.20014  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -14.57658 -21.79107 -17.73943 1.000 30.07511  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -14.87826 -21.11054 -19.06870 1.000 26.72639  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -14.98142 -19.72539 -19.17729 1.000 28.18306  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.08342 -21.88577 -20.19613 1.000 31.00038  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -15.24794 -19.12466 -20.42420 1.000 30.57257  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -15.37205 -21.30666 -21.43311 1.000 32.93078  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -15.45686 -19.91655 -21.54143 1.000 30.38934  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -16.22079 -22.75367 -15.09041 1.000 27.90113  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -16.24505 -23.75468 -14.03504 1.000 31.30781  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -16.09439 -25.13005 -14.66986 1.000 34.25602  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.39946 -25.32562 -15.85192 1.000 36.53087  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -17.52772 -23.61035 -13.20034 1.000 43.35752  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -17.69615 -22.17724 -12.78873 1.000 46.41862  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -18.62877 -23.85466 -14.05212 1.000 39.82638  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -15.55982 -26.07622 -13.92508 1.000 36.36520  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -15.35646 -27.39087 -14.51949 1.000 42.45938  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -16.58663 -28.27420 -14.40115 1.000 42.84476  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -17.36993 -28.16867 -13.45516 1.000 42.08148  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -14.15002 -28.09734 -13.92260 1.000 49.26970  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -12.92010 -27.25633 -13.95140 1.000 47.71819  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -11.69981 -28.10975 -13.77922 1.000 55.58715  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -11.60822 -29.13052 -14.49978 1.000 60.73924  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -10.84422 -27.76944 -12.94200 1.000 61.54649  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -16.74759 -29.16110 -15.38823 1.000 46.96932  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.95951 -29.96989 -15.46436 1.000 44.85424  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -17.93289 -31.16088 -14.51038 1.000 58.23468  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -18.99141 -31.56589 -14.02367 1.000 63.35054  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.20859 -30.44448 -16.90902 1.000 43.50132  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.03656 -29.35489 -17.96581 1.000 43.80612  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.41453 -29.85476 -19.35118 1.000 44.34547  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.19408 -30.48097 -20.02757 1.000 41.44836  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.00479 -29.60336 -19.96568 1.000 40.27724  ? 224 LYS   A NZ  1 
ATOM   1645 N N   . GLU   A 1 218 ? -16.75924 -31.71632 -14.21683 1.000 61.56584  ? 225 GLU   A N   1 
ATOM   1646 C CA  . GLU   A 1 218 ? -16.67964 -32.88686 -13.33777 1.000 72.87820  ? 225 GLU   A CA  1 
ATOM   1647 C C   . GLU   A 1 218 ? -16.97120 -32.45994 -11.90131 1.000 71.32357  ? 225 GLU   A C   1 
ATOM   1648 O O   . GLU   A 1 218 ? -17.38096 -33.27458 -11.07317 1.000 79.42040  ? 225 GLU   A O   1 
ATOM   1649 C CB  . GLU   A 1 218 ? -15.30457 -33.57969 -13.41065 1.000 66.70381  ? 225 GLU   A CB  1 
ATOM   1650 C CG  . GLU   A 1 218 ? -14.79609 -33.95397 -14.81212 1.000 100.59493 ? 225 GLU   A CG  1 
ATOM   1651 C CD  . GLU   A 1 218 ? -14.51894 -32.73742 -15.71155 1.000 104.42211 ? 225 GLU   A CD  1 
ATOM   1652 O OE1 . GLU   A 1 218 ? -14.18491 -31.65355 -15.17796 1.000 104.68280 ? 225 GLU   A OE1 1 
ATOM   1653 O OE2 . GLU   A 1 218 ? -14.63543 -32.86049 -16.95178 1.000 87.62309  ? 225 GLU   A OE2 1 
HETATM 1654 C C1  . A1AXS B 2 .   ? 3.35365   -14.72797 -24.58816 0.833 42.62481  ? 301 A1AXS A C1  1 
HETATM 1655 C C10 . A1AXS B 2 .   ? 6.63866   -15.45669 -26.20718 0.833 40.19578  ? 301 A1AXS A C10 1 
HETATM 1656 C C11 . A1AXS B 2 .   ? 6.40107   -15.46244 -24.92356 0.833 33.94144  ? 301 A1AXS A C11 1 
HETATM 1657 C C12 . A1AXS B 2 .   ? 6.52114   -14.04194 -24.41804 0.833 42.17490  ? 301 A1AXS A C12 1 
HETATM 1658 C C13 . A1AXS B 2 .   ? 7.63051   -13.55530 -25.35799 0.833 42.76959  ? 301 A1AXS A C13 1 
HETATM 1659 C C2  . A1AXS B 2 .   ? 3.07775   -12.34157 -24.31020 0.833 47.82147  ? 301 A1AXS A C2  1 
HETATM 1660 C C3  . A1AXS B 2 .   ? 3.60176   -10.94990 -24.08163 0.833 47.54800  ? 301 A1AXS A C3  1 
HETATM 1661 C C4  . A1AXS B 2 .   ? 4.84925   -10.56066 -23.50039 0.833 41.60046  ? 301 A1AXS A C4  1 
HETATM 1662 C C5  . A1AXS B 2 .   ? 4.95482   -9.13320  -23.47715 0.833 45.78070  ? 301 A1AXS A C5  1 
HETATM 1663 C C6  . A1AXS B 2 .   ? 3.90744   -8.45599  -23.97420 0.833 52.74098  ? 301 A1AXS A C6  1 
HETATM 1664 C C7  . A1AXS B 2 .   ? 5.35339   -13.17174 -24.98913 0.833 35.49392  ? 301 A1AXS A C7  1 
HETATM 1665 C C8  . A1AXS B 2 .   ? 5.52108   -13.44212 -26.50104 0.833 42.56448  ? 301 A1AXS A C8  1 
HETATM 1666 C C9  . A1AXS B 2 .   ? 6.92760   -14.04617 -26.61546 0.833 35.28809  ? 301 A1AXS A C9  1 
HETATM 1667 N N1  . A1AXS B 2 .   ? 3.93576   -13.38168 -24.58220 0.833 37.53159  ? 301 A1AXS A N1  1 
HETATM 1668 O O1  . A1AXS B 2 .   ? 1.84960   -12.51354 -24.23296 0.833 48.15741  ? 301 A1AXS A O1  1 
HETATM 1669 S S1  . A1AXS B 2 .   ? 2.67383   -9.54833  -24.53547 0.833 57.43270  ? 301 A1AXS A S1  1 
HETATM 1670 O O   . HOH   C 3 .   ? -10.43945 -23.71819 -2.46951  1.000 54.83716  ? 401 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 19.06060  -9.86299  -9.30472  1.000 50.50131  ? 402 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -6.92776  -27.96648 -7.58830  1.000 43.14546  ? 403 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -1.03831  -28.61865 -5.37389  1.000 37.97703  ? 404 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -3.20002  -0.26632  -23.00569 1.000 41.18880  ? 405 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 5.75307   -25.02036 -38.06858 1.000 47.46207  ? 406 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -12.22606 -29.01392 -16.95400 1.000 55.66886  ? 407 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -4.84547  -31.25702 -11.35750 1.000 40.41330  ? 408 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -15.94451 -24.97956 -9.45631  1.000 55.05631  ? 409 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 8.77671   -22.89395 -13.59069 1.000 40.50861  ? 410 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 8.45763   -26.75965 -26.92536 1.000 42.53976  ? 411 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 17.36503  -1.30049  -18.76037 1.000 37.60076  ? 412 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -4.93254  -2.38247  -20.47547 1.000 30.53624  ? 413 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 6.06268   -20.67662 0.27599   1.000 38.41905  ? 414 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 3.79952   -5.11738  -6.13777  1.000 54.40545  ? 415 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -19.34011 -14.43142 -19.93464 1.000 47.70963  ? 416 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -15.56777 -26.05250 -18.22631 1.000 41.50616  ? 417 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 18.70740  -26.34437 -20.04318 1.000 49.39473  ? 418 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -3.87703  -10.99397 -27.86296 1.000 26.33578  ? 419 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 0.66131   -5.70067  -19.00577 1.000 37.72008  ? 420 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 6.91868   -20.22860 -40.31241 1.000 43.73875  ? 421 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 8.18504   -18.42124 -6.03203  1.000 35.78682  ? 422 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -6.74984  -13.01246 -37.07607 1.000 35.04933  ? 423 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 1.24971   -20.55741 -4.53451  1.000 41.22201  ? 424 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 13.40829  -0.60391  -20.08201 1.000 41.87815  ? 425 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 8.34868   -22.16380 -36.71569 1.000 47.84655  ? 426 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 14.02541  -27.88163 -33.39712 1.000 32.91710  ? 427 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 3.85306   -5.74096  -11.35712 1.000 41.94095  ? 428 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 11.43067  -3.61199  -21.46963 1.000 40.58941  ? 429 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -11.84436 -26.00105 -11.23701 1.000 51.21355  ? 430 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 1.26985   -5.40010  -14.54003 1.000 42.51055  ? 431 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 19.30709  -16.13067 -12.73631 1.000 41.23156  ? 432 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -5.39161  -27.99575 -21.18026 1.000 50.65437  ? 433 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 19.26698  -18.77535 -23.58627 1.000 46.05792  ? 434 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 10.35899  -26.08507 -16.23251 1.000 39.08630  ? 435 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -10.065   -0.328    -16.764   1.000 47.17227  ? 436 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -13.76114 -11.92446 -30.74702 1.000 37.71472  ? 437 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -13.83990 -30.54011 -21.22557 1.000 57.15553  ? 438 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -15.24900 -13.19856 -20.85837 1.000 29.52462  ? 439 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -6.97411  -25.04267 -19.19121 1.000 26.14646  ? 440 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -17.62652 -11.62734 -24.83682 1.000 42.61162  ? 441 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 10.35315  -17.17100 -7.24141  1.000 29.77838  ? 442 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 5.53232   -8.20019  -36.26596 1.000 44.42824  ? 443 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 16.67135  -19.94513 -17.84341 1.000 36.16721  ? 444 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -18.73056 -19.45245 -14.62356 1.000 32.57109  ? 445 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 21.04048  -2.54511  -8.18367  1.000 57.46341  ? 446 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -10.63548 -14.20504 0.42623   1.000 40.16919  ? 447 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 14.10698  -15.33004 -1.24628  1.000 48.00229  ? 448 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -8.36858  -2.67395  -18.58134 1.000 34.89046  ? 449 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -2.77463  -5.53067  -7.02544  1.000 44.01625  ? 450 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? 9.14821   -27.80372 -23.32716 1.000 37.52615  ? 451 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 1.39120   -7.77426  -31.63693 1.000 39.63199  ? 452 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -4.65437  -7.56473  -13.91413 1.000 26.26537  ? 453 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -3.80299  -14.08962 -1.06006  1.000 50.71156  ? 454 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 12.65412  -25.62057 -25.82981 1.000 38.59623  ? 455 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -0.23541  -14.45593 -35.76990 1.000 32.84923  ? 456 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 11.35714  -14.18446 -24.80134 1.000 35.93211  ? 457 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? 6.21860   -28.43803 -7.70356  1.000 53.73968  ? 458 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 10.80833  -16.99864 -39.27281 1.000 53.81130  ? 459 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -3.14063  -20.73094 -0.58842  1.000 54.06904  ? 460 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -13.75032 -7.29892  -15.65974 1.000 47.14786  ? 461 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -4.68634  -8.72419  -35.17644 1.000 28.09485  ? 462 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 3.02901   -20.00802 -2.36163  1.000 41.91016  ? 463 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -4.60454  -6.02541  -39.85438 1.000 42.92825  ? 464 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 13.29101  -28.36020 -29.12505 1.000 40.78065  ? 465 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -3.35690  -4.95179  -9.06716  1.000 48.16481  ? 466 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 0.88616   -26.67442 -32.14127 1.000 51.11371  ? 467 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 2.23635   -7.87190  -16.99402 1.000 31.82484  ? 468 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -0.67790  -10.73010 -3.35557  1.000 50.43060  ? 469 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 10.34587  -12.20835 -28.95152 1.000 36.58171  ? 470 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -8.97850  -15.35361 -38.43605 1.000 48.26498  ? 471 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -2.83450  -11.83033 -9.37069  1.000 37.08662  ? 472 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -13.42332 -16.62196 -3.41794  1.000 37.01058  ? 473 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -4.412    6.004     -35.493   1.000 56.91479  ? 474 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? 16.34644  -0.54561  -11.97134 1.000 42.09635  ? 475 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 10.26966  -15.81932 -27.11623 1.000 38.28960  ? 476 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -6.07794  0.68642   -37.72403 1.000 36.60222  ? 477 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 6.03195   -24.57396 -30.21736 1.000 30.47653  ? 478 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -17.88298 -11.34108 -33.83710 1.000 63.05966  ? 479 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 9.29485   -20.22097 -8.55743  1.000 35.86116  ? 480 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -6.52122  -24.76338 -23.09437 1.000 39.14291  ? 481 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 8.06898   -29.69813 -19.41044 1.000 42.85935  ? 482 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 14.58912  -9.05987  -3.81690  1.000 56.83535  ? 483 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -13.63314 -22.36328 -11.90975 1.000 42.17799  ? 484 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 12.10452  -25.26942 -22.83401 1.000 29.11700  ? 485 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -7.90066  1.18906   -26.64577 1.000 38.82153  ? 486 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 8.19812   -7.17354  -24.28472 1.000 41.77973  ? 487 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -3.66067  -8.74954  -43.25120 1.000 53.58798  ? 488 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -0.60975  -32.27000 -7.41509  1.000 52.60452  ? 489 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 5.09983   -9.26093  -20.13772 1.000 31.92283  ? 490 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -5.46719  -11.23021 -10.62925 1.000 35.01289  ? 491 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -1.26740  -25.07538 -4.48741  1.000 34.18296  ? 492 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -12.41539 -7.63451  -13.22703 1.000 44.21010  ? 493 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -10.18561 -11.03548 -2.91818  1.000 37.00748  ? 494 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 8.796     -5.309    -22.226   1.000 47.43133  ? 495 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -14.69919 -29.19613 -17.49156 1.000 46.30505  ? 496 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -11.78119 -0.93538  -21.46185 1.000 40.52909  ? 497 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -16.45558 -4.71156  -30.57644 1.000 50.26703  ? 498 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -4.81576  -4.93412  -12.49735 1.000 48.71229  ? 499 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 14.91728  -20.24859 -19.83227 1.000 33.45718  ? 500 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -6.10264  -13.59379 0.45431   1.000 41.20635  ? 501 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 0.15209   -10.29351 -43.92069 1.000 57.26580  ? 502 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -15.01279 -3.48825  -22.77468 1.000 46.98971  ? 503 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 3.97283   -6.69621  -20.54471 1.000 45.87996  ? 504 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -13.20168 -0.97499  -15.50012 1.000 43.05345  ? 505 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 10.60457  -20.86727 -6.38513  1.000 44.49181  ? 506 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -8.83821  -0.88320  -20.80986 1.000 33.51872  ? 507 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -8.71550  -15.79891 -28.88210 1.000 36.80143  ? 508 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 15.86462  -17.80286 -2.63018  1.000 44.57561  ? 509 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 8.44426   -23.09956 -6.77331  1.000 45.93217  ? 510 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -17.14856 -15.57017 -14.36580 1.000 43.61833  ? 511 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 0.79782   -12.66674 -21.53518 1.000 35.89710  ? 512 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -3.80687  -14.60851 -22.90513 1.000 30.02377  ? 513 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -2.13892  -13.16271 -21.25735 1.000 37.83615  ? 514 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -13.15552 -25.34390 -7.93776  1.000 45.05142  ? 515 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 15.08658  -3.40272  -24.71051 1.000 50.52849  ? 516 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 11.00383  -20.21649 -40.92961 1.000 60.90035  ? 517 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 11.93300  -14.29100 -28.25023 1.000 54.23783  ? 518 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -7.04825  -11.74832 -41.05352 1.000 53.82794  ? 519 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 4.49183   -6.63126  -17.94226 1.000 31.54068  ? 520 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -15.95788 -5.80164  -24.26118 1.000 41.06507  ? 521 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -7.65648  -3.64317  -11.56458 1.000 50.78688  ? 522 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -16.88819 -6.83798  -26.89906 1.000 48.74650  ? 523 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 4.34214   -26.49879 -29.12371 1.000 50.58676  ? 524 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -5.38051  -24.37303 -30.77982 1.000 50.79479  ? 525 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -6.36514  1.40878   -21.04285 1.000 40.91881  ? 526 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 21.82485  -12.96929 -25.59253 1.000 51.95285  ? 527 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 9.12886   -20.11263 -3.74852  1.000 33.66246  ? 528 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -12.33618 -19.22541 -24.95287 1.000 34.08065  ? 529 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 1.40983   -29.64186 -15.58202 1.000 41.48096  ? 530 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -15.40400 -8.86589  -15.58509 1.000 46.15847  ? 531 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -3.60425  -19.86842 -39.39441 1.000 41.29177  ? 532 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 1.63634   -15.03461 -42.96274 1.000 57.69324  ? 533 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 5.80687   -30.28437 -11.10527 1.000 48.40916  ? 534 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 1.85471   -6.69407  -38.87010 1.000 56.80872  ? 535 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -14.40439 -25.24902 -11.29477 1.000 46.99638  ? 536 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 5.84412   -12.20261 -38.50445 1.000 37.05776  ? 537 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -4.72889  -14.75878 -41.64103 1.000 53.60485  ? 538 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 13.82761  -27.21516 -18.35811 1.000 52.09664  ? 539 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -6.66158  -18.91077 -37.16595 1.000 52.67069  ? 540 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -11.37443 -13.14434 -31.78374 1.000 35.36756  ? 541 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 3.14206   -4.10793  -17.70280 1.000 50.74400  ? 542 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -12.92993 -16.88835 -26.75649 1.000 45.57521  ? 543 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 0.25536   -16.33972 -3.43106  1.000 35.35969  ? 544 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 7.013     1.810     -14.115   1.000 52.83618  ? 545 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 4.46960   -22.25309 -3.09029  1.000 45.23126  ? 546 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -13.41376 -23.77516 -5.30055  1.000 43.40707  ? 547 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 11.10391  -7.87555  -37.05998 1.000 49.72089  ? 548 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 1.30427   -8.34089  -4.00248  1.000 42.39784  ? 549 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 1.63763   -17.71531 0.02194   1.000 47.35160  ? 550 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 8.39587   -10.41967 -23.51270 1.000 45.00927  ? 551 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 11.32809  -10.96312 -4.11459  1.000 43.26612  ? 552 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 20.92944  -23.85560 -20.56606 1.000 57.63536  ? 553 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -1.03760  -10.53450 -27.27695 1.000 49.82109  ? 554 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -5.08905  -23.56458 -36.68342 1.000 51.96971  ? 555 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -1.075    5.469     -32.029   1.000 49.50528  ? 556 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -4.73590  -6.07644  -36.68429 1.000 30.48667  ? 557 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 12.93638  -18.45954 -38.24122 1.000 48.82337  ? 558 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -1.65219  -1.42807  -25.28969 1.000 45.96647  ? 559 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -5.98944  -25.01938 -26.18619 1.000 59.05085  ? 560 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 19.543    -24.119   -23.871   1.000 46.61685  ? 561 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 7.49540   -9.38260  -22.01490 1.000 45.15756  ? 562 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 14.25655  -13.91286 -25.94159 1.000 24.82295  ? 563 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? 15.69168  -22.11742 -16.14027 1.000 40.88572  ? 564 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? -1.976    1.366     -33.684   1.000 50.85015  ? 565 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 6.209     -10.654   -0.825    1.000 55.08423  ? 566 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -7.72143  2.69827   -22.47997 1.000 45.86991  ? 567 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -12.77188 -26.49624 -18.45215 1.000 37.63001  ? 568 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -0.68380  -27.35754 -24.50930 1.000 47.73072  ? 569 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 10.62603  -25.78180 -25.44780 1.000 43.80834  ? 570 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 20.754    -21.276   -24.441   1.000 60.02872  ? 571 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -8.73876  -26.42878 -20.76236 1.000 42.00159  ? 572 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -19.48171 -19.08344 -11.86463 1.000 48.65118  ? 573 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 7.680     -0.980    -18.735   1.000 49.52619  ? 574 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 14.71045  -0.79146  -5.62025  1.000 56.82363  ? 575 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 18.99229  -21.08452 -18.83746 1.000 47.34617  ? 576 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 3.24864   -7.96139  -1.88939  1.000 60.08429  ? 577 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -10.71559 -17.35078 -28.71993 1.000 48.37889  ? 578 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 12.54025  -0.76879  -4.15829  1.000 61.40112  ? 579 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 6.684     1.954     -16.874   1.000 48.23481  ? 580 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -13.72323 -13.98504 -3.69401  1.000 46.42614  ? 581 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 16.80386  -23.15070 -13.88654 1.000 58.84077  ? 582 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 9.93522   -14.25732 -37.95756 1.000 51.32868  ? 583 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -15.618   -0.753    -19.238   1.000 41.55502  ? 584 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -14.03223 -9.49744  -12.35271 1.000 49.48460  ? 585 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -0.84728  -2.49890  -30.87656 1.000 58.51137  ? 586 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -8.43716  -18.17343 -38.16407 1.000 61.82701  ? 587 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -17.60915 -12.27324 -22.34620 1.000 41.73271  ? 588 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? -11.51014 -26.73235 -20.68720 1.000 39.27918  ? 589 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -2.95735  -26.64627 -2.76771  1.000 53.35722  ? 590 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -6.12028  -30.65428 -8.49463  1.000 49.32990  ? 591 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 8.03314   -29.97554 -24.39182 1.000 48.68707  ? 592 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 12.13381  -0.87369  -17.69713 1.000 38.40907  ? 593 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 19.58825  -3.61949  -22.39598 1.000 62.21289  ? 594 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -15.58385 -2.16040  -16.70414 1.000 48.86859  ? 595 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 14.69588  -26.98794 -16.48977 1.000 60.94783  ? 596 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 1.53746   -27.06635 -30.33936 1.000 50.59179  ? 597 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 18.24041  -3.30552  -24.98485 1.000 54.03052  ? 598 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 19.19958  -1.29210  -20.97547 1.000 47.14241  ? 599 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? -10.37928 -8.15707  -2.25323  1.000 49.78377  ? 600 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 8.10847   -13.52736 -39.87295 1.000 45.08467  ? 601 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -10.69566 -21.22437 -25.74705 1.000 48.96944  ? 602 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 2.04373   -1.12175  -29.26433 1.000 49.89607  ? 603 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -14.62863 -1.29891  -13.23109 1.000 46.80715  ? 604 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? -8.69213  -10.94374 -0.52800  1.000 56.44452  ? 605 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -4.73574  -17.96437 -41.33500 1.000 54.31756  ? 606 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 7.16191   -21.35746 -2.17893  1.000 43.12497  ? 607 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? 4.98691   -10.05588 -39.68585 1.000 56.07407  ? 608 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 10.82212  -29.94642 -29.35135 1.000 49.84776  ? 609 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 14.19063  -25.00302 -14.88642 1.000 52.86828  ? 610 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 0.92111   -2.79898  -31.42549 1.000 54.43890  ? 611 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -4.87909  -6.44593  -44.58526 1.000 60.20790  ? 612 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 14.59721  -12.69491 -2.12720  1.000 57.81424  ? 613 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -9.23098  -23.67011 -23.74139 1.000 51.30818  ? 614 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 10.49444  -25.31000 -13.61087 1.000 54.05452  ? 615 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -6.990    -22.775   -2.253    1.000 44.50092  ? 616 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -12.20646 -12.59534 -1.91674  1.000 46.79801  ? 617 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 13.99810  -11.37362 -4.57472  1.000 53.72805  ? 618 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -2.97063  -28.71433 -23.18087 1.000 56.46703  ? 619 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 16.41106  0.70612   -7.63540  1.000 55.32943  ? 620 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -15.20378 -18.10410 -1.67159  1.000 58.05366  ? 621 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -10.56563 -11.20892 1.33169   1.000 55.32034  ? 622 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 17.74198  -27.33573 -17.32375 1.000 61.27671  ? 623 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 22.486    -20.002   -25.988   1.000 54.11221  ? 624 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -1.80946  -26.88707 -26.92063 1.000 55.25671  ? 625 HOH   A 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   . GLU A 9   ? 0.92452 0.83016 0.72975 -0.01786 -0.05258 -0.21068 16  GLU A N   
2    C CA  . GLU A 9   ? 0.85082 0.75171 0.65570 0.00958  -0.04728 -0.18755 16  GLU A CA  
3    C C   . GLU A 9   ? 0.82950 0.74464 0.66353 0.01433  -0.04818 -0.16505 16  GLU A C   
4    O O   . GLU A 9   ? 0.84658 0.80054 0.69699 0.01377  -0.05869 -0.15946 16  GLU A O   
5    C CB  . GLU A 9   ? 0.98760 0.91991 0.77921 0.02601  -0.05465 -0.18601 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.23122 1.17256 1.03084 0.04834  -0.05042 -0.16014 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.56155 1.49717 1.33658 0.06654  -0.04352 -0.15827 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.56811 1.49729 1.31734 0.06463  -0.04473 -0.17709 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.40553 1.34473 1.18681 0.08126  -0.03617 -0.13898 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.63800 0.52200 0.47585 0.02125  -0.03707 -0.15256 17  VAL A N   
11   C CA  . VAL A 10  ? 0.63981 0.53373 0.50220 0.02498  -0.03709 -0.13319 17  VAL A CA  
12   C C   . VAL A 10  ? 0.60537 0.50390 0.46936 0.04648  -0.03204 -0.11599 17  VAL A C   
13   O O   . VAL A 10  ? 0.62336 0.49975 0.47317 0.05844  -0.02264 -0.11615 17  VAL A O   
14   C CB  . VAL A 10  ? 0.71052 0.56977 0.57555 0.01495  -0.02875 -0.13292 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.60547 0.47933 0.49469 0.01765  -0.03036 -0.11466 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.74371 0.59223 0.60231 -0.01091 -0.02941 -0.15397 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.48781 0.41500 0.36799 0.05109  -0.03692 -0.10217 18  GLU A N   
18   C CA  . GLU A 11  ? 0.49375 0.42786 0.37921 0.06537  -0.03067 -0.08685 18  GLU A CA  
19   C C   . GLU A 11  ? 0.45667 0.39044 0.36249 0.06391  -0.02899 -0.07503 18  GLU A C   
20   O O   . GLU A 11  ? 0.42036 0.36070 0.33879 0.05401  -0.03479 -0.07315 18  GLU A O   
21   C CB  . GLU A 11  ? 0.42658 0.38516 0.31001 0.07083  -0.03365 -0.07936 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.50852 0.46982 0.36732 0.07649  -0.03478 -0.08929 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.75454 0.73474 0.60577 0.08425  -0.03630 -0.07928 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.61288 0.60731 0.46802 0.08175  -0.04526 -0.07745 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.81517 0.79483 0.65415 0.09408  -0.02715 -0.07314 18  GLU A OE2 
26   N N   . THR A 12  ? 0.40560 0.33615 0.31433 0.07510  -0.02120 -0.06765 19  THR A N   
27   C CA  . THR A 12  ? 0.37982 0.31462 0.30570 0.07584  -0.02044 -0.05738 19  THR A CA  
28   C C   . THR A 12  ? 0.40006 0.36286 0.33947 0.07957  -0.01828 -0.04697 19  THR A C   
29   O O   . THR A 12  ? 0.39516 0.36839 0.33037 0.08802  -0.01188 -0.04609 19  THR A O   
30   C CB  . THR A 12  ? 0.41546 0.32793 0.33353 0.08722  -0.01353 -0.05761 19  THR A CB  
31   O OG1 . THR A 12  ? 0.47782 0.35514 0.37802 0.08059  -0.01201 -0.06882 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.38631 0.30592 0.31890 0.08982  -0.01437 -0.04720 19  THR A CG2 
33   N N   . PHE A 13  ? 0.36247 0.33661 0.31723 0.07189  -0.02204 -0.04009 20  PHE A N   
34   C CA  . PHE A 13  ? 0.36937 0.36571 0.33539 0.06906  -0.01922 -0.03251 20  PHE A CA  
35   C C   . PHE A 13  ? 0.38719 0.39558 0.36939 0.06777  -0.02032 -0.02775 20  PHE A C   
36   O O   . PHE A 13  ? 0.39389 0.39068 0.37739 0.06657  -0.02495 -0.02788 20  PHE A O   
37   C CB  . PHE A 13  ? 0.35110 0.34663 0.31475 0.06004  -0.02244 -0.02996 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.37345 0.36241 0.31957 0.06319  -0.02381 -0.03407 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.41518 0.39607 0.35514 0.06157  -0.03139 -0.04234 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.37389 0.36708 0.30859 0.06693  -0.01703 -0.03041 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.39416 0.37645 0.31741 0.06494  -0.03466 -0.04819 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.40361 0.39260 0.31793 0.07257  -0.01928 -0.03377 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.45037 0.43654 0.35956 0.07226  -0.02923 -0.04334 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.31050 0.34436 0.30419 0.06697  -0.01555 -0.02432 21  ALA A N   
45   C CA  . ALA A 14  ? 0.38706 0.44009 0.39654 0.06278  -0.01823 -0.02159 21  ALA A CA  
46   C C   . ALA A 14  ? 0.38705 0.43540 0.39902 0.04687  -0.02022 -0.02002 21  ALA A C   
47   O O   . ALA A 14  ? 0.40397 0.44648 0.40963 0.03956  -0.01538 -0.01893 21  ALA A O   
48   C CB  . ALA A 14  ? 0.35511 0.44597 0.37872 0.06575  -0.01249 -0.02145 21  ALA A CB  
49   N N   . PHE A 15  ? 0.35034 0.39796 0.36773 0.04326  -0.02606 -0.01933 22  PHE A N   
50   C CA  . PHE A 15  ? 0.38090 0.42585 0.40002 0.02923  -0.02612 -0.01883 22  PHE A CA  
51   C C   . PHE A 15  ? 0.36203 0.43084 0.39055 0.01823  -0.01956 -0.02043 22  PHE A C   
52   O O   . PHE A 15  ? 0.36404 0.46365 0.40469 0.02215  -0.01859 -0.02227 22  PHE A O   
53   C CB  . PHE A 15  ? 0.34228 0.38546 0.36457 0.02817  -0.03277 -0.01870 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.35291 0.37233 0.36698 0.03154  -0.03664 -0.01791 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.36117 0.36599 0.36894 0.02660  -0.03651 -0.01788 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.33111 0.34372 0.34275 0.03990  -0.03914 -0.01719 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.36197 0.35538 0.36657 0.02826  -0.04009 -0.01883 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.38253 0.37575 0.38820 0.03837  -0.04061 -0.01801 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.34546 0.33395 0.35038 0.03162  -0.04171 -0.01967 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.41076 0.46600 0.43284 0.00432  -0.01379 -0.02021 23  GLN A N   
61   C CA  . GLN A 16  ? 0.50753 0.58364 0.53913 -0.01278 -0.00712 -0.02442 23  GLN A CA  
62   C C   . GLN A 16  ? 0.48027 0.58545 0.52684 -0.01482 -0.01545 -0.02949 23  GLN A C   
63   O O   . GLN A 16  ? 0.45121 0.54594 0.49438 -0.00742 -0.02409 -0.02826 23  GLN A O   
64   C CB  . GLN A 16  ? 0.61639 0.66164 0.63285 -0.02802 0.00153  -0.02384 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.69348 0.71339 0.69178 -0.02430 0.01102  -0.01762 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.73500 0.71719 0.71233 -0.03461 0.02087  -0.01505 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.88124 0.85497 0.85121 -0.05067 0.03555  -0.01535 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.81449 0.77179 0.78029 -0.02560 0.01470  -0.01257 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.46516 0.61085 0.52803 -0.02511 -0.01244 -0.03561 24  ALA A N   
70   C CA  . ALA A 17  ? 0.49501 0.67934 0.57212 -0.02226 -0.02214 -0.04064 24  ALA A CA  
71   C C   . ALA A 17  ? 0.48530 0.65281 0.55466 -0.03248 -0.02742 -0.04415 24  ALA A C   
72   O O   . ALA A 17  ? 0.40596 0.58288 0.47540 -0.02075 -0.03768 -0.04335 24  ALA A O   
73   C CB  . ALA A 17  ? 0.51895 0.75893 0.61742 -0.03434 -0.01793 -0.04901 24  ALA A CB  
74   N N   . GLU A 18  ? 0.37677 0.51494 0.43531 -0.05252 -0.01901 -0.04739 25  GLU A N   
75   C CA  . GLU A 18  ? 0.44380 0.56218 0.49180 -0.06201 -0.02189 -0.05195 25  GLU A CA  
76   C C   . GLU A 18  ? 0.37988 0.46896 0.41609 -0.04325 -0.02898 -0.04395 25  GLU A C   
77   O O   . GLU A 18  ? 0.36794 0.45795 0.40062 -0.04168 -0.03577 -0.04635 25  GLU A O   
78   C CB  . GLU A 18  ? 0.56440 0.64554 0.59668 -0.08359 -0.00822 -0.05560 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.64406 0.74641 0.68472 -0.11071 0.00315  -0.06558 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.82306 0.94546 0.87452 -0.10795 0.01055  -0.06092 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.79207 0.88903 0.83334 -0.08932 0.01178  -0.04952 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.73706 0.90260 0.80668 -0.12590 0.01594  -0.06996 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.39201 0.45666 0.42130 -0.03060 -0.02675 -0.03552 26  ILE A N   
84   C CA  . ILE A 19  ? 0.41377 0.45513 0.43437 -0.01680 -0.03200 -0.02985 26  ILE A CA  
85   C C   . ILE A 19  ? 0.39347 0.45370 0.42113 -0.00274 -0.04048 -0.02738 26  ILE A C   
86   O O   . ILE A 19  ? 0.36046 0.41227 0.38289 0.00244  -0.04494 -0.02568 26  ILE A O   
87   C CB  . ILE A 19  ? 0.41638 0.43294 0.42791 -0.00893 -0.02802 -0.02401 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.50041 0.48761 0.49618 -0.01625 -0.01925 -0.02328 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.40551 0.41121 0.41419 0.00321  -0.03401 -0.02060 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.63845 0.62557 0.63186 -0.03209 -0.00866 -0.02628 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.32727 0.41091 0.36407 0.00502  -0.04107 -0.02651 27  ALA A N   
92   C CA  . ALA A 20  ? 0.37036 0.46811 0.40869 0.02165  -0.04725 -0.02317 27  ALA A CA  
93   C C   . ALA A 20  ? 0.29119 0.41149 0.33099 0.02009  -0.05365 -0.02623 27  ALA A C   
94   O O   . ALA A 20  ? 0.32718 0.44004 0.35804 0.03212  -0.05789 -0.02145 27  ALA A O   
95   C CB  . ALA A 20  ? 0.37055 0.49237 0.41706 0.03291  -0.04557 -0.02238 27  ALA A CB  
96   N N   . GLN A 21  ? 0.32504 0.47227 0.37379 0.00423  -0.05359 -0.03482 28  GLN A N   
97   C CA  . GLN A 21  ? 0.33771 0.50888 0.38592 0.00088  -0.06085 -0.04041 28  GLN A CA  
98   C C   . GLN A 21  ? 0.37851 0.51487 0.41089 -0.00280 -0.06112 -0.03942 28  GLN A C   
99   O O   . GLN A 21  ? 0.30439 0.44735 0.32860 0.00526  -0.06731 -0.03828 28  GLN A O   
100  C CB  . GLN A 21  ? 0.35520 0.56109 0.41571 -0.02151 -0.05959 -0.05350 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.45687 0.70875 0.53691 -0.02093 -0.05834 -0.05666 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.68621 0.96451 0.77812 -0.05131 -0.05273 -0.07107 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.59470 0.85333 0.67696 -0.07195 -0.05048 -0.07935 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.66715 0.98627 0.77827 -0.05560 -0.04816 -0.07467 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.34543 0.44628 0.37150 -0.01306 -0.05384 -0.03954 29  LEU A N   
106  C CA  . LEU A 22  ? 0.39250 0.46323 0.40454 -0.01388 -0.05286 -0.03860 29  LEU A CA  
107  C C   . LEU A 22  ? 0.39358 0.45186 0.40034 0.00299  -0.05524 -0.02915 29  LEU A C   
108  O O   . LEU A 22  ? 0.40369 0.45655 0.40086 0.00637  -0.05712 -0.02804 29  LEU A O   
109  C CB  . LEU A 22  ? 0.39840 0.43565 0.40340 -0.02211 -0.04420 -0.03895 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.45309 0.46297 0.44521 -0.01792 -0.04242 -0.03701 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.52925 0.54052 0.51175 -0.02631 -0.04344 -0.04513 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.46634 0.44628 0.45047 -0.01754 -0.03460 -0.03452 29  LEU A CD2 
113  N N   . MET A 23  ? 0.31858 0.36962 0.32924 0.01218  -0.05364 -0.02298 30  MET A N   
114  C CA  . MET A 23  ? 0.37266 0.40680 0.37602 0.02316  -0.05336 -0.01593 30  MET A CA  
115  C C   . MET A 23  ? 0.35293 0.39993 0.34962 0.03562  -0.05735 -0.01161 30  MET A C   
116  O O   . MET A 23  ? 0.39068 0.42226 0.37543 0.04085  -0.05579 -0.00651 30  MET A O   
117  C CB  . MET A 23  ? 0.36109 0.37932 0.36611 0.02797  -0.04998 -0.01258 30  MET A CB  
118  C CG  . MET A 23  ? 0.36827 0.37537 0.37626 0.02061  -0.04697 -0.01532 30  MET A CG  
119  S SD  . MET A 23  ? 0.39569 0.40052 0.40673 0.02517  -0.04512 -0.01524 30  MET A SD  
120  C CE  . MET A 23  ? 0.42850 0.41486 0.43326 0.02951  -0.04409 -0.01316 30  MET A CE  
121  N N   . SER A 24  ? 0.30887 0.38646 0.31170 0.04121  -0.06188 -0.01339 31  SER A N   
122  C CA  . SER A 24  ? 0.37439 0.46690 0.36732 0.05834  -0.06651 -0.00808 31  SER A CA  
123  C C   . SER A 24  ? 0.37146 0.47418 0.35575 0.05344  -0.07100 -0.01157 31  SER A C   
124  O O   . SER A 24  ? 0.38882 0.48438 0.35582 0.06673  -0.07181 -0.00430 31  SER A O   
125  C CB  . SER A 24  ? 0.41031 0.54200 0.41399 0.06897  -0.07085 -0.00963 31  SER A CB  
126  O OG  . SER A 24  ? 0.61373 0.77901 0.61196 0.08053  -0.07884 -0.00960 31  SER A OG  
127  N N   . LEU A 25  ? 0.37801 0.49200 0.36991 0.03434  -0.07230 -0.02266 32  LEU A N   
128  C CA  . LEU A 25  ? 0.33632 0.45471 0.31678 0.02816  -0.07548 -0.02824 32  LEU A CA  
129  C C   . LEU A 25  ? 0.35270 0.43340 0.31845 0.03067  -0.06922 -0.02155 32  LEU A C   
130  O O   . LEU A 25  ? 0.40903 0.48969 0.35867 0.03683  -0.07076 -0.01941 32  LEU A O   
131  C CB  . LEU A 25  ? 0.37390 0.50115 0.36172 0.00497  -0.07490 -0.04280 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.59358 0.72053 0.56807 -0.00636 -0.07655 -0.05310 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.56346 0.70801 0.54581 -0.03051 -0.07622 -0.06978 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.50723 0.59006 0.46867 -0.00729 -0.06826 -0.04955 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.33580 0.38856 0.30683 0.02594  -0.06195 -0.01883 33  ILE A N   
136  C CA  . ILE A 26  ? 0.37372 0.39950 0.33585 0.02650  -0.05529 -0.01415 33  ILE A CA  
137  C C   . ILE A 26  ? 0.45465 0.46907 0.40509 0.03973  -0.05238 -0.00297 33  ILE A C   
138  O O   . ILE A 26  ? 0.40462 0.40692 0.34124 0.04183  -0.04773 0.00118  33  ILE A O   
139  C CB  . ILE A 26  ? 0.39074 0.39947 0.36336 0.01963  -0.04986 -0.01526 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.37175 0.37829 0.34518 0.00899  -0.04880 -0.02407 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.40383 0.39472 0.37327 0.02137  -0.04300 -0.01010 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.42659 0.42001 0.40721 0.00649  -0.04465 -0.02417 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.39740 0.41232 0.34991 0.04935  -0.05320 0.00226  34  ILE A N   
144  C CA  . ILE A 27  ? 0.41585 0.40918 0.35164 0.06241  -0.04753 0.01337  34  ILE A CA  
145  C C   . ILE A 27  ? 0.48343 0.48901 0.39958 0.07842  -0.05168 0.01932  34  ILE A C   
146  O O   . ILE A 27  ? 0.55003 0.53281 0.44410 0.08629  -0.04475 0.02878  34  ILE A O   
147  C CB  . ILE A 27  ? 0.48828 0.47250 0.42892 0.06907  -0.04566 0.01590  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.47055 0.43894 0.42433 0.05426  -0.04068 0.01087  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.53676 0.49468 0.45309 0.08710  -0.03911 0.02784  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.50824 0.47702 0.47053 0.05725  -0.04138 0.00867  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.46484 0.50881 0.38733 0.08292  -0.06252 0.01351  35  ASN A N   
152  C CA  . ASN A 28  ? 0.46037 0.52499 0.36416 0.10236  -0.06882 0.01885  35  ASN A CA  
153  C C   . ASN A 28  ? 0.46637 0.54776 0.35980 0.09678  -0.07391 0.01282  35  ASN A C   
154  O O   . ASN A 28  ? 0.51721 0.60920 0.38793 0.11486  -0.07770 0.01939  35  ASN A O   
155  C CB  . ASN A 28  ? 0.48972 0.59753 0.40634 0.11347  -0.07866 0.01515  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.58396 0.67430 0.50419 0.12498  -0.07300 0.02211  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.61375 0.65872 0.51602 0.13317  -0.06264 0.03291  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.63469 0.75848 0.57708 0.12339  -0.07797 0.01485  35  ASN A ND2 
159  N N   . THR A 29  ? 0.46470 0.54671 0.36957 0.07498  -0.07360 0.00088  36  THR A N   
160  C CA  . THR A 29  ? 0.48527 0.58119 0.37708 0.06976  -0.07792 -0.00708 36  THR A CA  
161  C C   . THR A 29  ? 0.50634 0.57046 0.37398 0.07583  -0.06831 0.00284  36  THR A C   
162  O O   . THR A 29  ? 0.51130 0.54277 0.38197 0.07032  -0.05683 0.00855  36  THR A O   
163  C CB  . THR A 29  ? 0.46641 0.56546 0.37320 0.04568  -0.07816 -0.02339 36  THR A CB  
164  O OG1 . THR A 29  ? 0.46579 0.59467 0.39311 0.03774  -0.08480 -0.03236 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.49145 0.60050 0.38125 0.03915  -0.08164 -0.03423 36  THR A CG2 
166  N N   . PHE A 30  ? 0.45153 0.52899 0.29487 0.08674  -0.07266 0.00425  37  PHE A N   
167  C CA  . PHE A 30  ? 0.48784 0.53670 0.30699 0.09017  -0.06177 0.01254  37  PHE A CA  
168  C C   . PHE A 30  ? 0.52856 0.57075 0.35394 0.07102  -0.05758 -0.00025 37  PHE A C   
169  O O   . PHE A 30  ? 0.47698 0.54094 0.30216 0.06239  -0.06589 -0.01538 37  PHE A O   
170  C CB  . PHE A 30  ? 0.53450 0.59815 0.32070 0.11028  -0.06706 0.01897  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.54293 0.57721 0.30094 0.11358  -0.05403 0.02798  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.63837 0.63263 0.38187 0.12143  -0.03817 0.04614  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.58192 0.62668 0.32616 0.10745  -0.05573 0.01755  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.67825 0.64677 0.39564 0.12238  -0.02349 0.05480  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.60902 0.62865 0.32648 0.11128  -0.04194 0.02626  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.61021 0.59343 0.31549 0.11826  -0.02547 0.04537  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.47296 0.48572 0.30294 0.06447  -0.04398 0.00482  38  TYR A N   
178  C CA  . TYR A 31  ? 0.44491 0.45050 0.28234 0.05080  -0.03854 -0.00589 38  TYR A CA  
179  C C   . TYR A 31  ? 0.45832 0.44095 0.29363 0.05037  -0.02272 0.00356  38  TYR A C   
180  O O   . TYR A 31  ? 0.45394 0.42595 0.30653 0.04630  -0.01717 0.00886  38  TYR A O   
181  C CB  . TYR A 31  ? 0.45161 0.46023 0.31581 0.03839  -0.04241 -0.01583 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.46675 0.46314 0.33295 0.02960  -0.03569 -0.02518 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.50042 0.50003 0.35191 0.02460  -0.03860 -0.03839 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.48780 0.47065 0.36916 0.02731  -0.02663 -0.02211 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.63963 0.62220 0.48701 0.02011  -0.03095 -0.04669 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.52545 0.49857 0.40516 0.02497  -0.02025 -0.02996 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.58089 0.55025 0.44193 0.02231  -0.02178 -0.04164 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.77904 0.73188 0.63213 0.02269  -0.01398 -0.04977 38  TYR A OH  
189  N N   . SER A 32  ? 0.52103 0.49896 0.33521 0.05338  -0.01499 0.00455  39  SER A N   
190  C CA  . SER A 32  ? 0.52552 0.48699 0.33655 0.05210  0.00193  0.01430  39  SER A CA  
191  C C   . SER A 32  ? 0.50291 0.46541 0.33833 0.04186  0.00979  0.00759  39  SER A C   
192  O O   . SER A 32  ? 0.52702 0.48392 0.37098 0.03676  0.02258  0.01406  39  SER A O   
193  C CB  . SER A 32  ? 0.49390 0.45191 0.27197 0.06010  0.00934  0.01868  39  SER A CB  
194  O OG  . SER A 32  ? 0.55990 0.51720 0.31141 0.07401  0.00328  0.02812  39  SER A OG  
195  N N   . ASN A 33  ? 0.48906 0.45866 0.33388 0.03908  0.00357  -0.00532 40  ASN A N   
196  C CA  . ASN A 33  ? 0.51293 0.48445 0.37450 0.03610  0.01125  -0.01094 40  ASN A CA  
197  C C   . ASN A 33  ? 0.41718 0.39213 0.30745 0.03082  0.00862  -0.01004 40  ASN A C   
198  O O   . ASN A 33  ? 0.42461 0.40039 0.32656 0.03069  0.00446  -0.01714 40  ASN A O   
199  C CB  . ASN A 33  ? 0.49221 0.46006 0.34308 0.03822  0.00829  -0.02405 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.50074 0.46823 0.36318 0.04174  0.01683  -0.02874 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.50966 0.48795 0.38082 0.04446  0.02792  -0.02399 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.54949 0.50473 0.40903 0.04254  0.01310  -0.03858 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.41024 0.34019 0.28167 0.03078  -0.03321 -0.00434 41  LYS A N   
204  C CA  . LYS A 34  ? 0.41495 0.36210 0.31482 0.02912  -0.02577 -0.00256 41  LYS A CA  
205  C C   . LYS A 34  ? 0.38529 0.32453 0.29180 0.02490  -0.01584 -0.00915 41  LYS A C   
206  O O   . LYS A 34  ? 0.38558 0.33821 0.31319 0.02111  -0.01374 -0.00918 41  LYS A O   
207  C CB  . LYS A 34  ? 0.43018 0.37882 0.33230 0.03956  -0.01594 0.00337  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.43498 0.40075 0.33921 0.04669  -0.02554 0.01198  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.44510 0.40286 0.34430 0.05971  -0.01530 0.01727  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.53220 0.50783 0.43244 0.07117  -0.02393 0.02699  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.41751 0.42431 0.34451 0.07392  -0.02583 0.03107  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.44088 0.36099 0.32955 0.02696  -0.00949 -0.01389 42  GLU A N   
213  C CA  . GLU A 35  ? 0.44538 0.36313 0.34330 0.02543  0.00147  -0.01804 42  GLU A CA  
214  C C   . GLU A 35  ? 0.47187 0.39500 0.38213 0.01813  -0.00558 -0.02220 42  GLU A C   
215  O O   . GLU A 35  ? 0.42193 0.34840 0.34470 0.01705  0.00190  -0.02448 42  GLU A O   
216  C CB  . GLU A 35  ? 0.44458 0.34600 0.32142 0.03166  0.01022  -0.02049 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.47870 0.36299 0.33028 0.03330  -0.00031 -0.02650 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.65863 0.52574 0.48229 0.04444  0.01003  -0.02826 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.64212 0.50984 0.45895 0.04977  0.02022  -0.02223 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.82166 0.67379 0.62886 0.04906  0.00897  -0.03488 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.40393 0.32726 0.31023 0.01215  -0.02067 -0.02232 43  ILE A N   
222  C CA  . ILE A 36  ? 0.40996 0.33457 0.32556 0.00364  -0.02806 -0.02447 43  ILE A CA  
223  C C   . ILE A 36  ? 0.43805 0.38515 0.38137 0.00025  -0.02375 -0.02056 43  ILE A C   
224  O O   . ILE A 36  ? 0.38016 0.32870 0.33198 -0.00555 -0.02647 -0.02142 43  ILE A O   
225  C CB  . ILE A 36  ? 0.44763 0.36746 0.35401 -0.00593 -0.04720 -0.02329 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.45053 0.39760 0.37358 -0.00980 -0.05460 -0.01413 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.53171 0.42214 0.40258 -0.00159 -0.05325 -0.02936 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.48563 0.45793 0.43611 -0.01908 -0.05826 -0.00739 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.35644 0.31769 0.31033 0.00510  -0.01703 -0.01635 44  PHE A N   
230  C CA  . PHE A 37  ? 0.34357 0.32163 0.31729 0.00440  -0.01252 -0.01405 44  PHE A CA  
231  C C   . PHE A 37  ? 0.35662 0.32795 0.33428 0.00346  -0.00545 -0.01933 44  PHE A C   
232  O O   . PHE A 37  ? 0.33504 0.31617 0.32463 0.00028  -0.00591 -0.01865 44  PHE A O   
233  C CB  . PHE A 37  ? 0.35220 0.33697 0.32913 0.01293  -0.00543 -0.01066 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.38620 0.35507 0.35674 0.01672  0.00542  -0.01441 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.35834 0.31276 0.31380 0.02016  0.00891  -0.01393 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.36213 0.33076 0.34113 0.01538  0.01129  -0.01746 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.41970 0.36217 0.37192 0.02071  0.01898  -0.01472 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.37628 0.33195 0.35192 0.01496  0.01905  -0.01945 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.37904 0.32277 0.34285 0.01693  0.02338  -0.01718 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.37559 0.33351 0.34424 0.00699  0.00168  -0.02320 45  LEU A N   
241  C CA  . LEU A 38  ? 0.37765 0.33603 0.35455 0.00669  0.00837  -0.02635 45  LEU A CA  
242  C C   . LEU A 38  ? 0.39926 0.35413 0.37574 0.00451  0.00308  -0.02884 45  LEU A C   
243  O O   . LEU A 38  ? 0.36009 0.32218 0.34799 0.00268  0.00357  -0.02934 45  LEU A O   
244  C CB  . LEU A 38  ? 0.37195 0.32340 0.34305 0.01068  0.01835  -0.02677 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.38022 0.33950 0.36544 0.00902  0.02470  -0.02778 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.34204 0.30825 0.33945 0.00426  0.02323  -0.02777 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.44939 0.40856 0.43329 0.01139  0.03537  -0.02508 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.35620 0.29622 0.31597 0.00519  -0.00307 -0.03054 46  ARG A N   
249  C CA  . ARG A 39  ? 0.40482 0.33296 0.35821 0.00293  -0.01054 -0.03271 46  ARG A CA  
250  C C   . ARG A 39  ? 0.35271 0.29247 0.32024 -0.00629 -0.01792 -0.02817 46  ARG A C   
251  O O   . ARG A 39  ? 0.37883 0.31562 0.34972 -0.00755 -0.01947 -0.02822 46  ARG A O   
252  C CB  . ARG A 39  ? 0.41741 0.32218 0.34523 0.00307  -0.01964 -0.03552 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.52707 0.41001 0.44197 -0.00068 -0.03025 -0.03793 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.58866 0.44360 0.47441 -0.00374 -0.04359 -0.04135 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.59299 0.46160 0.48680 -0.01644 -0.05511 -0.03549 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.71913 0.57433 0.59279 -0.01959 -0.06654 -0.03690 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.63631 0.46022 0.47576 -0.00988 -0.06705 -0.04508 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.65589 0.53050 0.54291 -0.03204 -0.07832 -0.02940 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.34874 0.30339 0.32438 -0.01155 -0.02201 -0.02279 47  GLU A N   
260  C CA  . GLU A 40  ? 0.28318 0.25371 0.27298 -0.01973 -0.02736 -0.01594 47  GLU A CA  
261  C C   . GLU A 40  ? 0.33791 0.32157 0.34051 -0.01603 -0.01887 -0.01563 47  GLU A C   
262  O O   . GLU A 40  ? 0.36446 0.35226 0.37261 -0.02042 -0.02136 -0.01209 47  GLU A O   
263  C CB  . GLU A 40  ? 0.29428 0.28470 0.29249 -0.02351 -0.03215 -0.00842 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.34398 0.32199 0.32825 -0.02962 -0.04487 -0.00823 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.55638 0.51047 0.52798 -0.04014 -0.05685 -0.00980 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.49365 0.45332 0.47575 -0.04758 -0.05876 -0.00471 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.53669 0.46313 0.48448 -0.04033 -0.06456 -0.01591 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.31345 0.30180 0.31867 -0.00883 -0.00994 -0.01869 48  LEU A N   
269  C CA  . LEU A 41  ? 0.33432 0.33141 0.34753 -0.00621 -0.00445 -0.01955 48  LEU A CA  
270  C C   . LEU A 41  ? 0.33802 0.32759 0.35126 -0.00589 -0.00388 -0.02347 48  LEU A C   
271  O O   . LEU A 41  ? 0.32526 0.32126 0.34341 -0.00635 -0.00435 -0.02251 48  LEU A O   
272  C CB  . LEU A 41  ? 0.30214 0.29943 0.31446 -0.00056 0.00244  -0.02203 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.27726 0.28324 0.28897 0.00346  0.00273  -0.01730 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.31841 0.31473 0.32360 0.01010  0.00923  -0.02031 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.33912 0.36434 0.35832 0.00458  0.00202  -0.01117 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.30070 0.27859 0.30783 -0.00300 -0.00204 -0.02729 49  ILE A N   
277  C CA  . ILE A 42  ? 0.33758 0.31186 0.34585 0.00033  -0.00120 -0.02953 49  ILE A CA  
278  C C   . ILE A 42  ? 0.36018 0.32532 0.36290 -0.00198 -0.00887 -0.02714 49  ILE A C   
279  O O   . ILE A 42  ? 0.34275 0.30994 0.34924 -0.00007 -0.00994 -0.02632 49  ILE A O   
280  C CB  . ILE A 42  ? 0.32908 0.29564 0.33088 0.00691  0.00456  -0.03250 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.32756 0.30509 0.33868 0.00640  0.01239  -0.03242 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.35331 0.31633 0.35421 0.01411  0.00508  -0.03359 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.32667 0.30200 0.33333 0.01232  0.02093  -0.03229 49  ILE A CD1 
284  N N   . SER A 43  ? 0.33271 0.28634 0.32555 -0.00715 -0.01569 -0.02515 50  SER A N   
285  C CA  . SER A 43  ? 0.37844 0.31962 0.36509 -0.01296 -0.02455 -0.02130 50  SER A CA  
286  C C   . SER A 43  ? 0.37983 0.33906 0.37933 -0.01814 -0.02482 -0.01436 50  SER A C   
287  O O   . SER A 43  ? 0.34716 0.29954 0.34431 -0.01866 -0.02784 -0.01137 50  SER A O   
288  C CB  . SER A 43  ? 0.40954 0.33674 0.38472 -0.02164 -0.03436 -0.01946 50  SER A CB  
289  O OG  . SER A 43  ? 0.52693 0.44143 0.49735 -0.03168 -0.04452 -0.01368 50  SER A OG  
290  N N   . ASN A 44  ? 0.31890 0.29991 0.32921 -0.01981 -0.02098 -0.01135 51  ASN A N   
291  C CA  . ASN A 44  ? 0.35743 0.35628 0.37606 -0.02124 -0.01899 -0.00503 51  ASN A CA  
292  C C   . ASN A 44  ? 0.33822 0.33739 0.35690 -0.01448 -0.01548 -0.00916 51  ASN A C   
293  O O   . ASN A 44  ? 0.31260 0.31505 0.33080 -0.01540 -0.01704 -0.00417 51  ASN A O   
294  C CB  . ASN A 44  ? 0.33691 0.35660 0.36286 -0.01920 -0.01396 -0.00221 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.43900 0.47040 0.47084 -0.02721 -0.01890 0.00704  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.41297 0.43450 0.44258 -0.03747 -0.02768 0.01129  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.42323 0.47546 0.46214 -0.02248 -0.01417 0.01084  51  ASN A ND2 
298  N N   . SER A 45  ? 0.31305 0.31047 0.33274 -0.00860 -0.01139 -0.01696 52  SER A N   
299  C CA  . SER A 45  ? 0.32991 0.33145 0.35251 -0.00421 -0.01046 -0.02017 52  SER A CA  
300  C C   . SER A 45  ? 0.33308 0.32533 0.35261 -0.00162 -0.01466 -0.01852 52  SER A C   
301  O O   . SER A 45  ? 0.32971 0.32648 0.34949 0.00044  -0.01713 -0.01631 52  SER A O   
302  C CB  . SER A 45  ? 0.35405 0.35757 0.38153 -0.00169 -0.00629 -0.02644 52  SER A CB  
303  O OG  . SER A 45  ? 0.37324 0.37990 0.39997 -0.00285 -0.00302 -0.02812 52  SER A OG  
304  N N   . SER A 46  ? 0.30575 0.28220 0.31883 0.00011  -0.01586 -0.01974 53  SER A N   
305  C CA  . SER A 46  ? 0.32230 0.28350 0.32749 0.00565  -0.01974 -0.01847 53  SER A CA  
306  C C   . SER A 46  ? 0.34770 0.30165 0.34696 -0.00036 -0.02597 -0.01061 53  SER A C   
307  O O   . SER A 46  ? 0.36358 0.31310 0.35959 0.00486  -0.02865 -0.00773 53  SER A O   
308  C CB  . SER A 46  ? 0.35955 0.29818 0.35124 0.00962  -0.02025 -0.02210 53  SER A CB  
309  O OG  . SER A 46  ? 0.42710 0.34519 0.40632 0.01826  -0.02366 -0.02163 53  SER A OG  
310  N N   . ASP A 47  ? 0.33769 0.29228 0.33629 -0.01137 -0.02839 -0.00531 54  ASP A N   
311  C CA  . ASP A 47  ? 0.35139 0.30291 0.34673 -0.01932 -0.03323 0.00521  54  ASP A CA  
312  C C   . ASP A 47  ? 0.32485 0.29568 0.32531 -0.01514 -0.02956 0.00848  54  ASP A C   
313  O O   . ASP A 47  ? 0.33022 0.29435 0.32422 -0.01472 -0.03275 0.01529  54  ASP A O   
314  C CB  . ASP A 47  ? 0.34053 0.30092 0.34090 -0.03240 -0.03529 0.01245  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.51767 0.45436 0.50846 -0.04023 -0.04363 0.01117  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.44728 0.35497 0.42263 -0.03431 -0.04727 0.00466  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.43611 0.38410 0.43375 -0.05127 -0.04689 0.01673  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.32132 0.31244 0.32965 -0.01160 -0.02365 0.00356  55  ALA A N   
319  C CA  . ALA A 48  ? 0.29784 0.30342 0.30532 -0.00718 -0.02150 0.00479  55  ALA A CA  
320  C C   . ALA A 48  ? 0.27112 0.27213 0.27624 0.00037  -0.02534 0.00145  55  ALA A C   
321  O O   . ALA A 48  ? 0.31728 0.32186 0.31609 0.00319  -0.02765 0.00609  55  ALA A O   
322  C CB  . ALA A 48  ? 0.27958 0.29883 0.29051 -0.00437 -0.01609 -0.00181 55  ALA A CB  
323  N N   . LEU A 49  ? 0.28879 0.28498 0.29915 0.00480  -0.02570 -0.00553 56  LEU A N   
324  C CA  . LEU A 49  ? 0.29251 0.29003 0.30496 0.01346  -0.02916 -0.00702 56  LEU A CA  
325  C C   . LEU A 49  ? 0.36886 0.34780 0.37023 0.01746  -0.03384 0.00017  56  LEU A C   
326  O O   . LEU A 49  ? 0.35715 0.33924 0.35563 0.02383  -0.03802 0.00379  56  LEU A O   
327  C CB  . LEU A 49  ? 0.28612 0.28725 0.30868 0.01802  -0.02591 -0.01377 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.30960 0.32758 0.34282 0.01351  -0.02301 -0.01957 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.31207 0.33148 0.35365 0.01502  -0.01721 -0.02347 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.26178 0.29593 0.30093 0.01457  -0.02858 -0.02051 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.35283 0.30938 0.34549 0.01352  -0.03462 0.00249  57  ASP A N   
332  C CA  . ASP A 50  ? 0.35023 0.28066 0.32765 0.01459  -0.04041 0.01009  57  ASP A CA  
333  C C   . ASP A 50  ? 0.34006 0.27656 0.31331 0.00977  -0.04251 0.02048  57  ASP A C   
334  O O   . ASP A 50  ? 0.36978 0.29366 0.33273 0.01608  -0.04696 0.02668  57  ASP A O   
335  C CB  . ASP A 50  ? 0.39983 0.30473 0.36702 0.00467  -0.04335 0.01158  57  ASP A CB  
336  C CG  . ASP A 50  ? 0.49791 0.38395 0.45765 0.01336  -0.04290 0.00259  57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.42760 0.32076 0.39113 0.02869  -0.03917 -0.00261 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.49648 0.36225 0.44624 0.00483  -0.04649 0.00151  57  ASP A OD2 
339  N N   . LYS A 51  ? 0.34679 0.30225 0.32601 0.00038  -0.03857 0.02339  58  LYS A N   
340  C CA  . LYS A 51  ? 0.34295 0.30530 0.31598 -0.00395 -0.03827 0.03517  58  LYS A CA  
341  C C   . LYS A 51  ? 0.36408 0.33775 0.33284 0.00697  -0.03955 0.03399  58  LYS A C   
342  O O   . LYS A 51  ? 0.36501 0.33115 0.32198 0.00920  -0.04270 0.04377  58  LYS A O   
343  C CB  . LYS A 51  ? 0.41611 0.39996 0.39657 -0.01261 -0.03175 0.03866  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.64712 0.62329 0.63182 -0.02684 -0.03330 0.04576  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.83481 0.83959 0.83092 -0.03332 -0.02635 0.05137  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.68449 0.68684 0.68981 -0.04482 -0.02971 0.05183  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.78981 0.82427 0.80842 -0.04616 -0.02251 0.05577  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.34628 0.33695 0.32317 0.01266  -0.03839 0.02290  59  ILE A N   
349  C CA  . ILE A 52  ? 0.34540 0.34679 0.31755 0.02106  -0.04289 0.02138  59  ILE A CA  
350  C C   . ILE A 52  ? 0.38857 0.38118 0.36084 0.03089  -0.04967 0.02261  59  ILE A C   
351  O O   . ILE A 52  ? 0.41790 0.41248 0.38105 0.03774  -0.05533 0.02785  59  ILE A O   
352  C CB  . ILE A 52  ? 0.32633 0.34508 0.30558 0.02152  -0.04246 0.00971  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.36447 0.39280 0.33431 0.02737  -0.04987 0.00835  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.28618 0.30787 0.28242 0.02188  -0.04241 0.00089  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.38518 0.41161 0.33436 0.02900  -0.04839 0.01732  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.36038 0.34346 0.34078 0.03413  -0.04897 0.01834  60  ARG A N   
357  C CA  . ARG A 53  ? 0.39320 0.36671 0.37139 0.04760  -0.05377 0.02074  60  ARG A CA  
358  C C   . ARG A 53  ? 0.40127 0.34889 0.35936 0.04960  -0.05781 0.03271  60  ARG A C   
359  O O   . ARG A 53  ? 0.42958 0.37643 0.38133 0.06132  -0.06356 0.03794  60  ARG A O   
360  C CB  . ARG A 53  ? 0.40291 0.36590 0.38692 0.05306  -0.05013 0.01476  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.50261 0.46630 0.48846 0.07235  -0.05308 0.01599  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.62608 0.57372 0.60989 0.08206  -0.04797 0.01129  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.88093 0.79508 0.84795 0.07174  -0.04658 0.01004  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.82157 0.71764 0.78147 0.07639  -0.04260 0.00406  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.71932 0.62975 0.68827 0.09237  -0.03678 -0.00044 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.59672 0.46144 0.53982 0.06452  -0.04476 0.00341  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.38681 0.31312 0.33512 0.03755  -0.05578 0.03845  61  TYR A N   
368  C CA  . TYR A 54  ? 0.40255 0.30058 0.33123 0.03575  -0.06008 0.05190  61  TYR A CA  
369  C C   . TYR A 54  ? 0.43993 0.35313 0.36171 0.03595  -0.06094 0.06126  61  TYR A C   
370  O O   . TYR A 54  ? 0.44390 0.34412 0.35164 0.04531  -0.06632 0.06970  61  TYR A O   
371  C CB  . TYR A 54  ? 0.43195 0.30924 0.35561 0.01802  -0.05910 0.05733  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.48041 0.33023 0.38591 0.00959  -0.06350 0.07380  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.50202 0.30833 0.38735 0.01597  -0.07083 0.07775  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.51260 0.37960 0.41928 -0.00344 -0.05967 0.08666  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.50695 0.28350 0.37352 0.00621  -0.07576 0.09470  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.57972 0.42443 0.47109 -0.01296 -0.06285 0.10468  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.62324 0.42077 0.49462 -0.00984 -0.07167 0.10886  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.64600 0.41690 0.50049 -0.02148 -0.07562 0.12827  61  TYR A OH  
379  N N   . GLU A 55  ? 0.42127 0.36084 0.34974 0.02808  -0.05553 0.05969  62  GLU A N   
380  C CA  . GLU A 55  ? 0.41578 0.36761 0.33189 0.02966  -0.05520 0.06851  62  GLU A CA  
381  C C   . GLU A 55  ? 0.47142 0.43259 0.38348 0.04477  -0.06291 0.06453  62  GLU A C   
382  O O   . GLU A 55  ? 0.47870 0.43641 0.37355 0.05051  -0.06669 0.07473  62  GLU A O   
383  C CB  . GLU A 55  ? 0.47159 0.44810 0.39246 0.02261  -0.04705 0.06538  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.53955 0.51430 0.46391 0.00774  -0.03971 0.07596  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.74018 0.74158 0.66429 0.00566  -0.02993 0.07847  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.60739 0.62175 0.52236 0.01588  -0.02930 0.07114  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.73403 0.74318 0.66621 -0.00562 -0.02349 0.08787  62  GLU A OE2 
388  N N   . SER A 56  ? 0.45388 0.42830 0.38218 0.05094  -0.06596 0.05141  63  SER A N   
389  C CA  . SER A 56  ? 0.48030 0.47079 0.40987 0.06311  -0.07515 0.04848  63  SER A CA  
390  C C   . SER A 56  ? 0.51912 0.49348 0.44123 0.07697  -0.08161 0.05727  63  SER A C   
391  O O   . SER A 56  ? 0.56752 0.55504 0.48722 0.08820  -0.09058 0.05930  63  SER A O   
392  C CB  . SER A 56  ? 0.46213 0.47501 0.41523 0.06340  -0.07653 0.03472  63  SER A CB  
393  O OG  . SER A 56  ? 0.56796 0.57172 0.53346 0.06777  -0.07328 0.03268  63  SER A OG  
394  N N   . LEU A 57  ? 0.49544 0.43917 0.41127 0.07711  -0.07856 0.06269  64  LEU A N   
395  C CA  . LEU A 57  ? 0.53371 0.45379 0.43602 0.09256  -0.08460 0.07164  64  LEU A CA  
396  C C   . LEU A 57  ? 0.66128 0.57123 0.54031 0.09380  -0.08888 0.08625  64  LEU A C   
397  O O   . LEU A 57  ? 0.69271 0.59733 0.56173 0.11015  -0.09657 0.09310  64  LEU A O   
398  C CB  . LEU A 57  ? 0.61335 0.49342 0.50673 0.09077  -0.08159 0.07326  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.58504 0.47133 0.49584 0.09494  -0.07740 0.05983  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.73217 0.57189 0.62584 0.09391  -0.07650 0.06073  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.70045 0.61206 0.62585 0.11571  -0.08041 0.05564  64  LEU A CD2 
402  N N   . THR A 58  ? 0.57907 0.48675 0.44847 0.07808  -0.08332 0.09296  65  THR A N   
403  C CA  . THR A 58  ? 0.64015 0.53988 0.48576 0.07946  -0.08548 0.10870  65  THR A CA  
404  C C   . THR A 58  ? 0.64966 0.58159 0.49121 0.08108  -0.08643 0.10574  65  THR A C   
405  O O   . THR A 58  ? 0.63503 0.56376 0.45423 0.08643  -0.08938 0.11770  65  THR A O   
406  C CB  . THR A 58  ? 0.70094 0.57654 0.53462 0.06235  -0.07859 0.12322  65  THR A CB  
407  O OG1 . THR A 58  ? 0.75301 0.65236 0.59892 0.04751  -0.06919 0.11895  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.66736 0.50491 0.50038 0.05844  -0.08038 0.12430  65  THR A CG2 
409  N N   . ASP A 59  ? 0.59227 0.55109 0.45083 0.07720  -0.08473 0.09020  66  ASP A N   
410  C CA  . ASP A 59  ? 0.58183 0.56466 0.43172 0.07981  -0.08839 0.08445  66  ASP A CA  
411  C C   . ASP A 59  ? 0.52951 0.53446 0.40238 0.08073  -0.09436 0.06681  66  ASP A C   
412  O O   . ASP A 59  ? 0.49949 0.51325 0.38404 0.07116  -0.08813 0.05602  66  ASP A O   
413  C CB  . ASP A 59  ? 0.58570 0.57303 0.42338 0.06990  -0.07686 0.08754  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.65950 0.66413 0.48024 0.07492  -0.08060 0.07966  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.76752 0.78131 0.58808 0.08249  -0.09425 0.07144  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.73393 0.74259 0.53959 0.07194  -0.07036 0.08271  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.65656 0.67257 0.53807 0.09191  -0.10650 0.06479  67  PRO A N   
418  C CA  . PRO A 60  ? 0.51487 0.55588 0.42299 0.09052  -0.11234 0.05100  67  PRO A CA  
419  C C   . PRO A 60  ? 0.57668 0.63173 0.48021 0.08088  -0.11532 0.03940  67  PRO A C   
420  O O   . PRO A 60  ? 0.54838 0.61723 0.47282 0.07338  -0.11614 0.02789  67  PRO A O   
421  C CB  . PRO A 60  ? 0.59548 0.65146 0.50948 0.10542  -0.12653 0.05569  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.71183 0.74182 0.60632 0.11696  -0.12510 0.07087  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.66209 0.66484 0.53565 0.10625  -0.11278 0.07723  67  PRO A CD  
424  N N   . SER A 61  ? 0.55570 0.60459 0.42909 0.08166  -0.11669 0.04251  68  SER A N   
425  C CA  . SER A 61  ? 0.56773 0.62256 0.42811 0.07565  -0.12051 0.03047  68  SER A CA  
426  C C   . SER A 61  ? 0.58930 0.63899 0.45753 0.06533  -0.10685 0.02201  68  SER A C   
427  O O   . SER A 61  ? 0.48601 0.53824 0.35025 0.05989  -0.11073 0.00922  68  SER A O   
428  C CB  . SER A 61  ? 0.60766 0.65419 0.42798 0.08295  -0.12320 0.03706  68  SER A CB  
429  O OG  . SER A 61  ? 0.66371 0.69807 0.46688 0.08132  -0.10612 0.04336  68  SER A OG  
430  N N   . LYS A 62  ? 0.47621 0.51715 0.35553 0.06218  -0.09273 0.02867  69  LYS A N   
431  C CA  . LYS A 62  ? 0.48811 0.52724 0.37839 0.05330  -0.08106 0.02163  69  LYS A CA  
432  C C   . LYS A 62  ? 0.44999 0.49845 0.36526 0.04730  -0.08550 0.00866  69  LYS A C   
433  O O   . LYS A 62  ? 0.44291 0.48925 0.36251 0.04079  -0.07843 0.00093  69  LYS A O   
434  C CB  . LYS A 62  ? 0.44992 0.47889 0.34865 0.04968  -0.06905 0.03225  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.54143 0.56377 0.41680 0.05179  -0.06283 0.04696  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.55378 0.57062 0.43611 0.04310  -0.05041 0.05662  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.56033 0.57507 0.42126 0.04388  -0.04414 0.07469  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.65559 0.66953 0.52844 0.03179  -0.03359 0.08573  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.44008 0.50071 0.37259 0.04991  -0.09641 0.00768  70  LEU A N   
440  C CA  . LEU A 63  ? 0.41475 0.48933 0.37280 0.04304  -0.10046 -0.00198 70  LEU A CA  
441  C C   . LEU A 63  ? 0.46979 0.55375 0.42137 0.03773  -0.11556 -0.01090 70  LEU A C   
442  O O   . LEU A 63  ? 0.41883 0.51758 0.39325 0.02976  -0.12199 -0.01665 70  LEU A O   
443  C CB  . LEU A 63  ? 0.40821 0.49586 0.39217 0.04942  -0.10228 0.00347  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.40121 0.47338 0.39072 0.05264  -0.08881 0.00863  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.51955 0.60154 0.52933 0.06316  -0.08989 0.01264  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.39249 0.45727 0.38728 0.04206  -0.07775 0.00148  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.45846 0.53340 0.37790 0.04143  -0.12208 -0.01142 71  ASP A N   
448  C CA  . ASP A 64  ? 0.49960 0.57625 0.40559 0.03558  -0.13893 -0.02156 71  ASP A CA  
449  C C   . ASP A 64  ? 0.51294 0.57840 0.41959 0.02386  -0.13616 -0.03419 71  ASP A C   
450  O O   . ASP A 64  ? 0.49808 0.56657 0.40801 0.01324  -0.15124 -0.04279 71  ASP A O   
451  C CB  . ASP A 64  ? 0.48068 0.54352 0.34359 0.04425  -0.14397 -0.02051 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.67588 0.75002 0.53585 0.05460  -0.15302 -0.00871 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.62292 0.71727 0.51468 0.05545  -0.15854 -0.00326 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.82161 0.88457 0.64627 0.06367  -0.15369 -0.00397 71  ASP A OD2 
455  N N   . SER A 65  ? 0.51831 0.57076 0.42274 0.02481  -0.11820 -0.03441 72  SER A N   
456  C CA  . SER A 65  ? 0.47941 0.51845 0.38315 0.01669  -0.11299 -0.04464 72  SER A CA  
457  C C   . SER A 65  ? 0.51990 0.57184 0.46213 0.00670  -0.11016 -0.04485 72  SER A C   
458  O O   . SER A 65  ? 0.49266 0.53314 0.43704 0.00067  -0.10311 -0.05079 72  SER A O   
459  C CB  . SER A 65  ? 0.47921 0.50395 0.36504 0.02450  -0.09472 -0.04241 72  SER A CB  
460  O OG  . SER A 65  ? 0.50308 0.53753 0.40590 0.02850  -0.08269 -0.02999 72  SER A OG  
461  N N   . GLY A 66  ? 0.49749 0.57274 0.46824 0.00720  -0.11397 -0.03746 73  GLY A N   
462  C CA  . GLY A 66  ? 0.40990 0.50078 0.41534 -0.00008 -0.11054 -0.03654 73  GLY A CA  
463  C C   . GLY A 66  ? 0.47124 0.57702 0.49740 0.01007  -0.10303 -0.02629 73  GLY A C   
464  O O   . GLY A 66  ? 0.42999 0.52212 0.44703 0.01754  -0.09124 -0.02213 73  GLY A O   
465  N N   . LYS A 67  ? 0.40741 0.54068 0.46047 0.01086  -0.11023 -0.02158 74  LYS A N   
466  C CA  . LYS A 67  ? 0.44280 0.58661 0.51031 0.02486  -0.10360 -0.01231 74  LYS A CA  
467  C C   . LYS A 67  ? 0.43483 0.57944 0.52069 0.02515  -0.08892 -0.01189 74  LYS A C   
468  O O   . LYS A 67  ? 0.39087 0.52755 0.47574 0.03741  -0.08015 -0.00692 74  LYS A O   
469  C CB  . LYS A 67  ? 0.57071 0.74733 0.65812 0.03047  -0.11703 -0.00583 74  LYS A CB  
470  C CG  . LYS A 67  ? 0.61650 0.78878 0.68291 0.04192  -0.12712 -0.00056 74  LYS A CG  
471  C CD  . LYS A 67  ? 0.94202 1.14511 1.03028 0.05604  -0.13460 0.00956  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.90902 1.09414 0.98593 0.07617  -0.12507 0.01790  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.88947 1.05035 0.93226 0.08184  -0.13022 0.02161  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.39942 0.54886 0.49773 0.01215  -0.08640 -0.01696 75  GLU A N   
475  C CA  . GLU A 68  ? 0.39124 0.54412 0.50601 0.01353  -0.07270 -0.01546 75  GLU A CA  
476  C C   . GLU A 68  ? 0.32391 0.44543 0.41846 0.01498  -0.06071 -0.01890 75  GLU A C   
477  O O   . GLU A 68  ? 0.38654 0.48936 0.46263 0.00785  -0.06111 -0.02424 75  GLU A O   
478  C CB  . GLU A 68  ? 0.43473 0.60467 0.57049 -0.00184 -0.07418 -0.01719 75  GLU A CB  
479  C CG  . GLU A 68  ? 0.47260 0.67875 0.63287 -0.00690 -0.08808 -0.01211 75  GLU A CG  
480  C CD  . GLU A 68  ? 0.86721 1.06507 1.01440 -0.02294 -0.10526 -0.01886 75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.85874 1.03121 0.97487 -0.01883 -0.10972 -0.02433 75  GLU A OE1 
482  O OE2 . GLU A 68  ? 1.19672 1.41175 1.36260 -0.03993 -0.11438 -0.01831 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.32671 0.44285 0.42381 0.02521  -0.05050 -0.01555 76  LEU A N   
484  C CA  . LEU A 69  ? 0.27650 0.36513 0.35656 0.02585  -0.04135 -0.01754 76  LEU A CA  
485  C C   . LEU A 69  ? 0.29738 0.38854 0.38832 0.02411  -0.03131 -0.01919 76  LEU A C   
486  O O   . LEU A 69  ? 0.27312 0.37201 0.37276 0.03487  -0.02579 -0.01583 76  LEU A O   
487  C CB  . LEU A 69  ? 0.31931 0.39152 0.38617 0.03833  -0.04062 -0.01253 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.31984 0.38793 0.37364 0.04134  -0.04947 -0.00830 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.38745 0.43067 0.42523 0.05079  -0.04778 -0.00255 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.34279 0.40441 0.38323 0.03052  -0.05143 -0.01130 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.27695 0.38249 0.33764 0.03396  -0.01280 0.03271  77  HIS A N   
492  C CA  . HIS A 70  ? 0.25958 0.35746 0.32120 0.02978  -0.00668 0.02981  77  HIS A CA  
493  C C   . HIS A 70  ? 0.28548 0.35584 0.32856 0.01850  -0.01223 0.01457  77  HIS A C   
494  O O   . HIS A 70  ? 0.27503 0.33657 0.30872 0.01259  -0.02114 0.00654  77  HIS A O   
495  C CB  . HIS A 70  ? 0.27973 0.41278 0.36631 0.02270  -0.01018 0.03903  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.31609 0.46378 0.40783 0.00524  -0.02805 0.03341  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.36819 0.55304 0.47919 0.00206  -0.03958 0.04070  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.37343 0.50184 0.45138 -0.00915 -0.03658 0.02053  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.38928 0.57451 0.49612 -0.01523 -0.05491 0.03066  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.34939 0.49903 0.43605 -0.02152 -0.05205 0.01884  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.27919 0.33735 0.31662 0.01759  -0.00570 0.01224  78  ILE A N   
502  C CA  . ILE A 71  ? 0.30757 0.34173 0.32743 0.01011  -0.00981 0.00046  78  ILE A CA  
503  C C   . ILE A 71  ? 0.32253 0.36367 0.34867 0.00240  -0.00806 0.00478  78  ILE A C   
504  O O   . ILE A 71  ? 0.32928 0.37937 0.36352 0.00842  0.00354  0.01447  78  ILE A O   
505  C CB  . ILE A 71  ? 0.28626 0.29178 0.28576 0.01939  -0.00274 -0.00724 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.33606 0.33189 0.33288 0.02446  -0.00254 -0.01127 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.34561 0.33215 0.32818 0.01368  -0.00874 -0.01756 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.37098 0.33963 0.35111 0.03207  0.00438  -0.01937 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.29454 0.32931 0.31666 -0.01014 -0.01729 -0.00154 79  ASN A N   
510  C CA  . ASN A 72  ? 0.30366 0.33788 0.33003 -0.01878 -0.01406 0.00239  79  ASN A CA  
511  C C   . ASN A 72  ? 0.34178 0.34502 0.34308 -0.01758 -0.01387 -0.00558 79  ASN A C   
512  O O   . ASN A 72  ? 0.35073 0.34040 0.33950 -0.01837 -0.02261 -0.01567 79  ASN A O   
513  C CB  . ASN A 72  ? 0.30565 0.35630 0.34900 -0.03559 -0.02444 0.00250  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.27770 0.36563 0.34824 -0.03697 -0.02750 0.01146  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.29285 0.39717 0.37613 -0.02622 -0.01704 0.02224  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.29697 0.39898 0.37562 -0.04936 -0.04194 0.00731  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.30596 0.29975 0.30026 -0.01415 -0.00302 0.00051  80  LEU A N   
518  C CA  . LEU A 73  ? 0.34196 0.30815 0.31124 -0.01101 -0.00241 -0.00401 80  LEU A CA  
519  C C   . LEU A 73  ? 0.36958 0.33165 0.34593 -0.02305 0.00110  0.00229  80  LEU A C   
520  O O   . LEU A 73  ? 0.34421 0.31840 0.33644 -0.02657 0.01221  0.01398  80  LEU A O   
521  C CB  . LEU A 73  ? 0.32959 0.28301 0.27790 0.00455  0.00819  -0.00161 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.36175 0.31546 0.30387 0.01483  0.00689  -0.00819 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.41245 0.34908 0.32800 0.02988  0.01716  -0.00776 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.36620 0.31268 0.30279 0.01275  -0.00748 -0.02171 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.36498 0.30949 0.33139 -0.02945 -0.00691 -0.00490 81  ILE A N   
526  C CA  . ILE A 74  ? 0.36114 0.29629 0.33433 -0.04364 -0.00453 -0.00126 81  ILE A CA  
527  C C   . ILE A 74  ? 0.42649 0.32833 0.37297 -0.03717 -0.00111 -0.00198 81  ILE A C   
528  O O   . ILE A 74  ? 0.47518 0.36206 0.40912 -0.03619 -0.00999 -0.01129 81  ILE A O   
529  C CB  . ILE A 74  ? 0.38025 0.32339 0.36655 -0.05888 -0.01752 -0.00968 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.36343 0.34110 0.37220 -0.06091 -0.02277 -0.00824 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.39905 0.33103 0.39472 -0.07690 -0.01473 -0.00708 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.45859 0.44704 0.47644 -0.07472 -0.03759 -0.01668 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.43160 0.32141 0.36725 -0.03002 0.01262  0.00884  82  PRO A N   
534  C CA  . PRO A 75  ? 0.47477 0.33235 0.38408 -0.02244 0.01696  0.01117  82  PRO A CA  
535  C C   . PRO A 75  ? 0.54180 0.38176 0.46011 -0.03911 0.02140  0.01428  82  PRO A C   
536  O O   . PRO A 75  ? 0.53502 0.38797 0.48019 -0.05650 0.02610  0.01925  82  PRO A O   
537  C CB  . PRO A 75  ? 0.55772 0.41027 0.45123 -0.00838 0.03201  0.02354  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.50598 0.38447 0.42918 -0.01807 0.04135  0.03191  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.44068 0.34563 0.38689 -0.02676 0.02691  0.02137  82  PRO A CD  
540  N N   . ASN A 76  ? 0.58159 0.39131 0.47791 -0.03358 0.01991  0.01126  83  ASN A N   
541  C CA  . ASN A 76  ? 0.59563 0.37801 0.49399 -0.04792 0.02537  0.01275  83  ASN A CA  
542  C C   . ASN A 76  ? 0.64550 0.39156 0.51278 -0.03149 0.03538  0.02108  83  ASN A C   
543  O O   . ASN A 76  ? 0.64731 0.38011 0.49472 -0.01797 0.02770  0.01453  83  ASN A O   
544  C CB  . ASN A 76  ? 0.60137 0.38126 0.50438 -0.05882 0.01116  -0.00284 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.69754 0.44821 0.60403 -0.07787 0.01582  -0.00441 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.70500 0.42120 0.59751 -0.07539 0.02933  0.00449  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.71608 0.47799 0.63899 -0.09685 0.00444  -0.01618 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.62843 0.35916 0.49272 -0.03189 0.05361  0.03701  84  LYS A N   
549  C CA  . LYS A 77  ? 0.66640 0.36211 0.49783 -0.01326 0.06470  0.04799  84  LYS A CA  
550  C C   . LYS A 77  ? 0.75904 0.41618 0.58092 -0.01800 0.06608  0.04465  84  LYS A C   
551  O O   . LYS A 77  ? 0.80673 0.43888 0.59910 0.00284  0.06825  0.04908  84  LYS A O   
552  C CB  . LYS A 77  ? 0.67096 0.35779 0.50007 -0.01178 0.08709  0.06800  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.80173 0.51234 0.61829 0.00674  0.08908  0.07353  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.90733 0.61354 0.72603 0.00666  0.11408  0.09398  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.93665 0.66522 0.74097 0.02488  0.11632  0.09689  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.96625 0.69367 0.77390 0.02628  0.14319  0.11759  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.82703 0.47807 0.67166 -0.04393 0.06456  0.03672  85  GLN A N   
558  C CA  . GLN A 78  ? 0.85061 0.45836 0.68265 -0.04912 0.06717  0.03158  85  GLN A CA  
559  C C   . GLN A 78  ? 0.86409 0.47079 0.67898 -0.03360 0.05221  0.01787  85  GLN A C   
560  O O   . GLN A 78  ? 0.83878 0.41146 0.62827 -0.01713 0.05745  0.02080  85  GLN A O   
561  C CB  . GLN A 78  ? 0.92969 0.53165 0.78871 -0.08270 0.06648  0.02317  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.16945 0.74617 1.04086 -0.10020 0.08706  0.03751  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.38885 1.00188 1.28505 -0.10414 0.09614  0.05211  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.53630 1.19306 1.46367 -0.11838 0.08543  0.04602  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.27748 0.87143 1.15888 -0.09020 0.11757  0.07277  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.72782 0.37159 0.55743 -0.03758 0.03519  0.00434  86  ASP A N   
567  C CA  . ASP A 79  ? 0.77766 0.42603 0.59555 -0.02286 0.02282  -0.00706 86  ASP A CA  
568  C C   . ASP A 79  ? 0.73513 0.40441 0.54193 0.00275  0.01801  -0.00203 86  ASP A C   
569  O O   . ASP A 79  ? 0.63879 0.31395 0.43879 0.01683  0.00918  -0.00895 86  ASP A O   
570  C CB  . ASP A 79  ? 0.77264 0.44966 0.60940 -0.03738 0.00814  -0.02252 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.96054 0.62121 0.80689 -0.06353 0.00787  -0.03088 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.98002 0.66759 0.84244 -0.07688 -0.00414 -0.04113 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.99612 0.61619 0.83287 -0.07059 0.01917  -0.02745 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.67030 0.35148 0.47551 0.00860  0.02360  0.00929  87  ARG A N   
575  C CA  . ARG A 80  ? 0.61888 0.32101 0.41212 0.03022  0.01659  0.01148  87  ARG A CA  
576  C C   . ARG A 80  ? 0.56912 0.30707 0.37877 0.02833  0.00007  -0.00265 87  ARG A C   
577  O O   . ARG A 80  ? 0.58431 0.33364 0.38798 0.04350  -0.01005 -0.00750 87  ARG A O   
578  C CB  . ARG A 80  ? 0.67270 0.35381 0.43914 0.05463  0.01758  0.01774  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.72060 0.41665 0.46974 0.07419  0.01428  0.02463  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.83773 0.53682 0.57137 0.09771  0.00397  0.02397  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.78988 0.45208 0.49925 0.11268  0.01649  0.03820  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.98019 0.63297 0.67983 0.13091  0.01302  0.03978  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.82333 0.50414 0.53791 0.13596  -0.00271 0.02811  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.96678 0.58117 0.64237 0.14544  0.02733  0.05488  87  ARG A NH2 
585  N N   . THR A 81  ? 0.54293 0.30015 0.37518 0.00986  -0.00213 -0.00800 88  THR A N   
586  C CA  . THR A 81  ? 0.53415 0.32207 0.38154 0.00779  -0.01495 -0.01925 88  THR A CA  
587  C C   . THR A 81  ? 0.50911 0.32158 0.36949 0.00249  -0.01388 -0.01679 88  THR A C   
588  O O   . THR A 81  ? 0.50654 0.31739 0.37372 -0.00639 -0.00375 -0.00822 88  THR A O   
589  C CB  . THR A 81  ? 0.57401 0.36294 0.43422 -0.00635 -0.02039 -0.02955 88  THR A CB  
590  O OG1 . THR A 81  ? 0.58254 0.36838 0.45556 -0.02634 -0.01561 -0.02773 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.60131 0.36478 0.44668 0.00165  -0.02017 -0.03330 88  THR A CG2 
592  N N   . LEU A 82  ? 0.43965 0.27415 0.30436 0.00877  -0.02299 -0.02370 89  LEU A N   
593  C CA  . LEU A 82  ? 0.43670 0.29327 0.31431 0.00477  -0.02239 -0.02358 89  LEU A CA  
594  C C   . LEU A 82  ? 0.48484 0.36006 0.38036 -0.00237 -0.03149 -0.03306 89  LEU A C   
595  O O   . LEU A 82  ? 0.46812 0.34638 0.36182 0.00383  -0.03948 -0.04062 89  LEU A O   
596  C CB  . LEU A 82  ? 0.43235 0.29180 0.29365 0.01985  -0.02294 -0.02312 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.46683 0.34443 0.33811 0.01849  -0.02145 -0.02475 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.49006 0.37144 0.37158 0.01159  -0.00787 -0.01339 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.47554 0.35003 0.32441 0.03355  -0.02453 -0.02883 89  LEU A CD2 
600  N N   . THR A 83  ? 0.42762 0.31672 0.34138 -0.01479 -0.02983 -0.03137 90  THR A N   
601  C CA  . THR A 83  ? 0.40538 0.31080 0.33291 -0.02054 -0.03733 -0.03809 90  THR A CA  
602  C C   . THR A 83  ? 0.39080 0.31682 0.32994 -0.01815 -0.03566 -0.03565 90  THR A C   
603  O O   . THR A 83  ? 0.44012 0.37422 0.38692 -0.02016 -0.02826 -0.02745 90  THR A O   
604  C CB  . THR A 83  ? 0.41401 0.32007 0.35098 -0.03561 -0.03945 -0.03894 90  THR A CB  
605  O OG1 . THR A 83  ? 0.48862 0.36906 0.41160 -0.03721 -0.03966 -0.04265 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.45444 0.37751 0.40002 -0.03821 -0.04715 -0.04474 90  THR A CG2 
607  N N   . ILE A 84  ? 0.37258 0.30626 0.31438 -0.01358 -0.04069 -0.04175 91  ILE A N   
608  C CA  . ILE A 84  ? 0.34120 0.28940 0.29274 -0.01053 -0.03820 -0.03998 91  ILE A CA  
609  C C   . ILE A 84  ? 0.39936 0.36139 0.36351 -0.01622 -0.04244 -0.04071 91  ILE A C   
610  O O   . ILE A 84  ? 0.38238 0.34089 0.34385 -0.01577 -0.04714 -0.04681 91  ILE A O   
611  C CB  . ILE A 84  ? 0.38376 0.32584 0.32724 -0.00124 -0.03938 -0.04627 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.47302 0.40182 0.39797 0.00652  -0.03690 -0.04600 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.41431 0.36523 0.36684 0.00154  -0.03488 -0.04473 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.50518 0.42273 0.41747 0.01010  -0.04343 -0.05021 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.32073 0.30001 0.29830 -0.02046 -0.04055 -0.03355 92  VAL A N   
616  C CA  . VAL A 85  ? 0.30393 0.29828 0.28999 -0.02475 -0.04626 -0.03312 92  VAL A CA  
617  C C   . VAL A 85  ? 0.39413 0.40314 0.39009 -0.01664 -0.04145 -0.02658 92  VAL A C   
618  O O   . VAL A 85  ? 0.36062 0.37783 0.36464 -0.01272 -0.03433 -0.01913 92  VAL A O   
619  C CB  . VAL A 85  ? 0.35139 0.35820 0.34689 -0.03699 -0.05127 -0.03015 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.35311 0.37768 0.35289 -0.03928 -0.05966 -0.03025 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.51866 0.50541 0.50393 -0.04577 -0.05349 -0.03579 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.33089 0.34226 0.32583 -0.01287 -0.04329 -0.02779 93  ASP A N   
623  C CA  . ASP A 86  ? 0.29707 0.32000 0.30050 -0.00422 -0.03759 -0.01964 93  ASP A CA  
624  C C   . ASP A 86  ? 0.31616 0.35416 0.32079 -0.00468 -0.04384 -0.01610 93  ASP A C   
625  O O   . ASP A 86  ? 0.32408 0.35715 0.31882 -0.01041 -0.05100 -0.02262 93  ASP A O   
626  C CB  . ASP A 86  ? 0.31800 0.32291 0.31643 0.00347  -0.03002 -0.02325 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.37918 0.37435 0.37261 0.00219  -0.03230 -0.02955 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.40903 0.41185 0.40289 0.00419  -0.03259 -0.02498 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.36211 0.34395 0.35093 -0.00018 -0.03400 -0.03836 93  ASP A OD2 
630  N N   . THR A 87  ? 0.27281 0.32893 0.28717 0.00309  -0.04088 -0.00521 94  THR A N   
631  C CA  . THR A 87  ? 0.28700 0.35800 0.29877 0.00677  -0.04646 0.00014  94  THR A CA  
632  C C   . THR A 87  ? 0.28198 0.34044 0.28815 0.01891  -0.03608 0.00488  94  THR A C   
633  O O   . THR A 87  ? 0.31051 0.38212 0.31833 0.02926  -0.03393 0.01625  94  THR A O   
634  C CB  . THR A 87  ? 0.32366 0.42816 0.35154 0.00814  -0.05199 0.01101  94  THR A CB  
635  O OG1 . THR A 87  ? 0.29143 0.40031 0.33335 0.01720  -0.04009 0.02000  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.32853 0.44516 0.36268 -0.00820 -0.06424 0.00501  94  THR A CG2 
637  N N   . GLY A 88  ? 0.29891 0.33228 0.29954 0.01779  -0.02943 -0.00303 95  GLY A N   
638  C CA  . GLY A 88  ? 0.32433 0.34292 0.32378 0.02607  -0.01796 0.00082  95  GLY A CA  
639  C C   . GLY A 88  ? 0.30613 0.32467 0.29554 0.02810  -0.01853 0.00296  95  GLY A C   
640  O O   . GLY A 88  ? 0.32411 0.35611 0.30442 0.02582  -0.02870 0.00259  95  GLY A O   
641  N N   . ILE A 89  ? 0.32634 0.32737 0.31651 0.03138  -0.00704 0.00402  96  ILE A N   
642  C CA  . ILE A 89  ? 0.32947 0.32877 0.30955 0.03613  -0.00265 0.00927  96  ILE A CA  
643  C C   . ILE A 89  ? 0.34634 0.34499 0.31670 0.02929  -0.00961 -0.00057 96  ILE A C   
644  O O   . ILE A 89  ? 0.36446 0.36504 0.31956 0.03464  -0.00844 0.00351  96  ILE A O   
645  C CB  . ILE A 89  ? 0.33113 0.31065 0.31959 0.03979  0.01443  0.01417  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.37333 0.35155 0.35026 0.04926  0.02379  0.02603  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.33396 0.29981 0.33549 0.02823  0.01569  0.00069  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.51824 0.47650 0.50407 0.05466  0.04356  0.03606  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.35729 0.35156 0.33271 0.01977  -0.01584 -0.01276 97  GLY A N   
650  C CA  . GLY A 90  ? 0.37683 0.36771 0.34214 0.01598  -0.02035 -0.02098 97  GLY A CA  
651  C C   . GLY A 90  ? 0.36771 0.34900 0.34019 0.01773  -0.00890 -0.02138 97  GLY A C   
652  O O   . GLY A 90  ? 0.39533 0.37154 0.38164 0.01940  0.00198  -0.01604 97  GLY A O   
653  N N   . MET A 91  ? 0.32994 0.30822 0.29413 0.01728  -0.01026 -0.02741 98  MET A N   
654  C CA  . MET A 91  ? 0.37835 0.35273 0.35477 0.01865  0.00035  -0.02788 98  MET A CA  
655  C C   . MET A 91  ? 0.34081 0.31235 0.29671 0.02633  0.00575  -0.02591 98  MET A C   
656  O O   . MET A 91  ? 0.36251 0.33054 0.29562 0.02676  -0.00327 -0.03210 98  MET A O   
657  C CB  . MET A 91  ? 0.34674 0.32092 0.33631 0.01248  -0.00657 -0.03818 98  MET A CB  
658  C CG  . MET A 91  ? 0.35729 0.33159 0.36342 0.00643  -0.01024 -0.04090 98  MET A CG  
659  S SD  . MET A 91  ? 0.41400 0.39073 0.43675 0.00200  -0.01675 -0.05132 98  MET A SD  
660  C CE  . MET A 91  ? 0.37766 0.34981 0.37783 0.00172  -0.02868 -0.05540 98  MET A CE  
661  N N   . THR A 92  ? 0.33779 0.30842 0.30055 0.03222  0.02169  -0.01748 99  THR A N   
662  C CA  . THR A 92  ? 0.39274 0.35886 0.33325 0.04206  0.03013  -0.01480 99  THR A CA  
663  C C   . THR A 92  ? 0.41914 0.38438 0.36763 0.04246  0.03230  -0.02242 99  THR A C   
664  O O   . THR A 92  ? 0.38999 0.36132 0.36521 0.03563  0.02835  -0.02765 99  THR A O   
665  C CB  . THR A 92  ? 0.45567 0.42079 0.40071 0.04989  0.05001  -0.00032 99  THR A CB  
666  O OG1 . THR A 92  ? 0.41195 0.38169 0.39611 0.04351  0.06038  0.00101  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.42292 0.38782 0.36184 0.05219  0.04970  0.00948  99  THR A CG2 
668  N N   . LYS A 93  ? 0.35719 0.31472 0.28071 0.05264  0.03953  -0.02234 100 LYS A N   
669  C CA  . LYS A 93  ? 0.43270 0.38976 0.36498 0.05708  0.04587  -0.02660 100 LYS A CA  
670  C C   . LYS A 93  ? 0.39045 0.36362 0.36762 0.05499  0.05858  -0.01968 100 LYS A C   
671  O O   . LYS A 93  ? 0.40206 0.38459 0.40374 0.05213  0.05445  -0.02496 100 LYS A O   
672  C CB  . LYS A 93  ? 0.44184 0.38514 0.33746 0.07127  0.05650  -0.02595 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.49951 0.43796 0.39700 0.07821  0.06121  -0.03205 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.55012 0.47095 0.40834 0.09480  0.07547  -0.03153 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.70829 0.62174 0.56745 0.10421  0.08155  -0.03704 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.76179 0.65901 0.58786 0.12347  0.10150  -0.03445 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.40249 0.37948 0.39179 0.05611  0.07367  -0.00756 101 ALA A N   
678  C CA  . ALA A 94  ? 0.41280 0.40503 0.44874 0.05083  0.08615  -0.00139 101 ALA A CA  
679  C C   . ALA A 94  ? 0.37110 0.37155 0.43827 0.03531  0.07141  -0.00912 101 ALA A C   
680  O O   . ALA A 94  ? 0.37275 0.38924 0.47825 0.02875  0.07158  -0.01153 101 ALA A O   
681  C CB  . ALA A 94  ? 0.40595 0.39506 0.44570 0.05464  0.10751  0.01428  101 ALA A CB  
682  N N   . ASP A 95  ? 0.38071 0.37175 0.43192 0.02998  0.05848  -0.01306 102 ASP A N   
683  C CA  . ASP A 95  ? 0.34822 0.34309 0.41986 0.01777  0.04412  -0.02207 102 ASP A CA  
684  C C   . ASP A 95  ? 0.39206 0.39586 0.47012 0.01714  0.03126  -0.03253 102 ASP A C   
685  O O   . ASP A 95  ? 0.36516 0.38113 0.47325 0.00960  0.02541  -0.03780 102 ASP A O   
686  C CB  . ASP A 95  ? 0.35104 0.33510 0.39966 0.01584  0.03307  -0.02422 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.41290 0.38882 0.46165 0.01613  0.04361  -0.01393 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.41296 0.38800 0.48597 0.01271  0.05780  -0.00761 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.41473 0.38545 0.44040 0.01984  0.03763  -0.01166 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.32224 0.31832 0.36994 0.02501  0.02562  -0.03604 103 LEU A N   
691  C CA  . LEU A 96  ? 0.33244 0.33097 0.37928 0.02701  0.01464  -0.04428 103 LEU A CA  
692  C C   . LEU A 96  ? 0.37930 0.39463 0.45375 0.03250  0.02224  -0.04217 103 LEU A C   
693  O O   . LEU A 96  ? 0.37655 0.40394 0.46929 0.03131  0.01230  -0.04725 103 LEU A O   
694  C CB  . LEU A 96  ? 0.35342 0.33434 0.36104 0.03360  0.01050  -0.04793 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.37843 0.34852 0.36336 0.02709  -0.00003 -0.05054 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.38685 0.33985 0.33562 0.03080  -0.00392 -0.05518 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.38880 0.36205 0.38557 0.01880  -0.01281 -0.05563 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.36035 0.37830 0.43730 0.04038  0.04012  -0.03375 104 ILE A N   
699  C CA  . ILE A 97  ? 0.37632 0.41235 0.47919 0.04859  0.04950  -0.03017 104 ILE A CA  
700  C C   . ILE A 97  ? 0.39002 0.45218 0.54482 0.03873  0.05408  -0.02599 104 ILE A C   
701  O O   . ILE A 97  ? 0.40360 0.48999 0.59172 0.03978  0.05069  -0.02696 104 ILE A O   
702  C CB  . ILE A 97  ? 0.41601 0.44150 0.49476 0.06393  0.06883  -0.02293 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.39657 0.39604 0.42710 0.07226  0.06124  -0.03090 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.45398 0.50228 0.56676 0.07341  0.08451  -0.01528 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.53898 0.51995 0.53224 0.08604  0.07789  -0.02674 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.32642 0.38448 0.49017 0.02921  0.06196  -0.02094 105 ASN A N   
707  C CA  . ASN A 98  ? 0.40422 0.48363 0.61896 0.01833  0.07023  -0.01634 105 ASN A CA  
708  C C   . ASN A 98  ? 0.40541 0.47686 0.63283 0.00090  0.06374  -0.02046 105 ASN A C   
709  O O   . ASN A 98  ? 0.42038 0.50839 0.68611 -0.01250 0.05525  -0.02676 105 ASN A O   
710  C CB  . ASN A 98  ? 0.48690 0.56926 0.71042 0.02621  0.09794  -0.00107 105 ASN A CB  
711  C CG  . ASN A 98  ? 0.72177 0.83174 1.00623 0.01512  0.10865  0.00485  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.87264 1.00836 1.19429 0.00696  0.09458  -0.00276 105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.78466 0.89039 1.08044 0.01448  0.13334  0.01891  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.51605 0.47372 0.49687 0.05012  0.01373  0.03998  106 ASN A N   
715  C CA  . ASN A 99  ? 0.46114 0.44640 0.47820 0.05831  0.00837  0.05040  106 ASN A CA  
716  C C   . ASN A 99  ? 0.47622 0.47257 0.52619 0.05392  0.00293  0.04462  106 ASN A C   
717  O O   . ASN A 99  ? 0.62179 0.61885 0.70154 0.06034  0.00817  0.04870  106 ASN A O   
718  C CB  . ASN A 99  ? 0.42155 0.43606 0.42645 0.05991  -0.00486 0.05585  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.53924 0.54644 0.50414 0.06540  -0.00225 0.06340  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.60769 0.58598 0.56011 0.07194  0.01445  0.06878  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.57281 0.61474 0.51831 0.06332  -0.01919 0.06440  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.40973 0.41382 0.45056 0.03924  -0.00623 0.03391  107 LEU A N   
723  C CA  . LEU A 100 ? 0.40310 0.42015 0.46923 0.03485  -0.01035 0.02915  107 LEU A CA  
724  C C   . LEU A 100 ? 0.45570 0.45044 0.52939 0.03793  -0.00435 0.02717  107 LEU A C   
725  O O   . LEU A 100 ? 0.41295 0.41760 0.51130 0.03958  -0.00586 0.02590  107 LEU A O   
726  C CB  . LEU A 100 ? 0.40567 0.43901 0.45787 0.01421  -0.01804 0.01872  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.38131 0.46215 0.43790 0.01269  -0.02843 0.02045  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.41236 0.52465 0.46610 -0.01354 -0.03458 0.00794  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.36754 0.47387 0.45730 0.03797  -0.02918 0.03249  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.44730 0.41410 0.49773 0.04114  0.00252  0.02669  108 GLY A N   
731  C CA  . GLY A 101 ? 0.45837 0.41607 0.51853 0.05190  0.00655  0.02805  108 GLY A CA  
732  C C   . GLY A 101 ? 0.52592 0.50673 0.62362 0.06132  0.01084  0.03374  108 GLY A C   
733  O O   . GLY A 101 ? 0.44914 0.44675 0.57130 0.06284  0.00738  0.03226  108 GLY A O   
734  N N   . THR A 102 ? 0.42036 0.40222 0.51911 0.06439  0.01912  0.03969  109 THR A N   
735  C CA  . THR A 102 ? 0.38298 0.38100 0.51377 0.06564  0.02742  0.04469  109 THR A CA  
736  C C   . THR A 102 ? 0.43158 0.43818 0.58499 0.05677  0.02163  0.04152  109 THR A C   
737  O O   . THR A 102 ? 0.43930 0.45982 0.61950 0.05020  0.02356  0.03752  109 THR A O   
738  C CB  . THR A 102 ? 0.47639 0.46407 0.59316 0.06899  0.03951  0.05395  109 THR A CB  
739  O OG1 . THR A 102 ? 0.57875 0.55723 0.67481 0.07779  0.04969  0.05457  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.46598 0.46029 0.61028 0.06371  0.05145  0.05928  109 THR A CG2 
741  N N   . ILE A 103 ? 0.36393 0.36539 0.50614 0.05637  0.01547  0.04195  110 ILE A N   
742  C CA  . ILE A 103 ? 0.42355 0.42675 0.58156 0.05323  0.01357  0.03791  110 ILE A CA  
743  C C   . ILE A 103 ? 0.48862 0.50184 0.65620 0.04505  0.00587  0.02628  110 ILE A C   
744  O O   . ILE A 103 ? 0.53480 0.54823 0.71746 0.03797  0.00757  0.01929  110 ILE A O   
745  C CB  . ILE A 103 ? 0.45851 0.46710 0.60589 0.06101  0.00855  0.04147  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.55978 0.56223 0.69111 0.07279  0.01298  0.05557  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.52028 0.52718 0.68118 0.06374  0.01067  0.03652  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.59843 0.57486 0.73406 0.08128  0.02698  0.06525  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.39493 0.41036 0.54652 0.04477  -0.00140 0.02384  111 ALA A N   
750  C CA  . ALA A 104 ? 0.43727 0.45748 0.58693 0.04000  -0.00883 0.01630  111 ALA A CA  
751  C C   . ALA A 104 ? 0.46537 0.50095 0.63210 0.04134  -0.01109 0.01464  111 ALA A C   
752  O O   . ALA A 104 ? 0.45783 0.50324 0.62375 0.03769  -0.01928 0.00842  111 ALA A O   
753  C CB  . ALA A 104 ? 0.47152 0.47706 0.58982 0.03909  -0.01187 0.01684  111 ALA A CB  
754  N N   . LYS A 105 ? 0.40658 0.45171 0.58896 0.04587  -0.00406 0.01987  112 LYS A N   
755  C CA  . LYS A 105 ? 0.37805 0.45682 0.58477 0.04677  -0.00692 0.01798  112 LYS A CA  
756  C C   . LYS A 105 ? 0.39400 0.49020 0.62133 0.02716  -0.01115 0.00591  112 LYS A C   
757  O O   . LYS A 105 ? 0.35525 0.48119 0.58956 0.02434  -0.02351 -0.00055 112 LYS A O   
758  C CB  . LYS A 105 ? 0.43409 0.52570 0.65735 0.05259  0.00636  0.02511  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.49246 0.62563 0.73532 0.06685  0.00489  0.02794  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.60430 0.74878 0.86088 0.07383  0.02377  0.03499  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.70271 0.91252 0.99748 0.08583  0.02479  0.03630  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.60903 0.86517 0.94884 0.06212  0.03724  0.03214  112 LYS A NZ  
763  N N   . SER A 106 ? 0.39193 0.46574 0.62282 0.01429  -0.00061 0.00250  113 SER A N   
764  C CA  . SER A 106 ? 0.34722 0.42387 0.58943 -0.00778 -0.00005 -0.01212 113 SER A CA  
765  C C   . SER A 106 ? 0.37646 0.44623 0.59940 -0.00924 -0.01104 -0.02253 113 SER A C   
766  O O   . SER A 106 ? 0.35635 0.44599 0.58269 -0.02468 -0.01961 -0.03643 113 SER A O   
767  C CB  . SER A 106 ? 0.47848 0.51442 0.71812 -0.01747 0.01898  -0.01171 113 SER A CB  
768  O OG  . SER A 106 ? 0.53041 0.53214 0.74767 -0.00086 0.02233  -0.00515 113 SER A OG  
769  N N   . GLY A 107 ? 0.39694 0.44367 0.59880 0.00414  -0.01028 -0.01707 114 GLY A N   
770  C CA  . GLY A 107 ? 0.38936 0.43133 0.57189 0.00256  -0.01621 -0.02591 114 GLY A CA  
771  C C   . GLY A 107 ? 0.36015 0.42535 0.53110 0.00489  -0.03152 -0.02572 114 GLY A C   
772  O O   . GLY A 107 ? 0.32824 0.39892 0.48533 -0.00325 -0.03848 -0.03649 114 GLY A O   
773  N N   . THR A 108 ? 0.34657 0.42084 0.51676 0.01885  -0.03555 -0.01274 115 THR A N   
774  C CA  . THR A 108 ? 0.35232 0.44287 0.50679 0.02955  -0.04855 -0.00797 115 THR A CA  
775  C C   . THR A 108 ? 0.33251 0.46883 0.50725 0.02202  -0.06116 -0.01652 115 THR A C   
776  O O   . THR A 108 ? 0.36505 0.51546 0.52040 0.02195  -0.07457 -0.02042 115 THR A O   
777  C CB  . THR A 108 ? 0.33441 0.41727 0.48188 0.05064  -0.04554 0.00739  115 THR A CB  
778  O OG1 . THR A 108 ? 0.45538 0.49774 0.57708 0.05007  -0.03618 0.01137  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.39091 0.48642 0.51966 0.07038  -0.05707 0.01590  115 THR A CG2 
780  N N   . LYS A 109 ? 0.29315 0.45709 0.50505 0.01316  -0.05690 -0.01971 116 LYS A N   
781  C CA  . LYS A 109 ? 0.30084 0.52026 0.53858 -0.00295 -0.06848 -0.03147 116 LYS A CA  
782  C C   . LYS A 109 ? 0.32135 0.53047 0.54338 -0.02959 -0.07278 -0.05222 116 LYS A C   
783  O O   . LYS A 109 ? 0.30153 0.55320 0.52115 -0.03874 -0.09073 -0.06222 116 LYS A O   
784  C CB  . LYS A 109 ? 0.33632 0.57971 0.61542 -0.01727 -0.05613 -0.03346 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.39843 0.70545 0.70902 -0.04575 -0.06576 -0.05016 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.40304 0.74571 0.75783 -0.05847 -0.05122 -0.04855 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.57995 0.98753 0.96798 -0.09969 -0.05795 -0.06990 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.64046 1.05047 1.05975 -0.12829 -0.03304 -0.07302 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.33315 0.48786 0.54193 -0.04016 -0.05618 -0.05925 117 ALA A N   
790  C CA  . ALA A 110 ? 0.38313 0.51729 0.57096 -0.06246 -0.05482 -0.08074 117 ALA A CA  
791  C C   . ALA A 110 ? 0.35043 0.48255 0.50070 -0.05232 -0.06652 -0.08148 117 ALA A C   
792  O O   . ALA A 110 ? 0.38018 0.52617 0.51144 -0.06912 -0.07692 -0.09869 117 ALA A O   
793  C CB  . ALA A 110 ? 0.35280 0.42638 0.53366 -0.06612 -0.03086 -0.08471 117 ALA A CB  
794  N N   . PHE A 111 ? 0.32277 0.43578 0.45719 -0.02870 -0.06364 -0.06402 118 PHE A N   
795  C CA  . PHE A 111 ? 0.39319 0.49675 0.48698 -0.02132 -0.06950 -0.06201 118 PHE A CA  
796  C C   . PHE A 111 ? 0.40971 0.55409 0.48976 -0.01486 -0.09259 -0.05786 118 PHE A C   
797  O O   . PHE A 111 ? 0.39128 0.54130 0.43821 -0.02251 -0.10208 -0.06768 118 PHE A O   
798  C CB  . PHE A 111 ? 0.36012 0.43549 0.44189 -0.00437 -0.05926 -0.04461 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.37852 0.43687 0.41548 -0.00073 -0.05939 -0.04024 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.40038 0.45085 0.41203 -0.01285 -0.05495 -0.05502 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.43755 0.47986 0.45110 0.01375  -0.06012 -0.02164 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.40184 0.43534 0.36788 -0.01146 -0.05147 -0.04956 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.47901 0.49634 0.44445 0.01341  -0.05607 -0.01604 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.43867 0.45490 0.38168 0.00027  -0.05182 -0.02921 118 PHE A CZ  
805  N N   . MET A 112 ? 0.32977 0.50697 0.43356 0.00183  -0.10174 -0.04327 119 MET A N   
806  C CA  . MET A 112 ? 0.41492 0.64153 0.50971 0.01641  -0.12501 -0.03614 119 MET A CA  
807  C C   . MET A 112 ? 0.38101 0.66346 0.48995 -0.00979 -0.14207 -0.05813 119 MET A C   
808  O O   . MET A 112 ? 0.48271 0.80064 0.56529 -0.00408 -0.16377 -0.05808 119 MET A O   
809  C CB  . MET A 112 ? 0.40523 0.65797 0.52590 0.04539  -0.12726 -0.01600 119 MET A CB  
810  C CG  . MET A 112 ? 0.52986 0.72682 0.61088 0.07363  -0.11763 0.00555  119 MET A CG  
811  S SD  . MET A 112 ? 0.67737 0.87247 0.78040 0.10438  -0.10732 0.02435  119 MET A SD  
812  C CE  . MET A 112 ? 0.68271 0.81955 0.71454 0.13632  -0.10661 0.04645  119 MET A CE  
813  N N   . GLU A 113 ? 0.39625 0.68579 0.54108 -0.03996 -0.13268 -0.07690 120 GLU A N   
814  C CA  . GLU A 113 ? 0.44644 0.77693 0.59629 -0.07587 -0.14526 -0.10380 120 GLU A CA  
815  C C   . GLU A 113 ? 0.46471 0.75402 0.56003 -0.09013 -0.14463 -0.12102 120 GLU A C   
816  O O   . GLU A 113 ? 0.50726 0.83637 0.57909 -0.10388 -0.16592 -0.13500 120 GLU A O   
817  C CB  . GLU A 113 ? 0.44718 0.77054 0.63623 -0.10892 -0.12741 -0.12000 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.54346 0.93369 0.78941 -0.10518 -0.13099 -0.10953 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.81501 1.20622 1.09412 -0.14831 -0.11410 -0.12862 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.96123 1.29096 1.24459 -0.14675 -0.08767 -0.12154 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.85574 1.28764 1.14214 -0.17804 -0.12307 -0.14289 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.42513 0.64093 0.49883 -0.08525 -0.12044 -0.11998 121 ALA A N   
823  C CA  . ALA A 114 ? 0.50349 0.67888 0.52690 -0.09585 -0.11332 -0.13655 121 ALA A CA  
824  C C   . ALA A 114 ? 0.51157 0.70338 0.48890 -0.07777 -0.13107 -0.12466 121 ALA A C   
825  O O   . ALA A 114 ? 0.56940 0.76335 0.50359 -0.09292 -0.13902 -0.14225 121 ALA A O   
826  C CB  . ALA A 114 ? 0.42353 0.53309 0.44268 -0.08666 -0.08323 -0.13336 121 ALA A CB  
827  N N   . LEU A 115 ? 0.50576 0.70082 0.48352 -0.04548 -0.13516 -0.09476 122 LEU A N   
828  C CA  . LEU A 115 ? 0.53937 0.73625 0.46503 -0.02434 -0.14840 -0.07794 122 LEU A CA  
829  C C   . LEU A 115 ? 0.62620 0.89164 0.54088 -0.02624 -0.18124 -0.08331 122 LEU A C   
830  O O   . LEU A 115 ? 0.62301 0.88880 0.48036 -0.02290 -0.19301 -0.08282 122 LEU A O   
831  C CB  . LEU A 115 ? 0.47373 0.65123 0.39920 0.00959  -0.14388 -0.04567 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.57241 0.68653 0.49122 0.01066  -0.11525 -0.03822 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.55557 0.65031 0.47766 0.03723  -0.11101 -0.01178 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.54036 0.61460 0.40248 0.00288  -0.10219 -0.04099 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.58056 0.91109 0.54932 -0.03279 -0.19640 -0.08855 123 GLN A N   
836  C CA  . GLN A 116 ? 0.60071 1.01660 0.56924 -0.04180 -0.22998 -0.09893 123 GLN A CA  
837  C C   . GLN A 116 ? 0.59228 0.99865 0.53238 -0.08667 -0.23041 -0.13494 123 GLN A C   
838  O O   . GLN A 116 ? 0.67526 1.10961 0.58559 -0.09055 -0.24973 -0.13781 123 GLN A O   
839  C CB  . GLN A 116 ? 0.62902 1.10885 0.66986 -0.04344 -0.23582 -0.09550 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.63098 1.12207 0.69693 0.00329  -0.23411 -0.06186 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.90338 1.38579 0.91658 0.04809  -0.24719 -0.03248 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.77365 1.29721 0.77200 0.05332  -0.26707 -0.02904 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.87927 1.29985 0.85954 0.07981  -0.23374 -0.01055 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.62031 0.97001 0.56718 -0.11631 -0.20347 -0.15853 124 ALA A N   
845  C CA  . ALA A 117 ? 0.72994 1.05171 0.64648 -0.15694 -0.19619 -0.19368 124 ALA A CA  
846  C C   . ALA A 117 ? 0.78430 1.05118 0.62762 -0.15432 -0.18555 -0.20216 124 ALA A C   
847  O O   . ALA A 117 ? 0.83757 1.06131 0.65026 -0.18115 -0.17093 -0.22955 124 ALA A O   
848  C CB  . ALA A 117 ? 0.71598 0.99294 0.66763 -0.18629 -0.16805 -0.21426 124 ALA A CB  
849  N N   . GLY A 118 ? 0.72461 0.97187 0.54087 -0.11676 -0.18315 -0.17134 125 GLY A N   
850  C CA  . GLY A 118 ? 0.79959 0.99597 0.54682 -0.11309 -0.16879 -0.17391 125 GLY A CA  
851  C C   . GLY A 118 ? 0.79845 0.92702 0.54878 -0.09911 -0.13170 -0.16287 125 GLY A C   
852  O O   . GLY A 118 ? 0.77775 0.86935 0.47544 -0.09625 -0.11535 -0.16369 125 GLY A O   
853  N N   . ALA A 119 ? 0.61364 0.73086 0.42308 -0.09165 -0.11765 -0.15326 126 ALA A N   
854  C CA  . ALA A 119 ? 0.65298 0.72336 0.46958 -0.07743 -0.08761 -0.14080 126 ALA A CA  
855  C C   . ALA A 119 ? 0.70987 0.77385 0.49669 -0.05406 -0.08976 -0.11007 126 ALA A C   
856  O O   . ALA A 119 ? 0.66130 0.75052 0.42294 -0.04133 -0.11374 -0.09446 126 ALA A O   
857  C CB  . ALA A 119 ? 0.57280 0.63819 0.45387 -0.07385 -0.07660 -0.13588 126 ALA A CB  
858  N N   . ASP A 120 ? 0.62757 0.65692 0.41369 -0.04844 -0.06323 -0.10113 127 ASP A N   
859  C CA  . ASP A 120 ? 0.70334 0.71394 0.45634 -0.03409 -0.05950 -0.07402 127 ASP A CA  
860  C C   . ASP A 120 ? 0.63112 0.62688 0.42505 -0.02918 -0.04207 -0.06141 127 ASP A C   
861  O O   . ASP A 120 ? 0.56688 0.56829 0.40861 -0.03408 -0.03094 -0.07296 127 ASP A O   
862  C CB  . ASP A 120 ? 0.75517 0.73982 0.44340 -0.04141 -0.04274 -0.07659 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.90343 0.87450 0.60805 -0.05303 -0.00970 -0.09253 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.94168 0.91787 0.66461 -0.06074 -0.00399 -0.11792 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.90609 0.86153 0.60345 -0.05442 0.01200  -0.07972 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.66692 0.63901 0.43366 -0.01955 -0.03919 -0.03731 128 ILE A N   
867  C CA  . ILE A 121 ? 0.54532 0.50318 0.34248 -0.01771 -0.02727 -0.02535 128 ILE A CA  
868  C C   . ILE A 121 ? 0.54906 0.51151 0.37428 -0.03349 -0.00249 -0.03825 128 ILE A C   
869  O O   . ILE A 121 ? 0.51683 0.48959 0.38802 -0.03312 0.00174  -0.03787 128 ILE A O   
870  C CB  . ILE A 121 ? 0.60832 0.52363 0.35287 -0.00885 -0.02419 0.00006  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.63166 0.55388 0.37332 0.01891  -0.04921 0.01569  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.58089 0.46862 0.33532 -0.02062 -0.00322 0.00711  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.73552 0.61297 0.40599 0.03893  -0.05096 0.04186  128 ILE A CD1 
874  N N   . SER A 122 ? 0.57806 0.54002 0.37789 -0.04452 0.01379  -0.05050 129 SER A N   
875  C CA  . SER A 122 ? 0.53744 0.51588 0.36785 -0.05358 0.03887  -0.06134 129 SER A CA  
876  C C   . SER A 122 ? 0.55395 0.55505 0.44264 -0.04438 0.03721  -0.07467 129 SER A C   
877  O O   . SER A 122 ? 0.53847 0.56067 0.46270 -0.04291 0.05368  -0.07830 129 SER A O   
878  C CB  . SER A 122 ? 0.62144 0.59770 0.41332 -0.06289 0.05948  -0.07322 129 SER A CB  
879  O OG  . SER A 122 ? 0.65411 0.63369 0.44433 -0.05780 0.05587  -0.09440 129 SER A OG  
880  N N   . MET A 123 ? 0.46309 0.46229 0.36154 -0.03823 0.01853  -0.08086 130 MET A N   
881  C CA  . MET A 123 ? 0.47322 0.47852 0.41521 -0.03198 0.02091  -0.09265 130 MET A CA  
882  C C   . MET A 123 ? 0.46676 0.48072 0.45124 -0.02418 0.01197  -0.07866 130 MET A C   
883  O O   . MET A 123 ? 0.42645 0.43954 0.44266 -0.01819 0.01345  -0.08390 130 MET A O   
884  C CB  . MET A 123 ? 0.52906 0.52530 0.45585 -0.03856 0.00948  -0.11021 130 MET A CB  
885  C CG  . MET A 123 ? 0.65800 0.63956 0.54509 -0.04537 0.02529  -0.13089 130 MET A CG  
886  S SD  . MET A 123 ? 0.77408 0.75158 0.61806 -0.06289 0.00383  -0.15038 130 MET A SD  
887  C CE  . MET A 123 ? 0.67468 0.64455 0.56424 -0.06931 0.00077  -0.16337 130 MET A CE  
888  N N   . ILE A 124 ? 0.39739 0.41169 0.37584 -0.02454 0.00620  -0.06117 131 ILE A N   
889  C CA  . ILE A 124 ? 0.33521 0.35239 0.34199 -0.01756 -0.00338 -0.04889 131 ILE A CA  
890  C C   . ILE A 124 ? 0.34227 0.37374 0.38973 -0.01182 0.00641  -0.05030 131 ILE A C   
891  O O   . ILE A 124 ? 0.36470 0.39691 0.43760 -0.00452 0.00009  -0.04563 131 ILE A O   
892  C CB  . ILE A 124 ? 0.38668 0.38756 0.36593 -0.02000 -0.00534 -0.03265 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.36102 0.35863 0.36076 -0.01123 -0.01342 -0.02178 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.39919 0.40121 0.36670 -0.03476 0.01324  -0.03270 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.35088 0.31472 0.31183 -0.01094 -0.01270 -0.00688 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.35616 0.40348 0.40989 -0.01245 0.02261  -0.05576 132 GLY A N   
897  C CA  . GLY A 125 ? 0.42067 0.49100 0.51181 -0.00038 0.02967  -0.05371 132 GLY A CA  
898  C C   . GLY A 125 ? 0.44569 0.50051 0.55301 0.01522  0.03302  -0.06012 132 GLY A C   
899  O O   . GLY A 125 ? 0.43853 0.49954 0.57078 0.02972  0.03411  -0.05264 132 GLY A O   
900  N N   . GLN A 126 ? 0.41594 0.44530 0.50290 0.01060  0.03541  -0.07412 133 GLN A N   
901  C CA  . GLN A 126 ? 0.47061 0.47104 0.56484 0.01862  0.04217  -0.08246 133 GLN A CA  
902  C C   . GLN A 126 ? 0.47174 0.46217 0.58035 0.01413  0.02948  -0.07444 133 GLN A C   
903  O O   . GLN A 126 ? 0.55257 0.51351 0.66569 0.01639  0.03753  -0.07920 133 GLN A O   
904  C CB  . GLN A 126 ? 0.47438 0.44648 0.53730 0.00757  0.04886  -0.10441 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.56482 0.54570 0.60603 0.01008  0.06381  -0.11383 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.87467 0.82655 0.87374 -0.00470 0.06762  -0.13693 133 GLN A CD  
907  O OE1 . GLN A 126 ? 1.03385 0.94928 1.02339 -0.01156 0.07039  -0.15205 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.76707 0.73173 0.73484 -0.01299 0.06938  -0.14080 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.37454 0.38379 0.48678 0.00804  0.01363  -0.06250 134 PHE A N   
910  C CA  . PHE A 127 ? 0.31108 0.31951 0.43913 0.00614  0.00400  -0.05378 134 PHE A CA  
911  C C   . PHE A 127 ? 0.34671 0.36656 0.48931 0.01706  0.00279  -0.03680 134 PHE A C   
912  O O   . PHE A 127 ? 0.35096 0.37053 0.50344 0.01728  -0.00260 -0.02854 134 PHE A O   
913  C CB  . PHE A 127 ? 0.34019 0.36129 0.45684 -0.00493 -0.01253 -0.05489 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.36509 0.38251 0.46325 -0.01906 -0.01534 -0.07354 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.36631 0.37960 0.47461 -0.03389 -0.01635 -0.08613 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.37337 0.38995 0.43994 -0.02165 -0.01491 -0.08019 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.38216 0.39233 0.46876 -0.05264 -0.01969 -0.10741 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.37931 0.39140 0.42091 -0.03618 -0.01802 -0.09975 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.44744 0.45722 0.49892 -0.05234 -0.02171 -0.11442 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.38065 0.41596 0.52451 0.02426  0.00811  -0.03285 135 GLY A N   
921  C CA  . GLY A 128 ? 0.36756 0.41853 0.52113 0.03037  0.00496  -0.01995 135 GLY A CA  
922  C C   . GLY A 128 ? 0.42061 0.47241 0.55914 0.01954  -0.00410 -0.01419 135 GLY A C   
923  O O   . GLY A 128 ? 0.39164 0.44873 0.53171 0.02137  -0.00677 -0.00620 135 GLY A O   
924  N N   . VAL A 129 ? 0.38506 0.42606 0.50198 0.01005  -0.00780 -0.01751 136 VAL A N   
925  C CA  . VAL A 129 ? 0.30976 0.33587 0.40316 0.00505  -0.01240 -0.01016 136 VAL A CA  
926  C C   . VAL A 129 ? 0.31654 0.33592 0.38051 -0.00932 -0.00718 -0.01241 136 VAL A C   
927  O O   . VAL A 129 ? 0.31336 0.30355 0.34321 -0.01224 -0.00825 -0.00674 136 VAL A O   
928  C CB  . VAL A 129 ? 0.32020 0.33449 0.40900 0.01345  -0.02056 -0.00608 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.41166 0.43392 0.52862 0.02143  -0.02088 -0.00322 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.32358 0.34435 0.40840 0.01137  -0.02552 -0.01408 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.30581 0.31658 0.38423 -0.02492 -0.02495 -0.02754 137 GLY A N   
932  C CA  . GLY A 130 ? 0.30242 0.31424 0.37062 -0.01983 -0.02790 -0.02837 137 GLY A CA  
933  C C   . GLY A 130 ? 0.32038 0.33030 0.37946 -0.01364 -0.02783 -0.02078 137 GLY A C   
934  O O   . GLY A 130 ? 0.34004 0.35346 0.39162 -0.01010 -0.02981 -0.02002 137 GLY A O   
935  N N   . PHE A 131 ? 0.30259 0.30610 0.36128 -0.01246 -0.02508 -0.01523 138 PHE A N   
936  C CA  . PHE A 131 ? 0.27770 0.27738 0.32752 -0.00750 -0.02490 -0.01058 138 PHE A CA  
937  C C   . PHE A 131 ? 0.30276 0.31034 0.34959 -0.00316 -0.02660 -0.00969 138 PHE A C   
938  O O   . PHE A 131 ? 0.32370 0.32563 0.36221 0.00029  -0.02695 -0.00726 138 PHE A O   
939  C CB  . PHE A 131 ? 0.32352 0.31954 0.37271 -0.00639 -0.02181 -0.00650 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.35842 0.35083 0.39889 -0.00148 -0.02143 -0.00442 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.35797 0.34144 0.39076 -0.00123 -0.02233 -0.00450 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.34884 0.34718 0.38984 0.00281  -0.01992 -0.00331 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.34240 0.31927 0.36733 0.00190  -0.02157 -0.00438 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.33565 0.32679 0.36804 0.00824  -0.01881 -0.00262 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.34308 0.32183 0.36718 0.00703  -0.01958 -0.00362 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.29850 0.31951 0.35281 -0.00313 -0.02735 -0.01104 139 TYR A N   
947  C CA  . TYR A 132 ? 0.28378 0.31467 0.33615 0.00364  -0.02901 -0.00870 139 TYR A CA  
948  C C   . TYR A 132 ? 0.30697 0.34213 0.35298 0.00607  -0.03263 -0.00899 139 TYR A C   
949  O O   . TYR A 132 ? 0.30647 0.34553 0.34742 0.01375  -0.03370 -0.00445 139 TYR A O   
950  C CB  . TYR A 132 ? 0.31376 0.36342 0.37832 0.00288  -0.02918 -0.01040 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.32674 0.37345 0.39636 0.00091  -0.02397 -0.00838 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.33323 0.37624 0.39764 0.00834  -0.02066 -0.00428 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.33817 0.38390 0.41614 -0.00788 -0.02164 -0.01035 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.31710 0.35933 0.38378 0.00692  -0.01533 -0.00243 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.40947 0.45262 0.49003 -0.00939 -0.01606 -0.00651 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.39110 0.43440 0.46565 -0.00204 -0.01304 -0.00265 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.44816 0.49144 0.52383 -0.00350 -0.00695 0.00117  139 TYR A OH  
958  N N   . SER A 133 ? 0.26792 0.30175 0.31296 0.00089  -0.03384 -0.01349 140 SER A N   
959  C CA  . SER A 133 ? 0.32007 0.35749 0.35620 0.00350  -0.03593 -0.01282 140 SER A CA  
960  C C   . SER A 133 ? 0.32379 0.34655 0.34942 0.00732  -0.03318 -0.00542 140 SER A C   
961  O O   . SER A 133 ? 0.31313 0.33803 0.33015 0.01061  -0.03362 -0.00165 140 SER A O   
962  C CB  . SER A 133 ? 0.27737 0.31627 0.31456 -0.00239 -0.03654 -0.02055 140 SER A CB  
963  O OG  . SER A 133 ? 0.32805 0.35148 0.36418 -0.00470 -0.03307 -0.01945 140 SER A OG  
964  N N   . ALA A 134 ? 0.32089 0.32910 0.34656 0.00634  -0.03011 -0.00340 141 ALA A N   
965  C CA  . ALA A 134 ? 0.30260 0.29619 0.31980 0.00871  -0.02746 0.00216  141 ALA A CA  
966  C C   . ALA A 134 ? 0.30124 0.29489 0.31253 0.01718  -0.02747 0.00865  141 ALA A C   
967  O O   . ALA A 134 ? 0.32664 0.30909 0.32948 0.01880  -0.02514 0.01440  141 ALA A O   
968  C CB  . ALA A 134 ? 0.28505 0.26663 0.30325 0.00718  -0.02521 0.00121  141 ALA A CB  
969  N N   . TYR A 135 ? 0.28004 0.28670 0.29635 0.02294  -0.02963 0.00860  142 TYR A N   
970  C CA  . TYR A 135 ? 0.33431 0.34317 0.34585 0.03386  -0.02998 0.01569  142 TYR A CA  
971  C C   . TYR A 135 ? 0.34909 0.37126 0.35458 0.03744  -0.03328 0.01957  142 TYR A C   
972  O O   . TYR A 135 ? 0.34756 0.37344 0.34798 0.04823  -0.03410 0.02727  142 TYR A O   
973  C CB  . TYR A 135 ? 0.25175 0.27413 0.27262 0.03965  -0.03091 0.01416  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.30960 0.31603 0.33132 0.03881  -0.02626 0.01227  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.30932 0.29765 0.32380 0.04672  -0.02251 0.01634  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.31593 0.32377 0.34398 0.03020  -0.02538 0.00638  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.33511 0.30948 0.34826 0.04591  -0.01848 0.01261  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.34255 0.33775 0.36849 0.02993  -0.02142 0.00473  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.33664 0.31616 0.35479 0.03752  -0.01829 0.00684  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.35252 0.32069 0.36689 0.03734  -0.01471 0.00315  142 TYR A OH  
981  N N   . LEU A 136 ? 0.29439 0.32338 0.29896 0.02994  -0.03479 0.01485  143 LEU A N   
982  C CA  . LEU A 136 ? 0.33626 0.37502 0.33080 0.03312  -0.03650 0.01898  143 LEU A CA  
983  C C   . LEU A 136 ? 0.37131 0.38992 0.35388 0.03580  -0.03115 0.02978  143 LEU A C   
984  O O   . LEU A 136 ? 0.36921 0.39194 0.34110 0.04335  -0.03125 0.03900  143 LEU A O   
985  C CB  . LEU A 136 ? 0.29363 0.34210 0.28946 0.02449  -0.03790 0.00979  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.32102 0.38884 0.32758 0.02029  -0.04296 -0.00180 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.29681 0.36550 0.30324 0.01249  -0.04230 -0.01099 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.31069 0.40395 0.31545 0.02747  -0.04916 -0.00107 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.31727 0.31524 0.30129 0.02879  -0.02637 0.02881  144 VAL A N   
990  C CA  . VAL A 137 ? 0.32773 0.30599 0.30277 0.02757  -0.02050 0.03745  144 VAL A CA  
991  C C   . VAL A 137 ? 0.39086 0.34461 0.36612 0.02920  -0.01666 0.04030  144 VAL A C   
992  O O   . VAL A 137 ? 0.39172 0.32604 0.35951 0.02901  -0.01134 0.04843  144 VAL A O   
993  C CB  . VAL A 137 ? 0.34312 0.32022 0.31921 0.01652  -0.01758 0.03351  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.35981 0.35943 0.33277 0.01622  -0.01999 0.03045  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.33701 0.30982 0.32391 0.00885  -0.01815 0.02378  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.36445 0.31721 0.34741 0.03014  -0.01829 0.03365  145 ALA A N   
997  C CA  . ALA A 138 ? 0.36573 0.29536 0.34799 0.03050  -0.01439 0.03308  145 ALA A CA  
998  C C   . ALA A 138 ? 0.42010 0.34813 0.40206 0.04377  -0.01448 0.03623  145 ALA A C   
999  O O   . ALA A 138 ? 0.43126 0.38087 0.41964 0.04906  -0.01858 0.03392  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.36234 0.29208 0.35186 0.02166  -0.01517 0.02261  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.42577 0.32826 0.40125 0.04912  -0.00946 0.04118  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.49073 0.38931 0.46651 0.06322  -0.00842 0.04304  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.52171 0.41618 0.50261 0.06087  -0.00724 0.03205  146 GLU A C   
1004 O O   . GLU A 139 ? 0.46129 0.36284 0.44576 0.07169  -0.00696 0.03080  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.55250 0.42221 0.51841 0.07202  -0.00267 0.05328  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.60448 0.44083 0.56608 0.06193  0.00342  0.04958  146 GLU A CG  
1007 C CD  . GLU A 139 ? 1.03940 0.84427 0.99103 0.06787  0.01020  0.06192  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.99767 0.80622 0.94458 0.08322  0.01006  0.07435  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.05523 0.83159 1.00404 0.05713  0.01577  0.05931  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.42432 0.31090 0.40561 0.04759  -0.00660 0.02426  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.38863 0.27315 0.37214 0.04510  -0.00578 0.01409  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.43839 0.33115 0.42511 0.03095  -0.00855 0.00814  147 LYS A C   
1013 O O   . LYS A 140 ? 0.39006 0.27803 0.37551 0.02249  -0.00867 0.01010  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.42007 0.27400 0.39613 0.04739  -0.00031 0.01051  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.46281 0.31489 0.43811 0.04358  0.00040  -0.00166 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.51639 0.33703 0.48364 0.04843  0.00621  -0.00632 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.65719 0.46161 0.62024 0.03427  0.00673  -0.01687 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.70867 0.47582 0.66466 0.03622  0.01301  -0.01902 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.36046 0.26685 0.35155 0.02920  -0.01025 0.00198  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.35979 0.27387 0.35360 0.01830  -0.01288 -0.00265 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.39047 0.29986 0.38057 0.01698  -0.01178 -0.01044 148 VAL A C   
1022 O O   . VAL A 141 ? 0.37083 0.28487 0.36047 0.02424  -0.00992 -0.01201 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.33975 0.27616 0.34173 0.01696  -0.01616 -0.00112 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.33141 0.27267 0.33566 0.00802  -0.01825 -0.00481 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.34027 0.28415 0.34425 0.01835  -0.01788 0.00463  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.41438 0.31692 0.40172 0.00799  -0.01282 -0.01560 149 THR A N   
1027 C CA  . THR A 142 ? 0.38622 0.28886 0.36870 0.00562  -0.01330 -0.02395 149 THR A CA  
1028 C C   . THR A 142 ? 0.40179 0.32190 0.38848 -0.00051 -0.01754 -0.02396 149 THR A C   
1029 O O   . THR A 142 ? 0.41025 0.33402 0.40194 -0.00683 -0.01974 -0.02193 149 THR A O   
1030 C CB  . THR A 142 ? 0.39527 0.27801 0.37159 -0.00025 -0.01197 -0.03147 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.46574 0.32788 0.43850 0.00634  -0.00722 -0.02960 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.44001 0.32456 0.40877 -0.00144 -0.01290 -0.04240 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.33853 0.26960 0.32298 0.00226  -0.01802 -0.02541 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.32658 0.27231 0.31391 -0.00123 -0.02153 -0.02371 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.41624 0.36518 0.39435 -0.00223 -0.02315 -0.03044 150 VAL A C   
1036 O O   . VAL A 143 ? 0.41218 0.36136 0.38289 0.00320  -0.02030 -0.03267 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.31716 0.27416 0.31023 0.00295  -0.02023 -0.01672 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.35044 0.31809 0.34506 0.00094  -0.02288 -0.01393 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.32492 0.28240 0.32692 0.00278  -0.02012 -0.01217 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.33536 0.28961 0.31388 -0.00880 -0.02774 -0.03410 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.32157 0.28426 0.29126 -0.01020 -0.03116 -0.04105 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.35670 0.33748 0.32911 -0.00776 -0.03451 -0.03372 151 ILE A C   
1043 O O   . ILE A 144 ? 0.36535 0.35102 0.34787 -0.00979 -0.03639 -0.02884 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.37939 0.33835 0.34928 -0.01986 -0.03459 -0.05107 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.47460 0.41011 0.44489 -0.02314 -0.03009 -0.05507 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.37192 0.34034 0.33101 -0.02143 -0.03865 -0.06123 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.43553 0.35728 0.39541 -0.01686 -0.02574 -0.06051 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.35098 0.34114 0.31389 -0.00248 -0.03456 -0.03229 152 THR A N   
1049 C CA  . THR A 145 ? 0.33970 0.34289 0.30504 0.00153  -0.03629 -0.02236 152 THR A CA  
1050 C C   . THR A 145 ? 0.38722 0.40445 0.33883 0.00533  -0.03920 -0.02350 152 THR A C   
1051 O O   . THR A 145 ? 0.40295 0.41895 0.34235 0.00673  -0.03730 -0.03021 152 THR A O   
1052 C CB  . THR A 145 ? 0.35613 0.35446 0.32703 0.00580  -0.03035 -0.01212 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.33923 0.34462 0.31447 0.00881  -0.03135 -0.00234 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.36890 0.36706 0.33033 0.01035  -0.02491 -0.01151 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.33284 0.36412 0.28588 0.00821  -0.04369 -0.01684 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.31776 0.36632 0.25691 0.01350  -0.04754 -0.01540 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.37784 0.43253 0.31963 0.02136  -0.04687 0.00064  153 LYS A C   
1058 O O   . LYS A 146 ? 0.33292 0.39021 0.28686 0.02168  -0.04995 0.00451  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.32991 0.39372 0.26735 0.00844  -0.05665 -0.02708 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.39567 0.48310 0.31890 0.01482  -0.06275 -0.02539 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.38105 0.46852 0.28417 0.01747  -0.05960 -0.03102 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.44289 0.55694 0.32860 0.02359  -0.06657 -0.03117 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.39224 0.51778 0.27520 0.03508  -0.06653 -0.01100 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.31799 0.37387 0.24866 0.02787  -0.04187 0.01011  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.38812 0.44721 0.31796 0.03603  -0.03996 0.02701  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.38078 0.46125 0.29318 0.04331  -0.04559 0.02979  154 HIS A C   
1067 O O   . HIS A 147 ? 0.38620 0.47580 0.28383 0.04225  -0.04706 0.02021  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.39596 0.44190 0.32586 0.03693  -0.02917 0.03705  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.41074 0.45211 0.34275 0.04309  -0.02481 0.05508  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.43086 0.48254 0.34762 0.05182  -0.02409 0.06763  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.35679 0.38222 0.30387 0.04165  -0.02018 0.06270  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.43674 0.47662 0.35968 0.05572  -0.01870 0.08350  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.38618 0.40944 0.32792 0.04914  -0.01625 0.07971  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.35392 0.44280 0.26726 0.05179  -0.04876 0.04275  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.38973 0.50271 0.28607 0.06071  -0.05533 0.04732  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.45296 0.56966 0.32759 0.06451  -0.04948 0.05211  155 ASN A C   
1077 O O   . ASN A 148 ? 0.46369 0.60275 0.31979 0.06916  -0.05541 0.04882  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.43883 0.55593 0.33914 0.07246  -0.05701 0.06536  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.47309 0.60033 0.39040 0.07262  -0.06569 0.05975  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.44528 0.58660 0.36678 0.06495  -0.07320 0.04332  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.44748 0.56709 0.37520 0.08137  -0.06376 0.07353  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.40846 0.50654 0.28487 0.06264  -0.03785 0.05956  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.52475 0.62779 0.38187 0.06700  -0.03014 0.06712  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.50110 0.60304 0.35224 0.06059  -0.02639 0.05073  156 ASP A C   
1085 O O   . ASP A 149 ? 0.49927 0.60498 0.33661 0.06364  -0.01808 0.05559  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.47027 0.55636 0.33342 0.06898  -0.01811 0.08729  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.53118 0.61550 0.39568 0.07823  -0.01958 0.10629  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.57356 0.67640 0.42944 0.08628  -0.02968 0.10697  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.54677 0.61115 0.42163 0.07757  -0.01041 0.12037  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.43553 0.53148 0.29693 0.05242  -0.03119 0.03234  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.48726 0.57751 0.34463 0.04790  -0.02671 0.01761  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.52106 0.61276 0.37943 0.04141  -0.03588 -0.00331 157 ASP A C   
1093 O O   . ASP A 150 ? 0.45639 0.55616 0.32032 0.03936  -0.04535 -0.00593 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.41705 0.48802 0.29183 0.04365  -0.01750 0.02147  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.57826 0.64779 0.44624 0.04428  -0.00875 0.01501  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.49510 0.57422 0.34533 0.04699  -0.01003 0.00367  157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.49193 0.55225 0.37288 0.04236  -0.00055 0.02068  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.46923 0.55299 0.32301 0.03823  -0.03236 -0.01815 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.48903 0.56787 0.34432 0.03062  -0.03882 -0.03848 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.49826 0.55732 0.37580 0.02325  -0.03844 -0.03991 158 GLU A C   
1101 O O   . GLU A 151 ? 0.43912 0.48908 0.32997 0.02432  -0.03339 -0.02732 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.48023 0.55447 0.32080 0.03170  -0.03398 -0.05375 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.64597 0.74086 0.46152 0.03916  -0.03350 -0.05479 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.06768 1.15555 0.87040 0.04205  -0.02571 -0.06881 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.05382 1.12528 0.86019 0.03636  -0.02692 -0.08679 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.20400 1.30163 0.99367 0.05037  -0.01733 -0.06124 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.36526 0.41741 0.24621 0.01509  -0.04339 -0.05596 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.40518 0.43902 0.30486 0.00814  -0.04256 -0.05699 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.45310 0.46629 0.35333 0.00974  -0.03394 -0.06089 159 GLN A C   
1110 O O   . GLN A 152 ? 0.46309 0.47104 0.35093 0.01085  -0.03173 -0.07364 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.42200 0.45679 0.32650 -0.00227 -0.05029 -0.07060 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.43326 0.45191 0.35671 -0.00982 -0.04923 -0.06934 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.52588 0.55285 0.45629 -0.02076 -0.05682 -0.07938 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.49286 0.54387 0.42443 -0.02051 -0.06414 -0.07745 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.52118 0.52937 0.45673 -0.03024 -0.05487 -0.08967 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.40957 0.41223 0.32402 0.01063  -0.02931 -0.05064 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.40709 0.39472 0.32426 0.01419  -0.02163 -0.05160 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.42265 0.39353 0.35366 0.00927  -0.02182 -0.05203 160 TYR A C   
1119 O O   . TYR A 153 ? 0.41928 0.39244 0.36097 0.00429  -0.02577 -0.04647 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.34341 0.33798 0.26449 0.02074  -0.01507 -0.03824 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.45902 0.46842 0.36481 0.02670  -0.01191 -0.03636 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.45799 0.46683 0.35218 0.03241  -0.00597 -0.04470 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.52762 0.55141 0.42971 0.02777  -0.01415 -0.02566 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.50780 0.53232 0.38623 0.03819  -0.00221 -0.04277 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.53802 0.57596 0.42424 0.03371  -0.01066 -0.02193 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.58950 0.62890 0.46344 0.03848  -0.00463 -0.03068 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.76182 0.81749 0.61837 0.04470  -0.00031 -0.02646 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.39525 0.35023 0.32564 0.01247  -0.01664 -0.05719 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.41343 0.35273 0.35522 0.01103  -0.01509 -0.05424 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.43881 0.37961 0.38641 0.01972  -0.00914 -0.04623 161 ALA A C   
1131 O O   . ALA A 154 ? 0.43433 0.37376 0.37566 0.02750  -0.00383 -0.05009 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.45828 0.37567 0.39564 0.00785  -0.01426 -0.06591 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.34974 0.29505 0.30986 0.01838  -0.01006 -0.03624 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.36406 0.31295 0.33296 0.02462  -0.00602 -0.02945 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.38244 0.31662 0.35612 0.02507  -0.00650 -0.02899 162 TRP A C   
1136 O O   . TRP A 155 ? 0.38227 0.30833 0.35706 0.01800  -0.01005 -0.02954 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.36370 0.32787 0.34258 0.02174  -0.00710 -0.02001 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.33544 0.30819 0.32620 0.02502  -0.00443 -0.01387 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.34856 0.33598 0.34428 0.02779  0.00020  -0.00971 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.35564 0.32629 0.35546 0.02472  -0.00659 -0.01120 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.33986 0.33550 0.34887 0.02841  0.00035  -0.00595 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.37089 0.35684 0.38136 0.02733  -0.00420 -0.00689 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.35905 0.31816 0.35866 0.02218  -0.01001 -0.01179 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.37192 0.36338 0.39182 0.02829  -0.00638 -0.00436 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.30519 0.26839 0.31258 0.02400  -0.01125 -0.00764 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.34129 0.32134 0.35831 0.02719  -0.01012 -0.00455 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.35394 0.28609 0.33041 0.03400  -0.00256 -0.02715 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.40003 0.31787 0.37900 0.03626  -0.00276 -0.02460 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.39998 0.32868 0.38703 0.04626  -0.00063 -0.01824 163 GLU A C   
1150 O O   . GLU A 156 ? 0.38661 0.32510 0.37449 0.05425  0.00342  -0.01956 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.44608 0.33915 0.41536 0.03880  0.00013  -0.03215 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.49448 0.36736 0.46405 0.03783  0.00028  -0.02863 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.68451 0.53004 0.64473 0.03409  0.00276  -0.03834 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.71953 0.55359 0.67358 0.04329  0.00742  -0.04453 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.59766 0.43420 0.55733 0.02181  0.00045  -0.04096 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.38777 0.31579 0.38012 0.04669  -0.00307 -0.01174 164 SER A N   
1157 C CA  . SER A 157 ? 0.37101 0.31135 0.37059 0.05747  -0.00210 -0.00621 164 SER A CA  
1158 C C   . SER A 157 ? 0.32996 0.26114 0.32876 0.06051  -0.00411 0.00039  164 SER A C   
1159 O O   . SER A 157 ? 0.37264 0.30191 0.37110 0.05160  -0.00748 0.00269  164 SER A O   
1160 C CB  . SER A 157 ? 0.30829 0.27704 0.31999 0.05435  -0.00415 -0.00340 164 SER A CB  
1161 O OG  . SER A 157 ? 0.35409 0.33900 0.37422 0.06472  -0.00386 0.00072  164 SER A OG  
1162 N N   . SER A 158 ? 0.36058 0.28914 0.35936 0.07432  -0.00172 0.00425  165 SER A N   
1163 C CA  . SER A 158 ? 0.41468 0.34057 0.41277 0.08124  -0.00348 0.01338  165 SER A CA  
1164 C C   . SER A 158 ? 0.36880 0.32711 0.37797 0.08856  -0.00710 0.01811  165 SER A C   
1165 O O   . SER A 158 ? 0.40884 0.37060 0.41757 0.10008  -0.00835 0.02600  165 SER A O   
1166 C CB  . SER A 158 ? 0.51329 0.41078 0.50275 0.09315  0.00176  0.01570  165 SER A CB  
1167 O OG  . SER A 158 ? 0.49088 0.35844 0.47119 0.08333  0.00449  0.01054  165 SER A OG  
1168 N N   . ALA A 159 ? 0.37018 0.35274 0.38939 0.08144  -0.00891 0.01371  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.43345 0.44980 0.46624 0.08542  -0.01199 0.01550  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.45182 0.47580 0.48849 0.10243  -0.00812 0.01715  166 ALA A C   
1171 O O   . ALA A 159 ? 0.45590 0.46337 0.48693 0.10772  -0.00202 0.01349  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.40670 0.43441 0.44029 0.08369  -0.01851 0.02036  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.42704 0.47803 0.47353 0.11201  -0.01162 0.02177  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.41781 0.48065 0.47053 0.12917  -0.00767 0.02309  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.42733 0.51339 0.49273 0.12598  -0.00336 0.01692  167 GLY A C   
1176 O O   . GLY A 160 ? 0.43089 0.52762 0.50172 0.14048  0.00150  0.01687  167 GLY A O   
1177 N N   . GLY A 161 ? 0.35481 0.44851 0.42495 0.10814  -0.00409 0.01242  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.37573 0.49279 0.45838 0.10333  0.00072  0.00868  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.34907 0.44718 0.42162 0.09979  0.00822  0.00430  168 GLY A C   
1180 O O   . GLY A 161 ? 0.35497 0.47197 0.43603 0.09583  0.01350  0.00261  168 GLY A O   
1181 N N   . SER A 162 ? 0.31871 0.38212 0.37352 0.10012  0.00892  0.00234  169 SER A N   
1182 C CA  . SER A 162 ? 0.36399 0.41245 0.40781 0.09770  0.01508  -0.00324 169 SER A CA  
1183 C C   . SER A 162 ? 0.33886 0.35894 0.36867 0.08643  0.01184  -0.00557 169 SER A C   
1184 O O   . SER A 162 ? 0.32418 0.33031 0.35067 0.08368  0.00665  -0.00306 169 SER A O   
1185 C CB  . SER A 162 ? 0.32783 0.36718 0.36519 0.11503  0.02178  -0.00685 169 SER A CB  
1186 O OG  . SER A 162 ? 0.40725 0.41498 0.43297 0.12198  0.02021  -0.00694 169 SER A OG  
1187 N N   . PHE A 163 ? 0.29060 0.30496 0.31216 0.08033  0.01515  -0.01009 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.33108 0.32309 0.34013 0.07060  0.01212  -0.01336 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.35834 0.34187 0.35420 0.07344  0.01731  -0.02095 170 PHE A C   
1190 O O   . PHE A 163 ? 0.36983 0.36809 0.36714 0.08076  0.02357  -0.02228 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.32349 0.32390 0.33765 0.05660  0.00789  -0.00977 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.34245 0.36128 0.36104 0.05230  0.01194  -0.00785 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.31738 0.36019 0.35193 0.05139  0.01391  -0.00340 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.35605 0.36930 0.36298 0.04831  0.01376  -0.00996 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.36607 0.42406 0.40546 0.04592  0.01907  -0.00020 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.38106 0.41023 0.39067 0.04465  0.01847  -0.00559 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.30276 0.35278 0.32895 0.04286  0.02181  -0.00019 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.35179 0.31350 0.33502 0.06776  0.01480  -0.02667 171 THR A N   
1199 C CA  . THR A 164 ? 0.33790 0.29176 0.30643 0.06907  0.01824  -0.03622 171 THR A CA  
1200 C C   . THR A 164 ? 0.38423 0.34064 0.34637 0.05698  0.01392  -0.03697 171 THR A C   
1201 O O   . THR A 164 ? 0.37673 0.33068 0.34371 0.04803  0.00812  -0.03268 171 THR A O   
1202 C CB  . THR A 164 ? 0.43553 0.36072 0.39384 0.07402  0.01943  -0.04539 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.45412 0.36138 0.41114 0.06363  0.01357  -0.04534 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.44650 0.36725 0.41038 0.08901  0.02409  -0.04332 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.40772 0.37067 0.35816 0.05809  0.01698  -0.04237 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.37492 0.34086 0.31637 0.04928  0.01253  -0.04373 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.46313 0.42096 0.38653 0.05184  0.01380  -0.05750 172 VAL A C   
1208 O O   . VAL A 165 ? 0.42323 0.38466 0.33979 0.06124  0.02072  -0.06276 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.38023 0.36845 0.32494 0.04718  0.01452  -0.03336 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.42142 0.41317 0.35430 0.04148  0.01007  -0.03414 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.40661 0.40047 0.36918 0.04246  0.01259  -0.02250 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.41499 0.36325 0.33133 0.04346  0.00727  -0.06455 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.48301 0.42692 0.38164 0.04338  0.00684  -0.07957 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.47692 0.43124 0.37007 0.03371  -0.00143 -0.08050 173 ARG A C   
1215 O O   . ARG A 166 ? 0.46763 0.42489 0.37174 0.02682  -0.00674 -0.07179 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.52258 0.43822 0.41833 0.04339  0.00776  -0.09292 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.58939 0.48910 0.49390 0.03183  0.00147  -0.09250 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.64798 0.51606 0.55327 0.03390  0.00537  -0.09975 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.81389 0.67761 0.73026 0.04352  0.00993  -0.08760 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.93865 0.77695 0.85701 0.04964  0.01431  -0.08841 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.83343 0.64320 0.74367 0.04685  0.01626  -0.10151 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.74714 0.58874 0.67572 0.05927  0.01696  -0.07592 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.48958 0.45164 0.36520 0.03428  -0.00256 -0.09164 174 THR A N   
1224 C CA  . THR A 167 ? 0.49359 0.46553 0.36348 0.02551  -0.01178 -0.09600 174 THR A CA  
1225 C C   . THR A 167 ? 0.56158 0.51406 0.43924 0.01498  -0.01684 -0.10554 174 THR A C   
1226 O O   . THR A 167 ? 0.59197 0.52114 0.46863 0.01515  -0.01299 -0.11628 174 THR A O   
1227 C CB  . THR A 167 ? 0.60476 0.58996 0.45242 0.02868  -0.01234 -0.10841 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.62129 0.62803 0.46192 0.03697  -0.00783 -0.09567 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.76394 0.76027 0.60601 0.01919  -0.02333 -0.11673 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.58005 0.54142 0.46632 0.00614  -0.02457 -0.10079 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.58282 0.52906 0.47877 -0.00532 -0.02845 -0.10774 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.81105 0.76175 0.69751 -0.01447 -0.03488 -0.12610 175 ASP A C   
1233 O O   . ASP A 168 ? 0.78747 0.76385 0.66635 -0.01484 -0.04145 -0.12737 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.56406 0.51895 0.47625 -0.01056 -0.03273 -0.09452 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.58843 0.52752 0.51136 -0.02214 -0.03435 -0.09990 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.80262 0.71575 0.72487 -0.02276 -0.02892 -0.10582 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.63622 0.58842 0.56840 -0.03014 -0.04025 -0.09775 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.88607 0.81180 0.77389 -0.02229 -0.03316 -0.13974 176 THR A N   
1239 C CA  . THR A 169 ? 1.10597 1.03178 0.98758 -0.03424 -0.03882 -0.16010 176 THR A CA  
1240 C C   . THR A 169 ? 0.92453 0.84839 0.82249 -0.05033 -0.04375 -0.16151 176 THR A C   
1241 O O   . THR A 169 ? 0.92804 0.85379 0.82441 -0.06315 -0.04887 -0.17899 176 THR A O   
1242 C CB  . THR A 169 ? 1.08700 0.98320 0.95730 -0.03261 -0.03210 -0.17750 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.98174 0.84500 0.86254 -0.03115 -0.02416 -0.17077 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.94031 0.84590 0.79284 -0.01734 -0.02770 -0.17930 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.82944 0.75160 0.74317 -0.05060 -0.04217 -0.14455 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.84239 0.76772 0.77224 -0.06495 -0.04587 -0.14385 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.87090 0.83351 0.80503 -0.07078 -0.05632 -0.14567 177 GLY A C   
1248 O O   . GLY A 170 ? 0.77389 0.75826 0.69543 -0.06592 -0.06193 -0.15161 177 GLY A O   
1249 N N   . GLU A 171 ? 0.83974 0.81178 0.79126 -0.08024 -0.05878 -0.14013 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.90204 0.91194 0.86070 -0.08454 -0.06868 -0.14095 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.72031 0.75249 0.67297 -0.06815 -0.07151 -0.12645 178 GLU A C   
1252 O O   . GLU A 171 ? 0.63016 0.65130 0.58475 -0.05823 -0.06553 -0.11112 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.91158 0.92715 0.89171 -0.09562 -0.06852 -0.13541 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.98242 1.03894 0.97479 -0.10266 -0.07857 -0.13892 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.26921 1.33777 1.26193 -0.11907 -0.08540 -0.16109 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.24283 1.29925 1.21899 -0.11950 -0.08607 -0.17511 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.01901 1.11100 1.02944 -0.13214 -0.09003 -0.16563 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.69681 0.75964 0.64156 -0.06483 -0.08023 -0.13054 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.61027 0.69375 0.55103 -0.04981 -0.08254 -0.11428 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.66082 0.75240 0.62063 -0.04839 -0.08246 -0.09967 179 PRO A C   
1261 O O   . PRO A 172 ? 0.64039 0.74396 0.61560 -0.05871 -0.08614 -0.10417 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.59002 0.70742 0.52034 -0.04901 -0.09327 -0.12312 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.62575 0.73413 0.54789 -0.06122 -0.09468 -0.14610 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.61115 0.68969 0.54824 -0.07434 -0.08810 -0.15091 179 PRO A CD  
1265 N N   . MET A 173 ? 0.50970 0.59530 0.46861 -0.03580 -0.07767 -0.08288 180 MET A N   
1266 C CA  . MET A 173 ? 0.61898 0.70568 0.59334 -0.03226 -0.07547 -0.06921 180 MET A CA  
1267 C C   . MET A 173 ? 0.55441 0.66932 0.53184 -0.02266 -0.08173 -0.05945 180 MET A C   
1268 O O   . MET A 173 ? 0.64055 0.76223 0.63308 -0.02117 -0.08166 -0.05215 180 MET A O   
1269 C CB  . MET A 173 ? 0.52726 0.58957 0.49852 -0.02469 -0.06654 -0.05845 180 MET A CB  
1270 C CG  . MET A 173 ? 0.70753 0.74463 0.68452 -0.03165 -0.06004 -0.06144 180 MET A CG  
1271 S SD  . MET A 173 ? 0.65703 0.67839 0.63400 -0.02117 -0.05233 -0.04708 180 MET A SD  
1272 C CE  . MET A 173 ? 0.45926 0.49608 0.45000 -0.01706 -0.05468 -0.03583 180 MET A CE  
1273 N N   . GLY A 174 ? 0.49069 0.62111 0.45318 -0.01450 -0.08624 -0.05808 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.47709 0.63160 0.44010 -0.00239 -0.09144 -0.04584 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.44516 0.58384 0.40323 0.01005  -0.08410 -0.02835 181 GLY A C   
1276 O O   . GLY A 174 ? 0.45199 0.59465 0.39396 0.01911  -0.08366 -0.02130 181 GLY A O   
1277 N N   . ARG A 175 ? 0.38626 0.50646 0.35776 0.00935  -0.07767 -0.02202 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.32207 0.42484 0.29276 0.01799  -0.07014 -0.00757 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.33189 0.41700 0.31815 0.01279  -0.06475 -0.00762 182 ARG A C   
1280 O O   . ARG A 175 ? 0.33908 0.43305 0.33850 0.00890  -0.06756 -0.01143 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.32885 0.44497 0.29869 0.03152  -0.07256 0.00708  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.34245 0.43706 0.31109 0.03875  -0.06363 0.02185  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.35270 0.45155 0.32759 0.05110  -0.06419 0.03613  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.35818 0.46103 0.35128 0.05002  -0.06629 0.03220  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.32522 0.45343 0.32520 0.05457  -0.07400 0.03064  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.33319 0.48647 0.32315 0.06091  -0.08178 0.03265  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.31527 0.44680 0.33271 0.05299  -0.07398 0.02662  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.32188 0.38517 0.30666 0.01269  -0.05709 -0.00371 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.31494 0.36420 0.31263 0.00933  -0.05258 -0.00295 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.39621 0.42776 0.39123 0.00335  -0.04745 -0.00793 183 GLY A C   
1291 O O   . GLY A 176 ? 0.35981 0.38719 0.34371 0.00392  -0.04559 -0.00979 183 GLY A O   
1292 N N   . THR A 177 ? 0.31312 0.33560 0.31787 -0.00119 -0.04489 -0.00981 184 THR A N   
1293 C CA  . THR A 177 ? 0.31644 0.32317 0.31973 -0.00469 -0.04019 -0.01246 184 THR A CA  
1294 C C   . THR A 177 ? 0.36730 0.37050 0.37687 -0.01211 -0.04034 -0.01821 184 THR A C   
1295 O O   . THR A 177 ? 0.34297 0.35372 0.36176 -0.01361 -0.04156 -0.01740 184 THR A O   
1296 C CB  . THR A 177 ? 0.34348 0.34197 0.35105 -0.00093 -0.03547 -0.00537 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.36092 0.36105 0.36239 0.00444  -0.03373 0.00090  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.38203 0.36914 0.38970 -0.00338 -0.03169 -0.00783 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.32085 0.31236 0.32515 -0.01612 -0.03833 -0.02353 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.34717 0.33017 0.35560 -0.02299 -0.03657 -0.02673 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.38474 0.35229 0.39052 -0.01990 -0.03175 -0.02378 185 LYS A C   
1302 O O   . LYS A 178 ? 0.35676 0.31611 0.35499 -0.01661 -0.02995 -0.02573 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.38469 0.36599 0.38930 -0.03079 -0.03862 -0.03612 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.50716 0.47300 0.51369 -0.03862 -0.03499 -0.03895 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.60899 0.57616 0.61618 -0.04988 -0.03741 -0.04939 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.60973 0.59087 0.61062 -0.04878 -0.04332 -0.05686 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.70183 0.68355 0.70281 -0.06109 -0.04605 -0.06995 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.33363 0.29957 0.34529 -0.02000 -0.02974 -0.01940 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.34261 0.29811 0.35228 -0.01650 -0.02629 -0.01612 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.38806 0.33244 0.39647 -0.02135 -0.02387 -0.01630 186 VAL A C   
1311 O O   . VAL A 179 ? 0.36310 0.31250 0.37637 -0.02608 -0.02349 -0.01477 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.29638 0.25906 0.31171 -0.01295 -0.02600 -0.01149 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.31384 0.27065 0.32732 -0.00907 -0.02370 -0.00844 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.35391 0.32368 0.37123 -0.00935 -0.02700 -0.01021 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.31515 0.24395 0.31706 -0.01962 -0.02133 -0.01756 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.37416 0.28652 0.37358 -0.02369 -0.01773 -0.01644 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.37292 0.27940 0.36979 -0.01540 -0.01506 -0.00865 187 ILE A C   
1318 O O   . ILE A 180 ? 0.38852 0.29076 0.38197 -0.00700 -0.01431 -0.00832 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.39587 0.29145 0.38934 -0.02686 -0.01634 -0.02405 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.43481 0.34231 0.43021 -0.03437 -0.02069 -0.03280 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.38216 0.25564 0.37370 -0.03215 -0.01124 -0.02186 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.52520 0.42106 0.51284 -0.03573 -0.02063 -0.04297 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.33992 0.24958 0.33846 -0.01700 -0.01371 -0.00234 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.37571 0.28325 0.37056 -0.00887 -0.01205 0.00567  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.36519 0.24993 0.35348 -0.00897 -0.00689 0.01091  188 LEU A C   
1326 O O   . LEU A 181 ? 0.43364 0.31276 0.42211 -0.01753 -0.00377 0.01336  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.32571 0.25003 0.32340 -0.00983 -0.01319 0.00937  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.33967 0.28189 0.34432 -0.01004 -0.01730 0.00410  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.38166 0.33783 0.38818 -0.01091 -0.01760 0.00574  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.36215 0.30854 0.36774 -0.00268 -0.01935 0.00322  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.40487 0.27594 0.38807 0.00059  -0.00515 0.01293  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.45419 0.29984 0.43034 0.00366  0.00051  0.01994  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.45193 0.30596 0.42433 0.01226  0.00071  0.03229  189 HIS A C   
1334 O O   . HIS A 182 ? 0.44998 0.31427 0.42178 0.02450  -0.00184 0.03529  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.45228 0.27961 0.42454 0.01233  0.00260  0.01607  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.45834 0.28186 0.43203 0.00519  0.00157  0.00254  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.53689 0.33657 0.50783 -0.00380 0.00515  -0.00400 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.47986 0.32134 0.45669 0.00533  -0.00262 -0.00557 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.54303 0.34848 0.51455 -0.00824 0.00227  -0.01657 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.51403 0.34445 0.48840 -0.00218 -0.00213 -0.01659 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.41501 0.26795 0.38500 0.00579  0.00368  0.03926  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.43485 0.30435 0.40054 0.01227  0.00254  0.04888  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.50559 0.36157 0.46180 0.02607  0.00531  0.06150  190 LEU A C   
1344 O O   . LEU A 183 ? 0.51472 0.34100 0.46622 0.02721  0.01134  0.06637  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.40821 0.28243 0.37322 0.00138  0.00608  0.05260  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.37953 0.27354 0.35439 -0.00909 0.00284  0.04175  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.43458 0.33798 0.40852 -0.01662 0.00706  0.04668  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.40441 0.32119 0.38370 -0.00308 -0.00424 0.03504  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.44251 0.32075 0.39604 0.03687  0.00079  0.06663  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.48678 0.35892 0.43041 0.05158  0.00244  0.08090  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.51362 0.36856 0.44709 0.04717  0.00990  0.09386  191 LYS A C   
1352 O O   . LYS A 184 ? 0.47727 0.33834 0.41203 0.03393  0.01198  0.09160  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.52828 0.43490 0.47155 0.06144  -0.00516 0.08226  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.52602 0.45208 0.48097 0.06528  -0.01174 0.07077  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.53274 0.49572 0.48967 0.06943  -0.01956 0.06892  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.61105 0.59408 0.58184 0.06979  -0.02500 0.05740  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.50643 0.52493 0.48234 0.06899  -0.03265 0.05144  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.54458 0.37871 0.46800 0.05928  0.01460  0.10869  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.59477 0.40645 0.50798 0.05493  0.02377  0.12340  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.63433 0.47230 0.54048 0.05156  0.02330  0.13023  192 GLU A C   
1361 O O   . GLU A 185 ? 0.59681 0.42512 0.50008 0.03946  0.03091  0.13573  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.70612 0.49106 0.60870 0.07197  0.02867  0.14004  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.96954 0.71557 0.86440 0.06468  0.04093  0.15334  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.18845 0.90155 1.07301 0.08284  0.04675  0.17006  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.08960 0.79070 0.97863 0.09408  0.04467  0.16355  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.26690 0.96570 1.13854 0.08656  0.05417  0.19035  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.54694 0.41943 0.45066 0.06119  0.01489  0.12893  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.58982 0.48786 0.48472 0.05903  0.01450  0.13374  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.55623 0.47872 0.46144 0.04576  0.01040  0.11630  193 ASP A C   
1370 O O   . ASP A 186 ? 0.50318 0.45209 0.40211 0.04585  0.00827  0.11579  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.64471 0.56784 0.52848 0.07711  0.00779  0.14250  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.69199 0.64073 0.58681 0.08326  -0.00348 0.12825  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.68192 0.62440 0.59151 0.07567  -0.00513 0.11401  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.85363 0.83073 0.74227 0.09536  -0.01067 0.13148  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.49287 0.40708 0.41266 0.03527  0.00953  0.10214  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.48156 0.41633 0.41139 0.02462  0.00604  0.08703  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.45917 0.38119 0.39614 0.00890  0.01272  0.08359  194 GLN A C   
1378 O O   . GLN A 187 ? 0.45018 0.38113 0.39904 0.00070  0.00980  0.07016  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.44397 0.38836 0.38539 0.02698  -0.00219 0.07313  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.41858 0.38051 0.35605 0.04128  -0.00906 0.07554  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.49123 0.48161 0.42098 0.04375  -0.01256 0.07566  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.46108 0.46245 0.39340 0.03470  -0.01204 0.06739  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.44327 0.44739 0.36352 0.05688  -0.01647 0.08409  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.51673 0.41878 0.44734 0.00442  0.02185  0.09604  195 THR A N   
1385 C CA  . THR A 188 ? 0.49786 0.38920 0.43805 -0.01206 0.02795  0.09174  195 THR A CA  
1386 C C   . THR A 188 ? 0.52326 0.43951 0.46637 -0.02052 0.03063  0.08904  195 THR A C   
1387 O O   . THR A 188 ? 0.47659 0.39107 0.42993 -0.03430 0.03527  0.08490  195 THR A O   
1388 C CB  . THR A 188 ? 0.55622 0.41396 0.49133 -0.01655 0.03778  0.10464  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.53508 0.39348 0.45542 -0.01106 0.04426  0.12267  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.62073 0.45218 0.55382 -0.00688 0.03561  0.10512  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.46517 0.40662 0.40033 -0.01255 0.02766  0.08983  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.52061 0.48702 0.45960 -0.01897 0.02983  0.08375  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.39938 0.37457 0.35568 -0.02550 0.02476  0.06673  196 GLU A C   
1394 O O   . GLU A 189 ? 0.42818 0.41787 0.39264 -0.03332 0.02826  0.06169  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.49025 0.48182 0.41677 -0.00836 0.02633  0.08400  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.41715 0.41888 0.34717 -0.00024 0.01510  0.07181  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.53770 0.56302 0.45421 0.00985  0.01091  0.07190  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.56325 0.58630 0.46831 0.01987  0.00847  0.08213  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.51070 0.55722 0.42785 0.00834  0.01001  0.06137  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.38568 0.35375 0.34776 -0.02156 0.01698  0.05856  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.41805 0.39399 0.39458 -0.02604 0.01207  0.04436  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.42763 0.39160 0.41481 -0.03762 0.01501  0.04191  197 TYR A C   
1403 O O   . TYR A 190 ? 0.41103 0.38086 0.40931 -0.04066 0.01056  0.03149  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.35118 0.32640 0.32904 -0.01781 0.00360  0.03760  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.33616 0.32781 0.30573 -0.00857 -0.00001 0.03758  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.39905 0.41084 0.36995 -0.00900 -0.00050 0.03030  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.37963 0.36780 0.34004 0.00083  -0.00276 0.04433  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.38263 0.41042 0.34516 -0.00185 -0.00404 0.02801  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.40485 0.41215 0.35799 0.00834  -0.00697 0.04326  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.45067 0.47738 0.40465 0.00607  -0.00775 0.03421  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.41384 0.46029 0.36029 0.01223  -0.01235 0.03042  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.39831 0.34581 0.38213 -0.04436 0.02243  0.05138  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.42016 0.36028 0.41517 -0.05848 0.02616  0.04804  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.46136 0.41965 0.46245 -0.06815 0.03348  0.05073  198 LEU A C   
1415 O O   . LEU A 191 ? 0.51001 0.46850 0.52307 -0.08147 0.03663  0.04728  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.43481 0.34201 0.42467 -0.06246 0.03098  0.05525  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.44813 0.33713 0.43295 -0.05244 0.02502  0.05207  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.58098 0.43477 0.56068 -0.05535 0.03094  0.05832  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.47681 0.37554 0.47192 -0.05415 0.01716  0.03706  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.44875 0.42398 0.44190 -0.06213 0.03659  0.05637  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.46835 0.46175 0.46571 -0.07042 0.04549  0.06043  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.42260 0.44479 0.43343 -0.07012 0.04177  0.04752  199 GLU A C   
1423 O O   . GLU A 192 ? 0.36449 0.39643 0.37270 -0.05915 0.03493  0.04011  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.53058 0.53031 0.51078 -0.06346 0.05181  0.07295  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.66118 0.63440 0.62508 -0.05854 0.05464  0.08790  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.93585 0.88827 0.90164 -0.07197 0.06591  0.09988  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.93977 0.90668 0.91662 -0.08486 0.07331  0.09919  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.01562 0.93730 0.97264 -0.06963 0.06792  0.10997  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.45358 0.48971 0.47941 -0.08210 0.04687  0.04523  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.43544 0.49937 0.47629 -0.08078 0.04346  0.03357  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.35195 0.43628 0.38572 -0.06904 0.04483  0.03165  200 GLU A C   
1432 O O   . GLU A 193 ? 0.36574 0.45971 0.40349 -0.05990 0.03817  0.02142  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.46889 0.54905 0.52746 -0.09585 0.05000  0.03318  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.60681 0.72236 0.68044 -0.09263 0.04978  0.02451  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.81186 0.94722 0.90717 -0.10785 0.05366  0.02204  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.70073 0.82524 0.79777 -0.12308 0.06100  0.02939  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.84300 1.00445 0.95428 -0.10458 0.04921  0.01275  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.35319 0.44327 0.37540 -0.06903 0.05388  0.04129  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.34333 0.45527 0.35852 -0.05839 0.05544  0.03681  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.30973 0.41184 0.31154 -0.04558 0.04642  0.03186  201 ARG A C   
1441 O O   . ARG A 194 ? 0.36826 0.48439 0.36978 -0.03682 0.04352  0.02135  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.43344 0.55699 0.43764 -0.06127 0.06781  0.04849  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.50777 0.60862 0.49305 -0.06125 0.07026  0.06355  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.62107 0.73377 0.59685 -0.06600 0.08433  0.07754  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.78088 0.87534 0.73380 -0.06095 0.08646  0.09326  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.86665 0.96900 0.80410 -0.06112 0.09776  0.10816  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.66338 0.79267 0.60584 -0.06664 0.10862  0.10855  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.84065 0.92550 0.75670 -0.05431 0.09839  0.12354  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.35965 0.43788 0.35186 -0.04449 0.04203  0.03833  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.31128 0.38337 0.29370 -0.03356 0.03316  0.03335  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.35416 0.42396 0.34996 -0.03135 0.02450  0.02033  202 ARG A C   
1452 O O   . ARG A 195 ? 0.31347 0.38959 0.30766 -0.02364 0.01943  0.01096  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.41509 0.46491 0.38547 -0.03184 0.03148  0.04469  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.36807 0.41516 0.33055 -0.02128 0.02222  0.04013  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.42524 0.49327 0.37317 -0.01332 0.02262  0.03854  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.38938 0.45661 0.32946 -0.00466 0.01386  0.03588  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.42413 0.50441 0.36497 -0.00010 0.00749  0.02221  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.34566 0.43877 0.29236 -0.00133 0.00931  0.01015  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.40364 0.48402 0.34041 0.00576  -0.00056 0.02011  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.32268 0.38323 0.33115 -0.03837 0.02294  0.01957  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.31473 0.37428 0.33426 -0.03548 0.01528  0.00921  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.27578 0.35609 0.30455 -0.03150 0.01630  0.00027  203 ILE A C   
1463 O O   . ILE A 196 ? 0.32942 0.40965 0.36031 -0.02414 0.01117  -0.00799 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.31193 0.36020 0.34115 -0.04347 0.01310  0.00978  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.36640 0.39064 0.38570 -0.04436 0.01180  0.01653  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.27168 0.32231 0.31080 -0.03933 0.00570  0.00062  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.43515 0.44574 0.46095 -0.05504 0.01280  0.01783  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.27929 0.37719 0.31441 -0.03610 0.02367  0.00193  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.31650 0.43555 0.36097 -0.03029 0.02557  -0.00663 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.33241 0.45373 0.36528 -0.02022 0.02522  -0.01297 204 LYS A C   
1471 O O   . LYS A 197 ? 0.30246 0.42617 0.34071 -0.01242 0.02215  -0.02291 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.35282 0.49442 0.40525 -0.03656 0.03512  -0.00319 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.47466 0.62227 0.54395 -0.04705 0.03526  -0.00122 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.51261 0.68671 0.59134 -0.05375 0.04577  0.00180  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.66790 0.85424 0.76740 -0.06491 0.04480  0.00095  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.69111 0.89661 0.79889 -0.07770 0.05614  0.00733  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.29508 0.41506 0.31135 -0.02019 0.02827  -0.00739 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.32471 0.45015 0.32851 -0.01162 0.02732  -0.01500 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.31320 0.42375 0.31790 -0.00689 0.01782  -0.02344 205 GLU A C   
1480 O O   . GLU A 198 ? 0.31479 0.42886 0.32017 -0.00058 0.01626  -0.03557 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.32894 0.45633 0.31349 -0.01234 0.03090  -0.00512 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.35221 0.48908 0.32109 -0.00429 0.02917  -0.01298 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.39904 0.53682 0.34757 -0.00352 0.03037  -0.00071 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.39366 0.51503 0.34085 -0.00675 0.02811  0.01111  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.37302 0.52835 0.30613 0.00128  0.03397  -0.00264 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.27780 0.37109 0.28320 -0.01026 0.01226  -0.01752 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.30374 0.38448 0.31018 -0.00701 0.00431  -0.02377 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.34194 0.41914 0.36297 -0.00481 0.00218  -0.03165 206 ILE A C   
1489 O O   . ILE A 199 ? 0.33822 0.41038 0.36086 -0.00071 -0.00112 -0.04072 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.33453 0.40004 0.33787 -0.01023 0.00039  -0.01464 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.36252 0.43076 0.35005 -0.00921 0.00212  -0.00618 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.31268 0.36751 0.32008 -0.00798 -0.00675 -0.02016 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.36051 0.41249 0.34562 -0.01142 0.00064  0.00452  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.30951 0.38895 0.34149 -0.00771 0.00387  -0.02789 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.31215 0.39018 0.35712 -0.00367 0.00159  -0.03321 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.34639 0.43438 0.39411 0.00404  0.00526  -0.04295 207 VAL A C   
1497 O O   . VAL A 200 ? 0.36029 0.43882 0.41138 0.00976  0.00291  -0.05020 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.27862 0.36311 0.33449 -0.00813 0.00197  -0.02783 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.29874 0.38810 0.36770 -0.00106 0.00011  -0.03241 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.30781 0.37776 0.36079 -0.01473 -0.00233 -0.02127 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.31071 0.41679 0.35632 0.00429  0.01202  -0.04338 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.37040 0.48673 0.41697 0.01277  0.01654  -0.05416 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.35575 0.46127 0.39168 0.01616  0.01394  -0.06418 208 LYS A C   
1504 O O   . LYS A 201 ? 0.39551 0.49638 0.43557 0.02334  0.01466  -0.07531 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.34214 0.48214 0.38570 0.01212  0.02535  -0.05265 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.54471 0.69898 0.59892 0.00484  0.02909  -0.04236 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.79658 0.94591 0.86708 0.00376  0.02329  -0.03986 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.48571 0.63714 0.56023 -0.00867 0.02309  -0.02955 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.83268 0.98610 0.92202 -0.01040 0.01767  -0.02848 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.40029 0.50167 0.42327 0.01127  0.01082  -0.06095 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.37714 0.47458 0.39057 0.01346  0.00794  -0.07220 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.38889 0.46605 0.41038 0.01318  0.00190  -0.07744 209 LYS A C   
1513 O O   . LYS A 202 ? 0.40686 0.47775 0.42901 0.01612  0.00153  -0.09074 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.43163 0.53581 0.42893 0.00977  0.00600  -0.06628 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.53342 0.63800 0.52097 0.01062  0.00086  -0.07765 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.57418 0.69106 0.54477 0.00956  -0.00066 -0.06934 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.75787 0.88171 0.71875 0.01033  -0.00699 -0.08108 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.76359 0.90141 0.70745 0.01150  -0.00945 -0.07078 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.36773 0.43385 0.39536 0.00929  -0.00207 -0.06754 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.41771 0.46653 0.45083 0.00759  -0.00715 -0.06981 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.43518 0.47208 0.48096 0.01003  -0.00726 -0.06589 210 HIS A C   
1522 O O   . HIS A 203 ? 0.42005 0.44160 0.47075 0.00947  -0.00963 -0.06816 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.36577 0.41218 0.39361 0.00207  -0.01200 -0.06160 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.47863 0.53646 0.49384 0.00102  -0.01370 -0.06446 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.49292 0.55333 0.50528 0.00083  -0.01613 -0.07749 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.46904 0.53682 0.47321 0.00044  -0.01348 -0.05570 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.53964 0.61474 0.53922 0.00079  -0.01827 -0.07685 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.46719 0.54595 0.46116 0.00132  -0.01638 -0.06256 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.50870 0.47405 0.30519 -0.05314 -0.04905 -0.03164 211 SER A N   
1530 C CA  . SER A 204 ? 0.46502 0.43125 0.30090 -0.04244 -0.03405 -0.03157 211 SER A CA  
1531 C C   . SER A 204 ? 0.47748 0.42909 0.29900 -0.02820 -0.00815 -0.03865 211 SER A C   
1532 O O   . SER A 204 ? 0.50723 0.46705 0.35958 -0.01610 0.00344  -0.03251 211 SER A O   
1533 C CB  . SER A 204 ? 0.48564 0.48126 0.36764 -0.03711 -0.03825 -0.01342 211 SER A CB  
1534 O OG  . SER A 204 ? 0.45839 0.46968 0.36396 -0.04751 -0.06078 -0.00851 211 SER A OG  
1535 N N   . GLN A 205 ? 0.55839 0.48938 0.33455 -0.02935 0.00097  -0.05299 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.61593 0.54078 0.38494 -0.01376 0.02763  -0.05924 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.61682 0.52188 0.40798 -0.00134 0.03941  -0.06857 212 GLN A C   
1538 O O   . GLN A 205 ? 0.64342 0.55158 0.44691 0.01543  0.05879  -0.06972 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.70634 0.61460 0.41905 -0.01851 0.03800  -0.07468 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.75886 0.63000 0.44119 -0.02543 0.03702  -0.09962 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.03871 0.89383 0.65728 -0.03350 0.04587  -0.11715 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.02662 0.88463 0.63014 -0.02301 0.07216  -0.12232 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.99084 0.83121 0.57120 -0.05363 0.02422  -0.12727 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.60507 0.49083 0.40429 -0.00923 0.02792  -0.07353 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.54929 0.40809 0.36302 0.00145  0.03786  -0.07979 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.56016 0.42940 0.41225 0.00166  0.03007  -0.06376 213 PHE A C   
1547 O O   . PHE A 206 ? 0.59424 0.43693 0.45415 0.00613  0.03367  -0.06516 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.57199 0.38771 0.35614 -0.00895 0.03636  -0.10119 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.62534 0.42395 0.36663 -0.00695 0.04934  -0.12189 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.63334 0.43438 0.37667 0.01409  0.07316  -0.12615 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.70865 0.49120 0.40817 -0.02688 0.03825  -0.13826 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.68808 0.47427 0.39043 0.01557  0.09025  -0.14782 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.84841 0.61364 0.50012 -0.02670 0.05216  -0.15962 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.78227 0.54884 0.43471 -0.00527 0.08039  -0.16488 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.50374 0.40819 0.37755 -0.00310 0.02054  -0.04868 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.47442 0.39180 0.38099 -0.00293 0.01671  -0.03551 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.46830 0.38311 0.38823 0.01579  0.02810  -0.02949 214 ILE A C   
1558 O O   . ILE A 207 ? 0.50137 0.42962 0.42415 0.02941  0.03744  -0.02893 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.38185 0.33646 0.30966 -0.00852 0.00754  -0.02404 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.45114 0.40977 0.37280 -0.02556 -0.00815 -0.02801 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.42441 0.39414 0.38257 -0.00674 0.00809  -0.01344 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.48762 0.43903 0.42380 -0.03975 -0.01516 -0.03135 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.47848 0.37702 0.40727 0.01565  0.02682  -0.02389 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.44570 0.33350 0.38285 0.03406  0.03334  -0.01774 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.47525 0.39584 0.43589 0.04065  0.03039  -0.00311 215 GLY A C   
1566 O O   . GLY A 208 ? 0.47007 0.38230 0.43716 0.04984  0.02872  0.00656  215 GLY A O   
1567 N N   . TYR A 209 ? 0.40409 0.35946 0.37595 0.03543  0.02825  -0.00112 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.36277 0.34956 0.35650 0.03878  0.02548  0.00884  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.37510 0.38938 0.37900 0.04170  0.02961  0.00748  216 TYR A C   
1570 O O   . TYR A 209 ? 0.38328 0.39550 0.37419 0.03490  0.03079  0.00206  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.36150 0.35804 0.36089 0.02330  0.01910  0.01281  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.41026 0.38038 0.39725 0.01681  0.01799  0.01601  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.39165 0.35536 0.37577 0.02364  0.01615  0.02632  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.36602 0.31609 0.34286 0.00268  0.01777  0.00989  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.45412 0.38791 0.42129 0.01625  0.01595  0.03267  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.37645 0.29922 0.34189 -0.00615 0.01900  0.01399  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.40610 0.31875 0.36463 0.00082  0.01904  0.02642  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.47533 0.35678 0.41782 -0.00946 0.02088  0.03390  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.38802 0.42761 0.41345 0.05001  0.03094  0.01316  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.34435 0.40918 0.38125 0.04962  0.03667  0.01355  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.33213 0.40571 0.37007 0.03501  0.03058  0.01608  217 PRO A C   
1582 O O   . PRO A 210 ? 0.35941 0.43892 0.40836 0.02824  0.02329  0.01841  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.35294 0.44417 0.41866 0.05820  0.03620  0.01896  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.40458 0.48603 0.46959 0.06121  0.02637  0.02319  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.33221 0.37804 0.37121 0.05815  0.02562  0.02047  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.30045 0.37397 0.32613 0.03073  0.03400  0.01564  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.32205 0.40229 0.35076 0.01967  0.02642  0.02100  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.37661 0.47517 0.41718 0.01954  0.03344  0.02826  218 ILE A C   
1589 O O   . ILE A 211 ? 0.35751 0.45595 0.38207 0.02139  0.04420  0.02855  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.40236 0.46569 0.40327 0.01248  0.02021  0.01832  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.36699 0.41256 0.36064 0.00902  0.01382  0.01045  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.34971 0.42125 0.35687 0.00393  0.00945  0.02764  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.42421 0.45343 0.38946 0.00043  0.00616  0.00465  218 ILE A CD1 
1594 N N   . THR A 212 ? 0.29051 0.40369 0.35831 0.01575  0.02940  0.03299  219 THR A N   
1595 C CA  . THR A 212 ? 0.29375 0.42232 0.37722 0.01264  0.03596  0.04021  219 THR A CA  
1596 C C   . THR A 212 ? 0.25974 0.38189 0.34482 0.00373  0.02800  0.04919  219 THR A C   
1597 O O   . THR A 212 ? 0.27064 0.39065 0.37226 0.00125  0.01802  0.04758  219 THR A O   
1598 C CB  . THR A 212 ? 0.28187 0.42986 0.39705 0.01378  0.03618  0.03783  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.27869 0.43236 0.39444 0.02431  0.03930  0.03239  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.26662 0.43107 0.40239 0.00745  0.04379  0.04441  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.28666 0.40514 0.35472 -0.00065 0.03305  0.05900  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.32185 0.43138 0.39061 -0.00805 0.02383  0.07242  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.31565 0.43423 0.41246 -0.01370 0.03102  0.07979  220 LEU A C   
1604 O O   . LEU A 213 ? 0.34648 0.47389 0.43869 -0.01723 0.04585  0.08422  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.33979 0.43646 0.36582 -0.01207 0.02336  0.08152  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.39131 0.47645 0.41064 -0.01978 0.01323  0.10173  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.32789 0.40746 0.37448 -0.01752 -0.00808 0.10455  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.40258 0.47513 0.36730 -0.02596 0.01324  0.11178  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.30066 0.41759 0.42890 -0.01545 0.02234  0.07886  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.32236 0.44297 0.47915 -0.02301 0.02748  0.08347  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.34638 0.45017 0.49230 -0.03076 0.02714  0.10455  221 PHE A C   
1612 O O   . PHE A 214 ? 0.43685 0.52415 0.56643 -0.02874 0.01455  0.11478  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.27825 0.39634 0.46813 -0.02278 0.01918  0.07321  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.22718 0.36185 0.42645 -0.01951 0.02077  0.05469  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.25001 0.39264 0.42818 -0.01228 0.02232  0.04892  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.27085 0.40979 0.49723 -0.02463 0.02004  0.04367  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.27468 0.42894 0.45800 -0.00953 0.02134  0.03615  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.29002 0.44331 0.51789 -0.02342 0.01924  0.02858  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.26269 0.42364 0.46833 -0.01550 0.01916  0.02693  221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.26543 0.37377 0.42091 -0.04057 0.03962  0.11238  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.31913 0.40765 0.46278 -0.05059 0.04073  0.13566  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.34819 0.42189 0.53149 -0.05637 0.03469  0.13904  222 VAL A C   
1623 O O   . VAL A 215 ? 0.36183 0.44696 0.57921 -0.05677 0.03589  0.12138  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.47362 0.57464 0.59913 -0.06054 0.06265  0.14359  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.51840 0.63358 0.61171 -0.05199 0.07050  0.13286  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.40794 0.53212 0.57315 -0.06591 0.07402  0.13236  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.38619 0.43159 0.56393 -0.06033 0.02637  0.16095  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.45669 0.48158 0.67499 -0.06413 0.02081  0.16285  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.45787 0.47917 0.69087 -0.08246 0.03651  0.17149  223 GLU A C   
1630 O O   . GLU A 216 ? 0.45565 0.48116 0.66210 -0.09328 0.05010  0.18749  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.55398 0.54684 0.77121 -0.05743 0.00170  0.18269  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.53481 0.53540 0.74287 -0.04183 -0.01443 0.17512  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.63503 0.61056 0.86646 -0.03234 -0.03511 0.18814  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.69093 0.65068 0.96621 -0.03130 -0.03457 0.18243  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.71937 0.69121 0.92791 -0.02574 -0.05252 0.20275  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.49825 0.51188 0.77450 -0.08760 0.03602  0.15894  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.46400 0.47797 0.76228 -0.10783 0.05037  0.16201  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.64819 0.62169 0.94278 -0.12002 0.05116  0.19311  224 LYS A C   
1639 O O   . LYS A 217 ? 0.71226 0.68808 1.00670 -0.13963 0.06754  0.20580  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.43008 0.45037 0.77240 -0.11188 0.04870  0.13381  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.42326 0.47603 0.76514 -0.09923 0.04413  0.10574  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.41633 0.47603 0.79256 -0.10717 0.04261  0.07869  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.38445 0.41467 0.77573 -0.09799 0.03292  0.06586  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.37538 0.40890 0.74607 -0.07779 0.02523  0.06497  224 LYS A NZ  
1645 N N   . GLU A 218 ? 0.70285 0.64016 0.99620 -0.10909 0.03393  0.20720  225 GLU A N   
1646 C CA  . GLU A 218 ? 0.86230 0.75477 1.15198 -0.11913 0.03118  0.24062  225 GLU A CA  
1647 C C   . GLU A 218 ? 0.86138 0.75467 1.09391 -0.12657 0.03742  0.27104  225 GLU A C   
1648 O O   . GLU A 218 ? 0.97955 0.84651 1.19155 -0.13978 0.04308  0.29372  225 GLU A O   
1649 C CB  . GLU A 218 ? 0.79023 0.64472 1.09949 -0.10174 0.00808  0.24862  225 GLU A CB  
1650 C CG  . GLU A 218 ? 1.20261 1.05485 1.56469 -0.09135 0.00345  0.21519  225 GLU A CG  
1651 C CD  . GLU A 218 ? 1.23674 1.13326 1.59756 -0.07899 0.00388  0.18163  225 GLU A CD  
1652 O OE1 . GLU A 218 ? 1.24429 1.16348 1.56970 -0.07026 -0.00071 0.18677  225 GLU A OE1 
1653 O OE2 . GLU A 218 ? 1.01035 0.91653 1.40239 -0.07942 0.00873  0.15026  225 GLU A OE2 
# 
