data_9BSO
# 
_entry.id   9BSO 
# 
_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   9BSO         pdb_00009bso 10.2210/pdb9bso/pdb 
WWPDB D_1000284066 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_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.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BSO 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wliu@chem.tamu.edu 
_pdbx_contact_author.name_first         Wenshe 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7078-6534 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Blankenship, L.R.' 1 0000-0002-1714-4399 
'Liu, W.R.'         2 0000-0002-7078-6534 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of the SARS-CoV-2 main protease' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Blankenship, L.R.' 1 ? 
primary 'Liu, W.R.'         2 ? 
# 
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 '3C-like proteinase nsp5'                                                               33825.547 1   3.4.22.69 
? ? ? 
2 non-polymer syn "N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-3-sulfanylpropanamide" 403.325   1   ?         
? ? ? 
3 water       nat water                                                                                   18.015    241 ?         
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-3-sulfanylpropanamide" A1ARW 
3 water                                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1ARW non-polymer         . "N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-3-sulfanylpropanamide" ? 
'C20 H16 Cl2 N2 O S' 403.325 
ALA   'L-peptide linking' y ALANINE                                                                                 ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                                ? 
'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                              ? 
'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                         ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                ? 
'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                               ? 
'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                         ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                                 ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                               ? 
'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER                                                                                   ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                              ? 
'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                 ? 
'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE                                                                                  ? 
'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE                                                                              ? 
'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                           ? 
'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE                                                                                 ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                                  ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                               ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                              ? 
'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                ? 
'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE                                                                                  ? 
'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ARW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ARW 
_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 A1ARW 1   401 401 A1ARW LIG A . 
C 3 HOH   1   501 151 HOH   HOH A . 
C 3 HOH   2   502 122 HOH   HOH A . 
C 3 HOH   3   503 179 HOH   HOH A . 
C 3 HOH   4   504 25  HOH   HOH A . 
C 3 HOH   5   505 226 HOH   HOH A . 
C 3 HOH   6   506 142 HOH   HOH A . 
C 3 HOH   7   507 182 HOH   HOH A . 
C 3 HOH   8   508 65  HOH   HOH A . 
C 3 HOH   9   509 117 HOH   HOH A . 
C 3 HOH   10  510 69  HOH   HOH A . 
C 3 HOH   11  511 172 HOH   HOH A . 
C 3 HOH   12  512 39  HOH   HOH A . 
C 3 HOH   13  513 155 HOH   HOH A . 
C 3 HOH   14  514 202 HOH   HOH A . 
C 3 HOH   15  515 33  HOH   HOH A . 
C 3 HOH   16  516 62  HOH   HOH A . 
C 3 HOH   17  517 51  HOH   HOH A . 
C 3 HOH   18  518 239 HOH   HOH A . 
C 3 HOH   19  519 150 HOH   HOH A . 
C 3 HOH   20  520 116 HOH   HOH A . 
C 3 HOH   21  521 140 HOH   HOH A . 
C 3 HOH   22  522 115 HOH   HOH A . 
C 3 HOH   23  523 147 HOH   HOH A . 
C 3 HOH   24  524 84  HOH   HOH A . 
C 3 HOH   25  525 120 HOH   HOH A . 
C 3 HOH   26  526 175 HOH   HOH A . 
C 3 HOH   27  527 82  HOH   HOH A . 
C 3 HOH   28  528 29  HOH   HOH A . 
C 3 HOH   29  529 187 HOH   HOH A . 
C 3 HOH   30  530 148 HOH   HOH A . 
C 3 HOH   31  531 57  HOH   HOH A . 
C 3 HOH   32  532 32  HOH   HOH A . 
C 3 HOH   33  533 63  HOH   HOH A . 
C 3 HOH   34  534 30  HOH   HOH A . 
C 3 HOH   35  535 194 HOH   HOH A . 
C 3 HOH   36  536 124 HOH   HOH A . 
C 3 HOH   37  537 91  HOH   HOH A . 
C 3 HOH   38  538 86  HOH   HOH A . 
C 3 HOH   39  539 129 HOH   HOH A . 
C 3 HOH   40  540 12  HOH   HOH A . 
C 3 HOH   41  541 71  HOH   HOH A . 
C 3 HOH   42  542 75  HOH   HOH A . 
C 3 HOH   43  543 90  HOH   HOH A . 
C 3 HOH   44  544 28  HOH   HOH A . 
C 3 HOH   45  545 21  HOH   HOH A . 
C 3 HOH   46  546 238 HOH   HOH A . 
C 3 HOH   47  547 170 HOH   HOH A . 
C 3 HOH   48  548 153 HOH   HOH A . 
C 3 HOH   49  549 112 HOH   HOH A . 
C 3 HOH   50  550 88  HOH   HOH A . 
C 3 HOH   51  551 100 HOH   HOH A . 
C 3 HOH   52  552 5   HOH   HOH A . 
C 3 HOH   53  553 55  HOH   HOH A . 
C 3 HOH   54  554 223 HOH   HOH A . 
C 3 HOH   55  555 97  HOH   HOH A . 
C 3 HOH   56  556 77  HOH   HOH A . 
C 3 HOH   57  557 68  HOH   HOH A . 
C 3 HOH   58  558 169 HOH   HOH A . 
C 3 HOH   59  559 126 HOH   HOH A . 
C 3 HOH   60  560 14  HOH   HOH A . 
C 3 HOH   61  561 54  HOH   HOH A . 
C 3 HOH   62  562 232 HOH   HOH A . 
C 3 HOH   63  563 207 HOH   HOH A . 
C 3 HOH   64  564 3   HOH   HOH A . 
C 3 HOH   65  565 204 HOH   HOH A . 
C 3 HOH   66  566 89  HOH   HOH A . 
C 3 HOH   67  567 80  HOH   HOH A . 
C 3 HOH   68  568 171 HOH   HOH A . 
C 3 HOH   69  569 41  HOH   HOH A . 
C 3 HOH   70  570 87  HOH   HOH A . 
C 3 HOH   71  571 114 HOH   HOH A . 
C 3 HOH   72  572 190 HOH   HOH A . 
C 3 HOH   73  573 141 HOH   HOH A . 
C 3 HOH   74  574 162 HOH   HOH A . 
C 3 HOH   75  575 27  HOH   HOH A . 
C 3 HOH   76  576 23  HOH   HOH A . 
C 3 HOH   77  577 98  HOH   HOH A . 
C 3 HOH   78  578 73  HOH   HOH A . 
C 3 HOH   79  579 15  HOH   HOH A . 
C 3 HOH   80  580 17  HOH   HOH A . 
C 3 HOH   81  581 231 HOH   HOH A . 
C 3 HOH   82  582 125 HOH   HOH A . 
C 3 HOH   83  583 101 HOH   HOH A . 
C 3 HOH   84  584 6   HOH   HOH A . 
C 3 HOH   85  585 121 HOH   HOH A . 
C 3 HOH   86  586 105 HOH   HOH A . 
C 3 HOH   87  587 46  HOH   HOH A . 
C 3 HOH   88  588 44  HOH   HOH A . 
C 3 HOH   89  589 227 HOH   HOH A . 
C 3 HOH   90  590 36  HOH   HOH A . 
C 3 HOH   91  591 37  HOH   HOH A . 
C 3 HOH   92  592 144 HOH   HOH A . 
C 3 HOH   93  593 19  HOH   HOH A . 
C 3 HOH   94  594 13  HOH   HOH A . 
C 3 HOH   95  595 78  HOH   HOH A . 
C 3 HOH   96  596 76  HOH   HOH A . 
C 3 HOH   97  597 59  HOH   HOH A . 
C 3 HOH   98  598 215 HOH   HOH A . 
C 3 HOH   99  599 131 HOH   HOH A . 
C 3 HOH   100 600 92  HOH   HOH A . 
C 3 HOH   101 601 60  HOH   HOH A . 
C 3 HOH   102 602 35  HOH   HOH A . 
C 3 HOH   103 603 74  HOH   HOH A . 
C 3 HOH   104 604 106 HOH   HOH A . 
C 3 HOH   105 605 108 HOH   HOH A . 
C 3 HOH   106 606 146 HOH   HOH A . 
C 3 HOH   107 607 166 HOH   HOH A . 
C 3 HOH   108 608 93  HOH   HOH A . 
C 3 HOH   109 609 18  HOH   HOH A . 
C 3 HOH   110 610 4   HOH   HOH A . 
C 3 HOH   111 611 118 HOH   HOH A . 
C 3 HOH   112 612 200 HOH   HOH A . 
C 3 HOH   113 613 31  HOH   HOH A . 
C 3 HOH   114 614 8   HOH   HOH A . 
C 3 HOH   115 615 81  HOH   HOH A . 
C 3 HOH   116 616 127 HOH   HOH A . 
C 3 HOH   117 617 45  HOH   HOH A . 
C 3 HOH   118 618 22  HOH   HOH A . 
C 3 HOH   119 619 221 HOH   HOH A . 
C 3 HOH   120 620 154 HOH   HOH A . 
C 3 HOH   121 621 26  HOH   HOH A . 
C 3 HOH   122 622 72  HOH   HOH A . 
C 3 HOH   123 623 47  HOH   HOH A . 
C 3 HOH   124 624 10  HOH   HOH A . 
C 3 HOH   125 625 16  HOH   HOH A . 
C 3 HOH   126 626 20  HOH   HOH A . 
C 3 HOH   127 627 1   HOH   HOH A . 
C 3 HOH   128 628 52  HOH   HOH A . 
C 3 HOH   129 629 83  HOH   HOH A . 
C 3 HOH   130 630 96  HOH   HOH A . 
C 3 HOH   131 631 128 HOH   HOH A . 
C 3 HOH   132 632 235 HOH   HOH A . 
C 3 HOH   133 633 113 HOH   HOH A . 
C 3 HOH   134 634 192 HOH   HOH A . 
C 3 HOH   135 635 109 HOH   HOH A . 
C 3 HOH   136 636 66  HOH   HOH A . 
C 3 HOH   137 637 160 HOH   HOH A . 
C 3 HOH   138 638 61  HOH   HOH A . 
C 3 HOH   139 639 99  HOH   HOH A . 
C 3 HOH   140 640 42  HOH   HOH A . 
C 3 HOH   141 641 58  HOH   HOH A . 
C 3 HOH   142 642 130 HOH   HOH A . 
C 3 HOH   143 643 103 HOH   HOH A . 
C 3 HOH   144 644 188 HOH   HOH A . 
C 3 HOH   145 645 152 HOH   HOH A . 
C 3 HOH   146 646 184 HOH   HOH A . 
C 3 HOH   147 647 38  HOH   HOH A . 
C 3 HOH   148 648 9   HOH   HOH A . 
C 3 HOH   149 649 168 HOH   HOH A . 
C 3 HOH   150 650 137 HOH   HOH A . 
C 3 HOH   151 651 225 HOH   HOH A . 
C 3 HOH   152 652 7   HOH   HOH A . 
C 3 HOH   153 653 157 HOH   HOH A . 
C 3 HOH   154 654 220 HOH   HOH A . 
C 3 HOH   155 655 183 HOH   HOH A . 
C 3 HOH   156 656 70  HOH   HOH A . 
C 3 HOH   157 657 237 HOH   HOH A . 
C 3 HOH   158 658 138 HOH   HOH A . 
C 3 HOH   159 659 111 HOH   HOH A . 
C 3 HOH   160 660 143 HOH   HOH A . 
C 3 HOH   161 661 11  HOH   HOH A . 
C 3 HOH   162 662 123 HOH   HOH A . 
C 3 HOH   163 663 2   HOH   HOH A . 
C 3 HOH   164 664 205 HOH   HOH A . 
C 3 HOH   165 665 24  HOH   HOH A . 
C 3 HOH   166 666 43  HOH   HOH A . 
C 3 HOH   167 667 53  HOH   HOH A . 
C 3 HOH   168 668 107 HOH   HOH A . 
C 3 HOH   169 669 210 HOH   HOH A . 
C 3 HOH   170 670 40  HOH   HOH A . 
C 3 HOH   171 671 185 HOH   HOH A . 
C 3 HOH   172 672 212 HOH   HOH A . 
C 3 HOH   173 673 229 HOH   HOH A . 
C 3 HOH   174 674 48  HOH   HOH A . 
C 3 HOH   175 675 164 HOH   HOH A . 
C 3 HOH   176 676 49  HOH   HOH A . 
C 3 HOH   177 677 64  HOH   HOH A . 
C 3 HOH   178 678 195 HOH   HOH A . 
C 3 HOH   179 679 186 HOH   HOH A . 
C 3 HOH   180 680 173 HOH   HOH A . 
C 3 HOH   181 681 218 HOH   HOH A . 
C 3 HOH   182 682 189 HOH   HOH A . 
C 3 HOH   183 683 145 HOH   HOH A . 
C 3 HOH   184 684 174 HOH   HOH A . 
C 3 HOH   185 685 230 HOH   HOH A . 
C 3 HOH   186 686 197 HOH   HOH A . 
C 3 HOH   187 687 196 HOH   HOH A . 
C 3 HOH   188 688 193 HOH   HOH A . 
C 3 HOH   189 689 203 HOH   HOH A . 
C 3 HOH   190 690 209 HOH   HOH A . 
C 3 HOH   191 691 85  HOH   HOH A . 
C 3 HOH   192 692 79  HOH   HOH A . 
C 3 HOH   193 693 134 HOH   HOH A . 
C 3 HOH   194 694 136 HOH   HOH A . 
C 3 HOH   195 695 50  HOH   HOH A . 
C 3 HOH   196 696 213 HOH   HOH A . 
C 3 HOH   197 697 208 HOH   HOH A . 
C 3 HOH   198 698 199 HOH   HOH A . 
C 3 HOH   199 699 110 HOH   HOH A . 
C 3 HOH   200 700 241 HOH   HOH A . 
C 3 HOH   201 701 224 HOH   HOH A . 
C 3 HOH   202 702 201 HOH   HOH A . 
C 3 HOH   203 703 95  HOH   HOH A . 
C 3 HOH   204 704 119 HOH   HOH A . 
C 3 HOH   205 705 132 HOH   HOH A . 
C 3 HOH   206 706 158 HOH   HOH A . 
C 3 HOH   207 707 102 HOH   HOH A . 
C 3 HOH   208 708 180 HOH   HOH A . 
C 3 HOH   209 709 167 HOH   HOH A . 
C 3 HOH   210 710 181 HOH   HOH A . 
C 3 HOH   211 711 177 HOH   HOH A . 
C 3 HOH   212 712 135 HOH   HOH A . 
C 3 HOH   213 713 56  HOH   HOH A . 
C 3 HOH   214 714 133 HOH   HOH A . 
C 3 HOH   215 715 161 HOH   HOH A . 
C 3 HOH   216 716 159 HOH   HOH A . 
C 3 HOH   217 717 165 HOH   HOH A . 
C 3 HOH   218 718 236 HOH   HOH A . 
C 3 HOH   219 719 211 HOH   HOH A . 
C 3 HOH   220 720 222 HOH   HOH A . 
C 3 HOH   221 721 198 HOH   HOH A . 
C 3 HOH   222 722 191 HOH   HOH A . 
C 3 HOH   223 723 234 HOH   HOH A . 
C 3 HOH   224 724 67  HOH   HOH A . 
C 3 HOH   225 725 139 HOH   HOH A . 
C 3 HOH   226 726 104 HOH   HOH A . 
C 3 HOH   227 727 214 HOH   HOH A . 
C 3 HOH   228 728 176 HOH   HOH A . 
C 3 HOH   229 729 178 HOH   HOH A . 
C 3 HOH   230 730 156 HOH   HOH A . 
C 3 HOH   231 731 163 HOH   HOH A . 
C 3 HOH   232 732 228 HOH   HOH A . 
C 3 HOH   233 733 34  HOH   HOH A . 
C 3 HOH   234 734 206 HOH   HOH A . 
C 3 HOH   235 735 94  HOH   HOH A . 
C 3 HOH   236 736 217 HOH   HOH A . 
C 3 HOH   237 737 149 HOH   HOH A . 
C 3 HOH   238 738 216 HOH   HOH A . 
C 3 HOH   239 739 240 HOH   HOH A . 
C 3 HOH   240 740 233 HOH   HOH A . 
C 3 HOH   241 741 219 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? 1.20.1_4487 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT    ? ? ? .           2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless        ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.460 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BSO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.747 
_cell.length_a_esd                 ? 
_cell.length_b                     82.360 
_cell.length_b_esd                 ? 
_cell.length_c                     89.965 
_cell.length_c_esd                 ? 
_cell.volume                       380985.825 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BSO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y (x,y,-x+z)' 
_symmetry.space_group_name_H-M             'I 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BSO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.54 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M Ammonium phosphate dibasic, 17%
W/v PEG3350, pH8.0
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     120 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'Bruker PHOTON II' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54301 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-002' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54301 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          15.94 
_reflns.entry_id                                       9BSO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.7 
_reflns.d_resolution_low                               24.22 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     40208 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.44 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.68 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.08457 
_reflns.pdbx_Rpim_I_all                                0.03283 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07735 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.7 
_reflns_shell.d_res_low                                     1.761 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.61 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3874 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.8461 
_reflns_shell.pdbx_Rpim_I_all                               0.4318 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.891 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.7568 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.31 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BSO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             24.22 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     40183 
_refine.ls_number_reflns_R_free                  2014 
_refine.ls_number_reflns_R_work                  38169 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.48 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2493 
_refine.ls_R_factor_R_free                       0.2703 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2482 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.2400 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2381 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        24.22 
_refine_hist.number_atoms_solvent             241 
_refine_hist.number_atoms_total               2633 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2367 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0091 ? 2447 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1253 ? 3326 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0572 ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0100 ? 432  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.2523 ? 331  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.74  . . 149 2588 93.73 . . . . 0.3842 . . . . . . . . . . . 0.4358 
'X-RAY DIFFRACTION' 1.74 1.79  . . 164 2656 95.37 . . . . 0.3529 . . . . . . . . . . . 0.3791 
'X-RAY DIFFRACTION' 1.79 1.84  . . 133 2658 95.42 . . . . 0.3513 . . . . . . . . . . . 0.3715 
'X-RAY DIFFRACTION' 1.84 1.90  . . 142 2653 95.17 . . . . 0.3337 . . . . . . . . . . . 0.3733 
'X-RAY DIFFRACTION' 1.90 1.97  . . 134 2631 95.18 . . . . 0.3146 . . . . . . . . . . . 0.2806 
'X-RAY DIFFRACTION' 1.97 2.05  . . 136 2723 97.78 . . . . 0.3065 . . . . . . . . . . . 0.3306 
'X-RAY DIFFRACTION' 2.05 2.14  . . 140 2791 98.55 . . . . 0.2905 . . . . . . . . . . . 0.3056 
'X-RAY DIFFRACTION' 2.14 2.25  . . 122 2778 99.11 . . . . 0.2965 . . . . . . . . . . . 0.3314 
'X-RAY DIFFRACTION' 2.25 2.40  . . 135 2753 99.01 . . . . 0.2793 . . . . . . . . . . . 0.3249 
'X-RAY DIFFRACTION' 2.40 2.58  . . 152 2780 99.12 . . . . 0.2785 . . . . . . . . . . . 0.3247 
'X-RAY DIFFRACTION' 2.58 2.84  . . 147 2794 99.49 . . . . 0.2582 . . . . . . . . . . . 0.2486 
'X-RAY DIFFRACTION' 2.84 3.25  . . 153 2782 99.49 . . . . 0.2220 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 3.25 4.09  . . 161 2788 99.63 . . . . 0.1843 . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 4.09 24.22 . . 146 2794 97.67 . . . . 0.1723 . . . . . . . . . . . 0.2088 
# 
_struct.entry_id                     9BSO 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor SR-B-13' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BSO 
_struct_keywords.text            'main protease, VIRAL PROTEIN, Hydrolase' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
# 
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                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BSO 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4820  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  24900 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_455 -x-1,y,-z -1.0000000000 0.0000000000 0.0000000000 -51.7470000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1ARW 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C20 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1ARW 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.607 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1ARW 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1ARW 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C20 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1ARW 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9BSO 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD2 A ASP 245 ? ? O  A HOH   501 ? ? 1.88 
2  1 O   A HOH 556 ? ? O  A HOH   727 ? ? 1.89 
3  1 SG  A CYS 145 ? ? C4 A A1ARW 401 ? ? 1.91 
4  1 O   A HOH 529 ? ? O  A HOH   661 ? ? 2.03 
5  1 O   A HOH 683 ? ? O  A HOH   709 ? ? 2.04 
6  1 OD1 A ASN 142 ? ? O  A HOH   502 ? ? 2.04 
7  1 O   A HOH 555 ? ? O  A HOH   705 ? ? 2.06 
8  1 O   A CYS 300 ? ? O  A HOH   503 ? ? 2.07 
9  1 O   A HOH 678 ? ? O  A HOH   687 ? ? 2.09 
10 1 O   A HOH 524 ? ? O  A HOH   725 ? ? 2.09 
11 1 O   A ALA 194 ? ? O  A HOH   504 ? ? 2.10 
12 1 O   A HOH 700 ? ? O  A HOH   726 ? ? 2.14 
13 1 O   A HOH 581 ? ? O  A HOH   673 ? ? 2.16 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 507 ? ? 1_555 O A HOH 628 ? ? 2_455 2.09 
2 1 O A HOH 589 ? ? 1_555 O A HOH 710 ? ? 2_455 2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 50.94  -131.05 
2 1 HIS A 41  ? ? -69.81 4.94    
3 1 LEU A 50  ? ? -68.44 -71.50  
4 1 ASN A 84  ? ? 49.54  -118.81 
5 1 TYR A 154 ? ? 46.99  -97.04  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 545 ? C HOH . 
2 1 A HOH 663 ? C HOH . 
3 1 A HOH 735 ? C HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -x,y,-z             
3 x+1/2,y+1/2,z+1/2   
4 -x+1/2,y+1/2,-z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -12.9381208442 
_pdbx_refine_tls.origin_y         -14.6184432469 
_pdbx_refine_tls.origin_z         -1.02415863183 
_pdbx_refine_tls.T[1][1]          0.0589722288421 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.00266214764853 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0235344068005 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.103136877016 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.00274082917877 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0202230406247 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.25711281913 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.352459463769 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.305590471404 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.83781444625 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.525155586395 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.5090784573 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0239373789814 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0104504205169 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.00495014215243 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0927309339918 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0415751078328 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0439051939374 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0314445004252 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0454054534238 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0210924257773 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   B 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     401 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 
A1ARW N1   N  N N 1   
A1ARW C4   C  N N 2   
A1ARW C5   C  Y N 3   
A1ARW C6   C  Y N 4   
A1ARW C7   C  Y N 5   
A1ARW C8   C  Y N 6   
A1ARW C10  C  Y N 7   
A1ARW C13  C  Y N 8   
A1ARW C15  C  Y N 9   
A1ARW C17  C  Y N 10  
A1ARW C20  C  N N 11  
A1ARW C1   C  Y N 12  
A1ARW C11  C  Y N 13  
A1ARW C12  C  Y N 14  
A1ARW C14  C  Y N 15  
A1ARW C16  C  Y N 16  
A1ARW C18  C  Y N 17  
A1ARW C19  C  Y N 18  
A1ARW C2   C  Y N 19  
A1ARW C3   C  N N 20  
A1ARW C9   C  Y N 21  
A1ARW N2   N  Y N 22  
A1ARW O1   O  N N 23  
A1ARW CL1  CL N N 24  
A1ARW CL2  CL N N 25  
A1ARW H1   H  N N 26  
A1ARW H2   H  N N 27  
A1ARW H3   H  N N 28  
A1ARW H4   H  N N 29  
A1ARW H5   H  N N 30  
A1ARW H8   H  N N 31  
A1ARW H10  H  N N 32  
A1ARW H14  H  N N 33  
A1ARW H15  H  N N 34  
A1ARW H7   H  N N 35  
A1ARW H9   H  N N 36  
A1ARW H11  H  N N 37  
A1ARW H12  H  N N 38  
A1ARW H13  H  N N 39  
A1ARW H6   H  N N 40  
A1ARW S1   S  N N 41  
A1ARW HS   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TRP   N    N  N N 363 
TRP   CA   C  N S 364 
TRP   C    C  N N 365 
TRP   O    O  N N 366 
TRP   CB   C  N N 367 
TRP   CG   C  Y N 368 
TRP   CD1  C  Y N 369 
TRP   CD2  C  Y N 370 
TRP   NE1  N  Y N 371 
TRP   CE2  C  Y N 372 
TRP   CE3  C  Y N 373 
TRP   CZ2  C  Y N 374 
TRP   CZ3  C  Y N 375 
TRP   CH2  C  Y N 376 
TRP   OXT  O  N N 377 
TRP   H    H  N N 378 
TRP   H2   H  N N 379 
TRP   HA   H  N N 380 
TRP   HB2  H  N N 381 
TRP   HB3  H  N N 382 
TRP   HD1  H  N N 383 
TRP   HE1  H  N N 384 
TRP   HE3  H  N N 385 
TRP   HZ2  H  N N 386 
TRP   HZ3  H  N N 387 
TRP   HH2  H  N N 388 
TRP   HXT  H  N N 389 
TYR   N    N  N N 390 
TYR   CA   C  N S 391 
TYR   C    C  N N 392 
TYR   O    O  N N 393 
TYR   CB   C  N N 394 
TYR   CG   C  Y N 395 
TYR   CD1  C  Y N 396 
TYR   CD2  C  Y N 397 
TYR   CE1  C  Y N 398 
TYR   CE2  C  Y N 399 
TYR   CZ   C  Y N 400 
TYR   OH   O  N N 401 
TYR   OXT  O  N N 402 
TYR   H    H  N N 403 
TYR   H2   H  N N 404 
TYR   HA   H  N N 405 
TYR   HB2  H  N N 406 
TYR   HB3  H  N N 407 
TYR   HD1  H  N N 408 
TYR   HD2  H  N N 409 
TYR   HE1  H  N N 410 
TYR   HE2  H  N N 411 
TYR   HH   H  N N 412 
TYR   HXT  H  N N 413 
VAL   N    N  N N 414 
VAL   CA   C  N S 415 
VAL   C    C  N N 416 
VAL   O    O  N N 417 
VAL   CB   C  N N 418 
VAL   CG1  C  N N 419 
VAL   CG2  C  N N 420 
VAL   OXT  O  N N 421 
VAL   H    H  N N 422 
VAL   H2   H  N N 423 
VAL   HA   H  N N 424 
VAL   HB   H  N N 425 
VAL   HG11 H  N N 426 
VAL   HG12 H  N N 427 
VAL   HG13 H  N N 428 
VAL   HG21 H  N N 429 
VAL   HG22 H  N N 430 
VAL   HG23 H  N N 431 
VAL   HXT  H  N N 432 
# 
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 
A1ARW C1  N1   sing N N 1   
A1ARW C1  C16  doub Y N 2   
A1ARW C1  C19  sing Y N 3   
A1ARW N1  C2   sing N N 4   
A1ARW N1  C3   sing N N 5   
A1ARW C2  C5   doub Y N 6   
A1ARW C2  C9   sing Y N 7   
A1ARW C3  C4   sing N N 8   
A1ARW C3  O1   doub N N 9   
A1ARW C4  C20  sing N N 10  
A1ARW C5  C6   sing Y N 11  
A1ARW C6  C7   doub Y N 12  
A1ARW C6  C10  sing N N 13  
A1ARW C7  C8   sing Y N 14  
A1ARW C8  C9   doub Y N 15  
A1ARW C10 C11  doub Y N 16  
A1ARW C10 C15  sing Y N 17  
A1ARW C11 C12  sing Y N 18  
A1ARW C12 C13  doub Y N 19  
A1ARW C12 CL1  sing N N 20  
A1ARW C13 C14  sing Y N 21  
A1ARW C14 C15  doub Y N 22  
A1ARW C16 C17  sing Y N 23  
A1ARW C17 C18  doub Y N 24  
A1ARW C17 CL2  sing N N 25  
A1ARW C18 N2   sing Y N 26  
A1ARW N2  C19  doub Y N 27  
A1ARW C4  H1   sing N N 28  
A1ARW C4  H2   sing N N 29  
A1ARW C5  H3   sing N N 30  
A1ARW C7  H4   sing N N 31  
A1ARW C8  H5   sing N N 32  
A1ARW C13 H8   sing N N 33  
A1ARW C15 H10  sing N N 34  
A1ARW C20 H14  sing N N 35  
A1ARW C20 H15  sing N N 36  
A1ARW C11 H7   sing N N 37  
A1ARW C14 H9   sing N N 38  
A1ARW C16 H11  sing N N 39  
A1ARW C18 H12  sing N N 40  
A1ARW C19 H13  sing N N 41  
A1ARW C9  H6   sing N N 42  
A1ARW C20 S1   sing N N 43  
A1ARW S1  HS   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_pdbx_audit_support.funding_organization   'Welch Foundation' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7JPY 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 1 2 1' 
_space_group.name_Hall        'C 2y (x,y,-x+z)' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BSO 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019325 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002188 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012142 
_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]   0.011186 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 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   . SER   A 1 1   ? -33.40681 -18.83451 15.08540  1.000 23.18636 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -32.55732 -19.88879 14.56287  1.000 23.75256 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -32.55714 -19.97445 13.03333  1.000 24.16445 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -33.05213 -19.07822 12.33027  1.000 23.05340 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -32.97391 -21.22755 15.13059  1.000 28.37030 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -34.15071 -21.67969 14.49202  1.000 30.94367 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -32.01627 -21.07874 12.52934  1.000 22.20777 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -31.71917 -21.19866 11.12351  1.000 22.43198 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -30.25358 -20.92013 10.85447  1.000 22.32309 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -29.53160 -20.35325 11.68123  1.000 21.32182 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -29.80493 -21.34021 9.67852   1.000 21.23666 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -28.40403 -21.17019 9.32096   1.000 19.75809 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -28.27914 -21.05502 7.81729   1.000 23.06205 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -28.59745 -22.00155 7.08688   1.000 24.30080 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -27.52607 -22.30673 9.83766   1.000 23.59191 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -26.08205 -21.89152 10.01208  1.000 19.85906 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -25.68968 -21.13270 11.11277  1.000 23.90501 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -25.14437 -22.18968 9.04385   1.000 22.42902 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -24.37258 -20.71781 11.26194  1.000 23.19751 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -23.82600 -21.77678 9.17992   1.000 20.98254 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -23.44071 -21.03546 10.30008  1.000 20.95901 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -27.81351 -19.89306 7.37048   1.000 21.06540 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -27.73781 -19.55775 5.96390   1.000 17.15419 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -26.33077 -19.12656 5.59899   1.000 16.71490 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -25.57100 -18.60956 6.42324   1.000 19.61434 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -28.68666 -18.44710 5.59391   1.000 19.26896 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -30.10998 -18.90663 5.49620   1.000 17.55269 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -30.38809 -19.42762 4.08865   1.000 19.95751 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -31.80760 -19.67812 3.82446   1.000 23.23683 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -32.22005 -20.47848 2.84962   1.000 23.91026 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -31.35916 -21.01037 1.98603   1.000 25.71721 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -33.51361 -20.74116 2.72620   1.000 21.23470 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -26.03337 -19.26774 4.32256   1.000 17.56542 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -24.78819 -18.73015 3.78703   1.000 16.41194 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -24.95418 -17.22053 3.60551   1.000 19.67955 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -25.45566 -16.75747 2.58007   1.000 24.23644 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -24.45536 -19.43892 2.48446   1.000 20.96912 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -22.98625 -19.70500 2.31681   1.000 21.92529 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -22.80014 -20.68814 1.18916   1.000 27.08594 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -21.54585 -21.49482 1.38641   1.000 24.49558 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -21.37516 -21.93622 2.77848   1.000 22.85022 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -24.55707 -16.45620 4.62463   1.000 14.52699 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -24.89438 -15.04303 4.78209   1.000 15.26053 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? -23.75837 -14.12701 4.36478   1.000 15.78170 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? -22.64079 -14.27062 4.85586   1.000 15.48536 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -25.21971 -14.74417 6.24461   1.000 15.61396 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -26.13796 -13.58549 6.41700   1.000 18.74625 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -26.57233 -13.47031 8.14738   1.000 27.82180 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -28.08534 -14.41983 8.18251   1.000 21.85321 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? -24.05637 -13.16037 3.51114   1.000 16.13684 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? -23.07073 -12.16823 3.10901   1.000 10.11111 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? -23.21322 -10.92526 3.98220   1.000 11.50750 ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? -24.23417 -10.73432 4.65071   1.000 13.69552 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? -23.25144 -11.80281 1.63795   1.000 14.07705 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? -22.16605 -10.08050 3.98714   1.000 13.05024 ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? -22.29262 -8.76497  4.60659   1.000 13.20239 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? -23.17945 -7.84768  3.77020   1.000 11.04656 ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? -23.27195 -7.99488  2.55545   1.000 11.55305 ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? -20.91743 -8.10938  4.77647   1.000 12.25006 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? -20.09387 -8.76122  5.82836   1.000 15.86581 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? -20.31392 -8.47562  7.16240   1.000 18.09111 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? -19.10644 -9.66642  5.49237   1.000 14.37447 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? -19.56378 -9.08508  8.15090   1.000 23.77207 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? -18.34104 -10.28251 6.49406   1.000 17.17424 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? -18.57492 -9.98228  7.82202   1.000 20.13291 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? -23.85809 -6.89558  4.40206   1.000 15.05747 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? -24.59309 -5.90105  3.61787   1.000 16.45607 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? -23.62598 -5.21153  2.66718   1.000 13.96810 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? -22.48551 -4.88506  3.03962   1.000 16.01097 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? -25.15714 -4.94559  4.67772   1.000 15.43034 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? -25.13283 -5.72916  5.98855   1.000 15.32993 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? -23.93875 -6.67133  5.85166   1.000 15.41506 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? -24.06296 -5.04684  1.40967   1.000 12.06954 ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? -23.15747 -4.64910  0.31956   1.000 13.84481 ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? -23.14242 -3.15248  0.04918   1.000 14.83747 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? -22.30852 -2.69985  -0.74139  1.000 12.71508 ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? -23.50439 -5.38685  -0.98488  1.000 10.59401 ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? -24.87239 -5.21618  -1.33987  1.000 13.50960 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? -24.02605 -2.38764  0.69067   1.000 13.91065 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? -24.18755 -0.97627  0.34580   1.000 14.24957 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? -22.87894 -0.21051  0.28528   1.000 16.09005 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? -22.64488 0.56937   -0.64745  1.000 17.40441 ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? -22.03167 -0.38512  1.30709   1.000 13.55550 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? -20.81363 0.41479   1.40933   1.000 16.90738 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? -19.88872 0.14564   0.24279   1.000 16.61027 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? -19.10421 1.02333   -0.14502  1.000 20.43458 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? -20.08975 0.12901   2.73162   1.000 15.17776 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? -20.69460 0.80835   3.94380   1.000 20.64772 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? -20.00595 0.37135   5.23230   1.000 25.06158 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? -20.53375 1.15392   6.44136   1.000 29.29274 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? -22.01160 1.04212   6.61915   1.000 32.53126 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? -19.92970 -1.06438  -0.30415  1.000 13.10236 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? -19.09166 -1.38286  -1.46681  1.000 17.78216 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? -19.76058 -0.95173  -2.76973  1.000 16.46815 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? -19.08836 -0.52149  -3.71034  1.000 17.16359 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? -18.76341 -2.88756  -1.45193  1.000 12.44747 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? -17.88097 -3.28437  -2.66915  1.000 15.61661 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? -18.03003 -3.22055  -0.15413  1.000 13.63086 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? -21.09337 -1.06356  -2.84905  1.000 12.40340 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? -21.79780 -0.60917  -4.04427  1.000 13.35441 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? -21.42960 0.81835   -4.39006  1.000 14.47066 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? -21.29129 1.15379   -5.56737  1.000 17.38624 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? -23.32497 -0.70771  -3.87355  1.000 14.52340 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? -23.83811 -2.15055  -3.69084  1.000 13.31416 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? -25.27201 -2.18265  -3.23000  1.000 14.71338 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? -26.09647 -1.46350  -3.81861  1.000 17.29076 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? -25.55704 -2.90715  -2.26173  1.000 15.51761 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? -21.26886 1.68171   -3.37839  1.000 16.39508 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? -20.96297 3.07892   -3.65814  1.000 16.32137 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? -19.57604 3.33678   -4.18919  1.000 18.71907 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? -19.24438 4.48596   -4.50408  1.000 18.22382 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? -18.76343 2.29763   -4.29103  1.000 14.95367 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? -17.39596 2.39148   -4.76917  1.000 16.00077 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? -17.19289 1.79296   -6.14879  1.000 16.74319 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? -16.08262 1.88674   -6.68225  1.000 16.90742 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? -16.43644 1.68933   -3.79506  1.000 13.94897 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? -16.46195 2.33109   -2.09554  1.000 16.94124 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? -18.19268 1.13422   -6.72258  1.000 15.95389 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? -17.97114 0.43246   -7.97679  1.000 15.80961 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? -18.13221 1.38662   -9.13984  1.000 18.16914 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? -19.05584 2.20383   -9.16780  1.000 20.03429 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? -18.89667 -0.77228  -8.12263  1.000 16.84839 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? -18.73453 -1.78053  -6.99600  1.000 14.16294 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? -17.05255 -2.31040  -6.61899  1.000 13.40388 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? -16.44327 -2.85353  -8.21680  1.000 15.54666 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? -17.19676 1.29806   -10.08408 1.000 18.97907 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? -17.18897 2.11410   -11.28687 1.000 20.76298 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? -16.83190 1.22536   -12.46926 1.000 20.78543 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? -16.35048 0.10644   -12.31386 1.000 19.78743 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? -16.19248 3.28625   -11.18543 1.000 21.10562 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? -16.54349 4.17840   -10.00668 1.000 21.90399 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? -14.76695 2.75708   -11.06888 1.000 18.66785 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? -17.06265 1.75974   -13.66035 1.000 25.39184 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? -16.72294 1.11651   -14.92094 1.000 25.33802 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? -15.40761 1.69383   -15.43490 1.000 24.54182 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? -15.25046 2.91898   -15.50831 1.000 25.20400 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? -17.83969 1.37184   -15.92909 1.000 27.27707 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? -17.67334 0.77566   -17.29891 1.000 29.44868 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? -19.00962 0.66001   -18.01524 1.000 30.52131 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? -19.90037 1.49071   -17.82720 1.000 35.23783 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? -19.16018 -0.36634  -18.83375 1.000 34.53708 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? -14.47037 0.82559   -15.80571 1.000 20.27012 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? -13.20041 1.26489   -16.37694 1.000 25.56872 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? -13.06560 0.71504   -17.79013 1.000 23.29852 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? -13.20490 -0.49051  -18.01290 1.000 23.96560 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? -12.00534 0.84187   -15.50823 1.000 23.49509 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? -10.71735 1.29286   -16.16679 1.000 23.15289 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? -12.12643 1.45147   -14.13529 1.000 22.29436 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? -12.77590 1.59383   -18.74013 1.000 25.12683 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? -12.66912 1.20072   -20.13679 1.000 27.52522 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? -11.33360 1.66687   -20.70193 1.000 28.91958 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? -10.89816 2.79227   -20.44488 1.000 29.63528 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? -13.83770 1.77954   -20.96183 1.000 29.91307 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? -15.07047 1.23338   -20.47439 1.000 28.85023 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? -13.68963 1.43820   -22.43786 1.000 30.78085 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? -10.68881 0.79223   -21.47005 1.000 28.45745 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? -9.42671  1.12005   -22.12773 1.000 30.30389 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? -9.41377  0.35810   -23.44404 1.000 31.09433 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? -9.36580  -0.87407  -23.44085 1.000 31.90508 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? -8.23707  0.74890   -21.23901 1.000 28.65527 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? -6.59835  1.00829   -21.94410 1.000 36.72227 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? -9.48456  1.08396   -24.56092 1.000 31.64031 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? -9.64824  0.44940   -25.85516 1.000 31.51856 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? -11.03190 -0.14710  -25.99049 1.000 34.29296 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? -12.02836 0.55701   -25.80817 1.000 36.58088 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? -11.11548 -1.44127  -26.29452 1.000 36.35795 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? -12.39122 -2.14267  -26.32689 1.000 37.05155 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? -12.61165 -2.99200  -25.08760 1.000 35.52992 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? -13.59575 -3.73418  -25.02520 1.000 40.07788 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? -12.49852 -3.02465  -27.57242 1.000 36.81262 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? -11.35021 -3.87574  -27.65614 1.000 39.77176 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? -12.57406 -2.16525  -28.82471 1.000 37.22713 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? -11.71880 -2.90809  -24.10613 1.000 35.09284 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? -11.84530 -3.67668  -22.87528 1.000 34.70782 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? -12.57235 -2.85497  -21.81635 1.000 31.34251 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? -12.18296 -1.72231  -21.52168 1.000 31.64366 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? -10.47054 -4.10263  -22.36069 1.000 33.37631 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? -9.77644  -4.82091  -23.39179 1.000 36.90745 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? -10.61296 -4.98104  -21.11058 1.000 30.36576 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? -13.63170 -3.42444  -21.25396 1.000 31.38418 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? -14.37609 -2.78151  -20.17818 1.000 29.75392 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? -14.48413 -3.75563  -19.01001 1.000 26.96008 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? -14.85251 -4.91968  -19.20446 1.000 27.15649 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? -15.75490 -2.32889  -20.66597 1.000 28.98110 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? -15.61119 -1.21298  -21.56144 1.000 33.20951 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? -16.59944 -1.90139  -19.52223 1.000 28.50374 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? -14.11660 -3.29343  -17.81386 1.000 22.59140 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? -14.23808 -4.08656  -16.59416 1.000 23.57394 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? -14.56031 -3.15405  -15.42561 1.000 19.25217 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? -14.82817 -1.96138  -15.60423 1.000 22.16845 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? -12.96942 -4.91574  -16.32542 1.000 22.07934 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? -11.55940 -4.34068  -16.51661 1.000 23.44502 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? -11.26220 -3.21724  -15.52966 1.000 21.58135 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? -10.55717 -5.46692  -16.33983 1.000 22.09891 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? -14.54802 -3.70446  -14.22397 1.000 20.47451 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? -14.94966 -2.96207  -13.03960 1.000 17.55903 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? -13.74139 -2.37368  -12.33643 1.000 16.98771 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? -12.65443 -2.95157  -12.35113 1.000 17.01976 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? -15.70876 -3.87804  -12.08548 1.000 18.10551 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? -16.90524 -4.50180  -12.75404 1.000 18.15594 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? -17.93012 -3.84920  -12.92286 1.000 19.27347 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? -16.77551 -5.76858  -13.16546 1.000 17.94474 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? -13.95129 -1.21747  -11.70715 1.000 17.05769 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? -12.93684 -0.61585  -10.87081 1.000 16.72864 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? -13.49787 -0.31595  -9.49272  1.000 15.87918 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? -14.71389 -0.21575  -9.29761  1.000 14.31370 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? -12.59423 -0.15362  -8.53986  1.000 15.55832 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? -12.95221 0.20933   -7.16866  1.000 17.41725 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? -12.45550 1.61942   -6.86504  1.000 15.08621 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? -11.24180 1.88493   -6.87828  1.000 17.30102 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? -12.38723 -0.80677  -6.17971  1.000 13.78320 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? -12.70653 -0.61030  -4.69813  1.000 13.02857 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? -14.14686 -1.06580  -4.37639  1.000 13.60427 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? -11.67259 -1.32917  -3.83778  1.000 16.51906 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? -13.39333 2.52258   -6.57595  1.000 17.17737 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? -13.12039 3.95073   -6.43606  1.000 17.75822 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? -13.10533 4.29705   -4.94677  1.000 21.74501 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? -14.15389 4.29452   -4.29335  1.000 16.80564 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? -14.18866 4.75124   -7.18978  1.000 18.22502 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? -14.03851 6.26652   -7.19325  1.000 22.54939 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? -12.89068 6.98830   -7.00260  1.000 20.89046 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? -15.08116 7.22756   -7.42665  1.000 22.96936 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? -13.15827 8.33471   -7.09591  1.000 22.10361 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? -14.49291 8.51011   -7.35854  1.000 25.37305 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? -16.45501 7.12678   -7.68549  1.000 25.39521 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? -15.23238 9.68576   -7.53095  1.000 27.02251 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? -17.18606 8.28620   -7.85798  1.000 26.25340 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? -16.57630 9.55233   -7.77595  1.000 26.70026 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? -11.91897 4.60117   -4.41607  1.000 18.51426 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? -11.74302 4.98371   -3.02053  1.000 18.26083 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? -10.92872 6.26191   -2.98741  1.000 21.34789 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? -9.83755  6.31290   -3.56914  1.000 20.04277 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? -11.02236 3.90189   -2.21951  1.000 17.86675 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? -11.64504 2.52281   -2.26207  1.000 18.91382 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? -10.65291 1.47587   -1.77275  1.000 15.86594 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? -12.87347 2.54001   -1.40983  1.000 19.41372 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? -11.44170 7.27409   -2.28909  1.000 20.63979 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? -10.86023 8.61465   -2.30848  1.000 23.20432 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? -10.70052 8.98034   -3.78447  1.000 24.83750 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? -11.65353 8.80199   -4.55563  1.000 24.57517 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? -9.59068  8.64666   -1.46316  1.000 25.59275 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? -9.84117  8.22263   -0.02398  1.000 26.16957 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? -10.76929 8.77412   0.60297   1.000 30.46451 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? -9.12793  7.33458   0.48061   1.000 28.08415 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? -9.53865  9.46559   -4.22901  1.000 24.98527 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? -9.37376  9.83400   -5.62779  1.000 23.18520 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? -8.56002  8.81158   -6.42395  1.000 22.82284 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? -7.84751  9.17660   -7.36313  1.000 25.15775 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? -8.75112  11.22342  -5.73554  1.000 27.04428 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? -7.34123  11.28283  -5.18125  1.000 27.54655 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? -6.90933  10.33537  -4.48857  1.000 25.89796 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? -6.66743  12.30291  -5.43534  1.000 29.48782 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? -8.67040  7.53015   -6.08939  1.000 23.15178 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? -7.99129  6.48025   -6.83658  1.000 20.19988 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? -9.00587  5.41846   -7.23808  1.000 20.56446 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? -9.88175  5.03697   -6.44639  1.000 20.48422 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? -6.82528  5.85582   -6.03785  1.000 22.49026 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? -6.20867  4.69640   -6.81856  1.000 19.66972 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? -5.76282  6.90702   -5.71029  1.000 21.46118 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? -8.88400  4.94307   -8.47505  1.000 17.48236 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? -9.64958  3.81596   -8.98556  1.000 17.51060 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? -8.68686  2.65443   -9.15429  1.000 19.45312 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? -7.65217  2.79073   -9.82506  1.000 17.32346 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? -10.34246 4.13690   -10.32227 1.000 18.41813 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? -10.95972 2.86325   -10.89720 1.000 18.09302 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? -11.37581 5.25949   -10.16153 1.000 19.44889 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? -9.03464  1.52194   -8.56055  1.000 14.76814 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? -8.25247  0.29409   -8.61045  1.000 17.67816 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? -8.88476  -0.67770  -9.59380  1.000 15.27418 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? -10.10333 -0.85981  -9.59707  1.000 16.95740 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? -8.15804  -0.35430  -7.22155  1.000 12.01112 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? -7.51822  0.51885   -6.18028  1.000 16.93290 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? -8.23935  1.50517   -5.52701  1.000 17.90843 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? -6.15471  0.40041   -5.89140  1.000 17.71831 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? -7.62953  2.31783   -4.57766  1.000 18.88415 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? -5.55181  1.19157   -4.93333  1.000 17.31933 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? -6.29237  2.15531   -4.29009  1.000 18.65997 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? -5.70246  2.95921   -3.35198  1.000 20.01260 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? -8.06371  -1.31461  -10.42949 1.000 16.09479 ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? -8.63550  -2.26697  -11.37143 1.000 15.43572 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? -7.54658  -3.23374  -11.82441 1.000 17.35389 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? -6.35756  -2.95739  -11.64678 1.000 16.39999 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? -9.26871  -1.54018  -12.56909 1.000 14.95039 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? -8.11630  -0.86044  -13.78261 1.000 19.99294 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? -7.92540  -4.37702  -12.40491 1.000 14.99774 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? -6.91255  -5.31404  -12.91888 1.000 18.25612 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? -6.06789  -4.67969  -14.02738 1.000 18.11267 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? -6.59050  -4.00964  -14.92209 1.000 17.35720 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? -7.75512  -6.47789  -13.45568 1.000 15.02936 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? -9.06938  -6.39522  -12.67731 1.000 14.89732 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? -9.29589  -4.91705  -12.52730 1.000 17.27105 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? -4.74263  -4.88690  -13.96508 1.000 18.89967 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? -3.89073  -4.25602  -14.97472 1.000 15.91822 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? -4.11110  -4.81664  -16.37280 1.000 18.50819 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? -3.80861  -4.12610  -17.35528 1.000 22.13680 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? -2.41055  -4.37384  -14.59503 1.000 16.70813 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? -1.83046  -5.76522  -14.74252 1.000 15.96165 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? -0.32912  -5.78482  -14.38143 1.000 17.09840 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 0.19163   -7.15051  -14.39161 1.000 17.35074 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 1.48390   -7.44488  -14.28587 1.000 22.02094 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 2.39223   -6.50429  -14.11731 1.000 18.86830 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 1.87222   -8.71226  -14.36423 1.000 19.89803 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? -4.61621  -6.04198  -16.49762 1.000 20.37203 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? -4.80198  -6.51024  -17.86903 1.000 25.73870 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? -5.95719  -5.75082  -18.61696 1.000 24.53566 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? -6.24474  -6.11496  -19.76356 1.000 27.38500 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? -5.02493  -8.02496  -17.89006 1.000 23.54150 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? -6.22443  -8.46021  -17.12009 1.000 24.53134 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? -7.48557  -7.98826  -17.39707 1.000 27.80314 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? -6.35898  -9.30351  -16.06829 1.000 26.96074 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? -8.34092  -8.49938  -16.53461 1.000 27.97451 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? -7.69018  -9.32433  -15.73455 1.000 24.92624 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? -6.56449  -4.72725  -18.00109 1.000 24.42358 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? -7.44279  -3.81796  -18.74040 1.000 23.49468 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? -6.71671  -3.19344  -19.92839 1.000 24.08550 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? -7.35855  -2.80765  -20.91578 1.000 25.99451 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? -8.00161  -2.71314  -17.82055 1.000 23.04347 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? -6.91031  -1.70497  -17.48872 1.000 21.98343 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? -9.18775  -2.01863  -18.47702 1.000 24.10261 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? -5.38097  -3.06859  -19.86393 1.000 24.45564 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? -4.64977  -2.41653  -20.95419 1.000 26.41292 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? -4.25328  -3.39039  -22.05135 1.000 29.96733 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? -3.60860  -2.98130  -23.03296 1.000 27.94773 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? -3.36327  -1.67958  -20.50462 1.000 26.34674 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? -2.23839  -2.65792  -20.12878 1.000 28.94177 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? -3.65118  -0.73398  -19.34368 1.000 24.74708 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? -1.07112  -1.99912  -19.34651 1.000 25.43481 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? -4.61219  -4.66172  -21.91810 1.000 30.50773 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? -4.23147  -5.70304  -22.85864 1.000 32.37162 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? -5.33889  -5.97762  -23.85827 1.000 38.87931 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? -6.52059  -6.04010  -23.50272 1.000 37.25905 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? -3.89417  -7.00822  -22.14257 1.000 35.61924 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? -2.46515  -6.89972  -21.08043 1.000 31.75450 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? -4.93839  -6.17719  -25.10378 1.000 42.65917 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? -5.84781  -6.63300  -26.13296 1.000 48.60945 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? -5.86200  -8.16013  -26.14171 1.000 51.40263 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? -5.23240  -8.81808  -25.30929 1.000 49.47326 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? -5.43684  -6.05469  -27.48138 1.000 48.63778 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? -4.02668  -6.23368  -27.66066 1.000 47.55548 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? -5.75382  -4.56781  -27.52524 1.000 47.75920 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? -6.59848  -8.73411  -27.09336 1.000 55.62532 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? -6.67163  -10.18806 -27.19675 1.000 56.61874 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? -5.28344  -10.79288 -27.38811 1.000 55.38262 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? -4.87584  -11.69506 -26.64691 1.000 53.09144 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? -7.60363  -10.57584 -28.34637 1.000 59.08785 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? -8.93862  -10.19251 -28.05956 1.000 61.91031 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? -4.52731  -10.28377 -28.36371 1.000 56.14518 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? -3.19481  -10.82561 -28.62097 1.000 56.36581 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? -2.18973  -10.42662 -27.54166 1.000 54.37861 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? -1.21134  -11.15136 -27.31468 1.000 51.98825 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? -2.71426  -10.39728 -30.01025 1.000 57.34660 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? -2.56122  -8.89167  -30.21878 1.000 58.90557 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? -3.81027  -8.26277  -30.81709 1.000 60.59807 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? -4.92898  -8.64353  -30.39926 1.000 60.42757 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? -3.67352  -7.40260  -31.71582 1.000 59.65121 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? -2.41378  -9.29749  -26.85975 1.000 52.44191 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? -1.52700  -8.90856  -25.76394 1.000 50.41803 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? -1.55805  -9.93048  -24.63710 1.000 48.32898 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? -0.52510  -10.22534 -24.02317 1.000 45.42238 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? -1.92119  -7.53808  -25.21299 1.000 47.10691 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? -1.34349  -6.38872  -26.01359 1.000 44.75700 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? -0.39791  -6.60695  -26.80966 1.000 44.69038 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? -1.84022  -5.25660  -25.83038 1.000 42.67954 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? -2.73947  -10.47282 -24.34532 1.000 49.81223 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? -2.95216  -11.33310 -23.18868 1.000 48.27436 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? -2.19655  -12.64577 -23.29255 1.000 49.12166 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? -2.20373  -13.42314 -22.33194 1.000 47.88649 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? -4.45212  -11.59281 -23.01626 1.000 46.51821 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? -5.09658  -10.77486 -21.91248 1.000 45.64844 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? -3.95388  -10.32697 -20.59791 1.000 40.05227 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? -3.78131  -11.91818 -19.78857 1.000 34.75407 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? -1.54163  -12.91002 -24.42090 1.000 48.17885 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? -0.79173  -14.14656 -24.58234 1.000 49.99403 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? 0.42084   -14.13344 -23.66053 1.000 49.80215 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? 0.42572   -14.83873 -22.64458 1.000 52.13503 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? -0.38749  -14.34677 -26.04617 1.000 53.24585 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? -1.58609  -14.63550 -26.96393 1.000 55.54890 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? -1.18553  -14.63506 -28.43978 1.000 54.07920 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? -2.29550  -15.93368 -26.57256 1.000 53.12527 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? 1.42935   -13.31307 -23.96751 1.000 48.16839 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? 2.60837   -13.15978 -23.10856 1.000 46.04610 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? 2.99549   -11.68333 -23.02791 1.000 44.43165 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? 3.88190   -11.21165 -23.74847 1.000 44.84994 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? 3.77163   -14.00936 -23.62581 1.000 50.79742 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? 4.74515   -14.40398 -22.52432 1.000 51.76988 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? 4.72634   -13.83940 -21.42457 1.000 51.65737 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? 5.59743   -15.38549 -22.81286 1.000 50.68117 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? 2.35981   -10.92498 -22.13483 1.000 42.76718 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? 2.51099   -9.46475  -22.13691 1.000 39.90418 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? 3.66663   -8.93735  -21.29967 1.000 37.04168 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? 4.03710   -9.49332  -20.26417 1.000 35.75615 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? 1.17836   -8.99893  -21.53723 1.000 36.91772 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? 0.84077   -10.08987 -20.55213 1.000 38.12591 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? 1.37043   -11.37905 -21.14403 1.000 40.55195 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? 4.23315   -7.82439  -21.76910 1.000 35.25165 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? 5.16387   -7.01630  -20.98023 1.000 32.25619 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? 4.39454   -5.76611  -20.54552 1.000 32.74926 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? 4.30310   -4.78159  -21.28462 1.000 27.88375 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? 6.42236   -6.65879  -21.77210 1.000 36.63594 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? 7.46437   -5.97141  -20.91444 1.000 38.39339 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? 7.26585   -4.84566  -20.45134 1.000 35.35963 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? 8.59584   -6.63920  -20.71426 1.000 44.08410 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? 3.82496   -5.82383  -19.33517 1.000 30.98502 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? 2.92868   -4.77078  -18.86095 1.000 27.64376 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? 3.61313   -3.41908  -18.71877 1.000 28.57741 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? 2.97098   -2.38247  -18.89743 1.000 25.17137 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? 2.31809   -5.17156  -17.52408 1.000 27.37977 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? 1.23301   -6.20144  -17.64240 1.000 24.53654 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? -0.05874  -5.82193  -17.97519 1.000 26.14449 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? 1.49664   -7.55406  -17.43186 1.000 24.45117 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? -1.06933  -6.74264  -18.06969 1.000 24.80157 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? 0.49658   -8.49703  -17.54153 1.000 25.46804 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? -0.79123  -8.07814  -17.85664 1.000 25.12534 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? -1.80203  -8.98481  -17.97427 1.000 23.35413 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? 4.89618   -3.39497  -18.37607 1.000 31.63863 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? 5.59189   -2.11710  -18.30170 1.000 31.74677 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? 5.63798   -1.44297  -19.67089 1.000 32.29983 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? 5.26808   -0.26927  -19.80179 1.000 28.92913 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? 6.98160   -2.32997  -17.70105 1.000 33.21100 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? 6.88862   -2.72889  -16.23903 1.000 38.84524 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? 6.90635   -4.24352  -16.03900 1.000 41.55020 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? 6.85719   -4.98641  -17.04574 1.000 42.02766 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? 6.90783   -4.69777  -14.87273 1.000 39.35222 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? 6.04753   -2.18651  -20.71037 1.000 32.07020 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? 5.99686   -1.66168  -22.07913 1.000 34.89404 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? 4.59490   -1.21731  -22.47019 1.000 32.96553 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? 4.42239   -0.18342  -23.12884 1.000 30.73685 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? 6.47392   -2.70688  -23.08854 1.000 36.85586 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? 7.95907   -2.85068  -23.13045 1.000 41.44078 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? 8.43409   -3.95812  -23.45657 1.000 44.73499 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? 8.65634   -1.84003  -22.90698 1.000 42.88422 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? 3.58370   -2.00975  -22.11333 1.000 29.71665 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? 2.22881   -1.70379  -22.54158 1.000 29.95294 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? 1.73757   -0.41986  -21.89592 1.000 27.73528 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? 1.04895   0.37993   -22.53538 1.000 29.37360 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? 1.30477   -2.87223  -22.19615 1.000 29.46058 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? 1.50098   -4.18027  -22.96296 1.000 33.48728 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? 0.31178   -5.10099  -22.72854 1.000 33.37344 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? 1.68618   -3.93466  -24.44839 1.000 32.38752 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? 2.10507   -0.19408  -20.63552 1.000 26.85248 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? 1.55751   0.93738   -19.89838 1.000 27.12403 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? 2.22609   2.24965   -20.29852 1.000 27.23469 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? 1.55192   3.27746   -20.40756 1.000 27.56171 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? 1.68838   0.69923   -18.39146 1.000 27.59970 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? 0.97146   1.70547   -17.49067 1.000 26.63511 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? -0.49782  1.81564   -17.89139 1.000 25.60733 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? 1.10059   1.32328   -16.02908 1.000 29.28489 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? 3.54326   2.24676   -20.52697 1.000 28.18057 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? 4.21211   3.48940   -20.91279 1.000 30.57518 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? 3.63185   4.04483   -22.20796 1.000 31.61922 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? 3.73041   5.24940   -22.47709 1.000 33.04950 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? 5.74545   3.28262   -21.03419 1.000 31.18786 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? 6.46384   4.62460   -21.08865 1.000 32.92861 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? 6.10332   2.49078   -22.28326 1.000 32.37761 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? 5.95942   5.63504   -20.07477 1.000 33.15665 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? 3.01626   3.19104   -23.01204 1.000 31.54451 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? 2.44104   3.54291   -24.29860 1.000 33.16997 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? 1.07703   4.18412   -24.15488 1.000 32.70837 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? 0.47778   4.57927   -25.15758 1.000 34.13497 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? 2.33982   2.26642   -25.11462 1.000 33.31425 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? 3.45382   2.04806   -26.04199 1.000 35.23587 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? 3.48908   0.59205   -26.39475 1.000 34.88513 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? 4.85890   0.11347   -26.29628 1.000 35.44026 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? 5.27565   -1.06969  -26.71918 1.000 36.75054 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? 4.41635   -2.02693  -27.03841 1.000 39.71682 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? 6.58532   -1.31010  -26.78912 1.000 36.87696 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? 0.57366   4.26599   -22.93307 1.000 31.76657 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? -0.76921  4.72690   -22.65219 1.000 31.87669 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? -0.71623  6.16598   -22.15008 1.000 32.80858 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? 0.26945   6.58807   -21.54875 1.000 33.38550 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? -1.41219  3.81448   -21.60365 1.000 31.77996 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? -1.76006  2.39797   -22.10908 1.000 27.86927 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? -3.10323  2.33927   -22.81423 1.000 33.49094 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? -3.18910  1.18307   -23.80618 1.000 33.53817 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? -3.85944  1.58535   -25.07299 1.000 36.65199 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? -1.78415  6.91628   -22.40447 1.000 37.54419 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? -1.99962  8.23582   -21.82120 1.000 37.30379 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? -3.17215  8.19906   -20.84053 1.000 37.25959 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? -4.00313  7.28871   -20.87145 1.000 34.89357 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? -2.27437  9.28166   -22.90828 1.000 34.84822 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? -1.51837  9.05209   -24.09088 1.000 42.31676 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? -3.24233  9.21040   -19.96437 1.000 36.33332 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? -4.39707  9.33192   -19.07227 1.000 33.62216 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? -5.70895  9.23164   -19.84678 1.000 35.16938 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? -6.61106  8.47912   -19.46464 1.000 34.69089 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? -4.35193  10.65344  -18.30315 1.000 34.56101 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? -3.27891  10.68628  -17.22939 1.000 34.48657 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? -2.78076  9.65202   -16.78937 1.000 34.15173 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? -2.90304  11.89592  -16.81521 1.000 31.56851 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? -5.82234  9.97212   -20.95578 1.000 37.32645 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? -7.06222  10.01288  -21.72721 1.000 38.65007 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? -7.41921  8.67243   -22.35998 1.000 38.01581 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? -8.54858  8.51642   -22.83713 1.000 38.41830 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? -6.97651  11.11156  -22.79805 1.000 40.50126 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? -6.28343  10.69525  -24.06021 1.000 41.67384 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? -4.98161  11.05425  -24.34510 1.000 42.85016 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? -6.72147  9.99079   -25.13303 1.000 42.87052 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? -4.64063  10.57284  -25.52888 1.000 42.47868 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? -5.67883  9.92401   -26.02890 1.000 45.38149 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? -6.50429  7.70151   -22.36532 1.000 36.83892 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? -6.84927  6.36509   -22.83459 1.000 35.38836 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? -7.74132  5.61062   -21.85397 1.000 34.07730 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? -8.26695  4.55301   -22.21501 1.000 34.32342 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? -5.57801  5.55547   -23.09674 1.000 35.16292 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? -4.82846  6.02448   -24.31882 1.000 37.21988 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? -3.61490  5.86159   -24.41717 1.000 36.95639 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? -5.55277  6.59953   -25.26904 1.000 38.17035 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? -7.91968  6.12074   -20.63594 1.000 33.47045 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? -8.71773  5.47140   -19.59886 1.000 34.05721 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? -10.01401 6.24256   -19.36848 1.000 34.21646 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? -9.99166  7.36441   -18.85155 1.000 34.74817 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? -7.93985  5.36090   -18.28605 1.000 29.73484 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? -6.66873  4.56713   -18.37969 1.000 29.57675 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? -6.69952  3.18941   -18.27883 1.000 27.18117 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? -5.44008  5.19851   -18.56427 1.000 31.45676 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? -5.53905  2.44894   -18.35112 1.000 28.22905 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? -4.27003  4.45717   -18.63945 1.000 30.14002 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? -4.32368  3.07990   -18.52495 1.000 26.76880 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? -11.13896 5.62575   -19.71777 1.000 32.80364 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? -12.45951 6.17264   -19.43312 1.000 34.53632 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? -13.00167 5.51297   -18.17270 1.000 30.01516 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? -13.11692 4.28730   -18.12042 1.000 30.46890 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? -13.42057 5.93856   -20.59965 1.000 35.37163 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? -12.86320 5.90546   -22.02595 1.000 37.96107 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? -13.96867 5.54545   -23.00938 1.000 37.52202 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? -12.23725 7.23455   -22.39007 1.000 38.84217 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? -13.32679 6.31908   -17.16328 1.000 32.49391 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? -13.93494 5.83891   -15.92455 1.000 30.34389 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? -15.34147 6.41272   -15.82104 1.000 32.93827 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? -15.52803 7.63150   -15.92181 1.000 32.22368 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? -13.09824 6.22450   -14.69000 1.000 28.63177 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? -13.73539 5.66231   -13.42749 1.000 27.92712 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? -11.67973 5.70669   -14.83745 1.000 29.59824 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? -16.32744 5.53903   -15.61044 1.000 29.89582 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? -17.72646 5.93731   -15.51675 1.000 32.81500 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? -18.21776 5.58472   -14.12174 1.000 32.48752 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? -18.20266 4.41010   -13.73710 1.000 28.83443 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? -18.58044 5.22859   -16.57289 1.000 35.93324 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? -19.12523 6.10222   -17.69632 1.000 41.65405 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? -18.08029 6.41553   -18.76672 1.000 45.34760 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? -17.61739 5.52114   -19.48314 1.000 43.97522 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? -17.70897 7.68983   -18.88072 1.000 42.66299 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? -18.62284 6.59468   -13.35999 1.000 33.02381 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? -19.25246 6.38998   -12.05841 1.000 35.48687 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? -20.73733 6.67205   -12.25108 1.000 37.89561 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? -21.16623 7.82649   -12.24530 1.000 36.48503 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? -18.63068 7.28327   -10.99106 1.000 34.27602 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? -21.52092 5.61156   -12.42978 1.000 39.80794 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? -22.89723 5.80546   -12.85176 1.000 40.81418 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? -22.92312 6.43993   -14.22507 1.000 42.35873 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? -22.15094 6.07459   -15.11908 1.000 41.54175 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? -23.80563 7.42677   -14.39792 1.000 44.81169 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? -23.88171 8.18165   -15.64376 1.000 49.96795 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? -22.99496 9.42224   -15.62726 1.000 48.78538 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? -23.29319 10.40462  -16.32212 1.000 51.52742 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? -25.33447 8.56385   -15.95131 1.000 51.13426 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? -26.06857 9.13476   -14.74257 1.000 56.21395 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? -25.44911 9.64750   -13.80854 1.000 58.52077 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? -27.39819 9.04465   -14.75744 1.000 55.21979 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? -21.90859 9.40202   -14.85623 1.000 45.49615 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? -21.03273 10.55577  -14.69622 1.000 46.41733 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? -19.60216 10.11621  -14.97707 1.000 43.73513 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? -19.17118 9.05496   -14.51323 1.000 41.43045 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? -21.16855 11.17100  -13.28921 1.000 45.14921 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? -19.92184 11.95712  -12.91373 1.000 45.83731 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? -22.39880 12.06662  -13.23480 1.000 48.31494 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? -18.87704 10.91874  -15.75069 1.000 46.75326 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? -17.53223 10.56348  -16.17675 1.000 43.20461 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? -16.51241 11.13251  -15.20102 1.000 41.77964 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? -16.59433 12.30042  -14.80946 1.000 42.12736 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? -17.22979 11.07551  -17.59371 1.000 45.27420 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? -18.23991 10.74792  -18.73069 1.000 46.58574 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? -19.70276 11.08979  -18.43124 1.000 50.98491 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? -20.10284 12.25999  -18.44811 1.000 52.94420 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? -20.50515 10.05978  -18.14860 1.000 50.07463 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? -15.54085 10.30246  -14.82936 1.000 36.69031 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? -14.42293 10.70968  -13.99022 1.000 35.60656 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? -13.19940 10.94079  -14.86976 1.000 39.20037 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? -12.83853 10.08248  -15.68308 1.000 40.77056 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? -14.12468 9.64954   -12.92749 1.000 34.49551 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? -15.22648 9.31029   -11.91641 1.000 33.02116 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? -14.69471 8.38530   -10.82742 1.000 29.77286 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? -15.80023 10.55961  -11.29146 1.000 35.16791 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? -12.56889 12.09762  -14.71528 1.000 38.87450 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? -11.37845 12.42022  -15.48856 1.000 37.22031 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? -10.15719 11.80546  -14.81616 1.000 35.86592 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? -9.90553  12.04817  -13.62879 1.000 34.87757 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? -11.21934 13.93071  -15.63098 1.000 39.41825 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? -9.98843  14.37355  -16.40801 1.000 40.44840 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? -10.07228 15.86361  -16.71371 1.000 44.24265 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? -8.76502  16.50952  -16.70006 1.000 50.72270 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? -8.35948  17.35198  -15.75846 1.000 50.98411 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? -9.11613  17.62826  -14.70474 1.000 49.29442 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? -7.16067  17.91913  -15.86792 1.000 50.67254 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? -9.41374  11.00187  -15.57297 1.000 34.77171 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? -8.16889  10.41770  -15.08892 1.000 33.16176 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? -7.05605  11.44997  -15.22315 1.000 34.21236 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? -6.83598  12.01053  -16.30494 1.000 33.60269 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? -7.83464  9.13152   -15.85994 1.000 33.12957 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? -6.41411  8.67087   -15.54285 1.000 31.60466 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? -8.85222  8.03085   -15.53801 1.000 30.46060 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? -6.35660  11.70941  -14.12082 1.000 32.10174 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? -5.24709  12.65909  -14.10607 1.000 32.51522 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? -3.90449  12.00161  -13.84367 1.000 30.17117 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? -2.87052  12.68137  -13.93907 1.000 32.66815 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? -5.48700  13.79381  -13.08564 1.000 33.61312 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? -5.33591  13.24767  -11.65533 1.000 33.95230 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? -6.79717  14.54750  -13.37817 1.000 35.12911 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? -5.83227  14.18781  -10.57152 1.000 37.16258 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? -3.87728  10.71593  -13.52845 1.000 33.04296 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? -2.63145  10.00420  -13.34305 1.000 30.05340 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? -2.89156  8.51865   -13.37329 1.000 30.65155 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? -4.02071  8.05791   -13.16181 1.000 30.74876 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? -1.82993  7.76814   -13.64337 1.000 30.11488 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? -1.94111  6.31987   -13.64199 1.000 27.55941 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? -0.61381  5.73316   -13.20447 1.000 27.67916 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? 0.45036   6.31292   -13.45034 1.000 28.70818 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? -2.32183  5.78759   -15.02164 1.000 28.08492 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? -1.31036  6.09380   -16.08370 1.000 29.86463 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? -1.26539  7.30207   -16.74470 1.000 31.21965 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? -0.30032  5.34993   -16.59132 1.000 29.60582 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? -0.27805  7.28463   -17.62373 1.000 34.02095 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? 0.32226   6.10948   -17.55097 1.000 32.99999 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? -0.68208  4.57070   -12.56634 1.000 23.58762 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? 0.52786   3.84897   -12.20426 1.000 26.64799 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? 0.17872   2.37760   -12.04447 1.000 23.37107 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? -0.97998  2.01121   -11.84252 1.000 27.30169 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? 1.15762   4.37538   -10.90687 1.000 25.68020 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? 0.20700   4.37858   -9.85809  1.000 29.03303 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? 1.20631   1.54364   -12.11048 1.000 22.31859 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? 1.06893   0.11229   -11.89243 1.000 25.41200 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? 1.61203   -0.27374  -10.52241 1.000 23.97209 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? 2.73968   0.10523   -10.16270 1.000 21.52207 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? 1.81574   -0.65979  -12.97753 1.000 25.23129 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? 1.43424   -2.11169  -12.99630 1.000 22.38869 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? 1.74533   -2.81747  -14.59642 1.000 27.99025 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? 3.33227   -2.10387  -15.04373 1.000 30.65647 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? 0.82792   -1.04469  -9.78557  1.000 22.05015 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? 1.22822   -1.68279  -8.52684  1.000 21.62745 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? 1.01140   -3.18860  -8.66921  1.000 19.55549 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? -0.12196  -3.66233  -8.58430  1.000 16.19350 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? 0.43991   -1.11173  -7.34057  1.000 23.56846 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? 0.68794   -1.83518  -6.01780  1.000 22.33036 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? 0.27740   -1.01217  -4.80976  1.000 28.74425 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? 0.63665   0.16128   -4.70156  1.000 32.91978 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? -0.51184  -1.61011  -3.90895  1.000 24.58041 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? 2.09742   -3.93666  -8.88857  1.000 17.02617 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? 2.01226   -5.37788  -9.13006  1.000 17.64248 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? 0.96818   -5.68163  -10.20420 1.000 16.22891 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? 1.11491   -5.19810  -11.31852 1.000 17.43801 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? 1.73895   -6.09765  -7.82287  1.000 15.95793 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? 2.76277   -5.72334  -6.74955  1.000 16.71803 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? 3.97444   -5.85583  -6.95272  1.000 16.13667 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? 2.28549   -5.17688  -5.64530  1.000 15.37096 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? -0.09241  -6.43818  -9.90296  1.000 15.55724 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? -1.07022  -6.79517  -10.92303 1.000 16.79735 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? -2.29293  -5.87021  -10.96579 1.000 16.75077 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? -3.26043  -6.17476  -11.68682 1.000 14.90623 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? -1.52769  -8.24794  -10.73474 1.000 14.24000 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? -0.15407  -9.35674  -11.06259 1.000 13.99780 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? -2.28037  -4.74340  -10.24854 1.000 13.81968 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? -3.39414  -3.80868  -10.36753 1.000 15.75931 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? -2.90151  -2.48270  -10.93621 1.000 16.23375 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? -1.71049  -2.14985  -10.90595 1.000 17.34215 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? -4.15666  -3.57333  -9.04257  1.000 15.53196 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? -4.69029  -4.90229  -8.46497  1.000 17.34704 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? -3.32289  -2.85465  -8.04124  1.000 15.95413 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? -3.84505  -1.75395  -11.52359 1.000 14.64265 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? -3.65541  -0.37535  -11.94534 1.000 15.63546 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? -4.22811  0.56059   -10.89739 1.000 19.96908 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? -5.25870  0.26355   -10.29019 1.000 17.02829 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? -4.36070  -0.08232  -13.26938 1.000 21.38476 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? -3.63033  -0.14775  -14.59482 1.000 22.28049 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? -4.57028  0.34332   -15.69606 1.000 24.88870 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? -2.33701  0.64792   -14.56609 1.000 25.65487 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? -3.58056  1.70100   -10.71097 1.000 17.86952 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? -4.09538  2.76990   -9.86236  1.000 21.70697 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? -4.32976  3.98921   -10.74352 1.000 21.44936 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? -3.37488  4.59877   -11.24311 1.000 24.64972 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? -3.14423  3.07520   -8.70994  1.000 22.93958 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? -2.88370  1.88847   -7.80587  1.000 20.51496 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? -1.93314  2.23502   -6.66985  1.000 24.20875 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? -2.49740  3.28953   -5.73905  1.000 25.78612 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? -1.76826  3.33598   -4.43258  1.000 32.71415 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? -5.60493  4.33038   -10.94825 1.000 22.11251 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? -6.00142  5.44686   -11.80456 1.000 23.31147 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? -6.33750  6.64294   -10.92309 1.000 24.38903 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? -7.34235  6.63428   -10.20407 1.000 24.95950 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? -7.19546  5.06696   -12.67773 1.000 24.05558 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? -6.92870  3.93640   -13.67072 1.000 25.00099 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? -8.10018  3.75436   -14.62636 1.000 24.92733 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? -5.63314  4.19525   -14.43815 1.000 24.39977 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? -5.50426  7.66906   -10.98375 1.000 25.80602 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? -5.73938  8.88625   -10.22176 1.000 28.33145 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? -6.81388  9.70920   -10.92648 1.000 29.07597 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? -6.66932  10.04429  -12.10174 1.000 32.53584 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? -4.42198  9.64582   -10.08422 1.000 28.64934 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? -4.40943  10.80856  -9.13138  1.000 31.64611 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? -4.10808  10.35166  -7.70537  1.000 33.08401 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? -3.88996  11.57466  -6.81484  1.000 32.98965 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? -4.32137  12.82100  -7.50040  1.000 37.63312 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? -7.91691  9.98493   -10.23643 1.000 28.83069 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? -9.01884  10.73999  -10.81396 1.000 30.10911 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? -9.11088  12.08522  -10.10181 1.000 31.48290 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? -8.57733  12.27259  -9.00368  1.000 30.80874 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? -10.34757 9.95430   -10.75142 1.000 31.36535 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? -10.20165 8.64811   -11.50191 1.000 30.07939 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? -10.72729 9.66321   -9.30595  1.000 27.30317 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? -9.74948  13.05608  -10.76413 1.000 32.97295 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? -9.80924  14.40023  -10.19374 1.000 36.00381 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? -10.87346 14.55598  -9.11632  1.000 36.04893 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? -10.96686 15.63183  -8.51479  1.000 38.27587 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? -10.05528 15.46562  -11.27723 1.000 38.54593 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? -11.38512 15.27810  -12.00564 1.000 39.58640 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? -11.43210 15.53960  -13.21813 1.000 44.45890 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? -12.36687 14.80687  -11.40154 1.000 42.24974 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? -11.69816 13.54171  -8.88900  1.000 34.17600 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? -12.79317 13.62058  -7.93268  1.000 34.32481 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? -12.62394 12.52248  -6.89397  1.000 29.95371 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? -12.48785 11.34750  -7.24503  1.000 26.95004 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? -14.14562 13.48050  -8.63436  1.000 33.02126 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? -14.20940 14.39219  -9.73494  1.000 40.00159 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? -15.28809 13.77262  -7.66700  1.000 35.92957 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? -12.61520 12.90750  -5.62123  1.000 29.96504 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? -12.65527 11.92387  -4.55114  1.000 26.40543 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? -14.08084 11.40640  -4.38596  1.000 28.39348 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? -15.04274 12.17829  -4.41819  1.000 30.81691 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? -12.15430 12.52861  -3.24240  1.000 27.94634 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? -14.20746 10.09761  -4.22267  1.000 26.64770 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? -15.50114 9.43511   -4.04676  1.000 24.19922 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? -16.15466 9.86738   -2.73913  1.000 25.85383 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? -15.68274 9.46387   -1.66624  1.000 26.60338 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? -15.30576 7.92247   -4.06873  1.000 22.53835 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? -16.61846 7.15144   -3.99586  1.000 20.80499 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? -17.69646 7.73710   -3.90282  1.000 22.20187 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? -16.52573 5.81780   -4.03321  1.000 19.65910 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? -17.24081 10.64834  -2.76820  1.000 26.76254 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? -17.86479 11.08099  -1.50688  1.000 26.04274 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? -18.47020 9.93626   -0.70943  1.000 25.46712 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? -18.78511 10.12574  0.47785   1.000 26.12956 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? -18.93506 12.08241  -1.96676  1.000 28.43591 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? -19.25383 11.69106  -3.37306  1.000 28.93309 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? -18.00572 11.07440  -3.95618  1.000 25.44573 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? -18.62517 8.75945   -1.31303  1.000 24.85149 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? -19.15610 7.59461   -0.62484  1.000 24.11813 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? -18.05716 6.68437   -0.09439  1.000 21.12062 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? -18.34223 5.54771   0.28840   1.000 22.83565 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? -20.09312 6.81569   -1.54807  1.000 23.26676 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? -21.34089 7.58580   -1.93419  1.000 26.01814 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? -22.00697 6.92482   -3.12835  1.000 28.17956 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? -23.12886 7.78122   -3.66642  1.000 28.17012 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? -24.44091 7.06817   -3.64266  1.000 36.18786 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? -16.80588 7.15363   -0.06195  1.000 23.09279 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? -15.71500 6.30753   0.41562   1.000 22.33759 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? -15.96476 5.89572   1.86219   1.000 19.85993 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? -16.02160 6.76598   2.74671   1.000 21.99644 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? -14.37470 7.03234   0.31279   1.000 21.51044 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? -14.15814 7.44240   -1.03659  1.000 24.45150 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? -13.22321 6.07469   0.70088   1.000 22.15627 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? -16.13007 4.61442   2.15266   1.000 19.88694 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? -16.25336 4.19064   3.54116   1.000 21.89139 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? -14.88348 4.16251   4.19152   1.000 20.67281 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? -13.85123 4.23342   3.52480   1.000 21.47081 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? -16.82695 2.78256   3.41675   1.000 17.96247 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? -16.20262 2.26905   2.21300   1.000 18.48743 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? -16.01781 3.45439   1.25893   1.000 18.50054 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? -14.88279 4.03637   5.51188   1.000 21.08043 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? -13.64176 3.64595   6.16123   1.000 21.26608 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? -13.24342 2.27049   5.66622   1.000 20.92176 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? -14.07793 1.37043   5.56401   1.000 17.70078 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? -13.77678 3.68098   7.67760   1.000 24.98722 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? -14.48116 4.92045   8.13929   1.000 25.66262 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? -14.39891 5.10253   9.64255   1.000 35.01633 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? -15.75309 5.47597   10.20884  1.000 36.48533 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? -16.08038 6.91279   9.95521   1.000 43.02561 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? -11.97886 2.12356   5.27170   1.000 18.14631 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? -11.58166 0.85699   4.69377   1.000 18.69857 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? -10.14957 0.52573   5.08182   1.000 18.94467 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? -9.39487  1.36201   5.59495   1.000 16.06600 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? -11.71557 0.85869   3.16681   1.000 18.17081 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? -10.70455 1.74875   2.46571   1.000 19.76566 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? -10.95437 3.09412   2.26842   1.000 19.67005 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? -9.51335  1.21856   1.96510   1.000 19.20850 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? -10.04369 3.90723   1.61346   1.000 22.89163 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? -8.59147  2.03034   1.30221   1.000 17.84145 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? -8.86674  3.36987   1.13897   1.000 21.29731 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? -7.94726  4.17754   0.49662   1.000 26.11550 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? -9.80079  -0.72577  4.79543   1.000 17.16532 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? -8.46218  -1.28660  4.89912   1.000 17.32720 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? -8.27157  -2.24085  3.73504   1.000 16.80632 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? -9.23590  -2.82749  3.23996   1.000 15.00858 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? -8.23672  -2.08813  6.19407   1.000 20.40719 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? -8.82897  -1.50167  7.42569   1.000 24.39297 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? -8.08475  -1.95732  8.65788   1.000 24.60511 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? -8.69970  -3.23731  9.19844   1.000 23.36458 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? -8.80419  -3.14761  10.71206  1.000 27.53095 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? -7.01147  -2.40098  3.32342   1.000 16.04980 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? -6.59892  -3.43912  2.38585   1.000 11.90446 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? -5.92166  -4.55083  3.18283   1.000 14.54387 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? -4.80036  -4.36582  3.67850   1.000 14.84674 ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? -5.61184  -2.89194  1.35169   1.000 13.94364 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? -6.21484  -2.02072  0.29348   1.000 13.44870 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? -7.58252  -1.86765  0.17810   1.000 12.03572 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? -5.38680  -1.37328  -0.61229  1.000 14.06010 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? -8.13200  -1.07042  -0.80745  1.000 14.43141 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? -5.92823  -0.58075  -1.62445  1.000 15.69838 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? -7.29599  -0.42716  -1.71770  1.000 12.87705 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? -6.57079  -5.71289  3.26210   1.000 9.80572  ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? -6.09055  -6.84148  4.05055   1.000 13.55066 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? -5.96662  -8.04275  3.12669   1.000 12.91711 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? -6.76481  -8.20176  2.19998   1.000 18.17142 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? -7.01313  -7.16276  5.24815   1.000 14.20689 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? -7.43203  -5.86902  5.97581   1.000 14.65615 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? -8.22228  -7.93312  4.80120   1.000 15.11434 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? -4.95926  -8.88876  3.36945   1.000 10.60653 ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? -4.84827  -10.16353 2.67425   1.000 9.14334  ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? -5.30789  -11.27004 3.62079   1.000 11.28441 ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? -4.83710  -11.33878 4.75822   1.000 12.21086 ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? -3.40292  -10.42351 2.23737   1.000 11.78192 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? -3.28298  -11.59530 1.28283   1.000 11.00754 ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? -1.79306  -11.78025 0.94798   1.000 10.03200 ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? -1.59238  -12.99385 0.17312   1.000 12.72851 ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? -1.62538  -13.02405 -1.14680  1.000 11.81596 ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? -1.94245  -11.95464 -1.83822  1.000 10.36386 ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? -1.36977  -14.16638 -1.78432  1.000 11.99814 ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? -6.21155  -12.12987 3.14837   1.000 15.58736 ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? -6.75011  -13.20099 3.98011   1.000 13.72948 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? -5.94587  -14.46900 3.76015   1.000 13.41862 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? -5.20400  -14.58836 2.78624   1.000 13.34195 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? -8.24033  -13.46565 3.68479   1.000 12.18953 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? -8.46083  -13.84744 2.21578   1.000 11.76408 ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? -9.08282  -12.29279 4.13693   1.000 16.92147 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? -9.90770  -14.44309 1.92993   1.000 16.41000 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? -6.14311  -15.42912 4.62353   1.000 11.64402 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? -5.64164  -16.79367 4.68681   1.000 14.65816 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? -6.60609  -17.76430 4.00500   1.000 15.24762 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? -7.82932  -17.62933 4.14501   1.000 15.09598 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? -5.44480  -17.20029 6.14016   1.000 15.68702 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? -4.27747  -16.48681 6.77726   1.000 16.95104 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? -2.98784  -16.99962 6.20650   1.000 16.21004 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? -2.88565  -18.19845 5.97616   1.000 16.97812 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? -1.99521  -16.11056 5.94522   1.000 15.32521 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? -6.09605  -18.77897 3.29972   1.000 14.03175 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? -6.95190  -19.92075 2.94461   1.000 18.07493 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? -7.71074  -20.38992 4.18248   1.000 14.14482 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? -7.18255  -20.38935 5.29620   1.000 17.79839 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? -5.95718  -20.98528 2.44315   1.000 15.64995 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? -4.57111  -20.40948 2.66962   1.000 21.08797 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? -4.71074  -18.92940 2.82725   1.000 16.96133 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? -8.96395  -20.77542 3.99631   1.000 12.80029 ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? -9.81886  -21.11570 5.09839   1.000 15.33616 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? -10.71670 -19.98647 5.54489   1.000 17.72264 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? -11.77872 -20.25581 6.12288   1.000 15.27988 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? -10.32360 -18.73548 5.29375   1.000 11.53591 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? -11.15039 -17.58973 5.66491   1.000 15.33199 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? -12.20712 -17.28151 4.59926   1.000 11.95892 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? -12.07472 -17.63165 3.41720   1.000 9.66182  ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? -10.28152 -16.33855 5.93579   1.000 12.96036 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? -9.34265  -16.47520 7.13910   1.000 15.88295 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? -8.58244  -15.17835 7.51138   1.000 23.37270 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? -7.78635  -14.63222 6.74207   1.000 15.47839 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? -8.88772  -14.65465 8.70737   1.000 30.64042 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? -13.31980 -16.69804 5.04767   1.000 10.91221 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? -14.43107 -16.37662 4.16297   1.000 11.22101 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? -14.47574 -14.88375 3.87540   1.000 13.69281 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? -13.84201 -14.07621 4.56974   1.000 10.34705 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? -15.76579 -16.79254 4.79377   1.000 11.06881 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? -15.82709 -16.21517 6.10073   1.000 15.82877 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? -15.83063 -18.28975 4.89481   1.000 11.75757 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? -15.29064 -14.53492 2.86663   1.000 12.41282 ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? -15.57157 -13.14433 2.51867   1.000 12.47041 ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? -16.79758 -13.06464 1.61807   1.000 12.49661 ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? -17.22879 -14.05202 1.01911   1.000 12.34144 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? -14.38316 -12.46025 1.83624   1.000 11.33399 ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? -13.84569 -13.17316 0.59904   1.000 13.68091 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? -12.95154 -14.23750 0.72030   1.000 14.99577 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? -14.15264 -12.71232 -0.68450  1.000 9.30106  ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? -12.40661 -14.85475 -0.43749  1.000 12.69692 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? -13.62249 -13.31988 -1.82567  1.000 11.99724 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? -12.73243 -14.38429 -1.69371  1.000 9.98500  ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? -17.33692 -11.85812 1.51835   1.000 11.68946 ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? -18.44921 -11.57067 0.63709   1.000 11.94981 ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? -17.91123 -11.01356 -0.67101  1.000 9.90876  ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? -16.94535 -10.23693 -0.67257  1.000 11.37816 ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? -19.40737 -10.56584 1.28644   1.000 11.62105 ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? -19.78469 -11.00751 2.57931   1.000 11.51193 ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? -18.56919 -11.38698 -1.76500  1.000 9.19619  ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? -18.23745 -10.95175 -3.11258  1.000 11.94887 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? -19.41854 -10.16138 -3.64976  1.000 13.07223 ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? -20.56803 -10.61617 -3.56870  1.000 11.30867 ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? -17.89612 -12.15018 -4.01953  1.000 10.21713 ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? -17.75798 -11.69703 -5.48829  1.000 13.89873 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? -16.65559 -12.88825 -3.55102  1.000 14.13388 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? -19.15127 -8.95531  -4.14172  1.000 12.02188 ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? -20.16312 -8.15525  -4.83447  1.000 12.30699 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? -19.87510 -8.27709  -6.32695  1.000 13.82476 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? -18.98739 -7.60208  -6.85890  1.000 11.84440 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? -20.12958 -6.70511  -4.35699  1.000 11.88318 ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? -21.11640 -5.78056  -5.07296  1.000 12.35092 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? -22.55942 -6.20715  -4.79145  1.000 14.80418 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? -20.88477 -4.32279  -4.67903  1.000 15.67828 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? -20.55405 -9.20193  -6.99045  1.000 13.23773 ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? -20.31644 -9.40694  -8.41116  1.000 12.83885 ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? -20.88557 -8.22927  -9.17932  1.000 17.22241 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? -22.02511 -7.82454  -8.93481  1.000 18.85362 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? -20.96174 -10.70892 -8.90111  1.000 13.77744 ? 116 ALA   A CB  1 
ATOM   907  N  N   . CYS   A 1 117 ? -20.09776 -7.68666  -10.11022 1.000 11.51074 ? 117 CYS   A N   1 
ATOM   908  C  CA  . CYS   A 1 117 ? -20.52608 -6.56084  -10.93112 1.000 17.49991 ? 117 CYS   A CA  1 
ATOM   909  C  C   . CYS   A 1 117 ? -20.10890 -6.70011  -12.38161 1.000 20.48233 ? 117 CYS   A C   1 
ATOM   910  O  O   . CYS   A 1 117 ? -19.15616 -7.39621  -12.73263 1.000 17.44315 ? 117 CYS   A O   1 
ATOM   911  C  CB  . CYS   A 1 117 ? -20.00658 -5.19359  -10.47435 1.000 21.96819 ? 117 CYS   A CB  1 
ATOM   912  S  SG  . CYS   A 1 117 ? -19.83828 -4.88900  -8.77288  1.000 23.94008 ? 117 CYS   A SG  1 
ATOM   913  N  N   . TYR   A 1 118 ? -20.83798 -5.96559  -13.21065 1.000 21.08090 ? 118 TYR   A N   1 
ATOM   914  C  CA  . TYR   A 1 118 ? -20.62579 -5.89908  -14.64769 1.000 21.63911 ? 118 TYR   A CA  1 
ATOM   915  C  C   . TYR   A 1 118 ? -20.82298 -4.44739  -15.04675 1.000 23.78976 ? 118 TYR   A C   1 
ATOM   916  O  O   . TYR   A 1 118 ? -21.77855 -3.81324  -14.58600 1.000 23.17690 ? 118 TYR   A O   1 
ATOM   917  C  CB  . TYR   A 1 118 ? -21.59297 -6.83954  -15.37952 1.000 23.49271 ? 118 TYR   A CB  1 
ATOM   918  C  CG  . TYR   A 1 118 ? -21.42390 -8.25401  -14.87417 1.000 24.10398 ? 118 TYR   A CG  1 
ATOM   919  C  CD1 . TYR   A 1 118 ? -22.14927 -8.71693  -13.77661 1.000 22.75801 ? 118 TYR   A CD1 1 
ATOM   920  C  CD2 . TYR   A 1 118 ? -20.50345 -9.10719  -15.45796 1.000 23.95681 ? 118 TYR   A CD2 1 
ATOM   921  C  CE1 . TYR   A 1 118 ? -21.94619 -9.99196  -13.27683 1.000 20.97347 ? 118 TYR   A CE1 1 
ATOM   922  C  CE2 . TYR   A 1 118 ? -20.30130 -10.37618 -14.97547 1.000 22.91942 ? 118 TYR   A CE2 1 
ATOM   923  C  CZ  . TYR   A 1 118 ? -21.02602 -10.81916 -13.89304 1.000 22.86864 ? 118 TYR   A CZ  1 
ATOM   924  O  OH  . TYR   A 1 118 ? -20.79585 -12.09362 -13.42470 1.000 22.12132 ? 118 TYR   A OH  1 
ATOM   925  N  N   . ASN   A 1 119 ? -19.89296 -3.90282  -15.84130 1.000 24.84220 ? 119 ASN   A N   1 
ATOM   926  C  CA  . ASN   A 1 119 ? -19.99671 -2.52017  -16.32795 1.000 23.53012 ? 119 ASN   A CA  1 
ATOM   927  C  C   . ASN   A 1 119 ? -20.10642 -1.51122  -15.18662 1.000 25.11282 ? 119 ASN   A C   1 
ATOM   928  O  O   . ASN   A 1 119 ? -20.77988 -0.48266  -15.32208 1.000 26.02510 ? 119 ASN   A O   1 
ATOM   929  C  CB  . ASN   A 1 119 ? -21.18199 -2.36029  -17.28863 1.000 27.31614 ? 119 ASN   A CB  1 
ATOM   930  C  CG  . ASN   A 1 119 ? -21.10780 -3.31694  -18.45216 1.000 30.08546 ? 119 ASN   A CG  1 
ATOM   931  O  OD1 . ASN   A 1 119 ? -20.21322 -3.20237  -19.29118 1.000 33.35109 ? 119 ASN   A OD1 1 
ATOM   932  N  ND2 . ASN   A 1 119 ? -22.01328 -4.29383  -18.49038 1.000 30.35491 ? 119 ASN   A ND2 1 
ATOM   933  N  N   . GLY   A 1 120 ? -19.45694 -1.80852  -14.05801 1.000 21.32910 ? 120 GLY   A N   1 
ATOM   934  C  CA  . GLY   A 1 120 ? -19.54886 -0.99056  -12.85716 1.000 22.52972 ? 120 GLY   A CA  1 
ATOM   935  C  C   . GLY   A 1 120 ? -20.88218 -1.03758  -12.13618 1.000 26.19973 ? 120 GLY   A C   1 
ATOM   936  O  O   . GLY   A 1 120 ? -21.13747 -0.18194  -11.27870 1.000 24.45342 ? 120 GLY   A O   1 
ATOM   937  N  N   . SER   A 1 121 ? -21.74464 -2.00545  -12.45134 1.000 26.88637 ? 121 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 121 ? -23.10004 -2.05879  -11.90415 1.000 26.40394 ? 121 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 121 ? -23.27535 -3.32805  -11.07905 1.000 25.38220 ? 121 SER   A C   1 
ATOM   940  O  O   . SER   A 1 121 ? -23.21448 -4.43320  -11.64639 1.000 20.01378 ? 121 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 121 ? -24.11623 -2.02541  -13.04037 1.000 31.46233 ? 121 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 121 ? -24.20393 -0.72819  -13.59132 1.000 32.11544 ? 121 SER   A OG  1 
ATOM   943  N  N   . PRO   A 1 122 ? -23.48398 -3.23845  -9.76177  1.000 24.67792 ? 122 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 122 ? -23.55774 -4.45925  -8.94090  1.000 22.62949 ? 122 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 122 ? -24.71799 -5.35254  -9.33821  1.000 23.39367 ? 122 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 122 ? -25.84402 -4.89342  -9.53232  1.000 26.90667 ? 122 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 122 ? -23.73237 -3.92954  -7.51461  1.000 24.14681 ? 122 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 122 ? -23.30419 -2.48895  -7.56159  1.000 25.53862 ? 122 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 122 ? -23.25929 -2.02031  -8.96851  1.000 25.93123 ? 122 PRO   A CD  1 
ATOM   950  N  N   . SER   A 1 123 ? -24.43544 -6.64789  -9.42817  1.000 23.00820 ? 123 SER   A N   1 
ATOM   951  C  CA  . SER   A 1 123 ? -25.41623 -7.64001  -9.84307  1.000 25.06689 ? 123 SER   A CA  1 
ATOM   952  C  C   . SER   A 1 123 ? -25.91792 -8.52320  -8.70985  1.000 21.86906 ? 123 SER   A C   1 
ATOM   953  O  O   . SER   A 1 123 ? -27.12072 -8.79561  -8.63327  1.000 19.95424 ? 123 SER   A O   1 
ATOM   954  C  CB  . SER   A 1 123 ? -24.81808 -8.52561  -10.93713 1.000 25.42240 ? 123 SER   A CB  1 
ATOM   955  O  OG  . SER   A 1 123 ? -25.66226 -9.62786  -11.18731 1.000 34.66904 ? 123 SER   A OG  1 
ATOM   956  N  N   . GLY   A 1 124 ? -25.02735 -9.00223  -7.84573  1.000 16.47479 ? 124 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? -25.42079 -9.86647  -6.75084  1.000 15.48526 ? 124 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? -24.33375 -9.91934  -5.71123  1.000 15.42303 ? 124 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? -23.21283 -9.44178  -5.92429  1.000 13.33568 ? 124 GLY   A O   1 
ATOM   960  N  N   . VAL   A 1 125 ? -24.68873 -10.48738 -4.56676  1.000 11.66516 ? 125 VAL   A N   1 
ATOM   961  C  CA  . VAL   A 1 125 ? -23.76374 -10.61797 -3.44955  1.000 14.10116 ? 125 VAL   A CA  1 
ATOM   962  C  C   . VAL   A 1 125 ? -23.83475 -12.04808 -2.93120  1.000 15.35513 ? 125 VAL   A C   1 
ATOM   963  O  O   . VAL   A 1 125 ? -24.90394 -12.66704 -2.90826  1.000 12.87942 ? 125 VAL   A O   1 
ATOM   964  C  CB  . VAL   A 1 125 ? -24.05764 -9.57336  -2.34410  1.000 14.20702 ? 125 VAL   A CB  1 
ATOM   965  C  CG1 . VAL   A 1 125 ? -25.35439 -9.85038  -1.68323  1.000 17.41801 ? 125 VAL   A CG1 1 
ATOM   966  C  CG2 . VAL   A 1 125 ? -22.89439 -9.52076  -1.33046  1.000 13.63166 ? 125 VAL   A CG2 1 
ATOM   967  N  N   . TYR   A 1 126 ? -22.68102 -12.60651 -2.58964  1.000 11.75278 ? 126 TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 126 ? -22.64264 -13.96058 -2.04879  1.000 13.01066 ? 126 TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 126 ? -21.37176 -14.16208 -1.23454  1.000 14.27052 ? 126 TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 126 ? -20.40270 -13.40054 -1.33027  1.000 11.79203 ? 126 TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 126 ? -22.75599 -15.03000 -3.15863  1.000 12.14290 ? 126 TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 126 ? -21.65415 -14.94324 -4.21143  1.000 13.83901 ? 126 TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 126 ? -20.43912 -15.59807 -4.04036  1.000 16.86951 ? 126 TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 126 ? -21.83915 -14.21898 -5.37226  1.000 16.84472 ? 126 TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 126 ? -19.43688 -15.49670 -5.00999  1.000 15.28316 ? 126 TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 126 ? -20.83371 -14.11342 -6.33227  1.000 17.03281 ? 126 TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 126 ? -19.65753 -14.75085 -6.15158  1.000 16.25782 ? 126 TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 126 ? -18.68450 -14.65725 -7.12892  1.000 20.31595 ? 126 TYR   A OH  1 
ATOM   979  N  N   . GLN   A 1 127 ? -21.38868 -15.22645 -0.44137  1.000 15.12513 ? 127 GLN   A N   1 
ATOM   980  C  CA  . GLN   A 1 127 ? -20.29418 -15.56852 0.45833   1.000 15.79353 ? 127 GLN   A CA  1 
ATOM   981  C  C   . GLN   A 1 127 ? -19.42404 -16.66298 -0.16249  1.000 13.92462 ? 127 GLN   A C   1 
ATOM   982  O  O   . GLN   A 1 127 ? -19.94971 -17.61095 -0.75892  1.000 17.01153 ? 127 GLN   A O   1 
ATOM   983  C  CB  . GLN   A 1 127 ? -20.91550 -16.00387 1.80606   1.000 16.74037 ? 127 GLN   A CB  1 
ATOM   984  C  CG  . GLN   A 1 127 ? -19.94940 -16.13018 2.89464   1.000 16.86563 ? 127 GLN   A CG  1 
ATOM   985  C  CD  . GLN   A 1 127 ? -19.54761 -14.81627 3.52627   1.000 14.09628 ? 127 GLN   A CD  1 
ATOM   986  O  OE1 . GLN   A 1 127 ? -19.74895 -13.72754 2.96920   1.000 14.86518 ? 127 GLN   A OE1 1 
ATOM   987  N  NE2 . GLN   A 1 127 ? -19.01489 -14.91344 4.72041   1.000 15.22775 ? 127 GLN   A NE2 1 
ATOM   988  N  N   . CYS   A 1 128 ? -18.08355 -16.48982 -0.07504  1.000 12.30637 ? 128 CYS   A N   1 
ATOM   989  C  CA  . CYS   A 1 128 ? -17.03462 -17.36897 -0.59699  1.000 18.15225 ? 128 CYS   A CA  1 
ATOM   990  C  C   . CYS   A 1 128 ? -16.02316 -17.67028 0.50072   1.000 14.16112 ? 128 CYS   A C   1 
ATOM   991  O  O   . CYS   A 1 128 ? -15.88833 -16.91113 1.45615   1.000 11.56785 ? 128 CYS   A O   1 
ATOM   992  C  CB  . CYS   A 1 128 ? -16.21326 -16.72655 -1.77478  1.000 13.02076 ? 128 CYS   A CB  1 
ATOM   993  S  SG  . CYS   A 1 128 ? -16.94985 -16.66509 -3.35035  1.000 26.49733 ? 128 CYS   A SG  1 
ATOM   994  N  N   . ALA   A 1 129 ? -15.27888 -18.76990 0.33995   1.000 16.27292 ? 129 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? -14.08398 -19.04596 1.13406   1.000 14.23926 ? 129 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? -12.85530 -19.10969 0.22593   1.000 16.65454 ? 129 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? -12.94359 -19.56570 -0.92311  1.000 15.08240 ? 129 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? -14.20338 -20.37472 1.91600   1.000 14.53158 ? 129 ALA   A CB  1 
ATOM   999  N  N   . MET   A 1 130 ? -11.71999 -18.64114 0.73570   1.000 12.88105 ? 130 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 130 ? -10.41995 -18.88393 0.10794   1.000 12.04935 ? 130 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 130 ? -10.11139 -20.36502 0.28207   1.000 15.11606 ? 130 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 130 ? -9.95132  -20.83377 1.41923   1.000 15.91703 ? 130 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 130 ? -9.35158  -18.01008 0.78089   1.000 13.44196 ? 130 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 130 ? -7.95972  -17.72391 0.11319   1.000 17.03386 ? 130 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 130 ? -7.94893  -17.69489 -1.64816  1.000 20.16197 ? 130 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 130 ? -8.49696  -16.00560 -1.85423  1.000 10.36355 ? 130 MET   A CE  1 
ATOM   1007 N  N   . ARG   A 1 131 ? -10.04340 -21.11766 -0.81809  1.000 11.23191 ? 131 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 131 ? -9.73156  -22.54019 -0.70406  1.000 14.35085 ? 131 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 131 ? -8.27922  -22.71292 -0.26003  1.000 15.41959 ? 131 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 131 ? -7.47536  -21.78948 -0.40116  1.000 16.01470 ? 131 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 131 ? -9.96002  -23.25178 -2.03941  1.000 15.61012 ? 131 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 131 ? -11.38607 -23.17994 -2.61378  1.000 16.82344 ? 131 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 131 ? -12.44987 -23.67194 -1.62446  1.000 15.17940 ? 131 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 131 ? -12.08048 -24.95584 -1.03936  1.000 16.43653 ? 131 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 131 ? -12.72999 -25.52897 -0.03717  1.000 16.05262 ? 131 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 131 ? -13.82426 -24.98158 0.47469   1.000 14.70986 ? 131 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 131 ? -12.28101 -26.68679 0.45113   1.000 18.52172 ? 131 ARG   A NH2 1 
ATOM   1018 N  N   . PRO   A 1 132 ? -7.92590  -23.87531 0.31134   1.000 13.81178 ? 132 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 132 ? -6.50643  -24.15145 0.59079   1.000 17.17657 ? 132 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 132 ? -5.61596  -24.02643 -0.63089  1.000 16.99683 ? 132 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 132 ? -4.42442  -23.71310 -0.47611  1.000 15.82576 ? 132 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 132 ? -6.54099  -25.58491 1.13589   1.000 19.60592 ? 132 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 132 ? -7.90155  -25.64277 1.85342   1.000 18.19877 ? 132 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 132 ? -8.81278  -24.90437 0.90487   1.000 17.05169 ? 132 PRO   A CD  1 
ATOM   1025 N  N   . ASN   A 1 133 ? -6.13449  -24.24938 -1.85011  1.000 15.19598 ? 133 ASN   A N   1 
ATOM   1026 C  CA  . ASN   A 1 133 ? -5.28713  -24.08672 -3.02849  1.000 17.04818 ? 133 ASN   A CA  1 
ATOM   1027 C  C   . ASN   A 1 133 ? -5.29595  -22.67370 -3.56538  1.000 13.71343 ? 133 ASN   A C   1 
ATOM   1028 O  O   . ASN   A 1 133 ? -4.81006  -22.45512 -4.68041  1.000 15.62741 ? 133 ASN   A O   1 
ATOM   1029 C  CB  . ASN   A 1 133 ? -5.67892  -25.05800 -4.14832  1.000 17.78251 ? 133 ASN   A CB  1 
ATOM   1030 C  CG  . ASN   A 1 133 ? -7.09056  -24.81953 -4.67935  1.000 14.82183 ? 133 ASN   A CG  1 
ATOM   1031 O  OD1 . ASN   A 1 133 ? -7.79345  -23.88643 -4.26652  1.000 13.72202 ? 133 ASN   A OD1 1 
ATOM   1032 N  ND2 . ASN   A 1 133 ? -7.50476  -25.67118 -5.61604  1.000 17.94265 ? 133 ASN   A ND2 1 
ATOM   1033 N  N   . PHE   A 1 134 ? -5.86034  -21.72509 -2.81298  1.000 13.54185 ? 134 PHE   A N   1 
ATOM   1034 C  CA  . PHE   A 1 134 ? -5.86422  -20.29928 -3.14050  1.000 14.51576 ? 134 PHE   A CA  1 
ATOM   1035 C  C   . PHE   A 1 134 ? -6.77564  -19.93517 -4.30452  1.000 14.77443 ? 134 PHE   A C   1 
ATOM   1036 O  O   . PHE   A 1 134 ? -6.60379  -18.86381 -4.89335  1.000 18.70926 ? 134 PHE   A O   1 
ATOM   1037 C  CB  . PHE   A 1 134 ? -4.44857  -19.77424 -3.43687  1.000 14.69205 ? 134 PHE   A CB  1 
ATOM   1038 C  CG  . PHE   A 1 134 ? -3.60959  -19.60780 -2.22164  1.000 16.07983 ? 134 PHE   A CG  1 
ATOM   1039 C  CD1 . PHE   A 1 134 ? -3.83485  -18.55203 -1.36274  1.000 13.41618 ? 134 PHE   A CD1 1 
ATOM   1040 C  CD2 . PHE   A 1 134 ? -2.57301  -20.48101 -1.94434  1.000 18.97561 ? 134 PHE   A CD2 1 
ATOM   1041 C  CE1 . PHE   A 1 134 ? -3.03204  -18.38097 -0.21482  1.000 16.76315 ? 134 PHE   A CE1 1 
ATOM   1042 C  CE2 . PHE   A 1 134 ? -1.77187  -20.31966 -0.79867  1.000 23.17953 ? 134 PHE   A CE2 1 
ATOM   1043 C  CZ  . PHE   A 1 134 ? -1.99870  -19.25964 0.05654   1.000 20.55878 ? 134 PHE   A CZ  1 
ATOM   1044 N  N   . THR   A 1 135 ? -7.71938  -20.79295 -4.67365  1.000 14.37903 ? 135 THR   A N   1 
ATOM   1045 C  CA  . THR   A 1 135 ? -8.79758  -20.43327 -5.58439  1.000 13.20058 ? 135 THR   A CA  1 
ATOM   1046 C  C   . THR   A 1 135 ? -10.02667 -20.13554 -4.74553  1.000 13.13982 ? 135 THR   A C   1 
ATOM   1047 O  O   . THR   A 1 135 ? -10.05221 -20.40036 -3.54334  1.000 11.76233 ? 135 THR   A O   1 
ATOM   1048 C  CB  . THR   A 1 135 ? -9.10626  -21.56342 -6.58271  1.000 12.99594 ? 135 THR   A CB  1 
ATOM   1049 O  OG1 . THR   A 1 135 ? -9.55551  -22.72176 -5.87752  1.000 14.53017 ? 135 THR   A OG1 1 
ATOM   1050 C  CG2 . THR   A 1 135 ? -7.87973  -21.96367 -7.40934  1.000 11.83692 ? 135 THR   A CG2 1 
ATOM   1051 N  N   . ILE   A 1 136 ? -11.05857 -19.62490 -5.40550  1.000 12.54436 ? 136 ILE   A N   1 
ATOM   1052 C  CA  . ILE   A 1 136 ? -12.37317 -19.47650 -4.80348  1.000 15.48574 ? 136 ILE   A CA  1 
ATOM   1053 C  C   . ILE   A 1 136 ? -13.39744 -20.05633 -5.77048  1.000 13.75669 ? 136 ILE   A C   1 
ATOM   1054 O  O   . ILE   A 1 136 ? -13.24207 -19.97290 -6.99513  1.000 14.53343 ? 136 ILE   A O   1 
ATOM   1055 C  CB  . ILE   A 1 136 ? -12.68751 -18.00330 -4.43337  1.000 15.48207 ? 136 ILE   A CB  1 
ATOM   1056 C  CG1 . ILE   A 1 136 ? -12.91320 -17.16538 -5.68291  1.000 13.16214 ? 136 ILE   A CG1 1 
ATOM   1057 C  CG2 . ILE   A 1 136 ? -11.54771 -17.38564 -3.57373  1.000 14.72680 ? 136 ILE   A CG2 1 
ATOM   1058 C  CD1 . ILE   A 1 136 ? -13.57061 -15.82771 -5.44463  1.000 13.22574 ? 136 ILE   A CD1 1 
ATOM   1059 N  N   . LYS   A 1 137 ? -14.40047 -20.73242 -5.22198  1.000 14.82178 ? 137 LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 137 ? -15.47626 -21.27666 -6.03908  1.000 17.12303 ? 137 LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 137 ? -16.50965 -20.15980 -6.12493  1.000 15.40711 ? 137 LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 137 ? -17.41763 -20.05683 -5.30664  1.000 18.02779 ? 137 LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 137 ? -16.01360 -22.55864 -5.41419  1.000 19.87563 ? 137 LYS   A CB  1 
ATOM   1064 C  CG  . LYS   A 1 137 ? -14.90797 -23.55111 -5.03710  1.000 18.20803 ? 137 LYS   A CG  1 
ATOM   1065 C  CD  . LYS   A 1 137 ? -15.45921 -24.90451 -4.58424  1.000 17.59325 ? 137 LYS   A CD  1 
ATOM   1066 C  CE  . LYS   A 1 137 ? -14.44495 -26.03672 -4.76986  1.000 21.02567 ? 137 LYS   A CE  1 
ATOM   1067 N  NZ  . LYS   A 1 137 ? -14.66668 -26.79731 -6.02853  1.000 26.93462 ? 137 LYS   A NZ  1 
ATOM   1068 N  N   . GLY   A 1 138 ? -16.31777 -19.25592 -7.08521  1.000 15.36941 ? 138 GLY   A N   1 
ATOM   1069 C  CA  . GLY   A 1 138 ? -17.16411 -18.09503 -7.21973  1.000 14.64388 ? 138 GLY   A CA  1 
ATOM   1070 C  C   . GLY   A 1 138 ? -18.28194 -18.32028 -8.21556  1.000 17.47553 ? 138 GLY   A C   1 
ATOM   1071 O  O   . GLY   A 1 138 ? -18.54973 -19.43482 -8.66707  1.000 18.85891 ? 138 GLY   A O   1 
ATOM   1072 N  N   . SER   A 1 139 ? -18.94388 -17.22306 -8.56898  1.000 15.52741 ? 139 SER   A N   1 
ATOM   1073 C  CA  . SER   A 1 139 ? -19.88583 -17.20589 -9.67381  1.000 15.16760 ? 139 SER   A CA  1 
ATOM   1074 C  C   . SER   A 1 139 ? -19.63693 -15.90609 -10.42254 1.000 16.92174 ? 139 SER   A C   1 
ATOM   1075 O  O   . SER   A 1 139 ? -19.97681 -14.82072 -9.93130  1.000 15.39253 ? 139 SER   A O   1 
ATOM   1076 C  CB  . SER   A 1 139 ? -21.33246 -17.31558 -9.17847  1.000 18.12915 ? 139 SER   A CB  1 
ATOM   1077 O  OG  . SER   A 1 139 ? -22.25053 -17.09368 -10.23286 1.000 20.56241 ? 139 SER   A OG  1 
ATOM   1078 N  N   . PHE   A 1 140 ? -19.03570 -16.02543 -11.60228 1.000 19.76172 ? 140 PHE   A N   1 
ATOM   1079 C  CA  . PHE   A 1 140 ? -18.46854 -14.91003 -12.34935 1.000 17.87577 ? 140 PHE   A CA  1 
ATOM   1080 C  C   . PHE   A 1 140 ? -18.63907 -15.19109 -13.83532 1.000 22.40647 ? 140 PHE   A C   1 
ATOM   1081 O  O   . PHE   A 1 140 ? -18.32767 -16.29309 -14.29449 1.000 23.07209 ? 140 PHE   A O   1 
ATOM   1082 C  CB  . PHE   A 1 140 ? -16.97241 -14.72865 -12.02649 1.000 17.64341 ? 140 PHE   A CB  1 
ATOM   1083 C  CG  . PHE   A 1 140 ? -16.67692 -14.12446 -10.68212 1.000 16.01939 ? 140 PHE   A CG  1 
ATOM   1084 C  CD1 . PHE   A 1 140 ? -17.12026 -12.85655 -10.36303 1.000 16.29975 ? 140 PHE   A CD1 1 
ATOM   1085 C  CD2 . PHE   A 1 140 ? -15.90749 -14.80749 -9.74351  1.000 16.41028 ? 140 PHE   A CD2 1 
ATOM   1086 C  CE1 . PHE   A 1 140 ? -16.82244 -12.28097 -9.13283  1.000 15.08077 ? 140 PHE   A CE1 1 
ATOM   1087 C  CE2 . PHE   A 1 140 ? -15.60965 -14.23275 -8.49616  1.000 17.43914 ? 140 PHE   A CE2 1 
ATOM   1088 C  CZ  . PHE   A 1 140 ? -16.06953 -12.95367 -8.20567  1.000 12.17269 ? 140 PHE   A CZ  1 
ATOM   1089 N  N   . LEU   A 1 141 ? -19.12689 -14.20928 -14.58642 1.000 19.98446 ? 141 LEU   A N   1 
ATOM   1090 C  CA  . LEU   A 1 141 ? -19.15687 -14.30533 -16.03682 1.000 24.54890 ? 141 LEU   A CA  1 
ATOM   1091 C  C   . LEU   A 1 141 ? -18.16383 -13.31215 -16.63408 1.000 24.42048 ? 141 LEU   A C   1 
ATOM   1092 O  O   . LEU   A 1 141 ? -17.51882 -12.54390 -15.92023 1.000 24.19614 ? 141 LEU   A O   1 
ATOM   1093 C  CB  . LEU   A 1 141 ? -20.57593 -14.06807 -16.55795 1.000 21.87793 ? 141 LEU   A CB  1 
ATOM   1094 C  CG  . LEU   A 1 141 ? -21.60644 -14.96924 -15.87761 1.000 27.85523 ? 141 LEU   A CG  1 
ATOM   1095 C  CD1 . LEU   A 1 141 ? -23.00321 -14.44472 -16.10828 1.000 29.20552 ? 141 LEU   A CD1 1 
ATOM   1096 C  CD2 . LEU   A 1 141 ? -21.49247 -16.40085 -16.35299 1.000 26.44396 ? 141 LEU   A CD2 1 
ATOM   1097 N  N   . ASN   A 1 142 ? -18.02883 -13.35701 -17.96047 1.000 27.12810 ? 142 ASN   A N   1 
ATOM   1098 C  CA  . ASN   A 1 142 ? -17.26684 -12.34753 -18.68225 1.000 27.21990 ? 142 ASN   A CA  1 
ATOM   1099 C  C   . ASN   A 1 142 ? -17.70858 -10.95568 -18.25596 1.000 26.21526 ? 142 ASN   A C   1 
ATOM   1100 O  O   . ASN   A 1 142 ? -18.90732 -10.64906 -18.22490 1.000 27.58948 ? 142 ASN   A O   1 
ATOM   1101 C  CB  . ASN   A 1 142 ? -17.46666 -12.50915 -20.18933 1.000 31.61158 ? 142 ASN   A CB  1 
ATOM   1102 C  CG  . ASN   A 1 142 ? -16.54177 -13.54001 -20.79708 1.000 36.52415 ? 142 ASN   A CG  1 
ATOM   1103 O  OD1 . ASN   A 1 142 ? -15.46035 -13.81347 -20.26512 1.000 39.32436 ? 142 ASN   A OD1 1 
ATOM   1104 N  ND2 . ASN   A 1 142 ? -16.96915 -14.13780 -21.91636 1.000 38.24000 ? 142 ASN   A ND2 1 
ATOM   1105 N  N   . GLY   A 1 143 ? -16.73462 -10.11380 -17.94029 1.000 23.43591 ? 143 GLY   A N   1 
ATOM   1106 C  CA  . GLY   A 1 143 ? -16.98690 -8.75007  -17.54209 1.000 23.87225 ? 143 GLY   A CA  1 
ATOM   1107 C  C   . GLY   A 1 143 ? -16.94224 -8.52265  -16.05202 1.000 22.20271 ? 143 GLY   A C   1 
ATOM   1108 O  O   . GLY   A 1 143 ? -17.04637 -7.37275  -15.61289 1.000 20.85203 ? 143 GLY   A O   1 
ATOM   1109 N  N   . SER   A 1 144 ? -16.79622 -9.58606  -15.26637 1.000 19.28242 ? 144 SER   A N   1 
ATOM   1110 C  CA  . SER   A 1 144 ? -16.81644 -9.47063  -13.81663 1.000 20.73798 ? 144 SER   A CA  1 
ATOM   1111 C  C   . SER   A 1 144 ? -15.47018 -9.07213  -13.22848 1.000 15.88360 ? 144 SER   A C   1 
ATOM   1112 O  O   . SER   A 1 144 ? -15.40467 -8.81925  -12.03038 1.000 15.32506 ? 144 SER   A O   1 
ATOM   1113 C  CB  . SER   A 1 144 ? -17.26798 -10.79501 -13.18942 1.000 19.13497 ? 144 SER   A CB  1 
ATOM   1114 O  OG  . SER   A 1 144 ? -16.38160 -11.83904 -13.56096 1.000 19.18279 ? 144 SER   A OG  1 
ATOM   1115 N  N   . CYS   A 1 145 ? -14.40073 -8.99910  -14.02729 1.000 18.02685 ? 145 CYS   A N   1 
ATOM   1116 C  CA  . CYS   A 1 145 ? -13.11480 -8.60626  -13.46252 1.000 20.17633 ? 145 CYS   A CA  1 
ATOM   1117 C  C   . CYS   A 1 145 ? -13.22145 -7.29042  -12.74172 1.000 15.66669 ? 145 CYS   A C   1 
ATOM   1118 O  O   . CYS   A 1 145 ? -13.89380 -6.35773  -13.19186 1.000 17.26026 ? 145 CYS   A O   1 
ATOM   1119 C  CB  . CYS   A 1 145 ? -12.04741 -8.40963  -14.52974 1.000 20.27789 ? 145 CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A 1 145 ? -11.12600 -9.90800  -14.86200 1.000 36.10312 ? 145 CYS   A SG  1 
ATOM   1121 N  N   . GLY   A 1 146 ? -12.46599 -7.19882  -11.66787 1.000 16.56324 ? 146 GLY   A N   1 
ATOM   1122 C  CA  . GLY   A 1 146 ? -12.47384 -6.02415  -10.86396 1.000 16.13961 ? 146 GLY   A CA  1 
ATOM   1123 C  C   . GLY   A 1 146 ? -13.51432 -6.04634  -9.79177  1.000 12.78168 ? 146 GLY   A C   1 
ATOM   1124 O  O   . GLY   A 1 146 ? -13.48024 -5.16808  -8.92170  1.000 14.58116 ? 146 GLY   A O   1 
ATOM   1125 N  N   . SER   A 1 147 ? -14.45068 -7.00549  -9.83563  1.000 14.25174 ? 147 SER   A N   1 
ATOM   1126 C  CA  . SER   A 1 147 ? -15.34121 -7.22004  -8.70279  1.000 12.88127 ? 147 SER   A CA  1 
ATOM   1127 C  C   . SER   A 1 147 ? -14.50145 -7.58010  -7.48511  1.000 13.19263 ? 147 SER   A C   1 
ATOM   1128 O  O   . SER   A 1 147 ? -13.44701 -8.22877  -7.60203  1.000 10.28239 ? 147 SER   A O   1 
ATOM   1129 C  CB  . SER   A 1 147 ? -16.35708 -8.33014  -9.00117  1.000 13.20558 ? 147 SER   A CB  1 
ATOM   1130 O  OG  . SER   A 1 147 ? -17.04838 -8.09419  -10.22985 1.000 14.72357 ? 147 SER   A OG  1 
ATOM   1131 N  N   . VAL   A 1 148 ? -14.94120 -7.12909  -6.30902  1.000 11.74068 ? 148 VAL   A N   1 
ATOM   1132 C  CA  . VAL   A 1 148 ? -14.13034 -7.27270  -5.11215  1.000 12.50685 ? 148 VAL   A CA  1 
ATOM   1133 C  C   . VAL   A 1 148 ? -14.81771 -8.12978  -4.04982  1.000 12.46754 ? 148 VAL   A C   1 
ATOM   1134 O  O   . VAL   A 1 148 ? -16.05856 -8.27052  -3.99723  1.000 10.69003 ? 148 VAL   A O   1 
ATOM   1135 C  CB  . VAL   A 1 148 ? -13.71873 -5.90171  -4.51954  1.000 13.40538 ? 148 VAL   A CB  1 
ATOM   1136 C  CG1 . VAL   A 1 148 ? -12.89610 -5.05949  -5.56385  1.000 11.42718 ? 148 VAL   A CG1 1 
ATOM   1137 C  CG2 . VAL   A 1 148 ? -14.91291 -5.15708  -4.02732  1.000 11.76679 ? 148 VAL   A CG2 1 
ATOM   1138 N  N   . GLY   A 1 149 ? -13.96264 -8.72298  -3.21001  1.000 10.44696 ? 149 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 149 ? -14.36703 -9.43615  -2.00865  1.000 8.95539  ? 149 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 149 ? -13.96499 -8.67527  -0.75510  1.000 10.99062 ? 149 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 149 ? -12.96494 -7.94280  -0.73166  1.000 9.66182  ? 149 GLY   A O   1 
ATOM   1142 N  N   . PHE   A 1 150 ? -14.72164 -8.87737  0.32064   1.000 9.66609  ? 150 PHE   A N   1 
ATOM   1143 C  CA  . PHE   A 1 150 ? -14.54423 -7.99438  1.44826   1.000 10.77810 ? 150 PHE   A CA  1 
ATOM   1144 C  C   . PHE   A 1 150 ? -15.24572 -8.57925  2.66022   1.000 12.28716 ? 150 PHE   A C   1 
ATOM   1145 O  O   . PHE   A 1 150 ? -16.10546 -9.45256  2.54141   1.000 10.72499 ? 150 PHE   A O   1 
ATOM   1146 C  CB  . PHE   A 1 150 ? -15.10419 -6.60609  1.14816   1.000 12.12188 ? 150 PHE   A CB  1 
ATOM   1147 C  CG  . PHE   A 1 150 ? -16.58357 -6.60899  0.93736   1.000 11.24520 ? 150 PHE   A CG  1 
ATOM   1148 C  CD1 . PHE   A 1 150 ? -17.11468 -6.93377  -0.31373  1.000 12.77899 ? 150 PHE   A CD1 1 
ATOM   1149 C  CD2 . PHE   A 1 150 ? -17.45691 -6.38673  2.00089   1.000 11.79400 ? 150 PHE   A CD2 1 
ATOM   1150 C  CE1 . PHE   A 1 150 ? -18.49784 -6.97974  -0.50854  1.000 12.86390 ? 150 PHE   A CE1 1 
ATOM   1151 C  CE2 . PHE   A 1 150 ? -18.83661 -6.42794  1.80189   1.000 14.33475 ? 150 PHE   A CE2 1 
ATOM   1152 C  CZ  . PHE   A 1 150 ? -19.34838 -6.72161  0.54287   1.000 14.77724 ? 150 PHE   A CZ  1 
ATOM   1153 N  N   . ASN   A 1 151 ? -14.86430 -8.06158  3.81728   1.000 13.15484 ? 151 ASN   A N   1 
ATOM   1154 C  CA  . ASN   A 1 151 ? -15.53485 -8.27886  5.08914   1.000 15.37050 ? 151 ASN   A CA  1 
ATOM   1155 C  C   . ASN   A 1 151 ? -15.79450 -6.91473  5.70535   1.000 15.40209 ? 151 ASN   A C   1 
ATOM   1156 O  O   . ASN   A 1 151 ? -15.15345 -5.93484  5.35413   1.000 13.56730 ? 151 ASN   A O   1 
ATOM   1157 C  CB  . ASN   A 1 151 ? -14.68612 -9.10247  6.04354   1.000 14.31679 ? 151 ASN   A CB  1 
ATOM   1158 C  CG  . ASN   A 1 151 ? -14.65772 -10.57410 5.68261   1.000 16.85907 ? 151 ASN   A CG  1 
ATOM   1159 O  OD1 . ASN   A 1 151 ? -15.60412 -11.32030 5.94127   1.000 15.86623 ? 151 ASN   A OD1 1 
ATOM   1160 N  ND2 . ASN   A 1 151 ? -13.58305 -10.98990 5.05208   1.000 12.09023 ? 151 ASN   A ND2 1 
ATOM   1161 N  N   . ILE   A 1 152 ? -16.72381 -6.84952  6.65081   1.000 14.76082 ? 152 ILE   A N   1 
ATOM   1162 C  CA  . ILE   A 1 152 ? -17.05548 -5.59721  7.31708   1.000 17.54018 ? 152 ILE   A CA  1 
ATOM   1163 C  C   . ILE   A 1 152 ? -16.96079 -5.82810  8.80924   1.000 24.12982 ? 152 ILE   A C   1 
ATOM   1164 O  O   . ILE   A 1 152 ? -17.49838 -6.81797  9.31903   1.000 20.23308 ? 152 ILE   A O   1 
ATOM   1165 C  CB  . ILE   A 1 152 ? -18.46665 -5.07953  6.96355   1.000 20.13633 ? 152 ILE   A CB  1 
ATOM   1166 C  CG1 . ILE   A 1 152 ? -18.72497 -5.17876  5.46042   1.000 19.56565 ? 152 ILE   A CG1 1 
ATOM   1167 C  CG2 . ILE   A 1 152 ? -18.64559 -3.64625  7.48884   1.000 21.18030 ? 152 ILE   A CG2 1 
ATOM   1168 C  CD1 . ILE   A 1 152 ? -17.91249 -4.25917  4.66834   1.000 18.43554 ? 152 ILE   A CD1 1 
ATOM   1169 N  N   . ASP   A 1 153 ? -16.30302 -4.90274  9.50190   1.000 27.91685 ? 153 ASP   A N   1 
ATOM   1170 C  CA  . ASP   A 1 153 ? -16.12677 -4.92894  10.95082  1.000 30.86882 ? 153 ASP   A CA  1 
ATOM   1171 C  C   . ASP   A 1 153 ? -16.65034 -3.60486  11.48107  1.000 34.25046 ? 153 ASP   A C   1 
ATOM   1172 O  O   . ASP   A 1 153 ? -16.04176 -2.55049  11.24322  1.000 34.47396 ? 153 ASP   A O   1 
ATOM   1173 C  CB  . ASP   A 1 153 ? -14.65975 -5.12112  11.33068  1.000 31.56781 ? 153 ASP   A CB  1 
ATOM   1174 C  CG  . ASP   A 1 153 ? -14.46535 -6.21909  12.33832  1.000 38.69939 ? 153 ASP   A CG  1 
ATOM   1175 O  OD1 . ASP   A 1 153 ? -15.24690 -6.25470  13.31483  1.000 39.48174 ? 153 ASP   A OD1 1 
ATOM   1176 O  OD2 . ASP   A 1 153 ? -13.52047 -7.03104  12.16485  1.000 41.78447 ? 153 ASP   A OD2 1 
ATOM   1177 N  N   . TYR   A 1 154 ? -17.76404 -3.67212  12.20542  1.000 35.33540 ? 154 TYR   A N   1 
ATOM   1178 C  CA  . TYR   A 1 154 ? -18.57599 -2.50881  12.51869  1.000 42.78032 ? 154 TYR   A CA  1 
ATOM   1179 C  C   . TYR   A 1 154 ? -18.80740 -1.67576  11.26412  1.000 41.46091 ? 154 TYR   A C   1 
ATOM   1180 O  O   . TYR   A 1 154 ? -19.68840 -1.97700  10.45401  1.000 43.22566 ? 154 TYR   A O   1 
ATOM   1181 C  CB  . TYR   A 1 154 ? -17.93685 -1.65609  13.61630  1.000 42.84148 ? 154 TYR   A CB  1 
ATOM   1182 C  CG  . TYR   A 1 154 ? -18.93043 -0.65720  14.18392  1.000 49.08669 ? 154 TYR   A CG  1 
ATOM   1183 C  CD1 . TYR   A 1 154 ? -20.27457 -1.00059  14.31577  1.000 50.65002 ? 154 TYR   A CD1 1 
ATOM   1184 C  CD2 . TYR   A 1 154 ? -18.53737 0.61625   14.58574  1.000 49.11683 ? 154 TYR   A CD2 1 
ATOM   1185 C  CE1 . TYR   A 1 154 ? -21.20146 -0.10680  14.83112  1.000 53.23178 ? 154 TYR   A CE1 1 
ATOM   1186 C  CE2 . TYR   A 1 154 ? -19.46092 1.52099   15.10401  1.000 51.92902 ? 154 TYR   A CE2 1 
ATOM   1187 C  CZ  . TYR   A 1 154 ? -20.79291 1.15353   15.22358  1.000 54.88334 ? 154 TYR   A CZ  1 
ATOM   1188 O  OH  . TYR   A 1 154 ? -21.72114 2.03981   15.73660  1.000 53.57577 ? 154 TYR   A OH  1 
ATOM   1189 N  N   . ASP   A 1 155 ? -18.00401 -0.64055  11.08276  1.000 37.32816 ? 155 ASP   A N   1 
ATOM   1190 C  CA  . ASP   A 1 155 ? -18.21449 0.31795   10.01136  1.000 36.24818 ? 155 ASP   A CA  1 
ATOM   1191 C  C   . ASP   A 1 155 ? -17.09202 0.34741   8.98072   1.000 31.75112 ? 155 ASP   A C   1 
ATOM   1192 O  O   . ASP   A 1 155 ? -17.13047 1.17838   8.05937   1.000 24.88586 ? 155 ASP   A O   1 
ATOM   1193 C  CB  . ASP   A 1 155 ? -18.41389 1.69890   10.63794  1.000 39.44392 ? 155 ASP   A CB  1 
ATOM   1194 C  CG  . ASP   A 1 155 ? -17.19995 2.15101   11.40477  1.000 40.46773 ? 155 ASP   A CG  1 
ATOM   1195 O  OD1 . ASP   A 1 155 ? -17.07082 3.36167   11.66264  1.000 42.95159 ? 155 ASP   A OD1 1 
ATOM   1196 O  OD2 . ASP   A 1 155 ? -16.36746 1.27779   11.75501  1.000 42.35139 ? 155 ASP   A OD2 1 
ATOM   1197 N  N   . CYS   A 1 156 ? -16.11599 -0.54808  9.09349   1.000 27.68634 ? 156 CYS   A N   1 
ATOM   1198 C  CA  . CYS   A 1 156 ? -14.90282 -0.50761  8.29143   1.000 22.71863 ? 156 CYS   A CA  1 
ATOM   1199 C  C   . CYS   A 1 156 ? -14.89158 -1.69194  7.33707   1.000 18.64339 ? 156 CYS   A C   1 
ATOM   1200 O  O   . CYS   A 1 156 ? -15.06322 -2.84161  7.76203   1.000 18.81130 ? 156 CYS   A O   1 
ATOM   1201 C  CB  . CYS   A 1 156 ? -13.66603 -0.54042  9.18259   1.000 24.09945 ? 156 CYS   A CB  1 
ATOM   1202 S  SG  . CYS   A 1 156 ? -12.13556 -0.78241  8.26443   1.000 23.13566 ? 156 CYS   A SG  1 
ATOM   1203 N  N   . VAL   A 1 157 ? -14.69955 -1.40646  6.05332   1.000 16.25462 ? 157 VAL   A N   1 
ATOM   1204 C  CA  . VAL   A 1 157 ? -14.67480 -2.43158  5.02065   1.000 14.02058 ? 157 VAL   A CA  1 
ATOM   1205 C  C   . VAL   A 1 157 ? -13.23914 -2.87984  4.84687   1.000 15.26983 ? 157 VAL   A C   1 
ATOM   1206 O  O   . VAL   A 1 157 ? -12.38653 -2.06814  4.47226   1.000 13.81328 ? 157 VAL   A O   1 
ATOM   1207 C  CB  . VAL   A 1 157 ? -15.20958 -1.90022  3.68523   1.000 14.05609 ? 157 VAL   A CB  1 
ATOM   1208 C  CG1 . VAL   A 1 157 ? -15.20456 -3.01231  2.65783   1.000 11.98723 ? 157 VAL   A CG1 1 
ATOM   1209 C  CG2 . VAL   A 1 157 ? -16.59565 -1.23454  3.83999   1.000 14.37705 ? 157 VAL   A CG2 1 
ATOM   1210 N  N   . SER   A 1 158 ? -12.97910 -4.17130  5.05396   1.000 14.04408 ? 158 SER   A N   1 
ATOM   1211 C  CA  . SER   A 1 158 ? -11.64362 -4.73587  4.81104   1.000 12.28783 ? 158 SER   A CA  1 
ATOM   1212 C  C   . SER   A 1 158 ? -11.70631 -5.42713  3.45623   1.000 11.81533 ? 158 SER   A C   1 
ATOM   1213 O  O   . SER   A 1 158 ? -12.28576 -6.50547  3.32328   1.000 12.97104 ? 158 SER   A O   1 
ATOM   1214 C  CB  . SER   A 1 158 ? -11.23776 -5.69745  5.92418   1.000 13.04279 ? 158 SER   A CB  1 
ATOM   1215 O  OG  . SER   A 1 158 ? -10.98816 -4.97344  7.12767   1.000 14.07212 ? 158 SER   A OG  1 
ATOM   1216 N  N   . PHE   A 1 159 ? -11.18549 -4.76987  2.43340   1.000 12.29311 ? 159 PHE   A N   1 
ATOM   1217 C  CA  . PHE   A 1 159 ? -11.13675 -5.37999  1.11367   1.000 11.66623 ? 159 PHE   A CA  1 
ATOM   1218 C  C   . PHE   A 1 159 ? -10.05312 -6.44198  1.10115   1.000 11.89984 ? 159 PHE   A C   1 
ATOM   1219 O  O   . PHE   A 1 159 ? -8.92349  -6.18080  1.51985   1.000 13.30309 ? 159 PHE   A O   1 
ATOM   1220 C  CB  . PHE   A 1 159 ? -10.85853 -4.31041  0.06028   1.000 13.67242 ? 159 PHE   A CB  1 
ATOM   1221 C  CG  . PHE   A 1 159 ? -12.00117 -3.32631  -0.12262  1.000 11.61712 ? 159 PHE   A CG  1 
ATOM   1222 C  CD1 . PHE   A 1 159 ? -13.13578 -3.68277  -0.85508  1.000 13.10496 ? 159 PHE   A CD1 1 
ATOM   1223 C  CD2 . PHE   A 1 159 ? -11.93933 -2.05673  0.45458   1.000 13.72228 ? 159 PHE   A CD2 1 
ATOM   1224 C  CE1 . PHE   A 1 159 ? -14.18037 -2.79177  -1.03773  1.000 11.31261 ? 159 PHE   A CE1 1 
ATOM   1225 C  CE2 . PHE   A 1 159 ? -12.97992 -1.15009  0.29701   1.000 12.57866 ? 159 PHE   A CE2 1 
ATOM   1226 C  CZ  . PHE   A 1 159 ? -14.12375 -1.53388  -0.46428  1.000 12.28576 ? 159 PHE   A CZ  1 
ATOM   1227 N  N   . CYS   A 1 160 ? -10.38397 -7.64109  0.62649   1.000 12.51828 ? 160 CYS   A N   1 
ATOM   1228 C  CA  . CYS   A 1 160 ? -9.37669  -8.67399  0.53477   1.000 11.76297 ? 160 CYS   A CA  1 
ATOM   1229 C  C   . CYS   A 1 160 ? -9.18826  -9.29281  -0.84083  1.000 13.13138 ? 160 CYS   A C   1 
ATOM   1230 O  O   . CYS   A 1 160 ? -8.19967  -10.01343 -1.00856  1.000 12.79365 ? 160 CYS   A O   1 
ATOM   1231 C  CB  . CYS   A 1 160 ? -9.66343  -9.80335  1.52959   1.000 9.78410  ? 160 CYS   A CB  1 
ATOM   1232 S  SG  . CYS   A 1 160 ? -11.32679 -10.48427 1.31460   1.000 12.28866 ? 160 CYS   A SG  1 
ATOM   1233 N  N   . TYR   A 1 161 ? -10.04771 -9.03018  -1.83187  1.000 9.16444  ? 161 TYR   A N   1 
ATOM   1234 C  CA  . TYR   A 1 161 ? -9.96623  -9.79276  -3.07796  1.000 11.31298 ? 161 TYR   A CA  1 
ATOM   1235 C  C   . TYR   A 1 161 ? -10.35167 -8.92549  -4.26599  1.000 14.02349 ? 161 TYR   A C   1 
ATOM   1236 O  O   . TYR   A 1 161 ? -11.31010 -8.16086  -4.19192  1.000 10.44215 ? 161 TYR   A O   1 
ATOM   1237 C  CB  . TYR   A 1 161 ? -10.85776 -11.04364 -3.03188  1.000 10.01229 ? 161 TYR   A CB  1 
ATOM   1238 C  CG  . TYR   A 1 161 ? -10.90096 -11.88319 -4.30905  1.000 9.87706  ? 161 TYR   A CG  1 
ATOM   1239 C  CD1 . TYR   A 1 161 ? -9.85619  -12.77965 -4.59440  1.000 11.93446 ? 161 TYR   A CD1 1 
ATOM   1240 C  CD2 . TYR   A 1 161 ? -11.96736 -11.80474 -5.21412  1.000 8.72179  ? 161 TYR   A CD2 1 
ATOM   1241 C  CE1 . TYR   A 1 161 ? -9.88067  -13.54618 -5.74365  1.000 10.18498 ? 161 TYR   A CE1 1 
ATOM   1242 C  CE2 . TYR   A 1 161 ? -12.00509 -12.57600 -6.39077  1.000 9.02345  ? 161 TYR   A CE2 1 
ATOM   1243 C  CZ  . TYR   A 1 161 ? -10.96365 -13.45362 -6.62690  1.000 10.74209 ? 161 TYR   A CZ  1 
ATOM   1244 O  OH  . TYR   A 1 161 ? -10.97820 -14.21426 -7.77270  1.000 11.14760 ? 161 TYR   A OH  1 
ATOM   1245 N  N   . MET   A 1 162 ? -9.57041  -9.00476  -5.34021  1.000 9.26107  ? 162 MET   A N   1 
ATOM   1246 C  CA  . MET   A 1 162 ? -10.01013 -8.48172  -6.62276  1.000 11.64483 ? 162 MET   A CA  1 
ATOM   1247 C  C   . MET   A 1 162 ? -10.01868 -9.60702  -7.64403  1.000 12.48536 ? 162 MET   A C   1 
ATOM   1248 O  O   . MET   A 1 162 ? -9.00596  -10.28956 -7.83541  1.000 8.38723  ? 162 MET   A O   1 
ATOM   1249 C  CB  . MET   A 1 162 ? -9.14207  -7.32313  -7.10530  1.000 14.18134 ? 162 MET   A CB  1 
ATOM   1250 C  CG  . MET   A 1 162 ? -9.77986  -6.58695  -8.28456  1.000 12.39200 ? 162 MET   A CG  1 
ATOM   1251 S  SD  . MET   A 1 162 ? -9.02290  -5.01911  -8.79491  1.000 17.03615 ? 162 MET   A SD  1 
ATOM   1252 C  CE  . MET   A 1 162 ? -9.97425  -3.81181  -7.87755  1.000 18.84038 ? 162 MET   A CE  1 
ATOM   1253 N  N   . HIS   A 1 163 ? -11.15667 -9.78168  -8.30308  1.000 10.04335 ? 163 HIS   A N   1 
ATOM   1254 C  CA  . HIS   A 1 163 ? -11.29404 -10.85918 -9.26956  1.000 10.95443 ? 163 HIS   A CA  1 
ATOM   1255 C  C   . HIS   A 1 163 ? -10.52694 -10.57358 -10.55644 1.000 11.92993 ? 163 HIS   A C   1 
ATOM   1256 O  O   . HIS   A 1 163 ? -10.68573 -9.51154  -11.15928 1.000 12.92225 ? 163 HIS   A O   1 
ATOM   1257 C  CB  . HIS   A 1 163 ? -12.75127 -11.07773 -9.62807  1.000 14.36292 ? 163 HIS   A CB  1 
ATOM   1258 C  CG  . HIS   A 1 163 ? -12.93299 -12.26759 -10.49366 1.000 12.57161 ? 163 HIS   A CG  1 
ATOM   1259 N  ND1 . HIS   A 1 163 ? -12.42581 -13.49836 -10.14507 1.000 14.74921 ? 163 HIS   A ND1 1 
ATOM   1260 C  CD2 . HIS   A 1 163 ? -13.50491 -12.42081 -11.70655 1.000 13.23486 ? 163 HIS   A CD2 1 
ATOM   1261 C  CE1 . HIS   A 1 163 ? -12.70104 -14.36812 -11.09640 1.000 13.49793 ? 163 HIS   A CE1 1 
ATOM   1262 N  NE2 . HIS   A 1 163 ? -13.36767 -13.74440 -12.04916 1.000 13.94025 ? 163 HIS   A NE2 1 
ATOM   1263 N  N   . HIS   A 1 164 ? -9.74545  -11.55670 -11.00753 1.000 14.76163 ? 164 HIS   A N   1 
ATOM   1264 C  CA  . HIS   A 1 164 ? -9.06323  -11.46727 -12.29780 1.000 13.59069 ? 164 HIS   A CA  1 
ATOM   1265 C  C   . HIS   A 1 164 ? -9.46360  -12.50903 -13.33009 1.000 17.02505 ? 164 HIS   A C   1 
ATOM   1266 O  O   . HIS   A 1 164 ? -9.55753  -12.17384 -14.50412 1.000 19.66299 ? 164 HIS   A O   1 
ATOM   1267 C  CB  . HIS   A 1 164 ? -7.54071  -11.55343 -12.10362 1.000 13.48453 ? 164 HIS   A CB  1 
ATOM   1268 C  CG  . HIS   A 1 164 ? -6.94457  -10.34150 -11.44902 1.000 14.55098 ? 164 HIS   A CG  1 
ATOM   1269 N  ND1 . HIS   A 1 164 ? -6.03740  -9.51470  -12.08435 1.000 14.29762 ? 164 HIS   A ND1 1 
ATOM   1270 C  CD2 . HIS   A 1 164 ? -7.13955  -9.81092  -10.21744 1.000 14.09858 ? 164 HIS   A CD2 1 
ATOM   1271 C  CE1 . HIS   A 1 164 ? -5.69144  -8.53466  -11.26691 1.000 13.96432 ? 164 HIS   A CE1 1 
ATOM   1272 N  NE2 . HIS   A 1 164 ? -6.32750  -8.70403  -10.11947 1.000 13.48231 ? 164 HIS   A NE2 1 
ATOM   1273 N  N   . MET   A 1 165 ? -9.63877  -13.77628 -12.98092 1.000 15.01797 ? 165 MET   A N   1 
ATOM   1274 C  CA  . MET   A 1 165 ? -9.72684  -14.74568 -14.07025 1.000 18.11969 ? 165 MET   A CA  1 
ATOM   1275 C  C   . MET   A 1 165 ? -10.42352 -16.00526 -13.61632 1.000 16.16345 ? 165 MET   A C   1 
ATOM   1276 O  O   . MET   A 1 165 ? -10.54375 -16.27082 -12.42014 1.000 18.11423 ? 165 MET   A O   1 
ATOM   1277 C  CB  . MET   A 1 165 ? -8.34255  -15.12522 -14.58874 1.000 18.11216 ? 165 MET   A CB  1 
ATOM   1278 C  CG  . MET   A 1 165 ? -7.36723  -15.21767 -13.46268 1.000 19.89669 ? 165 MET   A CG  1 
ATOM   1279 S  SD  . MET   A 1 165 ? -5.77062  -15.75818 -14.06587 1.000 32.50577 ? 165 MET   A SD  1 
ATOM   1280 C  CE  . MET   A 1 165 ? -5.89912  -17.46553 -13.60443 1.000 21.35247 ? 165 MET   A CE  1 
ATOM   1281 N  N   . GLU   A 1 166 ? -10.88308 -16.78104 -14.59475 1.000 17.34627 ? 166 GLU   A N   1 
ATOM   1282 C  CA  . GLU   A 1 166 ? -11.43574 -18.09754 -14.32708 1.000 18.70973 ? 166 GLU   A CA  1 
ATOM   1283 C  C   . GLU   A 1 166 ? -10.45768 -19.13814 -14.85067 1.000 18.42467 ? 166 GLU   A C   1 
ATOM   1284 O  O   . GLU   A 1 166 ? -9.85775  -18.95331 -15.91259 1.000 20.37252 ? 166 GLU   A O   1 
ATOM   1285 C  CB  . GLU   A 1 166 ? -12.82700 -18.26979 -14.94938 1.000 19.69231 ? 166 GLU   A CB  1 
ATOM   1286 C  CG  . GLU   A 1 166 ? -13.40653 -19.67850 -14.76621 1.000 21.98453 ? 166 GLU   A CG  1 
ATOM   1287 C  CD  . GLU   A 1 166 ? -14.89089 -19.74898 -15.12993 1.000 24.76832 ? 166 GLU   A CD  1 
ATOM   1288 O  OE1 . GLU   A 1 166 ? -15.67991 -18.90011 -14.66708 1.000 23.93167 ? 166 GLU   A OE1 1 
ATOM   1289 O  OE2 . GLU   A 1 166 ? -15.26043 -20.61711 -15.94338 1.000 28.13946 ? 166 GLU   A OE2 1 
ATOM   1290 N  N   . LEU   A 1 167 ? -10.22247 -20.17765 -14.04801 1.000 21.04545 ? 167 LEU   A N   1 
ATOM   1291 C  CA  . LEU   A 1 167 ? -9.33762  -21.28779 -14.37248 1.000 21.81203 ? 167 LEU   A CA  1 
ATOM   1292 C  C   . LEU   A 1 167 ? -10.14087 -22.37821 -15.06450 1.000 24.18636 ? 167 LEU   A C   1 
ATOM   1293 O  O   . LEU   A 1 167 ? -11.37253 -22.36417 -15.01493 1.000 25.01852 ? 167 LEU   A O   1 
ATOM   1294 C  CB  . LEU   A 1 167 ? -8.69253  -21.82223 -13.09771 1.000 20.87060 ? 167 LEU   A CB  1 
ATOM   1295 C  CG  . LEU   A 1 167 ? -7.69683  -20.92546 -12.35944 1.000 18.88213 ? 167 LEU   A CG  1 
ATOM   1296 C  CD1 . LEU   A 1 167 ? -7.42966  -21.50879 -10.99534 1.000 17.48563 ? 167 LEU   A CD1 1 
ATOM   1297 C  CD2 . LEU   A 1 167 ? -6.40019  -20.85317 -13.14673 1.000 21.52077 ? 167 LEU   A CD2 1 
ATOM   1298 N  N   . PRO   A 1 168 ? -9.48319  -23.34665 -15.72036 1.000 25.06010 ? 168 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 168 ? -10.23872 -24.30140 -16.55647 1.000 25.33070 ? 168 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 168 ? -11.26343 -25.14683 -15.80260 1.000 25.91212 ? 168 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 168 ? -12.23346 -25.60435 -16.42174 1.000 28.39862 ? 168 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 168 ? -9.13741  -25.17496 -17.17465 1.000 27.27600 ? 168 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 168 ? -7.90039  -24.32887 -17.12817 1.000 27.60257 ? 168 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 168 ? -8.02433  -23.53630 -15.85552 1.000 25.64119 ? 168 PRO   A CD  1 
ATOM   1305 N  N   . THR   A 1 169 ? -11.08790 -25.38938 -14.50799 1.000 22.40611 ? 169 THR   A N   1 
ATOM   1306 C  CA  . THR   A 1 169 ? -12.10591 -26.13271 -13.76477 1.000 24.98018 ? 169 THR   A CA  1 
ATOM   1307 C  C   . THR   A 1 169 ? -13.30571 -25.28117 -13.36640 1.000 22.93867 ? 169 THR   A C   1 
ATOM   1308 O  O   . THR   A 1 169 ? -14.18423 -25.78192 -12.65457 1.000 24.05972 ? 169 THR   A O   1 
ATOM   1309 C  CB  . THR   A 1 169 ? -11.51041 -26.77265 -12.50395 1.000 24.42438 ? 169 THR   A CB  1 
ATOM   1310 O  OG1 . THR   A 1 169 ? -10.77718 -25.79007 -11.76028 1.000 22.81775 ? 169 THR   A OG1 1 
ATOM   1311 C  CG2 . THR   A 1 169 ? -10.60245 -27.92454 -12.86729 1.000 23.37742 ? 169 THR   A CG2 1 
ATOM   1312 N  N   . GLY   A 1 170 ? -13.37819 -24.02780 -13.79992 1.000 23.54495 ? 170 GLY   A N   1 
ATOM   1313 C  CA  . GLY   A 1 170 ? -14.49973 -23.18605 -13.42437 1.000 22.27301 ? 170 GLY   A CA  1 
ATOM   1314 C  C   . GLY   A 1 170 ? -14.37995 -22.48471 -12.08666 1.000 20.09548 ? 170 GLY   A C   1 
ATOM   1315 O  O   . GLY   A 1 170 ? -15.35644 -21.85155 -11.65394 1.000 21.67849 ? 170 GLY   A O   1 
ATOM   1316 N  N   . VAL   A 1 171 ? -13.23395 -22.58119 -11.41807 1.000 19.36045 ? 171 VAL   A N   1 
ATOM   1317 C  CA  . VAL   A 1 171 ? -12.95676 -21.82272 -10.20857 1.000 16.10237 ? 171 VAL   A CA  1 
ATOM   1318 C  C   . VAL   A 1 171 ? -12.18659 -20.56888 -10.58991 1.000 15.97154 ? 171 VAL   A C   1 
ATOM   1319 O  O   . VAL   A 1 171 ? -11.77938 -20.38196 -11.73823 1.000 15.86669 ? 171 VAL   A O   1 
ATOM   1320 C  CB  . VAL   A 1 171 ? -12.18006 -22.66697 -9.15819  1.000 16.66080 ? 171 VAL   A CB  1 
ATOM   1321 C  CG1 . VAL   A 1 171 ? -12.95709 -23.94394 -8.80793  1.000 18.87248 ? 171 VAL   A CG1 1 
ATOM   1322 C  CG2 . VAL   A 1 171 ? -10.76974 -23.01131 -9.66556  1.000 17.02271 ? 171 VAL   A CG2 1 
ATOM   1323 N  N   . HIS   A 1 172 ? -11.97016 -19.68706 -9.61684  1.000 13.61319 ? 172 HIS   A N   1 
ATOM   1324 C  CA  . HIS   A 1 172 ? -11.60984 -18.30858 -9.90379  1.000 12.50745 ? 172 HIS   A CA  1 
ATOM   1325 C  C   . HIS   A 1 172 ? -10.32969 -17.93658 -9.17005  1.000 12.81872 ? 172 HIS   A C   1 
ATOM   1326 O  O   . HIS   A 1 172 ? -10.03849 -18.45149 -8.08685  1.000 10.58120 ? 172 HIS   A O   1 
ATOM   1327 C  CB  . HIS   A 1 172 ? -12.80735 -17.40424 -9.54899  1.000 16.02107 ? 172 HIS   A CB  1 
ATOM   1328 C  CG  . HIS   A 1 172 ? -14.04730 -17.77635 -10.31301 1.000 15.53157 ? 172 HIS   A CG  1 
ATOM   1329 N  ND1 . HIS   A 1 172 ? -15.09579 -18.47455 -9.74397  1.000 14.59321 ? 172 HIS   A ND1 1 
ATOM   1330 C  CD2 . HIS   A 1 172 ? -14.35881 -17.63423 -11.62438 1.000 16.43386 ? 172 HIS   A CD2 1 
ATOM   1331 C  CE1 . HIS   A 1 172 ? -16.01930 -18.70232 -10.66232 1.000 17.42679 ? 172 HIS   A CE1 1 
ATOM   1332 N  NE2 . HIS   A 1 172 ? -15.59798 -18.20680 -11.81472 1.000 13.55589 ? 172 HIS   A NE2 1 
ATOM   1333 N  N   . ALA   A 1 173 ? -9.54094  -17.07333 -9.79975  1.000 14.80910 ? 173 ALA   A N   1 
ATOM   1334 C  CA  . ALA   A 1 173 ? -8.30762  -16.60028 -9.20218  1.000 11.46546 ? 173 ALA   A CA  1 
ATOM   1335 C  C   . ALA   A 1 173 ? -8.26314  -15.08124 -9.25142  1.000 12.31135 ? 173 ALA   A C   1 
ATOM   1336 O  O   . ALA   A 1 173 ? -8.83977  -14.45166 -10.14353 1.000 11.50563 ? 173 ALA   A O   1 
ATOM   1337 C  CB  . ALA   A 1 173 ? -7.08579  -17.21084 -9.90739  1.000 13.44287 ? 173 ALA   A CB  1 
ATOM   1338 N  N   . GLY   A 1 174 ? -7.58892  -14.49406 -8.27011  1.000 10.85297 ? 174 GLY   A N   1 
ATOM   1339 C  CA  . GLY   A 1 174 ? -7.46742  -13.05153 -8.24860  1.000 10.49707 ? 174 GLY   A CA  1 
ATOM   1340 C  C   . GLY   A 1 174 ? -6.38223  -12.61831 -7.29631  1.000 11.69541 ? 174 GLY   A C   1 
ATOM   1341 O  O   . GLY   A 1 174 ? -5.60406  -13.43290 -6.79248  1.000 10.14225 ? 174 GLY   A O   1 
ATOM   1342 N  N   . THR   A 1 175 ? -6.38576  -11.32647 -6.99413  1.000 10.26436 ? 175 THR   A N   1 
ATOM   1343 C  CA  . THR   A 1 175 ? -5.34682  -10.73878 -6.16959  1.000 10.55072 ? 175 THR   A CA  1 
ATOM   1344 C  C   . THR   A 1 175 ? -5.94246  -10.15656 -4.89513  1.000 8.96641  ? 175 THR   A C   1 
ATOM   1345 O  O   . THR   A 1 175 ? -7.17326  -10.00923 -4.75378  1.000 8.99412  ? 175 THR   A O   1 
ATOM   1346 C  CB  . THR   A 1 175 ? -4.59769  -9.62451  -6.92939  1.000 13.16231 ? 175 THR   A CB  1 
ATOM   1347 O  OG1 . THR   A 1 175 ? -5.49853  -8.51736  -7.15469  1.000 9.49361  ? 175 THR   A OG1 1 
ATOM   1348 C  CG2 . THR   A 1 175 ? -3.97881  -10.14031 -8.23463  1.000 11.98559 ? 175 THR   A CG2 1 
ATOM   1349 N  N   . ASP   A 1 176 ? -5.05271  -9.78983  -3.98535  1.000 9.34617  ? 176 ASP   A N   1 
ATOM   1350 C  CA  . ASP   A 1 176 ? -5.40210  -8.85334  -2.93631  1.000 12.07232 ? 176 ASP   A CA  1 
ATOM   1351 C  C   . ASP   A 1 176 ? -5.41952  -7.46481  -3.57525  1.000 9.37480  ? 176 ASP   A C   1 
ATOM   1352 O  O   . ASP   A 1 176 ? -5.20161  -7.32126  -4.77616  1.000 10.64672 ? 176 ASP   A O   1 
ATOM   1353 C  CB  . ASP   A 1 176 ? -4.48484  -8.99562  -1.71323  1.000 10.94699 ? 176 ASP   A CB  1 
ATOM   1354 C  CG  . ASP   A 1 176 ? -3.04002  -8.64516  -1.95480  1.000 12.92252 ? 176 ASP   A CG  1 
ATOM   1355 O  OD1 . ASP   A 1 176 ? -2.73852  -7.84742  -2.87135  1.000 9.08844  ? 176 ASP   A OD1 1 
ATOM   1356 O  OD2 . ASP   A 1 176 ? -2.20603  -9.08412  -1.09689  1.000 12.28745 ? 176 ASP   A OD2 1 
ATOM   1357 N  N   . LEU   A 1 177 ? -5.76126  -6.43861  -2.79556  1.000 12.18022 ? 177 LEU   A N   1 
ATOM   1358 C  CA  . LEU   A 1 177 ? -5.91345  -5.09628  -3.35900  1.000 11.59122 ? 177 LEU   A CA  1 
ATOM   1359 C  C   . LEU   A 1 177 ? -4.58104  -4.36967  -3.48174  1.000 14.37592 ? 177 LEU   A C   1 
ATOM   1360 O  O   . LEU   A 1 177 ? -4.56213  -3.21701  -3.92823  1.000 16.91108 ? 177 LEU   A O   1 
ATOM   1361 C  CB  . LEU   A 1 177 ? -6.91521  -4.26609  -2.53240  1.000 13.95038 ? 177 LEU   A CB  1 
ATOM   1362 C  CG  . LEU   A 1 177 ? -8.40322  -4.34374  -2.98111  1.000 15.31475 ? 177 LEU   A CG  1 
ATOM   1363 C  CD1 . LEU   A 1 177 ? -8.66691  -3.69666  -4.34076  1.000 12.21282 ? 177 LEU   A CD1 1 
ATOM   1364 C  CD2 . LEU   A 1 177 ? -8.91906  -5.79513  -3.02697  1.000 13.56495 ? 177 LEU   A CD2 1 
ATOM   1365 N  N   . GLU   A 1 178 ? -3.48248  -4.99415  -3.06746  1.000 13.25408 ? 178 GLU   A N   1 
ATOM   1366 C  CA  . GLU   A 1 178 ? -2.15544  -4.52857  -3.48406  1.000 15.04540 ? 178 GLU   A CA  1 
ATOM   1367 C  C   . GLU   A 1 178 ? -1.71903  -5.13524  -4.80962  1.000 13.65450 ? 178 GLU   A C   1 
ATOM   1368 O  O   . GLU   A 1 178 ? -0.62612  -4.82144  -5.28508  1.000 13.54065 ? 178 GLU   A O   1 
ATOM   1369 C  CB  . GLU   A 1 178 ? -1.10861  -4.82681  -2.40006  1.000 15.41431 ? 178 GLU   A CB  1 
ATOM   1370 C  CG  . GLU   A 1 178 ? -1.70754  -4.61311  -1.03533  1.000 18.41768 ? 178 GLU   A CG  1 
ATOM   1371 C  CD  . GLU   A 1 178 ? -1.57543  -3.20926  -0.51365  1.000 22.25740 ? 178 GLU   A CD  1 
ATOM   1372 O  OE1 . GLU   A 1 178 ? -1.42217  -2.25398  -1.31951  1.000 21.36815 ? 178 GLU   A OE1 1 
ATOM   1373 O  OE2 . GLU   A 1 178 ? -1.71165  -3.05873  0.73860   1.000 24.67209 ? 178 GLU   A OE2 1 
ATOM   1374 N  N   . GLY   A 1 179 ? -2.54671  -5.96695  -5.42896  1.000 12.91507 ? 179 GLY   A N   1 
ATOM   1375 C  CA  . GLY   A 1 179 ? -2.23198  -6.55374  -6.70983  1.000 13.45883 ? 179 GLY   A CA  1 
ATOM   1376 C  C   . GLY   A 1 179 ? -1.40102  -7.81666  -6.66626  1.000 12.60940 ? 179 GLY   A C   1 
ATOM   1377 O  O   . GLY   A 1 179 ? -0.87426  -8.22382  -7.71214  1.000 15.15604 ? 179 GLY   A O   1 
ATOM   1378 N  N   . ASN   A 1 180 ? -1.26641  -8.45088  -5.50153  1.000 10.56801 ? 180 ASN   A N   1 
ATOM   1379 C  CA  . ASN   A 1 180 ? -0.49043  -9.67904  -5.38383  1.000 13.04999 ? 180 ASN   A CA  1 
ATOM   1380 C  C   . ASN   A 1 180 ? -1.44005  -10.86020 -5.48085  1.000 11.34036 ? 180 ASN   A C   1 
ATOM   1381 O  O   . ASN   A 1 180 ? -2.36092  -10.96946 -4.68336  1.000 12.19024 ? 180 ASN   A O   1 
ATOM   1382 C  CB  . ASN   A 1 180 ? 0.29326   -9.67637  -4.06969  1.000 10.35206 ? 180 ASN   A CB  1 
ATOM   1383 C  CG  . ASN   A 1 180 ? 1.21509   -8.50617  -3.99607  1.000 13.38851 ? 180 ASN   A CG  1 
ATOM   1384 O  OD1 . ASN   A 1 180 ? 2.12656   -8.37740  -4.81725  1.000 13.67600 ? 180 ASN   A OD1 1 
ATOM   1385 N  ND2 . ASN   A 1 180 ? 0.98480   -7.60745  -3.02219  1.000 12.90814 ? 180 ASN   A ND2 1 
ATOM   1386 N  N   . PHE   A 1 181 ? -1.20331  -11.74627 -6.45691  1.000 12.32259 ? 181 PHE   A N   1 
ATOM   1387 C  CA  . PHE   A 1 181 ? -2.09826  -12.87539 -6.64228  1.000 12.53750 ? 181 PHE   A CA  1 
ATOM   1388 C  C   . PHE   A 1 181 ? -2.18891  -13.74341 -5.39568  1.000 13.17443 ? 181 PHE   A C   1 
ATOM   1389 O  O   . PHE   A 1 181 ? -1.21580  -13.93191 -4.65625  1.000 9.91546  ? 181 PHE   A O   1 
ATOM   1390 C  CB  . PHE   A 1 181 ? -1.67545  -13.73807 -7.82471  1.000 12.39394 ? 181 PHE   A CB  1 
ATOM   1391 C  CG  . PHE   A 1 181 ? -2.45244  -13.46754 -9.04431  1.000 12.64977 ? 181 PHE   A CG  1 
ATOM   1392 C  CD1 . PHE   A 1 181 ? -3.72177  -14.03669 -9.21553  1.000 12.66087 ? 181 PHE   A CD1 1 
ATOM   1393 C  CD2 . PHE   A 1 181 ? -1.99791  -12.55547 -9.97181  1.000 10.62714 ? 181 PHE   A CD2 1 
ATOM   1394 C  CE1 . PHE   A 1 181 ? -4.44740  -13.75731 -10.35970 1.000 10.83996 ? 181 PHE   A CE1 1 
ATOM   1395 C  CE2 . PHE   A 1 181 ? -2.72477  -12.27411 -11.10410 1.000 16.58114 ? 181 PHE   A CE2 1 
ATOM   1396 C  CZ  . PHE   A 1 181 ? -3.97443  -12.86673 -11.28307 1.000 15.48103 ? 181 PHE   A CZ  1 
ATOM   1397 N  N   . TYR   A 1 182 ? -3.40710  -14.23858 -5.15917  1.000 10.55452 ? 182 TYR   A N   1 
ATOM   1398 C  CA  . TYR   A 1 182 ? -3.64987  -15.37652 -4.28740  1.000 9.66664  ? 182 TYR   A CA  1 
ATOM   1399 C  C   . TYR   A 1 182 ? -3.26198  -16.64120 -5.03504  1.000 13.77228 ? 182 TYR   A C   1 
ATOM   1400 O  O   . TYR   A 1 182 ? -3.87091  -16.96408 -6.05583  1.000 11.42456 ? 182 TYR   A O   1 
ATOM   1401 C  CB  . TYR   A 1 182 ? -5.11162  -15.41240 -3.84814  1.000 9.01560  ? 182 TYR   A CB  1 
ATOM   1402 C  CG  . TYR   A 1 182 ? -5.44175  -14.38329 -2.79634  1.000 11.59003 ? 182 TYR   A CG  1 
ATOM   1403 C  CD1 . TYR   A 1 182 ? -5.14647  -14.62912 -1.45094  1.000 12.88767 ? 182 TYR   A CD1 1 
ATOM   1404 C  CD2 . TYR   A 1 182 ? -6.12979  -13.22129 -3.11256  1.000 10.81253 ? 182 TYR   A CD2 1 
ATOM   1405 C  CE1 . TYR   A 1 182 ? -5.46862  -13.69772 -0.43506  1.000 10.01220 ? 182 TYR   A CE1 1 
ATOM   1406 C  CE2 . TYR   A 1 182 ? -6.47217  -12.28483 -2.10229  1.000 9.42206  ? 182 TYR   A CE2 1 
ATOM   1407 C  CZ  . TYR   A 1 182 ? -6.15159  -12.53892 -0.79115  1.000 11.93578 ? 182 TYR   A CZ  1 
ATOM   1408 O  OH  . TYR   A 1 182 ? -6.48205  -11.60994 0.15927   1.000 10.74044 ? 182 TYR   A OH  1 
ATOM   1409 N  N   . GLY   A 1 183 ? -2.19457  -17.30543 -4.57971  1.000 12.42532 ? 183 GLY   A N   1 
ATOM   1410 C  CA  . GLY   A 1 183 ? -1.78267  -18.55954 -5.16670  1.000 14.57865 ? 183 GLY   A CA  1 
ATOM   1411 C  C   . GLY   A 1 183 ? -0.84192  -18.41045 -6.34968  1.000 13.99593 ? 183 GLY   A C   1 
ATOM   1412 O  O   . GLY   A 1 183 ? -0.42736  -17.30944 -6.73212  1.000 10.79845 ? 183 GLY   A O   1 
ATOM   1413 N  N   . PRO   A 1 184 ? -0.49547  -19.52842 -6.94993  1.000 11.76757 ? 184 PRO   A N   1 
ATOM   1414 C  CA  . PRO   A 1 184 ? 0.52582   -19.54970 -8.01729  1.000 15.03312 ? 184 PRO   A CA  1 
ATOM   1415 C  C   . PRO   A 1 184 ? -0.07594  -19.31353 -9.40244  1.000 16.48276 ? 184 PRO   A C   1 
ATOM   1416 O  O   . PRO   A 1 184 ? 0.02008   -20.16453 -10.30493 1.000 19.61318 ? 184 PRO   A O   1 
ATOM   1417 C  CB  . PRO   A 1 184 ? 1.09931   -20.96139 -7.87896  1.000 18.22226 ? 184 PRO   A CB  1 
ATOM   1418 C  CG  . PRO   A 1 184 ? -0.09699  -21.78634 -7.42151  1.000 17.68806 ? 184 PRO   A CG  1 
ATOM   1419 C  CD  . PRO   A 1 184 ? -0.93434  -20.88199 -6.56041  1.000 15.87564 ? 184 PRO   A CD  1 
ATOM   1420 N  N   . PHE   A 1 185 ? -0.67109  -18.13765 -9.59301  1.000 13.63355 ? 185 PHE   A N   1 
ATOM   1421 C  CA  . PHE   A 1 185 ? -1.34551  -17.78688 -10.83958 1.000 14.32337 ? 185 PHE   A CA  1 
ATOM   1422 C  C   . PHE   A 1 185 ? -0.82288  -16.45107 -11.34937 1.000 18.84100 ? 185 PHE   A C   1 
ATOM   1423 O  O   . PHE   A 1 185 ? -0.33781  -15.61372 -10.57395 1.000 17.31573 ? 185 PHE   A O   1 
ATOM   1424 C  CB  . PHE   A 1 185 ? -2.87544  -17.73521 -10.65049 1.000 15.85113 ? 185 PHE   A CB  1 
ATOM   1425 C  CG  . PHE   A 1 185 ? -3.42384  -18.95215 -9.98637  1.000 15.55750 ? 185 PHE   A CG  1 
ATOM   1426 C  CD1 . PHE   A 1 185 ? -3.37591  -20.17416 -10.61970 1.000 16.67951 ? 185 PHE   A CD1 1 
ATOM   1427 C  CD2 . PHE   A 1 185 ? -3.95542  -18.88378 -8.72226  1.000 14.22693 ? 185 PHE   A CD2 1 
ATOM   1428 C  CE1 . PHE   A 1 185 ? -3.85415  -21.31095 -9.98839  1.000 16.41267 ? 185 PHE   A CE1 1 
ATOM   1429 C  CE2 . PHE   A 1 185 ? -4.41527  -20.01279 -8.08833  1.000 14.82734 ? 185 PHE   A CE2 1 
ATOM   1430 C  CZ  . PHE   A 1 185 ? -4.36936  -21.23492 -8.73083  1.000 14.73200 ? 185 PHE   A CZ  1 
ATOM   1431 N  N   . VAL   A 1 186 ? -0.91053  -16.25891 -12.66358 1.000 18.83631 ? 186 VAL   A N   1 
ATOM   1432 C  CA  . VAL   A 1 186 ? -0.35187  -15.07892 -13.31142 1.000 18.48636 ? 186 VAL   A CA  1 
ATOM   1433 C  C   . VAL   A 1 186 ? -1.40253  -14.48785 -14.24363 1.000 22.06984 ? 186 VAL   A C   1 
ATOM   1434 O  O   . VAL   A 1 186 ? -2.30840  -15.18646 -14.70969 1.000 21.05231 ? 186 VAL   A O   1 
ATOM   1435 C  CB  . VAL   A 1 186 ? 0.95559   -15.41812 -14.06067 1.000 24.96394 ? 186 VAL   A CB  1 
ATOM   1436 C  CG1 . VAL   A 1 186 ? 2.03472   -15.82461 -13.04942 1.000 22.36784 ? 186 VAL   A CG1 1 
ATOM   1437 C  CG2 . VAL   A 1 186 ? 0.73211   -16.51524 -15.09209 1.000 24.91748 ? 186 VAL   A CG2 1 
ATOM   1438 N  N   . ASP   A 1 187 ? -1.29324  -13.18705 -14.51230 1.000 19.72752 ? 187 ASP   A N   1 
ATOM   1439 C  CA  . ASP   A 1 187 ? -2.23869  -12.55388 -15.43871 1.000 23.36392 ? 187 ASP   A CA  1 
ATOM   1440 C  C   . ASP   A 1 187 ? -1.67767  -12.56323 -16.86334 1.000 24.02736 ? 187 ASP   A C   1 
ATOM   1441 O  O   . ASP   A 1 187 ? -1.37119  -11.54290 -17.47529 1.000 23.21536 ? 187 ASP   A O   1 
ATOM   1442 C  CB  . ASP   A 1 187 ? -2.62070  -11.15455 -14.96387 1.000 20.86981 ? 187 ASP   A CB  1 
ATOM   1443 C  CG  . ASP   A 1 187 ? -1.43696  -10.29199 -14.60691 1.000 19.40609 ? 187 ASP   A CG  1 
ATOM   1444 O  OD1 . ASP   A 1 187 ? -0.28022  -10.77906 -14.58893 1.000 17.60480 ? 187 ASP   A OD1 1 
ATOM   1445 O  OD2 . ASP   A 1 187 ? -1.69016  -9.10860  -14.28813 1.000 17.42588 ? 187 ASP   A OD2 1 
ATOM   1446 N  N   . ARG   A 1 188 ? -1.49332  -13.79144 -17.34339 1.000 26.91755 ? 188 ARG   A N   1 
ATOM   1447 C  CA  . ARG   A 1 188 ? -1.21937  -14.13182 -18.73057 1.000 31.59745 ? 188 ARG   A CA  1 
ATOM   1448 C  C   . ARG   A 1 188 ? -1.99760  -15.39196 -19.04599 1.000 34.98866 ? 188 ARG   A C   1 
ATOM   1449 O  O   . ARG   A 1 188 ? -2.41457  -16.12172 -18.13905 1.000 30.03156 ? 188 ARG   A O   1 
ATOM   1450 C  CB  . ARG   A 1 188 ? 0.25071   -14.42156 -19.02296 1.000 34.76005 ? 188 ARG   A CB  1 
ATOM   1451 C  CG  . ARG   A 1 188 ? 1.23764   -13.54304 -18.36694 1.000 34.61327 ? 188 ARG   A CG  1 
ATOM   1452 C  CD  . ARG   A 1 188 ? 2.64153   -14.05095 -18.67382 1.000 37.96651 ? 188 ARG   A CD  1 
ATOM   1453 N  NE  . ARG   A 1 188 ? 3.23107   -14.65513 -17.48713 1.000 37.37056 ? 188 ARG   A NE  1 
ATOM   1454 C  CZ  . ARG   A 1 188 ? 3.79236   -15.85488 -17.44908 1.000 35.41238 ? 188 ARG   A CZ  1 
ATOM   1455 N  NH1 . ARG   A 1 188 ? 3.73980   -16.67778 -18.48426 1.000 36.83857 ? 188 ARG   A NH1 1 
ATOM   1456 N  NH2 . ARG   A 1 188 ? 4.39392   -16.25121 -16.33093 1.000 35.81071 ? 188 ARG   A NH2 1 
ATOM   1457 N  N   . GLN   A 1 189 ? -2.14392  -15.67710 -20.33925 1.000 37.10358 ? 189 GLN   A N   1 
ATOM   1458 C  CA  . GLN   A 1 189 ? -2.90263  -16.85838 -20.73994 1.000 39.95448 ? 189 GLN   A CA  1 
ATOM   1459 C  C   . GLN   A 1 189 ? -1.91904  -18.00043 -20.94765 1.000 36.77497 ? 189 GLN   A C   1 
ATOM   1460 O  O   . GLN   A 1 189 ? -1.34166  -18.17853 -22.02134 1.000 41.91690 ? 189 GLN   A O   1 
ATOM   1461 C  CB  . GLN   A 1 189 ? -3.76575  -16.57849 -21.96361 1.000 43.16321 ? 189 GLN   A CB  1 
ATOM   1462 C  CG  . GLN   A 1 189 ? -4.57219  -17.78806 -22.41954 1.000 45.43799 ? 189 GLN   A CG  1 
ATOM   1463 C  CD  . GLN   A 1 189 ? -5.94945  -17.39761 -22.94675 1.000 54.04330 ? 189 GLN   A CD  1 
ATOM   1464 O  OE1 . GLN   A 1 189 ? -6.30376  -16.21076 -22.98153 1.000 54.65524 ? 189 GLN   A OE1 1 
ATOM   1465 N  NE2 . GLN   A 1 189 ? -6.73304  -18.39121 -23.35588 1.000 56.66493 ? 189 GLN   A NE2 1 
ATOM   1466 N  N   . THR   A 1 190 ? -1.72082  -18.76735 -19.88016 1.000 33.57300 ? 190 THR   A N   1 
ATOM   1467 C  CA  . THR   A 1 190 ? -0.94415  -19.99487 -19.85035 1.000 33.56196 ? 190 THR   A CA  1 
ATOM   1468 C  C   . THR   A 1 190 ? -1.88994  -21.15980 -19.59632 1.000 32.41887 ? 190 THR   A C   1 
ATOM   1469 O  O   . THR   A 1 190 ? -3.10860  -20.99184 -19.49147 1.000 32.64726 ? 190 THR   A O   1 
ATOM   1470 C  CB  . THR   A 1 190 ? 0.12475   -19.93708 -18.75762 1.000 31.73461 ? 190 THR   A CB  1 
ATOM   1471 O  OG1 . THR   A 1 190 ? -0.50962  -19.93832 -17.47707 1.000 32.13426 ? 190 THR   A OG1 1 
ATOM   1472 C  CG2 . THR   A 1 190 ? 0.93961   -18.66366 -18.87735 1.000 34.84948 ? 190 THR   A CG2 1 
ATOM   1473 N  N   . ALA   A 1 191 ? -1.31616  -22.35340 -19.46024 1.000 31.45034 ? 191 ALA   A N   1 
ATOM   1474 C  CA  . ALA   A 1 191 ? -2.09331  -23.52417 -19.07600 1.000 30.97333 ? 191 ALA   A CA  1 
ATOM   1475 C  C   . ALA   A 1 191 ? -2.21239  -23.68361 -17.55669 1.000 29.77318 ? 191 ALA   A C   1 
ATOM   1476 O  O   . ALA   A 1 191 ? -2.34241  -24.81476 -17.07380 1.000 31.22271 ? 191 ALA   A O   1 
ATOM   1477 C  CB  . ALA   A 1 191 ? -1.49443  -24.78201 -19.71022 1.000 30.96916 ? 191 ALA   A CB  1 
ATOM   1478 N  N   . GLN   A 1 192 ? -2.18980  -22.58742 -16.79199 1.000 27.62089 ? 192 GLN   A N   1 
ATOM   1479 C  CA  . GLN   A 1 192 ? -2.25754  -22.68994 -15.33671 1.000 27.49524 ? 192 GLN   A CA  1 
ATOM   1480 C  C   . GLN   A 1 192 ? -3.52612  -23.40921 -14.90448 1.000 28.11538 ? 192 GLN   A C   1 
ATOM   1481 O  O   . GLN   A 1 192 ? -4.59380  -23.23509 -15.50612 1.000 27.67162 ? 192 GLN   A O   1 
ATOM   1482 C  CB  . GLN   A 1 192 ? -2.25828  -21.31711 -14.66088 1.000 25.92210 ? 192 GLN   A CB  1 
ATOM   1483 C  CG  . GLN   A 1 192 ? -2.88893  -20.21995 -15.46482 1.000 25.54337 ? 192 GLN   A CG  1 
ATOM   1484 C  CD  . GLN   A 1 192 ? -2.59541  -18.83738 -14.91515 1.000 23.53245 ? 192 GLN   A CD  1 
ATOM   1485 O  OE1 . GLN   A 1 192 ? -2.01497  -18.68196 -13.82664 1.000 22.37784 ? 192 GLN   A OE1 1 
ATOM   1486 N  NE2 . GLN   A 1 192 ? -2.98354  -17.81526 -15.67107 1.000 23.78807 ? 192 GLN   A NE2 1 
ATOM   1487 N  N   . ALA   A 1 193 ? -3.42144  -24.17397 -13.81877 1.000 26.00312 ? 193 ALA   A N   1 
ATOM   1488 C  CA  . ALA   A 1 193 ? -4.57648  -24.88106 -13.28171 1.000 22.63512 ? 193 ALA   A CA  1 
ATOM   1489 C  C   . ALA   A 1 193 ? -4.54002  -24.88097 -11.75861 1.000 24.50694 ? 193 ALA   A C   1 
ATOM   1490 O  O   . ALA   A 1 193 ? -3.50311  -24.65066 -11.13281 1.000 24.45366 ? 193 ALA   A O   1 
ATOM   1491 C  CB  . ALA   A 1 193 ? -4.65280  -26.32256 -13.80636 1.000 25.35383 ? 193 ALA   A CB  1 
ATOM   1492 N  N   . ALA   A 1 194 ? -5.69982  -25.18112 -11.17071 1.000 21.08184 ? 194 ALA   A N   1 
ATOM   1493 C  CA  . ALA   A 1 194 ? -5.87590  -25.07002 -9.72134  1.000 24.51987 ? 194 ALA   A CA  1 
ATOM   1494 C  C   . ALA   A 1 194 ? -4.85596  -25.90987 -8.94115  1.000 26.02892 ? 194 ALA   A C   1 
ATOM   1495 O  O   . ALA   A 1 194 ? -4.16841  -25.39788 -8.04786  1.000 29.89838 ? 194 ALA   A O   1 
ATOM   1496 C  CB  . ALA   A 1 194 ? -7.30086  -25.47677 -9.34906  1.000 20.83481 ? 194 ALA   A CB  1 
ATOM   1497 N  N   . GLY   A 1 195 ? -4.74499  -27.19930 -9.23566  1.000 29.69466 ? 195 GLY   A N   1 
ATOM   1498 C  CA  . GLY   A 1 195 ? -3.95895  -28.00043 -8.31486  1.000 29.32150 ? 195 GLY   A CA  1 
ATOM   1499 C  C   . GLY   A 1 195 ? -4.76908  -28.42907 -7.09935  1.000 28.79058 ? 195 GLY   A C   1 
ATOM   1500 O  O   . GLY   A 1 195 ? -5.83166  -27.88851 -6.79679  1.000 25.70019 ? 195 GLY   A O   1 
ATOM   1501 N  N   . THR   A 1 196 ? -4.25712  -29.44050 -6.39876  1.000 26.70461 ? 196 THR   A N   1 
ATOM   1502 C  CA  . THR   A 1 196 ? -5.10958  -30.21271 -5.50473  1.000 25.59994 ? 196 THR   A CA  1 
ATOM   1503 C  C   . THR   A 1 196 ? -5.55689  -29.38449 -4.30079  1.000 23.74702 ? 196 THR   A C   1 
ATOM   1504 O  O   . THR   A 1 196 ? -4.80861  -28.54712 -3.77802  1.000 22.48489 ? 196 THR   A O   1 
ATOM   1505 C  CB  . THR   A 1 196 ? -4.38187  -31.47282 -5.04946  1.000 27.91085 ? 196 THR   A CB  1 
ATOM   1506 O  OG1 . THR   A 1 196 ? -3.24079  -31.09334 -4.27097  1.000 33.88574 ? 196 THR   A OG1 1 
ATOM   1507 C  CG2 . THR   A 1 196 ? -3.90476  -32.29195 -6.26213  1.000 27.14203 ? 196 THR   A CG2 1 
ATOM   1508 N  N   . ASP   A 1 197 ? -6.80189  -29.60377 -3.89075  1.000 22.43773 ? 197 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 197 ? -7.45869  -28.92841 -2.77399  1.000 21.43785 ? 197 ASP   A CA  1 
ATOM   1510 C  C   . ASP   A 1 197 ? -7.64788  -29.89419 -1.60533  1.000 23.21607 ? 197 ASP   A C   1 
ATOM   1511 O  O   . ASP   A 1 197 ? -7.50291  -31.11096 -1.73786  1.000 24.20793 ? 197 ASP   A O   1 
ATOM   1512 C  CB  . ASP   A 1 197 ? -8.82564  -28.38019 -3.19752  1.000 20.55292 ? 197 ASP   A CB  1 
ATOM   1513 C  CG  . ASP   A 1 197 ? -9.23396  -27.12736 -2.42710  1.000 20.03591 ? 197 ASP   A CG  1 
ATOM   1514 O  OD1 . ASP   A 1 197 ? -8.36704  -26.48699 -1.78282  1.000 20.26844 ? 197 ASP   A OD1 1 
ATOM   1515 O  OD2 . ASP   A 1 197 ? -10.44750 -26.80309 -2.42791  1.000 19.30127 ? 197 ASP   A OD2 1 
ATOM   1516 N  N   . THR   A 1 198 ? -8.00020  -29.32883 -0.45276  1.000 22.94081 ? 198 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 198 ? -8.32687  -30.08668 0.74459   1.000 21.39375 ? 198 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 198 ? -9.57678  -29.49359 1.37362   1.000 21.18055 ? 198 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 198 ? -10.04700 -28.42470 0.97662   1.000 19.79176 ? 198 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 198 ? -7.16187  -30.10203 1.75484   1.000 25.42838 ? 198 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 198 ? -6.60569  -28.78493 1.89366   1.000 22.21202 ? 198 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 198 ? -6.08607  -31.03249 1.30558   1.000 25.48761 ? 198 THR   A CG2 1 
ATOM   1523 N  N   . THR   A 1 199 ? -10.14135 -30.21729 2.34014   1.000 21.39155 ? 199 THR   A N   1 
ATOM   1524 C  CA  . THR   A 1 199 ? -11.31022 -29.72715 3.05759   1.000 21.37172 ? 199 THR   A CA  1 
ATOM   1525 C  C   . THR   A 1 199 ? -10.85486 -28.98187 4.30610   1.000 19.65367 ? 199 THR   A C   1 
ATOM   1526 O  O   . THR   A 1 199 ? -9.88787  -29.37713 4.96781   1.000 17.45175 ? 199 THR   A O   1 
ATOM   1527 C  CB  . THR   A 1 199 ? -12.25251 -30.88775 3.40462   1.000 21.95853 ? 199 THR   A CB  1 
ATOM   1528 O  OG1 . THR   A 1 199 ? -12.70316 -31.49342 2.18809   1.000 21.50932 ? 199 THR   A OG1 1 
ATOM   1529 C  CG2 . THR   A 1 199 ? -13.48828 -30.40409 4.17544   1.000 18.55560 ? 199 THR   A CG2 1 
ATOM   1530 N  N   . ILE   A 1 200 ? -11.53136 -27.87597 4.60210   1.000 16.20778 ? 200 ILE   A N   1 
ATOM   1531 C  CA  . ILE   A 1 200 ? -11.11883 -27.03070 5.71481   1.000 14.87947 ? 200 ILE   A CA  1 
ATOM   1532 C  C   . ILE   A 1 200 ? -11.69687 -27.60390 7.01084   1.000 16.89908 ? 200 ILE   A C   1 
ATOM   1533 O  O   . ILE   A 1 200 ? -12.85337 -27.33882 7.36623   1.000 14.31823 ? 200 ILE   A O   1 
ATOM   1534 C  CB  . ILE   A 1 200 ? -11.51045 -25.55746 5.48269   1.000 13.62842 ? 200 ILE   A CB  1 
ATOM   1535 C  CG1 . ILE   A 1 200 ? -11.06728 -25.08164 4.09062   1.000 15.62979 ? 200 ILE   A CG1 1 
ATOM   1536 C  CG2 . ILE   A 1 200 ? -10.92406 -24.66325 6.58505   1.000 14.40259 ? 200 ILE   A CG2 1 
ATOM   1537 C  CD1 . ILE   A 1 200 ? -11.91631 -23.93442 3.50588   1.000 12.22561 ? 200 ILE   A CD1 1 
ATOM   1538 N  N   . THR   A 1 201 ? -10.88120 -28.40355 7.71188   1.000 14.89763 ? 201 THR   A N   1 
ATOM   1539 C  CA  . THR   A 1 201 ? -11.34489 -29.19255 8.86311   1.000 16.34287 ? 201 THR   A CA  1 
ATOM   1540 C  C   . THR   A 1 201 ? -11.94260 -28.31497 9.95211   1.000 17.76111 ? 201 THR   A C   1 
ATOM   1541 O  O   . THR   A 1 201 ? -13.03091 -28.60764 10.45626  1.000 17.93009 ? 201 THR   A O   1 
ATOM   1542 C  CB  . THR   A 1 201 ? -10.19523 -30.02063 9.43753   1.000 20.01932 ? 201 THR   A CB  1 
ATOM   1543 O  OG1 . THR   A 1 201 ? -9.57656  -30.76572 8.38218   1.000 20.15336 ? 201 THR   A OG1 1 
ATOM   1544 C  CG2 . THR   A 1 201 ? -10.70614 -30.99730 10.51509  1.000 22.20543 ? 201 THR   A CG2 1 
ATOM   1545 N  N   . VAL   A 1 202 ? -11.23904 -27.24731 10.35199  1.000 15.50059 ? 202 VAL   A N   1 
ATOM   1546 C  CA  . VAL   A 1 202 ? -11.74494 -26.46009 11.47402  1.000 16.86975 ? 202 VAL   A CA  1 
ATOM   1547 C  C   . VAL   A 1 202 ? -13.10275 -25.87517 11.12874  1.000 13.71969 ? 202 VAL   A C   1 
ATOM   1548 O  O   . VAL   A 1 202 ? -13.96709 -25.73229 12.00814  1.000 15.68593 ? 202 VAL   A O   1 
ATOM   1549 C  CB  . VAL   A 1 202 ? -10.77084 -25.34620 11.89747  1.000 15.38533 ? 202 VAL   A CB  1 
ATOM   1550 C  CG1 . VAL   A 1 202 ? -10.51257 -24.39719 10.75488  1.000 18.04660 ? 202 VAL   A CG1 1 
ATOM   1551 C  CG2 . VAL   A 1 202 ? -11.32272 -24.58956 13.12793  1.000 18.00636 ? 202 VAL   A CG2 1 
ATOM   1552 N  N   . ASN   A 1 203 ? -13.32207 -25.53611 9.85380   1.000 15.54259 ? 203 ASN   A N   1 
ATOM   1553 C  CA  . ASN   A 1 203 ? -14.60150 -24.95605 9.44471   1.000 13.29082 ? 203 ASN   A CA  1 
ATOM   1554 C  C   . ASN   A 1 203 ? -15.72086 -25.99455 9.50217   1.000 16.19735 ? 203 ASN   A C   1 
ATOM   1555 O  O   . ASN   A 1 203 ? -16.84310 -25.68073 9.91295   1.000 14.88843 ? 203 ASN   A O   1 
ATOM   1556 C  CB  . ASN   A 1 203 ? -14.49567 -24.37251 8.03045   1.000 15.97179 ? 203 ASN   A CB  1 
ATOM   1557 C  CG  . ASN   A 1 203 ? -13.72929 -23.02443 7.97477   1.000 12.47192 ? 203 ASN   A CG  1 
ATOM   1558 O  OD1 . ASN   A 1 203 ? -13.23173 -22.50390 8.99173   1.000 11.60260 ? 203 ASN   A OD1 1 
ATOM   1559 N  ND2 . ASN   A 1 203 ? -13.61159 -22.49227 6.76875   1.000 10.57353 ? 203 ASN   A ND2 1 
ATOM   1560 N  N   . VAL   A 1 204 ? -15.44267 -27.23263 9.07787   1.000 15.93896 ? 204 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 204 ? -16.43685 -28.29750 9.20747   1.000 15.08031 ? 204 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 204 ? -16.86400 -28.45528 10.66302  1.000 17.70768 ? 204 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 204 ? -18.05526 -28.60264 10.95762  1.000 16.43190 ? 204 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 204 ? -15.90100 -29.63014 8.64537   1.000 17.17054 ? 204 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 204 ? -16.89971 -30.74179 8.90993   1.000 19.56202 ? 204 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 204 ? -15.61590 -29.52257 7.13394   1.000 16.25227 ? 204 VAL   A CG2 1 
ATOM   1567 N  N   . LEU   A 1 205 ? -15.89420 -28.46775 11.58763  1.000 15.63015 ? 205 LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 205 ? -16.21080 -28.57382 13.00646  1.000 17.16416 ? 205 LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 205 ? -17.06181 -27.39748 13.46123  1.000 16.62929 ? 205 LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 205 ? -18.04491 -27.58415 14.18030  1.000 16.24899 ? 205 LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 205 ? -14.92162 -28.67085 13.83434  1.000 15.78939 ? 205 LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 205 ? -14.10048 -29.94533 13.64047  1.000 16.31380 ? 205 LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 205 ? -12.70619 -29.86501 14.30640  1.000 17.72121 ? 205 LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 205 ? -14.85217 -31.17076 14.11749  1.000 19.82180 ? 205 LEU   A CD2 1 
ATOM   1575 N  N   . ALA   A 1 206 ? -16.72694 -26.18072 13.01404  1.000 14.95101 ? 206 ALA   A N   1 
ATOM   1576 C  CA  . ALA   A 1 206 ? -17.54525 -25.01805 13.35597  1.000 16.74072 ? 206 ALA   A CA  1 
ATOM   1577 C  C   . ALA   A 1 206 ? -19.00362 -25.21971 12.94050  1.000 16.88790 ? 206 ALA   A C   1 
ATOM   1578 O  O   . ALA   A 1 206 ? -19.93356 -24.84889 13.67108  1.000 17.65832 ? 206 ALA   A O   1 
ATOM   1579 C  CB  . ALA   A 1 206 ? -16.97256 -23.76327 12.69186  1.000 17.26239 ? 206 ALA   A CB  1 
ATOM   1580 N  N   . TRP   A 1 207 ? -19.21495 -25.81460 11.77347  1.000 16.03110 ? 207 TRP   A N   1 
ATOM   1581 C  CA  . TRP   A 1 207 ? -20.54413 -25.99608 11.20637  1.000 18.30260 ? 207 TRP   A CA  1 
ATOM   1582 C  C   . TRP   A 1 207 ? -21.29958 -27.10026 11.94152  1.000 18.64147 ? 207 TRP   A C   1 
ATOM   1583 O  O   . TRP   A 1 207 ? -22.52531 -27.02635 12.11552  1.000 18.26225 ? 207 TRP   A O   1 
ATOM   1584 C  CB  . TRP   A 1 207 ? -20.37166 -26.28151 9.71566   1.000 18.34747 ? 207 TRP   A CB  1 
ATOM   1585 C  CG  . TRP   A 1 207 ? -21.58114 -26.75742 8.95749   1.000 16.80779 ? 207 TRP   A CG  1 
ATOM   1586 C  CD1 . TRP   A 1 207 ? -22.59486 -25.99413 8.46043   1.000 19.18526 ? 207 TRP   A CD1 1 
ATOM   1587 C  CD2 . TRP   A 1 207 ? -21.83934 -28.09323 8.53185   1.000 17.33539 ? 207 TRP   A CD2 1 
ATOM   1588 N  NE1 . TRP   A 1 207 ? -23.50761 -26.78821 7.80048   1.000 16.67262 ? 207 TRP   A NE1 1 
ATOM   1589 C  CE2 . TRP   A 1 207 ? -23.06014 -28.07876 7.82122   1.000 17.16581 ? 207 TRP   A CE2 1 
ATOM   1590 C  CE3 . TRP   A 1 207 ? -21.17419 -29.31216 8.71213   1.000 19.40960 ? 207 TRP   A CE3 1 
ATOM   1591 C  CZ2 . TRP   A 1 207 ? -23.61628 -29.22941 7.27137   1.000 19.55598 ? 207 TRP   A CZ2 1 
ATOM   1592 C  CZ3 . TRP   A 1 207 ? -21.73722 -30.46016 8.17314   1.000 20.50319 ? 207 TRP   A CZ3 1 
ATOM   1593 C  CH2 . TRP   A 1 207 ? -22.94559 -30.40768 7.46078   1.000 19.83355 ? 207 TRP   A CH2 1 
ATOM   1594 N  N   . LEU   A 1 208 ? -20.58248 -28.12283 12.40364  1.000 18.52805 ? 208 LEU   A N   1 
ATOM   1595 C  CA  . LEU   A 1 208 ? -21.20802 -29.12375 13.26118  1.000 18.62282 ? 208 LEU   A CA  1 
ATOM   1596 C  C   . LEU   A 1 208 ? -21.71609 -28.49604 14.55922  1.000 20.60861 ? 208 LEU   A C   1 
ATOM   1597 O  O   . LEU   A 1 208 ? -22.83237 -28.78676 14.99760  1.000 21.75353 ? 208 LEU   A O   1 
ATOM   1598 C  CB  . LEU   A 1 208 ? -20.22239 -30.25460 13.54255  1.000 18.61404 ? 208 LEU   A CB  1 
ATOM   1599 C  CG  . LEU   A 1 208 ? -19.98907 -31.18312 12.34952  1.000 21.74599 ? 208 LEU   A CG  1 
ATOM   1600 C  CD1 . LEU   A 1 208 ? -18.94697 -32.23694 12.67438  1.000 21.57746 ? 208 LEU   A CD1 1 
ATOM   1601 C  CD2 . LEU   A 1 208 ? -21.27976 -31.84335 11.85184  1.000 21.40253 ? 208 LEU   A CD2 1 
ATOM   1602 N  N   . TYR   A 1 209 ? -20.92050 -27.59877 15.16213  1.000 22.31508 ? 209 TYR   A N   1 
ATOM   1603 C  CA  . TYR   A 1 209 ? -21.38621 -26.81264 16.30843  1.000 20.52642 ? 209 TYR   A CA  1 
ATOM   1604 C  C   . TYR   A 1 209 ? -22.58446 -25.93231 15.95069  1.000 21.50391 ? 209 TYR   A C   1 
ATOM   1605 O  O   . TYR   A 1 209 ? -23.53259 -25.81679 16.74056  1.000 19.13812 ? 209 TYR   A O   1 
ATOM   1606 C  CB  . TYR   A 1 209 ? -20.23464 -25.95612 16.83609  1.000 19.57913 ? 209 TYR   A CB  1 
ATOM   1607 C  CG  . TYR   A 1 209 ? -19.27125 -26.71820 17.71184  1.000 21.38119 ? 209 TYR   A CG  1 
ATOM   1608 C  CD1 . TYR   A 1 209 ? -19.63858 -27.14549 18.98063  1.000 22.92470 ? 209 TYR   A CD1 1 
ATOM   1609 C  CD2 . TYR   A 1 209 ? -17.98999 -27.02904 17.26317  1.000 20.03070 ? 209 TYR   A CD2 1 
ATOM   1610 C  CE1 . TYR   A 1 209 ? -18.75853 -27.85569 19.78684  1.000 23.71423 ? 209 TYR   A CE1 1 
ATOM   1611 C  CE2 . TYR   A 1 209 ? -17.10391 -27.74182 18.06526  1.000 22.74551 ? 209 TYR   A CE2 1 
ATOM   1612 C  CZ  . TYR   A 1 209 ? -17.49641 -28.14834 19.32302  1.000 25.30590 ? 209 TYR   A CZ  1 
ATOM   1613 O  OH  . TYR   A 1 209 ? -16.63347 -28.85246 20.12544  1.000 29.03158 ? 209 TYR   A OH  1 
ATOM   1614 N  N   . ALA   A 1 210 ? -22.55025 -25.27442 14.78554  1.000 17.74364 ? 210 ALA   A N   1 
ATOM   1615 C  CA  . ALA   A 1 210 ? -23.73895 -24.56924 14.30129  1.000 19.31421 ? 210 ALA   A CA  1 
ATOM   1616 C  C   . ALA   A 1 210 ? -24.95374 -25.48259 14.28380  1.000 21.16984 ? 210 ALA   A C   1 
ATOM   1617 O  O   . ALA   A 1 210 ? -26.05597 -25.07514 14.66464  1.000 19.00381 ? 210 ALA   A O   1 
ATOM   1618 C  CB  . ALA   A 1 210 ? -23.50471 -24.01680 12.89872  1.000 21.73961 ? 210 ALA   A CB  1 
ATOM   1619 N  N   . ALA   A 1 211 ? -24.77091 -26.72392 13.82959  1.000 19.71346 ? 211 ALA   A N   1 
ATOM   1620 C  CA  . ALA   A 1 211 ? -25.89733 -27.64731 13.74369  1.000 19.99343 ? 211 ALA   A CA  1 
ATOM   1621 C  C   . ALA   A 1 211 ? -26.44667 -27.98607 15.12434  1.000 23.16494 ? 211 ALA   A C   1 
ATOM   1622 O  O   . ALA   A 1 211 ? -27.66753 -27.97787 15.32997  1.000 20.76369 ? 211 ALA   A O   1 
ATOM   1623 C  CB  . ALA   A 1 211 ? -25.47132 -28.91558 13.00670  1.000 18.96681 ? 211 ALA   A CB  1 
ATOM   1624 N  N   . VAL   A 1 212 ? -25.56103 -28.28153 16.08044  1.000 22.21369 ? 212 VAL   A N   1 
ATOM   1625 C  CA  . VAL   A 1 212 ? -25.99679 -28.59932 17.43896  1.000 23.89350 ? 212 VAL   A CA  1 
ATOM   1626 C  C   . VAL   A 1 212 ? -26.72920 -27.41387 18.05282  1.000 24.56175 ? 212 VAL   A C   1 
ATOM   1627 O  O   . VAL   A 1 212 ? -27.74856 -27.58073 18.73554  1.000 25.05213 ? 212 VAL   A O   1 
ATOM   1628 C  CB  . VAL   A 1 212 ? -24.80035 -29.02842 18.31486  1.000 23.79638 ? 212 VAL   A CB  1 
ATOM   1629 C  CG1 . VAL   A 1 212 ? -25.26719 -29.21377 19.75823  1.000 24.06859 ? 212 VAL   A CG1 1 
ATOM   1630 C  CG2 . VAL   A 1 212 ? -24.16298 -30.32752 17.79299  1.000 21.82224 ? 212 VAL   A CG2 1 
ATOM   1631 N  N   . ILE   A 1 213 ? -26.21129 -26.20179 17.83776  1.000 23.40488 ? 213 ILE   A N   1 
ATOM   1632 C  CA  . ILE   A 1 213 ? -26.90521 -25.00716 18.30875  1.000 24.88297 ? 213 ILE   A CA  1 
ATOM   1633 C  C   . ILE   A 1 213 ? -28.30009 -24.93477 17.70875  1.000 25.16296 ? 213 ILE   A C   1 
ATOM   1634 O  O   . ILE   A 1 213 ? -29.24739 -24.49891 18.37275  1.000 28.46422 ? 213 ILE   A O   1 
ATOM   1635 C  CB  . ILE   A 1 213 ? -26.06269 -23.75085 17.99775  1.000 26.40310 ? 213 ILE   A CB  1 
ATOM   1636 C  CG1 . ILE   A 1 213 ? -24.80972 -23.74295 18.88876  1.000 26.56096 ? 213 ILE   A CG1 1 
ATOM   1637 C  CG2 . ILE   A 1 213 ? -26.87299 -22.47000 18.19012  1.000 26.99182 ? 213 ILE   A CG2 1 
ATOM   1638 C  CD1 . ILE   A 1 213 ? -23.71955 -22.77782 18.46766  1.000 24.16494 ? 213 ILE   A CD1 1 
ATOM   1639 N  N   . ASN   A 1 214 ? -28.46513 -25.41989 16.47825  1.000 25.18838 ? 214 ASN   A N   1 
ATOM   1640 C  CA  . ASN   A 1 214 ? -29.72162 -25.32361 15.74540  1.000 25.70608 ? 214 ASN   A CA  1 
ATOM   1641 C  C   . ASN   A 1 214 ? -30.56315 -26.60228 15.80786  1.000 27.39705 ? 214 ASN   A C   1 
ATOM   1642 O  O   . ASN   A 1 214 ? -31.57306 -26.70485 15.09474  1.000 28.76876 ? 214 ASN   A O   1 
ATOM   1643 C  CB  . ASN   A 1 214 ? -29.42969 -24.93301 14.29390  1.000 24.11688 ? 214 ASN   A CB  1 
ATOM   1644 C  CG  . ASN   A 1 214 ? -29.31042 -23.40504 14.10671  1.000 25.44115 ? 214 ASN   A CG  1 
ATOM   1645 O  OD1 . ASN   A 1 214 ? -30.29494 -22.73470 13.81510  1.000 28.24122 ? 214 ASN   A OD1 1 
ATOM   1646 N  ND2 . ASN   A 1 214 ? -28.12415 -22.86196 14.32329  1.000 28.56984 ? 214 ASN   A ND2 1 
ATOM   1647 N  N   . GLY   A 1 215 ? -30.18213 -27.57912 16.63872  1.000 27.34744 ? 215 GLY   A N   1 
ATOM   1648 C  CA  . GLY   A 1 215 ? -31.03844 -28.70989 16.95208  1.000 26.42758 ? 215 GLY   A CA  1 
ATOM   1649 C  C   . GLY   A 1 215 ? -30.74339 -30.02566 16.25239  1.000 28.65336 ? 215 GLY   A C   1 
ATOM   1650 O  O   . GLY   A 1 215 ? -31.45082 -31.00572 16.51272  1.000 29.25171 ? 215 GLY   A O   1 
ATOM   1651 N  N   . ASP   A 1 216 ? -29.75330 -30.08228 15.36108  1.000 27.26968 ? 216 ASP   A N   1 
ATOM   1652 C  CA  . ASP   A 1 216 ? -29.33255 -31.34051 14.74871  1.000 26.72651 ? 216 ASP   A CA  1 
ATOM   1653 C  C   . ASP   A 1 216 ? -28.33683 -32.02772 15.68527  1.000 30.07964 ? 216 ASP   A C   1 
ATOM   1654 O  O   . ASP   A 1 216 ? -27.23438 -31.50758 15.90115  1.000 28.93679 ? 216 ASP   A O   1 
ATOM   1655 C  CB  . ASP   A 1 216 ? -28.65842 -31.08677 13.39514  1.000 27.01734 ? 216 ASP   A CB  1 
ATOM   1656 C  CG  . ASP   A 1 216 ? -29.64404 -30.91306 12.25245  1.000 29.35233 ? 216 ASP   A CG  1 
ATOM   1657 O  OD1 . ASP   A 1 216 ? -30.64461 -31.64666 12.22862  1.000 33.13507 ? 216 ASP   A OD1 1 
ATOM   1658 O  OD2 . ASP   A 1 216 ? -29.38854 -30.05851 11.35888  1.000 26.59329 ? 216 ASP   A OD2 1 
ATOM   1659 N  N   . ARG   A 1 217 ? -28.70281 -33.19431 16.24274  1.000 30.05488 ? 217 ARG   A N   1 
ATOM   1660 C  CA  . ARG   A 1 217 ? -27.80465 -33.88221 17.17077  1.000 30.99618 ? 217 ARG   A CA  1 
ATOM   1661 C  C   . ARG   A 1 217 ? -27.53710 -35.33951 16.82485  1.000 28.75444 ? 217 ARG   A C   1 
ATOM   1662 O  O   . ARG   A 1 217 ? -26.77651 -35.99198 17.54478  1.000 28.07016 ? 217 ARG   A O   1 
ATOM   1663 C  CB  . ARG   A 1 217 ? -28.34942 -33.82672 18.60698  1.000 29.07446 ? 217 ARG   A CB  1 
ATOM   1664 C  CG  . ARG   A 1 217 ? -28.95933 -32.49578 18.99114  1.000 32.76274 ? 217 ARG   A CG  1 
ATOM   1665 C  CD  . ARG   A 1 217 ? -29.37270 -32.44957 20.47349  1.000 32.38497 ? 217 ARG   A CD  1 
ATOM   1666 N  NE  . ARG   A 1 217 ? -28.42981 -33.13537 21.35296  1.000 30.39579 ? 217 ARG   A NE  1 
ATOM   1667 C  CZ  . ARG   A 1 217 ? -27.49301 -32.52425 22.06742  1.000 31.02037 ? 217 ARG   A CZ  1 
ATOM   1668 N  NH1 . ARG   A 1 217 ? -27.29911 -31.21593 21.97821  1.000 28.63707 ? 217 ARG   A NH1 1 
ATOM   1669 N  NH2 . ARG   A 1 217 ? -26.71606 -33.24484 22.87500  1.000 31.10466 ? 217 ARG   A NH2 1 
ATOM   1670 N  N   . TRP   A 1 218 ? -28.13232 -35.86607 15.75203  1.000 29.11426 ? 218 TRP   A N   1 
ATOM   1671 C  CA  . TRP   A 1 218 ? -28.09001 -37.29974 15.48188  1.000 28.60642 ? 218 TRP   A CA  1 
ATOM   1672 C  C   . TRP   A 1 218 ? -26.67547 -37.82992 15.29418  1.000 28.89570 ? 218 TRP   A C   1 
ATOM   1673 O  O   . TRP   A 1 218 ? -26.44528 -39.02842 15.49324  1.000 29.83968 ? 218 TRP   A O   1 
ATOM   1674 C  CB  . TRP   A 1 218 ? -28.92613 -37.61068 14.24406  1.000 29.07481 ? 218 TRP   A CB  1 
ATOM   1675 C  CG  . TRP   A 1 218 ? -28.44257 -36.95304 12.96115  1.000 29.63226 ? 218 TRP   A CG  1 
ATOM   1676 C  CD1 . TRP   A 1 218 ? -28.93829 -35.81678 12.39370  1.000 29.85190 ? 218 TRP   A CD1 1 
ATOM   1677 C  CD2 . TRP   A 1 218 ? -27.41559 -37.42408 12.07742  1.000 29.60659 ? 218 TRP   A CD2 1 
ATOM   1678 N  NE1 . TRP   A 1 218 ? -28.27433 -35.53964 11.22437  1.000 29.02613 ? 218 TRP   A NE1 1 
ATOM   1679 C  CE2 . TRP   A 1 218 ? -27.33688 -36.51220 11.00465  1.000 29.37322 ? 218 TRP   A CE2 1 
ATOM   1680 C  CE3 . TRP   A 1 218 ? -26.55306 -38.52457 12.09077  1.000 32.30306 ? 218 TRP   A CE3 1 
ATOM   1681 C  CZ2 . TRP   A 1 218 ? -26.42763 -36.66196 9.96122   1.000 29.57490 ? 218 TRP   A CZ2 1 
ATOM   1682 C  CZ3 . TRP   A 1 218 ? -25.65365 -38.67503 11.05467  1.000 33.10992 ? 218 TRP   A CZ3 1 
ATOM   1683 C  CH2 . TRP   A 1 218 ? -25.59492 -37.74235 10.00245  1.000 30.59204 ? 218 TRP   A CH2 1 
ATOM   1684 N  N   . PHE   A 1 219 ? -25.74107 -36.97090 14.88901  1.000 27.96953 ? 219 PHE   A N   1 
ATOM   1685 C  CA  . PHE   A 1 219 ? -24.36582 -37.34552 14.59221  1.000 29.24805 ? 219 PHE   A CA  1 
ATOM   1686 C  C   . PHE   A 1 219 ? -23.46166 -37.33505 15.81943  1.000 28.32075 ? 219 PHE   A C   1 
ATOM   1687 O  O   . PHE   A 1 219 ? -22.29494 -37.73488 15.71794  1.000 26.91853 ? 219 PHE   A O   1 
ATOM   1688 C  CB  . PHE   A 1 219 ? -23.80169 -36.39788 13.51644  1.000 29.86521 ? 219 PHE   A CB  1 
ATOM   1689 C  CG  . PHE   A 1 219 ? -24.02222 -34.94125 13.82266  1.000 25.74640 ? 219 PHE   A CG  1 
ATOM   1690 C  CD1 . PHE   A 1 219 ? -23.15291 -34.25227 14.64472  1.000 24.02103 ? 219 PHE   A CD1 1 
ATOM   1691 C  CD2 . PHE   A 1 219 ? -25.12446 -34.27154 13.31304  1.000 24.14344 ? 219 PHE   A CD2 1 
ATOM   1692 C  CE1 . PHE   A 1 219 ? -23.35410 -32.91321 14.93161  1.000 23.68273 ? 219 PHE   A CE1 1 
ATOM   1693 C  CE2 . PHE   A 1 219 ? -25.33623 -32.93272 13.60375  1.000 26.30435 ? 219 PHE   A CE2 1 
ATOM   1694 C  CZ  . PHE   A 1 219 ? -24.44768 -32.24840 14.41576  1.000 23.39647 ? 219 PHE   A CZ  1 
ATOM   1695 N  N   . LEU   A 1 220 ? -23.96246 -36.87917 16.96378  1.000 27.56732 ? 220 LEU   A N   1 
ATOM   1696 C  CA  . LEU   A 1 220 ? -23.19531 -36.90418 18.19795  1.000 28.17560 ? 220 LEU   A CA  1 
ATOM   1697 C  C   . LEU   A 1 220 ? -23.02455 -38.33909 18.68845  1.000 30.30069 ? 220 LEU   A C   1 
ATOM   1698 O  O   . LEU   A 1 220 ? -23.75237 -39.25191 18.29223  1.000 31.32140 ? 220 LEU   A O   1 
ATOM   1699 C  CB  . LEU   A 1 220 ? -23.88933 -36.06879 19.27236  1.000 29.83000 ? 220 LEU   A CB  1 
ATOM   1700 C  CG  . LEU   A 1 220 ? -23.96450 -34.58867 18.91531  1.000 26.62609 ? 220 LEU   A CG  1 
ATOM   1701 C  CD1 . LEU   A 1 220 ? -24.68915 -33.81789 20.00155  1.000 27.29923 ? 220 LEU   A CD1 1 
ATOM   1702 C  CD2 . LEU   A 1 220 ? -22.56032 -34.03110 18.67195  1.000 26.47789 ? 220 LEU   A CD2 1 
ATOM   1703 N  N   . ASN   A 1 221 ? -22.05026 -38.52969 19.57084  1.000 31.63198 ? 221 ASN   A N   1 
ATOM   1704 C  CA  . ASN   A 1 221 ? -21.75751 -39.85464 20.09174  1.000 33.56254 ? 221 ASN   A CA  1 
ATOM   1705 C  C   . ASN   A 1 221 ? -20.96350 -39.72429 21.38365  1.000 36.74721 ? 221 ASN   A C   1 
ATOM   1706 O  O   . ASN   A 1 221 ? -20.45320 -38.65065 21.71193  1.000 33.33932 ? 221 ASN   A O   1 
ATOM   1707 C  CB  . ASN   A 1 221 ? -21.05141 -40.70804 19.02492  1.000 36.73133 ? 221 ASN   A CB  1 
ATOM   1708 C  CG  . ASN   A 1 221 ? -19.69644 -40.15437 18.60894  1.000 39.07615 ? 221 ASN   A CG  1 
ATOM   1709 O  OD1 . ASN   A 1 221 ? -18.80447 -39.91902 19.43320  1.000 40.13970 ? 221 ASN   A OD1 1 
ATOM   1710 N  ND2 . ASN   A 1 221 ? -19.54773 -39.91571 17.30603  1.000 37.87160 ? 221 ASN   A ND2 1 
ATOM   1711 N  N   . ARG   A 1 222 ? -20.92505 -40.82586 22.14748  1.000 37.51493 ? 222 ARG   A N   1 
ATOM   1712 C  CA  . ARG   A 1 222 ? -20.24846 -40.83366 23.43951  1.000 38.28884 ? 222 ARG   A CA  1 
ATOM   1713 C  C   . ARG   A 1 222 ? -18.73229 -40.90735 23.32159  1.000 41.44442 ? 222 ARG   A C   1 
ATOM   1714 O  O   . ARG   A 1 222 ? -18.04034 -40.49569 24.25702  1.000 44.49221 ? 222 ARG   A O   1 
ATOM   1715 C  CB  . ARG   A 1 222 ? -20.72938 -42.01165 24.30440  1.000 43.30479 ? 222 ARG   A CB  1 
ATOM   1716 C  CG  . ARG   A 1 222 ? -20.05498 -43.35358 23.96248  1.000 43.47695 ? 222 ARG   A CG  1 
ATOM   1717 C  CD  . ARG   A 1 222 ? -20.71806 -44.52382 24.66897  1.000 45.38157 ? 222 ARG   A CD  1 
ATOM   1718 N  NE  . ARG   A 1 222 ? -20.30878 -44.60368 26.06740  1.000 49.15526 ? 222 ARG   A NE  1 
ATOM   1719 C  CZ  . ARG   A 1 222 ? -20.75940 -45.50448 26.93193  1.000 51.90028 ? 222 ARG   A CZ  1 
ATOM   1720 N  NH1 . ARG   A 1 222 ? -21.68066 -46.39435 26.58843  1.000 51.19049 ? 222 ARG   A NH1 1 
ATOM   1721 N  NH2 . ARG   A 1 222 ? -20.27791 -45.51208 28.17530  1.000 54.36204 ? 222 ARG   A NH2 1 
ATOM   1722 N  N   . PHE   A 1 223 ? -18.20297 -41.42235 22.21270  1.000 42.37449 ? 223 PHE   A N   1 
ATOM   1723 C  CA  . PHE   A 1 223 ? -16.76447 -41.61265 22.08825  1.000 43.10353 ? 223 PHE   A CA  1 
ATOM   1724 C  C   . PHE   A 1 223 ? -16.02784 -40.27914 22.05133  1.000 40.28905 ? 223 PHE   A C   1 
ATOM   1725 O  O   . PHE   A 1 223 ? -16.59964 -39.21675 21.79202  1.000 38.41565 ? 223 PHE   A O   1 
ATOM   1726 C  CB  . PHE   A 1 223 ? -16.40997 -42.40499 20.82740  1.000 42.44750 ? 223 PHE   A CB  1 
ATOM   1727 C  CG  . PHE   A 1 223 ? -17.49003 -43.32411 20.35549  1.000 45.41829 ? 223 PHE   A CG  1 
ATOM   1728 C  CD1 . PHE   A 1 223 ? -17.71751 -44.53296 20.99023  1.000 48.08617 ? 223 PHE   A CD1 1 
ATOM   1729 C  CD2 . PHE   A 1 223 ? -18.27037 -42.98697 19.26424  1.000 45.31249 ? 223 PHE   A CD2 1 
ATOM   1730 C  CE1 . PHE   A 1 223 ? -18.71575 -45.38992 20.54871  1.000 49.05832 ? 223 PHE   A CE1 1 
ATOM   1731 C  CE2 . PHE   A 1 223 ? -19.27348 -43.83161 18.82168  1.000 45.16220 ? 223 PHE   A CE2 1 
ATOM   1732 C  CZ  . PHE   A 1 223 ? -19.49636 -45.03236 19.45854  1.000 49.06066 ? 223 PHE   A CZ  1 
ATOM   1733 N  N   . THR   A 1 224 ? -14.72917 -40.35464 22.31668  1.000 41.04342 ? 224 THR   A N   1 
ATOM   1734 C  CA  . THR   A 1 224 ? -13.81058 -39.24476 22.13242  1.000 38.82441 ? 224 THR   A CA  1 
ATOM   1735 C  C   . THR   A 1 224 ? -12.62098 -39.72890 21.30877  1.000 39.46657 ? 224 THR   A C   1 
ATOM   1736 O  O   . THR   A 1 224 ? -12.54193 -40.89806 20.91647  1.000 41.33730 ? 224 THR   A O   1 
ATOM   1737 C  CB  . THR   A 1 224 ? -13.36060 -38.65952 23.48024  1.000 39.81798 ? 224 THR   A CB  1 
ATOM   1738 O  OG1 . THR   A 1 224 ? -12.98704 -37.28594 23.30347  1.000 38.31232 ? 224 THR   A OG1 1 
ATOM   1739 C  CG2 . THR   A 1 224 ? -12.19397 -39.45188 24.07410  1.000 40.14097 ? 224 THR   A CG2 1 
ATOM   1740 N  N   . THR   A 1 225 ? -11.69565 -38.81436 21.03644  1.000 38.19078 ? 225 THR   A N   1 
ATOM   1741 C  CA  . THR   A 1 225 ? -10.47954 -39.14428 20.30908  1.000 39.19677 ? 225 THR   A CA  1 
ATOM   1742 C  C   . THR   A 1 225 ? -9.37750  -38.18149 20.72398  1.000 38.78668 ? 225 THR   A C   1 
ATOM   1743 O  O   . THR   A 1 225 ? -9.63959  -37.08835 21.23668  1.000 40.41491 ? 225 THR   A O   1 
ATOM   1744 C  CB  . THR   A 1 225 ? -10.69488 -39.09579 18.78528  1.000 37.28544 ? 225 THR   A CB  1 
ATOM   1745 O  OG1 . THR   A 1 225 ? -9.56190  -39.67477 18.12504  1.000 40.10947 ? 225 THR   A OG1 1 
ATOM   1746 C  CG2 . THR   A 1 225 ? -10.88589 -37.66165 18.30574  1.000 35.43643 ? 225 THR   A CG2 1 
ATOM   1747 N  N   . THR   A 1 226 ? -8.13547  -38.60889 20.51472  1.000 39.58088 ? 226 THR   A N   1 
ATOM   1748 C  CA  . THR   A 1 226 ? -7.00780  -37.70519 20.68210  1.000 40.92780 ? 226 THR   A CA  1 
ATOM   1749 C  C   . THR   A 1 226 ? -6.84800  -36.84454 19.43595  1.000 36.37016 ? 226 THR   A C   1 
ATOM   1750 O  O   . THR   A 1 226 ? -7.29381  -37.20033 18.34036  1.000 34.67048 ? 226 THR   A O   1 
ATOM   1751 C  CB  . THR   A 1 226 ? -5.70208  -38.46630 20.93890  1.000 40.97379 ? 226 THR   A CB  1 
ATOM   1752 O  OG1 . THR   A 1 226 ? -5.60683  -39.58848 20.05124  1.000 42.76974 ? 226 THR   A OG1 1 
ATOM   1753 C  CG2 . THR   A 1 226 ? -5.63700  -38.96333 22.37698  1.000 39.62916 ? 226 THR   A CG2 1 
ATOM   1754 N  N   . LEU   A 1 227 ? -6.19203  -35.69742 19.61450  1.000 37.06301 ? 227 LEU   A N   1 
ATOM   1755 C  CA  . LEU   A 1 227 ? -5.89345  -34.84437 18.47119  1.000 37.19311 ? 227 LEU   A CA  1 
ATOM   1756 C  C   . LEU   A 1 227 ? -5.04487  -35.58407 17.44116  1.000 37.04182 ? 227 LEU   A C   1 
ATOM   1757 O  O   . LEU   A 1 227 ? -5.31195  -35.50309 16.23726  1.000 36.08318 ? 227 LEU   A O   1 
ATOM   1758 C  CB  . LEU   A 1 227 ? -5.20372  -33.56535 18.94190  1.000 35.85371 ? 227 LEU   A CB  1 
ATOM   1759 C  CG  . LEU   A 1 227 ? -4.99128  -32.46037 17.91180  1.000 32.78864 ? 227 LEU   A CG  1 
ATOM   1760 C  CD1 . LEU   A 1 227 ? -6.29654  -32.17346 17.17959  1.000 32.19924 ? 227 LEU   A CD1 1 
ATOM   1761 C  CD2 . LEU   A 1 227 ? -4.48064  -31.20225 18.58413  1.000 31.54098 ? 227 LEU   A CD2 1 
ATOM   1762 N  N   . ASN   A 1 228 ? -4.03856  -36.33897 17.89502  1.000 36.77449 ? 228 ASN   A N   1 
ATOM   1763 C  CA  . ASN   A 1 228 ? -3.19980  -37.09581 16.96663  1.000 39.13074 ? 228 ASN   A CA  1 
ATOM   1764 C  C   . ASN   A 1 228 ? -4.01551  -38.12225 16.19044  1.000 38.72020 ? 228 ASN   A C   1 
ATOM   1765 O  O   . ASN   A 1 228 ? -3.89536  -38.23223 14.96271  1.000 38.29341 ? 228 ASN   A O   1 
ATOM   1766 C  CB  . ASN   A 1 228 ? -2.06378  -37.78818 17.72081  1.000 40.37571 ? 228 ASN   A CB  1 
ATOM   1767 C  CG  . ASN   A 1 228 ? -1.01137  -36.81671 18.19696  1.000 42.80591 ? 228 ASN   A CG  1 
ATOM   1768 O  OD1 . ASN   A 1 228 ? -0.60773  -35.91158 17.46184  1.000 44.96950 ? 228 ASN   A OD1 1 
ATOM   1769 N  ND2 . ASN   A 1 228 ? -0.55197  -36.99906 19.43241  1.000 44.26477 ? 228 ASN   A ND2 1 
ATOM   1770 N  N   . ASP   A 1 229 ? -4.85609  -38.88557 16.89288  1.000 39.68253 ? 229 ASP   A N   1 
ATOM   1771 C  CA  . ASP   A 1 229 ? -5.59755  -39.95077 16.22988  1.000 39.15088 ? 229 ASP   A CA  1 
ATOM   1772 C  C   . ASP   A 1 229 ? -6.65217  -39.39771 15.27890  1.000 38.74594 ? 229 ASP   A C   1 
ATOM   1773 O  O   . ASP   A 1 229 ? -6.94387  -40.01868 14.24934  1.000 39.08540 ? 229 ASP   A O   1 
ATOM   1774 C  CB  . ASP   A 1 229 ? -6.22973  -40.86726 17.27287  1.000 40.73571 ? 229 ASP   A CB  1 
ATOM   1775 C  CG  . ASP   A 1 229 ? -5.36223  -42.06532 17.58400  1.000 44.97859 ? 229 ASP   A CG  1 
ATOM   1776 O  OD1 . ASP   A 1 229 ? -4.28597  -42.19829 16.95857  1.000 45.88020 ? 229 ASP   A OD1 1 
ATOM   1777 O  OD2 . ASP   A 1 229 ? -5.73477  -42.86309 18.46605  1.000 47.89305 ? 229 ASP   A OD2 1 
ATOM   1778 N  N   . PHE   A 1 230 ? -7.23038  -38.23591 15.59211  1.000 36.81487 ? 230 PHE   A N   1 
ATOM   1779 C  CA  . PHE   A 1 230 ? -8.12265  -37.59885 14.63139  1.000 36.20077 ? 230 PHE   A CA  1 
ATOM   1780 C  C   . PHE   A 1 230 ? -7.36814  -37.18865 13.37438  1.000 34.55060 ? 230 PHE   A C   1 
ATOM   1781 O  O   . PHE   A 1 230 ? -7.86295  -37.37148 12.25718  1.000 33.93771 ? 230 PHE   A O   1 
ATOM   1782 C  CB  . PHE   A 1 230 ? -8.81262  -36.37933 15.24285  1.000 33.64898 ? 230 PHE   A CB  1 
ATOM   1783 C  CG  . PHE   A 1 230 ? -9.61532  -35.59423 14.23607  1.000 32.94823 ? 230 PHE   A CG  1 
ATOM   1784 C  CD1 . PHE   A 1 230 ? -10.87714 -36.03132 13.84329  1.000 29.94355 ? 230 PHE   A CD1 1 
ATOM   1785 C  CD2 . PHE   A 1 230 ? -9.08835  -34.45849 13.63662  1.000 29.70776 ? 230 PHE   A CD2 1 
ATOM   1786 C  CE1 . PHE   A 1 230 ? -11.59693 -35.33960 12.90429  1.000 28.95030 ? 230 PHE   A CE1 1 
ATOM   1787 C  CE2 . PHE   A 1 230 ? -9.81529  -33.76328 12.69336  1.000 30.97049 ? 230 PHE   A CE2 1 
ATOM   1788 C  CZ  . PHE   A 1 230 ? -11.06553 -34.20415 12.32648  1.000 27.90367 ? 230 PHE   A CZ  1 
ATOM   1789 N  N   . ASN   A 1 231 ? -6.16546  -36.63214 13.53594  1.000 36.54017 ? 231 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 231 ? -5.41796  -36.13338 12.38166  1.000 36.84095 ? 231 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 231 ? -4.97817  -37.26843 11.46516  1.000 35.88088 ? 231 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 231 ? -4.82119  -37.06452 10.25500  1.000 36.61245 ? 231 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 231 ? -4.22036  -35.30737 12.85741  1.000 33.19613 ? 231 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 231 ? -4.60289  -33.87359 13.15660  1.000 31.00719 ? 231 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 231 ? -5.34820  -33.27068 12.40598  1.000 34.78741 ? 231 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 231 ? -4.10997  -33.33018 14.25950  1.000 32.49352 ? 231 ASN   A ND2 1 
ATOM   1797 N  N   . LEU   A 1 232 ? -4.80255  -38.46758 12.01974  1.000 37.92534 ? 232 LEU   A N   1 
ATOM   1798 C  CA  . LEU   A 1 232 ? -4.51260  -39.63710 11.20123  1.000 37.48823 ? 232 LEU   A CA  1 
ATOM   1799 C  C   . LEU   A 1 232 ? -5.67290  -39.93342 10.26231  1.000 37.68848 ? 232 LEU   A C   1 
ATOM   1800 O  O   . LEU   A 1 232 ? -5.46853  -40.29844 9.09771   1.000 37.83188 ? 232 LEU   A O   1 
ATOM   1801 C  CB  . LEU   A 1 232 ? -4.22886  -40.83367 12.11209  1.000 37.47809 ? 232 LEU   A CB  1 
ATOM   1802 C  CG  . LEU   A 1 232 ? -2.76720  -41.18619 12.41666  1.000 40.31822 ? 232 LEU   A CG  1 
ATOM   1803 C  CD1 . LEU   A 1 232 ? -2.61747  -42.65760 12.75479  1.000 41.47012 ? 232 LEU   A CD1 1 
ATOM   1804 C  CD2 . LEU   A 1 232 ? -1.84636  -40.78925 11.26656  1.000 39.27174 ? 232 LEU   A CD2 1 
ATOM   1805 N  N   . VAL   A 1 233 ? -6.90393  -39.76043 10.74875  1.000 38.08608 ? 233 VAL   A N   1 
ATOM   1806 C  CA  . VAL   A 1 233 ? -8.07802  -39.99470 9.91525   1.000 36.90780 ? 233 VAL   A CA  1 
ATOM   1807 C  C   . VAL   A 1 233 ? -8.31143  -38.82931 8.96206   1.000 36.67280 ? 233 VAL   A C   1 
ATOM   1808 O  O   . VAL   A 1 233 ? -8.69185  -39.02969 7.80099   1.000 37.48649 ? 233 VAL   A O   1 
ATOM   1809 C  CB  . VAL   A 1 233 ? -9.30581  -40.26798 10.80286  1.000 37.91661 ? 233 VAL   A CB  1 
ATOM   1810 C  CG1 . VAL   A 1 233 ? -10.59321 -39.83831 10.09106  1.000 37.08349 ? 233 VAL   A CG1 1 
ATOM   1811 C  CG2 . VAL   A 1 233 ? -9.34972  -41.72923 11.19960  1.000 39.22316 ? 233 VAL   A CG2 1 
ATOM   1812 N  N   . ALA   A 1 234 ? -8.08694  -37.59603 9.42772   1.000 37.16882 ? 234 ALA   A N   1 
ATOM   1813 C  CA  . ALA   A 1 234 ? -8.23341  -36.43028 8.56162   1.000 34.55035 ? 234 ALA   A CA  1 
ATOM   1814 C  C   . ALA   A 1 234 ? -7.38179  -36.56275 7.30666   1.000 34.71551 ? 234 ALA   A C   1 
ATOM   1815 O  O   . ALA   A 1 234 ? -7.85667  -36.33060 6.18972   1.000 35.01888 ? 234 ALA   A O   1 
ATOM   1816 C  CB  . ALA   A 1 234 ? -7.85624  -35.15546 9.32208   1.000 32.73548 ? 234 ALA   A CB  1 
ATOM   1817 N  N   . MET   A 1 235 ? -6.11231  -36.93057 7.47977   1.000 34.63988 ? 235 MET   A N   1 
ATOM   1818 C  CA  . MET   A 1 235 ? -5.20662  -37.06479 6.34352   1.000 36.52407 ? 235 MET   A CA  1 
ATOM   1819 C  C   . MET   A 1 235 ? -5.74735  -38.07111 5.33073   1.000 36.48679 ? 235 MET   A C   1 
ATOM   1820 O  O   . MET   A 1 235 ? -5.69919  -37.83282 4.11568   1.000 35.00814 ? 235 MET   A O   1 
ATOM   1821 C  CB  . MET   A 1 235 ? -3.82226  -37.47440 6.85098   1.000 37.77489 ? 235 MET   A CB  1 
ATOM   1822 C  CG  . MET   A 1 235 ? -2.72826  -37.52485 5.79827   1.000 42.37635 ? 235 MET   A CG  1 
ATOM   1823 S  SD  . MET   A 1 235 ? -1.12158  -37.85670 6.55966   1.000 56.13069 ? 235 MET   A SD  1 
ATOM   1824 C  CE  . MET   A 1 235 ? -0.89551  -36.35785 7.51799   1.000 41.65585 ? 235 MET   A CE  1 
ATOM   1825 N  N   . LYS   A 1 236 ? -6.31680  -39.17904 5.81928   1.000 37.51697 ? 236 LYS   A N   1 
ATOM   1826 C  CA  . LYS   A 1 236 ? -6.81710  -40.22045 4.92864   1.000 35.10627 ? 236 LYS   A CA  1 
ATOM   1827 C  C   . LYS   A 1 236 ? -7.94982  -39.71463 4.04152   1.000 34.15925 ? 236 LYS   A C   1 
ATOM   1828 O  O   . LYS   A 1 236 ? -8.07758  -40.16019 2.89558   1.000 35.19028 ? 236 LYS   A O   1 
ATOM   1829 C  CB  . LYS   A 1 236 ? -7.27027  -41.43430 5.74585   1.000 34.84208 ? 236 LYS   A CB  1 
ATOM   1830 C  CG  . LYS   A 1 236 ? -8.04134  -42.47234 4.93262   1.000 38.72958 ? 236 LYS   A CG  1 
ATOM   1831 C  CD  . LYS   A 1 236 ? -7.69499  -43.90138 5.36339   1.000 41.57531 ? 236 LYS   A CD  1 
ATOM   1832 C  CE  . LYS   A 1 236 ? -8.74411  -44.50246 6.28206   1.000 40.76690 ? 236 LYS   A CE  1 
ATOM   1833 N  NZ  . LYS   A 1 236 ? -10.06514 -44.63033 5.59754   1.000 42.26765 ? 236 LYS   A NZ  1 
ATOM   1834 N  N   . TYR   A 1 237 ? -8.76246  -38.77212 4.53407   1.000 34.01520 ? 237 TYR   A N   1 
ATOM   1835 C  CA  . TYR   A 1 237 ? -9.90832  -38.23768 3.80226   1.000 30.37190 ? 237 TYR   A CA  1 
ATOM   1836 C  C   . TYR   A 1 237 ? -9.62846  -36.87594 3.17313   1.000 29.49593 ? 237 TYR   A C   1 
ATOM   1837 O  O   . TYR   A 1 237 ? -10.56996 -36.15353 2.82684   1.000 28.57845 ? 237 TYR   A O   1 
ATOM   1838 C  CB  . TYR   A 1 237 ? -11.12822 -38.15620 4.71753   1.000 32.20589 ? 237 TYR   A CB  1 
ATOM   1839 C  CG  . TYR   A 1 237 ? -11.67075 -39.52284 5.05376   1.000 33.19053 ? 237 TYR   A CG  1 
ATOM   1840 C  CD1 . TYR   A 1 237 ? -12.57932 -40.15656 4.21074   1.000 35.15963 ? 237 TYR   A CD1 1 
ATOM   1841 C  CD2 . TYR   A 1 237 ? -11.24095 -40.20229 6.18655   1.000 35.42545 ? 237 TYR   A CD2 1 
ATOM   1842 C  CE1 . TYR   A 1 237 ? -13.06759 -41.42486 4.50386   1.000 33.50754 ? 237 TYR   A CE1 1 
ATOM   1843 C  CE2 . TYR   A 1 237 ? -11.72022 -41.46949 6.48493   1.000 36.71335 ? 237 TYR   A CE2 1 
ATOM   1844 C  CZ  . TYR   A 1 237 ? -12.63421 -42.07310 5.63992   1.000 36.79535 ? 237 TYR   A CZ  1 
ATOM   1845 O  OH  . TYR   A 1 237 ? -13.11479 -43.33334 5.94173   1.000 38.06569 ? 237 TYR   A OH  1 
ATOM   1846 N  N   . ASN   A 1 238 ? -8.35435  -36.51350 3.01952   1.000 28.76272 ? 238 ASN   A N   1 
ATOM   1847 C  CA  . ASN   A 1 238 ? -7.96670  -35.29094 2.31824   1.000 29.46029 ? 238 ASN   A CA  1 
ATOM   1848 C  C   . ASN   A 1 238 ? -8.41610  -34.03916 3.08497   1.000 26.06239 ? 238 ASN   A C   1 
ATOM   1849 O  O   . ASN   A 1 238 ? -8.64393  -32.97781 2.50066   1.000 26.00302 ? 238 ASN   A O   1 
ATOM   1850 C  CB  . ASN   A 1 238 ? -8.52940  -35.26912 0.89378   1.000 28.80563 ? 238 ASN   A CB  1 
ATOM   1851 C  CG  . ASN   A 1 238 ? -7.85430  -34.24134 0.03471   1.000 31.65845 ? 238 ASN   A CG  1 
ATOM   1852 O  OD1 . ASN   A 1 238 ? -8.36148  -33.83111 -1.01392  1.000 34.35221 ? 238 ASN   A OD1 1 
ATOM   1853 N  ND2 . ASN   A 1 238 ? -6.63914  -33.89412 0.42503   1.000 31.57398 ? 238 ASN   A ND2 1 
ATOM   1854 N  N   . TYR   A 1 239 ? -8.57896  -34.16322 4.39394   1.000 27.99711 ? 239 TYR   A N   1 
ATOM   1855 C  CA  . TYR   A 1 239 ? -8.87114  -33.04101 5.27132   1.000 25.98299 ? 239 TYR   A CA  1 
ATOM   1856 C  C   . TYR   A 1 239 ? -7.54956  -32.50204 5.79367   1.000 25.23517 ? 239 TYR   A C   1 
ATOM   1857 O  O   . TYR   A 1 239 ? -6.58974  -33.24795 5.96130   1.000 24.80505 ? 239 TYR   A O   1 
ATOM   1858 C  CB  . TYR   A 1 239 ? -9.74854  -33.47917 6.44880   1.000 25.59339 ? 239 TYR   A CB  1 
ATOM   1859 C  CG  . TYR   A 1 239 ? -11.24766 -33.46716 6.21772   1.000 23.76414 ? 239 TYR   A CG  1 
ATOM   1860 C  CD1 . TYR   A 1 239 ? -11.82831 -34.13508 5.13553   1.000 24.12660 ? 239 TYR   A CD1 1 
ATOM   1861 C  CD2 . TYR   A 1 239 ? -12.08451 -32.79257 7.09875   1.000 22.61518 ? 239 TYR   A CD2 1 
ATOM   1862 C  CE1 . TYR   A 1 239 ? -13.22216 -34.11968 4.93995   1.000 25.44946 ? 239 TYR   A CE1 1 
ATOM   1863 C  CE2 . TYR   A 1 239 ? -13.46596 -32.77377 6.91903   1.000 23.36321 ? 239 TYR   A CE2 1 
ATOM   1864 C  CZ  . TYR   A 1 239 ? -14.02939 -33.44254 5.84337   1.000 22.56518 ? 239 TYR   A CZ  1 
ATOM   1865 O  OH  . TYR   A 1 239 ? -15.39790 -33.41453 5.68183   1.000 21.55581 ? 239 TYR   A OH  1 
ATOM   1866 N  N   . GLU   A 1 240 ? -7.48880  -31.21411 6.05852   1.000 24.21457 ? 240 GLU   A N   1 
ATOM   1867 C  CA  . GLU   A 1 240 ? -6.20525  -30.68559 6.48634   1.000 27.45726 ? 240 GLU   A CA  1 
ATOM   1868 C  C   . GLU   A 1 240 ? -6.05581  -30.82172 7.99263   1.000 26.90079 ? 240 GLU   A C   1 
ATOM   1869 O  O   . GLU   A 1 240 ? -7.02368  -31.08162 8.71776   1.000 26.16066 ? 240 GLU   A O   1 
ATOM   1870 C  CB  . GLU   A 1 240 ? -6.04682  -29.25527 6.00481   1.000 27.93538 ? 240 GLU   A CB  1 
ATOM   1871 C  CG  . GLU   A 1 240 ? -6.96574  -28.25689 6.54250   1.000 24.23929 ? 240 GLU   A CG  1 
ATOM   1872 C  CD  . GLU   A 1 240 ? -6.80871  -26.97714 5.75913   1.000 26.46270 ? 240 GLU   A CD  1 
ATOM   1873 O  OE1 . GLU   A 1 240 ? -5.80607  -26.88046 5.00319   1.000 32.14892 ? 240 GLU   A OE1 1 
ATOM   1874 O  OE2 . GLU   A 1 240 ? -7.62722  -26.04996 5.93932   1.000 27.88817 ? 240 GLU   A OE2 1 
ATOM   1875 N  N   . PRO   A 1 241 ? -4.82717  -30.76112 8.50301   1.000 28.37506 ? 241 PRO   A N   1 
ATOM   1876 C  CA  . PRO   A 1 241 ? -4.62772  -31.05561 9.92578   1.000 27.81892 ? 241 PRO   A CA  1 
ATOM   1877 C  C   . PRO   A 1 241 ? -5.32710  -30.04397 10.81937  1.000 25.79169 ? 241 PRO   A C   1 
ATOM   1878 O  O   . PRO   A 1 241 ? -5.47886  -28.86673 10.48016  1.000 29.20863 ? 241 PRO   A O   1 
ATOM   1879 C  CB  . PRO   A 1 241 ? -3.10394  -30.99734 10.11419  1.000 29.49168 ? 241 PRO   A CB  1 
ATOM   1880 C  CG  . PRO   A 1 241 ? -2.50233  -30.84032 8.76074   1.000 31.19596 ? 241 PRO   A CG  1 
ATOM   1881 C  CD  . PRO   A 1 241 ? -3.57178  -30.81794 7.72421   1.000 31.19329 ? 241 PRO   A CD  1 
ATOM   1882 N  N   . LEU   A 1 242 ? -5.77313  -30.53080 11.97175  1.000 28.19525 ? 242 LEU   A N   1 
ATOM   1883 C  CA  . LEU   A 1 242 ? -6.33258  -29.68715 13.01798  1.000 26.24204 ? 242 LEU   A CA  1 
ATOM   1884 C  C   . LEU   A 1 242 ? -5.24202  -29.36482 14.03450  1.000 27.25096 ? 242 LEU   A C   1 
ATOM   1885 O  O   . LEU   A 1 242 ? -4.53899  -30.26297 14.50088  1.000 25.59900 ? 242 LEU   A O   1 
ATOM   1886 C  CB  . LEU   A 1 242 ? -7.50593  -30.38967 13.70776  1.000 27.16495 ? 242 LEU   A CB  1 
ATOM   1887 C  CG  . LEU   A 1 242 ? -8.47263  -29.46551 14.43227  1.000 25.83354 ? 242 LEU   A CG  1 
ATOM   1888 C  CD1 . LEU   A 1 242 ? -9.27719  -28.65928 13.42691  1.000 23.84472 ? 242 LEU   A CD1 1 
ATOM   1889 C  CD2 . LEU   A 1 242 ? -9.37360  -30.28812 15.34109  1.000 27.57666 ? 242 LEU   A CD2 1 
ATOM   1890 N  N   . THR   A 1 243 ? -5.10599  -28.09169 14.37745  1.000 26.31442 ? 243 THR   A N   1 
ATOM   1891 C  CA  . THR   A 1 243 ? -4.08441  -27.66805 15.32042  1.000 29.02037 ? 243 THR   A CA  1 
ATOM   1892 C  C   . THR   A 1 243 ? -4.67997  -27.38095 16.69314  1.000 28.05964 ? 243 THR   A C   1 
ATOM   1893 O  O   . THR   A 1 243 ? -5.89475  -27.20170 16.85464  1.000 27.87709 ? 243 THR   A O   1 
ATOM   1894 C  CB  . THR   A 1 243 ? -3.35881  -26.41964 14.81338  1.000 27.33478 ? 243 THR   A CB  1 
ATOM   1895 O  OG1 . THR   A 1 243 ? -4.26498  -25.30611 14.82391  1.000 28.83145 ? 243 THR   A OG1 1 
ATOM   1896 C  CG2 . THR   A 1 243 ? -2.83348  -26.65037 13.40560  1.000 26.68961 ? 243 THR   A CG2 1 
ATOM   1897 N  N   . GLN   A 1 244 ? -3.78719  -27.32239 17.68891  1.000 29.24026 ? 244 GLN   A N   1 
ATOM   1898 C  CA  . GLN   A 1 244 ? -4.18243  -26.86046 19.01440  1.000 28.34994 ? 244 GLN   A CA  1 
ATOM   1899 C  C   . GLN   A 1 244 ? -4.79236  -25.46754 18.95771  1.000 30.49077 ? 244 GLN   A C   1 
ATOM   1900 O  O   . GLN   A 1 244 ? -5.71388  -25.15095 19.72381  1.000 29.83331 ? 244 GLN   A O   1 
ATOM   1901 C  CB  . GLN   A 1 244 ? -2.98632  -26.87035 19.96075  1.000 28.38383 ? 244 GLN   A CB  1 
ATOM   1902 C  CG  . GLN   A 1 244 ? -3.39326  -26.50305 21.36535  1.000 29.86596 ? 244 GLN   A CG  1 
ATOM   1903 C  CD  . GLN   A 1 244 ? -4.52493  -27.37732 21.86289  1.000 30.84327 ? 244 GLN   A CD  1 
ATOM   1904 O  OE1 . GLN   A 1 244 ? -4.52054  -28.59353 21.66245  1.000 31.10751 ? 244 GLN   A OE1 1 
ATOM   1905 N  NE2 . GLN   A 1 244 ? -5.52184  -26.75442 22.48604  1.000 32.85890 ? 244 GLN   A NE2 1 
ATOM   1906 N  N   . ASP   A 1 245 ? -4.30284  -24.62341 18.04311  1.000 28.58798 ? 245 ASP   A N   1 
ATOM   1907 C  CA  . ASP   A 1 245 ? -4.92264  -23.31575 17.85642  1.000 29.40875 ? 245 ASP   A CA  1 
ATOM   1908 C  C   . ASP   A 1 245 ? -6.34703  -23.42435 17.31729  1.000 29.21816 ? 245 ASP   A C   1 
ATOM   1909 O  O   . ASP   A 1 245 ? -7.22811  -22.66893 17.74395  1.000 30.17123 ? 245 ASP   A O   1 
ATOM   1910 C  CB  . ASP   A 1 245 ? -4.08806  -22.43938 16.93327  1.000 31.19689 ? 245 ASP   A CB  1 
ATOM   1911 C  CG  . ASP   A 1 245 ? -4.43153  -20.97024 17.09655  1.000 33.20164 ? 245 ASP   A CG  1 
ATOM   1912 O  OD1 . ASP   A 1 245 ? -4.42619  -20.49049 18.25140  1.000 35.77716 ? 245 ASP   A OD1 1 
ATOM   1913 O  OD2 . ASP   A 1 245 ? -4.76011  -20.32056 16.08160  1.000 34.92707 ? 245 ASP   A OD2 1 
ATOM   1914 N  N   . HIS   A 1 246 ? -6.59350  -24.32624 16.35873  1.000 28.14239 ? 246 HIS   A N   1 
ATOM   1915 C  CA  . HIS   A 1 246 ? -7.97646  -24.57400 15.93389  1.000 26.02903 ? 246 HIS   A CA  1 
ATOM   1916 C  C   . HIS   A 1 246 ? -8.84615  -25.01603 17.10628  1.000 27.43113 ? 246 HIS   A C   1 
ATOM   1917 O  O   . HIS   A 1 246 ? -10.00569 -24.59774 17.22642  1.000 27.20112 ? 246 HIS   A O   1 
ATOM   1918 C  CB  . HIS   A 1 246 ? -8.03957  -25.64788 14.84856  1.000 25.55868 ? 246 HIS   A CB  1 
ATOM   1919 C  CG  . HIS   A 1 246 ? -7.37596  -25.27720 13.55919  1.000 23.64062 ? 246 HIS   A CG  1 
ATOM   1920 N  ND1 . HIS   A 1 246 ? -6.74644  -26.20950 12.76271  1.000 23.90476 ? 246 HIS   A ND1 1 
ATOM   1921 C  CD2 . HIS   A 1 246 ? -7.26745  -24.09368 12.91292  1.000 24.75060 ? 246 HIS   A CD2 1 
ATOM   1922 C  CE1 . HIS   A 1 246 ? -6.28082  -25.61612 11.67684  1.000 25.75629 ? 246 HIS   A CE1 1 
ATOM   1923 N  NE2 . HIS   A 1 246 ? -6.57660  -24.33057 11.74661  1.000 23.47132 ? 246 HIS   A NE2 1 
ATOM   1924 N  N   . VAL   A 1 247 ? -8.32246  -25.90483 17.94919  1.000 27.06914 ? 247 VAL   A N   1 
ATOM   1925 C  CA  . VAL   A 1 247 ? -9.06690  -26.34911 19.12491  1.000 27.80354 ? 247 VAL   A CA  1 
ATOM   1926 C  C   . VAL   A 1 247 ? -9.39320  -25.15737 20.01658  1.000 29.12068 ? 247 VAL   A C   1 
ATOM   1927 O  O   . VAL   A 1 247 ? -10.52433 -25.00621 20.49811  1.000 29.86474 ? 247 VAL   A O   1 
ATOM   1928 C  CB  . VAL   A 1 247 ? -8.27385  -27.43170 19.88345  1.000 30.30579 ? 247 VAL   A CB  1 
ATOM   1929 C  CG1 . VAL   A 1 247 ? -8.94187  -27.75945 21.21731  1.000 30.41680 ? 247 VAL   A CG1 1 
ATOM   1930 C  CG2 . VAL   A 1 247 ? -8.12884  -28.68134 19.03294  1.000 29.70093 ? 247 VAL   A CG2 1 
ATOM   1931 N  N   . ASP   A 1 248 ? -8.40255  -24.28916 20.24594  1.000 29.00736 ? 248 ASP   A N   1 
ATOM   1932 C  CA  . ASP   A 1 248 ? -8.62903  -23.09474 21.05666  1.000 31.50515 ? 248 ASP   A CA  1 
ATOM   1933 C  C   . ASP   A 1 248 ? -9.69721  -22.20122 20.43738  1.000 28.55429 ? 248 ASP   A C   1 
ATOM   1934 O  O   . ASP   A 1 248 ? -10.61929 -21.75068 21.12890  1.000 30.48037 ? 248 ASP   A O   1 
ATOM   1935 C  CB  . ASP   A 1 248 ? -7.31095  -22.32886 21.25156  1.000 29.03780 ? 248 ASP   A CB  1 
ATOM   1936 C  CG  . ASP   A 1 248 ? -6.28914  -23.11465 22.07091  1.000 30.23819 ? 248 ASP   A CG  1 
ATOM   1937 O  OD1 . ASP   A 1 248 ? -6.68697  -24.06600 22.78166  1.000 33.92561 ? 248 ASP   A OD1 1 
ATOM   1938 O  OD2 . ASP   A 1 248 ? -5.08362  -22.78271 22.01405  1.000 32.85822 ? 248 ASP   A OD2 1 
ATOM   1939 N  N   . ILE   A 1 249 ? -9.60604  -21.95702 19.12363  1.000 28.31529 ? 249 ILE   A N   1 
ATOM   1940 C  CA  . ILE   A 1 249 ? -10.58391 -21.11007 18.43608  1.000 28.23653 ? 249 ILE   A CA  1 
ATOM   1941 C  C   . ILE   A 1 249 ? -11.98968 -21.68547 18.56500  1.000 26.49030 ? 249 ILE   A C   1 
ATOM   1942 O  O   . ILE   A 1 249 ? -12.97156 -20.93497 18.63757  1.000 28.03378 ? 249 ILE   A O   1 
ATOM   1943 C  CB  . ILE   A 1 249 ? -10.19053 -20.91694 16.95212  1.000 27.51490 ? 249 ILE   A CB  1 
ATOM   1944 C  CG1 . ILE   A 1 249 ? -8.96081  -20.02020 16.81976  1.000 29.06909 ? 249 ILE   A CG1 1 
ATOM   1945 C  CG2 . ILE   A 1 249 ? -11.33062 -20.35036 16.12600  1.000 27.65503 ? 249 ILE   A CG2 1 
ATOM   1946 C  CD1 . ILE   A 1 249 ? -8.02527  -20.45414 15.69626  1.000 30.28447 ? 249 ILE   A CD1 1 
ATOM   1947 N  N   . LEU   A 1 250 ? -12.11565 -23.01341 18.60373  1.000 26.47141 ? 250 LEU   A N   1 
ATOM   1948 C  CA  . LEU   A 1 250 ? -13.41496 -23.66118 18.77173  1.000 27.15696 ? 250 LEU   A CA  1 
ATOM   1949 C  C   . LEU   A 1 250 ? -13.89607 -23.67094 20.22218  1.000 27.99940 ? 250 LEU   A C   1 
ATOM   1950 O  O   . LEU   A 1 250 ? -15.00397 -24.16198 20.48767  1.000 26.44756 ? 250 LEU   A O   1 
ATOM   1951 C  CB  . LEU   A 1 250 ? -13.35360 -25.09649 18.23831  1.000 26.10319 ? 250 LEU   A CB  1 
ATOM   1952 C  CG  . LEU   A 1 250 ? -13.16162 -25.23593 16.72660  1.000 24.74171 ? 250 LEU   A CG  1 
ATOM   1953 C  CD1 . LEU   A 1 250 ? -12.86189 -26.69278 16.36906  1.000 22.94773 ? 250 LEU   A CD1 1 
ATOM   1954 C  CD2 . LEU   A 1 250 ? -14.37796 -24.71990 15.96418  1.000 22.14535 ? 250 LEU   A CD2 1 
ATOM   1955 N  N   . GLY   A 1 251 ? -13.10331 -23.13229 21.15360  1.000 26.94581 ? 251 GLY   A N   1 
ATOM   1956 C  CA  . GLY   A 1 251 ? -13.43935 -23.09736 22.56073  1.000 28.00735 ? 251 GLY   A CA  1 
ATOM   1957 C  C   . GLY   A 1 251 ? -14.81075 -22.52906 22.88849  1.000 27.95192 ? 251 GLY   A C   1 
ATOM   1958 O  O   . GLY   A 1 251 ? -15.61987 -23.17630 23.56420  1.000 29.79511 ? 251 GLY   A O   1 
ATOM   1959 N  N   . PRO   A 1 252 ? -15.09228 -21.29321 22.45040  1.000 29.94698 ? 252 PRO   A N   1 
ATOM   1960 C  CA  . PRO   A 1 252 ? -16.41237 -20.70697 22.75375  1.000 29.72981 ? 252 PRO   A CA  1 
ATOM   1961 C  C   . PRO   A 1 252 ? -17.57613 -21.56566 22.29123  1.000 28.91791 ? 252 PRO   A C   1 
ATOM   1962 O  O   . PRO   A 1 252 ? -18.53758 -21.76302 23.04797  1.000 29.47208 ? 252 PRO   A O   1 
ATOM   1963 C  CB  . PRO   A 1 252 ? -16.37368 -19.36671 22.00835  1.000 30.21317 ? 252 PRO   A CB  1 
ATOM   1964 C  CG  . PRO   A 1 252 ? -14.93148 -19.00710 21.98437  1.000 30.43903 ? 252 PRO   A CG  1 
ATOM   1965 C  CD  . PRO   A 1 252 ? -14.19189 -20.30823 21.82111  1.000 29.84317 ? 252 PRO   A CD  1 
ATOM   1966 N  N   . LEU   A 1 253 ? -17.50451 -22.08582 21.06477  1.000 28.61391 ? 253 LEU   A N   1 
ATOM   1967 C  CA  . LEU   A 1 253 ? -18.56612 -22.93903 20.53831  1.000 25.78625 ? 253 LEU   A CA  1 
ATOM   1968 C  C   . LEU   A 1 253 ? -18.69723 -24.21393 21.35668  1.000 26.73149 ? 253 LEU   A C   1 
ATOM   1969 O  O   . LEU   A 1 253 ? -19.81110 -24.64552 21.67297  1.000 26.19611 ? 253 LEU   A O   1 
ATOM   1970 C  CB  . LEU   A 1 253 ? -18.27596 -23.27011 19.07828  1.000 23.99487 ? 253 LEU   A CB  1 
ATOM   1971 C  CG  . LEU   A 1 253 ? -18.52307 -22.15663 18.05919  1.000 23.59632 ? 253 LEU   A CG  1 
ATOM   1972 C  CD1 . LEU   A 1 253 ? -18.17876 -22.61176 16.63987  1.000 20.34460 ? 253 LEU   A CD1 1 
ATOM   1973 C  CD2 . LEU   A 1 253 ? -19.97161 -21.73123 18.16431  1.000 22.59333 ? 253 LEU   A CD2 1 
ATOM   1974 N  N   . SER   A 1 254 ? -17.56540 -24.82976 21.70244  1.000 26.27955 ? 254 SER   A N   1 
ATOM   1975 C  CA  . SER   A 1 254 ? -17.57068 -25.97289 22.61126  1.000 27.95321 ? 254 SER   A CA  1 
ATOM   1976 C  C   . SER   A 1 254 ? -18.28996 -25.64292 23.91086  1.000 29.47515 ? 254 SER   A C   1 
ATOM   1977 O  O   . SER   A 1 254 ? -19.17677 -26.38460 24.35370  1.000 32.09848 ? 254 SER   A O   1 
ATOM   1978 C  CB  . SER   A 1 254 ? -16.12973 -26.40994 22.90025  1.000 27.90726 ? 254 SER   A CB  1 
ATOM   1979 O  OG  . SER   A 1 254 ? -16.08472 -27.63921 23.60860  1.000 30.49051 ? 254 SER   A OG  1 
ATOM   1980 N  N   . ALA   A 1 255 ? -17.90967 -24.52962 24.54318  1.000 28.88382 ? 255 ALA   A N   1 
ATOM   1981 C  CA  . ALA   A 1 255 ? -18.45514 -24.18783 25.85187  1.000 32.86043 ? 255 ALA   A CA  1 
ATOM   1982 C  C   . ALA   A 1 255 ? -19.94522 -23.88535 25.77685  1.000 31.56639 ? 255 ALA   A C   1 
ATOM   1983 O  O   . ALA   A 1 255 ? -20.69440 -24.21071 26.70574  1.000 32.98966 ? 255 ALA   A O   1 
ATOM   1984 C  CB  . ALA   A 1 255 ? -17.69011 -22.99871 26.43548  1.000 33.75309 ? 255 ALA   A CB  1 
ATOM   1985 N  N   . GLN   A 1 256 ? -20.39351 -23.28660 24.67400  1.000 31.27106 ? 256 GLN   A N   1 
ATOM   1986 C  CA  . GLN   A 1 256 ? -21.81224 -23.00200 24.50400  1.000 29.87671 ? 256 GLN   A CA  1 
ATOM   1987 C  C   . GLN   A 1 256 ? -22.63090 -24.27205 24.30723  1.000 32.01488 ? 256 GLN   A C   1 
ATOM   1988 O  O   . GLN   A 1 256 ? -23.75833 -24.36172 24.80928  1.000 34.36687 ? 256 GLN   A O   1 
ATOM   1989 C  CB  . GLN   A 1 256 ? -22.00279 -22.04532 23.33351  1.000 29.70206 ? 256 GLN   A CB  1 
ATOM   1990 C  CG  . GLN   A 1 256 ? -23.39880 -21.48876 23.18517  1.000 33.39415 ? 256 GLN   A CG  1 
ATOM   1991 C  CD  . GLN   A 1 256 ? -23.59285 -20.87629 21.82160  1.000 33.79820 ? 256 GLN   A CD  1 
ATOM   1992 O  OE1 . GLN   A 1 256 ? -22.61695 -20.59837 21.12453  1.000 33.73523 ? 256 GLN   A OE1 1 
ATOM   1993 N  NE2 . GLN   A 1 256 ? -24.84790 -20.66273 21.42446  1.000 33.00092 ? 256 GLN   A NE2 1 
ATOM   1994 N  N   . THR   A 1 257 ? -22.08375 -25.27132 23.61583  1.000 30.18312 ? 257 THR   A N   1 
ATOM   1995 C  CA  . THR   A 1 257 ? -22.82497 -26.50204 23.37016  1.000 29.21026 ? 257 THR   A CA  1 
ATOM   1996 C  C   . THR   A 1 257 ? -22.57107 -27.57814 24.41475  1.000 30.32037 ? 257 THR   A C   1 
ATOM   1997 O  O   . THR   A 1 257 ? -23.35310 -28.52959 24.50185  1.000 32.78931 ? 257 THR   A O   1 
ATOM   1998 C  CB  . THR   A 1 257 ? -22.48712 -27.05889 21.98444  1.000 27.85027 ? 257 THR   A CB  1 
ATOM   1999 O  OG1 . THR   A 1 257 ? -21.07112 -27.24669 21.88324  1.000 28.78466 ? 257 THR   A OG1 1 
ATOM   2000 C  CG2 . THR   A 1 257 ? -22.93492 -26.07449 20.91089  1.000 24.61785 ? 257 THR   A CG2 1 
ATOM   2001 N  N   . GLY   A 1 258 ? -21.52221 -27.44674 25.21836  1.000 28.81553 ? 258 GLY   A N   1 
ATOM   2002 C  CA  . GLY   A 1 258 ? -21.18261 -28.49484 26.15516  1.000 31.69205 ? 258 GLY   A CA  1 
ATOM   2003 C  C   . GLY   A 1 258 ? -20.57839 -29.72287 25.52108  1.000 31.07585 ? 258 GLY   A C   1 
ATOM   2004 O  O   . GLY   A 1 258 ? -20.53435 -30.78010 26.15731  1.000 33.39438 ? 258 GLY   A O   1 
ATOM   2005 N  N   . ILE   A 1 259 ? -20.11540 -29.61996 24.27956  1.000 31.09517 ? 259 ILE   A N   1 
ATOM   2006 C  CA  . ILE   A 1 259 ? -19.51007 -30.73676 23.56828  1.000 31.29788 ? 259 ILE   A CA  1 
ATOM   2007 C  C   . ILE   A 1 259 ? -18.03008 -30.42049 23.40377  1.000 31.44426 ? 259 ILE   A C   1 
ATOM   2008 O  O   . ILE   A 1 259 ? -17.66964 -29.45445 22.72098  1.000 29.34692 ? 259 ILE   A O   1 
ATOM   2009 C  CB  . ILE   A 1 259 ? -20.18155 -30.97953 22.21120  1.000 29.56773 ? 259 ILE   A CB  1 
ATOM   2010 C  CG1 . ILE   A 1 259 ? -21.62445 -31.44697 22.40473  1.000 32.49380 ? 259 ILE   A CG1 1 
ATOM   2011 C  CG2 . ILE   A 1 259 ? -19.39909 -32.00510 21.39840  1.000 29.53743 ? 259 ILE   A CG2 1 
ATOM   2012 C  CD1 . ILE   A 1 259 ? -22.43797 -31.24098 21.17349  1.000 29.82802 ? 259 ILE   A CD1 1 
ATOM   2013 N  N   . ALA   A 1 260 ? -17.17249 -31.22076 24.04329  1.000 30.22781 ? 260 ALA   A N   1 
ATOM   2014 C  CA  . ALA   A 1 260 ? -15.73501 -31.00370 23.94927  1.000 32.06977 ? 260 ALA   A CA  1 
ATOM   2015 C  C   . ALA   A 1 260 ? -15.28214 -31.06016 22.49019  1.000 27.44543 ? 260 ALA   A C   1 
ATOM   2016 O  O   . ALA   A 1 260 ? -15.85698 -31.77605 21.66786  1.000 29.76337 ? 260 ALA   A O   1 
ATOM   2017 C  CB  . ALA   A 1 260 ? -14.99702 -32.04760 24.79026  1.000 31.25792 ? 260 ALA   A CB  1 
ATOM   2018 N  N   . VAL   A 1 261 ? -14.25807 -30.27226 22.15431  1.000 29.75586 ? 261 VAL   A N   1 
ATOM   2019 C  CA  . VAL   A 1 261 ? -13.81536 -30.22140 20.76104  1.000 27.30631 ? 261 VAL   A CA  1 
ATOM   2020 C  C   . VAL   A 1 261 ? -13.42505 -31.61469 20.28308  1.000 28.20086 ? 261 VAL   A C   1 
ATOM   2021 O  O   . VAL   A 1 261 ? -13.87376 -32.07634 19.22970  1.000 27.69714 ? 261 VAL   A O   1 
ATOM   2022 C  CB  . VAL   A 1 261 ? -12.65840 -29.22176 20.58783  1.000 27.60941 ? 261 VAL   A CB  1 
ATOM   2023 C  CG1 . VAL   A 1 261 ? -12.07123 -29.32843 19.17201  1.000 23.31303 ? 261 VAL   A CG1 1 
ATOM   2024 C  CG2 . VAL   A 1 261 ? -13.11436 -27.80693 20.87801  1.000 24.26183 ? 261 VAL   A CG2 1 
ATOM   2025 N  N   . LEU   A 1 262 ? -12.61832 -32.32430 21.07571  1.000 30.82114 ? 262 LEU   A N   1 
ATOM   2026 C  CA  . LEU   A 1 262 ? -12.18255 -33.66054 20.67724  1.000 32.01039 ? 262 LEU   A CA  1 
ATOM   2027 C  C   . LEU   A 1 262 ? -13.35925 -34.62761 20.57381  1.000 30.45908 ? 262 LEU   A C   1 
ATOM   2028 O  O   . LEU   A 1 262 ? -13.29618 -35.60534 19.81574  1.000 29.12508 ? 262 LEU   A O   1 
ATOM   2029 C  CB  . LEU   A 1 262 ? -11.14488 -34.20785 21.66211  1.000 32.41135 ? 262 LEU   A CB  1 
ATOM   2030 C  CG  . LEU   A 1 262 ? -9.73817  -33.58485 21.63909  1.000 34.09627 ? 262 LEU   A CG  1 
ATOM   2031 C  CD1 . LEU   A 1 262 ? -9.07278  -33.68757 20.25967  1.000 35.50418 ? 262 LEU   A CD1 1 
ATOM   2032 C  CD2 . LEU   A 1 262 ? -9.71174  -32.16016 22.18246  1.000 36.18733 ? 262 LEU   A CD2 1 
ATOM   2033 N  N   . ASP   A 1 263 ? -14.43629 -34.37573 21.32618  1.000 29.21162 ? 263 ASP   A N   1 
ATOM   2034 C  CA  . ASP   A 1 263 ? -15.64932 -35.17438 21.16733  1.000 31.92108 ? 263 ASP   A CA  1 
ATOM   2035 C  C   . ASP   A 1 263 ? -16.28645 -34.92699 19.80292  1.000 28.50369 ? 263 ASP   A C   1 
ATOM   2036 O  O   . ASP   A 1 263 ? -16.68346 -35.87314 19.11060  1.000 28.79621 ? 263 ASP   A O   1 
ATOM   2037 C  CB  . ASP   A 1 263 ? -16.64225 -34.86006 22.29607  1.000 29.67827 ? 263 ASP   A CB  1 
ATOM   2038 C  CG  . ASP   A 1 263 ? -16.20918 -35.43693 23.64879  1.000 32.97701 ? 263 ASP   A CG  1 
ATOM   2039 O  OD1 . ASP   A 1 263 ? -15.09854 -35.99359 23.74693  1.000 34.01496 ? 263 ASP   A OD1 1 
ATOM   2040 O  OD2 . ASP   A 1 263 ? -16.99504 -35.35009 24.62056  1.000 34.00711 ? 263 ASP   A OD2 1 
ATOM   2041 N  N   . MET   A 1 264 ? -16.39878 -33.66118 19.39747  1.000 28.31125 ? 264 MET   A N   1 
ATOM   2042 C  CA  . MET   A 1 264 ? -16.85403 -33.37058 18.04298  1.000 25.56098 ? 264 MET   A CA  1 
ATOM   2043 C  C   . MET   A 1 264 ? -15.93121 -33.97123 16.99260  1.000 27.27172 ? 264 MET   A C   1 
ATOM   2044 O  O   . MET   A 1 264 ? -16.40276 -34.37043 15.92177  1.000 26.89218 ? 264 MET   A O   1 
ATOM   2045 C  CB  . MET   A 1 264 ? -16.99514 -31.86013 17.82175  1.000 26.29191 ? 264 MET   A CB  1 
ATOM   2046 C  CG  . MET   A 1 264 ? -17.85841 -31.50493 16.60643  1.000 22.53708 ? 264 MET   A CG  1 
ATOM   2047 S  SD  . MET   A 1 264 ? -19.59231 -31.93577 16.83219  1.000 22.68217 ? 264 MET   A SD  1 
ATOM   2048 C  CE  . MET   A 1 264 ? -20.21871 -30.46774 17.64107  1.000 22.46630 ? 264 MET   A CE  1 
ATOM   2049 N  N   . CYS   A 1 265 ? -14.61962 -34.02824 17.26030  1.000 29.00757 ? 265 CYS   A N   1 
ATOM   2050 C  CA  . CYS   A 1 265 ? -13.72444 -34.68601 16.31340  1.000 26.74341 ? 265 CYS   A CA  1 
ATOM   2051 C  C   . CYS   A 1 265 ? -14.09072 -36.15210 16.14657  1.000 27.42391 ? 265 CYS   A C   1 
ATOM   2052 O  O   . CYS   A 1 265 ? -14.10684 -36.66515 15.02312  1.000 28.51593 ? 265 CYS   A O   1 
ATOM   2053 C  CB  . CYS   A 1 265 ? -12.26418 -34.53451 16.74789  1.000 29.15684 ? 265 CYS   A CB  1 
ATOM   2054 S  SG  . CYS   A 1 265 ? -11.61256 -32.85954 16.58350  1.000 25.94157 ? 265 CYS   A SG  1 
ATOM   2055 N  N   . ALA   A 1 266 ? -14.39187 -36.84521 17.25487  1.000 30.21912 ? 266 ALA   A N   1 
ATOM   2056 C  CA  . ALA   A 1 266 ? -14.86588 -38.22063 17.15739  1.000 28.76242 ? 266 ALA   A CA  1 
ATOM   2057 C  C   . ALA   A 1 266 ? -16.09293 -38.31597 16.25752  1.000 30.26990 ? 266 ALA   A C   1 
ATOM   2058 O  O   . ALA   A 1 266 ? -16.18966 -39.22697 15.42670  1.000 31.90794 ? 266 ALA   A O   1 
ATOM   2059 C  CB  . ALA   A 1 266 ? -15.16734 -38.77250 18.54870  1.000 31.76856 ? 266 ALA   A CB  1 
ATOM   2060 N  N   . SER   A 1 267 ? -17.02927 -37.36551 16.38770  1.000 28.22810 ? 267 SER   A N   1 
ATOM   2061 C  CA  . SER   A 1 267 ? -18.21956 -37.37655 15.54334  1.000 27.69727 ? 267 SER   A CA  1 
ATOM   2062 C  C   . SER   A 1 267 ? -17.86854 -37.16415 14.07912  1.000 28.87042 ? 267 SER   A C   1 
ATOM   2063 O  O   . SER   A 1 267 ? -18.41676 -37.83580 13.19936  1.000 29.40853 ? 267 SER   A O   1 
ATOM   2064 C  CB  . SER   A 1 267 ? -19.20596 -36.30725 16.00999  1.000 28.79470 ? 267 SER   A CB  1 
ATOM   2065 O  OG  . SER   A 1 267 ? -19.77337 -36.69598 17.24046  1.000 32.44476 ? 267 SER   A OG  1 
ATOM   2066 N  N   . LEU   A 1 268 ? -16.98135 -36.21046 13.79415  1.000 27.13012 ? 268 LEU   A N   1 
ATOM   2067 C  CA  . LEU   A 1 268 ? -16.53003 -36.02156 12.42282  1.000 27.73638 ? 268 LEU   A CA  1 
ATOM   2068 C  C   . LEU   A 1 268 ? -15.85235 -37.27814 11.88975  1.000 29.32222 ? 268 LEU   A C   1 
ATOM   2069 O  O   . LEU   A 1 268 ? -16.09681 -37.68117 10.74839  1.000 31.88405 ? 268 LEU   A O   1 
ATOM   2070 C  CB  . LEU   A 1 268 ? -15.59071 -34.81769 12.34127  1.000 26.88527 ? 268 LEU   A CB  1 
ATOM   2071 C  CG  . LEU   A 1 268 ? -15.06968 -34.43091 10.95756  1.000 24.64458 ? 268 LEU   A CG  1 
ATOM   2072 C  CD1 . LEU   A 1 268 ? -16.20265 -34.38468 9.93539   1.000 25.36283 ? 268 LEU   A CD1 1 
ATOM   2073 C  CD2 . LEU   A 1 268 ? -14.34780 -33.09348 11.02056  1.000 24.20423 ? 268 LEU   A CD2 1 
ATOM   2074 N  N   . LYS   A 1 269 ? -15.00040 -37.90935 12.70257  1.000 27.85243 ? 269 LYS   A N   1 
ATOM   2075 C  CA  . LYS   A 1 269 ? -14.38312 -39.17643 12.31602  1.000 30.43786 ? 269 LYS   A CA  1 
ATOM   2076 C  C   . LYS   A 1 269 ? -15.43185 -40.18796 11.87496  1.000 32.60769 ? 269 LYS   A C   1 
ATOM   2077 O  O   . LYS   A 1 269 ? -15.31333 -40.80069 10.80868  1.000 33.41454 ? 269 LYS   A O   1 
ATOM   2078 C  CB  . LYS   A 1 269 ? -13.57387 -39.74776 13.48117  1.000 31.74329 ? 269 LYS   A CB  1 
ATOM   2079 C  CG  . LYS   A 1 269 ? -13.12030 -41.18861 13.26015  1.000 34.95708 ? 269 LYS   A CG  1 
ATOM   2080 C  CD  . LYS   A 1 269 ? -11.75479 -41.50384 13.85658  1.000 37.85450 ? 269 LYS   A CD  1 
ATOM   2081 C  CE  . LYS   A 1 269 ? -11.53690 -40.80422 15.19755  1.000 38.90507 ? 269 LYS   A CE  1 
ATOM   2082 N  NZ  . LYS   A 1 269 ? -10.27185 -41.25817 15.87063  1.000 44.50550 ? 269 LYS   A NZ  1 
ATOM   2083 N  N   . GLU   A 1 270 ? -16.47950 -40.36688 12.68785  1.000 33.28681 ? 270 GLU   A N   1 
ATOM   2084 C  CA  . GLU   A 1 270 ? -17.52178 -41.33236 12.35296  1.000 34.56771 ? 270 GLU   A CA  1 
ATOM   2085 C  C   . GLU   A 1 270 ? -18.26527 -40.92986 11.08260  1.000 34.63672 ? 270 GLU   A C   1 
ATOM   2086 O  O   . GLU   A 1 270 ? -18.61185 -41.78909 10.26347  1.000 36.51160 ? 270 GLU   A O   1 
ATOM   2087 C  CB  . GLU   A 1 270 ? -18.50082 -41.48006 13.52036  1.000 35.18945 ? 270 GLU   A CB  1 
ATOM   2088 C  CG  . GLU   A 1 270 ? -17.96082 -42.31077 14.67115  1.000 37.40023 ? 270 GLU   A CG  1 
ATOM   2089 C  CD  . GLU   A 1 270 ? -17.43097 -43.66213 14.24034  1.000 42.24314 ? 270 GLU   A CD  1 
ATOM   2090 O  OE1 . GLU   A 1 270 ? -16.25595 -43.96253 14.54127  1.000 46.07896 ? 270 GLU   A OE1 1 
ATOM   2091 O  OE2 . GLU   A 1 270 ? -18.18666 -44.42908 13.60433  1.000 46.27390 ? 270 GLU   A OE2 1 
ATOM   2092 N  N   . LEU   A 1 271 ? -18.52569 -39.62948 10.90380  1.000 31.90177 ? 271 LEU   A N   1 
ATOM   2093 C  CA  . LEU   A 1 271 ? -19.20155 -39.16458 9.69444   1.000 32.06303 ? 271 LEU   A CA  1 
ATOM   2094 C  C   . LEU   A 1 271 ? -18.34475 -39.40662 8.45947   1.000 34.72527 ? 271 LEU   A C   1 
ATOM   2095 O  O   . LEU   A 1 271 ? -18.86786 -39.70333 7.37798   1.000 33.43760 ? 271 LEU   A O   1 
ATOM   2096 C  CB  . LEU   A 1 271 ? -19.54426 -37.68234 9.82658   1.000 31.76412 ? 271 LEU   A CB  1 
ATOM   2097 C  CG  . LEU   A 1 271 ? -20.74091 -37.34633 10.71512  1.000 31.52551 ? 271 LEU   A CG  1 
ATOM   2098 C  CD1 . LEU   A 1 271 ? -20.79776 -35.85167 10.99140  1.000 29.22364 ? 271 LEU   A CD1 1 
ATOM   2099 C  CD2 . LEU   A 1 271 ? -22.00750 -37.80703 10.03283  1.000 33.10643 ? 271 LEU   A CD2 1 
ATOM   2100 N  N   . LEU   A 1 272 ? -17.02120 -39.29758 8.60773   1.000 33.27000 ? 272 LEU   A N   1 
ATOM   2101 C  CA  . LEU   A 1 272 ? -16.12485 -39.54095 7.48339   1.000 32.10232 ? 272 LEU   A CA  1 
ATOM   2102 C  C   . LEU   A 1 272 ? -16.06655 -41.02275 7.14366   1.000 35.90252 ? 272 LEU   A C   1 
ATOM   2103 O  O   . LEU   A 1 272 ? -16.02807 -41.39336 5.96483   1.000 37.59579 ? 272 LEU   A O   1 
ATOM   2104 C  CB  . LEU   A 1 272 ? -14.73156 -39.00999 7.80770   1.000 32.00581 ? 272 LEU   A CB  1 
ATOM   2105 C  CG  . LEU   A 1 272 ? -14.59595 -37.49116 7.86811   1.000 29.42489 ? 272 LEU   A CG  1 
ATOM   2106 C  CD1 . LEU   A 1 272 ? -13.23106 -37.09842 8.41923   1.000 31.96036 ? 272 LEU   A CD1 1 
ATOM   2107 C  CD2 . LEU   A 1 272 ? -14.83161 -36.87513 6.50426   1.000 29.65018 ? 272 LEU   A CD2 1 
ATOM   2108 N  N   . GLN   A 1 273 ? -16.07702 -41.88545 8.16356   1.000 37.51335 ? 273 GLN   A N   1 
ATOM   2109 C  CA  . GLN   A 1 273 ? -15.91572 -43.31896 7.94964   1.000 39.01649 ? 273 GLN   A CA  1 
ATOM   2110 C  C   . GLN   A 1 273 ? -17.21552 -44.01053 7.56581   1.000 39.37667 ? 273 GLN   A C   1 
ATOM   2111 O  O   . GLN   A 1 273 ? -17.16938 -45.08363 6.95421   1.000 41.69782 ? 273 GLN   A O   1 
ATOM   2112 C  CB  . GLN   A 1 273 ? -15.34368 -43.98530 9.20349   1.000 37.92755 ? 273 GLN   A CB  1 
ATOM   2113 C  CG  . GLN   A 1 273 ? -13.92144 -43.56339 9.54914   1.000 38.32544 ? 273 GLN   A CG  1 
ATOM   2114 C  CD  . GLN   A 1 273 ? -13.49430 -44.03126 10.93233  1.000 41.27498 ? 273 GLN   A CD  1 
ATOM   2115 O  OE1 . GLN   A 1 273 ? -14.32438 -44.43626 11.75258  1.000 44.49538 ? 273 GLN   A OE1 1 
ATOM   2116 N  NE2 . GLN   A 1 273 ? -12.19495 -43.97185 11.20032  1.000 41.08390 ? 273 GLN   A NE2 1 
ATOM   2117 N  N   . ASN   A 1 274 ? -18.36809 -43.43047 7.90948   1.000 38.69286 ? 274 ASN   A N   1 
ATOM   2118 C  CA  . ASN   A 1 274 ? -19.65377 -44.06776 7.66802   1.000 39.47786 ? 274 ASN   A CA  1 
ATOM   2119 C  C   . ASN   A 1 274 ? -20.56005 -43.29994 6.72454   1.000 40.31773 ? 274 ASN   A C   1 
ATOM   2120 O  O   . ASN   A 1 274 ? -21.58040 -43.85083 6.29703   1.000 41.03791 ? 274 ASN   A O   1 
ATOM   2121 C  CB  . ASN   A 1 274 ? -20.41031 -44.28485 8.98794   1.000 38.93574 ? 274 ASN   A CB  1 
ATOM   2122 C  CG  . ASN   A 1 274 ? -19.56505 -44.96562 10.04456  1.000 43.86152 ? 274 ASN   A CG  1 
ATOM   2123 O  OD1 . ASN   A 1 274 ? -18.61432 -45.68918 9.73225   1.000 44.82643 ? 274 ASN   A OD1 1 
ATOM   2124 N  ND2 . ASN   A 1 274 ? -19.92280 -44.75498 11.31111  1.000 44.16868 ? 274 ASN   A ND2 1 
ATOM   2125 N  N   . GLY   A 1 275 ? -20.22929 -42.06553 6.38649   1.000 40.14115 ? 275 GLY   A N   1 
ATOM   2126 C  CA  . GLY   A 1 275 ? -21.16525 -41.26632 5.64258   1.000 41.06252 ? 275 GLY   A CA  1 
ATOM   2127 C  C   . GLY   A 1 275 ? -22.29956 -40.79948 6.54187   1.000 40.77675 ? 275 GLY   A C   1 
ATOM   2128 O  O   . GLY   A 1 275 ? -22.26786 -40.92106 7.76317   1.000 39.08421 ? 275 GLY   A O   1 
ATOM   2129 N  N   . MET   A 1 276 ? -23.33095 -40.26491 5.89959   1.000 43.58280 ? 276 MET   A N   1 
ATOM   2130 C  CA  . MET   A 1 276 ? -24.41314 -39.62272 6.61871   1.000 41.07188 ? 276 MET   A CA  1 
ATOM   2131 C  C   . MET   A 1 276 ? -25.67337 -40.47587 6.62285   1.000 44.80734 ? 276 MET   A C   1 
ATOM   2132 O  O   . MET   A 1 276 ? -26.61233 -40.17969 7.37569   1.000 42.14269 ? 276 MET   A O   1 
ATOM   2133 C  CB  . MET   A 1 276 ? -24.65986 -38.24481 5.99326   1.000 41.58386 ? 276 MET   A CB  1 
ATOM   2134 C  CG  . MET   A 1 276 ? -23.70594 -37.20360 6.58487   1.000 37.25002 ? 276 MET   A CG  1 
ATOM   2135 S  SD  . MET   A 1 276 ? -23.95906 -35.48514 6.15870   1.000 47.05411 ? 276 MET   A SD  1 
ATOM   2136 C  CE  . MET   A 1 276 ? -25.66129 -35.28901 6.58011   1.000 32.68540 ? 276 MET   A CE  1 
ATOM   2137 N  N   . ASN   A 1 277 ? -25.69288 -41.54788 5.82362   1.000 47.07500 ? 277 ASN   A N   1 
ATOM   2138 C  CA  . ASN   A 1 277 ? -26.70754 -42.59814 5.89921   1.000 45.63774 ? 277 ASN   A CA  1 
ATOM   2139 C  C   . ASN   A 1 277 ? -28.10586 -42.05640 5.61502   1.000 45.71167 ? 277 ASN   A C   1 
ATOM   2140 O  O   . ASN   A 1 277 ? -29.08091 -42.41361 6.28445   1.000 46.22965 ? 277 ASN   A O   1 
ATOM   2141 C  CB  . ASN   A 1 277 ? -26.65796 -43.31375 7.25255   1.000 48.40123 ? 277 ASN   A CB  1 
ATOM   2142 C  CG  . ASN   A 1 277 ? -27.40655 -44.62988 7.24113   1.000 52.99093 ? 277 ASN   A CG  1 
ATOM   2143 O  OD1 . ASN   A 1 277 ? -27.32235 -45.39833 6.28047   1.000 56.37073 ? 277 ASN   A OD1 1 
ATOM   2144 N  ND2 . ASN   A 1 277 ? -28.15246 -44.89658 8.30796   1.000 54.64808 ? 277 ASN   A ND2 1 
ATOM   2145 N  N   . GLY   A 1 278 ? -28.20602 -41.19340 4.60727   1.000 42.49200 ? 278 GLY   A N   1 
ATOM   2146 C  CA  . GLY   A 1 278 ? -29.48989 -40.66616 4.19777   1.000 43.51274 ? 278 GLY   A CA  1 
ATOM   2147 C  C   . GLY   A 1 278 ? -30.03544 -39.54775 5.05487   1.000 41.42339 ? 278 GLY   A C   1 
ATOM   2148 O  O   . GLY   A 1 278 ? -31.18043 -39.13509 4.85033   1.000 42.19635 ? 278 GLY   A O   1 
ATOM   2149 N  N   . ARG   A 1 279 ? -29.26351 -39.04328 6.00475   1.000 40.69721 ? 279 ARG   A N   1 
ATOM   2150 C  CA  . ARG   A 1 279 ? -29.69543 -37.94571 6.85070   1.000 37.05287 ? 279 ARG   A CA  1 
ATOM   2151 C  C   . ARG   A 1 279 ? -29.02787 -36.66041 6.38940   1.000 34.06221 ? 279 ARG   A C   1 
ATOM   2152 O  O   . ARG   A 1 279 ? -28.16158 -36.66112 5.51241   1.000 35.26660 ? 279 ARG   A O   1 
ATOM   2153 C  CB  . ARG   A 1 279 ? -29.37272 -38.25084 8.31584   1.000 37.25408 ? 279 ARG   A CB  1 
ATOM   2154 C  CG  . ARG   A 1 279 ? -30.22315 -39.38322 8.87902   1.000 39.43533 ? 279 ARG   A CG  1 
ATOM   2155 C  CD  . ARG   A 1 279 ? -29.69967 -39.83683 10.22093  1.000 40.68067 ? 279 ARG   A CD  1 
ATOM   2156 N  NE  . ARG   A 1 279 ? -28.42641 -40.53711 10.07716  1.000 42.84168 ? 279 ARG   A NE  1 
ATOM   2157 C  CZ  . ARG   A 1 279 ? -27.92314 -41.37252 10.97680  1.000 40.77979 ? 279 ARG   A CZ  1 
ATOM   2158 N  NH1 . ARG   A 1 279 ? -28.56937 -41.65033 12.10109  1.000 40.56517 ? 279 ARG   A NH1 1 
ATOM   2159 N  NH2 . ARG   A 1 279 ? -26.73969 -41.93826 10.74595  1.000 39.78202 ? 279 ARG   A NH2 1 
ATOM   2160 N  N   . THR   A 1 280 ? -29.45598 -35.54725 6.97536   1.000 33.06240 ? 280 THR   A N   1 
ATOM   2161 C  CA  . THR   A 1 280 ? -28.92943 -34.24384 6.60257   1.000 29.05888 ? 280 THR   A CA  1 
ATOM   2162 C  C   . THR   A 1 280 ? -28.55228 -33.45548 7.84857   1.000 26.72566 ? 280 THR   A C   1 
ATOM   2163 O  O   . THR   A 1 280 ? -29.02345 -33.72585 8.95718   1.000 25.37688 ? 280 THR   A O   1 
ATOM   2164 C  CB  . THR   A 1 280 ? -29.92087 -33.44556 5.74198   1.000 28.90027 ? 280 THR   A CB  1 
ATOM   2165 O  OG1 . THR   A 1 280 ? -31.14714 -33.24983 6.46356   1.000 29.60555 ? 280 THR   A OG1 1 
ATOM   2166 C  CG2 . THR   A 1 280 ? -30.20720 -34.19272 4.44058   1.000 30.20453 ? 280 THR   A CG2 1 
ATOM   2167 N  N   . ILE   A 1 281 ? -27.65977 -32.49578 7.64711   1.000 24.90849 ? 281 ILE   A N   1 
ATOM   2168 C  CA  . ILE   A 1 281 ? -27.19469 -31.58909 8.68654   1.000 22.67759 ? 281 ILE   A CA  1 
ATOM   2169 C  C   . ILE   A 1 281 ? -27.37280 -30.17128 8.16570   1.000 23.72037 ? 281 ILE   A C   1 
ATOM   2170 O  O   . ILE   A 1 281 ? -26.77914 -29.80852 7.14459   1.000 22.83568 ? 281 ILE   A O   1 
ATOM   2171 C  CB  . ILE   A 1 281 ? -25.72300 -31.84871 9.05944   1.000 20.29058 ? 281 ILE   A CB  1 
ATOM   2172 C  CG1 . ILE   A 1 281 ? -25.52079 -33.28341 9.55532   1.000 21.41719 ? 281 ILE   A CG1 1 
ATOM   2173 C  CG2 . ILE   A 1 281 ? -25.23974 -30.83385 10.07926  1.000 20.22564 ? 281 ILE   A CG2 1 
ATOM   2174 C  CD1 . ILE   A 1 281 ? -24.07199 -33.61854 10.00232  1.000 23.62950 ? 281 ILE   A CD1 1 
ATOM   2175 N  N   . LEU   A 1 282 ? -28.17986 -29.36851 8.86733   1.000 23.66069 ? 282 LEU   A N   1 
ATOM   2176 C  CA  . LEU   A 1 282 ? -28.44974 -27.97710 8.46819   1.000 25.46191 ? 282 LEU   A CA  1 
ATOM   2177 C  C   . LEU   A 1 282 ? -28.84013 -27.90373 6.99232   1.000 24.81587 ? 282 LEU   A C   1 
ATOM   2178 O  O   . LEU   A 1 282 ? -28.38693 -27.03461 6.23955   1.000 25.92595 ? 282 LEU   A O   1 
ATOM   2179 C  CB  . LEU   A 1 282 ? -27.25329 -27.05432 8.78183   1.000 20.33288 ? 282 LEU   A CB  1 
ATOM   2180 C  CG  . LEU   A 1 282 ? -27.13177 -26.74408 10.28686  1.000 19.88715 ? 282 LEU   A CG  1 
ATOM   2181 C  CD1 . LEU   A 1 282 ? -25.86660 -25.95555 10.63012  1.000 22.09920 ? 282 LEU   A CD1 1 
ATOM   2182 C  CD2 . LEU   A 1 282 ? -28.38214 -26.06467 10.87559  1.000 22.51982 ? 282 LEU   A CD2 1 
ATOM   2183 N  N   . GLY   A 1 283 ? -29.67238 -28.85526 6.57112   1.000 25.34536 ? 283 GLY   A N   1 
ATOM   2184 C  CA  . GLY   A 1 283 ? -30.14137 -28.90914 5.20011   1.000 30.15288 ? 283 GLY   A CA  1 
ATOM   2185 C  C   . GLY   A 1 283 ? -29.11526 -29.32198 4.17093   1.000 29.09446 ? 283 GLY   A C   1 
ATOM   2186 O  O   . GLY   A 1 283 ? -29.31498 -29.05766 2.98141   1.000 32.55608 ? 283 GLY   A O   1 
ATOM   2187 N  N   . SER   A 1 284 ? -28.01427 -29.94370 4.57856   1.000 27.69895 ? 284 SER   A N   1 
ATOM   2188 C  CA  . SER   A 1 284 ? -26.97365 -30.36594 3.64894   1.000 26.72989 ? 284 SER   A CA  1 
ATOM   2189 C  C   . SER   A 1 284 ? -26.74438 -31.86350 3.79269   1.000 27.67053 ? 284 SER   A C   1 
ATOM   2190 O  O   . SER   A 1 284 ? -26.84830 -32.41531 4.89465   1.000 25.33897 ? 284 SER   A O   1 
ATOM   2191 C  CB  . SER   A 1 284 ? -25.66417 -29.58262 3.88677   1.000 26.65109 ? 284 SER   A CB  1 
ATOM   2192 O  OG  . SER   A 1 284 ? -24.63409 -30.00567 2.99894   1.000 26.64053 ? 284 SER   A OG  1 
ATOM   2193 N  N   . ALA   A 1 285 ? -26.47896 -32.52824 2.66830   1.000 26.38526 ? 285 ALA   A N   1 
ATOM   2194 C  CA  . ALA   A 1 285 ? -26.10233 -33.93122 2.66601   1.000 26.48831 ? 285 ALA   A CA  1 
ATOM   2195 C  C   . ALA   A 1 285 ? -24.59560 -34.12376 2.53312   1.000 28.99705 ? 285 ALA   A C   1 
ATOM   2196 O  O   . ALA   A 1 285 ? -24.14207 -35.26122 2.34783   1.000 28.40659 ? 285 ALA   A O   1 
ATOM   2197 C  CB  . ALA   A 1 285 ? -26.82406 -34.67734 1.54579   1.000 27.49297 ? 285 ALA   A CB  1 
ATOM   2198 N  N   . LEU   A 1 286 ? -23.82150 -33.04153 2.61564   1.000 25.73233 ? 286 LEU   A N   1 
ATOM   2199 C  CA  . LEU   A 1 286 ? -22.36571 -33.09203 2.61400   1.000 29.81318 ? 286 LEU   A CA  1 
ATOM   2200 C  C   . LEU   A 1 286 ? -21.84766 -32.30531 3.80962   1.000 26.73027 ? 286 LEU   A C   1 
ATOM   2201 O  O   . LEU   A 1 286 ? -22.51633 -31.40259 4.31880   1.000 24.02612 ? 286 LEU   A O   1 
ATOM   2202 C  CB  . LEU   A 1 286 ? -21.74486 -32.45957 1.36217   1.000 28.65058 ? 286 LEU   A CB  1 
ATOM   2203 C  CG  . LEU   A 1 286 ? -22.32060 -32.64868 -0.02313  1.000 30.05290 ? 286 LEU   A CG  1 
ATOM   2204 C  CD1 . LEU   A 1 286 ? -23.31425 -31.51774 -0.23086  1.000 33.05053 ? 286 LEU   A CD1 1 
ATOM   2205 C  CD2 . LEU   A 1 286 ? -21.23748 -32.58209 -1.06209  1.000 28.50231 ? 286 LEU   A CD2 1 
ATOM   2206 N  N   . LEU   A 1 287 ? -20.62693 -32.62295 4.22963   1.000 26.73089 ? 287 LEU   A N   1 
ATOM   2207 C  CA  . LEU   A 1 287 ? -19.97879 -31.86293 5.28943   1.000 23.48923 ? 287 LEU   A CA  1 
ATOM   2208 C  C   . LEU   A 1 287 ? -19.50761 -30.53082 4.72279   1.000 21.02652 ? 287 LEU   A C   1 
ATOM   2209 O  O   . LEU   A 1 287 ? -18.66505 -30.49416 3.82297   1.000 20.78962 ? 287 LEU   A O   1 
ATOM   2210 C  CB  . LEU   A 1 287 ? -18.81818 -32.66723 5.87974   1.000 22.66002 ? 287 LEU   A CB  1 
ATOM   2211 C  CG  . LEU   A 1 287 ? -19.30294 -34.02363 6.40552   1.000 25.24831 ? 287 LEU   A CG  1 
ATOM   2212 C  CD1 . LEU   A 1 287 ? -18.15324 -34.94461 6.80911   1.000 28.89444 ? 287 LEU   A CD1 1 
ATOM   2213 C  CD2 . LEU   A 1 287 ? -20.26485 -33.81226 7.57091   1.000 25.98978 ? 287 LEU   A CD2 1 
ATOM   2214 N  N   . GLU   A 1 288 ? -20.04217 -29.43919 5.25697   1.000 18.35088 ? 288 GLU   A N   1 
ATOM   2215 C  CA  . GLU   A 1 288 ? -19.83496 -28.11415 4.70119   1.000 19.31219 ? 288 GLU   A CA  1 
ATOM   2216 C  C   . GLU   A 1 288 ? -18.61736 -27.44524 5.33388   1.000 16.66348 ? 288 GLU   A C   1 
ATOM   2217 O  O   . GLU   A 1 288 ? -18.47271 -27.44014 6.55766   1.000 15.20355 ? 288 GLU   A O   1 
ATOM   2218 C  CB  . GLU   A 1 288 ? -21.09166 -27.27581 4.91519   1.000 21.30538 ? 288 GLU   A CB  1 
ATOM   2219 C  CG  . GLU   A 1 288 ? -20.82347 -25.83308 4.79215   1.000 21.06044 ? 288 GLU   A CG  1 
ATOM   2220 C  CD  . GLU   A 1 288 ? -20.93263 -25.42274 3.32602   1.000 24.53131 ? 288 GLU   A CD  1 
ATOM   2221 O  OE1 . GLU   A 1 288 ? -21.82259 -25.95639 2.61932   1.000 26.77986 ? 288 GLU   A OE1 1 
ATOM   2222 O  OE2 . GLU   A 1 288 ? -20.05833 -24.67607 2.84981   1.000 20.06775 ? 288 GLU   A OE2 1 
ATOM   2223 N  N   . ASP   A 1 289 ? -17.71719 -26.88583 4.50998   1.000 16.33187 ? 289 ASP   A N   1 
ATOM   2224 C  CA  . ASP   A 1 289 ? -16.49369 -26.34583 5.09158   1.000 17.27190 ? 289 ASP   A CA  1 
ATOM   2225 C  C   . ASP   A 1 289 ? -16.26395 -24.85977 4.80424   1.000 16.71011 ? 289 ASP   A C   1 
ATOM   2226 O  O   . ASP   A 1 289 ? -15.13097 -24.38740 4.95845   1.000 13.68709 ? 289 ASP   A O   1 
ATOM   2227 C  CB  . ASP   A 1 289 ? -15.28407 -27.18072 4.64543   1.000 14.77667 ? 289 ASP   A CB  1 
ATOM   2228 C  CG  . ASP   A 1 289 ? -14.80249 -26.85805 3.22741   1.000 18.02690 ? 289 ASP   A CG  1 
ATOM   2229 O  OD1 . ASP   A 1 289 ? -15.56867 -26.30742 2.39882   1.000 16.38168 ? 289 ASP   A OD1 1 
ATOM   2230 O  OD2 . ASP   A 1 289 ? -13.61432 -27.19401 2.96220   1.000 14.79545 ? 289 ASP   A OD2 1 
ATOM   2231 N  N   . GLU   A 1 290 ? -17.30078 -24.10339 4.41897   1.000 14.41304 ? 290 GLU   A N   1 
ATOM   2232 C  CA  . GLU   A 1 290 ? -17.12087 -22.70279 4.06266   1.000 14.00963 ? 290 GLU   A CA  1 
ATOM   2233 C  C   . GLU   A 1 290 ? -17.75345 -21.75012 5.07817   1.000 15.73487 ? 290 GLU   A C   1 
ATOM   2234 O  O   . GLU   A 1 290 ? -18.04818 -20.60164 4.75060   1.000 18.28744 ? 290 GLU   A O   1 
ATOM   2235 C  CB  . GLU   A 1 290 ? -17.61307 -22.45497 2.62967   1.000 19.65746 ? 290 GLU   A CB  1 
ATOM   2236 C  CG  . GLU   A 1 290 ? -16.62160 -23.08654 1.58483   1.000 17.92973 ? 290 GLU   A CG  1 
ATOM   2237 C  CD  . GLU   A 1 290 ? -16.50794 -22.36588 0.23077   1.000 19.90920 ? 290 GLU   A CD  1 
ATOM   2238 O  OE1 . GLU   A 1 290 ? -17.28824 -21.40631 -0.03353  1.000 18.43084 ? 290 GLU   A OE1 1 
ATOM   2239 O  OE2 . GLU   A 1 290 ? -15.65340 -22.81439 -0.59891  1.000 18.86436 ? 290 GLU   A OE2 1 
ATOM   2240 N  N   . PHE   A 1 291 ? -17.91918 -22.18796 6.33492   1.000 16.01308 ? 291 PHE   A N   1 
ATOM   2241 C  CA  . PHE   A 1 291 ? -18.17878 -21.27933 7.45326   1.000 15.03297 ? 291 PHE   A CA  1 
ATOM   2242 C  C   . PHE   A 1 291 ? -17.07852 -21.38095 8.50359   1.000 13.36607 ? 291 PHE   A C   1 
ATOM   2243 O  O   . PHE   A 1 291 ? -16.78636 -22.47864 9.01178   1.000 11.88673 ? 291 PHE   A O   1 
ATOM   2244 C  CB  . PHE   A 1 291 ? -19.50994 -21.52932 8.19095   1.000 14.96154 ? 291 PHE   A CB  1 
ATOM   2245 C  CG  . PHE   A 1 291 ? -20.72811 -21.63580 7.32324   1.000 17.52728 ? 291 PHE   A CG  1 
ATOM   2246 C  CD1 . PHE   A 1 291 ? -21.12833 -22.84967 6.78185   1.000 16.88566 ? 291 PHE   A CD1 1 
ATOM   2247 C  CD2 . PHE   A 1 291 ? -21.48626 -20.50657 7.05791   1.000 21.13008 ? 291 PHE   A CD2 1 
ATOM   2248 C  CE1 . PHE   A 1 291 ? -22.28380 -22.93359 6.00578   1.000 21.51990 ? 291 PHE   A CE1 1 
ATOM   2249 C  CE2 . PHE   A 1 291 ? -22.64777 -20.58303 6.26042   1.000 20.19174 ? 291 PHE   A CE2 1 
ATOM   2250 C  CZ  . PHE   A 1 291 ? -23.03392 -21.79138 5.74344   1.000 20.00881 ? 291 PHE   A CZ  1 
ATOM   2251 N  N   . THR   A 1 292 ? -16.54888 -20.23424 8.91560   1.000 13.36152 ? 292 THR   A N   1 
ATOM   2252 C  CA  . THR   A 1 292 ? -15.50993 -20.21035 9.94211   1.000 16.36344 ? 292 THR   A CA  1 
ATOM   2253 C  C   . THR   A 1 292 ? -16.13878 -20.21299 11.33376  1.000 15.77591 ? 292 THR   A C   1 
ATOM   2254 O  O   . THR   A 1 292 ? -17.32973 -19.95697 11.50825  1.000 15.97725 ? 292 THR   A O   1 
ATOM   2255 C  CB  . THR   A 1 292 ? -14.62591 -18.97547 9.78456   1.000 15.87646 ? 292 THR   A CB  1 
ATOM   2256 O  OG1 . THR   A 1 292 ? -15.37156 -17.81195 10.15690  1.000 18.74390 ? 292 THR   A OG1 1 
ATOM   2257 C  CG2 . THR   A 1 292 ? -14.03695 -18.83323 8.37001   1.000 16.49468 ? 292 THR   A CG2 1 
ATOM   2258 N  N   . PRO   A 1 293 ? -15.34976 -20.49791 12.36429  1.000 18.81895 ? 293 PRO   A N   1 
ATOM   2259 C  CA  . PRO   A 1 293 ? -15.86338 -20.32687 13.73452  1.000 17.10653 ? 293 PRO   A CA  1 
ATOM   2260 C  C   . PRO   A 1 293 ? -16.40784 -18.92820 13.97361  1.000 18.99500 ? 293 PRO   A C   1 
ATOM   2261 O  O   . PRO   A 1 293 ? -17.44676 -18.77239 14.62435  1.000 20.00271 ? 293 PRO   A O   1 
ATOM   2262 C  CB  . PRO   A 1 293 ? -14.63109 -20.64525 14.59811  1.000 17.54841 ? 293 PRO   A CB  1 
ATOM   2263 C  CG  . PRO   A 1 293 ? -13.84164 -21.60292 13.75934  1.000 18.19915 ? 293 PRO   A CG  1 
ATOM   2264 C  CD  . PRO   A 1 293 ? -14.01093 -21.11362 12.34569  1.000 17.75886 ? 293 PRO   A CD  1 
ATOM   2265 N  N   . PHE   A 1 294 ? -15.74834 -17.90818 13.41026  1.000 18.94649 ? 294 PHE   A N   1 
ATOM   2266 C  CA  . PHE   A 1 294 ? -16.25374 -16.53582 13.47630  1.000 19.34785 ? 294 PHE   A CA  1 
ATOM   2267 C  C   . PHE   A 1 294 ? -17.64187 -16.42223 12.86010  1.000 19.98001 ? 294 PHE   A C   1 
ATOM   2268 O  O   . PHE   A 1 294 ? -18.54648 -15.81679 13.45606  1.000 20.27469 ? 294 PHE   A O   1 
ATOM   2269 C  CB  . PHE   A 1 294 ? -15.26553 -15.59906 12.76919  1.000 22.12596 ? 294 PHE   A CB  1 
ATOM   2270 C  CG  . PHE   A 1 294 ? -15.48332 -14.12762 13.05784  1.000 29.27327 ? 294 PHE   A CG  1 
ATOM   2271 C  CD1 . PHE   A 1 294 ? -16.57429 -13.45483 12.53187  1.000 30.42882 ? 294 PHE   A CD1 1 
ATOM   2272 C  CD2 . PHE   A 1 294 ? -14.59112 -13.42045 13.85360  1.000 32.56690 ? 294 PHE   A CD2 1 
ATOM   2273 C  CE1 . PHE   A 1 294 ? -16.77801 -12.10581 12.78704  1.000 31.33956 ? 294 PHE   A CE1 1 
ATOM   2274 C  CE2 . PHE   A 1 294 ? -14.78901 -12.07010 14.10581  1.000 33.85746 ? 294 PHE   A CE2 1 
ATOM   2275 C  CZ  . PHE   A 1 294 ? -15.89209 -11.41933 13.57164  1.000 36.52446 ? 294 PHE   A CZ  1 
ATOM   2276 N  N   . ASP   A 1 295 ? -17.81635 -16.98343 11.65295  1.000 17.08039 ? 295 ASP   A N   1 
ATOM   2277 C  CA  . ASP   A 1 295 ? -19.10110 -16.94488 10.95030  1.000 17.65620 ? 295 ASP   A CA  1 
ATOM   2278 C  C   . ASP   A 1 295 ? -20.21670 -17.57480 11.77768  1.000 20.51704 ? 295 ASP   A C   1 
ATOM   2279 O  O   . ASP   A 1 295 ? -21.34291 -17.06262 11.80371  1.000 19.34010 ? 295 ASP   A O   1 
ATOM   2280 C  CB  . ASP   A 1 295 ? -18.99249 -17.67395 9.61407   1.000 16.13712 ? 295 ASP   A CB  1 
ATOM   2281 C  CG  . ASP   A 1 295 ? -18.01226 -17.01331 8.67178   1.000 18.37052 ? 295 ASP   A CG  1 
ATOM   2282 O  OD1 . ASP   A 1 295 ? -17.68958 -15.83247 8.91967   1.000 19.14246 ? 295 ASP   A OD1 1 
ATOM   2283 O  OD2 . ASP   A 1 295 ? -17.54997 -17.67495 7.71313   1.000 18.51199 ? 295 ASP   A OD2 1 
ATOM   2284 N  N   . VAL   A 1 296 ? -19.93310 -18.70364 12.43378  1.000 16.57122 ? 296 VAL   A N   1 
ATOM   2285 C  CA  . VAL   A 1 296 ? -20.96693 -19.39188 13.20576  1.000 19.59816 ? 296 VAL   A CA  1 
ATOM   2286 C  C   . VAL   A 1 296 ? -21.37629 -18.55195 14.40727  1.000 20.14680 ? 296 VAL   A C   1 
ATOM   2287 O  O   . VAL   A 1 296 ? -22.56566 -18.38175 14.69205  1.000 21.78016 ? 296 VAL   A O   1 
ATOM   2288 C  CB  . VAL   A 1 296 ? -20.48632 -20.78890 13.63715  1.000 17.88264 ? 296 VAL   A CB  1 
ATOM   2289 C  CG1 . VAL   A 1 296 ? -21.49028 -21.40021 14.58980  1.000 20.66845 ? 296 VAL   A CG1 1 
ATOM   2290 C  CG2 . VAL   A 1 296 ? -20.29452 -21.69075 12.42124  1.000 16.62818 ? 296 VAL   A CG2 1 
ATOM   2291 N  N   . VAL   A 1 297 ? -20.39107 -18.01092 15.12256  1.000 22.08592 ? 297 VAL   A N   1 
ATOM   2292 C  CA  . VAL   A 1 297 ? -20.67225 -17.16937 16.28098  1.000 23.98305 ? 297 VAL   A CA  1 
ATOM   2293 C  C   . VAL   A 1 297 ? -21.45646 -15.92889 15.86246  1.000 24.41849 ? 297 VAL   A C   1 
ATOM   2294 O  O   . VAL   A 1 297 ? -22.41777 -15.53687 16.52904  1.000 27.76361 ? 297 VAL   A O   1 
ATOM   2295 C  CB  . VAL   A 1 297 ? -19.35938 -16.79206 16.99384  1.000 22.01071 ? 297 VAL   A CB  1 
ATOM   2296 C  CG1 . VAL   A 1 297 ? -19.64141 -15.79208 18.09212  1.000 25.55292 ? 297 VAL   A CG1 1 
ATOM   2297 C  CG2 . VAL   A 1 297 ? -18.66788 -18.02549 17.56659  1.000 25.82464 ? 297 VAL   A CG2 1 
ATOM   2298 N  N   . ARG   A 1 298 ? -21.05574 -15.28860 14.75694  1.000 23.40638 ? 298 ARG   A N   1 
ATOM   2299 C  CA  . ARG   A 1 298 ? -21.78080 -14.11709 14.27190  1.000 27.29811 ? 298 ARG   A CA  1 
ATOM   2300 C  C   . ARG   A 1 298 ? -23.24246 -14.44411 13.99264  1.000 28.33994 ? 298 ARG   A C   1 
ATOM   2301 O  O   . ARG   A 1 298 ? -24.13492 -13.68991 14.38970  1.000 33.02857 ? 298 ARG   A O   1 
ATOM   2302 C  CB  . ARG   A 1 298 ? -21.12733 -13.53944 13.00331  1.000 27.92863 ? 298 ARG   A CB  1 
ATOM   2303 C  CG  . ARG   A 1 298 ? -22.16872 -12.83941 12.06865  1.000 31.54440 ? 298 ARG   A CG  1 
ATOM   2304 C  CD  . ARG   A 1 298 ? -21.59268 -11.97727 10.91660  1.000 34.23747 ? 298 ARG   A CD  1 
ATOM   2305 N  NE  . ARG   A 1 298 ? -21.23725 -12.71883 9.70774   1.000 32.63698 ? 298 ARG   A NE  1 
ATOM   2306 C  CZ  . ARG   A 1 298 ? -21.61438 -12.38484 8.47686   1.000 25.41006 ? 298 ARG   A CZ  1 
ATOM   2307 N  NH1 . ARG   A 1 298 ? -22.40962 -11.34631 8.24940   1.000 27.12879 ? 298 ARG   A NH1 1 
ATOM   2308 N  NH2 . ARG   A 1 298 ? -21.16607 -13.09568 7.44708   1.000 24.75716 ? 298 ARG   A NH2 1 
ATOM   2309 N  N   . GLN   A 1 299 ? -23.51503 -15.56692 13.32401  1.000 26.43461 ? 299 GLN   A N   1 
ATOM   2310 C  CA  . GLN   A 1 299 ? -24.88153 -15.84710 12.89266  1.000 26.10869 ? 299 GLN   A CA  1 
ATOM   2311 C  C   . GLN   A 1 299 ? -25.72542 -16.43746 14.00900  1.000 30.21367 ? 299 GLN   A C   1 
ATOM   2312 O  O   . GLN   A 1 299 ? -26.92319 -16.14351 14.10094  1.000 30.16994 ? 299 GLN   A O   1 
ATOM   2313 C  CB  . GLN   A 1 299 ? -24.87537 -16.78750 11.69027  1.000 25.09765 ? 299 GLN   A CB  1 
ATOM   2314 C  CG  . GLN   A 1 299 ? -26.18992 -16.82354 10.96188  1.000 22.98963 ? 299 GLN   A CG  1 
ATOM   2315 C  CD  . GLN   A 1 299 ? -26.08139 -17.51250 9.62958   1.000 21.08716 ? 299 GLN   A CD  1 
ATOM   2316 O  OE1 . GLN   A 1 299 ? -27.04860 -18.03462 9.08758   1.000 21.39455 ? 299 GLN   A OE1 1 
ATOM   2317 N  NE2 . GLN   A 1 299 ? -24.86017 -17.57257 9.11566   1.000 18.63126 ? 299 GLN   A NE2 1 
ATOM   2318 N  N   . CYS   A 1 300 ? -25.14101 -17.28704 14.84517  1.000 27.62790 ? 300 CYS   A N   1 
ATOM   2319 C  CA  . CYS   A 1 300 ? -25.90679 -17.90585 15.91346  1.000 29.98874 ? 300 CYS   A CA  1 
ATOM   2320 C  C   . CYS   A 1 300 ? -26.00343 -17.03539 17.16419  1.000 35.08261 ? 300 CYS   A C   1 
ATOM   2321 O  O   . CYS   A 1 300 ? -26.75045 -17.39343 18.08387  1.000 38.92450 ? 300 CYS   A O   1 
ATOM   2322 C  CB  . CYS   A 1 300 ? -25.33058 -19.29403 16.23648  1.000 28.78721 ? 300 CYS   A CB  1 
ATOM   2323 S  SG  . CYS   A 1 300 ? -25.28130 -20.45755 14.80264  1.000 28.26660 ? 300 CYS   A SG  1 
ATOM   2324 N  N   . SER   A 1 301 ? -25.32189 -15.88164 17.19188  1.000 36.88146 ? 301 SER   A N   1 
ATOM   2325 C  CA  . SER   A 1 301 ? -25.40213 -14.91560 18.28739  1.000 40.64671 ? 301 SER   A CA  1 
ATOM   2326 C  C   . SER   A 1 301 ? -25.98840 -13.57837 17.85094  1.000 41.71707 ? 301 SER   A C   1 
ATOM   2327 O  O   . SER   A 1 301 ? -26.82271 -13.01231 18.57277  1.000 41.04113 ? 301 SER   A O   1 
ATOM   2328 C  CB  . SER   A 1 301 ? -24.01286 -14.70329 18.92378  1.000 42.34084 ? 301 SER   A CB  1 
ATOM   2329 O  OG  . SER   A 1 301 ? -23.97619 -13.52845 19.72306  1.000 49.14906 ? 301 SER   A OG  1 
ATOM   2330 N  N   . GLY   A 1 302 ? -25.56701 -13.03868 16.69970  1.000 41.46126 ? 302 GLY   A N   1 
ATOM   2331 C  CA  . GLY   A 1 302 ? -26.31173 -11.96616 16.04569  1.000 44.57470 ? 302 GLY   A CA  1 
ATOM   2332 C  C   . GLY   A 1 302 ? -25.69027 -10.58327 15.96652  1.000 45.85589 ? 302 GLY   A C   1 
ATOM   2333 O  O   . GLY   A 1 302 ? -26.34670 -9.58343  16.28708  1.000 47.63521 ? 302 GLY   A O   1 
ATOM   2334 N  N   . VAL   A 1 303 ? -24.44885 -10.50639 15.50606  1.000 47.65349 ? 303 VAL   A N   1 
ATOM   2335 C  CA  . VAL   A 1 303 ? -23.71779 -9.24275  15.47161  1.000 50.40394 ? 303 VAL   A CA  1 
ATOM   2336 C  C   . VAL   A 1 303 ? -24.09900 -8.46985  14.21317  1.000 48.96413 ? 303 VAL   A C   1 
ATOM   2337 O  O   . VAL   A 1 303 ? -24.32162 -9.06186  13.14791  1.000 47.64293 ? 303 VAL   A O   1 
ATOM   2338 C  CB  . VAL   A 1 303 ? -22.20050 -9.50760  15.54939  1.000 47.19975 ? 303 VAL   A CB  1 
ATOM   2339 C  CG1 . VAL   A 1 303 ? -21.39985 -8.21951  15.35494  1.000 51.35323 ? 303 VAL   A CG1 1 
ATOM   2340 C  CG2 . VAL   A 1 303 ? -21.84886 -10.17203 16.87879  1.000 47.63681 ? 303 VAL   A CG2 1 
ATOM   2341 N  N   . THR   A 1 304 ? -24.18669 -7.14153  14.33412  1.000 48.46621 ? 304 THR   A N   1 
ATOM   2342 C  CA  . THR   A 1 304 ? -24.52757 -6.24502  13.23078  1.000 46.01273 ? 304 THR   A CA  1 
ATOM   2343 C  C   . THR   A 1 304 ? -23.32828 -5.36281  12.89507  1.000 51.04695 ? 304 THR   A C   1 
ATOM   2344 O  O   . THR   A 1 304 ? -22.25636 -5.47136  13.49976  1.000 52.72977 ? 304 THR   A O   1 
ATOM   2345 C  CB  . THR   A 1 304 ? -25.73715 -5.36652  13.57225  1.000 41.39821 ? 304 THR   A CB  1 
ATOM   2346 O  OG1 . THR   A 1 304 ? -25.53208 -4.74089  14.84590  1.000 48.25481 ? 304 THR   A OG1 1 
ATOM   2347 C  CG2 . THR   A 1 304 ? -27.00701 -6.20354  13.64802  1.000 33.40640 ? 304 THR   A CG2 1 
ATOM   2348 N  N   . PHE   A 1 305 ? -23.52481 -4.46837  11.92405  1.000 50.80183 ? 305 PHE   A N   1 
ATOM   2349 C  CA  . PHE   A 1 305 ? -22.45792 -3.59389  11.44135  1.000 54.66901 ? 305 PHE   A CA  1 
ATOM   2350 C  C   . PHE   A 1 305 ? -23.05137 -2.23753  11.07169  1.000 53.53656 ? 305 PHE   A C   1 
ATOM   2351 O  O   . PHE   A 1 305 ? -24.13783 -2.17119  10.48531  1.000 54.21061 ? 305 PHE   A O   1 
ATOM   2352 C  CB  . PHE   A 1 305 ? -21.73037 -4.23938  10.24380  1.000 50.14389 ? 305 PHE   A CB  1 
ATOM   2353 C  CG  . PHE   A 1 305 ? -21.41169 -5.70108  10.45856  1.000 48.76272 ? 305 PHE   A CG  1 
ATOM   2354 C  CD1 . PHE   A 1 305 ? -20.26867 -6.08082  11.15575  1.000 46.51393 ? 305 PHE   A CD1 1 
ATOM   2355 C  CD2 . PHE   A 1 305 ? -22.29036 -6.69330  10.01945  1.000 46.58878 ? 305 PHE   A CD2 1 
ATOM   2356 C  CE1 . PHE   A 1 305 ? -19.98926 -7.42026  11.38422  1.000 47.99142 ? 305 PHE   A CE1 1 
ATOM   2357 C  CE2 . PHE   A 1 305 ? -22.02397 -8.03851  10.25003  1.000 45.70264 ? 305 PHE   A CE2 1 
ATOM   2358 C  CZ  . PHE   A 1 305 ? -20.87487 -8.40213  10.93764  1.000 47.21198 ? 305 PHE   A CZ  1 
ATOM   2359 N  N   . GLN   A 1 306 ? -22.35132 -1.16208  11.43072  1.000 53.39822 ? 306 GLN   A N   1 
ATOM   2360 C  CA  . GLN   A 1 306 ? -22.83919 0.18133   11.13704  1.000 53.57463 ? 306 GLN   A CA  1 
ATOM   2361 C  C   . GLN   A 1 306 ? -21.71577 1.07963   10.64556  1.000 49.45954 ? 306 GLN   A C   1 
ATOM   2362 O  O   . GLN   A 1 306 ? -21.31381 0.99898   9.48601   1.000 45.63992 ? 306 GLN   A O   1 
ATOM   2363 C  CB  . GLN   A 1 306 ? -23.49983 0.78579   12.37284  1.000 53.88156 ? 306 GLN   A CB  1 
ATOM   2364 C  CG  . GLN   A 1 306 ? -24.96832 0.40624   12.47545  1.000 53.61971 ? 306 GLN   A CG  1 
ATOM   2365 C  CD  . GLN   A 1 306 ? -25.90825 1.48775   11.97801  1.000 54.43500 ? 306 GLN   A CD  1 
ATOM   2366 O  OE1 . GLN   A 1 306 ? -26.75291 1.24099   11.10960  1.000 54.03214 ? 306 GLN   A OE1 1 
ATOM   2367 N  NE2 . GLN   A 1 306 ? -25.79256 2.68572   12.55037  1.000 54.15495 ? 306 GLN   A NE2 1 
HETATM 2368 N  N1  . A1ARW B 2 .   ? -12.72415 -12.33769 -16.98751 1.000 31.86090 ? 401 A1ARW A N1  1 
HETATM 2369 C  C4  . A1ARW B 2 .   ? -12.33200 -9.79200  -16.33800 1.000 29.04096 ? 401 A1ARW A C4  1 
HETATM 2370 C  C5  . A1ARW B 2 .   ? -10.34892 -12.97634 -17.66397 1.000 28.69127 ? 401 A1ARW A C5  1 
HETATM 2371 C  C6  . A1ARW B 2 .   ? -9.39847  -13.30571 -18.66745 1.000 33.25276 ? 401 A1ARW A C6  1 
HETATM 2372 C  C7  . A1ARW B 2 .   ? -9.79436  -13.32681 -20.00619 1.000 32.42223 ? 401 A1ARW A C7  1 
HETATM 2373 C  C8  . A1ARW B 2 .   ? -11.11155 -13.03118 -20.33427 1.000 34.84878 ? 401 A1ARW A C8  1 
HETATM 2374 C  C10 . A1ARW B 2 .   ? -7.98475  -13.62701 -18.31841 1.000 31.19819 ? 401 A1ARW A C10 1 
HETATM 2375 C  C13 . A1ARW B 2 .   ? -5.33027  -14.13305 -17.50974 1.000 30.84819 ? 401 A1ARW A C13 1 
HETATM 2376 C  C15 . A1ARW B 2 .   ? -7.16745  -14.51270 -19.03730 1.000 34.75583 ? 401 A1ARW A C15 1 
HETATM 2377 C  C17 . A1ARW B 2 .   ? -14.95252 -15.39875 -16.77396 1.000 28.35511 ? 401 A1ARW A C17 1 
HETATM 2378 C  C20 . A1ARW B 2 .   ? -10.90300 -9.84100  -16.45200 1.000 29.64235 ? 401 A1ARW A C20 1 
HETATM 2379 C  C1  . A1ARW B 2 .   ? -13.56006 -13.47162 -16.58582 1.000 26.21927 ? 401 A1ARW A C1  1 
HETATM 2380 C  C11 . A1ARW B 2 .   ? -7.44664  -13.00559 -17.20302 1.000 29.13319 ? 401 A1ARW A C11 1 
HETATM 2381 C  C12 . A1ARW B 2 .   ? -6.15986  -13.26463 -16.81492 1.000 28.75613 ? 401 A1ARW A C12 1 
HETATM 2382 C  C14 . A1ARW B 2 .   ? -5.85071  -14.75982 -18.63501 1.000 34.40314 ? 401 A1ARW A C14 1 
HETATM 2383 C  C16 . A1ARW B 2 .   ? -14.23644 -14.37618 -17.40950 1.000 29.60778 ? 401 A1ARW A C16 1 
HETATM 2384 C  C18 . A1ARW B 2 .   ? -14.97740 -15.51218 -15.40781 1.000 25.29215 ? 401 A1ARW A C18 1 
HETATM 2385 C  C19 . A1ARW B 2 .   ? -13.62667 -13.72363 -15.20920 1.000 26.02965 ? 401 A1ARW A C19 1 
HETATM 2386 C  C2  . A1ARW B 2 .   ? -11.67818 -12.66062 -17.98785 1.000 31.38605 ? 401 A1ARW A C2  1 
HETATM 2387 C  C3  . A1ARW B 2 .   ? -13.03270 -11.12556 -16.27416 1.000 30.26511 ? 401 A1ARW A C3  1 
HETATM 2388 C  C9  . A1ARW B 2 .   ? -12.03376 -12.70463 -19.34247 1.000 33.44595 ? 401 A1ARW A C9  1 
HETATM 2389 N  N2  . A1ARW B 2 .   ? -14.31911 -14.68976 -14.60907 1.000 20.64682 ? 401 A1ARW A N2  1 
HETATM 2390 O  O1  . A1ARW B 2 .   ? -13.96188 -11.09242 -15.47685 1.000 33.43620 ? 401 A1ARW A O1  1 
HETATM 2391 CL CL1 . A1ARW B 2 .   ? -5.62967  -12.41935 -15.40311 1.000 36.92336 ? 401 A1ARW A CL1 1 
HETATM 2392 CL CL2 . A1ARW B 2 .   ? -15.86254 -16.59668 -17.63334 1.000 34.90953 ? 401 A1ARW A CL2 1 
HETATM 2393 O  O   . HOH   C 3 .   ? -4.386    -18.487   16.251    1.000 38.96759 ? 501 HOH   A O   1 
HETATM 2394 O  O   . HOH   C 3 .   ? -14.19210 -15.30335 -20.83837 1.000 35.67405 ? 502 HOH   A O   1 
HETATM 2395 O  O   . HOH   C 3 .   ? -26.05331 -18.55463 19.65533  1.000 36.91672 ? 503 HOH   A O   1 
HETATM 2396 O  O   . HOH   C 3 .   ? -3.56657  -24.03532 -6.56840  1.000 21.71503 ? 504 HOH   A O   1 
HETATM 2397 O  O   . HOH   C 3 .   ? -24.52553 -2.35713  8.28601   1.000 43.34463 ? 505 HOH   A O   1 
HETATM 2398 O  O   . HOH   C 3 .   ? -19.11522 -13.92335 7.94914   1.000 44.22918 ? 506 HOH   A O   1 
HETATM 2399 O  O   . HOH   C 3 .   ? -27.386   -17.811   1.965     1.000 32.75056 ? 507 HOH   A O   1 
HETATM 2400 O  O   . HOH   C 3 .   ? 5.30260   -5.92671  -13.70902 1.000 28.77083 ? 508 HOH   A O   1 
HETATM 2401 O  O   . HOH   C 3 .   ? -16.69394 -16.45938 -21.66911 1.000 35.92163 ? 509 HOH   A O   1 
HETATM 2402 O  O   . HOH   C 3 .   ? -7.37367  13.99912  -6.92432  1.000 29.50450 ? 510 HOH   A O   1 
HETATM 2403 O  O   . HOH   C 3 .   ? -7.90456  -18.35665 -25.41249 1.000 49.89023 ? 511 HOH   A O   1 
HETATM 2404 O  O   . HOH   C 3 .   ? -16.18340 -34.35012 3.65012   1.000 27.15181 ? 512 HOH   A O   1 
HETATM 2405 O  O   . HOH   C 3 .   ? -3.33802  -21.20787 20.24541  1.000 33.88339 ? 513 HOH   A O   1 
HETATM 2406 O  O   . HOH   C 3 .   ? 1.76822   -16.32375 -21.31479 1.000 41.05902 ? 514 HOH   A O   1 
HETATM 2407 O  O   . HOH   C 3 .   ? -7.48686  -23.71329 5.39207   1.000 21.67491 ? 515 HOH   A O   1 
HETATM 2408 O  O   . HOH   C 3 .   ? -12.97539 9.10146   -17.89150 1.000 34.19790 ? 516 HOH   A O   1 
HETATM 2409 O  O   . HOH   C 3 .   ? -12.96452 -4.61269  8.53045   1.000 22.92284 ? 517 HOH   A O   1 
HETATM 2410 O  O   . HOH   C 3 .   ? -5.75196  2.86874   -25.97916 1.000 38.12514 ? 518 HOH   A O   1 
HETATM 2411 O  O   . HOH   C 3 .   ? -7.33108  -25.16020 8.21339   1.000 30.96599 ? 519 HOH   A O   1 
HETATM 2412 O  O   . HOH   C 3 .   ? -27.24585 -4.26513  16.55630  1.000 32.34289 ? 520 HOH   A O   1 
HETATM 2413 O  O   . HOH   C 3 .   ? -22.33904 -16.19196 -12.54732 1.000 25.31947 ? 521 HOH   A O   1 
HETATM 2414 O  O   . HOH   C 3 .   ? -14.94597 -32.50937 1.71585   1.000 28.75883 ? 522 HOH   A O   1 
HETATM 2415 O  O   . HOH   C 3 .   ? -1.99906  -34.33628 15.19908  1.000 37.52777 ? 523 HOH   A O   1 
HETATM 2416 O  O   . HOH   C 3 .   ? 0.30384   1.43559   -2.55220  1.000 35.53855 ? 524 HOH   A O   1 
HETATM 2417 O  O   . HOH   C 3 .   ? -18.43371 -33.42475 25.41021  1.000 31.28993 ? 525 HOH   A O   1 
HETATM 2418 O  O   . HOH   C 3 .   ? -19.42334 -20.21812 0.66557   1.000 20.74169 ? 526 HOH   A O   1 
HETATM 2419 O  O   . HOH   C 3 .   ? -15.52493 -20.90583 18.66871  1.000 25.86276 ? 527 HOH   A O   1 
HETATM 2420 O  O   . HOH   C 3 .   ? -16.89458 -13.52419 6.17271   1.000 17.75474 ? 528 HOH   A O   1 
HETATM 2421 O  O   . HOH   C 3 .   ? -1.66160  -16.70162 -2.05229  1.000 32.45240 ? 529 HOH   A O   1 
HETATM 2422 O  O   . HOH   C 3 .   ? -2.48175  -27.53427 -4.18343  1.000 28.49212 ? 530 HOH   A O   1 
HETATM 2423 O  O   . HOH   C 3 .   ? -17.66328 3.44023   6.94492   1.000 27.05950 ? 531 HOH   A O   1 
HETATM 2424 O  O   . HOH   C 3 .   ? -21.92500 -13.02739 -11.28867 1.000 22.82543 ? 532 HOH   A O   1 
HETATM 2425 O  O   . HOH   C 3 .   ? -15.88004 3.05556   -18.81921 1.000 30.51644 ? 533 HOH   A O   1 
HETATM 2426 O  O   . HOH   C 3 .   ? -11.06603 -21.09029 9.17972   1.000 15.53897 ? 534 HOH   A O   1 
HETATM 2427 O  O   . HOH   C 3 .   ? -10.30048 -20.47459 -17.96880 1.000 34.14898 ? 535 HOH   A O   1 
HETATM 2428 O  O   . HOH   C 3 .   ? -19.99404 -36.42052 19.81264  1.000 32.80965 ? 536 HOH   A O   1 
HETATM 2429 O  O   . HOH   C 3 .   ? -29.84741 -18.94686 13.84165  1.000 31.91495 ? 537 HOH   A O   1 
HETATM 2430 O  O   . HOH   C 3 .   ? -20.97472 -39.15150 13.98495  1.000 30.86136 ? 538 HOH   A O   1 
HETATM 2431 O  O   . HOH   C 3 .   ? -20.93262 -11.79375 -19.38592 1.000 30.51905 ? 539 HOH   A O   1 
HETATM 2432 O  O   . HOH   C 3 .   ? -17.40050 -5.55551  -6.58438  1.000 14.59515 ? 540 HOH   A O   1 
HETATM 2433 O  O   . HOH   C 3 .   ? -7.80921  -19.78447 7.75157   1.000 23.13757 ? 541 HOH   A O   1 
HETATM 2434 O  O   . HOH   C 3 .   ? -1.91642  -24.43955 -9.00795  1.000 25.82454 ? 542 HOH   A O   1 
HETATM 2435 O  O   . HOH   C 3 .   ? -12.71349 -36.90654 1.50349   1.000 34.44043 ? 543 HOH   A O   1 
HETATM 2436 O  O   . HOH   C 3 .   ? -2.48280  -4.97394  2.36842   1.000 15.90070 ? 544 HOH   A O   1 
HETATM 2437 O  O   . HOH   C 3 .   ? -0.00000  -8.13529  0.00000   0.50  10.88113 ? 545 HOH   A O   1 
HETATM 2438 O  O   . HOH   C 3 .   ? -1.96772  -2.27414  -24.98402 1.000 51.30825 ? 546 HOH   A O   1 
HETATM 2439 O  O   . HOH   C 3 .   ? 1.08884   -23.44926 -19.59419 1.000 42.76514 ? 547 HOH   A O   1 
HETATM 2440 O  O   . HOH   C 3 .   ? -11.14271 -33.09935 0.77210   1.000 31.67425 ? 548 HOH   A O   1 
HETATM 2441 O  O   . HOH   C 3 .   ? -5.47081  -21.94893 -17.65181 1.000 29.37087 ? 549 HOH   A O   1 
HETATM 2442 O  O   . HOH   C 3 .   ? -25.88447 -0.77699  -6.37039  1.000 25.62998 ? 550 HOH   A O   1 
HETATM 2443 O  O   . HOH   C 3 .   ? -23.03580 -28.17190 1.81326   1.000 28.68261 ? 551 HOH   A O   1 
HETATM 2444 O  O   . HOH   C 3 .   ? -18.21648 -24.93573 7.40144   1.000 14.16203 ? 552 HOH   A O   1 
HETATM 2445 O  O   . HOH   C 3 .   ? 1.16167   -20.45736 -15.47884 1.000 29.42101 ? 553 HOH   A O   1 
HETATM 2446 O  O   . HOH   C 3 .   ? -25.49066 -22.83837 26.12770  1.000 37.33684 ? 554 HOH   A O   1 
HETATM 2447 O  O   . HOH   C 3 .   ? -1.63761  6.30900   -9.78438  1.000 28.00517 ? 555 HOH   A O   1 
HETATM 2448 O  O   . HOH   C 3 .   ? -1.94358  -24.13206 -1.38494  1.000 24.81049 ? 556 HOH   A O   1 
HETATM 2449 O  O   . HOH   C 3 .   ? -11.25694 -26.76186 -4.98882  1.000 24.65322 ? 557 HOH   A O   1 
HETATM 2450 O  O   . HOH   C 3 .   ? -24.01070 -43.45714 4.96057   1.000 44.70735 ? 558 HOH   A O   1 
HETATM 2451 O  O   . HOH   C 3 .   ? -8.59786  -25.24059 24.26320  1.000 33.84442 ? 559 HOH   A O   1 
HETATM 2452 O  O   . HOH   C 3 .   ? 1.15840   -12.19585 -12.81182 1.000 19.23084 ? 560 HOH   A O   1 
HETATM 2453 O  O   . HOH   C 3 .   ? -31.33654 -30.57960 7.79461   1.000 26.95788 ? 561 HOH   A O   1 
HETATM 2454 O  O   . HOH   C 3 .   ? -30.01503 -24.28496 6.88525   1.000 37.34948 ? 562 HOH   A O   1 
HETATM 2455 O  O   . HOH   C 3 .   ? 1.21856   8.44913   -19.84140 1.000 34.37077 ? 563 HOH   A O   1 
HETATM 2456 O  O   . HOH   C 3 .   ? -6.50530  -16.73341 -6.60936  1.000 10.99891 ? 564 HOH   A O   1 
HETATM 2457 O  O   . HOH   C 3 .   ? -28.54946 1.86080   13.04608  1.000 38.70065 ? 565 HOH   A O   1 
HETATM 2458 O  O   . HOH   C 3 .   ? -17.76439 -5.16565  -17.05262 1.000 25.78114 ? 566 HOH   A O   1 
HETATM 2459 O  O   . HOH   C 3 .   ? -28.74284 -29.34100 20.61358  1.000 27.78385 ? 567 HOH   A O   1 
HETATM 2460 O  O   . HOH   C 3 .   ? -28.87117 -18.54665 19.37341  1.000 37.82352 ? 568 HOH   A O   1 
HETATM 2461 O  O   . HOH   C 3 .   ? -20.22374 3.51405   -0.34972  1.000 20.70062 ? 569 HOH   A O   1 
HETATM 2462 O  O   . HOH   C 3 .   ? -4.05979  -33.65624 6.94599   1.000 33.34709 ? 570 HOH   A O   1 
HETATM 2463 O  O   . HOH   C 3 .   ? -24.48717 -26.05443 3.27507   1.000 28.30254 ? 571 HOH   A O   1 
HETATM 2464 O  O   . HOH   C 3 .   ? -2.64981  -35.76397 20.71501  1.000 37.77409 ? 572 HOH   A O   1 
HETATM 2465 O  O   . HOH   C 3 .   ? 5.32268   1.64627   -17.82689 1.000 31.52876 ? 573 HOH   A O   1 
HETATM 2466 O  O   . HOH   C 3 .   ? -15.44324 -46.66145 5.49572   1.000 38.47587 ? 574 HOH   A O   1 
HETATM 2467 O  O   . HOH   C 3 .   ? -28.78072 -2.04925  -3.58448  1.000 17.24108 ? 575 HOH   A O   1 
HETATM 2468 O  O   . HOH   C 3 .   ? -14.99986 -15.24898 9.09456   1.000 19.96098 ? 576 HOH   A O   1 
HETATM 2469 O  O   . HOH   C 3 .   ? 2.23106   5.79912   -19.52085 1.000 31.64953 ? 577 HOH   A O   1 
HETATM 2470 O  O   . HOH   C 3 .   ? -12.21641 -28.90488 -2.16610  1.000 22.01626 ? 578 HOH   A O   1 
HETATM 2471 O  O   . HOH   C 3 .   ? -1.18258  -19.23500 4.06721   1.000 17.11827 ? 579 HOH   A O   1 
HETATM 2472 O  O   . HOH   C 3 .   ? -16.50343 -21.80233 -9.14221  1.000 16.89555 ? 580 HOH   A O   1 
HETATM 2473 O  O   . HOH   C 3 .   ? 3.40987   -10.80484 -17.91044 1.000 33.12580 ? 581 HOH   A O   1 
HETATM 2474 O  O   . HOH   C 3 .   ? 3.75332   -4.50651  -11.78683 1.000 22.03108 ? 582 HOH   A O   1 
HETATM 2475 O  O   . HOH   C 3 .   ? -3.10898  -0.75270  -3.44782  1.000 24.57898 ? 583 HOH   A O   1 
HETATM 2476 O  O   . HOH   C 3 .   ? -14.87289 -20.86205 -2.44301  1.000 16.20477 ? 584 HOH   A O   1 
HETATM 2477 O  O   . HOH   C 3 .   ? 4.624     -3.177    -6.531    1.000 22.94971 ? 585 HOH   A O   1 
HETATM 2478 O  O   . HOH   C 3 .   ? -0.01973  -0.58437  -24.93171 1.000 31.92758 ? 586 HOH   A O   1 
HETATM 2479 O  O   . HOH   C 3 .   ? -20.92318 2.97755   -11.68804 1.000 29.46024 ? 587 HOH   A O   1 
HETATM 2480 O  O   . HOH   C 3 .   ? -18.22197 -26.33708 1.48401   1.000 23.80173 ? 588 HOH   A O   1 
HETATM 2481 O  O   . HOH   C 3 .   ? -19.46186 -21.82506 -7.50293  1.000 38.50502 ? 589 HOH   A O   1 
HETATM 2482 O  O   . HOH   C 3 .   ? 1.72649   -11.85353 -16.23997 1.000 26.27557 ? 590 HOH   A O   1 
HETATM 2483 O  O   . HOH   C 3 .   ? -3.53419  -23.20227 13.09206  1.000 27.37020 ? 591 HOH   A O   1 
HETATM 2484 O  O   . HOH   C 3 .   ? -13.86986 -7.56185  -19.33515 1.000 30.34417 ? 592 HOH   A O   1 
HETATM 2485 O  O   . HOH   C 3 .   ? -10.03018 -25.33651 -6.84270  1.000 19.06022 ? 593 HOH   A O   1 
HETATM 2486 O  O   . HOH   C 3 .   ? -6.16432  -6.49723  0.02528   1.000 14.55426 ? 594 HOH   A O   1 
HETATM 2487 O  O   . HOH   C 3 .   ? -0.73738  -24.68470 -13.05971 1.000 27.25322 ? 595 HOH   A O   1 
HETATM 2488 O  O   . HOH   C 3 .   ? -7.96077  -29.31780 -8.02834  1.000 28.13925 ? 596 HOH   A O   1 
HETATM 2489 O  O   . HOH   C 3 .   ? -10.82092 -15.89713 -17.29866 1.000 28.57468 ? 597 HOH   A O   1 
HETATM 2490 O  O   . HOH   C 3 .   ? -3.12448  -28.57684 -11.12669 1.000 31.87479 ? 598 HOH   A O   1 
HETATM 2491 O  O   . HOH   C 3 .   ? -24.61749 -12.25163 -11.54482 1.000 30.11599 ? 599 HOH   A O   1 
HETATM 2492 O  O   . HOH   C 3 .   ? -32.02677 -28.47398 2.32200   1.000 31.41879 ? 600 HOH   A O   1 
HETATM 2493 O  O   . HOH   C 3 .   ? -8.23261  -25.54551 -13.02647 1.000 23.33326 ? 601 HOH   A O   1 
HETATM 2494 O  O   . HOH   C 3 .   ? -9.57030  -6.66220  8.94383   1.000 21.21435 ? 602 HOH   A O   1 
HETATM 2495 O  O   . HOH   C 3 .   ? -22.30351 -1.77515  6.24336   1.000 29.99906 ? 603 HOH   A O   1 
HETATM 2496 O  O   . HOH   C 3 .   ? 4.87402   -8.26714  -8.19407  1.000 24.90806 ? 604 HOH   A O   1 
HETATM 2497 O  O   . HOH   C 3 .   ? 0.91963   -19.75805 -12.98697 1.000 26.05923 ? 605 HOH   A O   1 
HETATM 2498 O  O   . HOH   C 3 .   ? -3.60981  -34.55686 9.59930   1.000 34.10568 ? 606 HOH   A O   1 
HETATM 2499 O  O   . HOH   C 3 .   ? 4.07484   -7.01350  -24.50946 1.000 36.03604 ? 607 HOH   A O   1 
HETATM 2500 O  O   . HOH   C 3 .   ? -3.08157  -23.58838 2.05545   1.000 26.02687 ? 608 HOH   A O   1 
HETATM 2501 O  O   . HOH   C 3 .   ? -11.49485 -9.10110  4.49947   1.000 14.16275 ? 609 HOH   A O   1 
HETATM 2502 O  O   . HOH   C 3 .   ? 1.21048   -11.59143 -8.00361  1.000 13.81617 ? 610 HOH   A O   1 
HETATM 2503 O  O   . HOH   C 3 .   ? -17.50696 -5.71287  -19.95884 1.000 33.29839 ? 611 HOH   A O   1 
HETATM 2504 O  O   . HOH   C 3 .   ? -31.44501 -23.67609 9.24690   1.000 30.53527 ? 612 HOH   A O   1 
HETATM 2505 O  O   . HOH   C 3 .   ? -10.78087 -26.69605 -9.01881  1.000 21.71897 ? 613 HOH   A O   1 
HETATM 2506 O  O   . HOH   C 3 .   ? 1.50822   -13.01541 -4.33674  1.000 12.76591 ? 614 HOH   A O   1 
HETATM 2507 O  O   . HOH   C 3 .   ? -20.19075 7.78892   -5.36718  1.000 27.93445 ? 615 HOH   A O   1 
HETATM 2508 O  O   . HOH   C 3 .   ? -15.85003 -28.15505 0.18031   1.000 26.43802 ? 616 HOH   A O   1 
HETATM 2509 O  O   . HOH   C 3 .   ? -7.49739  5.18394   -2.27773  1.000 23.03883 ? 617 HOH   A O   1 
HETATM 2510 O  O   . HOH   C 3 .   ? -4.38484  -8.02995  -14.21711 1.000 18.73136 ? 618 HOH   A O   1 
HETATM 2511 O  O   . HOH   C 3 .   ? 4.785     -2.882    -9.231    1.000 28.84428 ? 619 HOH   A O   1 
HETATM 2512 O  O   . HOH   C 3 .   ? -10.98091 -25.46147 23.33583  1.000 30.64650 ? 620 HOH   A O   1 
HETATM 2513 O  O   . HOH   C 3 .   ? -12.93486 -14.33253 7.32465   1.000 18.82561 ? 621 HOH   A O   1 
HETATM 2514 O  O   . HOH   C 3 .   ? -19.41610 -23.99569 0.09136   1.000 24.37005 ? 622 HOH   A O   1 
HETATM 2515 O  O   . HOH   C 3 .   ? -32.93330 -18.42040 17.93622  1.000 29.40148 ? 623 HOH   A O   1 
HETATM 2516 O  O   . HOH   C 3 .   ? -22.24136 -16.18405 9.16456   1.000 18.10150 ? 624 HOH   A O   1 
HETATM 2517 O  O   . HOH   C 3 .   ? -19.40840 -17.81263 5.46034   1.000 16.99740 ? 625 HOH   A O   1 
HETATM 2518 O  O   . HOH   C 3 .   ? -8.43597  -27.04404 9.52427   1.000 20.54718 ? 626 HOH   A O   1 
HETATM 2519 O  O   . HOH   C 3 .   ? -2.29952  -14.95474 2.52121   1.000 12.95834 ? 627 HOH   A O   1 
HETATM 2520 O  O   . HOH   C 3 .   ? -24.00494 -16.56302 -0.33086  1.000 19.28477 ? 628 HOH   A O   1 
HETATM 2521 O  O   . HOH   C 3 .   ? 0.55253   9.22004   -14.57702 1.000 29.51910 ? 629 HOH   A O   1 
HETATM 2522 O  O   . HOH   C 3 .   ? -4.53106  -20.56708 6.56090   1.000 21.93354 ? 630 HOH   A O   1 
HETATM 2523 O  O   . HOH   C 3 .   ? -2.53536  15.35088  -15.13416 1.000 36.31840 ? 631 HOH   A O   1 
HETATM 2524 O  O   . HOH   C 3 .   ? -28.17586 -8.25867  18.18512  1.000 45.52181 ? 632 HOH   A O   1 
HETATM 2525 O  O   . HOH   C 3 .   ? 5.37118   -4.61382  -25.93009 1.000 36.92303 ? 633 HOH   A O   1 
HETATM 2526 O  O   . HOH   C 3 .   ? -4.06822  12.27553  -21.62927 1.000 36.76386 ? 634 HOH   A O   1 
HETATM 2527 O  O   . HOH   C 3 .   ? -18.98486 -34.70340 2.85791   1.000 29.61960 ? 635 HOH   A O   1 
HETATM 2528 O  O   . HOH   C 3 .   ? -12.88405 -17.88743 12.55575  1.000 20.91786 ? 636 HOH   A O   1 
HETATM 2529 O  O   . HOH   C 3 .   ? -12.81642 15.75026  -4.71710  1.000 39.44208 ? 637 HOH   A O   1 
HETATM 2530 O  O   . HOH   C 3 .   ? -25.66507 -25.84218 5.86276   1.000 23.24057 ? 638 HOH   A O   1 
HETATM 2531 O  O   . HOH   C 3 .   ? 3.85275   2.68954   -12.92280 1.000 28.21575 ? 639 HOH   A O   1 
HETATM 2532 O  O   . HOH   C 3 .   ? -4.47029  -18.58007 -18.33745 1.000 32.60335 ? 640 HOH   A O   1 
HETATM 2533 O  O   . HOH   C 3 .   ? 5.21882   -7.61781  -17.37296 1.000 31.74776 ? 641 HOH   A O   1 
HETATM 2534 O  O   . HOH   C 3 .   ? 0.37705   -23.10149 -10.83815 1.000 27.02346 ? 642 HOH   A O   1 
HETATM 2535 O  O   . HOH   C 3 .   ? -15.15312 -11.51664 8.91367   1.000 23.29440 ? 643 HOH   A O   1 
HETATM 2536 O  O   . HOH   C 3 .   ? -19.44749 -19.52832 24.86416  1.000 33.82784 ? 644 HOH   A O   1 
HETATM 2537 O  O   . HOH   C 3 .   ? -18.94564 -15.77700 -19.52049 1.000 33.02707 ? 645 HOH   A O   1 
HETATM 2538 O  O   . HOH   C 3 .   ? 5.40486   -16.47768 -13.48995 1.000 31.69943 ? 646 HOH   A O   1 
HETATM 2539 O  O   . HOH   C 3 .   ? -5.03973  -0.64719  4.81914   1.000 20.72271 ? 647 HOH   A O   1 
HETATM 2540 O  O   . HOH   C 3 .   ? 1.44724   -13.17439 -10.30276 1.000 14.23523 ? 648 HOH   A O   1 
HETATM 2541 O  O   . HOH   C 3 .   ? -4.82845  -24.14231 4.10513   1.000 30.61745 ? 649 HOH   A O   1 
HETATM 2542 O  O   . HOH   C 3 .   ? -9.64818  1.77706   8.60784   1.000 30.23418 ? 650 HOH   A O   1 
HETATM 2543 O  O   . HOH   C 3 .   ? -28.52184 -25.68586 3.49443   1.000 38.06144 ? 651 HOH   A O   1 
HETATM 2544 O  O   . HOH   C 3 .   ? -22.04449 -16.90079 6.31903   1.000 15.51776 ? 652 HOH   A O   1 
HETATM 2545 O  O   . HOH   C 3 .   ? -6.49272  -30.93452 21.82436  1.000 37.84009 ? 653 HOH   A O   1 
HETATM 2546 O  O   . HOH   C 3 .   ? 2.95028   1.91257   -7.69211  1.000 31.29602 ? 654 HOH   A O   1 
HETATM 2547 O  O   . HOH   C 3 .   ? -31.34993 -34.43943 15.31055  1.000 30.34082 ? 655 HOH   A O   1 
HETATM 2548 O  O   . HOH   C 3 .   ? -1.36398  -24.48432 17.15113  1.000 29.14265 ? 656 HOH   A O   1 
HETATM 2549 O  O   . HOH   C 3 .   ? 3.34921   6.62737   -14.42592 1.000 35.78342 ? 657 HOH   A O   1 
HETATM 2550 O  O   . HOH   C 3 .   ? -19.07174 -25.73130 28.83035  1.000 38.36905 ? 658 HOH   A O   1 
HETATM 2551 O  O   . HOH   C 3 .   ? -16.19179 -39.56409 3.49481   1.000 31.67845 ? 659 HOH   A O   1 
HETATM 2552 O  O   . HOH   C 3 .   ? -7.98967  4.02285   4.91260   1.000 34.97809 ? 660 HOH   A O   1 
HETATM 2553 O  O   . HOH   C 3 .   ? 0.24032   -16.97263 -2.70948  1.000 15.33999 ? 661 HOH   A O   1 
HETATM 2554 O  O   . HOH   C 3 .   ? -11.79768 6.37846   4.37576   1.000 26.27199 ? 662 HOH   A O   1 
HETATM 2555 O  O   . HOH   C 3 .   ? -0.00000  -16.28588 0.00000   0.50  13.32582 ? 663 HOH   A O   1 
HETATM 2556 O  O   . HOH   C 3 .   ? -12.59709 -17.94601 19.33616  1.000 34.32413 ? 664 HOH   A O   1 
HETATM 2557 O  O   . HOH   C 3 .   ? -2.96301  -13.22147 6.50157   1.000 15.82399 ? 665 HOH   A O   1 
HETATM 2558 O  O   . HOH   C 3 .   ? -3.49328  -6.95220  0.76603   1.000 17.46287 ? 666 HOH   A O   1 
HETATM 2559 O  O   . HOH   C 3 .   ? -5.38053  -13.21635 8.12736   1.000 19.76687 ? 667 HOH   A O   1 
HETATM 2560 O  O   . HOH   C 3 .   ? -11.84983 -3.81158  10.91758  1.000 30.88494 ? 668 HOH   A O   1 
HETATM 2561 O  O   . HOH   C 3 .   ? -25.15614 -31.19029 24.64946  1.000 33.66140 ? 669 HOH   A O   1 
HETATM 2562 O  O   . HOH   C 3 .   ? -10.05912 4.45122   6.14806   1.000 25.41579 ? 670 HOH   A O   1 
HETATM 2563 O  O   . HOH   C 3 .   ? -27.902   -28.047   0.363     1.000 37.28720 ? 671 HOH   A O   1 
HETATM 2564 O  O   . HOH   C 3 .   ? -1.22444  -29.86236 -7.27494  1.000 35.14120 ? 672 HOH   A O   1 
HETATM 2565 O  O   . HOH   C 3 .   ? 4.25133   -9.81483  -16.17871 1.000 35.59243 ? 673 HOH   A O   1 
HETATM 2566 O  O   . HOH   C 3 .   ? -28.00472 -20.53205 2.10844   1.000 22.68451 ? 674 HOH   A O   1 
HETATM 2567 O  O   . HOH   C 3 .   ? -13.87199 -29.44532 -0.04906  1.000 24.88150 ? 675 HOH   A O   1 
HETATM 2568 O  O   . HOH   C 3 .   ? 1.20623   -1.61512  -27.21553 1.000 31.53924 ? 676 HOH   A O   1 
HETATM 2569 O  O   . HOH   C 3 .   ? 2.483     -16.691   -9.386    1.000 19.52160 ? 677 HOH   A O   1 
HETATM 2570 O  O   . HOH   C 3 .   ? -26.41936 -18.29249 22.99794  1.000 46.66535 ? 678 HOH   A O   1 
HETATM 2571 O  O   . HOH   C 3 .   ? -5.09989  -21.23288 12.96970  1.000 30.69572 ? 679 HOH   A O   1 
HETATM 2572 O  O   . HOH   C 3 .   ? -7.94832  -13.00441 11.41246  1.000 32.05415 ? 680 HOH   A O   1 
HETATM 2573 O  O   . HOH   C 3 .   ? -14.74512 -27.77634 -16.41960 1.000 38.09563 ? 681 HOH   A O   1 
HETATM 2574 O  O   . HOH   C 3 .   ? -7.78811  -28.21730 24.42890  1.000 33.29934 ? 682 HOH   A O   1 
HETATM 2575 O  O   . HOH   C 3 .   ? -13.56480 -7.12155  8.83254   1.000 29.56612 ? 683 HOH   A O   1 
HETATM 2576 O  O   . HOH   C 3 .   ? -4.80201  -34.37294 22.37871  1.000 34.90466 ? 684 HOH   A O   1 
HETATM 2577 O  O   . HOH   C 3 .   ? -21.19957 2.76496   -14.49017 1.000 34.48113 ? 685 HOH   A O   1 
HETATM 2578 O  O   . HOH   C 3 .   ? -15.57985 -25.10915 -16.37255 1.000 37.37798 ? 686 HOH   A O   1 
HETATM 2579 O  O   . HOH   C 3 .   ? -26.27421 -16.93030 21.42277  1.000 40.25975 ? 687 HOH   A O   1 
HETATM 2580 O  O   . HOH   C 3 .   ? -22.49835 -3.44919  7.77112   1.000 34.08851 ? 688 HOH   A O   1 
HETATM 2581 O  O   . HOH   C 3 .   ? -20.32905 -34.57374 24.20937  1.000 38.40227 ? 689 HOH   A O   1 
HETATM 2582 O  O   . HOH   C 3 .   ? -0.86796  8.53956   -10.42309 1.000 32.06609 ? 690 HOH   A O   1 
HETATM 2583 O  O   . HOH   C 3 .   ? -29.21423 -20.08327 16.20771  1.000 28.62950 ? 691 HOH   A O   1 
HETATM 2584 O  O   . HOH   C 3 .   ? 3.88297   4.25367   -17.63903 1.000 30.78026 ? 692 HOH   A O   1 
HETATM 2585 O  O   . HOH   C 3 .   ? -15.14750 -9.40926  9.86830   1.000 27.50957 ? 693 HOH   A O   1 
HETATM 2586 O  O   . HOH   C 3 .   ? 2.93739   4.46203   -15.23201 1.000 30.13393 ? 694 HOH   A O   1 
HETATM 2587 O  O   . HOH   C 3 .   ? -1.212    -23.378   14.569    1.000 28.53631 ? 695 HOH   A O   1 
HETATM 2588 O  O   . HOH   C 3 .   ? -20.07903 -7.41134  -19.39118 1.000 49.37146 ? 696 HOH   A O   1 
HETATM 2589 O  O   . HOH   C 3 .   ? -5.87697  1.19198   6.50707   1.000 42.41160 ? 697 HOH   A O   1 
HETATM 2590 O  O   . HOH   C 3 .   ? 3.51292   -12.56864 -14.50665 1.000 32.82449 ? 698 HOH   A O   1 
HETATM 2591 O  O   . HOH   C 3 .   ? -1.02589  -26.93293 -12.54040 1.000 30.42173 ? 699 HOH   A O   1 
HETATM 2592 O  O   . HOH   C 3 .   ? -20.31848 5.23566   3.39981   1.000 38.55099 ? 700 HOH   A O   1 
HETATM 2593 O  O   . HOH   C 3 .   ? 0.96025   5.06636   -2.61832  1.000 41.00549 ? 701 HOH   A O   1 
HETATM 2594 O  O   . HOH   C 3 .   ? 1.393     -20.670   -22.277   1.000 39.05787 ? 702 HOH   A O   1 
HETATM 2595 O  O   . HOH   C 3 .   ? -12.95612 -28.11024 -9.05842  1.000 42.83360 ? 703 HOH   A O   1 
HETATM 2596 O  O   . HOH   C 3 .   ? -21.81228 4.75788   6.42301   1.000 34.37315 ? 704 HOH   A O   1 
HETATM 2597 O  O   . HOH   C 3 .   ? -1.78041  6.86533   -7.80583  1.000 31.76230 ? 705 HOH   A O   1 
HETATM 2598 O  O   . HOH   C 3 .   ? -22.63524 4.10172   0.76269   1.000 27.96140 ? 706 HOH   A O   1 
HETATM 2599 O  O   . HOH   C 3 .   ? -3.07462  -23.32334 10.50328  1.000 27.36297 ? 707 HOH   A O   1 
HETATM 2600 O  O   . HOH   C 3 .   ? -7.63944  -20.66225 12.30077  1.000 27.67003 ? 708 HOH   A O   1 
HETATM 2601 O  O   . HOH   C 3 .   ? -12.64434 -8.93687  8.91026   1.000 28.66294 ? 709 HOH   A O   1 
HETATM 2602 O  O   . HOH   C 3 .   ? -32.084   -23.419   6.131     1.000 25.51981 ? 710 HOH   A O   1 
HETATM 2603 O  O   . HOH   C 3 .   ? -27.63441 -20.10196 24.13900  1.000 47.32967 ? 711 HOH   A O   1 
HETATM 2604 O  O   . HOH   C 3 .   ? 3.64356   -18.58083 -10.28729 1.000 29.95988 ? 712 HOH   A O   1 
HETATM 2605 O  O   . HOH   C 3 .   ? -10.72754 -9.36940  7.26082   1.000 21.23363 ? 713 HOH   A O   1 
HETATM 2606 O  O   . HOH   C 3 .   ? -8.66835  -10.82717 7.67878   1.000 28.18938 ? 714 HOH   A O   1 
HETATM 2607 O  O   . HOH   C 3 .   ? -8.47098  -21.62355 8.85695   1.000 26.43528 ? 715 HOH   A O   1 
HETATM 2608 O  O   . HOH   C 3 .   ? -1.06777  -24.78815 -5.54162  1.000 28.62018 ? 716 HOH   A O   1 
HETATM 2609 O  O   . HOH   C 3 .   ? -7.68174  -27.63925 -14.63543 1.000 29.02711 ? 717 HOH   A O   1 
HETATM 2610 O  O   . HOH   C 3 .   ? -0.32255  -26.73988 -8.47877  1.000 34.16937 ? 718 HOH   A O   1 
HETATM 2611 O  O   . HOH   C 3 .   ? -33.60968 -29.93129 6.19645   1.000 35.58647 ? 719 HOH   A O   1 
HETATM 2612 O  O   . HOH   C 3 .   ? -5.50822  6.80424   -1.82841  1.000 32.77860 ? 720 HOH   A O   1 
HETATM 2613 O  O   . HOH   C 3 .   ? -15.15978 -17.39409 18.72611  1.000 36.12298 ? 721 HOH   A O   1 
HETATM 2614 O  O   . HOH   C 3 .   ? -2.48855  -26.16976 2.54308   1.000 41.45082 ? 722 HOH   A O   1 
HETATM 2615 O  O   . HOH   C 3 .   ? -23.15297 -40.75862 12.92118  1.000 36.12149 ? 723 HOH   A O   1 
HETATM 2616 O  O   . HOH   C 3 .   ? -0.82760  -23.31909 -3.62897  1.000 25.87078 ? 724 HOH   A O   1 
HETATM 2617 O  O   . HOH   C 3 .   ? 0.97115   2.89903   -1.21418  1.000 37.87824 ? 725 HOH   A O   1 
HETATM 2618 O  O   . HOH   C 3 .   ? -19.59428 4.22759   5.14707   1.000 28.77285 ? 726 HOH   A O   1 
HETATM 2619 O  O   . HOH   C 3 .   ? -0.09102  -23.85712 -1.13948  1.000 51.67919 ? 727 HOH   A O   1 
HETATM 2620 O  O   . HOH   C 3 .   ? -3.36216  -22.69118 5.57384   1.000 23.74785 ? 728 HOH   A O   1 
HETATM 2621 O  O   . HOH   C 3 .   ? 5.324     -14.403   -12.318   1.000 30.74012 ? 729 HOH   A O   1 
HETATM 2622 O  O   . HOH   C 3 .   ? -20.07391 -37.07510 3.20532   1.000 35.01487 ? 730 HOH   A O   1 
HETATM 2623 O  O   . HOH   C 3 .   ? -10.72610 -19.60761 11.45850  1.000 26.28884 ? 731 HOH   A O   1 
HETATM 2624 O  O   . HOH   C 3 .   ? -32.65664 -21.03618 19.03303  1.000 35.84174 ? 732 HOH   A O   1 
HETATM 2625 O  O   . HOH   C 3 .   ? 3.949     -14.216   -9.736    1.000 20.42868 ? 733 HOH   A O   1 
HETATM 2626 O  O   . HOH   C 3 .   ? 4.64067   1.33329   -15.50815 1.000 45.20985 ? 734 HOH   A O   1 
HETATM 2627 O  O   . HOH   C 3 .   ? -25.87350 -20.94712 0.00000   0.50  25.30097 ? 735 HOH   A O   1 
HETATM 2628 O  O   . HOH   C 3 .   ? -1.09244  -34.06140 10.72904  1.000 37.76698 ? 736 HOH   A O   1 
HETATM 2629 O  O   . HOH   C 3 .   ? -13.31417 -9.40291  -21.04089 1.000 36.06644 ? 737 HOH   A O   1 
HETATM 2630 O  O   . HOH   C 3 .   ? -15.52614 -37.25144 2.74953   1.000 36.64078 ? 738 HOH   A O   1 
HETATM 2631 O  O   . HOH   C 3 .   ? -8.53565  -28.02569 -19.24224 1.000 42.45727 ? 739 HOH   A O   1 
HETATM 2632 O  O   . HOH   C 3 .   ? -6.50892  -28.04150 -17.06910 1.000 36.46322 ? 740 HOH   A O   1 
HETATM 2633 O  O   . HOH   C 3 .   ? -1.20390  -27.82590 0.28642   1.000 51.02994 ? 741 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   . SER   A 1   ? 0.19179 0.38687 0.30232 0.00241  0.09850  0.07546  1   SER   A N   
2    C  CA  . SER   A 1   ? 0.20427 0.39036 0.30786 -0.00307 0.08674  0.08178  1   SER   A CA  
3    C  C   . SER   A 1   ? 0.20479 0.38787 0.32549 -0.00505 0.07349  0.08284  1   SER   A C   
4    O  O   . SER   A 1   ? 0.18460 0.37150 0.31982 -0.00121 0.07181  0.07834  1   SER   A O   
5    C  CB  . SER   A 1   ? 0.26084 0.44976 0.36733 -0.00980 0.08856  0.09339  1   SER   A CB  
6    O  OG  . SER   A 1   ? 0.28135 0.47840 0.41597 -0.01400 0.08614  0.09986  1   SER   A OG  
7    N  N   . GLY   A 2   ? 0.18317 0.35867 0.30196 -0.01134 0.06400  0.08889  2   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.18508 0.35464 0.31260 -0.01426 0.05097  0.08789  2   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.19394 0.35307 0.30117 -0.01177 0.04597  0.08234  2   GLY   A C   
10   O  O   . GLY   A 2   ? 0.18845 0.34581 0.27587 -0.00667 0.05196  0.07743  2   GLY   A O   
11   N  N   . PHE   A 3   ? 0.18117 0.33311 0.29261 -0.01617 0.03443  0.08246  3   PHE   A N   
12   C  CA  . PHE   A 3   ? 0.17110 0.31417 0.26545 -0.01457 0.02946  0.07796  3   PHE   A CA  
13   C  C   . PHE   A 3   ? 0.21256 0.34927 0.31442 -0.01734 0.01700  0.07356  3   PHE   A C   
14   O  O   . PHE   A 3   ? 0.22647 0.35850 0.33835 -0.02512 0.00940  0.07697  3   PHE   A O   
15   C  CB  . PHE   A 3   ? 0.22742 0.36124 0.30773 -0.01774 0.02903  0.08370  3   PHE   A CB  
16   C  CG  . PHE   A 3   ? 0.19133 0.31576 0.24746 -0.01251 0.02667  0.07696  3   PHE   A CG  
17   C  CD1 . PHE   A 3   ? 0.24604 0.37660 0.28564 -0.00711 0.03445  0.07390  3   PHE   A CD1 
18   C  CD2 . PHE   A 3   ? 0.23101 0.34037 0.28082 -0.01314 0.01642  0.07205  3   PHE   A CD2 
19   C  CE1 . PHE   A 3   ? 0.24621 0.36991 0.26528 -0.00355 0.03095  0.06760  3   PHE   A CE1 
20   C  CE2 . PHE   A 3   ? 0.22126 0.32399 0.25199 -0.00841 0.01411  0.06618  3   PHE   A CE2 
21   C  CZ  . PHE   A 3   ? 0.22321 0.33374 0.23940 -0.00403 0.02068  0.06431  3   PHE   A CZ  
22   N  N   . ARG   A 4   ? 0.19069 0.32458 0.28512 -0.01126 0.01460  0.06493  4   ARG   A N   
23   C  CA  . ARG   A 4   ? 0.14189 0.26984 0.24006 -0.01264 0.00318  0.06040  4   ARG   A CA  
24   C  C   . ARG   A 4   ? 0.14846 0.26205 0.22458 -0.00904 -0.00095 0.05205  4   ARG   A C   
25   O  O   . ARG   A 4   ? 0.19064 0.30234 0.25227 -0.00391 0.00506  0.04834  4   ARG   A O   
26   C  CB  . ARG   A 4   ? 0.15856 0.29894 0.27463 -0.00877 0.00381  0.06057  4   ARG   A CB  
27   C  CG  . ARG   A 4   ? 0.12833 0.27554 0.26305 -0.01291 0.00339  0.06628  4   ARG   A CG  
28   C  CD  . ARG   A 4   ? 0.15944 0.30065 0.29820 -0.02032 -0.01059 0.06615  4   ARG   A CD  
29   N  NE  . ARG   A 4   ? 0.19188 0.34167 0.34935 -0.02411 -0.01267 0.07103  4   ARG   A NE  
30   C  CZ  . ARG   A 4   ? 0.20045 0.34658 0.36145 -0.03285 -0.02327 0.07169  4   ARG   A CZ  
31   N  NH1 . ARG   A 4   ? 0.23274 0.36534 0.37905 -0.03794 -0.03217 0.06668  4   ARG   A NH1 
32   N  NH2 . ARG   A 4   ? 0.15722 0.31344 0.33616 -0.03664 -0.02475 0.07668  4   ARG   A NH2 
33   N  N   . LYS   A 5   ? 0.16275 0.26778 0.23688 -0.01227 -0.01132 0.04892  5   LYS   A N   
34   C  CA  . LYS   A 5   ? 0.15779 0.25144 0.21435 -0.00900 -0.01500 0.04156  5   LYS   A CA  
35   C  C   . LYS   A 5   ? 0.19651 0.29495 0.25627 -0.00323 -0.01367 0.03853  5   LYS   A C   
36   O  O   . LYS   A 5   ? 0.25064 0.35125 0.31897 -0.00416 -0.02022 0.03941  5   LYS   A O   
37   C  CB  . LYS   A 5   ? 0.22059 0.30360 0.27254 -0.01463 -0.02487 0.03917  5   LYS   A CB  
38   C  CG  . LYS   A 5   ? 0.24328 0.31310 0.27668 -0.01274 -0.02548 0.03382  5   LYS   A CG  
39   C  CD  . LYS   A 5   ? 0.31373 0.37221 0.34320 -0.01871 -0.03250 0.03111  5   LYS   A CD  
40   C  CE  . LYS   A 5   ? 0.28903 0.33519 0.30651 -0.01683 -0.03009 0.02861  5   LYS   A CE  
41   N  NZ  . LYS   A 5   ? 0.26651 0.31585 0.28584 -0.01403 -0.02339 0.03445  5   LYS   A NZ  
42   N  N   . MET   A 6   ? 0.13311 0.23287 0.18597 0.00242  -0.00528 0.03527  6   MET   A N   
43   C  CA  . MET   A 6   ? 0.13917 0.24263 0.19804 0.00846  -0.00059 0.03231  6   MET   A CA  
44   C  C   . MET   A 6   ? 0.15386 0.24654 0.19923 0.01090  -0.00317 0.02544  6   MET   A C   
45   O  O   . MET   A 6   ? 0.15758 0.24429 0.18650 0.01056  -0.00206 0.02106  6   MET   A O   
46   C  CB  . MET   A 6   ? 0.14148 0.25198 0.19980 0.01232  0.01181  0.03111  6   MET   A CB  
47   C  CG  . MET   A 6   ? 0.17379 0.29090 0.24757 0.01843  0.01878  0.03015  6   MET   A CG  
48   S  SD  . MET   A 6   ? 0.28705 0.41284 0.35721 0.02194  0.03506  0.02794  6   MET   A SD  
49   C  CE  . MET   A 6   ? 0.19718 0.34045 0.29269 0.01914  0.03774  0.03991  6   MET   A CE  
50   N  N   . ALA   A 7   ? 0.15594 0.24739 0.20980 0.01329  -0.00648 0.02568  7   ALA   A N   
51   C  CA  . ALA   A 7   ? 0.08637 0.16763 0.13017 0.01522  -0.00797 0.02040  7   ALA   A CA  
52   C  C   . ALA   A 7   ? 0.10342 0.18336 0.15045 0.02108  0.00139  0.01531  7   ALA   A C   
53   O  O   . ALA   A 7   ? 0.12427 0.21208 0.18401 0.02479  0.00878  0.01666  7   ALA   A O   
54   C  CB  . ALA   A 7   ? 0.13541 0.21455 0.18491 0.01410  -0.01694 0.02473  7   ALA   A CB  
55   N  N   . PHE   A 8   ? 0.13015 0.19972 0.16598 0.02157  0.00182  0.00880  8   PHE   A N   
56   C  CA  . PHE   A 8   ? 0.13264 0.19686 0.17213 0.02645  0.00997  0.00261  8   PHE   A CA  
57   C  C   . PHE   A 8   ? 0.09900 0.16219 0.15853 0.03140  0.00915  0.00815  8   PHE   A C   
58   O  O   . PHE   A 8   ? 0.10347 0.16750 0.16799 0.02963  0.00004  0.01570  8   PHE   A O   
59   C  CB  . PHE   A 8   ? 0.12956 0.18251 0.15337 0.02391  0.00950  -0.00561 8   PHE   A CB  
60   C  CG  . PHE   A 8   ? 0.18031 0.23604 0.18648 0.02026  0.01115  -0.01111 8   PHE   A CG  
61   C  CD1 . PHE   A 8   ? 0.20996 0.26755 0.20987 0.02172  0.02009  -0.01819 8   PHE   A CD1 
62   C  CD2 . PHE   A 8   ? 0.16444 0.22156 0.16016 0.01571  0.00407  -0.00880 8   PHE   A CD2 
63   C  CE1 . PHE   A 8   ? 0.28629 0.34837 0.26857 0.01795  0.02036  -0.02163 8   PHE   A CE1 
64   C  CE2 . PHE   A 8   ? 0.20321 0.26466 0.18467 0.01302  0.00474  -0.01174 8   PHE   A CE2 
65   C  CZ  . PHE   A 8   ? 0.24210 0.30659 0.21627 0.01378  0.01211  -0.01755 8   PHE   A CZ  
66   N  N   . PRO   A 9   ? 0.14642 0.20802 0.21768 0.03794  0.01882  0.00484  9   PRO   A N   
67   C  CA  . PRO   A 9   ? 0.15789 0.21711 0.25026 0.04394  0.01816  0.01115  9   PRO   A CA  
68   C  C   . PRO   A 9   ? 0.13317 0.17914 0.21842 0.04140  0.01110  0.01191  9   PRO   A C   
69   O  O   . PRO   A 9   ? 0.16823 0.20317 0.23694 0.03783  0.01271  0.00305  9   PRO   A O   
70   C  CB  . PRO   A 9   ? 0.14312 0.19823 0.24494 0.05166  0.03254  0.00358  9   PRO   A CB  
71   C  CG  . PRO   A 9   ? 0.14408 0.20638 0.23200 0.04937  0.04039  -0.00383 9   PRO   A CG  
72   C  CD  . PRO   A 9   ? 0.15325 0.21453 0.21792 0.04031  0.03113  -0.00494 9   PRO   A CD  
73   N  N   . SER   A 10  ? 0.10415 0.15300 0.20144 0.04223  0.00249  0.02349  10  SER   A N   
74   C  CA  . SER   A 10  ? 0.13280 0.17226 0.22098 0.03828  -0.00546 0.02711  10  SER   A CA  
75   C  C   . SER   A 10  ? 0.14598 0.17203 0.24574 0.04347  -0.00208 0.02920  10  SER   A C   
76   O  O   . SER   A 10  ? 0.12476 0.14167 0.21669 0.03984  -0.00686 0.03212  10  SER   A O   
77   C  CB  . SER   A 10  ? 0.08801 0.13765 0.17687 0.03446  -0.01781 0.03863  10  SER   A CB  
78   O  OG  . SER   A 10  ? 0.11343 0.17436 0.22551 0.03954  -0.02037 0.04901  10  SER   A OG  
79   N  N   . GLY   A 11  ? 0.12856 0.15263 0.24735 0.05196  0.00701  0.02795  11  GLY   A N   
80   C  CA  . GLY   A 11  ? 0.13215 0.14240 0.26687 0.05832  0.01032  0.03202  11  GLY   A CA  
81   C  C   . GLY   A 11  ? 0.16674 0.15744 0.28717 0.05327  0.01135  0.02527  11  GLY   A C   
82   O  O   . GLY   A 11  ? 0.18442 0.16601 0.31087 0.05354  0.00709  0.03450  11  GLY   A O   
83   N  N   . LYS   A 12  ? 0.14259 0.12738 0.24508 0.04828  0.01696  0.00993  12  LYS   A N   
84   C  CA  . LYS   A 12  ? 0.19454 0.16160 0.28627 0.04266  0.01857  0.00208  12  LYS   A CA  
85   C  C   . LYS   A 12  ? 0.19370 0.16220 0.27522 0.03526  0.00821  0.01082  12  LYS   A C   
86   O  O   . LYS   A 12  ? 0.24702 0.20145 0.32795 0.03173  0.00816  0.01136  12  LYS   A O   
87   C  CB  . LYS   A 12  ? 0.17943 0.14459 0.25266 0.03745  0.02425  -0.01520 12  LYS   A CB  
88   C  CG  . LYS   A 12  ? 0.24979 0.20620 0.32854 0.04325  0.03712  -0.02770 12  LYS   A CG  
89   C  CD  . LYS   A 12  ? 0.31255 0.27093 0.36874 0.03690  0.04086  -0.04352 12  LYS   A CD  
90   C  CE  . LYS   A 12  ? 0.36938 0.31676 0.42686 0.04173  0.05487  -0.05831 12  LYS   A CE  
91   N  NZ  . LYS   A 12  ? 0.40144 0.35730 0.47730 0.05301  0.06315  -0.05343 12  LYS   A NZ  
92   N  N   . VAL   A 13  ? 0.14675 0.13133 0.21975 0.03231  0.00034  0.01695  13  VAL   A N   
93   C  CA  . VAL   A 13  ? 0.20905 0.19568 0.27091 0.02582  -0.00811 0.02461  13  VAL   A CA  
94   C  C   . VAL   A 13  ? 0.18820 0.17604 0.26147 0.02894  -0.01434 0.04095  13  VAL   A C   
95   O  O   . VAL   A 13  ? 0.20053 0.18290 0.26870 0.02501  -0.01804 0.04822  13  VAL   A O   
96   C  CB  . VAL   A 13  ? 0.14202 0.14272 0.18820 0.02114  -0.01277 0.02209  13  VAL   A CB  
97   C  CG1 . VAL   A 13  ? 0.18570 0.18855 0.21911 0.01498  -0.01967 0.02846  13  VAL   A CG1 
98   C  CG2 . VAL   A 13  ? 0.16083 0.16086 0.19622 0.01821  -0.00744 0.00826  13  VAL   A CG2 
99   N  N   . GLU   A 14  ? 0.12841 0.12518 0.21768 0.03574  -0.01582 0.04807  14  GLU   A N   
100  C  CA  . GLU   A 14  ? 0.13516 0.13533 0.23692 0.03898  -0.02313 0.06515  14  GLU   A CA  
101  C  C   . GLU   A 14  ? 0.15219 0.13471 0.26293 0.04123  -0.01998 0.07094  14  GLU   A C   
102  O  O   . GLU   A 14  ? 0.19054 0.17346 0.29659 0.03799  -0.02609 0.08220  14  GLU   A O   
103  C  CB  . GLU   A 14  ? 0.13980 0.15198 0.26004 0.04549  -0.02290 0.06937  14  GLU   A CB  
104  C  CG  . GLU   A 14  ? 0.12091 0.15063 0.23434 0.04193  -0.02696 0.06611  14  GLU   A CG  
105  C  CD  . GLU   A 14  ? 0.12923 0.16908 0.26073 0.04708  -0.02348 0.06710  14  GLU   A CD  
106  O  OE1 . GLU   A 14  ? 0.15728 0.19845 0.30124 0.04995  -0.02505 0.07548  14  GLU   A OE1 
107  O  OE2 . GLU   A 14  ? 0.13621 0.18333 0.27006 0.04824  -0.01875 0.06015  14  GLU   A OE2 
108  N  N   . GLY   A 15  ? 0.17899 0.14576 0.29819 0.04474  -0.00926 0.06041  15  GLY   A N   
109  C  CA  . GLY   A 15  ? 0.18102 0.12777 0.31135 0.04672  -0.00545 0.06542  15  GLY   A CA  
110  C  C   . GLY   A 15  ? 0.21993 0.15731 0.33401 0.03681  -0.00746 0.06552  15  GLY   A C   
111  O  O   . GLY   A 15  ? 0.21643 0.13645 0.33954 0.03684  -0.00468 0.07112  15  GLY   A O   
112  N  N   . CYS   A 16  ? 0.17583 0.12420 0.26814 0.02858  -0.01151 0.06003  16  CYS   A N   
113  C  CA  . CYS   A 16  ? 0.19557 0.13926 0.27313 0.01906  -0.01261 0.05975  16  CYS   A CA  
114  C  C   . CYS   A 16  ? 0.20510 0.16091 0.27016 0.01508  -0.02115 0.07326  16  CYS   A C   
115  O  O   . CYS   A 16  ? 0.21172 0.16523 0.26545 0.00766  -0.02110 0.07502  16  CYS   A O   
116  C  CB  . CYS   A 16  ? 0.17342 0.12058 0.23600 0.01271  -0.00951 0.04252  16  CYS   A CB  
117  S  SG  . CYS   A 16  ? 0.21360 0.14723 0.28286 0.01449  0.00031  0.02364  16  CYS   A SG  
118  N  N   . MET   A 17  ? 0.19026 0.15992 0.25600 0.01891  -0.02820 0.08186  17  MET   A N   
119  C  CA  . MET   A 17  ? 0.19021 0.17169 0.23880 0.01370  -0.03606 0.09085  17  MET   A CA  
120  C  C   . MET   A 17  ? 0.22048 0.19922 0.27065 0.01316  -0.03736 0.10230  17  MET   A C   
121  O  O   . MET   A 17  ? 0.23948 0.21522 0.30650 0.01914  -0.03698 0.10790  17  MET   A O   
122  C  CB  . MET   A 17  ? 0.19965 0.19814 0.24237 0.01439  -0.04123 0.08686  17  MET   A CB  
123  C  CG  . MET   A 17  ? 0.16526 0.16803 0.20484 0.01446  -0.03927 0.07460  17  MET   A CG  
124  S  SD  . MET   A 17  ? 0.16321 0.16267 0.18341 0.00690  -0.03391 0.06150  17  MET   A SD  
125  C  CE  . MET   A 17  ? 0.19503 0.20104 0.19463 0.00044  -0.03973 0.07029  17  MET   A CE  
126  N  N   . VAL   A 18  ? 0.23600 0.21613 0.26899 0.00624  -0.03815 0.10588  18  VAL   A N   
127  C  CA  . VAL   A 18  ? 0.25976 0.23844 0.29070 0.00482  -0.03948 0.11740  18  VAL   A CA  
128  C  C   . VAL   A 18  ? 0.26388 0.25470 0.27117 -0.00098 -0.04308 0.11745  18  VAL   A C   
129  O  O   . VAL   A 18  ? 0.25378 0.25091 0.24714 -0.00429 -0.04270 0.10783  18  VAL   A O   
130  C  CB  . VAL   A 18  ? 0.26750 0.22976 0.30466 0.00208  -0.03312 0.12178  18  VAL   A CB  
131  C  CG1 . VAL   A 18  ? 0.27519 0.22150 0.33556 0.00771  -0.02801 0.11821  18  VAL   A CG1 
132  C  CG2 . VAL   A 18  ? 0.24152 0.20378 0.26400 -0.00599 -0.02941 0.11609  18  VAL   A CG2 
133  N  N   . GLN   A 19  ? 0.32290 0.31577 0.32611 -0.00182 -0.04593 0.12807  19  GLN   A N   
134  C  CA  . GLN   A 19  ? 0.32680 0.32841 0.30752 -0.00696 -0.04834 0.12898  19  GLN   A CA  
135  C  C   . GLN   A 19  ? 0.32185 0.31707 0.29355 -0.01190 -0.04234 0.13379  19  GLN   A C   
136  O  O   . GLN   A 19  ? 0.32963 0.31531 0.31271 -0.01119 -0.04003 0.14385  19  GLN   A O   
137  C  CB  . GLN   A 19  ? 0.34869 0.35740 0.33031 -0.00515 -0.05575 0.13899  19  GLN   A CB  
138  C  CG  . GLN   A 19  ? 0.38127 0.39806 0.33958 -0.01008 -0.05909 0.14061  19  GLN   A CG  
139  C  CD  . GLN   A 19  ? 0.39090 0.41759 0.35118 -0.00868 -0.06844 0.14711  19  GLN   A CD  
140  O  OE1 . GLN   A 19  ? 0.44403 0.47077 0.42407 -0.00391 -0.07173 0.15658  19  GLN   A OE1 
141  N  NE2 . GLN   A 19  ? 0.44548 0.48040 0.38637 -0.01277 -0.07255 0.14206  19  GLN   A NE2 
142  N  N   . VAL   A 20  ? 0.27249 0.27255 0.22514 -0.01679 -0.03901 0.12660  20  VAL   A N   
143  C  CA  . VAL   A 20  ? 0.34368 0.34048 0.28734 -0.02192 -0.03230 0.13101  20  VAL   A CA  
144  C  C   . VAL   A 20  ? 0.31989 0.32454 0.24081 -0.02466 -0.03325 0.13268  20  VAL   A C   
145  O  O   . VAL   A 20  ? 0.33054 0.34210 0.23794 -0.02489 -0.03481 0.12262  20  VAL   A O   
146  C  CB  . VAL   A 20  ? 0.31785 0.31337 0.26148 -0.02531 -0.02514 0.12150  20  VAL   A CB  
147  C  CG1 . VAL   A 20  ? 0.31628 0.31072 0.25271 -0.03103 -0.01750 0.12659  20  VAL   A CG1 
148  C  CG2 . VAL   A 20  ? 0.29881 0.28477 0.26351 -0.02346 -0.02436 0.12019  20  VAL   A CG2 
149  N  N   . THR   A 21  ? 0.34534 0.34753 0.26184 -0.02684 -0.03180 0.14519  21  THR   A N   
150  C  CA  . THR   A 21  ? 0.38120 0.38987 0.27476 -0.02950 -0.03254 0.14839  21  THR   A CA  
151  C  C   . THR   A 21  ? 0.40267 0.40873 0.28742 -0.03434 -0.02308 0.15361  21  THR   A C   
152  O  O   . THR   A 21  ? 0.40975 0.40801 0.30825 -0.03569 -0.01932 0.16269  21  THR   A O   
153  C  CB  . THR   A 21  ? 0.41039 0.42151 0.30465 -0.02745 -0.04152 0.16108  21  THR   A CB  
154  O  OG1 . THR   A 21  ? 0.39242 0.40832 0.29544 -0.02356 -0.04965 0.15561  21  THR   A OG1 
155  C  CG2 . THR   A 21  ? 0.42797 0.44535 0.29621 -0.03097 -0.04250 0.16533  21  THR   A CG2 
156  N  N   . CYS   A 22  ? 0.40224 0.41409 0.26492 -0.03696 -0.01855 0.14749  22  CYS   A N   
157  C  CA  . CYS   A 22  ? 0.42910 0.44055 0.28176 -0.04149 -0.00838 0.15223  22  CYS   A CA  
158  C  C   . CYS   A 22  ? 0.44656 0.46395 0.27094 -0.04260 -0.00781 0.15065  22  CYS   A C   
159  O  O   . CYS   A 22  ? 0.45946 0.48064 0.27215 -0.04140 -0.00694 0.13707  22  CYS   A O   
160  C  CB  . CYS   A 22  ? 0.40547 0.41729 0.26601 -0.04335 0.00105  0.14231  22  CYS   A CB  
161  S  SG  . CYS   A 22  ? 0.50973 0.52391 0.36164 -0.04908 0.01534  0.14638  22  CYS   A SG  
162  N  N   . GLY   A 23  ? 0.45725 0.47453 0.27041 -0.04479 -0.00839 0.16457  23  GLY   A N   
163  C  CA  . GLY   A 23  ? 0.46349 0.48605 0.24803 -0.04598 -0.00945 0.16433  23  GLY   A CA  
164  C  C   . GLY   A 23  ? 0.49855 0.52525 0.27918 -0.04338 -0.02241 0.16058  23  GLY   A C   
165  O  O   . GLY   A 23  ? 0.52271 0.54928 0.31792 -0.04154 -0.03183 0.17004  23  GLY   A O   
166  N  N   . THR   A 24  ? 0.52943 0.55972 0.29229 -0.04318 -0.02272 0.14686  24  THR   A N   
167  C  CA  . THR   A 24  ? 0.53740 0.57191 0.29848 -0.04178 -0.03465 0.14127  24  THR   A CA  
168  C  C   . THR   A 24  ? 0.51335 0.54645 0.29018 -0.03881 -0.03545 0.12634  24  THR   A C   
169  O  O   . THR   A 24  ? 0.56999 0.60638 0.34641 -0.03811 -0.04397 0.11971  24  THR   A O   
170  C  CB  . THR   A 24  ? 0.54341 0.58211 0.27320 -0.04434 -0.03608 0.13639  24  THR   A CB  
171  O  OG1 . THR   A 24  ? 0.58654 0.62248 0.30213 -0.04441 -0.02383 0.12394  24  THR   A OG1 
172  C  CG2 . THR   A 24  ? 0.55316 0.59482 0.26648 -0.04739 -0.03827 0.15297  24  THR   A CG2 
173  N  N   . THR   A 25  ? 0.50458 0.53348 0.29531 -0.03759 -0.02691 0.12140  25  THR   A N   
174  C  CA  . THR   A 25  ? 0.49528 0.52292 0.30054 -0.03482 -0.02717 0.10828  25  THR   A CA  
175  C  C   . THR   A 25  ? 0.44443 0.47037 0.27607 -0.03246 -0.03299 0.11409  25  THR   A C   
176  O  O   . THR   A 25  ? 0.44529 0.46765 0.28938 -0.03280 -0.03006 0.12401  25  THR   A O   
177  C  CB  . THR   A 25  ? 0.47899 0.50457 0.28459 -0.03483 -0.01513 0.09965  25  THR   A CB  
178  O  OG1 . THR   A 25  ? 0.53140 0.55810 0.31282 -0.03609 -0.00816 0.09475  25  THR   A OG1 
179  C  CG2 . THR   A 25  ? 0.43670 0.46143 0.25564 -0.03189 -0.01595 0.08653  25  THR   A CG2 
180  N  N   . THR   A 26  ? 0.44134 0.46929 0.28183 -0.03012 -0.04060 0.10796  26  THR   A N   
181  C  CA  . THR   A 26  ? 0.41293 0.43940 0.27818 -0.02698 -0.04504 0.11170  26  THR   A CA  
182  C  C   . THR   A 26  ? 0.37481 0.40085 0.24871 -0.02485 -0.04418 0.09769  26  THR   A C   
183  O  O   . THR   A 26  ? 0.37947 0.40819 0.24416 -0.02515 -0.04656 0.08798  26  THR   A O   
184  C  CB  . THR   A 26  ? 0.39978 0.43082 0.27055 -0.02584 -0.05555 0.12156  26  THR   A CB  
185  O  OG1 . THR   A 26  ? 0.45481 0.48516 0.32184 -0.02710 -0.05607 0.13697  26  THR   A OG1 
186  C  CG2 . THR   A 26  ? 0.38559 0.41565 0.28177 -0.02160 -0.05908 0.12292  26  THR   A CG2 
187  N  N   . LEU   A 27  ? 0.31519 0.33726 0.20592 -0.02310 -0.04054 0.09684  27  LEU   A N   
188  C  CA  . LEU   A 27  ? 0.32464 0.34646 0.22460 -0.02091 -0.03990 0.08533  27  LEU   A CA  
189  C  C   . LEU   A 27  ? 0.26393 0.28201 0.18555 -0.01817 -0.04067 0.09009  27  LEU   A C   
190  O  O   . LEU   A 27  ? 0.29884 0.31363 0.22983 -0.01732 -0.04221 0.10184  27  LEU   A O   
191  C  CB  . LEU   A 27  ? 0.30884 0.32997 0.20010 -0.02226 -0.03181 0.07492  27  LEU   A CB  
192  C  CG  . LEU   A 27  ? 0.32779 0.34765 0.21537 -0.02515 -0.02335 0.07871  27  LEU   A CG  
193  C  CD1 . LEU   A 27  ? 0.29942 0.31561 0.20496 -0.02567 -0.02186 0.08514  27  LEU   A CD1 
194  C  CD2 . LEU   A 27  ? 0.31277 0.33452 0.19236 -0.02530 -0.01635 0.06708  27  LEU   A CD2 
195  N  N   . ASN   A 28  ? 0.27687 0.29449 0.20658 -0.01640 -0.03937 0.08109  28  ASN   A N   
196  C  CA  . ASN   A 28  ? 0.23489 0.24843 0.18384 -0.01327 -0.04015 0.08402  28  ASN   A CA  
197  C  C   . ASN   A 28  ? 0.22825 0.23593 0.18128 -0.01558 -0.03407 0.08479  28  ASN   A C   
198  O  O   . ASN   A 28  ? 0.23117 0.24140 0.17410 -0.01897 -0.02920 0.07878  28  ASN   A O   
199  C  CB  . ASN   A 28  ? 0.23863 0.25552 0.19378 -0.01030 -0.04243 0.07461  28  ASN   A CB  
200  C  CG  . ASN   A 28  ? 0.23804 0.26091 0.19089 -0.00954 -0.04828 0.07407  28  ASN   A CG  
201  O  OD1 . ASN   A 28  ? 0.24788 0.27258 0.21185 -0.00712 -0.05287 0.08218  28  ASN   A OD1 
202  N  ND2 . ASN   A 28  ? 0.23889 0.26449 0.17843 -0.01165 -0.04807 0.06497  28  ASN   A ND2 
203  N  N   . GLY   A 29  ? 0.22639 0.22547 0.19625 -0.01370 -0.03391 0.09210  29  GLY   A N   
204  C  CA  . GLY   A 29  ? 0.22259 0.21319 0.19983 -0.01697 -0.02865 0.09246  29  GLY   A CA  
205  C  C   . GLY   A 29  ? 0.20831 0.19169 0.20334 -0.01217 -0.02784 0.08456  29  GLY   A C   
206  O  O   . GLY   A 29  ? 0.18532 0.16837 0.19016 -0.00604 -0.03195 0.08763  29  GLY   A O   
207  N  N   . LEU   A 30  ? 0.20421 0.18312 0.20382 -0.01502 -0.02187 0.07312  30  LEU   A N   
208  C  CA  . LEU   A 30  ? 0.22577 0.19698 0.23903 -0.01161 -0.01923 0.06219  30  LEU   A CA  
209  C  C   . LEU   A 30  ? 0.19734 0.15213 0.22373 -0.01461 -0.01433 0.06299  30  LEU   A C   
210  O  O   . LEU   A 30  ? 0.22652 0.17996 0.25087 -0.02215 -0.01103 0.06069  30  LEU   A O   
211  C  CB  . LEU   A 30  ? 0.17919 0.15892 0.18559 -0.01314 -0.01763 0.04720  30  LEU   A CB  
212  C  CG  . LEU   A 30  ? 0.16853 0.14305 0.18344 -0.01053 -0.01482 0.03463  30  LEU   A CG  
213  C  CD1 . LEU   A 30  ? 0.17322 0.15124 0.19244 -0.00267 -0.01698 0.03466  30  LEU   A CD1 
214  C  CD2 . LEU   A 30  ? 0.21254 0.19502 0.22009 -0.01492 -0.01338 0.02278  30  LEU   A CD2 
215  N  N   . TRP   A 31  ? 0.22292 0.16506 0.26468 -0.00879 -0.01344 0.06607  31  TRP   A N   
216  C  CA  . TRP   A 31  ? 0.23204 0.15439 0.28830 -0.01073 -0.00872 0.06860  31  TRP   A CA  
217  C  C   . TRP   A 31  ? 0.28355 0.19545 0.34721 -0.01030 -0.00341 0.05051  31  TRP   A C   
218  O  O   . TRP   A 31  ? 0.21936 0.12872 0.29046 -0.00219 -0.00197 0.04558  31  TRP   A O   
219  C  CB  . TRP   A 31  ? 0.23629 0.15027 0.30591 -0.00349 -0.01075 0.08541  31  TRP   A CB  
220  C  CG  . TRP   A 31  ? 0.29302 0.18354 0.38022 -0.00416 -0.00569 0.09118  31  TRP   A CG  
221  C  CD1 . TRP   A 31  ? 0.27560 0.15326 0.36489 -0.01351 -0.00083 0.08692  31  TRP   A CD1 
222  C  CD2 . TRP   A 31  ? 0.29621 0.17877 0.39776 0.00458  -0.00484 0.09811  31  TRP   A CD2 
223  N  NE1 . TRP   A 31  ? 0.29238 0.15254 0.39492 -0.01101 0.00296  0.09045  31  TRP   A NE1 
224  C  CE2 . TRP   A 31  ? 0.33028 0.19336 0.44042 0.00048  0.00079  0.09740  31  TRP   A CE2 
225  C  CE3 . TRP   A 31  ? 0.32147 0.21352 0.42991 0.01479  -0.00843 0.10425  31  TRP   A CE3 
226  C  CZ2 . TRP   A 31  ? 0.35023 0.20134 0.47516 0.00722  0.00319  0.10317  31  TRP   A CZ2 
227  C  CZ3 . TRP   A 31  ? 0.33028 0.21249 0.45474 0.02118  -0.00602 0.11025  31  TRP   A CZ3 
228  C  CH2 . TRP   A 31  ? 0.34031 0.20144 0.47274 0.01791  -0.00011 0.10989  31  TRP   A CH2 
229  N  N   . LEU   A 32  ? 0.24500 0.15201 0.30645 -0.01951 -0.00041 0.04068  32  LEU   A N   
230  C  CA  . LEU   A 32  ? 0.24405 0.14104 0.30875 -0.02167 0.00387  0.02246  32  LEU   A CA  
231  C  C   . LEU   A 32  ? 0.28631 0.16382 0.36099 -0.03028 0.00760  0.02119  32  LEU   A C   
232  O  O   . LEU   A 32  ? 0.26897 0.15128 0.34129 -0.03944 0.00633  0.02677  32  LEU   A O   
233  C  CB  . LEU   A 32  ? 0.23811 0.15218 0.28856 -0.02637 0.00177  0.00954  32  LEU   A CB  
234  C  CG  . LEU   A 32  ? 0.24850 0.18146 0.28868 -0.01975 -0.00185 0.01079  32  LEU   A CG  
235  C  CD1 . LEU   A 32  ? 0.20845 0.15814 0.23625 -0.02527 -0.00429 0.00289  32  LEU   A CD1 
236  C  CD2 . LEU   A 32  ? 0.25482 0.18333 0.29948 -0.01125 0.00092  0.00396  32  LEU   A CD2 
237  N  N   . ASP   A 33  ? 0.28076 0.13619 0.36727 -0.02766 0.01297  0.01324  33  ASP   A N   
238  C  CA  . ASP   A 33  ? 0.31705 0.14850 0.41611 -0.03524 0.01710  0.01267  33  ASP   A CA  
239  C  C   . ASP   A 33  ? 0.33581 0.16644 0.44146 -0.03601 0.01523  0.03590  33  ASP   A C   
240  O  O   . ASP   A 33  ? 0.33010 0.16511 0.43854 -0.02598 0.01317  0.05068  33  ASP   A O   
241  C  CB  . ASP   A 33  ? 0.34912 0.18190 0.44138 -0.04907 0.01664  -0.00359 33  ASP   A CB  
242  C  CG  . ASP   A 33  ? 0.35885 0.19457 0.44091 -0.04784 0.01770  -0.02496 33  ASP   A CG  
243  O  OD1 . ASP   A 33  ? 0.41712 0.23568 0.50471 -0.04054 0.02358  -0.03339 33  ASP   A OD1 
244  O  OD2 . ASP   A 33  ? 0.38090 0.23654 0.44963 -0.05361 0.01319  -0.03263 33  ASP   A OD2 
245  N  N   . ASP   A 34  ? 0.33820 0.16682 0.44431 -0.04762 0.01536  0.04021  34  ASP   A N   
246  C  CA  . ASP   A 34  ? 0.31437 0.14631 0.42025 -0.04776 0.01427  0.06118  34  ASP   A CA  
247  C  C   . ASP   A 34  ? 0.30578 0.16081 0.40057 -0.05385 0.01110  0.07047  34  ASP   A C   
248  O  O   . ASP   A 34  ? 0.33498 0.19373 0.42716 -0.05947 0.01223  0.08205  34  ASP   A O   
249  C  CB  . ASP   A 34  ? 0.36679 0.18055 0.48022 -0.05491 0.01794  0.06198  34  ASP   A CB  
250  C  CG  . ASP   A 34  ? 0.37294 0.18884 0.48487 -0.07010 0.01852  0.05056  34  ASP   A CG  
251  O  OD1 . ASP   A 34  ? 0.34919 0.17915 0.45567 -0.07440 0.01628  0.03881  34  ASP   A OD1 
252  O  OD2 . ASP   A 34  ? 0.39962 0.20403 0.51675 -0.07800 0.02075  0.05368  34  ASP   A OD2 
253  N  N   . VAL   A 35  ? 0.30755 0.18256 0.38956 -0.05064 0.00766  0.06278  35  VAL   A N   
254  C  CA  . VAL   A 35  ? 0.26702 0.16606 0.33443 -0.05358 0.00537  0.06871  35  VAL   A CA  
255  C  C   . VAL   A 35  ? 0.27117 0.18394 0.32625 -0.04303 0.00095  0.07261  35  VAL   A C   
256  O  O   . VAL   A 35  ? 0.27020 0.18272 0.32539 -0.03564 -0.00072 0.06293  35  VAL   A O   
257  C  CB  . VAL   A 35  ? 0.29284 0.20593 0.35576 -0.06171 0.00540  0.05387  35  VAL   A CB  
258  C  CG1 . VAL   A 35  ? 0.25351 0.19083 0.30302 -0.06228 0.00454  0.05967  35  VAL   A CG1 
259  C  CG2 . VAL   A 35  ? 0.27915 0.18092 0.35536 -0.07441 0.00854  0.05060  35  VAL   A CG2 
260  N  N   . VAL   A 36  ? 0.23178 0.15676 0.27571 -0.04315 -0.00064 0.08656  36  VAL   A N   
261  C  CA  . VAL   A 36  ? 0.23201 0.17188 0.26144 -0.03607 -0.00550 0.08948  36  VAL   A CA  
262  C  C   . VAL   A 36  ? 0.25527 0.21394 0.26992 -0.04024 -0.00448 0.08339  36  VAL   A C   
263  O  O   . VAL   A 36  ? 0.22771 0.19143 0.23907 -0.04721 -0.00055 0.08960  36  VAL   A O   
264  C  CB  . VAL   A 36  ? 0.24510 0.18422 0.27049 -0.03297 -0.00878 0.10969  36  VAL   A CB  
265  C  CG1 . VAL   A 36  ? 0.24122 0.19757 0.24867 -0.02851 -0.01447 0.11042  36  VAL   A CG1 
266  C  CG2 . VAL   A 36  ? 0.25795 0.18074 0.30028 -0.02606 -0.00956 0.11459  36  VAL   A CG2 
267  N  N   . TYR   A 37  ? 0.19499 0.16386 0.20227 -0.03563 -0.00719 0.07216  37  TYR   A N   
268  C  CA  . TYR   A 37  ? 0.23034 0.21577 0.22558 -0.03734 -0.00613 0.06550  37  TYR   A CA  
269  C  C   . TYR   A 37  ? 0.20244 0.19682 0.18109 -0.03314 -0.00940 0.07105  37  TYR   A C   
270  O  O   . TYR   A 37  ? 0.22480 0.21696 0.20254 -0.02744 -0.01470 0.07270  37  TYR   A O   
271  C  CB  . TYR   A 37  ? 0.15610 0.14582 0.15445 -0.03560 -0.00699 0.04957  37  TYR   A CB  
272  C  CG  . TYR   A 37  ? 0.21662 0.19875 0.22800 -0.04109 -0.00491 0.04166  37  TYR   A CG  
273  C  CD1 . TYR   A 37  ? 0.23108 0.19669 0.25267 -0.03955 -0.00502 0.03868  37  TYR   A CD1 
274  C  CD2 . TYR   A 37  ? 0.22241 0.21401 0.23680 -0.04837 -0.00260 0.03716  37  TYR   A CD2 
275  C  CE1 . TYR   A 37  ? 0.24313 0.19996 0.27442 -0.04597 -0.00311 0.02935  37  TYR   A CE1 
276  C  CE2 . TYR   A 37  ? 0.21561 0.20129 0.24116 -0.05523 -0.00220 0.02914  37  TYR   A CE2 
277  C  CZ  . TYR   A 37  ? 0.23646 0.20362 0.26892 -0.05453 -0.00250 0.02455  37  TYR   A CZ  
278  O  OH  . TYR   A 37  ? 0.25327 0.21250 0.29462 -0.06250 -0.00209 0.01472  37  TYR   A OH  
279  N  N   . CYS   A 38  ? 0.21357 0.21854 0.17942 -0.03629 -0.00598 0.07334  38  CYS   A N   
280  C  CA  . CYS   A 38  ? 0.20910 0.22103 0.15635 -0.03350 -0.00896 0.07625  38  CYS   A CA  
281  C  C   . CYS   A 38  ? 0.23346 0.25675 0.16916 -0.03545 -0.00266 0.07084  38  CYS   A C   
282  O  O   . CYS   A 38  ? 0.21760 0.24516 0.16037 -0.03979 0.00391  0.07034  38  CYS   A O   
283  C  CB  . CYS   A 38  ? 0.20594 0.21308 0.14903 -0.03259 -0.01143 0.08780  38  CYS   A CB  
284  S  SG  . CYS   A 38  ? 0.27126 0.27959 0.20879 -0.03797 -0.00369 0.09629  38  CYS   A SG  
285  N  N   . PRO   A 39  ? 0.20673 0.23332 0.12980 -0.03086 -0.00389 0.06342  39  PRO   A N   
286  C  CA  . PRO   A 39  ? 0.24856 0.28215 0.16294 -0.03061 0.00337  0.05687  39  PRO   A CA  
287  C  C   . PRO   A 39  ? 0.24794 0.28305 0.15721 -0.03429 0.01025  0.06462  39  PRO   A C   
288  O  O   . PRO   A 39  ? 0.24216 0.27209 0.14524 -0.03501 0.00787  0.07282  39  PRO   A O   
289  C  CB  . PRO   A 39  ? 0.21269 0.24334 0.11501 -0.02574 -0.00030 0.04927  39  PRO   A CB  
290  C  CG  . PRO   A 39  ? 0.20981 0.23631 0.11991 -0.02325 -0.00909 0.04855  39  PRO   A CG  
291  C  CD  . PRO   A 39  ? 0.23796 0.26112 0.15714 -0.02598 -0.01137 0.06006  39  PRO   A CD  
292  N  N   . ARG   A 40  ? 0.25381 0.29724 0.16705 -0.03642 0.01913  0.06254  40  ARG   A N   
293  C  CA  . ARG   A 40  ? 0.21640 0.26183 0.12659 -0.04010 0.02684  0.07019  40  ARG   A CA  
294  C  C   . ARG   A 40  ? 0.25731 0.29989 0.14602 -0.03743 0.02913  0.06940  40  ARG   A C   
295  O  O   . ARG   A 40  ? 0.30587 0.34733 0.18789 -0.04034 0.03321  0.07802  40  ARG   A O   
296  C  CB  . ARG   A 40  ? 0.21831 0.27542 0.14111 -0.04275 0.03633  0.06814  40  ARG   A CB  
297  C  CG  . ARG   A 40  ? 0.20854 0.27257 0.12536 -0.03751 0.04250  0.05792  40  ARG   A CG  
298  C  CD  . ARG   A 40  ? 0.21241 0.29064 0.14661 -0.03953 0.05191  0.05755  40  ARG   A CD  
299  N  NE  . ARG   A 40  ? 0.21438 0.29848 0.14639 -0.03308 0.05791  0.04808  40  ARG   A NE  
300  C  CZ  . ARG   A 40  ? 0.26442 0.36160 0.21068 -0.03239 0.06717  0.04693  40  ARG   A CZ  
301  N  NH1 . ARG   A 40  ? 0.21536 0.32209 0.17946 -0.03851 0.07058  0.05387  40  ARG   A NH1 
302  N  NH2 . ARG   A 40  ? 0.23727 0.33726 0.18151 -0.02551 0.07317  0.03877  40  ARG   A NH2 
303  N  N   . HIS   A 41  ? 0.28534 0.32592 0.16279 -0.03255 0.02685  0.05948  41  HIS   A N   
304  C  CA  . HIS   A 41  ? 0.36170 0.39872 0.21753 -0.03123 0.02912  0.05884  41  HIS   A CA  
305  C  C   . HIS   A 41  ? 0.35118 0.38261 0.19846 -0.03256 0.02032  0.06775  41  HIS   A C   
306  O  O   . HIS   A 41  ? 0.39435 0.42385 0.22231 -0.03203 0.02039  0.06764  41  HIS   A O   
307  C  CB  . HIS   A 41  ? 0.33798 0.37245 0.18403 -0.02632 0.02932  0.04606  41  HIS   A CB  
308  C  CG  . HIS   A 41  ? 0.35014 0.38033 0.20161 -0.02399 0.01844  0.04117  41  HIS   A CG  
309  N  ND1 . HIS   A 41  ? 0.39363 0.42010 0.24266 -0.02470 0.00847  0.04605  41  HIS   A ND1 
310  C  CD2 . HIS   A 41  ? 0.37794 0.40778 0.23866 -0.02096 0.01646  0.03270  41  HIS   A CD2 
311  C  CE1 . HIS   A 41  ? 0.39366 0.41802 0.25122 -0.02232 0.00146  0.04055  41  HIS   A CE1 
312  N  NE2 . HIS   A 41  ? 0.35267 0.37823 0.21618 -0.02010 0.00601  0.03237  41  HIS   A NE2 
313  N  N   . VAL   A 42  ? 0.34576 0.37504 0.20719 -0.03408 0.01342  0.07551  42  VAL   A N   
314  C  CA  . VAL   A 42  ? 0.33673 0.36204 0.19392 -0.03518 0.00693  0.08671  42  VAL   A CA  
315  C  C   . VAL   A 42  ? 0.34782 0.37388 0.19344 -0.03863 0.01395  0.09614  42  VAL   A C   
316  O  O   . VAL   A 42  ? 0.37656 0.40078 0.21033 -0.03910 0.00960  0.10400  42  VAL   A O   
317  C  CB  . VAL   A 42  ? 0.32562 0.34690 0.20303 -0.03567 0.00104  0.09433  42  VAL   A CB  
318  C  CG1 . VAL   A 42  ? 0.30819 0.32884 0.19823 -0.04022 0.00828  0.10153  42  VAL   A CG1 
319  C  CG2 . VAL   A 42  ? 0.34092 0.35851 0.21636 -0.03458 -0.00738 0.10436  42  VAL   A CG2 
320  N  N   . ILE   A 43  ? 0.34992 0.37980 0.19948 -0.04132 0.02493  0.09625  43  ILE   A N   
321  C  CA  . ILE   A 43  ? 0.37758 0.40831 0.21768 -0.04505 0.03288  0.10602  43  ILE   A CA  
322  C  C   . ILE   A 43  ? 0.42982 0.46301 0.24579 -0.04351 0.04000  0.10005  43  ILE   A C   
323  O  O   . ILE   A 43  ? 0.40760 0.44198 0.21231 -0.04636 0.04811  0.10736  43  ILE   A O   
324  C  CB  . ILE   A 43  ? 0.36974 0.40411 0.22721 -0.04979 0.04243  0.11079  43  ILE   A CB  
325  C  CG1 . ILE   A 43  ? 0.39860 0.44162 0.25943 -0.04874 0.05232  0.09971  43  ILE   A CG1 
326  C  CG2 . ILE   A 43  ? 0.34289 0.37299 0.22440 -0.05184 0.03639  0.11529  43  ILE   A CG2 
327  C  CD1 . ILE   A 43  ? 0.34389 0.39345 0.22907 -0.05371 0.05906  0.10268  43  ILE   A CD1 
328  N  N   . CYS   A 44  ? 0.43955 0.47251 0.24709 -0.03914 0.03785  0.08710  44  CYS   A N   
329  C  CA  . CYS   A 44  ? 0.47051 0.50380 0.25567 -0.03687 0.04525  0.07938  44  CYS   A CA  
330  C  C   . CYS   A 44  ? 0.56142 0.59127 0.32455 -0.03625 0.03669  0.07995  44  CYS   A C   
331  O  O   . CYS   A 44  ? 0.54003 0.56788 0.30776 -0.03535 0.02418  0.07900  44  CYS   A O   
332  C  CB  . CYS   A 44  ? 0.50992 0.54389 0.29956 -0.03228 0.04879  0.06452  44  CYS   A CB  
333  S  SG  . CYS   A 44  ? 0.45021 0.49187 0.26445 -0.03289 0.05966  0.06285  44  CYS   A SG  
334  N  N   . THR   A 45  ? 0.61703 0.64732 0.35650 -0.03691 0.04388  0.08121  45  THR   A N   
335  C  CA  . THR   A 45  ? 0.70099 0.72977 0.41618 -0.03677 0.03671  0.07966  45  THR   A CA  
336  C  C   . THR   A 45  ? 0.74050 0.76752 0.44504 -0.03261 0.03877  0.06282  45  THR   A C   
337  O  O   . THR   A 45  ? 0.71191 0.73855 0.42930 -0.02921 0.04512  0.05369  45  THR   A O   
338  C  CB  . THR   A 45  ? 0.70834 0.73855 0.40113 -0.03986 0.04318  0.08982  45  THR   A CB  
339  O  OG1 . THR   A 45  ? 0.69498 0.72681 0.38510 -0.03913 0.06046  0.08752  45  THR   A OG1 
340  C  CG2 . THR   A 45  ? 0.69359 0.72423 0.39681 -0.04397 0.03752  0.10749  45  THR   A CG2 
341  N  N   . SER   A 46  ? 0.80200 0.82826 0.48325 -0.03319 0.03292  0.05887  46  SER   A N   
342  C  CA  . SER   A 46  ? 0.81912 0.84297 0.48916 -0.02998 0.03433  0.04252  46  SER   A CA  
343  C  C   . SER   A 46  ? 0.80545 0.82956 0.46928 -0.02582 0.05209  0.03537  46  SER   A C   
344  O  O   . SER   A 46  ? 0.77312 0.79585 0.44826 -0.02130 0.05680  0.02437  46  SER   A O   
345  C  CB  . SER   A 46  ? 0.85919 0.88321 0.50267 -0.03305 0.02562  0.04026  46  SER   A CB  
346  O  OG  . SER   A 46  ? 0.89124 0.91649 0.54458 -0.03609 0.00919  0.04563  46  SER   A OG  
347  N  N   . GLU   A 47  ? 0.81978 0.84639 0.46709 -0.02694 0.06278  0.04247  47  GLU   A N   
348  C  CA  . GLU   A 47  ? 0.82357 0.85214 0.46593 -0.02229 0.08134  0.03660  47  GLU   A CA  
349  C  C   . GLU   A 47  ? 0.78773 0.81894 0.45947 -0.02076 0.09032  0.04011  47  GLU   A C   
350  O  O   . GLU   A 47  ? 0.75462 0.78835 0.43234 -0.01521 0.10348  0.03245  47  GLU   A O   
351  C  CB  . GLU   A 47  ? 0.84429 0.87519 0.45944 -0.02417 0.09100  0.04364  47  GLU   A CB  
352  C  CG  . GLU   A 47  ? 0.86188 0.89449 0.48177 -0.03012 0.09102  0.06228  47  GLU   A CG  
353  C  CD  . GLU   A 47  ? 0.88812 0.91980 0.49454 -0.03537 0.07484  0.07131  47  GLU   A CD  
354  O  OE1 . GLU   A 47  ? 0.88488 0.91483 0.49627 -0.03554 0.05969  0.06597  47  GLU   A OE1 
355  O  OE2 . GLU   A 47  ? 0.88054 0.91384 0.47209 -0.03935 0.07757  0.08429  47  GLU   A OE2 
356  N  N   . ASP   A 48  ? 0.75640 0.78828 0.44788 -0.02556 0.08326  0.05131  48  ASP   A N   
357  C  CA  . ASP   A 48  ? 0.71998 0.75548 0.44020 -0.02587 0.08973  0.05356  48  ASP   A CA  
358  C  C   . ASP   A 48  ? 0.68842 0.72306 0.42480 -0.02082 0.08755  0.04123  48  ASP   A C   
359  O  O   . ASP   A 48  ? 0.64477 0.68358 0.39749 -0.01834 0.09823  0.03788  48  ASP   A O   
360  C  CB  . ASP   A 48  ? 0.67177 0.70844 0.40963 -0.03197 0.08037  0.06646  48  ASP   A CB  
361  C  CG  . ASP   A 48  ? 0.64286 0.68211 0.37559 -0.03734 0.08757  0.08052  48  ASP   A CG  
362  O  OD1 . ASP   A 48  ? 0.64545 0.68699 0.36559 -0.03684 0.10243  0.08033  48  ASP   A OD1 
363  O  OD2 . ASP   A 48  ? 0.61357 0.65225 0.35581 -0.04181 0.07889  0.09214  48  ASP   A OD2 
364  N  N   . MET   A 49  ? 0.70979 0.73965 0.44320 -0.01972 0.07383  0.03501  49  MET   A N   
365  C  CA  . MET   A 49  ? 0.68551 0.71357 0.43512 -0.01598 0.06959  0.02515  49  MET   A CA  
366  C  C   . MET   A 49  ? 0.69757 0.72596 0.44287 -0.00898 0.08103  0.01310  49  MET   A C   
367  O  O   . MET   A 49  ? 0.67755 0.70485 0.43708 -0.00526 0.07951  0.00540  49  MET   A O   
368  C  CB  . MET   A 49  ? 0.66601 0.68912 0.41235 -0.01726 0.05297  0.02215  49  MET   A CB  
369  C  CG  . MET   A 49  ? 0.64753 0.67117 0.41573 -0.02003 0.04220  0.02869  49  MET   A CG  
370  S  SD  . MET   A 49  ? 0.56562 0.59491 0.36127 -0.01989 0.04976  0.03097  49  MET   A SD  
371  C  CE  . MET   A 49  ? 0.49753 0.52406 0.29891 -0.01360 0.05235  0.01645  49  MET   A CE  
372  N  N   . LEU   A 50  ? 0.69103 0.72181 0.41773 -0.00653 0.09281  0.01161  50  LEU   A N   
373  C  CA  . LEU   A 50  ? 0.71337 0.74767 0.43851 0.00127  0.10420  -0.00009 50  LEU   A CA  
374  C  C   . LEU   A 50  ? 0.69884 0.74028 0.45313 0.00455  0.11459  0.00158  50  LEU   A C   
375  O  O   . LEU   A 50  ? 0.72232 0.76416 0.49441 0.00826  0.11180  -0.00489 50  LEU   A O   
376  C  CB  . LEU   A 50  ? 0.76222 0.79974 0.46115 0.00279  0.11431  -0.00201 50  LEU   A CB  
377  C  CG  . LEU   A 50  ? 0.80347 0.83403 0.47311 -0.00095 0.10323  -0.00700 50  LEU   A CG  
378  C  CD1 . LEU   A 50  ? 0.79373 0.82721 0.43382 -0.00072 0.11331  -0.00716 50  LEU   A CD1 
379  C  CD2 . LEU   A 50  ? 0.77453 0.79938 0.44461 0.00082  0.09524  -0.02267 50  LEU   A CD2 
380  N  N   . ASN   A 51  ? 0.67436 0.72114 0.43468 0.00218  0.12621  0.01066  51  ASN   A N   
381  C  CA  . ASN   A 51  ? 0.63564 0.68860 0.42530 0.00221  0.13609  0.01277  51  ASN   A CA  
382  C  C   . ASN   A 51  ? 0.61103 0.66729 0.40987 -0.00872 0.13785  0.02487  51  ASN   A C   
383  O  O   . ASN   A 51  ? 0.61520 0.67635 0.41255 -0.01168 0.15040  0.02995  51  ASN   A O   
384  C  CB  . ASN   A 51  ? 0.69070 0.75470 0.48467 0.01202  0.15180  0.00822  51  ASN   A CB  
385  C  CG  . ASN   A 51  ? 0.69155 0.75784 0.51763 0.01384  0.15933  0.00540  51  ASN   A CG  
386  O  OD1 . ASN   A 51  ? 0.68429 0.74832 0.53013 -0.00013 0.15428  0.00394  51  ASN   A OD1 
387  N  ND2 . ASN   A 51  ? 0.65000 0.77977 0.49588 0.02292  0.15679  -0.00238 51  ASN   A ND2 
388  N  N   . PRO   A 52  ? 0.58619 0.64257 0.39620 -0.01432 0.12533  0.03006  52  PRO   A N   
389  C  CA  . PRO   A 52  ? 0.54508 0.60738 0.36372 -0.02306 0.12279  0.04280  52  PRO   A CA  
390  C  C   . PRO   A 52  ? 0.49314 0.57043 0.34385 -0.02730 0.12866  0.04622  52  PRO   A C   
391  O  O   . PRO   A 52  ? 0.46732 0.55197 0.33928 -0.02461 0.12798  0.04002  52  PRO   A O   
392  C  CB  . PRO   A 52  ? 0.50879 0.56578 0.32814 -0.02505 0.10375  0.04551  52  PRO   A CB  
393  C  CG  . PRO   A 52  ? 0.52192 0.57688 0.34981 -0.01951 0.09865  0.03440  52  PRO   A CG  
394  C  CD  . PRO   A 52  ? 0.55787 0.60944 0.37347 -0.01218 0.11107  0.02464  52  PRO   A CD  
395  N  N   . ASN   A 53  ? 0.46700 0.55034 0.32206 -0.03414 0.13357  0.05698  53  ASN   A N   
396  C  CA  . ASN   A 53  ? 0.41336 0.51197 0.30026 -0.03966 0.13499  0.06302  53  ASN   A CA  
397  C  C   . ASN   A 53  ? 0.41914 0.51379 0.31139 -0.04522 0.12110  0.07314  53  ASN   A C   
398  O  O   . ASN   A 53  ? 0.36159 0.45234 0.24552 -0.05069 0.12190  0.08364  53  ASN   A O   
399  C  CB  . ASN   A 53  ? 0.46405 0.57251 0.35544 -0.04419 0.15124  0.06768  53  ASN   A CB  
400  C  CG  . ASN   A 53  ? 0.46833 0.59474 0.39571 -0.04939 0.15213  0.07268  53  ASN   A CG  
401  O  OD1 . ASN   A 53  ? 0.42590 0.55241 0.36519 -0.05541 0.14334  0.08176  53  ASN   A OD1 
402  N  ND2 . ASN   A 53  ? 0.52908 0.67095 0.47497 -0.04727 0.16263  0.06665  53  ASN   A ND2 
403  N  N   . TYR   A 54  ? 0.39212 0.48699 0.29818 -0.04375 0.10890  0.06994  54  TYR   A N   
404  C  CA  . TYR   A 54  ? 0.35078 0.43899 0.26057 -0.04809 0.09588  0.07740  54  TYR   A CA  
405  C  C   . TYR   A 54  ? 0.35456 0.44783 0.28342 -0.05658 0.09784  0.08845  54  TYR   A C   
406  O  O   . TYR   A 54  ? 0.31559 0.39950 0.24131 -0.06089 0.09144  0.09748  54  TYR   A O   
407  C  CB  . TYR   A 54  ? 0.34341 0.43193 0.26497 -0.04512 0.08478  0.07068  54  TYR   A CB  
408  C  CG  . TYR   A 54  ? 0.31725 0.39591 0.21912 -0.03856 0.07863  0.06213  54  TYR   A CG  
409  C  CD1 . TYR   A 54  ? 0.34661 0.41327 0.23348 -0.03898 0.06842  0.06547  54  TYR   A CD1 
410  C  CD2 . TYR   A 54  ? 0.31589 0.39697 0.21617 -0.03202 0.08291  0.05102  54  TYR   A CD2 
411  C  CE1 . TYR   A 54  ? 0.33743 0.39589 0.20903 -0.03391 0.06181  0.05765  54  TYR   A CE1 
412  C  CE2 . TYR   A 54  ? 0.33803 0.40833 0.22131 -0.02693 0.07707  0.04307  54  TYR   A CE2 
413  C  CZ  . TYR   A 54  ? 0.34193 0.40151 0.21121 -0.02831 0.06609  0.04629  54  TYR   A CZ  
414  O  OH  . TYR   A 54  ? 0.32739 0.37751 0.18245 -0.02414 0.05941  0.03872  54  TYR   A OH  
415  N  N   . GLU   A 55  ? 0.38133 0.48886 0.33193 -0.05918 0.10610  0.08803  55  GLU   A N   
416  C  CA  . GLU   A 55  ? 0.37520 0.48666 0.34437 -0.06837 0.10815  0.09803  55  GLU   A CA  
417  C  C   . GLU   A 55  ? 0.39024 0.49501 0.34199 -0.07230 0.11550  0.10810  55  GLU   A C   
418  O  O   . GLU   A 55  ? 0.35009 0.44580 0.30329 -0.07824 0.11084  0.11827  55  GLU   A O   
419  C  CB  . GLU   A 55  ? 0.37824 0.50853 0.37509 -0.07031 0.11488  0.09489  55  GLU   A CB  
420  C  CG  . GLU   A 55  ? 0.44123 0.57777 0.45693 -0.06802 0.10501  0.08749  55  GLU   A CG  
421  C  CD  . GLU   A 55  ? 0.47506 0.61773 0.48593 -0.05778 0.10728  0.07674  55  GLU   A CD  
422  O  OE1 . GLU   A 55  ? 0.48909 0.62791 0.47986 -0.05261 0.11605  0.07367  55  GLU   A OE1 
423  O  OE2 . GLU   A 55  ? 0.43997 0.58946 0.46577 -0.05505 0.09998  0.07107  55  GLU   A OE2 
424  N  N   . ASP   A 56  ? 0.39225 0.49998 0.32629 -0.06890 0.12719  0.10533  56  ASP   A N   
425  C  CA  . ASP   A 56  ? 0.43755 0.53853 0.34973 -0.07213 0.13413  0.11459  56  ASP   A CA  
426  C  C   . ASP   A 56  ? 0.42556 0.51035 0.31663 -0.07106 0.12246  0.12028  56  ASP   A C   
427  O  O   . ASP   A 56  ? 0.40143 0.47993 0.28650 -0.07630 0.12218  0.13274  56  ASP   A O   
428  C  CB  . ASP   A 56  ? 0.46823 0.57218 0.35994 -0.06765 0.14807  0.10804  56  ASP   A CB  
429  C  CG  . ASP   A 56  ? 0.51438 0.63501 0.42517 -0.07061 0.16290  0.10666  56  ASP   A CG  
430  O  OD1 . ASP   A 56  ? 0.55670 0.68223 0.46079 -0.06543 0.17352  0.09674  56  ASP   A OD1 
431  O  OD2 . ASP   A 56  ? 0.52283 0.65133 0.45525 -0.07854 0.16449  0.11558  56  ASP   A OD2 
432  N  N   . LEU   A 57  ? 0.39010 0.46865 0.27034 -0.06425 0.11282  0.11168  57  LEU   A N   
433  C  CA  . LEU   A 57  ? 0.40374 0.46942 0.26492 -0.06271 0.10141  0.11635  57  LEU   A CA  
434  C  C   . LEU   A 57  ? 0.37183 0.43155 0.25043 -0.06749 0.09145  0.12620  57  LEU   A C   
435  O  O   . LEU   A 57  ? 0.39893 0.44974 0.26740 -0.06929 0.08650  0.13687  57  LEU   A O   
436  C  CB  . LEU   A 57  ? 0.40259 0.46430 0.25248 -0.05510 0.09323  0.10405  57  LEU   A CB  
437  C  CG  . LEU   A 57  ? 0.46092 0.52274 0.28870 -0.04945 0.10152  0.09383  57  LEU   A CG  
438  C  CD1 . LEU   A 57  ? 0.46598 0.52051 0.28156 -0.04339 0.09027  0.08424  57  LEU   A CD1 
439  C  CD2 . LEU   A 57  ? 0.45623 0.51521 0.25914 -0.05133 0.10991  0.10090  57  LEU   A CD2 
440  N  N   . LEU   A 58  ? 0.35034 0.41439 0.25554 -0.06959 0.08872  0.12293  58  LEU   A N   
441  C  CA  . LEU   A 58  ? 0.35131 0.40649 0.27279 -0.07353 0.07931  0.12982  58  LEU   A CA  
442  C  C   . LEU   A 58  ? 0.35004 0.40235 0.28240 -0.08188 0.08480  0.14264  58  LEU   A C   
443  O  O   . LEU   A 58  ? 0.35792 0.39755 0.29175 -0.08413 0.07868  0.15241  58  LEU   A O   
444  C  CB  . LEU   A 58  ? 0.34841 0.40795 0.29230 -0.07351 0.07428  0.12088  58  LEU   A CB  
445  C  CG  . LEU   A 58  ? 0.33524 0.38268 0.29410 -0.07660 0.06435  0.12471  58  LEU   A CG  
446  C  CD1 . LEU   A 58  ? 0.33188 0.36674 0.27434 -0.07148 0.05512  0.12860  58  LEU   A CD1 
447  C  CD2 . LEU   A 58  ? 0.36109 0.41360 0.33800 -0.07680 0.05977  0.11449  58  LEU   A CD2 
448  N  N   . ILE   A 59  ? 0.35522 0.41886 0.29665 -0.08648 0.09652  0.14309  59  ILE   A N   
449  C  CA  . ILE   A 59  ? 0.38271 0.44372 0.33529 -0.09540 0.10206  0.15529  59  ILE   A CA  
450  C  C   . ILE   A 59  ? 0.40684 0.45791 0.33664 -0.09555 0.10278  0.16795  59  ILE   A C   
451  O  O   . ILE   A 59  ? 0.42523 0.46808 0.36243 -0.10196 0.10328  0.18033  59  ILE   A O   
452  C  CB  . ILE   A 59  ? 0.38048 0.45813 0.34639 -0.10019 0.11530  0.15347  59  ILE   A CB  
453  C  CG1 . ILE   A 59  ? 0.39712 0.47228 0.38174 -0.11103 0.11912  0.16451  59  ILE   A CG1 
454  C  CG2 . ILE   A 59  ? 0.40119 0.48586 0.34316 -0.09663 0.12692  0.15315  59  ILE   A CG2 
455  C  CD1 . ILE   A 59  ? 0.39834 0.45961 0.40185 -0.11549 0.10818  0.16616  59  ILE   A CD1 
456  N  N   . ARG   A 60  ? 0.41510 0.46621 0.31724 -0.08884 0.10234  0.16506  60  ARG   A N   
457  C  CA  . ARG   A 60  ? 0.44639 0.49043 0.32349 -0.08845 0.10224  0.17608  60  ARG   A CA  
458  C  C   . ARG   A 60  ? 0.44553 0.47625 0.32099 -0.08592 0.08793  0.18280  60  ARG   A C   
459  O  O   . ARG   A 60  ? 0.47154 0.49669 0.32874 -0.08543 0.08538  0.19349  60  ARG   A O   
460  C  CB  . ARG   A 60  ? 0.45589 0.50524 0.30466 -0.08246 0.10691  0.16754  60  ARG   A CB  
461  C  CG  . ARG   A 60  ? 0.48102 0.53845 0.31933 -0.08555 0.12306  0.16931  60  ARG   A CG  
462  C  CD  . ARG   A 60  ? 0.48188 0.54367 0.29993 -0.07863 0.12839  0.15537  60  ARG   A CD  
463  N  NE  . ARG   A 60  ? 0.48100 0.55490 0.31067 -0.08025 0.14376  0.14908  60  ARG   A NE  
464  C  CZ  . ARG   A 60  ? 0.50101 0.57918 0.31617 -0.07525 0.15408  0.13796  60  ARG   A CZ  
465  N  NH1 . ARG   A 60  ? 0.54910 0.61998 0.33998 -0.06781 0.14908  0.12923  60  ARG   A NH1 
466  N  NH2 . ARG   A 60  ? 0.49462 0.58468 0.32185 -0.07779 0.16973  0.13503  60  ARG   A NH2 
467  N  N   . LYS   A 61  ? 0.42882 0.45511 0.32305 -0.08405 0.07882  0.17676  61  LYS   A N   
468  C  CA  . LYS   A 61  ? 0.43376 0.44833 0.32908 -0.08022 0.06571  0.18078  61  LYS   A CA  
469  C  C   . LYS   A 61  ? 0.44185 0.44426 0.36046 -0.08553 0.06388  0.19087  61  LYS   A C   
470  O  O   . LYS   A 61  ? 0.44223 0.44580 0.38048 -0.09196 0.06996  0.18927  61  LYS   A O   
471  C  CB  . LYS   A 61  ? 0.43042 0.44685 0.33022 -0.07430 0.05780  0.16657  61  LYS   A CB  
472  C  CG  . LYS   A 61  ? 0.38624 0.41042 0.26224 -0.06823 0.05719  0.15625  61  LYS   A CG  
473  C  CD  . LYS   A 61  ? 0.46520 0.48407 0.32323 -0.06371 0.04703  0.16063  61  LYS   A CD  
474  C  CE  . LYS   A 61  ? 0.47329 0.49808 0.30292 -0.06057 0.04950  0.15385  61  LYS   A CE  
475  N  NZ  . LYS   A 61  ? 0.52053 0.54245 0.32964 -0.06075 0.04551  0.16526  61  LYS   A NZ  
476  N  N   . SER   A 62  ? 0.50621 0.49673 0.42357 -0.08285 0.05538  0.20090  62  SER   A N   
477  C  CA  . SER   A 62  ? 0.50084 0.47571 0.44083 -0.08572 0.05217  0.20870  62  SER   A CA  
478  C  C   . SER   A 62  ? 0.49966 0.46606 0.44998 -0.07915 0.04129  0.20245  62  SER   A C   
479  O  O   . SER   A 62  ? 0.47184 0.44443 0.40952 -0.07236 0.03482  0.19622  62  SER   A O   
480  C  CB  . SER   A 62  ? 0.47459 0.44106 0.40842 -0.08731 0.05217  0.22731  62  SER   A CB  
481  O  OG  . SER   A 62  ? 0.57227 0.54863 0.48694 -0.09112 0.06101  0.23368  62  SER   A OG  
482  N  N   . ASN   A 63  ? 0.48519 0.43640 0.45891 -0.08148 0.03977  0.20355  63  ASN   A N   
483  C  CA  . ASN   A 63  ? 0.45067 0.39157 0.43525 -0.07482 0.03079  0.19877  63  ASN   A CA  
484  C  C   . ASN   A 63  ? 0.47429 0.41598 0.44600 -0.06650 0.02244  0.20703  63  ASN   A C   
485  O  O   . ASN   A 63  ? 0.46792 0.41420 0.43598 -0.05980 0.01542  0.19951  63  ASN   A O   
486  C  CB  . ASN   A 63  ? 0.46121 0.38161 0.47033 -0.07825 0.03143  0.20099  63  ASN   A CB  
487  C  CG  . ASN   A 63  ? 0.45554 0.37463 0.48016 -0.08648 0.03669  0.18880  63  ASN   A CG  
488  O  OD1 . ASN   A 63  ? 0.44779 0.38143 0.46839 -0.08752 0.03808  0.17752  63  ASN   A OD1 
489  N  ND2 . ASN   A 63  ? 0.41828 0.32001 0.46117 -0.09283 0.03937  0.19091  63  ASN   A ND2 
490  N  N   . HIS   A 64  ? 0.50488 0.44337 0.46998 -0.06737 0.02285  0.22293  64  HIS   A N   
491  C  CA  . HIS   A 64  ? 0.52436 0.46449 0.47968 -0.06036 0.01408  0.23252  64  HIS   A CA  
492  C  C   . HIS   A 64  ? 0.51900 0.47631 0.44911 -0.05731 0.01036  0.22626  64  HIS   A C   
493  O  O   . HIS   A 64  ? 0.52526 0.48613 0.44833 -0.05173 0.00143  0.23089  64  HIS   A O   
494  C  CB  . HIS   A 64  ? 0.55065 0.48430 0.50392 -0.06301 0.01580  0.25206  64  HIS   A CB  
495  C  CG  . HIS   A 64  ? 0.56991 0.51567 0.49784 -0.06773 0.02121  0.25816  64  HIS   A CG  
496  N  ND1 . HIS   A 64  ? 0.58510 0.53031 0.51269 -0.07621 0.03231  0.26165  64  HIS   A ND1 
497  C  CD2 . HIS   A 64  ? 0.58958 0.54768 0.49162 -0.06545 0.01751  0.26137  64  HIS   A CD2 
498  C  CE1 . HIS   A 64  ? 0.58507 0.54171 0.48721 -0.07825 0.03614  0.26674  64  HIS   A CE1 
499  N  NE2 . HIS   A 64  ? 0.62508 0.58889 0.51032 -0.07194 0.02715  0.26626  64  HIS   A NE2 
500  N  N   . ASN   A 65  ? 0.50472 0.47258 0.42241 -0.06085 0.01696  0.21535  65  ASN   A N   
501  C  CA  . ASN   A 65  ? 0.48948 0.47063 0.38449 -0.05767 0.01390  0.20633  65  ASN   A CA  
502  C  C   . ASN   A 65  ? 0.46997 0.45280 0.37201 -0.05180 0.00597  0.19366  65  ASN   A C   
503  O  O   . ASN   A 65  ? 0.47564 0.46747 0.36103 -0.04881 0.00150  0.18637  65  ASN   A O   
504  C  CB  . ASN   A 65  ? 0.48785 0.47847 0.36971 -0.06217 0.02467  0.19794  65  ASN   A CB  
505  C  CG  . ASN   A 65  ? 0.51803 0.51031 0.38584 -0.06730 0.03273  0.20988  65  ASN   A CG  
506  O  OD1 . ASN   A 65  ? 0.51355 0.51058 0.38004 -0.07222 0.04391  0.20705  65  ASN   A OD1 
507  N  ND2 . ASN   A 65  ? 0.53439 0.52388 0.39203 -0.06617 0.02726  0.22385  65  ASN   A ND2 
508  N  N   . PHE   A 66  ? 0.45748 0.43102 0.38322 -0.05049 0.00456  0.19048  66  PHE   A N   
509  C  CA  . PHE   A 66  ? 0.46191 0.43634 0.39576 -0.04523 -0.00174 0.17896  66  PHE   A CA  
510  C  C   . PHE   A 66  ? 0.46176 0.42780 0.41051 -0.03923 -0.00990 0.18642  66  PHE   A C   
511  O  O   . PHE   A 66  ? 0.46650 0.41874 0.43504 -0.03925 -0.00811 0.19201  66  PHE   A O   
512  C  CB  . PHE   A 66  ? 0.40332 0.37423 0.35223 -0.04806 0.00343  0.16808  66  PHE   A CB  
513  C  CG  . PHE   A 66  ? 0.40117 0.38254 0.34008 -0.05316 0.01162  0.16029  66  PHE   A CG  
514  C  CD1 . PHE   A 66  ? 0.37141 0.36417 0.29718 -0.05066 0.01072  0.14821  66  PHE   A CD1 
515  C  CD2 . PHE   A 66  ? 0.42360 0.40350 0.36812 -0.06028 0.02067  0.16485  66  PHE   A CD2 
516  C  CE1 . PHE   A 66  ? 0.38375 0.38618 0.30265 -0.05398 0.01898  0.14087  66  PHE   A CE1 
517  C  CE2 . PHE   A 66  ? 0.40505 0.39669 0.34344 -0.06417 0.02886  0.15775  66  PHE   A CE2 
518  C  CZ  . PHE   A 66  ? 0.36279 0.36565 0.28866 -0.06044 0.02817  0.14579  66  PHE   A CZ  
519  N  N   . LEU   A 67  ? 0.44381 0.41793 0.38465 -0.03417 -0.01841 0.18550  67  LEU   A N   
520  C  CA  . LEU   A 67  ? 0.46177 0.43172 0.41873 -0.02753 -0.02618 0.19111  67  LEU   A CA  
521  C  C   . LEU   A 67  ? 0.40063 0.37121 0.36860 -0.02336 -0.02859 0.17762  67  LEU   A C   
522  O  O   . LEU   A 67  ? 0.40712 0.38833 0.36223 -0.02346 -0.03082 0.16693  67  LEU   A O   
523  C  CB  . LEU   A 67  ? 0.47323 0.45358 0.41715 -0.02536 -0.03459 0.19942  67  LEU   A CB  
524  C  CG  . LEU   A 67  ? 0.51200 0.49811 0.43224 -0.03037 -0.03293 0.20799  67  LEU   A CG  
525  C  CD1 . LEU   A 67  ? 0.50691 0.50390 0.41485 -0.02834 -0.04303 0.21397  67  LEU   A CD1 
526  C  CD2 . LEU   A 67  ? 0.52422 0.49955 0.45205 -0.03305 -0.02749 0.22272  67  LEU   A CD2 
527  N  N   . VAL   A 68  ? 0.42839 0.38646 0.41977 -0.01969 -0.02752 0.17766  68  VAL   A N   
528  C  CA  . VAL   A 68  ? 0.39744 0.35467 0.40082 -0.01501 -0.02924 0.16624  68  VAL   A CA  
529  C  C   . VAL   A 68  ? 0.42519 0.38046 0.44585 -0.00690 -0.03475 0.17262  68  VAL   A C   
530  O  O   . VAL   A 68  ? 0.41502 0.35863 0.45071 -0.00444 -0.03317 0.18251  68  VAL   A O   
531  C  CB  . VAL   A 68  ? 0.37593 0.31954 0.39241 -0.01758 -0.02196 0.15809  68  VAL   A CB  
532  C  CG1 . VAL   A 68  ? 0.36384 0.30697 0.39029 -0.01266 -0.02352 0.14636  68  VAL   A CG1 
533  C  CG2 . VAL   A 68  ? 0.39135 0.33957 0.39368 -0.02606 -0.01628 0.15328  68  VAL   A CG2 
534  N  N   . GLN   A 69  ? 0.38306 0.34982 0.40303 -0.00284 -0.04067 0.16691  69  GLN   A N   
535  C  CA  . GLN   A 69  ? 0.41345 0.38244 0.45094 0.00476  -0.04577 0.17255  69  GLN   A CA  
536  C  C   . GLN   A 69  ? 0.40526 0.37173 0.45739 0.00975  -0.04374 0.16063  69  GLN   A C   
537  O  O   . GLN   A 69  ? 0.35933 0.33490 0.40134 0.00807  -0.04522 0.14986  69  GLN   A O   
538  C  CB  . GLN   A 69  ? 0.45119 0.43771 0.47640 0.00432  -0.05481 0.17725  69  GLN   A CB  
539  C  CG  . GLN   A 69  ? 0.52188 0.51050 0.55028 0.00573  -0.05967 0.19462  69  GLN   A CG  
540  C  CD  . GLN   A 69  ? 0.57585 0.56193 0.58522 -0.00074 -0.05747 0.20251  69  GLN   A CD  
541  O  OE1 . GLN   A 69  ? 0.56358 0.55870 0.54858 -0.00638 -0.05880 0.19833  69  GLN   A OE1 
542  N  NE2 . GLN   A 69  ? 0.54243 0.51539 0.56318 0.00012  -0.05328 0.21361  69  GLN   A NE2 
543  N  N   . ALA   A 70  ? 0.40873 0.36191 0.48412 0.01591  -0.03953 0.16194  70  ALA   A N   
544  C  CA  . ALA   A 70  ? 0.43567 0.38608 0.52659 0.02202  -0.03661 0.15128  70  ALA   A CA  
545  C  C   . ALA   A 70  ? 0.45779 0.41650 0.56557 0.02983  -0.04079 0.15865  70  ALA   A C   
546  O  O   . ALA   A 70  ? 0.43704 0.38578 0.56344 0.03534  -0.03805 0.16623  70  ALA   A O   
547  C  CB  . ALA   A 70  ? 0.42319 0.35154 0.52760 0.02313  -0.02720 0.14426  70  ALA   A CB  
548  N  N   . GLY   A 71  ? 0.47784 0.45475 0.57993 0.02987  -0.04723 0.15644  71  GLY   A N   
549  C  CA  . GLY   A 71  ? 0.48198 0.47023 0.59854 0.03521  -0.05269 0.16566  71  GLY   A CA  
550  C  C   . GLY   A 71  ? 0.50219 0.49313 0.61412 0.03315  -0.05831 0.18166  71  GLY   A C   
551  O  O   . GLY   A 71  ? 0.49838 0.49239 0.58762 0.02578  -0.06138 0.18380  71  GLY   A O   
552  N  N   . ASN   A 72  ? 0.52637 0.51599 0.66028 0.04006  -0.05901 0.19337  72  ASN   A N   
553  C  CA  . ASN   A 72  ? 0.59157 0.58273 0.72425 0.03919  -0.06418 0.21071  72  ASN   A CA  
554  C  C   . ASN   A 72  ? 0.58188 0.55195 0.71980 0.03974  -0.05696 0.21604  72  ASN   A C   
555  O  O   . ASN   A 72  ? 0.61424 0.58108 0.76249 0.04263  -0.05881 0.23159  72  ASN   A O   
556  C  CB  . ASN   A 72  ? 0.59521 0.59796 0.74969 0.04608  -0.06989 0.22286  72  ASN   A CB  
557  C  CG  . ASN   A 72  ? 0.65220 0.64729 0.83638 0.05608  -0.06222 0.21838  72  ASN   A CG  
558  O  OD1 . ASN   A 72  ? 0.68560 0.66191 0.87601 0.05857  -0.05219 0.20926  72  ASN   A OD1 
559  N  ND2 . ASN   A 72  ? 0.62864 0.63830 0.83116 0.06157  -0.06653 0.22436  72  ASN   A ND2 
560  N  N   . VAL   A 73  ? 0.54718 0.50268 0.67878 0.03653  -0.04900 0.20397  73  VAL   A N   
561  C  CA  . VAL   A 73  ? 0.56410 0.49762 0.70193 0.03577  -0.04135 0.20664  73  VAL   A CA  
562  C  C   . VAL   A 73  ? 0.53919 0.46975 0.65279 0.02563  -0.03935 0.20184  73  VAL   A C   
563  O  O   . VAL   A 73  ? 0.51244 0.44930 0.61244 0.02172  -0.03901 0.18909  73  VAL   A O   
564  C  CB  . VAL   A 73  ? 0.54686 0.46230 0.70631 0.04209  -0.03184 0.19533  73  VAL   A CB  
565  C  CG1 . VAL   A 73  ? 0.56372 0.45589 0.72199 0.03712  -0.02354 0.19068  73  VAL   A CG1 
566  C  CG2 . VAL   A 73  ? 0.57869 0.49203 0.76503 0.05244  -0.03132 0.20434  73  VAL   A CG2 
567  N  N   . GLN   A 74  ? 0.58189 0.50367 0.69085 0.02141  -0.03772 0.21275  74  GLN   A N   
568  C  CA  . GLN   A 74  ? 0.54454 0.46568 0.63136 0.01156  -0.03521 0.21053  74  GLN   A CA  
569  C  C   . GLN   A 74  ? 0.53076 0.43134 0.62534 0.00812  -0.02562 0.20098  74  GLN   A C   
570  O  O   . GLN   A 74  ? 0.53493 0.41706 0.64866 0.01123  -0.02083 0.20374  74  GLN   A O   
571  C  CB  . GLN   A 74  ? 0.57348 0.49755 0.64919 0.00761  -0.03794 0.22773  74  GLN   A CB  
572  C  CG  . GLN   A 74  ? 0.58636 0.52908 0.65460 0.01003  -0.04817 0.23994  74  GLN   A CG  
573  C  CD  . GLN   A 74  ? 0.63300 0.57938 0.72481 0.01971  -0.05297 0.24481  74  GLN   A CD  
574  O  OE1 . GLN   A 74  ? 0.65456 0.59004 0.76704 0.02517  -0.05140 0.25599  74  GLN   A OE1 
575  N  NE2 . GLN   A 74  ? 0.61699 0.57876 0.70686 0.02180  -0.05829 0.23645  74  GLN   A NE2 
576  N  N   . LEU   A 75  ? 0.47018 0.37389 0.55000 0.00118  -0.02287 0.18947  75  LEU   A N   
577  C  CA  . LEU   A 75  ? 0.46043 0.34762 0.54483 -0.00480 -0.01466 0.18001  75  LEU   A CA  
578  C  C   . LEU   A 75  ? 0.51042 0.39762 0.58139 -0.01442 -0.01166 0.18749  75  LEU   A C   
579  O  O   . LEU   A 75  ? 0.53166 0.43543 0.58201 -0.01830 -0.01418 0.18994  75  LEU   A O   
580  C  CB  . LEU   A 75  ? 0.44645 0.33827 0.52595 -0.00650 -0.01336 0.16296  75  LEU   A CB  
581  C  CG  . LEU   A 75  ? 0.42355 0.31576 0.51534 0.00231  -0.01476 0.15359  75  LEU   A CG  
582  C  CD1 . LEU   A 75  ? 0.38364 0.27726 0.47034 -0.00099 -0.01238 0.13745  75  LEU   A CD1 
583  C  CD2 . LEU   A 75  ? 0.44948 0.32219 0.56455 0.00864  -0.01009 0.15299  75  LEU   A CD2 
584  N  N   . ARG   A 76  ? 0.50869 0.37712 0.59124 -0.01842 -0.00565 0.19038  76  ARG   A N   
585  C  CA  . ARG   A 76  ? 0.49122 0.35902 0.56397 -0.02808 -0.00155 0.19782  76  ARG   A CA  
586  C  C   . ARG   A 76  ? 0.47526 0.34545 0.54203 -0.03717 0.00356  0.18413  76  ARG   A C   
587  O  O   . ARG   A 76  ? 0.46277 0.32022 0.54220 -0.03913 0.00695  0.17119  76  ARG   A O   
588  C  CB  . ARG   A 76  ? 0.52074 0.36746 0.60951 -0.02944 0.00253  0.20731  76  ARG   A CB  
589  C  CG  . ARG   A 76  ? 0.53692 0.38200 0.61794 -0.03999 0.00759  0.21598  76  ARG   A CG  
590  C  CD  . ARG   A 76  ? 0.58652 0.41126 0.68324 -0.03994 0.01017  0.22859  76  ARG   A CD  
591  N  NE  . ARG   A 76  ? 0.67138 0.48509 0.77076 -0.05179 0.01753  0.22863  76  ARG   A NE  
592  C  CZ  . ARG   A 76  ? 0.67632 0.46821 0.79264 -0.05630 0.02233  0.21938  76  ARG   A CZ  
593  N  NH1 . ARG   A 76  ? 0.65476 0.43267 0.78553 -0.04952 0.02160  0.20794  76  ARG   A NH1 
594  N  NH2 . ARG   A 76  ? 0.67423 0.45850 0.79259 -0.06836 0.02829  0.22069  76  ARG   A NH2 
595  N  N   . VAL   A 77  ? 0.46215 0.34927 0.50975 -0.04266 0.00426  0.18633  77  VAL   A N   
596  C  CA  . VAL   A 77  ? 0.44130 0.33426 0.48443 -0.05147 0.00956  0.17555  77  VAL   A CA  
597  C  C   . VAL   A 77  ? 0.45555 0.33718 0.50718 -0.06112 0.01663  0.17987  77  VAL   A C   
598  O  O   . VAL   A 77  ? 0.44959 0.33113 0.49603 -0.06321 0.01840  0.19405  77  VAL   A O   
599  C  CB  . VAL   A 77  ? 0.44095 0.35671 0.46111 -0.05244 0.00874  0.17527  77  VAL   A CB  
600  C  CG1 . VAL   A 77  ? 0.41976 0.34326 0.43781 -0.06162 0.01566  0.16705  77  VAL   A CG1 
601  C  CG2 . VAL   A 77  ? 0.40614 0.33221 0.41901 -0.04458 0.00174  0.16792  77  VAL   A CG2 
602  N  N   . ILE   A 78  ? 0.42760 0.29991 0.49220 -0.06776 0.02038  0.16744  78  ILE   A N   
603  C  CA  . ILE   A 78  ? 0.43302 0.29502 0.50739 -0.07867 0.02665  0.16897  78  ILE   A CA  
604  C  C   . ILE   A 78  ? 0.39919 0.27625 0.47093 -0.08878 0.03112  0.16044  78  ILE   A C   
605  O  O   . ILE   A 78  ? 0.42955 0.30274 0.50895 -0.09900 0.03645  0.16226  78  ILE   A O   
606  C  CB  . ILE   A 78  ? 0.44907 0.28504 0.54304 -0.07990 0.02730  0.16135  78  ILE   A CB  
607  C  CG1 . ILE   A 78  ? 0.45180 0.28729 0.55094 -0.08216 0.02638  0.14073  78  ILE   A CG1 
608  C  CG2 . ILE   A 78  ? 0.47101 0.29241 0.57133 -0.06886 0.02406  0.17090  78  ILE   A CG2 
609  C  CD1 . ILE   A 78  ? 0.49594 0.30603 0.61004 -0.08083 0.02651  0.12969  78  ILE   A CD1 
610  N  N   . GLY   A 79  ? 0.43266 0.32756 0.49526 -0.08632 0.02919  0.15172  79  GLY   A N   
611  C  CA  . GLY   A 79  ? 0.38930 0.30195 0.45064 -0.09428 0.03339  0.14461  79  GLY   A CA  
612  C  C   . GLY   A 79  ? 0.39513 0.32765 0.44184 -0.08807 0.03074  0.13957  79  GLY   A C   
613  O  O   . GLY   A 79  ? 0.39901 0.32943 0.43988 -0.07933 0.02480  0.13773  79  GLY   A O   
614  N  N   . HIS   A 80  ? 0.38349 0.33559 0.42516 -0.09245 0.03555  0.13720  80  HIS   A N   
615  C  CA  . HIS   A 80  ? 0.34952 0.32011 0.37750 -0.08699 0.03402  0.13101  80  HIS   A CA  
616  C  C   . HIS   A 80  ? 0.34270 0.33092 0.37806 -0.09336 0.03896  0.12275  80  HIS   A C   
617  O  O   . HIS   A 80  ? 0.35154 0.34268 0.39656 -0.10114 0.04505  0.12579  80  HIS   A O   
618  C  CB  . HIS   A 80  ? 0.36102 0.33969 0.36639 -0.08083 0.03497  0.13985  80  HIS   A CB  
619  C  CG  . HIS   A 80  ? 0.38284 0.36822 0.38366 -0.08602 0.04350  0.14815  80  HIS   A CG  
620  N  ND1 . HIS   A 80  ? 0.40285 0.37612 0.40723 -0.08971 0.04574  0.16058  80  HIS   A ND1 
621  C  CD2 . HIS   A 80  ? 0.37618 0.37885 0.36986 -0.08787 0.05106  0.14589  80  HIS   A CD2 
622  C  CE1 . HIS   A 80  ? 0.43694 0.42023 0.43547 -0.09432 0.05422  0.16608  80  HIS   A CE1 
623  N  NE2 . HIS   A 80  ? 0.42013 0.42127 0.41245 -0.09299 0.05794  0.15697  80  HIS   A NE2 
624  N  N   . SER   A 81  ? 0.28785 0.28886 0.31951 -0.08984 0.03618  0.11276  81  SER   A N   
625  C  CA  . SER   A 81  ? 0.31757 0.33875 0.35618 -0.09352 0.04030  0.10534  81  SER   A CA  
626  C  C   . SER   A 81  ? 0.27599 0.31078 0.30122 -0.08567 0.03823  0.09824  81  SER   A C   
627  O  O   . SER   A 81  ? 0.33167 0.35919 0.34648 -0.07979 0.03213  0.09663  81  SER   A O   
628  C  CB  . SER   A 81  ? 0.29828 0.31816 0.35929 -0.10217 0.03746  0.09610  81  SER   A CB  
629  O  OG  . SER   A 81  ? 0.34409 0.35229 0.40674 -0.10047 0.02941  0.08818  81  SER   A OG  
630  N  N   . MET   A 82  ? 0.25553 0.30976 0.28271 -0.08536 0.04364  0.09379  82  MET   A N   
631  C  CA  . MET   A 82  ? 0.29373 0.36085 0.31096 -0.07786 0.04297  0.08569  82  MET   A CA  
632  C  C   . MET   A 82  ? 0.26590 0.34462 0.30031 -0.08057 0.03909  0.07570  82  MET   A C   
633  O  O   . MET   A 82  ? 0.22558 0.31365 0.27851 -0.08675 0.04118  0.07448  82  MET   A O   
634  C  CB  . MET   A 82  ? 0.29071 0.37012 0.29784 -0.07343 0.05247  0.08679  82  MET   A CB  
635  C  CG  . MET   A 82  ? 0.25746 0.34318 0.25002 -0.06417 0.05214  0.07849  82  MET   A CG  
636  S  SD  . MET   A 82  ? 0.33479 0.42252 0.30619 -0.05862 0.06233  0.07983  82  MET   A SD  
637  C  CE  . MET   A 82  ? 0.35915 0.45786 0.34779 -0.06560 0.07358  0.08642  82  MET   A CE  
638  N  N   . GLN   A 83  ? 0.24443 0.32157 0.27180 -0.07433 0.03255  0.06702  83  GLN   A N   
639  C  CA  . GLN   A 83  ? 0.23209 0.31967 0.26998 -0.07264 0.02757  0.05546  83  GLN   A CA  
640  C  C   . GLN   A 83  ? 0.20712 0.30337 0.23252 -0.06186 0.02890  0.05050  83  GLN   A C   
641  O  O   . GLN   A 83  ? 0.17300 0.25836 0.18392 -0.05510 0.02427  0.04660  83  GLN   A O   
642  C  CB  . GLN   A 83  ? 0.26076 0.33327 0.30147 -0.07381 0.01802  0.04730  83  GLN   A CB  
643  C  CG  . GLN   A 83  ? 0.23974 0.32271 0.28600 -0.07162 0.01187  0.03597  83  GLN   A CG  
644  C  CD  . GLN   A 83  ? 0.32348 0.39407 0.37461 -0.07660 0.00440  0.02752  83  GLN   A CD  
645  O  OE1 . GLN   A 83  ? 0.37538 0.43815 0.43727 -0.08644 0.00434  0.02851  83  GLN   A OE1 
646  N  NE2 . GLN   A 83  ? 0.27469 0.34203 0.31723 -0.07010 -0.00113 0.01888  83  GLN   A NE2 
647  N  N   . ASN   A 84  ? 0.16611 0.28174 0.19907 -0.06028 0.03571  0.05085  84  ASN   A N   
648  C  CA  . ASN   A 84  ? 0.17516 0.29726 0.19791 -0.04993 0.03909  0.04629  84  ASN   A CA  
649  C  C   . ASN   A 84  ? 0.17030 0.27868 0.16764 -0.04540 0.04117  0.04801  84  ASN   A C   
650  O  O   . ASN   A 84  ? 0.18964 0.29390 0.17903 -0.04764 0.04690  0.05455  84  ASN   A O   
651  C  CB  . ASN   A 84  ? 0.15165 0.27545 0.17922 -0.04491 0.03047  0.03737  84  ASN   A CB  
652  C  CG  . ASN   A 84  ? 0.14848 0.28737 0.19936 -0.05092 0.02639  0.03620  84  ASN   A CG  
653  O  OD1 . ASN   A 84  ? 0.12942 0.28729 0.19641 -0.05280 0.03233  0.04007  84  ASN   A OD1 
654  N  ND2 . ASN   A 84  ? 0.13332 0.26449 0.18622 -0.05480 0.01653  0.03103  84  ASN   A ND2 
655  N  N   . CYS   A 85  ? 0.16929 0.26798 0.15384 -0.03869 0.03502  0.04151  85  CYS   A N   
656  C  CA  . CYS   A 85  ? 0.19642 0.28436 0.15745 -0.03554 0.03553  0.04271  85  CYS   A CA  
657  C  C   . CYS   A 85  ? 0.20325 0.27574 0.15747 -0.03819 0.02725  0.04718  85  CYS   A C   
658  O  O   . CYS   A 85  ? 0.18860 0.25206 0.12571 -0.03511 0.02429  0.04759  85  CYS   A O   
659  C  CB  . CYS   A 85  ? 0.16761 0.25389 0.11955 -0.02716 0.03420  0.03350  85  CYS   A CB  
660  S  SG  . CYS   A 85  ? 0.15812 0.25647 0.11726 -0.02147 0.04547  0.02907  85  CYS   A SG  
661  N  N   . VAL   A 86  ? 0.16280 0.23057 0.13171 -0.04317 0.02306  0.04958  86  VAL   A N   
662  C  CA  . VAL   A 86  ? 0.19366 0.24618 0.15894 -0.04448 0.01702  0.05494  86  VAL   A CA  
663  C  C   . VAL   A 86  ? 0.19857 0.24738 0.17086 -0.05221 0.02078  0.06610  86  VAL   A C   
664  O  O   . VAL   A 86  ? 0.20562 0.26340 0.18990 -0.05798 0.02665  0.06795  86  VAL   A O   
665  C  CB  . VAL   A 86  ? 0.19049 0.23462 0.16503 -0.04242 0.00907  0.04760  86  VAL   A CB  
666  C  CG1 . VAL   A 86  ? 0.21444 0.26219 0.18247 -0.03525 0.00561  0.03834  86  VAL   A CG1 
667  C  CG2 . VAL   A 86  ? 0.18920 0.23526 0.18172 -0.04821 0.00905  0.04382  86  VAL   A CG2 
668  N  N   . LEU   A 87  ? 0.18480 0.22114 0.15041 -0.05231 0.01736  0.07505  87  LEU   A N   
669  C  CA  . LEU   A 87  ? 0.19750 0.22516 0.17142 -0.05890 0.01934  0.08715  87  LEU   A CA  
670  C  C   . LEU   A 87  ? 0.25213 0.26454 0.24206 -0.05941 0.01368  0.08376  87  LEU   A C   
671  O  O   . LEU   A 87  ? 0.21744 0.22387 0.20568 -0.05305 0.00752  0.07726  87  LEU   A O   
672  C  CB  . LEU   A 87  ? 0.27746 0.29848 0.23658 -0.05524 0.01824  0.09642  87  LEU   A CB  
673  C  CG  . LEU   A 87  ? 0.29062 0.31764 0.23830 -0.05599 0.02551  0.10092  87  LEU   A CG  
674  C  CD1 . LEU   A 87  ? 0.33074 0.34911 0.26581 -0.05314 0.02152  0.11011  87  LEU   A CD1 
675  C  CD2 . LEU   A 87  ? 0.32738 0.35742 0.28996 -0.06360 0.03337  0.10531  87  LEU   A CD2 
676  N  N   . LYS   A 88  ? 0.22261 0.22814 0.22822 -0.06727 0.01653  0.08801  88  LYS   A N   
677  C  CA  . LYS   A 88  ? 0.27251 0.25949 0.29277 -0.06863 0.01289  0.08514  88  LYS   A CA  
678  C  C   . LYS   A 88  ? 0.27258 0.24505 0.29735 -0.07203 0.01493  0.10192  88  LYS   A C   
679  O  O   . LYS   A 88  ? 0.31096 0.28477 0.34085 -0.07823 0.02052  0.10665  88  LYS   A O   
680  C  CB  . LYS   A 88  ? 0.28232 0.27097 0.31831 -0.07607 0.01344  0.07336  88  LYS   A CB  
681  C  CG  . LYS   A 88  ? 0.24773 0.25174 0.28000 -0.07256 0.01069  0.05912  88  LYS   A CG  
682  C  CD  . LYS   A 88  ? 0.28834 0.29616 0.33533 -0.08100 0.00943  0.04866  88  LYS   A CD  
683  C  CE  . LYS   A 88  ? 0.31264 0.29940 0.36771 -0.08379 0.00622  0.04108  88  LYS   A CE  
684  N  NZ  . LYS   A 88  ? 0.39584 0.38828 0.45886 -0.09098 0.00263  0.02691  88  LYS   A NZ  
685  N  N   . LEU   A 89  ? 0.28602 0.24581 0.30834 -0.06466 0.01040  0.10743  89  LEU   A N   
686  C  CA  . LEU   A 89  ? 0.30476 0.25180 0.32916 -0.06259 0.01117  0.11916  89  LEU   A CA  
687  C  C   . LEU   A 89  ? 0.31923 0.24394 0.36351 -0.06355 0.01098  0.11590  89  LEU   A C   
688  O  O   . LEU   A 89  ? 0.32758 0.24317 0.37760 -0.05712 0.00713  0.11085  89  LEU   A O   
689  C  CB  . LEU   A 89  ? 0.31781 0.26822 0.32797 -0.05314 0.00581  0.12655  89  LEU   A CB  
690  C  CG  . LEU   A 89  ? 0.33096 0.30012 0.31884 -0.05210 0.00630  0.12711  89  LEU   A CG  
691  C  CD1 . LEU   A 89  ? 0.33361 0.30478 0.30873 -0.04487 0.00011  0.13361  89  LEU   A CD1 
692  C  CD2 . LEU   A 89  ? 0.32258 0.29767 0.30683 -0.05906 0.01435  0.13157  89  LEU   A CD2 
693  N  N   . LYS   A 90  ? 0.33684 0.25229 0.39138 -0.07130 0.01578  0.11773  90  LYS   A N   
694  C  CA  . LYS   A 90  ? 0.37104 0.26301 0.44242 -0.07286 0.01657  0.11286  90  LYS   A CA  
695  C  C   . LYS   A 90  ? 0.38444 0.26320 0.45711 -0.06426 0.01504  0.12514  90  LYS   A C   
696  O  O   . LYS   A 90  ? 0.42930 0.31149 0.49543 -0.06456 0.01619  0.13914  90  LYS   A O   
697  C  CB  . LYS   A 90  ? 0.37328 0.26136 0.45391 -0.08538 0.02163  0.11022  90  LYS   A CB  
698  C  CG  . LYS   A 90  ? 0.41411 0.27857 0.50973 -0.08996 0.02256  0.10042  90  LYS   A CG  
699  C  CD  . LYS   A 90  ? 0.43022 0.29658 0.53025 -0.09469 0.02040  0.08033  90  LYS   A CD  
700  C  CE  . LYS   A 90  ? 0.43312 0.27638 0.54395 -0.10160 0.02155  0.06873  90  LYS   A CE  
701  N  NZ  . LYS   A 90  ? 0.49706 0.31945 0.61338 -0.09874 0.02438  0.08061  90  LYS   A NZ  
702  N  N   . VAL   A 91  ? 0.38284 0.24863 0.46396 -0.05605 0.01251  0.12002  91  VAL   A N   
703  C  CA  . VAL   A 91  ? 0.40072 0.25669 0.48660 -0.04671 0.01062  0.13129  91  VAL   A CA  
704  C  C   . VAL   A 91  ? 0.42084 0.25102 0.52435 -0.04745 0.01446  0.12576  91  VAL   A C   
705  O  O   . VAL   A 91  ? 0.41352 0.23372 0.52334 -0.05364 0.01729  0.11003  91  VAL   A O   
706  C  CB  . VAL   A 91  ? 0.41472 0.27994 0.49708 -0.03493 0.00491  0.13146  91  VAL   A CB  
707  C  CG1 . VAL   A 91  ? 0.39704 0.28623 0.45961 -0.03543 0.00098  0.13557  91  VAL   A CG1 
708  C  CG2 . VAL   A 91  ? 0.36278 0.22077 0.45385 -0.03206 0.00573  0.11434  91  VAL   A CG2 
709  N  N   . ASP   A 92  ? 0.44085 0.26039 0.55158 -0.04181 0.01439  0.13852  92  ASP   A N   
710  C  CA  . ASP   A 92  ? 0.48241 0.27598 0.60959 -0.04245 0.01867  0.13425  92  ASP   A CA  
711  C  C   . ASP   A 92  ? 0.48312 0.26529 0.62129 -0.03265 0.01939  0.12177  92  ASP   A C   
712  O  O   . ASP   A 92  ? 0.51462 0.27423 0.66546 -0.03253 0.02372  0.11510  92  ASP   A O   
713  C  CB  . ASP   A 92  ? 0.51549 0.30044 0.64864 -0.04012 0.01904  0.15328  92  ASP   A CB  
714  C  CG  . ASP   A 92  ? 0.52520 0.32029 0.65862 -0.02713 0.01374  0.16656  92  ASP   A CG  
715  O  OD1 . ASP   A 92  ? 0.58639 0.38785 0.71500 -0.02683 0.01143  0.18443  92  ASP   A OD1 
716  O  OD2 . ASP   A 92  ? 0.55622 0.35531 0.69376 -0.01790 0.01153  0.15930  92  ASP   A OD2 
717  N  N   . THR   A 93  ? 0.45597 0.25296 0.58960 -0.02432 0.01582  0.11864  93  THR   A N   
718  C  CA  . THR   A 93  ? 0.45687 0.24638 0.60094 -0.01394 0.01746  0.10788  93  THR   A CA  
719  C  C   . THR   A 93  ? 0.40126 0.19927 0.53757 -0.01582 0.01739  0.09044  93  THR   A C   
720  O  O   . THR   A 93  ? 0.36051 0.17861 0.48487 -0.01694 0.01282  0.09381  93  THR   A O   
721  C  CB  . THR   A 93  ? 0.43491 0.23581 0.58394 -0.00112 0.01312  0.12183  93  THR   A CB  
722  O  OG1 . THR   A 93  ? 0.52317 0.31944 0.67727 -0.00051 0.01201  0.13993  93  THR   A OG1 
723  C  CG2 . THR   A 93  ? 0.46965 0.26214 0.63337 0.00993  0.01681  0.11179  93  THR   A CG2 
724  N  N   . ALA   A 94  ? 0.40470 0.18734 0.54649 -0.01652 0.02251  0.07143  94  ALA   A N   
725  C  CA  . ALA   A 94  ? 0.35936 0.14960 0.49432 -0.01659 0.02283  0.05423  94  ALA   A CA  
726  C  C   . ALA   A 94  ? 0.38002 0.17910 0.51970 -0.00232 0.02236  0.05581  94  ALA   A C   
727  O  O   . ALA   A 94  ? 0.40926 0.20000 0.56164 0.00725  0.02520  0.05979  94  ALA   A O   
728  C  CB  . ALA   A 94  ? 0.38460 0.15735 0.51988 -0.02305 0.02813  0.03205  94  ALA   A CB  
729  N  N   . ASN   A 95  ? 0.35492 0.17187 0.48570 -0.00123 0.01877  0.05330  95  ASN   A N   
730  C  CA  . ASN   A 95  ? 0.31863 0.14760 0.45323 0.01092  0.01762  0.05470  95  ASN   A CA  
731  C  C   . ASN   A 95  ? 0.34104 0.15824 0.48305 0.01715  0.02580  0.03695  95  ASN   A C   
732  O  O   . ASN   A 95  ? 0.35425 0.16896 0.48759 0.01225  0.02913  0.01836  95  ASN   A O   
733  C  CB  . ASN   A 95  ? 0.29521 0.14369 0.41745 0.00874  0.01218  0.05433  95  ASN   A CB  
734  C  CG  . ASN   A 95  ? 0.26694 0.13082 0.39274 0.02013  0.00969  0.05754  95  ASN   A CG  
735  O  OD1 . ASN   A 95  ? 0.28099 0.14294 0.41964 0.02950  0.01246  0.05979  95  ASN   A OD1 
736  N  ND2 . ASN   A 95  ? 0.25049 0.13734 0.35912 0.01779  0.00407  0.05478  95  ASN   A ND2 
737  N  N   . PRO   A 96  ? 0.34951 0.16124 0.50610 0.02756  0.02938  0.04146  96  PRO   A N   
738  C  CA  . PRO   A 96  ? 0.34205 0.14330 0.50416 0.03350  0.03861  0.02413  96  PRO   A CA  
739  C  C   . PRO   A 96  ? 0.33135 0.14845 0.48784 0.03842  0.04005  0.01441  96  PRO   A C   
740  O  O   . PRO   A 96  ? 0.34250 0.15306 0.49724 0.04102  0.04829  -0.00288 96  PRO   A O   
741  C  CB  . PRO   A 96  ? 0.36774 0.16338 0.54931 0.04405  0.04121  0.03581  96  PRO   A CB  
742  C  CG  . PRO   A 96  ? 0.36723 0.18039 0.55171 0.04611  0.03152  0.05894  96  PRO   A CG  
743  C  CD  . PRO   A 96  ? 0.32699 0.14510 0.49473 0.03438  0.02492  0.06266  96  PRO   A CD  
744  N  N   . LYS   A 97  ? 0.31810 0.15599 0.47015 0.03924  0.03241  0.02479  97  LYS   A N   
745  C  CA  . LYS   A 97  ? 0.30515 0.15901 0.45223 0.04335  0.03320  0.01709  97  LYS   A CA  
746  C  C   . LYS   A 97  ? 0.27230 0.13140 0.39878 0.03299  0.03103  0.00444  97  LYS   A C   
747  O  O   . LYS   A 97  ? 0.29095 0.17033 0.40637 0.03380  0.02861  0.00062  97  LYS   A O   
748  C  CB  . LYS   A 97  ? 0.28470 0.16141 0.43792 0.04981  0.02501  0.03519  97  LYS   A CB  
749  C  CG  . LYS   A 97  ? 0.31261 0.19176 0.48420 0.05922  0.02631  0.04578  97  LYS   A CG  
750  C  CD  . LYS   A 97  ? 0.33177 0.23353 0.50539 0.06090  0.01510  0.06472  97  LYS   A CD  
751  C  CE  . LYS   A 97  ? 0.32459 0.22856 0.51719 0.06854  0.01508  0.07677  97  LYS   A CE  
752  N  NZ  . LYS   A 97  ? 0.41570 0.34192 0.61736 0.07453  0.01245  0.08127  97  LYS   A NZ  
753  N  N   . THR   A 98  ? 0.30422 0.15131 0.42189 0.02164  0.03048  -0.00172 98  THR   A N   
754  C  CA  . THR   A 98  ? 0.29779 0.15784 0.39309 0.01053  0.02631  -0.01258 98  THR   A CA  
755  C  C   . THR   A 98  ? 0.26870 0.13223 0.35365 0.01158  0.03188  -0.03203 98  THR   A C   
756  O  O   . THR   A 98  ? 0.30118 0.14552 0.38906 0.01147  0.04030  -0.04668 98  THR   A O   
757  C  CB  . THR   A 98  ? 0.29286 0.13940 0.38504 -0.00204 0.02558  -0.01649 98  THR   A CB  
758  O  OG1 . THR   A 98  ? 0.32817 0.17162 0.42925 -0.00311 0.02163  0.00291  98  THR   A OG1 
759  C  CG2 . THR   A 98  ? 0.30164 0.16634 0.37385 -0.01277 0.01996  -0.02462 98  THR   A CG2 
760  N  N   . PRO   A 99  ? 0.26576 0.15191 0.33795 0.01237  0.02811  -0.03295 99  PRO   A N   
761  C  CA  . PRO   A 99  ? 0.29382 0.18461 0.35334 0.01201  0.03313  -0.04997 99  PRO   A CA  
762  C  C   . PRO   A 99  ? 0.28430 0.17462 0.32655 -0.00095 0.03013  -0.06266 99  PRO   A C   
763  O  O   . PRO   A 99  ? 0.29454 0.18578 0.33547 -0.00920 0.02377  -0.05703 99  PRO   A O   
764  C  CB  . PRO   A 99  ? 0.23772 0.15315 0.29162 0.01637  0.02864  -0.04230 99  PRO   A CB  
765  C  CG  . PRO   A 99  ? 0.24193 0.16680 0.29371 0.01201  0.01896  -0.02857 99  PRO   A CG  
766  C  CD  . PRO   A 99  ? 0.24319 0.15090 0.30884 0.01157  0.01892  -0.01960 99  PRO   A CD  
767  N  N   . LYS   A 100 ? 0.29370 0.18464 0.32262 -0.00294 0.03468  -0.07930 100 LYS   A N   
768  C  CA  . LYS   A 100 ? 0.29929 0.19881 0.30992 -0.01503 0.02885  -0.08874 100 LYS   A CA  
769  C  C   . LYS   A 100 ? 0.28886 0.21328 0.29280 -0.01587 0.01989  -0.07686 100 LYS   A C   
770  O  O   . LYS   A 100 ? 0.24380 0.18096 0.24780 -0.00799 0.02014  -0.06976 100 LYS   A O   
771  C  CB  . LYS   A 100 ? 0.35237 0.25038 0.34665 -0.01708 0.03457  -0.10771 100 LYS   A CB  
772  C  CG  . LYS   A 100 ? 0.36567 0.24285 0.36654 -0.01186 0.04391  -0.11477 100 LYS   A CG  
773  C  CD  . LYS   A 100 ? 0.49029 0.36916 0.47102 -0.01495 0.04606  -0.12822 100 LYS   A CD  
774  C  CE  . LYS   A 100 ? 0.50977 0.38188 0.49463 -0.00337 0.05775  -0.13204 100 LYS   A CE  
775  N  NZ  . LYS   A 100 ? 0.59583 0.44305 0.59590 0.00001  0.06419  -0.13488 100 LYS   A NZ  
776  N  N   . TYR   A 101 ? 0.25268 0.18345 0.25334 -0.02530 0.01246  -0.07393 101 TYR   A N   
777  C  CA  . TYR   A 101 ? 0.25401 0.20597 0.25048 -0.02496 0.00543  -0.06266 101 TYR   A CA  
778  C  C   . TYR   A 101 ? 0.25609 0.21979 0.24393 -0.03557 -0.00102 -0.06681 101 TYR   A C   
779  O  O   . TYR   A 101 ? 0.22269 0.17835 0.20940 -0.04482 -0.00154 -0.07674 101 TYR   A O   
780  C  CB  . TYR   A 101 ? 0.24373 0.19493 0.25175 -0.02158 0.00332  -0.04655 101 TYR   A CB  
781  C  CG  . TYR   A 101 ? 0.26458 0.20670 0.27973 -0.02977 0.00181  -0.04329 101 TYR   A CG  
782  C  CD1 . TYR   A 101 ? 0.26686 0.18699 0.29352 -0.03031 0.00644  -0.04429 101 TYR   A CD1 
783  C  CD2 . TYR   A 101 ? 0.25395 0.20969 0.26620 -0.03653 -0.00342 -0.03805 101 TYR   A CD2 
784  C  CE1 . TYR   A 101 ? 0.30803 0.21938 0.34237 -0.03858 0.00548  -0.03983 101 TYR   A CE1 
785  C  CE2 . TYR   A 101 ? 0.23615 0.18530 0.25644 -0.04456 -0.00382 -0.03385 101 TYR   A CE2 
786  C  CZ  . TYR   A 101 ? 0.28384 0.21065 0.31471 -0.04609 0.00039  -0.03453 101 TYR   A CZ  
787  O  OH  . TYR   A 101 ? 0.34424 0.26403 0.38401 -0.05500 0.00034  -0.02930 101 TYR   A OH  
788  N  N   . LYS   A 102 ? 0.22859 0.21159 0.21202 -0.03409 -0.00607 -0.05864 102 LYS   A N   
789  C  CA  . LYS   A 102 ? 0.22653 0.22541 0.20642 -0.04146 -0.01258 -0.05760 102 LYS   A CA  
790  C  C   . LYS   A 102 ? 0.21480 0.22485 0.19892 -0.03716 -0.01478 -0.04394 102 LYS   A C   
791  O  O   . LYS   A 102 ? 0.19212 0.20202 0.17612 -0.02900 -0.01305 -0.03761 102 LYS   A O   
792  C  CB  . LYS   A 102 ? 0.26520 0.27859 0.23159 -0.04296 -0.01587 -0.06427 102 LYS   A CB  
793  C  CG  . LYS   A 102 ? 0.32202 0.32586 0.27894 -0.04298 -0.01190 -0.07606 102 LYS   A CG  
794  C  CD  . LYS   A 102 ? 0.32413 0.33954 0.27122 -0.04481 -0.01667 -0.07550 102 LYS   A CD  
795  C  CE  . LYS   A 102 ? 0.30712 0.33361 0.24701 -0.03700 -0.01599 -0.06872 102 LYS   A CE  
796  N  NZ  . LYS   A 102 ? 0.36437 0.39088 0.29079 -0.03799 -0.01534 -0.07473 102 LYS   A NZ  
797  N  N   . PHE   A 103 ? 0.20045 0.22083 0.18854 -0.04318 -0.01836 -0.04011 103 PHE   A N   
798  C  CA  . PHE   A 103 ? 0.14308 0.17618 0.13305 -0.03965 -0.01960 -0.02961 103 PHE   A CA  
799  C  C   . PHE   A 103 ? 0.17180 0.22354 0.15726 -0.03969 -0.02390 -0.03064 103 PHE   A C   
800  O  O   . PHE   A 103 ? 0.17131 0.23260 0.16021 -0.04651 -0.02746 -0.03303 103 PHE   A O   
801  C  CB  . PHE   A 103 ? 0.16555 0.19927 0.16497 -0.04537 -0.01884 -0.02346 103 PHE   A CB  
802  C  CG  . PHE   A 103 ? 0.16312 0.18090 0.16698 -0.04421 -0.01498 -0.01751 103 PHE   A CG  
803  C  CD1 . PHE   A 103 ? 0.14998 0.15589 0.15143 -0.03713 -0.01310 -0.01663 103 PHE   A CD1 
804  C  CD2 . PHE   A 103 ? 0.16860 0.18518 0.18044 -0.05022 -0.01328 -0.01105 103 PHE   A CD2 
805  C  CE1 . PHE   A 103 ? 0.18282 0.17576 0.18975 -0.03557 -0.01068 -0.00895 103 PHE   A CE1 
806  C  CE2 . PHE   A 103 ? 0.19289 0.19537 0.20821 -0.04912 -0.01014 -0.00307 103 PHE   A CE2 
807  C  CZ  . PHE   A 103 ? 0.16189 0.15261 0.17477 -0.04160 -0.00942 -0.00175 103 PHE   A CZ  
808  N  N   . VAL   A 104 ? 0.11200 0.16887 0.09170 -0.03196 -0.02379 -0.02720 104 VAL   A N   
809  C  CA  . VAL   A 104 ? 0.15706 0.22239 0.13541 -0.02734 -0.02476 -0.02353 104 VAL   A CA  
810  C  C   . VAL   A 104 ? 0.14647 0.21638 0.12794 -0.02134 -0.02311 -0.01541 104 VAL   A C   
811  O  O   . VAL   A 104 ? 0.21543 0.27986 0.19514 -0.01829 -0.02129 -0.01309 104 VAL   A O   
812  C  CB  . VAL   A 104 ? 0.16957 0.23040 0.13983 -0.02347 -0.02368 -0.02626 104 VAL   A CB  
813  C  CG1 . VAL   A 104 ? 0.17977 0.23248 0.14462 -0.02865 -0.02315 -0.03676 104 VAL   A CG1 
814  C  CG2 . VAL   A 104 ? 0.18303 0.23953 0.15171 -0.01663 -0.02082 -0.02221 104 VAL   A CG2 
815  N  N   . ARG   A 105 ? 0.11240 0.19231 0.09829 -0.01992 -0.02388 -0.01152 105 ARG   A N   
816  C  CA  . ARG   A 105 ? 0.09199 0.17519 0.08022 -0.01399 -0.02158 -0.00581 105 ARG   A CA  
817  C  C   . ARG   A 105 ? 0.12080 0.20166 0.10629 -0.00917 -0.02141 -0.00399 105 ARG   A C   
818  O  O   . ARG   A 105 ? 0.13083 0.21707 0.11605 -0.01056 -0.02398 -0.00413 105 ARG   A O   
819  C  CB  . ARG   A 105 ? 0.11718 0.21588 0.11460 -0.01541 -0.02211 -0.00228 105 ARG   A CB  
820  C  CG  . ARG   A 105 ? 0.10513 0.20844 0.10466 -0.00924 -0.01894 0.00215  105 ARG   A CG  
821  C  CD  . ARG   A 105 ? 0.08196 0.20460 0.09461 -0.00982 -0.01869 0.00614  105 ARG   A CD  
822  N  NE  . ARG   A 105 ? 0.11294 0.24123 0.12946 -0.00201 -0.01453 0.00982  105 ARG   A NE  
823  C  CZ  . ARG   A 105 ? 0.10489 0.22577 0.11829 -0.00059 -0.00739 0.00953  105 ARG   A CZ  
824  N  NH1 . ARG   A 105 ? 0.09107 0.20408 0.09863 -0.00625 -0.00590 0.00797  105 ARG   A NH1 
825  N  NH2 . ARG   A 105 ? 0.10685 0.22708 0.12195 0.00676  -0.00138 0.01085  105 ARG   A NH2 
826  N  N   . ILE   A 106 ? 0.17845 0.25199 0.16181 -0.00454 -0.01894 -0.00203 106 ILE   A N   
827  C  CA  . ILE   A 106 ? 0.15611 0.22777 0.13778 -0.00125 -0.01876 0.00023  106 ILE   A CA  
828  C  C   . ILE   A 106 ? 0.14794 0.22743 0.13448 0.00256  -0.01870 0.00501  106 ILE   A C   
829  O  O   . ILE   A 106 ? 0.14358 0.22912 0.13423 0.00382  -0.01777 0.00613  106 ILE   A O   
830  C  CB  . ILE   A 106 ? 0.14137 0.20223 0.11955 0.00058  -0.01688 -0.00018 106 ILE   A CB  
831  C  CG1 . ILE   A 106 ? 0.13735 0.19357 0.11606 0.00218  -0.01553 0.00069  106 ILE   A CG1 
832  C  CG2 . ILE   A 106 ? 0.20398 0.26062 0.17834 -0.00173 -0.01693 -0.00411 106 ILE   A CG2 
833  C  CD1 . ILE   A 106 ? 0.19989 0.24737 0.17624 0.00349  -0.01504 0.00131  106 ILE   A CD1 
834  N  N   . GLN   A 107 ? 0.12525 0.20582 0.11136 0.00495  -0.01945 0.00837  107 GLN   A N   
835  C  CA  . GLN   A 107 ? 0.15989 0.24636 0.15069 0.00986  -0.01978 0.01437  107 GLN   A CA  
836  C  C   . GLN   A 107 ? 0.17084 0.24874 0.15975 0.01354  -0.01776 0.01545  107 GLN   A C   
837  O  O   . GLN   A 107 ? 0.17361 0.24251 0.15745 0.01159  -0.01713 0.01327  107 GLN   A O   
838  C  CB  . GLN   A 107 ? 0.17137 0.26316 0.16150 0.00957  -0.02250 0.01834  107 GLN   A CB  
839  C  CG  . GLN   A 107 ? 0.18291 0.28563 0.17553 0.00627  -0.02602 0.01830  107 GLN   A CG  
840  C  CD  . GLN   A 107 ? 0.16601 0.27993 0.16997 0.00968  -0.02670 0.02323  107 GLN   A CD  
841  O  OE1 . GLN   A 107 ? 0.17352 0.28842 0.18315 0.01580  -0.02549 0.02903  107 GLN   A OE1 
842  N  NE2 . GLN   A 107 ? 0.15012 0.27288 0.15929 0.00618  -0.02830 0.02144  107 GLN   A NE2 
843  N  N   . PRO   A 108 ? 0.15262 0.23407 0.14645 0.01954  -0.01691 0.01928  108 PRO   A N   
844  C  CA  . PRO   A 108 ? 0.20709 0.28056 0.19911 0.02384  -0.01618 0.02174  108 PRO   A CA  
845  C  C   . PRO   A 108 ? 0.15894 0.22912 0.14938 0.02201  -0.01743 0.02554  108 PRO   A C   
846  O  O   . PRO   A 108 ? 0.20231 0.27913 0.19482 0.02117  -0.01887 0.02900  108 PRO   A O   
847  C  CB  . PRO   A 108 ? 0.17158 0.24918 0.17386 0.03283  -0.01392 0.02670  108 PRO   A CB  
848  C  CG  . PRO   A 108 ? 0.23248 0.32532 0.24345 0.03289  -0.01449 0.02834  108 PRO   A CG  
849  C  CD  . PRO   A 108 ? 0.18248 0.27614 0.18582 0.02381  -0.01623 0.02211  108 PRO   A CD  
850  N  N   . GLY   A 109 ? 0.14623 0.20774 0.13239 0.02115  -0.01716 0.02530  109 GLY   A N   
851  C  CA  . GLY   A 109 ? 0.17927 0.23966 0.16377 0.01915  -0.01742 0.02905  109 GLY   A CA  
852  C  C   . GLY   A 109 ? 0.21154 0.27097 0.19087 0.01382  -0.01668 0.02351  109 GLY   A C   
853  O  O   . GLY   A 109 ? 0.18137 0.24021 0.15898 0.01267  -0.01591 0.02604  109 GLY   A O   
854  N  N   . GLN   A 110 ? 0.13341 0.19330 0.11160 0.01130  -0.01643 0.01729  110 GLN   A N   
855  C  CA  . GLN   A 110 ? 0.18309 0.24140 0.15806 0.00809  -0.01537 0.01285  110 GLN   A CA  
856  C  C   . GLN   A 110 ? 0.14265 0.19400 0.11774 0.00724  -0.01483 0.01021  110 GLN   A C   
857  O  O   . GLN   A 110 ? 0.11490 0.16162 0.09059 0.00778  -0.01564 0.00963  110 GLN   A O   
858  C  CB  . GLN   A 110 ? 0.15236 0.21364 0.12644 0.00588  -0.01593 0.00868  110 GLN   A CB  
859  C  CG  . GLN   A 110 ? 0.18688 0.25686 0.15974 0.00545  -0.01781 0.01104  110 GLN   A CG  
860  C  CD  . GLN   A 110 ? 0.28129 0.35471 0.25206 0.00199  -0.01942 0.00640  110 GLN   A CD  
861  O  OE1 . GLN   A 110 ? 0.17991 0.25394 0.15426 0.00099  -0.02011 0.00452  110 GLN   A OE1 
862  N  NE2 . GLN   A 110 ? 0.37470 0.45089 0.33861 -0.00028 -0.01995 0.00432  110 GLN   A NE2 
863  N  N   . THR   A 111 ? 0.12934 0.18198 0.10329 0.00618  -0.01371 0.00921  111 THR   A N   
864  C  CA  . THR   A 111 ? 0.13378 0.18323 0.10934 0.00557  -0.01415 0.00821  111 THR   A CA  
865  C  C   . THR   A 111 ? 0.16543 0.21422 0.14061 0.00484  -0.01388 0.00404  111 THR   A C   
866  O  O   . THR   A 111 ? 0.12305 0.17430 0.09579 0.00430  -0.01302 0.00120  111 THR   A O   
867  C  CB  . THR   A 111 ? 0.12924 0.18525 0.10608 0.00579  -0.01320 0.01201  111 THR   A CB  
868  O  OG1 . THR   A 111 ? 0.18825 0.25179 0.16139 0.00627  -0.01029 0.01120  111 THR   A OG1 
869  C  CG2 . THR   A 111 ? 0.13769 0.19342 0.11563 0.00600  -0.01414 0.01788  111 THR   A CG2 
870  N  N   . PHE   A 112 ? 0.14930 0.19555 0.12678 0.00457  -0.01548 0.00419  112 PHE   A N   
871  C  CA  . PHE   A 112 ? 0.14944 0.19688 0.12750 0.00480  -0.01612 0.00206  112 PHE   A CA  
872  C  C   . PHE   A 112 ? 0.14766 0.19606 0.13109 0.00514  -0.01908 0.00525  112 PHE   A C   
873  O  O   . PHE   A 112 ? 0.14629 0.19139 0.13124 0.00367  -0.02101 0.00758  112 PHE   A O   
874  C  CB  . PHE   A 112 ? 0.13760 0.17957 0.11347 0.00330  -0.01669 0.00004  112 PHE   A CB  
875  C  CG  . PHE   A 112 ? 0.16994 0.20509 0.14478 0.00232  -0.01778 0.00159  112 PHE   A CG  
876  C  CD1 . PHE   A 112 ? 0.18707 0.22174 0.16096 0.00271  -0.01673 0.00176  112 PHE   A CD1 
877  C  CD2 . PHE   A 112 ? 0.11614 0.14741 0.08984 0.00148  -0.02000 0.00277  112 PHE   A CD2 
878  C  CE1 . PHE   A 112 ? 0.16007 0.19126 0.13109 0.00253  -0.01715 0.00185  112 PHE   A CE1 
879  C  CE2 . PHE   A 112 ? 0.15338 0.17973 0.12272 0.00068  -0.02042 0.00287  112 PHE   A CE2 
880  C  CZ  . PHE   A 112 ? 0.12836 0.15500 0.09602 0.00121  -0.01860 0.00184  112 PHE   A CZ  
881  N  N   . SER   A 113 ? 0.13493 0.18620 0.12302 0.00699  -0.01934 0.00520  113 SER   A N   
882  C  CA  . SER   A 113 ? 0.13504 0.18651 0.13249 0.00754  -0.02230 0.00998  113 SER   A CA  
883  C  C   . SER   A 113 ? 0.11226 0.15845 0.10579 0.00587  -0.02651 0.01181  113 SER   A C   
884  O  O   . SER   A 113 ? 0.13382 0.17553 0.12297 0.00553  -0.02468 0.00911  113 SER   A O   
885  C  CB  . SER   A 113 ? 0.12635 0.17963 0.13556 0.01154  -0.01758 0.00998  113 SER   A CB  
886  O  OG  . SER   A 113 ? 0.12295 0.18166 0.13279 0.01287  -0.01187 0.00767  113 SER   A OG  
887  N  N   . VAL   A 114 ? 0.10369 0.14700 0.09872 0.00407  -0.03048 0.01524  114 VAL   A N   
888  C  CA  . VAL   A 114 ? 0.14240 0.17967 0.13194 0.00260  -0.03296 0.01681  114 VAL   A CA  
889  C  C   . VAL   A 114 ? 0.15170 0.19311 0.15188 0.00397  -0.03681 0.02387  114 VAL   A C   
890  O  O   . VAL   A 114 ? 0.12478 0.17136 0.13354 0.00408  -0.03853 0.02590  114 VAL   A O   
891  C  CB  . VAL   A 114 ? 0.12558 0.15706 0.10557 0.00020  -0.03319 0.01330  114 VAL   A CB  
892  C  CG1 . VAL   A 114 ? 0.17501 0.20430 0.14878 -0.00125 -0.03545 0.01573  114 VAL   A CG1 
893  C  CG2 . VAL   A 114 ? 0.17897 0.20572 0.15233 0.00016  -0.02933 0.00846  114 VAL   A CG2 
894  N  N   . LEU   A 115 ? 0.13847 0.17788 0.14042 0.00508  -0.03806 0.02885  115 LEU   A N   
895  C  CA  . LEU   A 115 ? 0.13793 0.17915 0.15053 0.00696  -0.04152 0.03699  115 LEU   A CA  
896  C  C   . LEU   A 115 ? 0.16256 0.20022 0.16250 0.00295  -0.04431 0.03849  115 LEU   A C   
897  O  O   . LEU   A 115 ? 0.14133 0.17427 0.13443 0.00192  -0.04368 0.04089  115 LEU   A O   
898  C  CB  . LEU   A 115 ? 0.12876 0.16752 0.15523 0.01222  -0.03991 0.04272  115 LEU   A CB  
899  C  CG  . LEU   A 115 ? 0.13016 0.16913 0.16999 0.01547  -0.04245 0.05225  115 LEU   A CG  
900  C  CD1 . LEU   A 115 ? 0.15357 0.20193 0.20699 0.01774  -0.04288 0.05327  115 LEU   A CD1 
901  C  CD2 . LEU   A 115 ? 0.17126 0.20042 0.22402 0.02100  -0.03767 0.05547  115 LEU   A CD2 
902  N  N   . ALA   A 116 ? 0.15534 0.19585 0.15178 0.00023  -0.04724 0.03707  116 ALA   A N   
903  C  CA  . ALA   A 116 ? 0.15510 0.19376 0.13896 -0.00332 -0.05005 0.03795  116 ALA   A CA  
904  C  C   . ALA   A 116 ? 0.20782 0.24895 0.19761 -0.00247 -0.05418 0.04818  116 ALA   A C   
905  O  O   . ALA   A 116 ? 0.22150 0.26841 0.22645 -0.00012 -0.05699 0.05386  116 ALA   A O   
906  C  CB  . ALA   A 116 ? 0.16756 0.20887 0.14705 -0.00685 -0.05329 0.03409  116 ALA   A CB  
907  N  N   . CYS   A 117 ? 0.14033 0.17765 0.11938 -0.00411 -0.05414 0.05134  117 CYS   A N   
908  C  CA  . CYS   A 117 ? 0.21420 0.25305 0.19767 -0.00347 -0.05800 0.06243  117 CYS   A CA  
909  C  C   . CYS   A 117 ? 0.25780 0.29641 0.22403 -0.00766 -0.06042 0.06439  117 CYS   A C   
910  O  O   . CYS   A 117 ? 0.22560 0.26076 0.17641 -0.01025 -0.05716 0.05746  117 CYS   A O   
911  C  CB  . CYS   A 117 ? 0.26964 0.30289 0.26216 -0.00008 -0.05494 0.06911  117 CYS   A CB  
912  S  SG  . CYS   A 117 ? 0.29097 0.32074 0.29790 0.00465  -0.05009 0.06542  117 CYS   A SG  
913  N  N   . TYR   A 118 ? 0.26270 0.30546 0.23281 -0.00766 -0.06591 0.07476  118 TYR   A N   
914  C  CA  . TYR   A 118 ? 0.27459 0.31871 0.22889 -0.01141 -0.06940 0.07931  118 TYR   A CA  
915  C  C   . TYR   A 118 ? 0.29889 0.34295 0.26207 -0.00912 -0.07138 0.09331  118 TYR   A C   
916  O  O   . TYR   A 118 ? 0.28353 0.33079 0.26630 -0.00510 -0.07395 0.10004  118 TYR   A O   
917  C  CB  . TYR   A 118 ? 0.29745 0.34911 0.24605 -0.01501 -0.07663 0.07748  118 TYR   A CB  
918  C  CG  . TYR   A 118 ? 0.30769 0.35743 0.25072 -0.01677 -0.07407 0.06427  118 TYR   A CG  
919  C  CD1 . TYR   A 118 ? 0.28476 0.33698 0.24296 -0.01499 -0.07385 0.06064  118 TYR   A CD1 
920  C  CD2 . TYR   A 118 ? 0.31389 0.35895 0.23741 -0.01969 -0.07107 0.05602  118 TYR   A CD2 
921  C  CE1 . TYR   A 118 ? 0.26446 0.31407 0.21837 -0.01652 -0.07118 0.04985  118 TYR   A CE1 
922  C  CE2 . TYR   A 118 ? 0.30281 0.34492 0.22311 -0.02053 -0.06833 0.04485  118 TYR   A CE2 
923  C  CZ  . TYR   A 118 ? 0.29642 0.34062 0.23187 -0.01918 -0.06870 0.04216  118 TYR   A CZ  
924  O  OH  . TYR   A 118 ? 0.28912 0.32990 0.22149 -0.02025 -0.06605 0.03229  118 TYR   A OH  
925  N  N   . ASN   A 119 ? 0.31784 0.35773 0.26832 -0.01112 -0.06917 0.09802  119 ASN   A N   
926  C  CA  . ASN   A 119 ? 0.29921 0.33760 0.25723 -0.00929 -0.07069 0.11256  119 ASN   A CA  
927  C  C   . ASN   A 119 ? 0.31368 0.34581 0.29468 -0.00366 -0.06705 0.11658  119 ASN   A C   
928  O  O   . ASN   A 119 ? 0.32014 0.35214 0.31656 0.00012  -0.06954 0.12809  119 ASN   A O   
929  C  CB  . ASN   A 119 ? 0.34342 0.39116 0.30330 -0.00979 -0.07991 0.12230  119 ASN   A CB  
930  C  CG  . ASN   A 119 ? 0.38469 0.43765 0.32077 -0.01566 -0.08405 0.11833  119 ASN   A CG  
931  O  OD1 . ASN   A 119 ? 0.43319 0.48311 0.35088 -0.01863 -0.08152 0.11994  119 ASN   A OD1 
932  N  ND2 . ASN   A 119 ? 0.38567 0.44599 0.32169 -0.01757 -0.08979 0.11268  119 ASN   A ND2 
933  N  N   . GLY   A 120 ? 0.26669 0.29326 0.25046 -0.00278 -0.06107 0.10714  120 GLY   A N   
934  C  CA  . GLY   A 120 ? 0.27744 0.29686 0.28173 0.00254  -0.05719 0.10854  120 GLY   A CA  
935  C  C   . GLY   A 120 ? 0.31573 0.34030 0.33944 0.00802  -0.05951 0.10834  120 GLY   A C   
936  O  O   . GLY   A 120 ? 0.28937 0.30732 0.33243 0.01390  -0.05578 0.11084  120 GLY   A O   
937  N  N   . SER   A 121 ? 0.32201 0.35743 0.34212 0.00627  -0.06469 0.10513  121 SER   A N   
938  C  CA  . SER   A 121 ? 0.30695 0.34980 0.34648 0.01069  -0.06700 0.10669  121 SER   A CA  
939  C  C   . SER   A 121 ? 0.29352 0.34059 0.33029 0.00923  -0.06569 0.09466  121 SER   A C   
940  O  O   . SER   A 121 ? 0.22937 0.28067 0.25039 0.00362  -0.06886 0.08891  121 SER   A O   
941  C  CB  . SER   A 121 ? 0.36707 0.42034 0.40802 0.00913  -0.07529 0.11604  121 SER   A CB  
942  O  OG  . SER   A 121 ? 0.37336 0.42355 0.42333 0.01237  -0.07626 0.12910  121 SER   A OG  
943  N  N   . PRO   A 122 ? 0.28031 0.32562 0.33172 0.01420  -0.06060 0.09043  122 PRO   A N   
944  C  CA  . PRO   A 122 ? 0.25429 0.30344 0.30209 0.01252  -0.05890 0.07976  122 PRO   A CA  
945  C  C   . PRO   A 122 ? 0.25943 0.31978 0.30964 0.00962  -0.06440 0.08002  122 PRO   A C   
946  O  O   . PRO   A 122 ? 0.29602 0.36386 0.36245 0.01232  -0.06756 0.08809  122 PRO   A O   
947  C  CB  . PRO   A 122 ? 0.26833 0.31466 0.33448 0.01965  -0.05229 0.07783  122 PRO   A CB  
948  C  CG  . PRO   A 122 ? 0.28657 0.32237 0.36140 0.02422  -0.04914 0.08445  122 PRO   A CG  
949  C  CD  . PRO   A 122 ? 0.29397 0.32988 0.36142 0.02095  -0.05459 0.09365  122 PRO   A CD  
950  N  N   . SER   A 123 ? 0.25920 0.32030 0.29471 0.00419  -0.06527 0.07131  123 SER   A N   
951  C  CA  . SER   A 123 ? 0.28218 0.35199 0.31825 -0.00005 -0.07078 0.07065  123 SER   A CA  
952  C  C   . SER   A 123 ? 0.23742 0.31108 0.28242 0.00025  -0.06784 0.06483  123 SER   A C   
953  O  O   . SER   A 123 ? 0.20528 0.28879 0.26411 -0.00028 -0.07117 0.06872  123 SER   A O   
954  C  CB  . SER   A 123 ? 0.29523 0.36199 0.30872 -0.00668 -0.07411 0.06556  123 SER   A CB  
955  O  OG  . SER   A 123 ? 0.41011 0.48340 0.42375 -0.01141 -0.07912 0.06311  123 SER   A OG  
956  N  N   . GLY   A 124 ? 0.17368 0.24081 0.21147 0.00070  -0.06193 0.05644  124 GLY   A N   
957  C  CA  . GLY   A 124 ? 0.15751 0.22833 0.20253 0.00070  -0.05889 0.05180  124 GLY   A CA  
958  C  C   . GLY   A 124 ? 0.16085 0.22502 0.20013 0.00311  -0.05219 0.04524  124 GLY   A C   
959  O  O   . GLY   A 124 ? 0.14068 0.19708 0.16894 0.00367  -0.05041 0.04329  124 GLY   A O   
960  N  N   . VAL   A 125 ? 0.10893 0.17763 0.15666 0.00423  -0.04863 0.04275  125 VAL   A N   
961  C  CA  . VAL   A 125 ? 0.14236 0.20770 0.18572 0.00632  -0.04286 0.03727  125 VAL   A CA  
962  C  C   . VAL   A 125 ? 0.15897 0.22592 0.19854 0.00237  -0.04205 0.03312  125 VAL   A C   
963  O  O   . VAL   A 125 ? 0.12195 0.19603 0.17138 0.00003  -0.04400 0.03594  125 VAL   A O   
964  C  CB  . VAL   A 125 ? 0.13622 0.20669 0.19689 0.01389  -0.03720 0.03993  125 VAL   A CB  
965  C  CG1 . VAL   A 125 ? 0.16720 0.24863 0.24597 0.01597  -0.03439 0.04278  125 VAL   A CG1 
966  C  CG2 . VAL   A 125 ? 0.13246 0.20003 0.18545 0.01579  -0.03178 0.03406  125 VAL   A CG2 
967  N  N   . TYR   A 126 ? 0.12015 0.18031 0.14609 0.00119  -0.03952 0.02725  126 TYR   A N   
968  C  CA  . TYR   A 126 ? 0.13692 0.19739 0.16003 -0.00199 -0.03851 0.02467  126 TYR   A CA  
969  C  C   . TYR   A 126 ? 0.15783 0.21371 0.17067 -0.00047 -0.03392 0.02017  126 TYR   A C   
970  O  O   . TYR   A 126 ? 0.13060 0.18140 0.13604 0.00151  -0.03229 0.01761  126 TYR   A O   
971  C  CB  . TYR   A 126 ? 0.13017 0.18565 0.14555 -0.00763 -0.04330 0.02275  126 TYR   A CB  
972  C  CG  . TYR   A 126 ? 0.16018 0.20596 0.15968 -0.00789 -0.04361 0.01825  126 TYR   A CG  
973  C  CD1 . TYR   A 126 ? 0.20455 0.24309 0.19332 -0.00750 -0.04035 0.01308  126 TYR   A CD1 
974  C  CD2 . TYR   A 126 ? 0.19928 0.24480 0.19594 -0.00828 -0.04688 0.02034  126 TYR   A CD2 
975  C  CE1 . TYR   A 126 ? 0.19061 0.22260 0.16748 -0.00713 -0.03956 0.00968  126 TYR   A CE1 
976  C  CE2 . TYR   A 126 ? 0.20847 0.24726 0.19144 -0.00853 -0.04629 0.01730  126 TYR   A CE2 
977  C  CZ  . TYR   A 126 ? 0.20382 0.23628 0.17762 -0.00786 -0.04231 0.01179  126 TYR   A CZ  
978  O  OH  . TYR   A 126 ? 0.26080 0.28839 0.22273 -0.00790 -0.04114 0.00941  126 TYR   A OH  
979  N  N   . GLN   A 127 ? 0.16761 0.22627 0.18081 -0.00197 -0.03218 0.02022  127 GLN   A N   
980  C  CA  . GLN   A 127 ? 0.17970 0.23631 0.18408 -0.00038 -0.02788 0.01737  127 GLN   A CA  
981  C  C   . GLN   A 127 ? 0.16282 0.20918 0.15707 -0.00275 -0.02932 0.01419  127 GLN   A C   
982  O  O   . GLN   A 127 ? 0.20193 0.24691 0.19752 -0.00682 -0.03334 0.01517  127 GLN   A O   
983  C  CB  . GLN   A 127 ? 0.18587 0.25251 0.19768 0.00065  -0.02349 0.02091  127 GLN   A CB  
984  C  CG  . GLN   A 127 ? 0.19089 0.25669 0.19324 0.00292  -0.01845 0.01860  127 GLN   A CG  
985  C  CD  . GLN   A 127 ? 0.15651 0.22377 0.15532 0.00647  -0.01419 0.01426  127 GLN   A CD  
986  O  OE1 . GLN   A 127 ? 0.16549 0.23101 0.16831 0.00788  -0.01494 0.01258  127 GLN   A OE1 
987  N  NE2 . GLN   A 127 ? 0.17241 0.24250 0.16367 0.00750  -0.00985 0.01273  127 GLN   A NE2 
988  N  N   . CYS   A 128 ? 0.14728 0.18739 0.13292 -0.00057 -0.02640 0.01050  128 CYS   A N   
989  C  CA  . CYS   A 128 ? 0.22631 0.25926 0.20413 -0.00084 -0.02656 0.00794  128 CYS   A CA  
990  C  C   . CYS   A 128 ? 0.17559 0.21043 0.15204 0.00172  -0.02276 0.00840  128 CYS   A C   
991  O  O   . CYS   A 128 ? 0.14070 0.17981 0.11901 0.00307  -0.01988 0.00847  128 CYS   A O   
992  C  CB  . CYS   A 128 ? 0.16587 0.19176 0.13710 -0.00058 -0.02659 0.00467  128 CYS   A CB  
993  S  SG  . CYS   A 128 ? 0.33831 0.36208 0.30639 -0.00285 -0.03080 0.00364  128 CYS   A SG  
994  N  N   . ALA   A 129 ? 0.20420 0.23725 0.17684 0.00251  -0.02323 0.00876  129 ALA   A N   
995  C  CA  . ALA   A 129 ? 0.17760 0.21341 0.15001 0.00589  -0.02044 0.01003  129 ALA   A CA  
996  C  C   . ALA   A 129 ? 0.21024 0.24416 0.17840 0.00763  -0.01975 0.00710  129 ALA   A C   
997  O  O   . ALA   A 129 ? 0.19411 0.22211 0.15685 0.00673  -0.02070 0.00400  129 ALA   A O   
998  C  CB  . ALA   A 129 ? 0.17984 0.21761 0.15469 0.00779  -0.02051 0.01617  129 ALA   A CB  
999  N  N   . MET   A 130 ? 0.15999 0.19861 0.13082 0.00941  -0.01747 0.00726  130 MET   A N   
1000 C  CA  . MET   A 130 ? 0.14870 0.19122 0.11790 0.01296  -0.01617 0.00639  130 MET   A CA  
1001 C  C   . MET   A 130 ? 0.18758 0.22642 0.16034 0.01765  -0.01453 0.00933  130 MET   A C   
1002 O  O   . MET   A 130 ? 0.19415 0.23835 0.17228 0.02016  -0.01530 0.01538  130 MET   A O   
1003 C  CB  . MET   A 130 ? 0.16185 0.21226 0.13663 0.01254  -0.01496 0.00692  130 MET   A CB  
1004 C  CG  . MET   A 130 ? 0.20403 0.26321 0.17997 0.01481  -0.01342 0.00629  130 MET   A CG  
1005 S  SD  . MET   A 130 ? 0.24879 0.30119 0.21609 0.01446  -0.01031 0.00185  130 MET   A SD  
1006 C  CE  . MET   A 130 ? 0.12620 0.17412 0.09345 0.00755  -0.01177 0.00075  130 MET   A CE  
1007 N  N   . ARG   A 131 ? 0.14306 0.17040 0.11329 0.01831  -0.01151 0.00503  131 ARG   A N   
1008 C  CA  . ARG   A 131 ? 0.18345 0.20205 0.15976 0.02280  -0.00817 0.00676  131 ARG   A CA  
1009 C  C   . ARG   A 131 ? 0.19065 0.21864 0.17658 0.02979  -0.00504 0.01109  131 ARG   A C   
1010 O  O   . ARG   A 131 ? 0.19426 0.23365 0.18057 0.02989  -0.00476 0.01031  131 ARG   A O   
1011 C  CB  . ARG   A 131 ? 0.20709 0.20942 0.17660 0.02135  -0.00486 -0.00139 131 ARG   A CB  
1012 C  CG  . ARG   A 131 ? 0.22795 0.22237 0.18889 0.01345  -0.00951 -0.00544 131 ARG   A CG  
1013 C  CD  . ARG   A 131 ? 0.20507 0.19860 0.17308 0.01095  -0.01312 0.00052  131 ARG   A CD  
1014 N  NE  . ARG   A 131 ? 0.22076 0.20605 0.19770 0.01537  -0.00963 0.00457  131 ARG   A NE  
1015 C  CZ  . ARG   A 131 ? 0.21346 0.19844 0.19803 0.01446  -0.01107 0.01225  131 ARG   A CZ  
1016 N  NH1 . ARG   A 131 ? 0.19386 0.18665 0.17839 0.00930  -0.01508 0.01548  131 ARG   A NH1 
1017 N  NH2 . ARG   A 131 ? 0.24453 0.22121 0.23800 0.01919  -0.00764 0.01754  131 ARG   A NH2 
1018 N  N   . PRO   A 132 ? 0.16820 0.19254 0.16404 0.03549  -0.00306 0.01692  132 PRO   A N   
1019 C  CA  . PRO   A 132 ? 0.20340 0.23754 0.21170 0.04327  -0.00004 0.02200  132 PRO   A CA  
1020 C  C   . PRO   A 132 ? 0.20152 0.23408 0.21020 0.04612  0.00690  0.01477  132 PRO   A C   
1021 O  O   . PRO   A 132 ? 0.17827 0.22572 0.19732 0.05045  0.00860  0.01838  132 PRO   A O   
1022 C  CB  . PRO   A 132 ? 0.23399 0.25831 0.25263 0.04908  0.00182  0.02916  132 PRO   A CB  
1023 C  CG  . PRO   A 132 ? 0.21979 0.23990 0.23178 0.04272  -0.00329 0.03239  132 PRO   A CG  
1024 C  CD  . PRO   A 132 ? 0.21179 0.22564 0.21046 0.03496  -0.00420 0.02169  132 PRO   A CD  
1025 N  N   . ASN   A 133 ? 0.18780 0.20434 0.18524 0.04329  0.01102  0.00483  133 ASN   A N   
1026 C  CA  . ASN   A 133 ? 0.21236 0.22832 0.20707 0.04563  0.01891  -0.00220 133 ASN   A CA  
1027 C  C   . ASN   A 133 ? 0.17023 0.19619 0.15463 0.03914  0.01673  -0.00499 133 ASN   A C   
1028 O  O   . ASN   A 133 ? 0.19721 0.22163 0.17493 0.03909  0.02330  -0.01094 133 ASN   A O   
1029 C  CB  . ASN   A 133 ? 0.23230 0.22598 0.21737 0.04573  0.02543  -0.01250 133 ASN   A CB  
1030 C  CG  . ASN   A 133 ? 0.20438 0.18713 0.17166 0.03571  0.01945  -0.01867 133 ASN   A CG  
1031 O  OD1 . ASN   A 133 ? 0.18872 0.18050 0.15215 0.02978  0.01151  -0.01495 133 ASN   A OD1 
1032 N  ND2 . ASN   A 133 ? 0.25378 0.21711 0.21084 0.03376  0.02335  -0.02852 133 ASN   A ND2 
1033 N  N   . PHE   A 134 ? 0.16569 0.20062 0.14822 0.03375  0.00853  -0.00084 134 PHE   A N   
1034 C  CA  . PHE   A 134 ? 0.17732 0.22094 0.15327 0.02789  0.00602  -0.00184 134 PHE   A CA  
1035 C  C   . PHE   A 134 ? 0.18973 0.22250 0.14913 0.02202  0.00557  -0.00798 134 PHE   A C   
1036 O  O   . PHE   A 134 ? 0.23973 0.27760 0.19353 0.01822  0.00568  -0.00837 134 PHE   A O   
1037 C  CB  . PHE   A 134 ? 0.17229 0.22942 0.15652 0.03026  0.01120  -0.00045 134 PHE   A CB  
1038 C  CG  . PHE   A 134 ? 0.17897 0.25288 0.17910 0.03284  0.00785  0.00685  134 PHE   A CG  
1039 C  CD1 . PHE   A 134 ? 0.14234 0.22539 0.14202 0.02721  0.00041  0.00936  134 PHE   A CD1 
1040 C  CD2 . PHE   A 134 ? 0.20805 0.28909 0.22384 0.04081  0.01202  0.01113  134 PHE   A CD2 
1041 C  CE1 . PHE   A 134 ? 0.17505 0.27485 0.18703 0.02807  -0.00400 0.01538  134 PHE   A CE1 
1042 C  CE2 . PHE   A 134 ? 0.25006 0.34974 0.28092 0.04254  0.00700  0.01929  134 PHE   A CE2 
1043 C  CZ  . PHE   A 134 ? 0.21478 0.32414 0.24222 0.03537  -0.00152 0.02096  134 PHE   A CZ  
1044 N  N   . THR   A 135 ? 0.19199 0.21044 0.14391 0.02058  0.00458  -0.01202 135 THR   A N   
1045 C  CA  . THR   A 135 ? 0.18451 0.19543 0.12162 0.01372  0.00073  -0.01615 135 THR   A CA  
1046 C  C   . THR   A 135 ? 0.18213 0.19454 0.12258 0.01010  -0.00739 -0.01201 135 THR   A C   
1047 O  O   . THR   A 135 ? 0.15979 0.17636 0.11076 0.01274  -0.00874 -0.00731 135 THR   A O   
1048 C  CB  . THR   A 135 ? 0.19092 0.18572 0.11715 0.01264  0.00399  -0.02444 135 THR   A CB  
1049 O  OG1 . THR   A 135 ? 0.21071 0.19631 0.14506 0.01443  0.00302  -0.02412 135 THR   A OG1 
1050 C  CG2 . THR   A 135 ? 0.17822 0.17050 0.10103 0.01746  0.01465  -0.02986 135 THR   A CG2 
1051 N  N   . ILE   A 136 ? 0.17842 0.18829 0.10992 0.00419  -0.01250 -0.01319 136 ILE   A N   
1052 C  CA  . ILE   A 136 ? 0.21383 0.22480 0.14976 0.00086  -0.01918 -0.00983 136 ILE   A CA  
1053 C  C   . ILE   A 136 ? 0.19793 0.19983 0.12494 -0.00503 -0.02341 -0.01391 136 ILE   A C   
1054 O  O   . ILE   A 136 ? 0.21211 0.21105 0.12905 -0.00691 -0.02245 -0.01811 136 ILE   A O   
1055 C  CB  . ILE   A 136 ? 0.20981 0.22493 0.15351 -0.00054 -0.02081 -0.00440 136 ILE   A CB  
1056 C  CG1 . ILE   A 136 ? 0.18401 0.19438 0.12172 -0.00214 -0.02199 -0.00468 136 ILE   A CG1 
1057 C  CG2 . ILE   A 136 ? 0.19507 0.21814 0.14634 0.00272  -0.01703 -0.00243 136 ILE   A CG2 
1058 C  CD1 . ILE   A 136 ? 0.18124 0.19421 0.12707 -0.00163 -0.02390 -0.00094 136 ILE   A CD1 
1059 N  N   . LYS   A 137 ? 0.21006 0.20906 0.14403 -0.00747 -0.02708 -0.01247 137 LYS   A N   
1060 C  CA  . LYS   A 137 ? 0.24343 0.23568 0.17149 -0.01480 -0.03287 -0.01599 137 LYS   A CA  
1061 C  C   . LYS   A 137 ? 0.21418 0.21895 0.15227 -0.01531 -0.03657 -0.01021 137 LYS   A C   
1062 O  O   . LYS   A 137 ? 0.24186 0.25193 0.19119 -0.01619 -0.03928 -0.00533 137 LYS   A O   
1063 C  CB  . LYS   A 137 ? 0.27812 0.26207 0.21500 -0.01645 -0.03286 -0.01629 137 LYS   A CB  
1064 C  CG  . LYS   A 137 ? 0.25959 0.23354 0.19870 -0.01035 -0.02478 -0.01876 137 LYS   A CG  
1065 C  CD  . LYS   A 137 ? 0.25306 0.21498 0.20043 -0.01277 -0.02460 -0.01870 137 LYS   A CD  
1066 C  CE  . LYS   A 137 ? 0.30208 0.24810 0.24870 -0.00770 -0.01677 -0.02398 137 LYS   A CE  
1067 N  NZ  . LYS   A 137 ? 0.38700 0.31553 0.32087 -0.01378 -0.01669 -0.03614 137 LYS   A NZ  
1068 N  N   . GLY   A 138 ? 0.21368 0.22180 0.14849 -0.01337 -0.03548 -0.01021 138 GLY   A N   
1069 C  CA  . GLY   A 138 ? 0.19950 0.21453 0.14237 -0.01236 -0.03795 -0.00483 138 GLY   A CA  
1070 C  C   . GLY   A 138 ? 0.23577 0.25175 0.17646 -0.01778 -0.04401 -0.00488 138 GLY   A C   
1071 O  O   . GLY   A 138 ? 0.25712 0.26792 0.19151 -0.02314 -0.04684 -0.00968 138 GLY   A O   
1072 N  N   . SER   A 139 ? 0.20755 0.22934 0.15309 -0.01693 -0.04650 0.00043  139 SER   A N   
1073 C  CA  . SER   A 139 ? 0.20314 0.22774 0.14541 -0.02157 -0.05294 0.00181  139 SER   A CA  
1074 C  C   . SER   A 139 ? 0.22584 0.25276 0.16435 -0.01908 -0.05289 0.00645  139 SER   A C   
1075 O  O   . SER   A 139 ? 0.20169 0.23277 0.15038 -0.01614 -0.05268 0.01248  139 SER   A O   
1076 C  CB  . SER   A 139 ? 0.23374 0.26515 0.18994 -0.02457 -0.05815 0.00625  139 SER   A CB  
1077 O  OG  . SER   A 139 ? 0.26337 0.29978 0.21812 -0.02862 -0.06517 0.00919  139 SER   A OG  
1078 N  N   . PHE   A 140 ? 0.26798 0.29164 0.19123 -0.02069 -0.05296 0.00370  140 PHE   A N   
1079 C  CA  . PHE   A 140 ? 0.24620 0.27038 0.16262 -0.01891 -0.05167 0.00808  140 PHE   A CA  
1080 C  C   . PHE   A 140 ? 0.30894 0.33316 0.20925 -0.02342 -0.05602 0.00684  140 PHE   A C   
1081 O  O   . PHE   A 140 ? 0.32280 0.34233 0.21150 -0.02608 -0.05537 -0.00110 140 PHE   A O   
1082 C  CB  . PHE   A 140 ? 0.24634 0.26564 0.15839 -0.01503 -0.04373 0.00556  140 PHE   A CB  
1083 C  CG  . PHE   A 140 ? 0.22115 0.24099 0.14653 -0.01104 -0.04009 0.00775  140 PHE   A CG  
1084 C  CD1 . PHE   A 140 ? 0.22052 0.24376 0.15504 -0.00990 -0.04152 0.01457  140 PHE   A CD1 
1085 C  CD2 . PHE   A 140 ? 0.22635 0.24312 0.15404 -0.00868 -0.03546 0.00306  140 PHE   A CD2 
1086 C  CE1 . PHE   A 140 ? 0.20172 0.22501 0.14628 -0.00698 -0.03833 0.01540  140 PHE   A CE1 
1087 C  CE2 . PHE   A 140 ? 0.23572 0.25320 0.17368 -0.00572 -0.03275 0.00475  140 PHE   A CE2 
1088 C  CZ  . PHE   A 140 ? 0.16540 0.18605 0.11106 -0.00516 -0.03409 0.01023  140 PHE   A CZ  
1089 N  N   . LEU   A 141 ? 0.27716 0.30631 0.17585 -0.02451 -0.06054 0.01456  141 LEU   A N   
1090 C  CA  . LEU   A 141 ? 0.34072 0.37059 0.22144 -0.02864 -0.06449 0.01450  141 LEU   A CA  
1091 C  C   . LEU   A 141 ? 0.34274 0.37123 0.21390 -0.02654 -0.05999 0.01935  141 LEU   A C   
1092 O  O   . LEU   A 141 ? 0.33749 0.36453 0.21732 -0.02262 -0.05465 0.02269  141 LEU   A O   
1093 C  CB  . LEU   A 141 ? 0.30274 0.34086 0.18767 -0.03277 -0.07473 0.02079  141 LEU   A CB  
1094 C  CG  . LEU   A 141 ? 0.37351 0.41418 0.27068 -0.03552 -0.07901 0.01743  141 LEU   A CG  
1095 C  CD1 . LEU   A 141 ? 0.38339 0.43466 0.29163 -0.03808 -0.08827 0.02642  141 LEU   A CD1 
1096 C  CD2 . LEU   A 141 ? 0.36198 0.39724 0.24553 -0.04079 -0.08020 0.00644  141 LEU   A CD2 
1097 N  N   . ASN   A 142 ? 0.38322 0.41221 0.23531 -0.02993 -0.06220 0.01958  142 ASN   A N   
1098 C  CA  . ASN   A 142 ? 0.38767 0.41679 0.22977 -0.02915 -0.05893 0.02647  142 ASN   A CA  
1099 C  C   . ASN   A 142 ? 0.36823 0.40157 0.22626 -0.02717 -0.06148 0.03859  142 ASN   A C   
1100 O  O   . ASN   A 142 ? 0.38026 0.41954 0.24847 -0.02823 -0.06936 0.04449  142 ASN   A O   
1101 C  CB  . ASN   A 142 ? 0.44995 0.48134 0.26980 -0.03386 -0.06351 0.02716  142 ASN   A CB  
1102 C  CG  . ASN   A 142 ? 0.52106 0.54635 0.32034 -0.03481 -0.05717 0.01595  142 ASN   A CG  
1103 O  OD1 . ASN   A 142 ? 0.55782 0.57782 0.35851 -0.03111 -0.04772 0.01076  142 ASN   A OD1 
1104 N  ND2 . ASN   A 142 ? 0.54894 0.57520 0.32881 -0.03988 -0.06237 0.01186  142 ASN   A ND2 
1105 N  N   . GLY   A 143 ? 0.33308 0.36355 0.19382 -0.02457 -0.05476 0.04249  143 GLY   A N   
1106 C  CA  . GLY   A 143 ? 0.33320 0.36567 0.20818 -0.02284 -0.05614 0.05358  143 GLY   A CA  
1107 C  C   . GLY   A 143 ? 0.30627 0.33676 0.20057 -0.01926 -0.05301 0.05169  143 GLY   A C   
1108 O  O   . GLY   A 143 ? 0.28505 0.31569 0.19154 -0.01754 -0.05321 0.06000  143 GLY   A O   
1109 N  N   . SER   A 144 ? 0.26910 0.29741 0.16613 -0.01810 -0.05023 0.04139  144 SER   A N   
1110 C  CA  . SER   A 144 ? 0.28244 0.30964 0.19587 -0.01494 -0.04769 0.03921  144 SER   A CA  
1111 C  C   . SER   A 144 ? 0.22209 0.24563 0.13578 -0.01378 -0.04032 0.03785  144 SER   A C   
1112 O  O   . SER   A 144 ? 0.21116 0.23422 0.13690 -0.01169 -0.03862 0.03679  144 SER   A O   
1113 C  CB  . SER   A 144 ? 0.26112 0.28813 0.17779 -0.01450 -0.04817 0.03020  144 SER   A CB  
1114 O  OG  . SER   A 144 ? 0.26740 0.29040 0.17105 -0.01521 -0.04406 0.02212  144 SER   A OG  
1115 N  N   . CYS   A 145 ? 0.25411 0.27609 0.15474 -0.01550 -0.03590 0.03815  145 CYS   A N   
1116 C  CA  . CYS   A 145 ? 0.28106 0.30179 0.18375 -0.01544 -0.02904 0.03773  145 CYS   A CA  
1117 C  C   . CYS   A 145 ? 0.21946 0.24041 0.13539 -0.01542 -0.03015 0.04571  145 CYS   A C   
1118 O  O   . CYS   A 145 ? 0.23851 0.25943 0.15787 -0.01574 -0.03430 0.05500  145 CYS   A O   
1119 C  CB  . CYS   A 145 ? 0.28705 0.30778 0.17563 -0.01786 -0.02370 0.04018  145 CYS   A CB  
1120 S  SG  . CYS   A 145 ? 0.49237 0.51145 0.36794 -0.01683 -0.01710 0.02896  145 CYS   A SG  
1121 N  N   . GLY   A 146 ? 0.22847 0.24947 0.15138 -0.01520 -0.02635 0.04272  146 GLY   A N   
1122 C  CA  . GLY   A 146 ? 0.21963 0.23933 0.15427 -0.01567 -0.02728 0.04942  146 GLY   A CA  
1123 C  C   . GLY   A 146 ? 0.17323 0.19252 0.11989 -0.01222 -0.03144 0.04766  146 GLY   A C   
1124 O  O   . GLY   A 146 ? 0.19358 0.21013 0.15031 -0.01193 -0.03207 0.05204  146 GLY   A O   
1125 N  N   . SER   A 147 ? 0.19131 0.21246 0.13773 -0.00990 -0.03409 0.04215  147 SER   A N   
1126 C  CA  . SER   A 147 ? 0.16968 0.19217 0.12758 -0.00675 -0.03620 0.03932  147 SER   A CA  
1127 C  C   . SER   A 147 ? 0.17299 0.19606 0.13221 -0.00652 -0.03243 0.03238  147 SER   A C   
1128 O  O   . SER   A 147 ? 0.13855 0.16191 0.09022 -0.00790 -0.02837 0.02700  147 SER   A O   
1129 C  CB  . SER   A 147 ? 0.17337 0.19818 0.13020 -0.00590 -0.03883 0.03493  147 SER   A CB  
1130 O  OG  . SER   A 147 ? 0.19327 0.21963 0.14653 -0.00728 -0.04323 0.04082  147 SER   A OG  
1131 N  N   . VAL   A 148 ? 0.15076 0.17491 0.12043 -0.00442 -0.03387 0.03301  148 VAL   A N   
1132 C  CA  . VAL   A 148 ? 0.15974 0.18385 0.13161 -0.00424 -0.02893 0.02449  148 VAL   A CA  
1133 C  C   . VAL   A 148 ? 0.15661 0.18480 0.13230 -0.00143 -0.02903 0.01905  148 VAL   A C   
1134 O  O   . VAL   A 148 ? 0.13120 0.16152 0.11345 0.00095  -0.03186 0.02192  148 VAL   A O   
1135 C  CB  . VAL   A 148 ? 0.17035 0.18742 0.15157 -0.00445 -0.02507 0.02363  148 VAL   A CB  
1136 C  CG1 . VAL   A 148 ? 0.14764 0.16049 0.12605 -0.00841 -0.02411 0.03034  148 VAL   A CG1 
1137 C  CG2 . VAL   A 148 ? 0.14685 0.15944 0.14079 -0.00004 -0.02512 0.02533  148 VAL   A CG2 
1138 N  N   . GLY   A 149 ? 0.13123 0.16203 0.10368 -0.00197 -0.02595 0.01237  149 GLY   A N   
1139 C  CA  . GLY   A 149 ? 0.11021 0.14486 0.08520 0.00020  -0.02482 0.00786  149 GLY   A CA  
1140 C  C   . GLY   A 149 ? 0.13509 0.16882 0.11368 0.00039  -0.02105 0.00235  149 GLY   A C   
1141 O  O   . GLY   A 149 ? 0.11926 0.15066 0.09719 -0.00242 -0.01970 0.00025  149 GLY   A O   
1142 N  N   . PHE   A 150 ? 0.11650 0.15261 0.09816 0.00285  -0.01914 -0.00045 150 PHE   A N   
1143 C  CA  . PHE   A 150 ? 0.13100 0.16461 0.11391 0.00270  -0.01520 -0.00688 150 PHE   A CA  
1144 C  C   . PHE   A 150 ? 0.14862 0.18774 0.13049 0.00506  -0.01234 -0.00972 150 PHE   A C   
1145 O  O   . PHE   A 150 ? 0.12642 0.17004 0.11104 0.00716  -0.01309 -0.00537 150 PHE   A O   
1146 C  CB  . PHE   A 150 ? 0.14821 0.17237 0.14000 0.00421  -0.01300 -0.00640 150 PHE   A CB  
1147 C  CG  . PHE   A 150 ? 0.13351 0.15851 0.13525 0.00925  -0.01248 -0.00151 150 PHE   A CG  
1148 C  CD1 . PHE   A 150 ? 0.15107 0.17825 0.15622 0.00976  -0.01772 0.00742  150 PHE   A CD1 
1149 C  CD2 . PHE   A 150 ? 0.13831 0.16414 0.14566 0.01310  -0.00685 -0.00569 150 PHE   A CD2 
1150 C  CE1 . PHE   A 150 ? 0.14691 0.17813 0.16373 0.01373  -0.01872 0.01302  150 PHE   A CE1 
1151 C  CE2 . PHE   A 150 ? 0.16491 0.19456 0.18518 0.01803  -0.00603 -0.00005 150 PHE   A CE2 
1152 C  CZ  . PHE   A 150 ? 0.16741 0.20044 0.19361 0.01814  -0.01272 0.00976  150 PHE   A CZ  
1153 N  N   . ASN   A 151 ? 0.16126 0.20005 0.13851 0.00377  -0.00901 -0.01710 151 ASN   A N   
1154 C  CA  . ASN   A 151 ? 0.18897 0.23204 0.16300 0.00569  -0.00433 -0.02094 151 ASN   A CA  
1155 C  C   . ASN   A 151 ? 0.19179 0.22621 0.16721 0.00619  0.00152  -0.02949 151 ASN   A C   
1156 O  O   . ASN   A 151 ? 0.17100 0.19660 0.14789 0.00344  0.00077  -0.03303 151 ASN   A O   
1157 C  CB  . ASN   A 151 ? 0.17662 0.22855 0.13880 0.00283  -0.00608 -0.02259 151 ASN   A CB  
1158 C  CG  . ASN   A 151 ? 0.20651 0.26422 0.16983 0.00381  -0.00938 -0.01410 151 ASN   A CG  
1159 O  OD1 . ASN   A 151 ? 0.19192 0.25423 0.15669 0.00621  -0.00759 -0.01034 151 ASN   A OD1 
1160 N  ND2 . ASN   A 151 ? 0.14655 0.19982 0.11300 0.00187  -0.01228 -0.01058 151 ASN   A ND2 
1161 N  N   . ILE   A 152 ? 0.18317 0.21939 0.15829 0.00950  0.00836  -0.03319 152 ILE   A N   
1162 C  CA  . ILE   A 152 ? 0.22139 0.24777 0.19728 0.01088  0.01603  -0.04318 152 ILE   A CA  
1163 C  C   . ILE   A 152 ? 0.30829 0.34039 0.26814 0.00889  0.02080  -0.05165 152 ILE   A C   
1164 O  O   . ILE   A 152 ? 0.25633 0.29974 0.21270 0.01071  0.02258  -0.04697 152 ILE   A O   
1165 C  CB  . ILE   A 152 ? 0.24973 0.27215 0.24321 0.01857  0.02240  -0.03993 152 ILE   A CB  
1166 C  CG1 . ILE   A 152 ? 0.23799 0.25993 0.24549 0.02032  0.01564  -0.02811 152 ILE   A CG1 
1167 C  CG2 . ILE   A 152 ? 0.26687 0.27465 0.26323 0.02065  0.03100  -0.05102 152 ILE   A CG2 
1168 C  CD1 . ILE   A 152 ? 0.22701 0.23721 0.23625 0.01748  0.01205  -0.02835 152 ILE   A CD1 
1169 N  N   . ASP   A 153 ? 0.36236 0.38641 0.31194 0.00443  0.02284  -0.06391 153 ASP   A N   
1170 C  CA  . ASP   A 153 ? 0.40479 0.43122 0.33686 0.00125  0.02594  -0.07104 153 ASP   A CA  
1171 C  C   . ASP   A 153 ? 0.45264 0.46378 0.38494 0.00324  0.03553  -0.08322 153 ASP   A C   
1172 O  O   . ASP   A 153 ? 0.45940 0.45704 0.39341 -0.00054 0.03428  -0.09083 153 ASP   A O   
1173 C  CB  . ASP   A 153 ? 0.41630 0.44494 0.33820 -0.00674 0.01581  -0.06917 153 ASP   A CB  
1174 C  CG  . ASP   A 153 ? 0.50645 0.54576 0.41819 -0.00771 0.01294  -0.06193 153 ASP   A CG  
1175 O  OD1 . ASP   A 153 ? 0.51907 0.55856 0.42249 -0.00545 0.01988  -0.06466 153 ASP   A OD1 
1176 O  OD2 . ASP   A 153 ? 0.54258 0.58927 0.45577 -0.01027 0.00463  -0.05350 153 ASP   A OD2 
1177 N  N   . TYR   A 154 ? 0.46610 0.47880 0.39768 0.00914  0.04531  -0.08422 154 TYR   A N   
1178 C  CA  . TYR   A 154 ? 0.56293 0.56179 0.50074 0.01467  0.05645  -0.09334 154 TYR   A CA  
1179 C  C   . TYR   A 154 ? 0.54264 0.52951 0.50317 0.01873  0.05828  -0.09391 154 TYR   A C   
1180 O  O   . TYR   A 154 ? 0.55657 0.54872 0.53708 0.02603  0.06043  -0.08445 154 TYR   A O   
1181 C  CB  . TYR   A 154 ? 0.57339 0.56115 0.49324 0.00928  0.05658  -0.10493 154 TYR   A CB  
1182 C  CG  . TYR   A 154 ? 0.65522 0.63110 0.57875 0.01629  0.06929  -0.11392 154 TYR   A CG  
1183 C  CD1 . TYR   A 154 ? 0.66907 0.65264 0.60276 0.02590  0.07938  -0.10916 154 TYR   A CD1 
1184 C  CD2 . TYR   A 154 ? 0.66320 0.62118 0.58184 0.01340  0.07126  -0.12661 154 TYR   A CD2 
1185 C  CE1 . TYR   A 154 ? 0.70280 0.67765 0.64212 0.03333  0.09117  -0.11649 154 TYR   A CE1 
1186 C  CE2 . TYR   A 154 ? 0.70115 0.64795 0.62396 0.02055  0.08327  -0.13493 154 TYR   A CE2 
1187 C  CZ  . TYR   A 154 ? 0.73204 0.68784 0.66543 0.03095  0.09329  -0.12969 154 TYR   A CZ  
1188 O  OH  . TYR   A 154 ? 0.71653 0.66311 0.65600 0.03879  0.10550  -0.13739 154 TYR   A OH  
1189 N  N   . ASP   A 155 ? 0.49610 0.46668 0.45552 0.01371  0.05550  -0.10135 155 ASP   A N   
1190 C  CA  . ASP   A 155 ? 0.48055 0.43491 0.46180 0.01766  0.05798  -0.10068 155 ASP   A CA  
1191 C  C   . ASP   A 155 ? 0.42343 0.37559 0.40738 0.01050  0.04590  -0.09370 155 ASP   A C   
1192 O  O   . ASP   A 155 ? 0.33552 0.27400 0.33603 0.01255  0.04545  -0.08879 155 ASP   A O   
1193 C  CB  . ASP   A 155 ? 0.52753 0.46216 0.50900 0.01896  0.06518  -0.11081 155 ASP   A CB  
1194 C  CG  . ASP   A 155 ? 0.54941 0.47778 0.51040 0.00763  0.05952  -0.12123 155 ASP   A CG  
1195 O  OD1 . ASP   A 155 ? 0.58659 0.49632 0.54906 0.00625  0.06308  -0.13003 155 ASP   A OD1 
1196 O  OD2 . ASP   A 155 ? 0.57377 0.51677 0.51862 0.00026  0.05089  -0.11938 155 ASP   A OD2 
1197 N  N   . CYS   A 156 ? 0.37212 0.33831 0.34152 0.00279  0.03639  -0.09122 156 CYS   A N   
1198 C  CA  . CYS   A 156 ? 0.30898 0.27493 0.27929 -0.00483 0.02620  -0.08614 156 CYS   A CA  
1199 C  C   . CYS   A 156 ? 0.25052 0.23214 0.22570 -0.00244 0.01863  -0.06998 156 CYS   A C   
1200 O  O   . CYS   A 156 ? 0.25025 0.24722 0.21727 -0.00122 0.01694  -0.06655 156 CYS   A O   
1201 C  CB  . CYS   A 156 ? 0.33119 0.30150 0.28298 -0.01589 0.02124  -0.09675 156 CYS   A CB  
1202 S  SG  . CYS   A 156 ? 0.31544 0.29310 0.27050 -0.02477 0.00903  -0.08830 156 CYS   A SG  
1203 N  N   . VAL   A 157 ? 0.21775 0.19446 0.20538 -0.00207 0.01458  -0.06020 157 VAL   A N   
1204 C  CA  . VAL   A 157 ? 0.18437 0.17318 0.17517 -0.00041 0.00794  -0.04649 157 VAL   A CA  
1205 C  C   . VAL   A 157 ? 0.20044 0.19688 0.18287 -0.00830 0.00097  -0.04581 157 VAL   A C   
1206 O  O   . VAL   A 157 ? 0.18358 0.17228 0.16898 -0.01403 -0.00055 -0.04734 157 VAL   A O   
1207 C  CB  . VAL   A 157 ? 0.18226 0.16344 0.18837 0.00376  0.00710  -0.03564 157 VAL   A CB  
1208 C  CG1 . VAL   A 157 ? 0.15220 0.14572 0.15754 0.00442  0.00035  -0.02372 157 VAL   A CG1 
1209 C  CG2 . VAL   A 157 ? 0.18443 0.15769 0.20415 0.01236  0.01426  -0.03547 157 VAL   A CG2 
1210 N  N   . SER   A 158 ? 0.18245 0.19409 0.15707 -0.00833 -0.00291 -0.04224 158 SER   A N   
1211 C  CA  . SER   A 158 ? 0.15846 0.17972 0.12869 -0.01390 -0.00905 -0.03966 158 SER   A CA  
1212 C  C   . SER   A 158 ? 0.14956 0.17418 0.12518 -0.01090 -0.01173 -0.02835 158 SER   A C   
1213 O  O   . SER   A 158 ? 0.16247 0.19383 0.13653 -0.00664 -0.01256 -0.02341 158 SER   A O   
1214 C  CB  . SER   A 158 ? 0.16720 0.20215 0.12622 -0.01535 -0.01142 -0.04234 158 SER   A CB  
1215 O  OG  . SER   A 158 ? 0.18390 0.21616 0.13462 -0.02012 -0.00996 -0.05354 158 SER   A OG  
1216 N  N   . PHE   A 159 ? 0.15563 0.17442 0.13703 -0.01358 -0.01260 -0.02445 159 PHE   A N   
1217 C  CA  . PHE   A 159 ? 0.14613 0.16823 0.12890 -0.01182 -0.01475 -0.01482 159 PHE   A CA  
1218 C  C   . PHE   A 159 ? 0.14650 0.18112 0.12451 -0.01373 -0.01725 -0.01370 159 PHE   A C   
1219 O  O   . PHE   A 159 ? 0.16245 0.20194 0.14107 -0.01881 -0.01822 -0.01696 159 PHE   A O   
1220 C  CB  . PHE   A 159 ? 0.17259 0.18541 0.16149 -0.01451 -0.01407 -0.00994 159 PHE   A CB  
1221 C  CG  . PHE   A 159 ? 0.14819 0.14827 0.14493 -0.01078 -0.01177 -0.00796 159 PHE   A CG  
1222 C  CD1 . PHE   A 159 ? 0.16589 0.16680 0.16523 -0.00510 -0.01323 -0.00010 159 PHE   A CD1 
1223 C  CD2 . PHE   A 159 ? 0.17707 0.16446 0.17985 -0.01302 -0.00832 -0.01408 159 PHE   A CD2 
1224 C  CE1 . PHE   A 159 ? 0.14275 0.13434 0.15274 -0.00064 -0.01151 0.00359  159 PHE   A CE1 
1225 C  CE2 . PHE   A 159 ? 0.16344 0.13822 0.17627 -0.00810 -0.00515 -0.01175 159 PHE   A CE2 
1226 C  CZ  . PHE   A 159 ? 0.15701 0.13519 0.17460 -0.00120 -0.00689 -0.00181 159 PHE   A CZ  
1227 N  N   . CYS   A 160 ? 0.15364 0.19352 0.12848 -0.00981 -0.01835 -0.00911 160 CYS   A N   
1228 C  CA  . CYS   A 160 ? 0.14162 0.19064 0.11468 -0.00988 -0.01913 -0.00748 160 CYS   A CA  
1229 C  C   . CYS   A 160 ? 0.15975 0.20760 0.13159 -0.00833 -0.01804 -0.00221 160 CYS   A C   
1230 O  O   . CYS   A 160 ? 0.15323 0.20625 0.12663 -0.00778 -0.01642 -0.00135 160 CYS   A O   
1231 C  CB  . CYS   A 160 ? 0.11668 0.16493 0.09013 -0.00588 -0.01774 -0.00739 160 CYS   A CB  
1232 S  SG  . CYS   A 160 ? 0.15063 0.19303 0.12325 -0.00186 -0.01720 -0.00496 160 CYS   A SG  
1233 N  N   . TYR   A 161 ? 0.11229 0.15484 0.08107 -0.00781 -0.01894 0.00135  161 TYR   A N   
1234 C  CA  . TYR   A 161 ? 0.14186 0.18144 0.10655 -0.00648 -0.01751 0.00450  161 TYR   A CA  
1235 C  C   . TYR   A 161 ? 0.17869 0.21539 0.13874 -0.00897 -0.01908 0.01024  161 TYR   A C   
1236 O  O   . TYR   A 161 ? 0.13376 0.16510 0.09789 -0.00836 -0.02115 0.01256  161 TYR   A O   
1237 C  CB  . TYR   A 161 ? 0.12752 0.16088 0.09202 -0.00291 -0.01761 0.00341  161 TYR   A CB  
1238 C  CG  . TYR   A 161 ? 0.12946 0.15838 0.08744 -0.00265 -0.01706 0.00414  161 TYR   A CG  
1239 C  CD1 . TYR   A 161 ? 0.15544 0.18736 0.11066 -0.00201 -0.01390 0.00253  161 TYR   A CD1 
1240 C  CD2 . TYR   A 161 ? 0.11788 0.14160 0.07191 -0.00287 -0.01988 0.00606  161 TYR   A CD2 
1241 C  CE1 . TYR   A 161 ? 0.13778 0.16525 0.08395 -0.00208 -0.01282 0.00159  161 TYR   A CE1 
1242 C  CE2 . TYR   A 161 ? 0.12591 0.14570 0.07124 -0.00321 -0.01989 0.00531  161 TYR   A CE2 
1243 C  CZ  . TYR   A 161 ? 0.14924 0.16948 0.08943 -0.00308 -0.01610 0.00252  161 TYR   A CZ  
1244 O  OH  . TYR   A 161 ? 0.15969 0.17538 0.08849 -0.00354 -0.01542 0.00041  161 TYR   A OH  
1245 N  N   . MET   A 162 ? 0.11983 0.15787 0.07418 -0.01091 -0.01647 0.01294  162 MET   A N   
1246 C  CA  . MET   A 162 ? 0.15368 0.18703 0.10174 -0.01256 -0.01737 0.01935  162 MET   A CA  
1247 C  C   . MET   A 162 ? 0.16798 0.19813 0.10827 -0.01053 -0.01528 0.01661  162 MET   A C   
1248 O  O   . MET   A 162 ? 0.11595 0.14953 0.05319 -0.01029 -0.01068 0.01365  162 MET   A O   
1249 C  CB  . MET   A 162 ? 0.18518 0.21824 0.13541 -0.01687 -0.01417 0.02471  162 MET   A CB  
1250 C  CG  . MET   A 162 ? 0.16621 0.19410 0.11053 -0.01849 -0.01635 0.03425  162 MET   A CG  
1251 S  SD  . MET   A 162 ? 0.22441 0.24793 0.17495 -0.02363 -0.01262 0.04325  162 MET   A SD  
1252 C  CE  . MET   A 162 ? 0.24566 0.25796 0.21223 -0.02173 -0.01601 0.04428  162 MET   A CE  
1253 N  N   . HIS   A 163 ? 0.13995 0.16475 0.07691 -0.00940 -0.01892 0.01784  163 HIS   A N   
1254 C  CA  . HIS   A 163 ? 0.15594 0.17713 0.08315 -0.00855 -0.01837 0.01452  163 HIS   A CA  
1255 C  C   . HIS   A 163 ? 0.17192 0.19375 0.08761 -0.01098 -0.01481 0.01739  163 HIS   A C   
1256 O  O   . HIS   A 163 ? 0.18480 0.20741 0.09877 -0.01334 -0.01615 0.02455  163 HIS   A O   
1257 C  CB  . HIS   A 163 ? 0.19984 0.21864 0.12725 -0.00781 -0.02408 0.01530  163 HIS   A CB  
1258 C  CG  . HIS   A 163 ? 0.18156 0.19754 0.09856 -0.00786 -0.02450 0.01081  163 HIS   A CG  
1259 N  ND1 . HIS   A 163 ? 0.21094 0.22411 0.12535 -0.00641 -0.02162 0.00439  163 HIS   A ND1 
1260 C  CD2 . HIS   A 163 ? 0.19327 0.20904 0.10056 -0.00974 -0.02762 0.01184  163 HIS   A CD2 
1261 C  CE1 . HIS   A 163 ? 0.19951 0.21033 0.10302 -0.00738 -0.02265 0.00076  163 HIS   A CE1 
1262 N  NE2 . HIS   A 163 ? 0.20602 0.21882 0.10483 -0.00968 -0.02654 0.00484  163 HIS   A NE2 
1263 N  N   . HIS   A 164 ? 0.21089 0.23187 0.11812 -0.01023 -0.00986 0.01239  164 HIS   A N   
1264 C  CA  . HIS   A 164 ? 0.20040 0.22162 0.09437 -0.01192 -0.00499 0.01392  164 HIS   A CA  
1265 C  C   . HIS   A 164 ? 0.25066 0.26645 0.12977 -0.01100 -0.00532 0.00892  164 HIS   A C   
1266 O  O   . HIS   A 164 ? 0.28815 0.30371 0.15524 -0.01284 -0.00525 0.01191  164 HIS   A O   
1267 C  CB  . HIS   A 164 ? 0.19634 0.22381 0.09220 -0.01201 0.00404  0.01273  164 HIS   A CB  
1268 C  CG  . HIS   A 164 ? 0.20318 0.23889 0.11080 -0.01484 0.00504  0.01890  164 HIS   A CG  
1269 N  ND1 . HIS   A 164 ? 0.19869 0.23973 0.10482 -0.01831 0.01094  0.02493  164 HIS   A ND1 
1270 C  CD2 . HIS   A 164 ? 0.19205 0.23121 0.11242 -0.01536 0.00108  0.02008  164 HIS   A CD2 
1271 C  CE1 . HIS   A 164 ? 0.18833 0.23551 0.10674 -0.02163 0.01026  0.02990  164 HIS   A CE1 
1272 N  NE2 . HIS   A 164 ? 0.18009 0.22628 0.10590 -0.01986 0.00425  0.02651  164 HIS   A NE2 
1273 N  N   . MET   A 165 ? 0.22686 0.23872 0.10503 -0.00866 -0.00538 0.00148  165 MET   A N   
1274 C  CA  . MET   A 165 ? 0.27287 0.28064 0.13496 -0.00849 -0.00390 -0.00442 165 MET   A CA  
1275 C  C   . MET   A 165 ? 0.24882 0.25254 0.11277 -0.00745 -0.00751 -0.01158 165 MET   A C   
1276 O  O   . MET   A 165 ? 0.26953 0.27297 0.14576 -0.00592 -0.00877 -0.01199 165 MET   A O   
1277 C  CB  . MET   A 165 ? 0.27589 0.28361 0.12869 -0.00681 0.00729  -0.00791 165 MET   A CB  
1278 C  CG  . MET   A 165 ? 0.29299 0.30411 0.15889 -0.00484 0.01332  -0.00835 165 MET   A CG  
1279 S  SD  . MET   A 165 ? 0.45397 0.46751 0.31359 -0.00178 0.02858  -0.01258 165 MET   A SD  
1280 C  CE  . MET   A 165 ? 0.31548 0.32135 0.17447 0.00313  0.03088  -0.02332 165 MET   A CE  
1281 N  N   . GLU   A 166 ? 0.26910 0.26995 0.12003 -0.00930 -0.00920 -0.01731 166 GLU   A N   
1282 C  CA  . GLU   A 166 ? 0.28793 0.28405 0.13890 -0.01023 -0.01152 -0.02566 166 GLU   A CA  
1283 C  C   . GLU   A 166 ? 0.29019 0.28061 0.12926 -0.00836 -0.00228 -0.03546 166 GLU   A C   
1284 O  O   . GLU   A 166 ? 0.31927 0.31009 0.14470 -0.00803 0.00292  -0.03670 166 GLU   A O   
1285 C  CB  . GLU   A 166 ? 0.30164 0.29788 0.14869 -0.01551 -0.02100 -0.02614 166 GLU   A CB  
1286 C  CG  . GLU   A 166 ? 0.33334 0.32265 0.17932 -0.01875 -0.02334 -0.03543 166 GLU   A CG  
1287 C  CD  . GLU   A 166 ? 0.36760 0.35905 0.21443 -0.02482 -0.03382 -0.03407 166 GLU   A CD  
1288 O  OE1 . GLU   A 166 ? 0.35025 0.34917 0.20987 -0.02480 -0.03934 -0.02527 166 GLU   A OE1 
1289 O  OE2 . GLU   A 166 ? 0.41640 0.40211 0.25066 -0.02971 -0.03623 -0.04206 166 GLU   A OE2 
1290 N  N   . LEU   A 167 ? 0.32309 0.30822 0.16832 -0.00658 0.00116  -0.04203 167 LEU   A N   
1291 C  CA  . LEU   A 167 ? 0.33760 0.31514 0.17602 -0.00370 0.01144  -0.05263 167 LEU   A CA  
1292 C  C   . LEU   A 167 ? 0.37520 0.34113 0.20265 -0.00856 0.00796  -0.06275 167 LEU   A C   
1293 O  O   . LEU   A 167 ? 0.38539 0.35101 0.21420 -0.01426 -0.00262 -0.06085 167 LEU   A O   
1294 C  CB  . LEU   A 167 ? 0.32169 0.29719 0.17411 0.00095  0.01765  -0.05396 167 LEU   A CB  
1295 C  CG  . LEU   A 167 ? 0.28898 0.27608 0.15238 0.00577  0.02270  -0.04579 167 LEU   A CG  
1296 C  CD1 . LEU   A 167 ? 0.26764 0.25226 0.14447 0.00900  0.02609  -0.04643 167 LEU   A CD1 
1297 C  CD2 . LEU   A 167 ? 0.32205 0.31395 0.18169 0.01033  0.03461  -0.04775 167 LEU   A CD2 
1298 N  N   . PRO   A 168 ? 0.39278 0.34895 0.21044 -0.00643 0.01700  -0.07382 168 PRO   A N   
1299 C  CA  . PRO   A 168 ? 0.40476 0.34876 0.20893 -0.01202 0.01327  -0.08434 168 PRO   A CA  
1300 C  C   . PRO   A 168 ? 0.41282 0.34620 0.22553 -0.01686 0.00609  -0.08758 168 PRO   A C   
1301 O  O   . PRO   A 168 ? 0.44896 0.37694 0.25312 -0.02403 -0.00157 -0.09272 168 PRO   A O   
1302 C  CB  . PRO   A 168 ? 0.43535 0.36975 0.23126 -0.00666 0.02686  -0.09574 168 PRO   A CB  
1303 C  CG  . PRO   A 168 ? 0.43350 0.38113 0.23414 0.00032  0.03616  -0.08881 168 PRO   A CG  
1304 C  CD  . PRO   A 168 ? 0.39945 0.35664 0.21816 0.00121  0.03127  -0.07713 168 PRO   A CD  
1305 N  N   . THR   A 169 ? 0.36422 0.29422 0.19289 -0.01364 0.00837  -0.08464 169 THR   A N   
1306 C  CA  . THR   A 169 ? 0.39763 0.31726 0.23424 -0.01889 0.00152  -0.08608 169 THR   A CA  
1307 C  C   . THR   A 169 ? 0.36497 0.29796 0.20864 -0.02476 -0.01133 -0.07556 169 THR   A C   
1308 O  O   . THR   A 169 ? 0.37815 0.30555 0.23046 -0.02944 -0.01720 -0.07472 169 THR   A O   
1309 C  CB  . THR   A 169 ? 0.38998 0.29815 0.23989 -0.01273 0.00922  -0.08606 169 THR   A CB  
1310 O  OG1 . THR   A 169 ? 0.36261 0.28425 0.22010 -0.00651 0.01253  -0.07646 169 THR   A OG1 
1311 C  CG2 . THR   A 169 ? 0.38270 0.27402 0.23152 -0.00645 0.02160  -0.09693 169 THR   A CG2 
1312 N  N   . GLY   A 170 ? 0.36767 0.31719 0.20975 -0.02411 -0.01515 -0.06704 170 GLY   A N   
1313 C  CA  . GLY   A 170 ? 0.34404 0.30581 0.19642 -0.02747 -0.02553 -0.05671 170 GLY   A CA  
1314 C  C   . GLY   A 170 ? 0.30847 0.27818 0.17689 -0.02341 -0.02542 -0.04719 170 GLY   A C   
1315 O  O   . GLY   A 170 ? 0.32179 0.30063 0.20126 -0.02521 -0.03263 -0.03919 170 GLY   A O   
1316 N  N   . VAL   A 171 ? 0.29954 0.26628 0.16979 -0.01770 -0.01706 -0.04802 171 VAL   A N   
1317 C  CA  . VAL   A 171 ? 0.25122 0.22667 0.13393 -0.01369 -0.01685 -0.03937 171 VAL   A CA  
1318 C  C   . VAL   A 171 ? 0.24572 0.23247 0.12865 -0.00930 -0.01392 -0.03362 171 VAL   A C   
1319 O  O   . VAL   A 171 ? 0.24817 0.23456 0.12013 -0.00911 -0.01112 -0.03596 171 VAL   A O   
1320 C  CB  . VAL   A 171 ? 0.26141 0.22549 0.14613 -0.00925 -0.01017 -0.04229 171 VAL   A CB  
1321 C  CG1 . VAL   A 171 ? 0.29218 0.24261 0.18228 -0.01222 -0.01273 -0.04612 171 VAL   A CG1 
1322 C  CG2 . VAL   A 171 ? 0.26904 0.22893 0.14882 -0.00278 0.00202  -0.04815 171 VAL   A CG2 
1323 N  N   . HIS   A 172 ? 0.20952 0.20402 0.10371 -0.00603 -0.01454 -0.02587 172 HIS   A N   
1324 C  CA  . HIS   A 172 ? 0.19339 0.19276 0.08907 -0.00423 -0.01428 -0.01888 172 HIS   A CA  
1325 C  C   . HIS   A 172 ? 0.19522 0.19673 0.09510 -0.00229 -0.00761 -0.01640 172 HIS   A C   
1326 O  O   . HIS   A 172 ? 0.16255 0.16846 0.07102 -0.00050 -0.00599 -0.01710 172 HIS   A O   
1327 C  CB  . HIS   A 172 ? 0.23252 0.23680 0.13941 -0.00545 -0.02151 -0.01240 172 HIS   A CB  
1328 C  CG  . HIS   A 172 ? 0.22713 0.23184 0.13116 -0.00963 -0.02744 -0.01393 172 HIS   A CG  
1329 N  ND1 . HIS   A 172 ? 0.21285 0.21769 0.12394 -0.01253 -0.03194 -0.01484 172 HIS   A ND1 
1330 C  CD2 . HIS   A 172 ? 0.24226 0.24668 0.13547 -0.01255 -0.02974 -0.01463 172 HIS   A CD2 
1331 C  CE1 . HIS   A 172 ? 0.25049 0.25511 0.15654 -0.01726 -0.03719 -0.01601 172 HIS   A CE1 
1332 N  NE2 . HIS   A 172 ? 0.20529 0.20990 0.09987 -0.01718 -0.03625 -0.01606 172 HIS   A NE2 
1333 N  N   . ALA   A 173 ? 0.22011 0.22533 0.11724 -0.00235 -0.00350 -0.01375 173 ALA   A N   
1334 C  CA  . ALA   A 173 ? 0.17109 0.18695 0.07760 -0.00059 0.00243  -0.01154 173 ALA   A CA  
1335 C  C   . ALA   A 173 ? 0.17830 0.19939 0.09008 -0.00286 0.00003  -0.00481 173 ALA   A C   
1336 O  O   . ALA   A 173 ? 0.17183 0.18881 0.07651 -0.00500 -0.00284 -0.00218 173 ALA   A O   
1337 C  CB  . ALA   A 173 ? 0.19775 0.21535 0.09767 0.00219  0.01321  -0.01633 173 ALA   A CB  
1338 N  N   . GLY   A 174 ? 0.15206 0.18375 0.07655 -0.00195 0.00095  -0.00214 174 GLY   A N   
1339 C  CA  . GLY   A 174 ? 0.14451 0.18087 0.07347 -0.00495 -0.00054 0.00323  174 GLY   A CA  
1340 C  C   . GLY   A 174 ? 0.15131 0.20146 0.09160 -0.00469 0.00189  0.00464  174 GLY   A C   
1341 O  O   . GLY   A 174 ? 0.12729 0.18567 0.07241 -0.00100 0.00542  0.00238  174 GLY   A O   
1342 N  N   . THR   A 175 ? 0.13059 0.18417 0.07523 -0.00861 -0.00051 0.00879  175 THR   A N   
1343 C  CA  . THR   A 175 ? 0.12647 0.19046 0.08395 -0.01040 0.00080  0.00975  175 THR   A CA  
1344 C  C   . THR   A 175 ? 0.10475 0.16670 0.06924 -0.01148 -0.00550 0.00825  175 THR   A C   
1345 O  O   . THR   A 175 ? 0.10932 0.16303 0.06938 -0.01076 -0.00965 0.00797  175 THR   A O   
1346 C  CB  . THR   A 175 ? 0.15790 0.22473 0.11747 -0.01574 0.00496  0.01494  175 THR   A CB  
1347 O  OG1 . THR   A 175 ? 0.11575 0.17293 0.07204 -0.01922 0.00086  0.01886  175 THR   A OG1 
1348 C  CG2 . THR   A 175 ? 0.14501 0.21494 0.09545 -0.01490 0.01310  0.01641  175 THR   A CG2 
1349 N  N   . ASP   A 176 ? 0.10298 0.17349 0.07864 -0.01360 -0.00596 0.00718  176 ASP   A N   
1350 C  CA  . ASP   A 176 ? 0.13688 0.20457 0.11724 -0.01699 -0.01041 0.00481  176 ASP   A CA  
1351 C  C   . ASP   A 176 ? 0.10462 0.16492 0.08666 -0.02245 -0.00917 0.00797  176 ASP   A C   
1352 O  O   . ASP   A 176 ? 0.12234 0.18145 0.10074 -0.02344 -0.00545 0.01312  176 ASP   A O   
1353 C  CB  . ASP   A 176 ? 0.11564 0.19542 0.10488 -0.01855 -0.01281 0.00196  176 ASP   A CB  
1354 C  CG  . ASP   A 176 ? 0.13299 0.22485 0.13316 -0.02298 -0.01046 0.00434  176 ASP   A CG  
1355 O  OD1 . ASP   A 176 ? 0.08489 0.17368 0.08674 -0.02715 -0.00676 0.00760  176 ASP   A OD1 
1356 O  OD2 . ASP   A 176 ? 0.11750 0.22334 0.12602 -0.02306 -0.01309 0.00372  176 ASP   A OD2 
1357 N  N   . LEU   A 177 ? 0.14088 0.19460 0.12731 -0.02585 -0.01178 0.00505  177 LEU   A N   
1358 C  CA  . LEU   A 177 ? 0.13587 0.17896 0.12558 -0.03034 -0.01047 0.00874  177 LEU   A CA  
1359 C  C   . LEU   A 177 ? 0.16610 0.21473 0.16539 -0.03807 -0.00815 0.01033  177 LEU   A C   
1360 O  O   . LEU   A 177 ? 0.19986 0.23900 0.20368 -0.04293 -0.00657 0.01424  177 LEU   A O   
1361 C  CB  . LEU   A 177 ? 0.16921 0.19986 0.16098 -0.02996 -0.01267 0.00426  177 LEU   A CB  
1362 C  CG  . LEU   A 177 ? 0.19093 0.21271 0.17825 -0.02377 -0.01364 0.00784  177 LEU   A CG  
1363 C  CD1 . LEU   A 177 ? 0.15409 0.16897 0.14097 -0.02443 -0.01268 0.01801  177 LEU   A CD1 
1364 C  CD2 . LEU   A 177 ? 0.16892 0.19823 0.14826 -0.01821 -0.01535 0.00737  177 LEU   A CD2 
1365 N  N   . GLU   A 178 ? 0.14496 0.20906 0.14958 -0.03947 -0.00809 0.00832  178 GLU   A N   
1366 C  CA  . GLU   A 178 ? 0.16073 0.23462 0.17630 -0.04634 -0.00482 0.01223  178 GLU   A CA  
1367 C  C   . GLU   A 178 ? 0.14200 0.22265 0.15415 -0.04334 0.00195  0.01944  178 GLU   A C   
1368 O  O   . GLU   A 178 ? 0.13409 0.22464 0.15576 -0.04834 0.00658  0.02395  178 GLU   A O   
1369 C  CB  . GLU   A 178 ? 0.15630 0.24678 0.18259 -0.04977 -0.00846 0.00773  178 GLU   A CB  
1370 C  CG  . GLU   A 178 ? 0.19744 0.28232 0.22002 -0.05074 -0.01507 -0.00091 178 GLU   A CG  
1371 C  CD  . GLU   A 178 ? 0.24742 0.32271 0.27555 -0.06065 -0.01725 -0.00583 178 GLU   A CD  
1372 O  OE1 . GLU   A 178 ? 0.23734 0.30350 0.27105 -0.06573 -0.01352 -0.00134 178 GLU   A OE1 
1373 O  OE2 . GLU   A 178 ? 0.27901 0.35408 0.30434 -0.06337 -0.02250 -0.01462 178 GLU   A OE2 
1374 N  N   . GLY   A 179 ? 0.13882 0.21447 0.13742 -0.03607 0.00308  0.02024  179 GLY   A N   
1375 C  CA  . GLY   A 179 ? 0.14690 0.22666 0.13782 -0.03351 0.00995  0.02500  179 GLY   A CA  
1376 C  C   . GLY   A 179 ? 0.13037 0.22411 0.12463 -0.02835 0.01414  0.02247  179 GLY   A C   
1377 O  O   . GLY   A 179 ? 0.16242 0.26112 0.15232 -0.02681 0.02221  0.02537  179 GLY   A O   
1378 N  N   . ASN   A 180 ? 0.09992 0.20003 0.10158 -0.02525 0.00956  0.01763  180 ASN   A N   
1379 C  CA  . ASN   A 180 ? 0.12501 0.23785 0.13299 -0.01902 0.01323  0.01664  180 ASN   A CA  
1380 C  C   . ASN   A 180 ? 0.11097 0.21407 0.10584 -0.01134 0.01254  0.01293  180 ASN   A C   
1381 O  O   . ASN   A 180 ? 0.12554 0.22138 0.11626 -0.01035 0.00568  0.01016  180 ASN   A O   
1382 C  CB  . ASN   A 180 ? 0.08038 0.20772 0.10522 -0.02068 0.00776  0.01584  180 ASN   A CB  
1383 C  CG  . ASN   A 180 ? 0.11118 0.24780 0.14972 -0.03011 0.00766  0.01871  180 ASN   A CG  
1384 O  OD1 . ASN   A 180 ? 0.10876 0.25519 0.15568 -0.03177 0.01529  0.02340  180 ASN   A OD1 
1385 N  ND2 . ASN   A 180 ? 0.10548 0.23854 0.14642 -0.03708 -0.00027 0.01547  180 ASN   A ND2 
1386 N  N   . PHE   A 181 ? 0.12564 0.22839 0.11418 -0.00640 0.02037  0.01240  181 PHE   A N   
1387 C  CA  . PHE   A 181 ? 0.13632 0.22779 0.11226 -0.00061 0.01982  0.00797  181 PHE   A CA  
1388 C  C   . PHE   A 181 ? 0.14056 0.23465 0.12536 0.00437  0.01488  0.00629  181 PHE   A C   
1389 O  O   . PHE   A 181 ? 0.08931 0.19723 0.09020 0.00633  0.01490  0.00856  181 PHE   A O   
1390 C  CB  . PHE   A 181 ? 0.13768 0.22768 0.10555 0.00366  0.03011  0.00562  181 PHE   A CB  
1391 C  CG  . PHE   A 181 ? 0.15185 0.23045 0.09834 0.00019  0.03145  0.00478  181 PHE   A CG  
1392 C  CD1 . PHE   A 181 ? 0.16175 0.22431 0.09499 0.00072  0.02534  0.00064  181 PHE   A CD1 
1393 C  CD2 . PHE   A 181 ? 0.12694 0.20694 0.06990 -0.00466 0.03586  0.00926  181 PHE   A CD2 
1394 C  CE1 . PHE   A 181 ? 0.14829 0.19792 0.06566 -0.00290 0.02371  0.00083  181 PHE   A CE1 
1395 C  CE2 . PHE   A 181 ? 0.21290 0.27916 0.13795 -0.00762 0.03463  0.00978  181 PHE   A CE2 
1396 C  CZ  . PHE   A 181 ? 0.20798 0.25968 0.12054 -0.00655 0.02788  0.00559  181 PHE   A CZ  
1397 N  N   . TYR   A 182 ? 0.11485 0.19668 0.08950 0.00581  0.01001  0.00351  182 TYR   A N   
1398 C  CA  . TYR   A 182 ? 0.10258 0.18320 0.08152 0.01134  0.00749  0.00250  182 TYR   A CA  
1399 C  C   . TYR   A 182 ? 0.15651 0.23274 0.13403 0.01771  0.01538  -0.00018 182 TYR   A C   
1400 O  O   . TYR   A 182 ? 0.13574 0.19981 0.09854 0.01700  0.01827  -0.00452 182 TYR   A O   
1401 C  CB  . TYR   A 182 ? 0.10100 0.17058 0.07097 0.00968  0.00072  0.00102  182 TYR   A CB  
1402 C  CG  . TYR   A 182 ? 0.13096 0.20475 0.10467 0.00558  -0.00567 0.00248  182 TYR   A CG  
1403 C  CD1 . TYR   A 182 ? 0.14186 0.22413 0.12368 0.00701  -0.00937 0.00401  182 TYR   A CD1 
1404 C  CD2 . TYR   A 182 ? 0.12484 0.19234 0.09365 0.00060  -0.00781 0.00225  182 TYR   A CD2 
1405 C  CE1 . TYR   A 182 ? 0.10532 0.18562 0.08948 0.00257  -0.01288 0.00305  182 TYR   A CE1 
1406 C  CE2 . TYR   A 182 ? 0.10603 0.17207 0.07990 -0.00247 -0.01142 0.00171  182 TYR   A CE2 
1407 C  CZ  . TYR   A 182 ? 0.13403 0.20532 0.11416 -0.00166 -0.01326 0.00116  182 TYR   A CZ  
1408 O  OH  . TYR   A 182 ? 0.11957 0.18779 0.10073 -0.00481 -0.01546 -0.00094 182 TYR   A OH  
1409 N  N   . GLY   A 183 ? 0.13079 0.21741 0.12391 0.02376  0.01913  0.00230  183 GLY   A N   
1410 C  CA  . GLY   A 183 ? 0.15932 0.24036 0.15424 0.03141  0.02788  -0.00061 183 GLY   A CA  
1411 C  C   . GLY   A 183 ? 0.15043 0.23625 0.14510 0.03268  0.03929  -0.00265 183 GLY   A C   
1412 O  O   . GLY   A 183 ? 0.10693 0.20198 0.10139 0.02711  0.04032  -0.00025 183 GLY   A O   
1413 N  N   . PRO   A 184 ? 0.12455 0.20324 0.11933 0.04001  0.04902  -0.00720 184 PRO   A N   
1414 C  CA  . PRO   A 184 ? 0.16339 0.24813 0.15968 0.04309  0.06274  -0.00952 184 PRO   A CA  
1415 C  C   . PRO   A 184 ? 0.19543 0.26640 0.16444 0.03736  0.06734  -0.01693 184 PRO   A C   
1416 O  O   . PRO   A 184 ? 0.24243 0.30061 0.20218 0.03956  0.07606  -0.02507 184 PRO   A O   
1417 C  CB  . PRO   A 184 ? 0.20042 0.28145 0.21049 0.05479  0.07116  -0.01162 184 PRO   A CB  
1418 C  CG  . PRO   A 184 ? 0.20353 0.26458 0.20396 0.05487  0.06355  -0.01518 184 PRO   A CG  
1419 C  CD  . PRO   A 184 ? 0.18051 0.24554 0.17715 0.04656  0.04895  -0.00993 184 PRO   A CD  
1420 N  N   . PHE   A 185 ? 0.16293 0.23488 0.12020 0.02811  0.06001  -0.01393 185 PHE   A N   
1421 C  CA  . PHE   A 185 ? 0.18462 0.24226 0.11734 0.02052  0.06004  -0.01770 185 PHE   A CA  
1422 C  C   . PHE   A 185 ? 0.23877 0.30534 0.17176 0.01421  0.06132  -0.01081 185 PHE   A C   
1423 O  O   . PHE   A 185 ? 0.20878 0.29067 0.15847 0.01282  0.05804  -0.00382 185 PHE   A O   
1424 C  CB  . PHE   A 185 ? 0.21306 0.25777 0.13144 0.01570  0.04780  -0.01918 185 PHE   A CB  
1425 C  CG  . PHE   A 185 ? 0.21130 0.24833 0.13148 0.02136  0.04567  -0.02458 185 PHE   A CG  
1426 C  CD1 . PHE   A 185 ? 0.23261 0.25617 0.14496 0.02498  0.05326  -0.03364 185 PHE   A CD1 
1427 C  CD2 . PHE   A 185 ? 0.18972 0.22863 0.12221 0.02143  0.03563  -0.01996 185 PHE   A CD2 
1428 C  CE1 . PHE   A 185 ? 0.23134 0.24352 0.14874 0.02946  0.05096  -0.03733 185 PHE   A CE1 
1429 C  CE2 . PHE   A 185 ? 0.19890 0.22820 0.13627 0.02540  0.03330  -0.02246 185 PHE   A CE2 
1430 C  CZ  . PHE   A 185 ? 0.20456 0.21989 0.13530 0.02930  0.04074  -0.03070 185 PHE   A CZ  
1431 N  N   . VAL   A 186 ? 0.24843 0.30488 0.16239 0.01015  0.06626  -0.01253 186 VAL   A N   
1432 C  CA  . VAL   A 186 ? 0.24200 0.30534 0.15506 0.00512  0.06955  -0.00541 186 VAL   A CA  
1433 C  C   . VAL   A 186 ? 0.29973 0.34939 0.18944 -0.00017 0.06310  -0.00333 186 VAL   A C   
1434 O  O   . VAL   A 186 ? 0.29737 0.33268 0.16984 0.00104  0.05932  -0.00871 186 VAL   A O   
1435 C  CB  . VAL   A 186 ? 0.32061 0.38994 0.23797 0.00764  0.08521  -0.00726 186 VAL   A CB  
1436 C  CG1 . VAL   A 186 ? 0.27166 0.35899 0.21922 0.01373  0.08903  -0.00636 186 VAL   A CG1 
1437 C  CG2 . VAL   A 186 ? 0.33280 0.38505 0.22890 0.00987  0.09335  -0.01703 186 VAL   A CG2 
1438 N  N   . ASP   A 187 ? 0.26772 0.32304 0.15881 -0.00549 0.06106  0.00532  187 ASP   A N   
1439 C  CA  . ASP   A 187 ? 0.32336 0.36865 0.19571 -0.00930 0.05479  0.00920  187 ASP   A CA  
1440 C  C   . ASP   A 187 ? 0.33823 0.38103 0.19367 -0.00914 0.06511  0.01004  187 ASP   A C   
1441 O  O   . ASP   A 187 ? 0.32748 0.37416 0.18044 -0.01334 0.06755  0.01822  187 ASP   A O   
1442 C  CB  . ASP   A 187 ? 0.28694 0.33701 0.16901 -0.01468 0.04649  0.01847  187 ASP   A CB  
1443 C  CG  . ASP   A 187 ? 0.25788 0.32202 0.15744 -0.01775 0.05279  0.02491  187 ASP   A CG  
1444 O  OD1 . ASP   A 187 ? 0.22901 0.30228 0.13760 -0.01527 0.06303  0.02251  187 ASP   A OD1 
1445 O  OD2 . ASP   A 187 ? 0.22975 0.29590 0.13645 -0.02275 0.04722  0.03264  187 ASP   A OD2 
1446 N  N   . ARG   A 188 ? 0.38068 0.41710 0.22496 -0.00347 0.07216  0.00131  188 ARG   A N   
1447 C  CA  . ARG   A 188 ? 0.44818 0.48107 0.27131 -0.00062 0.08072  -0.00066 188 ARG   A CA  
1448 C  C   . ARG   A 188 ? 0.49815 0.52367 0.30758 0.00446  0.07605  -0.01118 188 ARG   A C   
1449 O  O   . ARG   A 188 ? 0.43326 0.45546 0.25234 0.00665  0.07069  -0.01685 188 ARG   A O   
1450 C  CB  . ARG   A 188 ? 0.48310 0.52323 0.31439 0.00291  0.09753  -0.00176 188 ARG   A CB  
1451 C  CG  . ARG   A 188 ? 0.46951 0.52184 0.32380 -0.00233 0.10334  0.00492  188 ARG   A CG  
1452 C  CD  . ARG   A 188 ? 0.50555 0.56556 0.37144 -0.00002 0.11972  0.00117  188 ARG   A CD  
1453 N  NE  . ARG   A 188 ? 0.48472 0.55658 0.37862 0.00143  0.12098  -0.00431 188 ARG   A NE  
1454 C  CZ  . ARG   A 188 ? 0.45466 0.53234 0.35851 0.00442  0.12799  -0.01585 188 ARG   A CZ  
1455 N  NH1 . ARG   A 188 ? 0.47497 0.55936 0.36537 0.00192  0.13053  -0.02815 188 ARG   A NH1 
1456 N  NH2 . ARG   A 188 ? 0.44436 0.53916 0.37712 0.00991  0.12767  -0.01655 188 ARG   A NH2 
1457 N  N   . GLN   A 189 ? 0.53255 0.55717 0.32005 0.00535  0.07848  -0.01449 189 GLN   A N   
1458 C  CA  . GLN   A 189 ? 0.57496 0.59405 0.34908 0.00711  0.07348  -0.02657 189 GLN   A CA  
1459 C  C   . GLN   A 189 ? 0.53202 0.55633 0.30893 0.01409  0.08634  -0.03735 189 GLN   A C   
1460 O  O   . GLN   A 189 ? 0.60049 0.62894 0.36322 0.01594  0.09598  -0.04063 189 GLN   A O   
1461 C  CB  . GLN   A 189 ? 0.62520 0.64015 0.37466 0.00181  0.06667  -0.02593 189 GLN   A CB  
1462 C  CG  . GLN   A 189 ? 0.66121 0.66861 0.39661 0.00093  0.06123  -0.03936 189 GLN   A CG  
1463 C  CD  . GLN   A 189 ? 0.77588 0.77924 0.49828 -0.00625 0.04654  -0.03619 189 GLN   A CD  
1464 O  OE1 . GLN   A 189 ? 0.78176 0.78851 0.50638 -0.00970 0.04058  -0.02378 189 GLN   A OE1 
1465 N  NE2 . GLN   A 189 ? 0.81543 0.81180 0.52578 -0.00888 0.04072  -0.04736 189 GLN   A NE2 
1466 N  N   . THR   A 190 ? 0.48458 0.50974 0.28130 0.01786  0.08671  -0.04291 190 THR   A N   
1467 C  CA  . THR   A 190 ? 0.48056 0.50938 0.28527 0.02406  0.09728  -0.05507 190 THR   A CA  
1468 C  C   . THR   A 190 ? 0.47332 0.48559 0.27286 0.02324  0.09053  -0.06709 190 THR   A C   
1469 O  O   . THR   A 190 ? 0.48219 0.48511 0.27314 0.01743  0.07740  -0.06558 190 THR   A O   
1470 C  CB  . THR   A 190 ? 0.44193 0.48540 0.27844 0.02779  0.10337  -0.05118 190 THR   A CB  
1471 O  OG1 . THR   A 190 ? 0.44399 0.48267 0.29429 0.02634  0.09337  -0.04859 190 THR   A OG1 
1472 C  CG2 . THR   A 190 ? 0.47362 0.53193 0.31857 0.02623  0.10726  -0.03758 190 THR   A CG2 
1473 N  N   . ALA   A 191 ? 0.45984 0.46733 0.26780 0.02883  0.09975  -0.07834 191 ALA   A N   
1474 C  CA  . ALA   A 191 ? 0.46033 0.44876 0.26775 0.02848  0.09492  -0.08868 191 ALA   A CA  
1475 C  C   . ALA   A 191 ? 0.43718 0.42486 0.26920 0.03039  0.09062  -0.08431 191 ALA   A C   
1476 O  O   . ALA   A 191 ? 0.45773 0.43103 0.29756 0.03383  0.09246  -0.09192 191 ALA   A O   
1477 C  CB  . ALA   A 191 ? 0.46528 0.44304 0.26836 0.03433  0.10733  -0.10280 191 ALA   A CB  
1478 N  N   . GLN   A 192 ? 0.40152 0.40280 0.24515 0.02835  0.08516  -0.07203 192 GLN   A N   
1479 C  CA  . GLN   A 192 ? 0.39244 0.39437 0.25788 0.03002  0.08178  -0.06787 192 GLN   A CA  
1480 C  C   . GLN   A 192 ? 0.40831 0.39197 0.26797 0.02671  0.07204  -0.07264 192 GLN   A C   
1481 O  O   . GLN   A 192 ? 0.41080 0.38801 0.25258 0.01979  0.06237  -0.07399 192 GLN   A O   
1482 C  CB  . GLN   A 192 ? 0.36445 0.38184 0.23863 0.02597  0.07550  -0.05513 192 GLN   A CB  
1483 C  CG  . GLN   A 192 ? 0.36642 0.38256 0.22155 0.02073  0.06776  -0.04749 192 GLN   A CG  
1484 C  CD  . GLN   A 192 ? 0.33829 0.35564 0.20019 0.01800  0.06675  -0.03338 192 GLN   A CD  
1485 O  OE1 . GLN   A 192 ? 0.31574 0.33711 0.19740 0.01449  0.07112  -0.03160 192 GLN   A OE1 
1486 N  NE2 . GLN   A 192 ? 0.34654 0.36255 0.19474 0.01211  0.06273  -0.02752 192 GLN   A NE2 
1487 N  N   . ALA   A 193 ? 0.37824 0.35454 0.25523 0.03175  0.07418  -0.07341 193 ALA   A N   
1488 C  CA  . ALA   A 193 ? 0.34232 0.30132 0.21638 0.02857  0.06594  -0.07682 193 ALA   A CA  
1489 C  C   . ALA   A 193 ? 0.35925 0.31920 0.25271 0.03329  0.06463  -0.06879 193 ALA   A C   
1490 O  O   . ALA   A 193 ? 0.34826 0.32051 0.26036 0.04125  0.07118  -0.06186 193 ALA   A O   
1491 C  CB  . ALA   A 193 ? 0.38507 0.32379 0.25447 0.03113  0.07122  -0.08917 193 ALA   A CB  
1492 N  N   . ALA   A 194 ? 0.32130 0.26896 0.21075 0.02889  0.05548  -0.06889 194 ALA   A N   
1493 C  CA  . ALA   A 194 ? 0.35579 0.31021 0.26564 0.03205  0.04850  -0.05765 194 ALA   A CA  
1494 C  C   . ALA   A 194 ? 0.36656 0.32154 0.30088 0.04413  0.05661  -0.05362 194 ALA   A C   
1495 O  O   . ALA   A 194 ? 0.40314 0.37662 0.35624 0.04895  0.05501  -0.04253 194 ALA   A O   
1496 C  CB  . ALA   A 194 ? 0.31437 0.25718 0.22008 0.02463  0.03715  -0.05823 194 ALA   A CB  
1497 N  N   . GLY   A 195 ? 0.41930 0.35420 0.35476 0.04903  0.06480  -0.06206 195 GLY   A N   
1498 C  CA  . GLY   A 195 ? 0.40541 0.34098 0.36769 0.06078  0.06990  -0.05475 195 GLY   A CA  
1499 C  C   . GLY   A 195 ? 0.39613 0.32783 0.36996 0.05917  0.05914  -0.04555 195 GLY   A C   
1500 O  O   . GLY   A 195 ? 0.35905 0.29350 0.32394 0.04968  0.04767  -0.04290 195 GLY   A O   
1501 N  N   . THR   A 196 ? 0.36471 0.29017 0.35977 0.06912  0.06373  -0.03974 196 THR   A N   
1502 C  CA  . THR   A 196 ? 0.35221 0.26559 0.35488 0.06726  0.05672  -0.03353 196 THR   A CA  
1503 C  C   . THR   A 196 ? 0.32015 0.25421 0.32792 0.06298  0.04399  -0.01948 196 THR   A C   
1504 O  O   . THR   A 196 ? 0.29359 0.25115 0.30958 0.06626  0.04187  -0.01102 196 THR   A O   
1505 C  CB  . THR   A 196 ? 0.37777 0.27952 0.40319 0.07986  0.06516  -0.02858 196 THR   A CB  
1506 O  OG1 . THR   A 196 ? 0.43816 0.36475 0.48459 0.08969  0.06568  -0.01480 196 THR   A OG1 
1507 C  CG2 . THR   A 196 ? 0.37642 0.25846 0.39640 0.08344  0.07792  -0.04404 196 THR   A CG2 
1508 N  N   . ASP   A 197 ? 0.30831 0.23354 0.31067 0.05483  0.03592  -0.01796 197 ASP   A N   
1509 C  CA  . ASP   A 197 ? 0.28963 0.23074 0.29417 0.04993  0.02523  -0.00661 197 ASP   A CA  
1510 C  C   . ASP   A 197 ? 0.30863 0.24455 0.32893 0.05378  0.02359  0.00558  197 ASP   A C   
1511 O  O   . ASP   A 197 ? 0.32483 0.24106 0.35390 0.05858  0.02962  0.00463  197 ASP   A O   
1512 C  CB  . ASP   A 197 ? 0.28511 0.22295 0.27286 0.03749  0.01787  -0.01274 197 ASP   A CB  
1513 C  CG  . ASP   A 197 ? 0.27198 0.23128 0.25801 0.03329  0.00953  -0.00504 197 ASP   A CG  
1514 O  OD1 . ASP   A 197 ? 0.26667 0.24372 0.25972 0.03830  0.00929  0.00195  197 ASP   A OD1 
1515 O  OD2 . ASP   A 197 ? 0.26536 0.22377 0.24423 0.02479  0.00323  -0.00605 197 ASP   A OD2 
1516 N  N   . THR   A 198 ? 0.29859 0.25148 0.32158 0.05137  0.01579  0.01711  198 THR   A N   
1517 C  CA  . THR   A 198 ? 0.27573 0.22705 0.31008 0.05317  0.01316  0.03068  198 THR   A CA  
1518 C  C   . THR   A 198 ? 0.27335 0.23228 0.29913 0.04344  0.00563  0.03404  198 THR   A C   
1519 O  O   . THR   A 198 ? 0.25691 0.22436 0.27072 0.03704  0.00212  0.02711  198 THR   A O   
1520 C  CB  . THR   A 198 ? 0.31598 0.28518 0.36501 0.06300  0.01266  0.04481  198 THR   A CB  
1521 O  OG1 . THR   A 198 ? 0.26902 0.26212 0.31281 0.06192  0.00876  0.04420  198 THR   A OG1 
1522 C  CG2 . THR   A 198 ? 0.31508 0.27411 0.37922 0.07422  0.02117  0.04484  198 THR   A CG2 
1523 N  N   . THR   A 199 ? 0.27480 0.23012 0.30787 0.04262  0.00401  0.04539  199 THR   A N   
1524 C  CA  . THR   A 199 ? 0.27354 0.23778 0.30072 0.03439  -0.00127 0.05000  199 THR   A CA  
1525 C  C   . THR   A 199 ? 0.24401 0.23225 0.27049 0.03734  -0.00494 0.06098  199 THR   A C   
1526 O  O   . THR   A 199 ? 0.21108 0.20589 0.24611 0.04503  -0.00463 0.07124  199 THR   A O   
1527 C  CB  . THR   A 199 ? 0.28393 0.23194 0.31846 0.03024  -0.00025 0.05636  199 THR   A CB  
1528 O  OG1 . THR   A 199 ? 0.28624 0.21175 0.31926 0.02548  0.00206  0.04358  199 THR   A OG1 
1529 C  CG2 . THR   A 199 ? 0.23834 0.19781 0.26888 0.02202  -0.00411 0.06200  199 THR   A CG2 
1530 N  N   . ILE   A 200 ? 0.19929 0.20089 0.21564 0.03123  -0.00858 0.05838  200 ILE   A N   
1531 C  CA  . ILE   A 200 ? 0.17672 0.19996 0.18867 0.03253  -0.01195 0.06517  200 ILE   A CA  
1532 C  C   . ILE   A 200 ? 0.20062 0.22769 0.21377 0.03085  -0.01220 0.07768  200 ILE   A C   
1533 O  O   . ILE   A 200 ? 0.16887 0.19798 0.17718 0.02478  -0.01199 0.07815  200 ILE   A O   
1534 C  CB  . ILE   A 200 ? 0.16109 0.19479 0.16193 0.02733  -0.01424 0.05554  200 ILE   A CB  
1535 C  CG1 . ILE   A 200 ? 0.18914 0.21673 0.18799 0.02747  -0.01322 0.04336  200 ILE   A CG1 
1536 C  CG2 . ILE   A 200 ? 0.16704 0.21750 0.16269 0.02621  -0.01616 0.05579  200 ILE   A CG2 
1537 C  CD1 . ILE   A 200 ? 0.14831 0.17775 0.13846 0.02115  -0.01491 0.03434  200 ILE   A CD1 
1538 N  N   . THR   A 201 ? 0.17263 0.20081 0.19260 0.03507  -0.01166 0.08531  201 THR   A N   
1539 C  CA  . THR   A 201 ? 0.19010 0.21896 0.21189 0.03304  -0.01074 0.09576  201 THR   A CA  
1540 C  C   . THR   A 201 ? 0.20677 0.25138 0.21669 0.02713  -0.01174 0.09469  201 THR   A C   
1541 O  O   . THR   A 201 ? 0.20967 0.25317 0.21843 0.02293  -0.00954 0.09951  201 THR   A O   
1542 C  CB  . THR   A 201 ? 0.23307 0.26402 0.26355 0.03906  -0.01111 0.10413  201 THR   A CB  
1543 O  OG1 . THR   A 201 ? 0.23582 0.25135 0.27857 0.04580  -0.00848 0.10302  201 THR   A OG1 
1544 C  CG2 . THR   A 201 ? 0.26030 0.28969 0.29371 0.03748  -0.00991 0.11650  201 THR   A CG2 
1545 N  N   . VAL   A 202 ? 0.17615 0.23449 0.17831 0.02656  -0.01428 0.08824  202 VAL   A N   
1546 C  CA  . VAL   A 202 ? 0.19312 0.26341 0.18444 0.02175  -0.01422 0.08655  202 VAL   A CA  
1547 C  C   . VAL   A 202 ? 0.15541 0.22338 0.14249 0.01735  -0.01144 0.08101  202 VAL   A C   
1548 O  O   . VAL   A 202 ? 0.18001 0.25392 0.16207 0.01415  -0.00895 0.08366  202 VAL   A O   
1549 C  CB  . VAL   A 202 ? 0.17278 0.25445 0.15734 0.02090  -0.01735 0.07928  202 VAL   A CB  
1550 C  CG1 . VAL   A 202 ? 0.20759 0.28603 0.19207 0.02052  -0.01781 0.06768  202 VAL   A CG1 
1551 C  CG2 . VAL   A 202 ? 0.20675 0.29801 0.17941 0.01640  -0.01674 0.07742  202 VAL   A CG2 
1552 N  N   . ASN   A 203 ? 0.18023 0.24070 0.16961 0.01734  -0.01172 0.07402  203 ASN   A N   
1553 C  CA  . ASN   A 203 ? 0.15261 0.21250 0.13988 0.01322  -0.00991 0.06973  203 ASN   A CA  
1554 C  C   . ASN   A 203 ? 0.18916 0.24271 0.18355 0.01060  -0.00732 0.07969  203 ASN   A C   
1555 O  O   . ASN   A 203 ? 0.17088 0.23040 0.16442 0.00663  -0.00434 0.08093  203 ASN   A O   
1556 C  CB  . ASN   A 203 ? 0.18836 0.24246 0.17603 0.01354  -0.01210 0.06085  203 ASN   A CB  
1557 C  CG  . ASN   A 203 ? 0.14405 0.20425 0.12557 0.01360  -0.01325 0.04974  203 ASN   A CG  
1558 O  OD1 . ASN   A 203 ? 0.13192 0.19984 0.10909 0.01311  -0.01301 0.04849  203 ASN   A OD1 
1559 N  ND2 . ASN   A 203 ? 0.12155 0.17713 0.10307 0.01359  -0.01474 0.04243  203 ASN   A ND2 
1560 N  N   . VAL   A 204 ? 0.18727 0.22761 0.19073 0.01251  -0.00764 0.08684  204 VAL   A N   
1561 C  CA  . VAL   A 204 ? 0.17637 0.20753 0.18908 0.00846  -0.00483 0.09626  204 VAL   A CA  
1562 C  C   . VAL   A 204 ? 0.20674 0.24958 0.21649 0.00685  -0.00160 0.10358  204 VAL   A C   
1563 O  O   . VAL   A 204 ? 0.18859 0.23365 0.20210 0.00163  0.00185  0.10773  204 VAL   A O   
1564 C  CB  . VAL   A 204 ? 0.20573 0.21711 0.22956 0.01134  -0.00482 0.10130  204 VAL   A CB  
1565 C  CG1 . VAL   A 204 ? 0.23607 0.23677 0.27042 0.00568  -0.00167 0.10979  204 VAL   A CG1 
1566 C  CG2 . VAL   A 204 ? 0.19812 0.19559 0.22380 0.01165  -0.00651 0.08762  204 VAL   A CG2 
1567 N  N   . LEU   A 205 ? 0.17971 0.23050 0.18367 0.01087  -0.00277 0.10592  205 LEU   A N   
1568 C  CA  . LEU   A 205 ? 0.19724 0.25923 0.19569 0.00939  -0.00041 0.11296  205 LEU   A CA  
1569 C  C   . LEU   A 205 ? 0.18949 0.26380 0.17855 0.00601  0.00238  0.10634  205 LEU   A C   
1570 O  O   . LEU   A 205 ? 0.18311 0.26243 0.17184 0.00285  0.00696  0.11197  205 LEU   A O   
1571 C  CB  . LEU   A 205 ? 0.17918 0.24825 0.17250 0.01353  -0.00377 0.11608  205 LEU   A CB  
1572 C  CG  . LEU   A 205 ? 0.18549 0.24433 0.19003 0.01805  -0.00535 0.12531  205 LEU   A CG  
1573 C  CD1 . LEU   A 205 ? 0.20103 0.26981 0.20249 0.02229  -0.00967 0.12776  205 LEU   A CD1 
1574 C  CD2 . LEU   A 205 ? 0.22979 0.28131 0.24204 0.01619  -0.00189 0.13807  205 LEU   A CD2 
1575 N  N   . ALA   A 206 ? 0.16906 0.24739 0.15161 0.00679  0.00044  0.09428  206 ALA   A N   
1576 C  CA  . ALA   A 206 ? 0.19107 0.27863 0.16637 0.00448  0.00384  0.08715  206 ALA   A CA  
1577 C  C   . ALA   A 206 ? 0.19020 0.27697 0.17450 0.00084  0.00852  0.09067  206 ALA   A C   
1578 O  O   . ALA   A 206 ? 0.19790 0.29336 0.17968 -0.00103 0.01411  0.09151  206 ALA   A O   
1579 C  CB  . ALA   A 206 ? 0.19912 0.28707 0.16970 0.00574  0.00092  0.07395  206 ALA   A CB  
1580 N  N   . TRP   A 207 ? 0.17913 0.25529 0.17469 -0.00068 0.00649  0.09274  207 TRP   A N   
1581 C  CA  . TRP   A 207 ? 0.20426 0.27941 0.21175 -0.00602 0.00939  0.09586  207 TRP   A CA  
1582 C  C   . TRP   A 207 ? 0.20597 0.28033 0.22199 -0.00958 0.01366  0.10712  207 TRP   A C   
1583 O  O   . TRP   A 207 ? 0.19613 0.27733 0.22043 -0.01389 0.01842  0.10956  207 TRP   A O   
1584 C  CB  . TRP   A 207 ? 0.20687 0.26795 0.22231 -0.00770 0.00399  0.09180  207 TRP   A CB  
1585 C  CG  . TRP   A 207 ? 0.18402 0.23914 0.21546 -0.01489 0.00368  0.09098  207 TRP   A CG  
1586 C  CD1 . TRP   A 207 ? 0.20920 0.27207 0.24769 -0.01824 0.00352  0.08466  207 TRP   A CD1 
1587 C  CD2 . TRP   A 207 ? 0.19186 0.23153 0.23528 -0.01997 0.00237  0.09613  207 TRP   A CD2 
1588 N  NE1 . TRP   A 207 ? 0.17441 0.23047 0.22860 -0.02598 0.00136  0.08637  207 TRP   A NE1 
1589 C  CE2 . TRP   A 207 ? 0.18505 0.22549 0.24168 -0.02774 0.00075  0.09238  207 TRP   A CE2 
1590 C  CE3 . TRP   A 207 ? 0.22229 0.24722 0.26797 -0.01874 0.00248  0.10411  207 TRP   A CE3 
1591 C  CZ2 . TRP   A 207 ? 0.21547 0.24191 0.28566 -0.03579 -0.00136 0.09470  207 TRP   A CZ2 
1592 C  CZ3 . TRP   A 207 ? 0.23693 0.24546 0.29664 -0.02575 0.00174  0.10642  207 TRP   A CZ3 
1593 C  CH2 . TRP   A 207 ? 0.22447 0.23369 0.29542 -0.03493 -0.00041 0.10100  207 TRP   A CH2 
1594 N  N   . LEU   A 208 ? 0.20722 0.27408 0.22269 -0.00758 0.01230  0.11427  208 LEU   A N   
1595 C  CA  . LEU   A 208 ? 0.20647 0.27327 0.22785 -0.01046 0.01649  0.12554  208 LEU   A CA  
1596 C  C   . LEU   A 208 ? 0.22958 0.31297 0.24048 -0.01020 0.02200  0.12663  208 LEU   A C   
1597 O  O   . LEU   A 208 ? 0.24031 0.32838 0.25784 -0.01430 0.02767  0.13228  208 LEU   A O   
1598 C  CB  . LEU   A 208 ? 0.20956 0.26576 0.23193 -0.00719 0.01387  0.13332  208 LEU   A CB  
1599 C  CG  . LEU   A 208 ? 0.25181 0.28713 0.28731 -0.00824 0.01093  0.13354  208 LEU   A CG  
1600 C  CD1 . LEU   A 208 ? 0.25233 0.27762 0.28990 -0.00319 0.00941  0.14092  208 LEU   A CD1 
1601 C  CD2 . LEU   A 208 ? 0.24524 0.27185 0.29611 -0.01673 0.01330  0.13628  208 LEU   A CD2 
1602 N  N   . TYR   A 209 ? 0.25386 0.34547 0.24854 -0.00598 0.02059  0.12020  209 TYR   A N   
1603 C  CA  . TYR   A 209 ? 0.23104 0.33580 0.21307 -0.00611 0.02609  0.11792  209 TYR   A CA  
1604 C  C   . TYR   A 209 ? 0.23959 0.35064 0.22682 -0.00806 0.03184  0.11141  209 TYR   A C   
1605 O  O   . TYR   A 209 ? 0.20728 0.32641 0.19347 -0.00984 0.03951  0.11409  209 TYR   A O   
1606 C  CB  . TYR   A 209 ? 0.22330 0.33240 0.18822 -0.00262 0.02212  0.10988  209 TYR   A CB  
1607 C  CG  . TYR   A 209 ? 0.24823 0.35773 0.20643 -0.00119 0.01848  0.11836  209 TYR   A CG  
1608 C  CD1 . TYR   A 209 ? 0.26833 0.38436 0.21835 -0.00287 0.02264  0.12737  209 TYR   A CD1 
1609 C  CD2 . TYR   A 209 ? 0.23209 0.33615 0.19284 0.00197  0.01120  0.11820  209 TYR   A CD2 
1610 C  CE1 . TYR   A 209 ? 0.27971 0.39733 0.22399 -0.00156 0.01872  0.13673  209 TYR   A CE1 
1611 C  CE2 . TYR   A 209 ? 0.26700 0.37313 0.22409 0.00370  0.00776  0.12732  209 TYR   A CE2 
1612 C  CZ  . TYR   A 209 ? 0.29987 0.41298 0.24865 0.00186  0.01106  0.13687  209 TYR   A CZ  
1613 O  OH  . TYR   A 209 ? 0.34717 0.46348 0.29242 0.00354  0.00712  0.14730  209 TYR   A OH  
1614 N  N   . ALA   A 210 ? 0.19096 0.29917 0.18405 -0.00746 0.02874  0.10306  210 ALA   A N   
1615 C  CA  . ALA   A 210 ? 0.20531 0.31986 0.20868 -0.00924 0.03363  0.09886  210 ALA   A CA  
1616 C  C   . ALA   A 210 ? 0.22252 0.33823 0.24361 -0.01449 0.03774  0.10845  210 ALA   A C   
1617 O  O   . ALA   A 210 ? 0.18975 0.31527 0.21704 -0.01554 0.04501  0.10816  210 ALA   A O   
1618 C  CB  . ALA   A 210 ? 0.23530 0.34552 0.24519 -0.00897 0.02821  0.09181  210 ALA   A CB  
1619 N  N   . ALA   A 211 ? 0.20456 0.30923 0.23522 -0.01795 0.03337  0.11633  211 ALA   A N   
1620 C  CA  . ALA   A 211 ? 0.20236 0.30596 0.25134 -0.02437 0.03610  0.12451  211 ALA   A CA  
1621 C  C   . ALA   A 211 ? 0.24123 0.35319 0.28574 -0.02473 0.04407  0.13240  211 ALA   A C   
1622 O  O   . ALA   A 211 ? 0.20407 0.32449 0.26037 -0.02826 0.05015  0.13501  211 ALA   A O   
1623 C  CB  . ALA   A 211 ? 0.19213 0.27807 0.25045 -0.02813 0.02991  0.12959  211 ALA   A CB  
1624 N  N   . VAL   A 212 ? 0.23514 0.34572 0.26316 -0.02136 0.04396  0.13652  212 VAL   A N   
1625 C  CA  . VAL   A 212 ? 0.25624 0.37473 0.27687 -0.02219 0.05129  0.14461  212 VAL   A CA  
1626 C  C   . VAL   A 212 ? 0.26261 0.39502 0.27560 -0.02078 0.05973  0.13742  212 VAL   A C   
1627 O  O   . VAL   A 212 ? 0.26473 0.40519 0.28195 -0.02357 0.06840  0.14269  212 VAL   A O   
1628 C  CB  . VAL   A 212 ? 0.26170 0.37730 0.26515 -0.01884 0.04794  0.14980  212 VAL   A CB  
1629 C  CG1 . VAL   A 212 ? 0.26565 0.39075 0.25810 -0.02018 0.05576  0.15776  212 VAL   A CG1 
1630 C  CG2 . VAL   A 212 ? 0.23813 0.33893 0.25209 -0.01951 0.04156  0.15825  212 VAL   A CG2 
1631 N  N   . ILE   A 213 ? 0.25095 0.38549 0.25283 -0.01644 0.05806  0.12501  213 ILE   A N   
1632 C  CA  . ILE   A 213 ? 0.26819 0.41284 0.26441 -0.01462 0.06679  0.11627  213 ILE   A CA  
1633 C  C   . ILE   A 213 ? 0.26180 0.41264 0.28164 -0.01720 0.07204  0.11709  213 ILE   A C   
1634 O  O   . ILE   A 213 ? 0.29981 0.46042 0.32128 -0.01721 0.08244  0.11608  213 ILE   A O   
1635 C  CB  . ILE   A 213 ? 0.29246 0.43508 0.27566 -0.01000 0.06303  0.10233  213 ILE   A CB  
1636 C  CG1 . ILE   A 213 ? 0.30330 0.44300 0.26290 -0.00843 0.05887  0.10131  213 ILE   A CG1 
1637 C  CG2 . ILE   A 213 ? 0.29760 0.44742 0.28054 -0.00777 0.07234  0.09193  213 ILE   A CG2 
1638 C  CD1 . ILE   A 213 ? 0.27794 0.41316 0.22706 -0.00525 0.05198  0.08923  213 ILE   A CD1 
1639 N  N   . ASN   A 214 ? 0.25749 0.40291 0.29664 -0.02003 0.06497  0.11921  214 ASN   A N   
1640 C  CA  . ASN   A 214 ? 0.25376 0.40542 0.31753 -0.02319 0.06683  0.11930  214 ASN   A CA  
1641 C  C   . ASN   A 214 ? 0.26948 0.42089 0.35059 -0.03036 0.06784  0.13109  214 ASN   A C   
1642 O  O   . ASN   A 214 ? 0.27786 0.43367 0.38156 -0.03456 0.06680  0.13179  214 ASN   A O   
1643 C  CB  . ASN   A 214 ? 0.23215 0.37846 0.30572 -0.02311 0.05743  0.11271  214 ASN   A CB  
1644 C  CG  . ASN   A 214 ? 0.24909 0.40088 0.31668 -0.01669 0.05955  0.10078  214 ASN   A CG  
1645 O  OD1 . ASN   A 214 ? 0.27657 0.43709 0.35938 -0.01565 0.06320  0.09753  214 ASN   A OD1 
1646 N  ND2 . ASN   A 214 ? 0.29755 0.44397 0.34400 -0.01232 0.05732  0.09439  214 ASN   A ND2 
1647 N  N   . GLY   A 215 ? 0.27358 0.42004 0.34547 -0.03218 0.06923  0.14048  215 GLY   A N   
1648 C  CA  . GLY   A 215 ? 0.25683 0.40398 0.34332 -0.03884 0.07264  0.15206  215 GLY   A CA  
1649 C  C   . GLY   A 215 ? 0.28648 0.41797 0.38425 -0.04461 0.06438  0.15876  215 GLY   A C   
1650 O  O   . GLY   A 215 ? 0.29018 0.42064 0.40061 -0.05087 0.06713  0.16831  215 GLY   A O   
1651 N  N   . ASP   A 216 ? 0.27451 0.39293 0.36868 -0.04307 0.05506  0.15359  216 ASP   A N   
1652 C  CA  . ASP   A 216 ? 0.27108 0.37109 0.37332 -0.04777 0.04830  0.15839  216 ASP   A CA  
1653 C  C   . ASP   A 216 ? 0.32110 0.41385 0.40794 -0.04387 0.04915  0.16668  216 ASP   A C   
1654 O  O   . ASP   A 216 ? 0.31260 0.40491 0.38196 -0.03700 0.04659  0.16271  216 ASP   A O   
1655 C  CB  . ASP   A 216 ? 0.27805 0.36654 0.38195 -0.04748 0.03891  0.14871  216 ASP   A CB  
1656 C  CG  . ASP   A 216 ? 0.30049 0.39086 0.42390 -0.05438 0.03469  0.14276  216 ASP   A CG  
1657 O  OD1 . ASP   A 216 ? 0.34278 0.43356 0.48264 -0.06192 0.03584  0.14769  216 ASP   A OD1 
1658 O  OD2 . ASP   A 216 ? 0.26556 0.35713 0.38773 -0.05264 0.02944  0.13324  216 ASP   A OD2 
1659 N  N   . ARG   A 217 ? 0.32013 0.40770 0.41412 -0.04837 0.05219  0.17848  217 ARG   A N   
1660 C  CA  . ARG   A 217 ? 0.33825 0.42019 0.41928 -0.04455 0.05264  0.18808  217 ARG   A CA  
1661 C  C   . ARG   A 217 ? 0.31268 0.37425 0.40561 -0.04825 0.04918  0.19612  217 ARG   A C   
1662 O  O   . ARG   A 217 ? 0.30845 0.36471 0.39338 -0.04465 0.04906  0.20533  217 ARG   A O   
1663 C  CB  . ARG   A 217 ? 0.31195 0.40889 0.38385 -0.04464 0.06174  0.19715  217 ARG   A CB  
1664 C  CG  . ARG   A 217 ? 0.35518 0.47074 0.41892 -0.04257 0.06806  0.18903  217 ARG   A CG  
1665 C  CD  . ARG   A 217 ? 0.35045 0.47896 0.40107 -0.04254 0.07793  0.19707  217 ARG   A CD  
1666 N  NE  . ARG   A 217 ? 0.33197 0.45558 0.36735 -0.04017 0.07597  0.20708  217 ARG   A NE  
1667 C  CZ  . ARG   A 217 ? 0.34619 0.47459 0.35785 -0.03457 0.07441  0.20382  217 ARG   A CZ  
1668 N  NH1 . ARG   A 217 ? 0.31764 0.45328 0.31716 -0.03076 0.07466  0.18984  217 ARG   A NH1 
1669 N  NH2 . ARG   A 217 ? 0.35193 0.47736 0.35255 -0.03309 0.07201  0.21481  217 ARG   A NH2 
1670 N  N   . TRP   A 218 ? 0.31500 0.36456 0.42666 -0.05551 0.04616  0.19248  218 TRP   A N   
1671 C  CA  . TRP   A 218 ? 0.31147 0.33994 0.43551 -0.06059 0.04450  0.19932  218 TRP   A CA  
1672 C  C   . TRP   A 218 ? 0.32356 0.33424 0.44011 -0.05377 0.03977  0.19983  218 TRP   A C   
1673 O  O   . TRP   A 218 ? 0.33870 0.33343 0.46164 -0.05503 0.04027  0.20876  218 TRP   A O   
1674 C  CB  . TRP   A 218 ? 0.31452 0.33286 0.45733 -0.07036 0.04077  0.19130  218 TRP   A CB  
1675 C  CG  . TRP   A 218 ? 0.32448 0.33610 0.46531 -0.06901 0.03337  0.17629  218 TRP   A CG  
1676 C  CD1 . TRP   A 218 ? 0.32208 0.34815 0.46400 -0.06984 0.03130  0.16662  218 TRP   A CD1 
1677 C  CD2 . TRP   A 218 ? 0.33277 0.32117 0.47097 -0.06683 0.02759  0.16967  218 TRP   A CD2 
1678 N  NE1 . TRP   A 218 ? 0.31663 0.33055 0.45567 -0.06897 0.02405  0.15504  218 TRP   A NE1 
1679 C  CE2 . TRP   A 218 ? 0.32977 0.32020 0.46607 -0.06714 0.02209  0.15614  218 TRP   A CE2 
1680 C  CE3 . TRP   A 218 ? 0.37458 0.34049 0.51230 -0.06413 0.02705  0.17395  218 TRP   A CE3 
1681 C  CZ2 . TRP   A 218 ? 0.34021 0.31088 0.47262 -0.06532 0.01650  0.14640  218 TRP   A CZ2 
1682 C  CZ3 . TRP   A 218 ? 0.39231 0.33838 0.52734 -0.06139 0.02207  0.16374  218 TRP   A CZ3 
1683 C  CH2 . TRP   A 218 ? 0.36075 0.30922 0.49239 -0.06220 0.01705  0.14983  218 TRP   A CH2 
1684 N  N   . PHE   A 219 ? 0.31504 0.32796 0.41971 -0.04653 0.03549  0.19053  219 PHE   A N   
1685 C  CA  . PHE   A 219 ? 0.33804 0.33608 0.43717 -0.03926 0.03099  0.18942  219 PHE   A CA  
1686 C  C   . PHE   A 219 ? 0.32765 0.33562 0.41278 -0.03110 0.03193  0.19910  219 PHE   A C   
1687 O  O   . PHE   A 219 ? 0.31401 0.31203 0.39675 -0.02446 0.02840  0.20042  219 PHE   A O   
1688 C  CB  . PHE   A 219 ? 0.34805 0.34475 0.44194 -0.03607 0.02585  0.17476  219 PHE   A CB  
1689 C  CG  . PHE   A 219 ? 0.29205 0.31189 0.37431 -0.03380 0.02678  0.16899  219 PHE   A CG  
1690 C  CD1 . PHE   A 219 ? 0.27160 0.30440 0.33670 -0.02589 0.02666  0.16974  219 PHE   A CD1 
1691 C  CD2 . PHE   A 219 ? 0.26646 0.29513 0.35575 -0.03991 0.02769  0.16244  219 PHE   A CD2 
1692 C  CE1 . PHE   A 219 ? 0.26497 0.31624 0.31862 -0.02408 0.02805  0.16276  219 PHE   A CE1 
1693 C  CE2 . PHE   A 219 ? 0.29047 0.33891 0.37006 -0.03698 0.02953  0.15690  219 PHE   A CE2 
1694 C  CZ  . PHE   A 219 ? 0.25652 0.31499 0.31745 -0.02907 0.03011  0.15648  219 PHE   A CZ  
1695 N  N   . LEU   A 220 ? 0.31463 0.34228 0.39052 -0.03156 0.03654  0.20537  220 LEU   A N   
1696 C  CA  . LEU   A 220 ? 0.32383 0.36154 0.38517 -0.02565 0.03689  0.21474  220 LEU   A CA  
1697 C  C   . LEU   A 220 ? 0.35203 0.37716 0.42211 -0.02621 0.03792  0.23029  220 LEU   A C   
1698 O  O   . LEU   A 220 ? 0.36426 0.37530 0.45051 -0.03255 0.04027  0.23439  220 LEU   A O   
1699 C  CB  . LEU   A 220 ? 0.34194 0.40170 0.38976 -0.02716 0.04257  0.21621  220 LEU   A CB  
1700 C  CG  . LEU   A 220 ? 0.30057 0.37255 0.33855 -0.02539 0.04205  0.20102  220 LEU   A CG  
1701 C  CD1 . LEU   A 220 ? 0.30717 0.39814 0.33193 -0.02667 0.04924  0.20160  220 LEU   A CD1 
1702 C  CD2 . LEU   A 220 ? 0.30271 0.37406 0.32927 -0.01809 0.03493  0.19349  220 LEU   A CD2 
1703 N  N   . ASN   A 221 ? 0.37058 0.40104 0.43025 -0.01993 0.03581  0.23910  221 ASN   A N   
1704 C  CA  . ASN   A 221 ? 0.39600 0.41545 0.46377 -0.01910 0.03635  0.25531  221 ASN   A CA  
1705 C  C   . ASN   A 221 ? 0.43650 0.47164 0.48809 -0.01375 0.03465  0.26589  221 ASN   A C   
1706 O  O   . ASN   A 221 ? 0.39359 0.44470 0.42845 -0.01037 0.03188  0.25837  221 ASN   A O   
1707 C  CB  . ASN   A 221 ? 0.43918 0.43398 0.52246 -0.01593 0.03260  0.25261  221 ASN   A CB  
1708 C  CG  . ASN   A 221 ? 0.47048 0.46695 0.54729 -0.00699 0.02645  0.24425  221 ASN   A CG  
1709 O  OD1 . ASN   A 221 ? 0.48307 0.49288 0.54918 -0.00106 0.02344  0.25024  221 ASN   A OD1 
1710 N  ND2 . ASN   A 221 ? 0.45741 0.44097 0.54056 -0.00667 0.02442  0.23002  221 ASN   A ND2 
1711 N  N   . ARG   A 222 ? 0.44617 0.47660 0.50263 -0.01397 0.03636  0.28372  222 ARG   A N   
1712 C  CA  . ARG   A 222 ? 0.45599 0.50140 0.49741 -0.01002 0.03445  0.29636  222 ARG   A CA  
1713 C  C   . ARG   A 222 ? 0.49635 0.54071 0.53764 -0.00112 0.02649  0.29681  222 ARG   A C   
1714 O  O   . ARG   A 222 ? 0.53461 0.59581 0.56008 0.00206  0.02279  0.30180  222 ARG   A O   
1715 C  CB  . ARG   A 222 ? 0.51901 0.56013 0.56625 -0.01335 0.03897  0.31720  222 ARG   A CB  
1716 C  CG  . ARG   A 222 ? 0.52178 0.54184 0.58830 -0.00922 0.03633  0.32840  222 ARG   A CG  
1717 C  CD  . ARG   A 222 ? 0.54552 0.55828 0.62049 -0.01394 0.04172  0.34820  222 ARG   A CD  
1718 N  NE  . ARG   A 222 ? 0.59278 0.62256 0.65233 -0.01156 0.04080  0.36512  222 ARG   A NE  
1719 C  CZ  . ARG   A 222 ? 0.62725 0.65554 0.68918 -0.01497 0.04515  0.38506  222 ARG   A CZ  
1720 N  NH1 . ARG   A 222 ? 0.61811 0.62900 0.69790 -0.02151 0.05115  0.39055  222 ARG   A NH1 
1721 N  NH2 . ARG   A 222 ? 0.65841 0.70306 0.70404 -0.01243 0.04323  0.40007  222 ARG   A NH2 
1722 N  N   . PHE   A 223 ? 0.50879 0.53410 0.56714 0.00264  0.02398  0.29161  223 PHE   A N   
1723 C  CA  . PHE   A 223 ? 0.51730 0.54135 0.57909 0.01160  0.01757  0.29349  223 PHE   A CA  
1724 C  C   . PHE   A 223 ? 0.48092 0.52268 0.52720 0.01472  0.01234  0.28018  223 PHE   A C   
1725 O  O   . PHE   A 223 ? 0.45813 0.50765 0.49384 0.01073  0.01372  0.26634  223 PHE   A O   
1726 C  CB  . PHE   A 223 ? 0.51061 0.50878 0.59343 0.01505  0.01760  0.28854  223 PHE   A CB  
1727 C  CG  . PHE   A 223 ? 0.55058 0.52726 0.64785 0.00842  0.02344  0.29093  223 PHE   A CG  
1728 C  CD1 . PHE   A 223 ? 0.58428 0.55140 0.69138 0.00732  0.02632  0.30898  223 PHE   A CD1 
1729 C  CD2 . PHE   A 223 ? 0.55145 0.51724 0.65298 0.00268  0.02563  0.27534  223 PHE   A CD2 
1730 C  CE1 . PHE   A 223 ? 0.59884 0.54519 0.71997 0.00002  0.03153  0.31058  223 PHE   A CE1 
1731 C  CE2 . PHE   A 223 ? 0.55149 0.49778 0.66669 -0.00491 0.03021  0.27673  223 PHE   A CE2 
1732 C  CZ  . PHE   A 223 ? 0.60095 0.53708 0.72605 -0.00650 0.03326  0.29383  223 PHE   A CZ  
1733 N  N   . THR   A 224 ? 0.48833 0.53642 0.53471 0.02185  0.00625  0.28495  224 THR   A N   
1734 C  CA  . THR   A 224 ? 0.45905 0.52074 0.49536 0.02519  0.00049  0.27259  224 THR   A CA  
1735 C  C   . THR   A 224 ? 0.46510 0.51622 0.51824 0.03336  -0.00305 0.27161  224 THR   A C   
1736 O  O   . THR   A 224 ? 0.48890 0.52147 0.56026 0.03664  -0.00068 0.27979  224 THR   A O   
1737 C  CB  . THR   A 224 ? 0.47028 0.55589 0.48673 0.02461  -0.00396 0.27907  224 THR   A CB  
1738 O  OG1 . THR   A 224 ? 0.45168 0.54989 0.45413 0.02383  -0.00748 0.26242  224 THR   A OG1 
1739 C  CG2 . THR   A 224 ? 0.47046 0.56051 0.49421 0.03101  -0.00961 0.29556  224 THR   A CG2 
1740 N  N   . THR   A 225 ? 0.44712 0.50941 0.49455 0.03655  -0.00815 0.26103  225 THR   A N   
1741 C  CA  . THR   A 225 ? 0.45692 0.51286 0.51951 0.04467  -0.01113 0.25975  225 THR   A CA  
1742 C  C   . THR   A 225 ? 0.44778 0.52563 0.50031 0.04677  -0.01829 0.25585  225 THR   A C   
1743 O  O   . THR   A 225 ? 0.46968 0.56290 0.50301 0.04139  -0.02032 0.24824  225 THR   A O   
1744 C  CB  . THR   A 225 ? 0.43593 0.47204 0.50871 0.04558  -0.00738 0.24448  225 THR   A CB  
1745 O  OG1 . THR   A 225 ? 0.46911 0.49611 0.55876 0.05433  -0.00836 0.24551  225 THR   A OG1 
1746 C  CG2 . THR   A 225 ? 0.41408 0.45971 0.47263 0.04169  -0.00866 0.22638  225 THR   A CG2 
1747 N  N   . THR   A 226 ? 0.45288 0.53162 0.51940 0.05450  -0.02183 0.26116  226 THR   A N   
1748 C  CA  . THR   A 226 ? 0.46542 0.56333 0.52632 0.05626  -0.02867 0.25600  226 THR   A CA  
1749 C  C   . THR   A 226 ? 0.40928 0.50171 0.47092 0.05640  -0.02732 0.23632  226 THR   A C   
1750 O  O   . THR   A 226 ? 0.39116 0.46370 0.46245 0.05788  -0.02176 0.22913  226 THR   A O   
1751 C  CB  . THR   A 226 ? 0.45856 0.56204 0.53622 0.06465  -0.03301 0.27022  226 THR   A CB  
1752 O  OG1 . THR   A 226 ? 0.48126 0.56226 0.58153 0.07166  -0.02746 0.27362  226 THR   A OG1 
1753 C  CG2 . THR   A 226 ? 0.43894 0.55610 0.51069 0.06367  -0.03727 0.28980  226 THR   A CG2 
1754 N  N   . LEU   A 227 ? 0.41581 0.52570 0.46671 0.05442  -0.03269 0.22770  227 LEU   A N   
1755 C  CA  . LEU   A 227 ? 0.41820 0.52471 0.47026 0.05480  -0.03192 0.21047  227 LEU   A CA  
1756 C  C   . LEU   A 227 ? 0.41284 0.50750 0.48708 0.06365  -0.02976 0.21156  227 LEU   A C   
1757 O  O   . LEU   A 227 ? 0.40412 0.48355 0.48332 0.06490  -0.02506 0.20007  227 LEU   A O   
1758 C  CB  . LEU   A 227 ? 0.39879 0.52592 0.43757 0.05104  -0.03842 0.20292  227 LEU   A CB  
1759 C  CG  . LEU   A 227 ? 0.36120 0.48707 0.39754 0.04955  -0.03790 0.18478  227 LEU   A CG  
1760 C  CD1 . LEU   A 227 ? 0.36087 0.47175 0.39080 0.04570  -0.03166 0.17365  227 LEU   A CD1 
1761 C  CD2 . LEU   A 227 ? 0.34409 0.48875 0.36557 0.04406  -0.04413 0.17799  227 LEU   A CD2 
1762 N  N   . ASN   A 228 ? 0.40272 0.50379 0.49076 0.07020  -0.03277 0.22561  228 ASN   A N   
1763 C  CA  . ASN   A 228 ? 0.42879 0.51846 0.53954 0.07974  -0.02953 0.22704  228 ASN   A CA  
1764 C  C   . ASN   A 228 ? 0.42962 0.49113 0.55044 0.08225  -0.02134 0.22639  228 ASN   A C   
1765 O  O   . ASN   A 228 ? 0.42647 0.47220 0.55631 0.08617  -0.01624 0.21569  228 ASN   A O   
1766 C  CB  . ASN   A 228 ? 0.43554 0.53789 0.56067 0.08650  -0.03411 0.24452  228 ASN   A CB  
1767 C  CG  . ASN   A 228 ? 0.45929 0.58771 0.57944 0.08499  -0.04232 0.24348  228 ASN   A CG  
1768 O  OD1 . ASN   A 228 ? 0.48603 0.61830 0.60431 0.08395  -0.04252 0.22951  228 ASN   A OD1 
1769 N  ND2 . ASN   A 228 ? 0.47244 0.61896 0.59046 0.08445  -0.04945 0.25866  228 ASN   A ND2 
1770 N  N   . ASP   A 229 ? 0.44479 0.49916 0.56381 0.07955  -0.01984 0.23754  229 ASP   A N   
1771 C  CA  . ASP   A 229 ? 0.44367 0.47011 0.57377 0.08110  -0.01247 0.23794  229 ASP   A CA  
1772 C  C   . ASP   A 229 ? 0.44636 0.45903 0.56678 0.07477  -0.00842 0.22095  229 ASP   A C   
1773 O  O   . ASP   A 229 ? 0.45541 0.44379 0.58586 0.07690  -0.00261 0.21433  229 ASP   A O   
1774 C  CB  . ASP   A 229 ? 0.46442 0.48800 0.59535 0.07888  -0.01209 0.25516  229 ASP   A CB  
1775 C  CG  . ASP   A 229 ? 0.51281 0.53181 0.66436 0.08808  -0.01187 0.27168  229 ASP   A CG  
1776 O  OD1 . ASP   A 229 ? 0.51979 0.53756 0.68589 0.09651  -0.01140 0.26903  229 ASP   A OD1 
1777 O  OD2 . ASP   A 229 ? 0.54946 0.56689 0.70337 0.08720  -0.01192 0.28793  229 ASP   A OD2 
1778 N  N   . PHE   A 230 ? 0.42351 0.45063 0.52465 0.06696  -0.01133 0.21336  230 PHE   A N   
1779 C  CA  . PHE   A 230 ? 0.42186 0.43847 0.51514 0.06167  -0.00823 0.19754  230 PHE   A CA  
1780 C  C   . PHE   A 230 ? 0.40091 0.41185 0.50001 0.06668  -0.00716 0.18435  230 PHE   A C   
1781 O  O   . PHE   A 230 ? 0.39866 0.38963 0.50119 0.06632  -0.00261 0.17438  230 PHE   A O   
1782 C  CB  . PHE   A 230 ? 0.39051 0.42474 0.46326 0.05335  -0.01111 0.19203  230 PHE   A CB  
1783 C  CG  . PHE   A 230 ? 0.38657 0.41302 0.45230 0.04863  -0.00875 0.17631  230 PHE   A CG  
1784 C  CD1 . PHE   A 230 ? 0.35349 0.36360 0.42063 0.04357  -0.00432 0.17500  230 PHE   A CD1 
1785 C  CD2 . PHE   A 230 ? 0.34481 0.37980 0.40414 0.04905  -0.01112 0.16354  230 PHE   A CD2 
1786 C  CE1 . PHE   A 230 ? 0.34475 0.34846 0.40678 0.03923  -0.00287 0.16195  230 PHE   A CE1 
1787 C  CE2 . PHE   A 230 ? 0.36510 0.39297 0.41866 0.04516  -0.00927 0.15059  230 PHE   A CE2 
1788 C  CZ  . PHE   A 230 ? 0.33090 0.34351 0.38581 0.04043  -0.00541 0.15009  230 PHE   A CZ  
1789 N  N   . ASN   A 231 ? 0.41986 0.44836 0.52014 0.07093  -0.01126 0.18413  231 ASN   A N   
1790 C  CA  . ASN   A 231 ? 0.42276 0.44900 0.52803 0.07535  -0.00987 0.17182  231 ASN   A CA  
1791 C  C   . ASN   A 231 ? 0.41152 0.41583 0.53596 0.08397  -0.00347 0.17180  231 ASN   A C   
1792 O  O   . ASN   A 231 ? 0.42360 0.41670 0.55081 0.08661  0.00067  0.15906  231 ASN   A O   
1793 C  CB  . ASN   A 231 ? 0.36878 0.42003 0.47249 0.07690  -0.01581 0.17281  231 ASN   A CB  
1794 C  CG  . ASN   A 231 ? 0.34255 0.40917 0.42641 0.06835  -0.02011 0.16345  231 ASN   A CG  
1795 O  OD1 . ASN   A 231 ? 0.39582 0.45454 0.47140 0.06442  -0.01776 0.15152  231 ASN   A OD1 
1796 N  ND2 . ASN   A 231 ? 0.35689 0.44457 0.43315 0.06537  -0.02639 0.16867  231 ASN   A ND2 
1797 N  N   . LEU   A 232 ? 0.43557 0.43259 0.57284 0.08839  -0.00202 0.18542  232 LEU   A N   
1798 C  CA  . LEU   A 232 ? 0.43223 0.40463 0.58753 0.09617  0.00517  0.18461  232 LEU   A CA  
1799 C  C   . LEU   A 232 ? 0.44529 0.39037 0.59633 0.09125  0.01073  0.17289  232 LEU   A C   
1800 O  O   . LEU   A 232 ? 0.45138 0.37647 0.60958 0.09555  0.01696  0.16149  232 LEU   A O   
1801 C  CB  . LEU   A 232 ? 0.42828 0.39830 0.59742 0.10084  0.00514  0.20300  232 LEU   A CB  
1802 C  CG  . LEU   A 232 ? 0.45423 0.43716 0.64052 0.11114  0.00382  0.21317  232 LEU   A CG  
1803 C  CD1 . LEU   A 232 ? 0.46786 0.43500 0.67282 0.11781  0.00756  0.22742  232 LEU   A CD1 
1804 C  CD2 . LEU   A 232 ? 0.43865 0.42091 0.63258 0.11771  0.00768  0.19999  232 LEU   A CD2 
1805 N  N   . VAL   A 233 ? 0.45459 0.39893 0.59358 0.08171  0.00875  0.17485  233 VAL   A N   
1806 C  CA  . VAL   A 233 ? 0.44896 0.36922 0.58415 0.07519  0.01285  0.16446  233 VAL   A CA  
1807 C  C   . VAL   A 233 ? 0.44907 0.37196 0.57237 0.07175  0.01230  0.14805  233 VAL   A C   
1808 O  O   . VAL   A 233 ? 0.46655 0.36724 0.59052 0.07044  0.01671  0.13510  233 VAL   A O   
1809 C  CB  . VAL   A 233 ? 0.46368 0.38399 0.59299 0.06613  0.01145  0.17389  233 VAL   A CB  
1810 C  CG1 . VAL   A 233 ? 0.46008 0.36897 0.57995 0.05627  0.01263  0.16202  233 VAL   A CG1 
1811 C  CG2 . VAL   A 233 ? 0.48114 0.38413 0.62503 0.06869  0.01485  0.18596  233 VAL   A CG2 
1812 N  N   . ALA   A 234 ? 0.45052 0.39959 0.56214 0.06975  0.00686  0.14772  234 ALA   A N   
1813 C  CA  . ALA   A 234 ? 0.41952 0.37263 0.52060 0.06712  0.00607  0.13354  234 ALA   A CA  
1814 C  C   . ALA   A 234 ? 0.42296 0.36383 0.53223 0.07469  0.01095  0.12250  234 ALA   A C   
1815 O  O   . ALA   A 234 ? 0.43337 0.35886 0.53832 0.07244  0.01418  0.10931  234 ALA   A O   
1816 C  CB  . ALA   A 234 ? 0.39052 0.37352 0.47976 0.06488  -0.00025 0.13489  234 ALA   A CB  
1817 N  N   . MET   A 235 ? 0.41559 0.36378 0.53679 0.08357  0.01194  0.12762  235 MET   A N   
1818 C  CA  . MET   A 235 ? 0.43948 0.37879 0.56948 0.09154  0.01802  0.11730  235 MET   A CA  
1819 C  C   . MET   A 235 ? 0.44894 0.35429 0.58311 0.09198  0.02594  0.10740  235 MET   A C   
1820 O  O   . MET   A 235 ? 0.43557 0.32864 0.56594 0.09286  0.03115  0.09176  235 MET   A O   
1821 C  CB  . MET   A 235 ? 0.44564 0.39863 0.59101 0.10073  0.01797  0.12730  235 MET   A CB  
1822 C  CG  . MET   A 235 ? 0.50145 0.45127 0.65739 0.10958  0.02479  0.11794  235 MET   A CG  
1823 S  SD  . MET   A 235 ? 0.66181 0.63350 0.83740 0.11924  0.02302  0.13239  235 MET   A SD  
1824 C  CE  . MET   A 235 ? 0.47096 0.47826 0.63351 0.11174  0.01146  0.13741  235 MET   A CE  
1825 N  N   . LYS   A 236 ? 0.46527 0.35469 0.60552 0.09009  0.02691  0.11540  236 LYS   A N   
1826 C  CA  . LYS   A 236 ? 0.44477 0.30033 0.58878 0.08903  0.03388  0.10536  236 LYS   A CA  
1827 C  C   . LYS   A 236 ? 0.44233 0.28393 0.57163 0.07886  0.03392  0.09020  236 LYS   A C   
1828 O  O   . LYS   A 236 ? 0.46423 0.28131 0.59153 0.07800  0.03981  0.07437  236 LYS   A O   
1829 C  CB  . LYS   A 236 ? 0.44241 0.28558 0.59586 0.08755  0.03395  0.11856  236 LYS   A CB  
1830 C  CG  . LYS   A 236 ? 0.50314 0.31039 0.65801 0.08277  0.03955  0.10789  236 LYS   A CG  
1831 C  CD  . LYS   A 236 ? 0.53892 0.33008 0.71068 0.08864  0.04358  0.11818  236 LYS   A CD  
1832 C  CE  . LYS   A 236 ? 0.53003 0.31593 0.70300 0.08020  0.04042  0.13132  236 LYS   A CE  
1833 N  NZ  . LYS   A 236 ? 0.55956 0.32353 0.72290 0.06718  0.04074  0.11872  236 LYS   A NZ  
1834 N  N   . TYR   A 237 ? 0.43895 0.29630 0.55717 0.07072  0.02743  0.09398  237 TYR   A N   
1835 C  CA  . TYR   A 237 ? 0.40033 0.24723 0.50644 0.06022  0.02634  0.08205  237 TYR   A CA  
1836 C  C   . TYR   A 237 ? 0.38799 0.24903 0.48369 0.06113  0.02507  0.07254  237 TYR   A C   
1837 O  O   . TYR   A 237 ? 0.37991 0.24031 0.46562 0.05242  0.02220  0.06660  237 TYR   A O   
1838 C  CB  . TYR   A 237 ? 0.42245 0.27616 0.52507 0.05002  0.02109  0.09272  237 TYR   A CB  
1839 C  CG  . TYR   A 237 ? 0.43848 0.27242 0.55020 0.04641  0.02338  0.09875  237 TYR   A CG  
1840 C  CD1 . TYR   A 237 ? 0.47274 0.27953 0.58363 0.03722  0.02546  0.08721  237 TYR   A CD1 
1841 C  CD2 . TYR   A 237 ? 0.46099 0.30304 0.58197 0.05160  0.02316  0.11545  237 TYR   A CD2 
1842 C  CE1 . TYR   A 237 ? 0.45521 0.24315 0.57478 0.03333  0.02750  0.09254  237 TYR   A CE1 
1843 C  CE2 . TYR   A 237 ? 0.48058 0.30356 0.61080 0.04865  0.02569  0.12182  237 TYR   A CE2 
1844 C  CZ  . TYR   A 237 ? 0.49089 0.28653 0.62064 0.03959  0.02803  0.11033  237 TYR   A CZ  
1845 O  OH  . TYR   A 237 ? 0.51032 0.28651 0.64949 0.03592  0.03040  0.11663  237 TYR   A OH  
1846 N  N   . ASN   A 238 ? 0.37302 0.24757 0.47226 0.07111  0.02717  0.07160  238 ASN   A N   
1847 C  CA  . ASN   A 238 ? 0.38068 0.26750 0.47117 0.07275  0.02742  0.06193  238 ASN   A CA  
1848 C  C   . ASN   A 238 ? 0.33212 0.24462 0.41351 0.06782  0.01908  0.06979  238 ASN   A C   
1849 O  O   . ASN   A 238 ? 0.33298 0.25513 0.39989 0.06211  0.01670  0.05836  238 ASN   A O   
1850 C  CB  . ASN   A 238 ? 0.38388 0.24689 0.46370 0.06743  0.03262  0.04184  238 ASN   A CB  
1851 C  CG  . ASN   A 238 ? 0.41911 0.29627 0.48750 0.06902  0.03422  0.02944  238 ASN   A CG  
1852 O  OD1 . ASN   A 238 ? 0.46119 0.33157 0.51247 0.06084  0.03437  0.01319  238 ASN   A OD1 
1853 N  ND2 . ASN   A 238 ? 0.40798 0.30454 0.48715 0.07978  0.03579  0.03771  238 ASN   A ND2 
1854 N  N   . TYR   A 239 ? 0.35108 0.27861 0.43407 0.06566  0.01353  0.08431  239 TYR   A N   
1855 C  CA  . TYR   A 239 ? 0.32043 0.27404 0.39276 0.06073  0.00628  0.09021  239 TYR   A CA  
1856 C  C   . TYR   A 239 ? 0.30224 0.27997 0.37662 0.06626  0.00353  0.09372  239 TYR   A C   
1857 O  O   . TYR   A 239 ? 0.29292 0.27008 0.37948 0.07314  0.00580  0.09854  239 TYR   A O   
1858 C  CB  . TYR   A 239 ? 0.31504 0.27184 0.38555 0.05428  0.00335  0.10157  239 TYR   A CB  
1859 C  CG  . TYR   A 239 ? 0.29748 0.24257 0.36288 0.04467  0.00328  0.09934  239 TYR   A CG  
1860 C  CD1 . TYR   A 239 ? 0.30973 0.22678 0.38019 0.04159  0.00727  0.09090  239 TYR   A CD1 
1861 C  CD2 . TYR   A 239 ? 0.28039 0.24265 0.33624 0.03755  -0.00040 0.10427  239 TYR   A CD2 
1862 C  CE1 . TYR   A 239 ? 0.33025 0.24070 0.39602 0.02951  0.00570  0.08639  239 TYR   A CE1 
1863 C  CE2 . TYR   A 239 ? 0.29294 0.24777 0.34698 0.02826  -0.00029 0.10331  239 TYR   A CE2 
1864 C  CZ  . TYR   A 239 ? 0.28917 0.21933 0.34887 0.02356  0.00205  0.09425  239 TYR   A CZ  
1865 O  OH  . TYR   A 239 ? 0.27780 0.20496 0.33626 0.01217  0.00088  0.09085  239 TYR   A OH  
1866 N  N   . GLU   A 240 ? 0.28606 0.28458 0.34940 0.06243  -0.00143 0.09100  240 GLU   A N   
1867 C  CA  . GLU   A 240 ? 0.31924 0.33862 0.38539 0.06554  -0.00422 0.09270  240 GLU   A CA  
1868 C  C   . GLU   A 240 ? 0.30800 0.34189 0.37221 0.06262  -0.00912 0.10364  240 GLU   A C   
1869 O  O   . GLU   A 240 ? 0.30162 0.33288 0.35950 0.05758  -0.01016 0.10871  240 GLU   A O   
1870 C  CB  . GLU   A 240 ? 0.32415 0.35681 0.38046 0.06225  -0.00658 0.08303  240 GLU   A CB  
1871 C  CG  . GLU   A 240 ? 0.27970 0.32106 0.32022 0.05314  -0.01111 0.08010  240 GLU   A CG  
1872 C  CD  . GLU   A 240 ? 0.30780 0.35667 0.34099 0.05085  -0.01197 0.06940  240 GLU   A CD  
1873 O  OE1 . GLU   A 240 ? 0.37628 0.42786 0.41737 0.05639  -0.00941 0.06627  240 GLU   A OE1 
1874 O  OE2 . GLU   A 240 ? 0.32872 0.38161 0.34930 0.04355  -0.01448 0.06414  240 GLU   A OE2 
1875 N  N   . PRO   A 241 ? 0.31939 0.36835 0.39039 0.06606  -0.01161 0.10846  241 PRO   A N   
1876 C  CA  . PRO   A 241 ? 0.30863 0.36971 0.37865 0.06429  -0.01601 0.12002  241 PRO   A CA  
1877 C  C   . PRO   A 241 ? 0.28501 0.35810 0.33685 0.05504  -0.02034 0.11727  241 PRO   A C   
1878 O  O   . PRO   A 241 ? 0.32982 0.40828 0.37170 0.05036  -0.02154 0.10652  241 PRO   A O   
1879 C  CB  . PRO   A 241 ? 0.32106 0.39715 0.40234 0.06937  -0.01846 0.12416  241 PRO   A CB  
1880 C  CG  . PRO   A 241 ? 0.34146 0.41190 0.43194 0.07476  -0.01374 0.11536  241 PRO   A CG  
1881 C  CD  . PRO   A 241 ? 0.34979 0.40134 0.43407 0.07352  -0.00884 0.10575  241 PRO   A CD  
1882 N  N   . LEU   A 242 ? 0.31565 0.39200 0.36364 0.05268  -0.02187 0.12698  242 LEU   A N   
1883 C  CA  . LEU   A 242 ? 0.29236 0.38084 0.32388 0.04502  -0.02495 0.12533  242 LEU   A CA  
1884 C  C   . LEU   A 242 ? 0.29937 0.40656 0.32948 0.04477  -0.03081 0.13060  242 LEU   A C   
1885 O  O   . LEU   A 242 ? 0.27371 0.38457 0.31437 0.04966  -0.03253 0.14285  242 LEU   A O   
1886 C  CB  . LEU   A 242 ? 0.30749 0.38976 0.33490 0.04232  -0.02256 0.13318  242 LEU   A CB  
1887 C  CG  . LEU   A 242 ? 0.29381 0.38363 0.30411 0.03469  -0.02268 0.12787  242 LEU   A CG  
1888 C  CD1 . LEU   A 242 ? 0.27272 0.35487 0.27840 0.03157  -0.01988 0.11468  242 LEU   A CD1 
1889 C  CD2 . LEU   A 242 ? 0.31719 0.40522 0.32538 0.03281  -0.02044 0.13917  242 LEU   A CD2 
1890 N  N   . THR   A 243 ? 0.28793 0.40616 0.30573 0.03897  -0.03400 0.12162  243 THR   A N   
1891 C  CA  . THR   A 243 ? 0.31724 0.45295 0.33245 0.03739  -0.04042 0.12531  243 THR   A CA  
1892 C  C   . THR   A 243 ? 0.30788 0.45162 0.30663 0.03160  -0.04278 0.12813  243 THR   A C   
1893 O  O   . THR   A 243 ? 0.31127 0.44833 0.29960 0.02806  -0.03886 0.12422  243 THR   A O   
1894 C  CB  . THR   A 243 ? 0.29429 0.43650 0.30781 0.03447  -0.04278 0.11349  243 THR   A CB  
1895 O  OG1 . THR   A 243 ? 0.31957 0.45807 0.31782 0.02777  -0.04107 0.10111  243 THR   A OG1 
1896 C  CG2 . THR   A 243 ? 0.28363 0.41845 0.31201 0.04016  -0.03947 0.11023  243 THR   A CG2 
1897 N  N   . GLN   A 244 ? 0.31836 0.47767 0.31496 0.03071  -0.04936 0.13522  244 GLN   A N   
1898 C  CA  . GLN   A 244 ? 0.31011 0.47883 0.28823 0.02468  -0.05242 0.13620  244 GLN   A CA  
1899 C  C   . GLN   A 244 ? 0.34317 0.50945 0.30588 0.01806  -0.05073 0.11980  244 GLN   A C   
1900 O  O   . GLN   A 244 ? 0.34016 0.50622 0.28716 0.01388  -0.04872 0.11758  244 GLN   A O   
1901 C  CB  . GLN   A 244 ? 0.30458 0.49139 0.28249 0.02417  -0.06115 0.14490  244 GLN   A CB  
1902 C  CG  . GLN   A 244 ? 0.32728 0.52344 0.28406 0.01811  -0.06447 0.14680  244 GLN   A CG  
1903 C  CD  . GLN   A 244 ? 0.34366 0.53319 0.29506 0.01906  -0.05933 0.15577  244 GLN   A CD  
1904 O  OE1 . GLN   A 244 ? 0.34387 0.52870 0.30938 0.02481  -0.05749 0.16855  244 GLN   A OE1 
1905 N  NE2 . GLN   A 244 ? 0.37618 0.56437 0.30794 0.01351  -0.05629 0.14899  244 GLN   A NE2 
1906 N  N   . ASP   A 245 ? 0.31823 0.48219 0.28579 0.01734  -0.05090 0.10858  245 ASP   A N   
1907 C  CA  . ASP   A 245 ? 0.33430 0.49319 0.28991 0.01184  -0.04849 0.09338  245 ASP   A CA  
1908 C  C   . ASP   A 245 ? 0.33722 0.48236 0.29058 0.01224  -0.04083 0.08899  245 ASP   A C   
1909 O  O   . ASP   A 245 ? 0.35440 0.49738 0.29459 0.00808  -0.03817 0.08159  245 ASP   A O   
1910 C  CB  . ASP   A 245 ? 0.35457 0.51338 0.31739 0.01104  -0.05004 0.08393  245 ASP   A CB  
1911 C  CG  . ASP   A 245 ? 0.38505 0.54176 0.33470 0.00455  -0.04977 0.07009  245 ASP   A CG  
1912 O  OD1 . ASP   A 245 ? 0.41997 0.58395 0.35545 -0.00005 -0.05328 0.06904  245 ASP   A OD1 
1913 O  OD2 . ASP   A 245 ? 0.40907 0.55609 0.36190 0.00421  -0.04584 0.06060  245 ASP   A OD2 
1914 N  N   . HIS   A 246 ? 0.32240 0.45815 0.28873 0.01720  -0.03723 0.09317  246 HIS   A N   
1915 C  CA  . HIS   A 246 ? 0.29991 0.42427 0.26480 0.01708  -0.03098 0.09122  246 HIS   A CA  
1916 C  C   . HIS   A 246 ? 0.31977 0.44751 0.27498 0.01511  -0.02927 0.09881  246 HIS   A C   
1917 O  O   . HIS   A 246 ? 0.32065 0.44488 0.26799 0.01223  -0.02475 0.09385  246 HIS   A O   
1918 C  CB  . HIS   A 246 ? 0.29266 0.40614 0.27231 0.02246  -0.02833 0.09636  246 HIS   A CB  
1919 C  CG  . HIS   A 246 ? 0.26715 0.37590 0.25518 0.02478  -0.02845 0.08877  246 HIS   A CG  
1920 N  ND1 . HIS   A 246 ? 0.26761 0.37088 0.26978 0.03099  -0.02793 0.09433  246 HIS   A ND1 
1921 C  CD2 . HIS   A 246 ? 0.28260 0.39068 0.26713 0.02200  -0.02838 0.07653  246 HIS   A CD2 
1922 C  CE1 . HIS   A 246 ? 0.29061 0.39143 0.29658 0.03192  -0.02746 0.08572  246 HIS   A CE1 
1923 N  NE2 . HIS   A 246 ? 0.26417 0.36800 0.25964 0.02618  -0.02797 0.07528  246 HIS   A NE2 
1924 N  N   . VAL   A 247 ? 0.31231 0.44720 0.26900 0.01699  -0.03242 0.11190  247 VAL   A N   
1925 C  CA  . VAL   A 247 ? 0.32361 0.46281 0.26999 0.01492  -0.03085 0.12056  247 VAL   A CA  
1926 C  C   . VAL   A 247 ? 0.34447 0.49084 0.27114 0.00925  -0.03108 0.11159  247 VAL   A C   
1927 O  O   . VAL   A 247 ? 0.35780 0.50267 0.27426 0.00669  -0.02587 0.11047  247 VAL   A O   
1928 C  CB  . VAL   A 247 ? 0.35110 0.49790 0.30249 0.01802  -0.03530 0.13692  247 VAL   A CB  
1929 C  CG1 . VAL   A 247 ? 0.35498 0.50825 0.29247 0.01510  -0.03425 0.14611  247 VAL   A CG1 
1930 C  CG2 . VAL   A 247 ? 0.34037 0.47660 0.31153 0.02415  -0.03333 0.14591  247 VAL   A CG2 
1931 N  N   . ASP   A 248 ? 0.34233 0.49616 0.26366 0.00714  -0.03676 0.10501  248 ASP   A N   
1932 C  CA  . ASP   A 248 ? 0.37893 0.53720 0.28092 0.00159  -0.03713 0.09506  248 ASP   A CA  
1933 C  C   . ASP   A 248 ? 0.34600 0.49400 0.24493 0.00001  -0.03031 0.08191  248 ASP   A C   
1934 O  O   . ASP   A 248 ? 0.37532 0.52306 0.25973 -0.00276 -0.02570 0.07815  248 ASP   A O   
1935 C  CB  . ASP   A 248 ? 0.34566 0.51239 0.24526 -0.00085 -0.04500 0.09011  248 ASP   A CB  
1936 C  CG  . ASP   A 248 ? 0.35600 0.53622 0.25670 0.00014  -0.05258 0.10390  248 ASP   A CG  
1937 O  OD1 . ASP   A 248 ? 0.40276 0.58613 0.30013 0.00159  -0.05168 0.11643  248 ASP   A OD1 
1938 O  OD2 . ASP   A 248 ? 0.38480 0.57324 0.29043 -0.00062 -0.05960 0.10313  248 ASP   A OD2 
1939 N  N   . ILE   A 249 ? 0.34122 0.48094 0.25370 0.00205  -0.02916 0.07544  249 ILE   A N   
1940 C  CA  . ILE   A 249 ? 0.34350 0.47420 0.25516 0.00100  -0.02344 0.06414  249 ILE   A CA  
1941 C  C   . ILE   A 249 ? 0.32277 0.45023 0.23350 0.00169  -0.01658 0.06887  249 ILE   A C   
1942 O  O   . ILE   A 249 ? 0.34554 0.47029 0.24932 -0.00005 -0.01120 0.06142  249 ILE   A O   
1943 C  CB  . ILE   A 249 ? 0.33199 0.45501 0.25844 0.00326  -0.02395 0.05874  249 ILE   A CB  
1944 C  CG1 . ILE   A 249 ? 0.35064 0.47690 0.27695 0.00135  -0.02920 0.05193  249 ILE   A CG1 
1945 C  CG2 . ILE   A 249 ? 0.33607 0.45018 0.26452 0.00312  -0.01828 0.05080  249 ILE   A CG2 
1946 C  CD1 . ILE   A 249 ? 0.36148 0.48583 0.30336 0.00475  -0.03150 0.05412  249 ILE   A CD1 
1947 N  N   . LEU   A 250 ? 0.31982 0.44752 0.23844 0.00423  -0.01626 0.08179  250 LEU   A N   
1948 C  CA  . LEU   A 250 ? 0.32905 0.45439 0.24839 0.00416  -0.00985 0.08825  250 LEU   A CA  
1949 C  C   . LEU   A 250 ? 0.34260 0.47574 0.24550 0.00144  -0.00709 0.09303  250 LEU   A C   
1950 O  O   . LEU   A 250 ? 0.32321 0.45572 0.22595 0.00080  -0.00077 0.09893  250 LEU   A O   
1951 C  CB  . LEU   A 250 ? 0.31231 0.43247 0.24702 0.00744  -0.01030 0.10061  250 LEU   A CB  
1952 C  CG  . LEU   A 250 ? 0.29357 0.40357 0.24293 0.01005  -0.01101 0.09629  250 LEU   A CG  
1953 C  CD1 . LEU   A 250 ? 0.26859 0.37195 0.23138 0.01360  -0.01184 0.10862  250 LEU   A CD1 
1954 C  CD2 . LEU   A 250 ? 0.26186 0.36634 0.21323 0.00834  -0.00604 0.08903  250 LEU   A CD2 
1955 N  N   . GLY   A 251 ? 0.33154 0.47210 0.22018 -0.00062 -0.01145 0.09068  251 GLY   A N   
1956 C  CA  . GLY   A 251 ? 0.34895 0.49685 0.21834 -0.00351 -0.00930 0.09460  251 GLY   A CA  
1957 C  C   . GLY   A 251 ? 0.35250 0.49805 0.21150 -0.00549 0.00055  0.08857  251 GLY   A C   
1958 O  O   . GLY   A 251 ? 0.37659 0.52489 0.23059 -0.00619 0.00627  0.09768  251 GLY   A O   
1959 N  N   . PRO   A 252 ? 0.38047 0.52105 0.23633 -0.00634 0.00339  0.07363  252 PRO   A N   
1960 C  CA  . PRO   A 252 ? 0.38123 0.51976 0.22861 -0.00739 0.01413  0.06766  252 PRO   A CA  
1961 C  C   . PRO   A 252 ? 0.36653 0.50404 0.22818 -0.00591 0.02089  0.07638  252 PRO   A C   
1962 O  O   . PRO   A 252 ? 0.37507 0.51582 0.22892 -0.00722 0.02946  0.08054  252 PRO   A O   
1963 C  CB  . PRO   A 252 ? 0.38910 0.52076 0.23810 -0.00723 0.01471  0.05172  252 PRO   A CB  
1964 C  CG  . PRO   A 252 ? 0.39246 0.52495 0.23913 -0.00837 0.00454  0.04803  252 PRO   A CG  
1965 C  CD  . PRO   A 252 ? 0.37948 0.51662 0.23780 -0.00665 -0.00231 0.06184  252 PRO   A CD  
1966 N  N   . LEU   A 253 ? 0.35736 0.49032 0.23952 -0.00361 0.01754  0.07927  253 LEU   A N   
1967 C  CA  . LEU   A 253 ? 0.31706 0.44841 0.21429 -0.00302 0.02276  0.08775  253 LEU   A CA  
1968 C  C   . LEU   A 253 ? 0.32808 0.46308 0.22452 -0.00392 0.02377  0.10359  253 LEU   A C   
1969 O  O   . LEU   A 253 ? 0.31982 0.45673 0.21878 -0.00548 0.03167  0.11005  253 LEU   A O   
1970 C  CB  . LEU   A 253 ? 0.29035 0.41468 0.20667 -0.00086 0.01777  0.08735  253 LEU   A CB  
1971 C  CG  . LEU   A 253 ? 0.28500 0.40553 0.20602 -0.00008 0.01845  0.07438  253 LEU   A CG  
1972 C  CD1 . LEU   A 253 ? 0.24079 0.35419 0.17802 0.00163  0.01336  0.07529  253 LEU   A CD1 
1973 C  CD2 . LEU   A 253 ? 0.27084 0.39433 0.19327 -0.00101 0.02818  0.07235  253 LEU   A CD2 
1974 N  N   . SER   A 254 ? 0.32256 0.45898 0.21697 -0.00296 0.01612  0.11070  254 SER   A N   
1975 C  CA  . SER   A 254 ? 0.34333 0.48367 0.23509 -0.00359 0.01651  0.12656  254 SER   A CA  
1976 C  C   . SER   A 254 ? 0.36685 0.51440 0.23867 -0.00674 0.02394  0.12762  254 SER   A C   
1977 O  O   . SER   A 254 ? 0.39894 0.54798 0.27268 -0.00828 0.03064  0.13826  254 SER   A O   
1978 C  CB  . SER   A 254 ? 0.34224 0.48543 0.23268 -0.00171 0.00685  0.13247  254 SER   A CB  
1979 O  OG  . SER   A 254 ? 0.37363 0.51937 0.26550 -0.00144 0.00652  0.14972  254 SER   A OG  
1980 N  N   . ALA   A 255 ? 0.36471 0.51598 0.21677 -0.00810 0.02339  0.11649  255 ALA   A N   
1981 C  CA  . ALA   A 255 ? 0.42082 0.57789 0.24983 -0.01108 0.03070  0.11650  255 ALA   A CA  
1982 C  C   . ALA   A 255 ? 0.40414 0.55976 0.23547 -0.01201 0.04389  0.11284  255 ALA   A C   
1983 O  O   . ALA   A 255 ? 0.42416 0.58435 0.24494 -0.01418 0.05247  0.11978  255 ALA   A O   
1984 C  CB  . ALA   A 255 ? 0.43872 0.59750 0.24624 -0.01260 0.02707  0.10343  255 ALA   A CB  
1985 N  N   . GLN   A 256 ? 0.39728 0.54754 0.24333 -0.01040 0.04596  0.10287  256 GLN   A N   
1986 C  CA  . GLN   A 256 ? 0.37723 0.52786 0.23009 -0.01087 0.05828  0.10001  256 GLN   A CA  
1987 C  C   . GLN   A 256 ? 0.39776 0.55021 0.26845 -0.01194 0.06181  0.11529  256 GLN   A C   
1988 O  O   . GLN   A 256 ? 0.42612 0.58303 0.29664 -0.01389 0.07316  0.11864  256 GLN   A O   
1989 C  CB  . GLN   A 256 ? 0.37260 0.51806 0.23788 -0.00864 0.05818  0.08669  256 GLN   A CB  
1990 C  CG  . GLN   A 256 ? 0.41627 0.56358 0.28897 -0.00845 0.07109  0.08151  256 GLN   A CG  
1991 C  CD  . GLN   A 256 ? 0.41657 0.55989 0.30772 -0.00592 0.06890  0.07323  256 GLN   A CD  
1992 O  OE1 . GLN   A 256 ? 0.41710 0.55517 0.30951 -0.00456 0.05890  0.06822  256 GLN   A OE1 
1993 N  NE2 . GLN   A 256 ? 0.40016 0.54693 0.30680 -0.00537 0.07822  0.07230  256 GLN   A NE2 
1994 N  N   . THR   A 257 ? 0.37065 0.51904 0.25712 -0.01098 0.05305  0.12464  257 THR   A N   
1995 C  CA  . THR   A 257 ? 0.35270 0.49987 0.25728 -0.01263 0.05591  0.13877  257 THR   A CA  
1996 C  C   . THR   A 257 ? 0.36838 0.51832 0.26533 -0.01420 0.05552  0.15465  257 THR   A C   
1997 O  O   . THR   A 257 ? 0.39586 0.54536 0.30462 -0.01665 0.06043  0.16684  257 THR   A O   
1998 C  CB  . THR   A 257 ? 0.33110 0.46926 0.25782 -0.01107 0.04821  0.14007  257 THR   A CB  
1999 O  OG1 . THR   A 257 ? 0.34557 0.48018 0.26794 -0.00829 0.03788  0.14032  257 THR   A OG1 
2000 C  CG2 . THR   A 257 ? 0.28774 0.42418 0.22345 -0.01009 0.04937  0.12671  257 THR   A CG2 
2001 N  N   . GLY   A 258 ? 0.35449 0.50766 0.23271 -0.01328 0.04973  0.15538  258 GLY   A N   
2002 C  CA  . GLY   A 258 ? 0.39195 0.54832 0.26389 -0.01425 0.04799  0.17191  258 GLY   A CA  
2003 C  C   . GLY   A 258 ? 0.37992 0.52900 0.27182 -0.01213 0.04030  0.18396  258 GLY   A C   
2004 O  O   . GLY   A 258 ? 0.40875 0.55852 0.30156 -0.01290 0.04036  0.20018  258 GLY   A O   
2005 N  N   . ILE   A 259 ? 0.37756 0.51867 0.28524 -0.00938 0.03436  0.17663  259 ILE   A N   
2006 C  CA  . ILE   A 259 ? 0.37698 0.50849 0.30370 -0.00687 0.02820  0.18586  259 ILE   A CA  
2007 C  C   . ILE   A 259 ? 0.37983 0.51236 0.30255 -0.00283 0.01832  0.18105  259 ILE   A C   
2008 O  O   . ILE   A 259 ? 0.35385 0.48569 0.27551 -0.00164 0.01550  0.16650  259 ILE   A O   
2009 C  CB  . ILE   A 259 ? 0.35156 0.47185 0.30004 -0.00747 0.03009  0.18181  259 ILE   A CB  
2010 C  CG1 . ILE   A 259 ? 0.38602 0.50632 0.34227 -0.01230 0.03935  0.18877  259 ILE   A CG1 
2011 C  CG2 . ILE   A 259 ? 0.34974 0.45720 0.31535 -0.00443 0.02386  0.18802  259 ILE   A CG2 
2012 C  CD1 . ILE   A 259 ? 0.34871 0.46250 0.32212 -0.01423 0.04148  0.18092  259 ILE   A CD1 
2013 N  N   . ALA   A 260 ? 0.36404 0.49898 0.28549 -0.00086 0.01320  0.19390  260 ALA   A N   
2014 C  CA  . ALA   A 260 ? 0.38676 0.52478 0.30696 0.00284  0.00388  0.19125  260 ALA   A CA  
2015 C  C   . ALA   A 260 ? 0.32566 0.45239 0.26475 0.00633  0.00084  0.18371  260 ALA   A C   
2016 O  O   . ALA   A 260 ? 0.35362 0.46812 0.30913 0.00665  0.00417  0.18671  260 ALA   A O   
2017 C  CB  . ALA   A 260 ? 0.37494 0.51716 0.29556 0.00489  -0.00059 0.20926  260 ALA   A CB  
2018 N  N   . VAL   A 261 ? 0.35473 0.48507 0.29079 0.00834  -0.00525 0.17338  261 VAL   A N   
2019 C  CA  . VAL   A 261 ? 0.32196 0.44212 0.27343 0.01150  -0.00733 0.16534  261 VAL   A CA  
2020 C  C   . VAL   A 261 ? 0.33066 0.43993 0.30092 0.01572  -0.00829 0.17771  261 VAL   A C   
2021 O  O   . VAL   A 261 ? 0.32441 0.41953 0.30843 0.01644  -0.00536 0.17585  261 VAL   A O   
2022 C  CB  . VAL   A 261 ? 0.32544 0.45230 0.27129 0.01273  -0.01364 0.15429  261 VAL   A CB  
2023 C  CG1 . VAL   A 261 ? 0.26910 0.38564 0.23104 0.01660  -0.01543 0.14835  261 VAL   A CG1 
2024 C  CG2 . VAL   A 261 ? 0.28656 0.41940 0.21588 0.00854  -0.01185 0.14009  261 VAL   A CG2 
2025 N  N   . LEU   A 262 ? 0.36169 0.47662 0.33275 0.01842  -0.01225 0.19091  262 LEU   A N   
2026 C  CA  . LEU   A 262 ? 0.37424 0.47772 0.36429 0.02335  -0.01271 0.20312  262 LEU   A CA  
2027 C  C   . LEU   A 262 ? 0.35608 0.44643 0.35480 0.02100  -0.00612 0.21146  262 LEU   A C   
2028 O  O   . LEU   A 262 ? 0.33881 0.41265 0.35517 0.02398  -0.00464 0.21591  262 LEU   A O   
2029 C  CB  . LEU   A 262 ? 0.37595 0.49006 0.36548 0.02672  -0.01831 0.21746  262 LEU   A CB  
2030 C  CG  . LEU   A 262 ? 0.39387 0.51939 0.38225 0.02989  -0.02583 0.21264  262 LEU   A CG  
2031 C  CD1 . LEU   A 262 ? 0.40968 0.52389 0.41542 0.03513  -0.02602 0.20502  262 LEU   A CD1 
2032 C  CD2 . LEU   A 262 ? 0.42259 0.56247 0.38989 0.02467  -0.02855 0.20029  262 LEU   A CD2 
2033 N  N   . ASP   A 263 ? 0.34210 0.43874 0.32907 0.01542  -0.00165 0.21332  263 ASP   A N   
2034 C  CA  . ASP   A 263 ? 0.37714 0.46233 0.37339 0.01179  0.00508  0.21992  263 ASP   A CA  
2035 C  C   . ASP   A 263 ? 0.33477 0.40686 0.34138 0.01001  0.00782  0.20735  263 ASP   A C   
2036 O  O   . ASP   A 263 ? 0.33879 0.39377 0.36157 0.00933  0.01028  0.21131  263 ASP   A O   
2037 C  CB  . ASP   A 263 ? 0.34987 0.44696 0.33080 0.00628  0.01010  0.22425  263 ASP   A CB  
2038 C  CG  . ASP   A 263 ? 0.39142 0.49823 0.36333 0.00705  0.00828  0.24075  263 ASP   A CG  
2039 O  OD1 . ASP   A 263 ? 0.40269 0.50906 0.38067 0.01207  0.00232  0.24874  263 ASP   A OD1 
2040 O  OD2 . ASP   A 263 ? 0.40597 0.52124 0.36490 0.00268  0.01315  0.24646  263 ASP   A OD2 
2041 N  N   . MET   A 264 ? 0.33310 0.41211 0.33048 0.00879  0.00726  0.19212  264 MET   A N   
2042 C  CA  . MET   A 264 ? 0.29897 0.36666 0.30558 0.00754  0.00849  0.18067  264 MET   A CA  
2043 C  C   . MET   A 264 ? 0.32126 0.37385 0.34110 0.01251  0.00500  0.17916  264 MET   A C   
2044 O  O   . MET   A 264 ? 0.31794 0.35445 0.34939 0.01092  0.00679  0.17536  264 MET   A O   
2045 C  CB  . MET   A 264 ? 0.30879 0.38703 0.30316 0.00628  0.00803  0.16541  264 MET   A CB  
2046 C  CG  . MET   A 264 ? 0.26133 0.33112 0.26385 0.00327  0.01042  0.15597  264 MET   A CG  
2047 S  SD  . MET   A 264 ? 0.26098 0.33001 0.27083 -0.00387 0.01796  0.16224  264 MET   A SD  
2048 C  CE  . MET   A 264 ? 0.25747 0.34594 0.25020 -0.00547 0.02201  0.15406  264 MET   A CE  
2049 N  N   . CYS   A 265 ? 0.34207 0.39946 0.36063 0.01830  0.00019  0.18163  265 CYS   A N   
2050 C  CA  . CYS   A 265 ? 0.31353 0.35652 0.34608 0.02407  -0.00171 0.18112  265 CYS   A CA  
2051 C  C   . CYS   A 265 ? 0.32324 0.34733 0.37141 0.02440  0.00170  0.19198  265 CYS   A C   
2052 O  O   . CYS   A 265 ? 0.33967 0.34416 0.39965 0.02560  0.00327  0.18700  265 CYS   A O   
2053 C  CB  . CYS   A 265 ? 0.34092 0.39514 0.37177 0.03013  -0.00709 0.18382  265 CYS   A CB  
2054 S  SG  . CYS   A 265 ? 0.29949 0.36991 0.31626 0.02957  -0.01146 0.16806  265 CYS   A SG  
2055 N  N   . ALA   A 266 ? 0.35730 0.38570 0.40519 0.02297  0.00308  0.20650  266 ALA   A N   
2056 C  CA  . ALA   A 266 ? 0.34014 0.34970 0.40300 0.02202  0.00684  0.21701  266 ALA   A CA  
2057 C  C   . ALA   A 266 ? 0.36226 0.35667 0.43119 0.01499  0.01106  0.20916  266 ALA   A C   
2058 O  O   . ALA   A 266 ? 0.38592 0.35737 0.46907 0.01487  0.01293  0.20825  266 ALA   A O   
2059 C  CB  . ALA   A 266 ? 0.37630 0.39546 0.43531 0.02020  0.00804  0.23393  266 ALA   A CB  
2060 N  N   . SER   A 267 ? 0.33571 0.34238 0.39445 0.00886  0.01255  0.20265  267 SER   A N   
2061 C  CA  . SER   A 267 ? 0.33032 0.32594 0.39611 0.00142  0.01576  0.19562  267 SER   A CA  
2062 C  C   . SER   A 267 ? 0.34842 0.32898 0.41954 0.00281  0.01356  0.18191  267 SER   A C   
2063 O  O   . SER   A 267 ? 0.35812 0.31842 0.44084 -0.00175 0.01511  0.17839  267 SER   A O   
2064 C  CB  . SER   A 267 ? 0.34153 0.35610 0.39644 -0.00401 0.01805  0.19165  267 SER   A CB  
2065 O  OG  . SER   A 267 ? 0.38565 0.40971 0.43740 -0.00676 0.02182  0.20431  267 SER   A OG  
2066 N  N   . LEU   A 268 ? 0.32628 0.31620 0.38834 0.00823  0.00995  0.17335  268 LEU   A N   
2067 C  CA  . LEU   A 268 ? 0.33733 0.31313 0.40339 0.01045  0.00822  0.16123  268 LEU   A CA  
2068 C  C   . LEU   A 268 ? 0.36071 0.31332 0.44008 0.01516  0.00920  0.16379  268 LEU   A C   
2069 O  O   . LEU   A 268 ? 0.39784 0.32894 0.48467 0.01280  0.01040  0.15525  268 LEU   A O   
2070 C  CB  . LEU   A 268 ? 0.32520 0.31665 0.37967 0.01583  0.00444  0.15326  268 LEU   A CB  
2071 C  CG  . LEU   A 268 ? 0.29994 0.28024 0.35621 0.01868  0.00286  0.14078  268 LEU   A CG  
2072 C  CD1 . LEU   A 268 ? 0.31230 0.27880 0.37258 0.01090  0.00416  0.13326  268 LEU   A CD1 
2073 C  CD2 . LEU   A 268 ? 0.29217 0.29138 0.33610 0.02197  -0.00065 0.13332  268 LEU   A CD2 
2074 N  N   . LYS   A 269 ? 0.33985 0.29605 0.42237 0.02164  0.00880  0.17492  269 LYS   A N   
2075 C  CA  . LYS   A 269 ? 0.37506 0.30940 0.47204 0.02692  0.01074  0.17876  269 LYS   A CA  
2076 C  C   . LYS   A 269 ? 0.40714 0.31745 0.51436 0.01950  0.01462  0.17890  269 LYS   A C   
2077 O  O   . LYS   A 269 ? 0.42285 0.30840 0.53835 0.01996  0.01656  0.17008  269 LYS   A O   
2078 C  CB  . LYS   A 269 ? 0.38711 0.33179 0.48720 0.03326  0.00962  0.19446  269 LYS   A CB  
2079 C  CG  . LYS   A 269 ? 0.42976 0.35149 0.54696 0.03836  0.01261  0.20136  269 LYS   A CG  
2080 C  CD  . LYS   A 269 ? 0.46126 0.39273 0.58431 0.04871  0.01037  0.21162  269 LYS   A CD  
2081 C  CE  . LYS   A 269 ? 0.46863 0.43041 0.57917 0.04811  0.00566  0.22167  269 LYS   A CE  
2082 N  NZ  . LYS   A 269 ? 0.53382 0.50522 0.65197 0.05692  0.00269  0.23427  269 LYS   A NZ  
2083 N  N   . GLU   A 270 ? 0.41374 0.33097 0.52004 0.01197  0.01608  0.18791  270 GLU   A N   
2084 C  CA  . GLU   A 270 ? 0.43336 0.32968 0.55038 0.00336  0.01943  0.18875  270 GLU   A CA  
2085 C  C   . GLU   A 270 ? 0.43811 0.32269 0.55524 -0.00454 0.01896  0.17230  270 GLU   A C   
2086 O  O   . GLU   A 270 ? 0.46743 0.32619 0.59366 -0.00949 0.02049  0.16596  270 GLU   A O   
2087 C  CB  . GLU   A 270 ? 0.43698 0.34713 0.55292 -0.00318 0.02151  0.20205  270 GLU   A CB  
2088 C  CG  . GLU   A 270 ? 0.46283 0.37610 0.58210 0.00221  0.02250  0.21992  270 GLU   A CG  
2089 C  CD  . GLU   A 270 ? 0.52834 0.41390 0.66281 0.00607  0.02423  0.22338  270 GLU   A CD  
2090 O  OE1 . GLU   A 270 ? 0.57563 0.46242 0.71274 0.01622  0.02286  0.22982  270 GLU   A OE1 
2091 O  OE2 . GLU   A 270 ? 0.58377 0.44633 0.72809 -0.00128 0.02695  0.21934  270 GLU   A OE2 
2092 N  N   . LEU   A 271 ? 0.40082 0.30375 0.50754 -0.00641 0.01655  0.16483  271 LEU   A N   
2093 C  CA  . LEU   A 271 ? 0.40568 0.29992 0.51264 -0.01406 0.01504  0.15001  271 LEU   A CA  
2094 C  C   . LEU   A 271 ? 0.44641 0.31839 0.55460 -0.00946 0.01430  0.13712  271 LEU   A C   
2095 O  O   . LEU   A 271 ? 0.43545 0.28796 0.54706 -0.01705 0.01384  0.12494  271 LEU   A O   
2096 C  CB  . LEU   A 271 ? 0.39704 0.31666 0.49319 -0.01541 0.01276  0.14624  271 LEU   A CB  
2097 C  CG  . LEU   A 271 ? 0.38763 0.32670 0.48350 -0.02246 0.01472  0.15367  271 LEU   A CG  
2098 C  CD1 . LEU   A 271 ? 0.35422 0.31846 0.43769 -0.02053 0.01345  0.14988  271 LEU   A CD1 
2099 C  CD2 . LEU   A 271 ? 0.40747 0.33532 0.51509 -0.03467 0.01497  0.14908  271 LEU   A CD2 
2100 N  N   . LEU   A 272 ? 0.42782 0.30320 0.53308 0.00257  0.01426  0.13882  272 LEU   A N   
2101 C  CA  . LEU   A 272 ? 0.41901 0.27470 0.52604 0.00862  0.01520  0.12665  272 LEU   A CA  
2102 C  C   . LEU   A 272 ? 0.47321 0.29955 0.59137 0.00839  0.01905  0.12585  272 LEU   A C   
2103 O  O   . LEU   A 272 ? 0.50239 0.30497 0.62111 0.00632  0.02057  0.11084  272 LEU   A O   
2104 C  CB  . LEU   A 272 ? 0.41380 0.28514 0.51713 0.02144  0.01434  0.12972  272 LEU   A CB  
2105 C  CG  . LEU   A 272 ? 0.37701 0.27311 0.46789 0.02220  0.01052  0.12616  272 LEU   A CG  
2106 C  CD1 . LEU   A 272 ? 0.40393 0.31800 0.49242 0.03315  0.00896  0.13104  272 LEU   A CD1 
2107 C  CD2 . LEU   A 272 ? 0.38487 0.26998 0.47172 0.01866  0.00994  0.10994  272 LEU   A CD2 
2108 N  N   . GLN   A 273 ? 0.49080 0.31777 0.61676 0.01004  0.02077  0.14126  273 GLN   A N   
2109 C  CA  . GLN   A 273 ? 0.51526 0.31433 0.65285 0.01118  0.02468  0.14245  273 GLN   A CA  
2110 C  C   . GLN   A 273 ? 0.52503 0.30453 0.66658 -0.00287 0.02547  0.13792  273 GLN   A C   
2111 O  O   . GLN   A 273 ? 0.56193 0.31231 0.71008 -0.00428 0.02836  0.13155  273 GLN   A O   
2112 C  CB  . GLN   A 273 ? 0.49599 0.30353 0.64155 0.01885  0.02586  0.16218  273 GLN   A CB  
2113 C  CG  . GLN   A 273 ? 0.49565 0.32001 0.64053 0.03252  0.02468  0.16681  273 GLN   A CG  
2114 C  CD  . GLN   A 273 ? 0.52628 0.36533 0.67665 0.03782  0.02396  0.18757  273 GLN   A CD  
2115 O  OE1 . GLN   A 273 ? 0.56582 0.40749 0.71731 0.03125  0.02429  0.19922  273 GLN   A OE1 
2116 N  NE2 . GLN   A 273 ? 0.51903 0.36883 0.67314 0.04933  0.02291  0.19258  273 GLN   A NE2 
2117 N  N   . ASN   A 274 ? 0.51223 0.30754 0.65038 -0.01350 0.02310  0.14062  274 ASN   A N   
2118 C  CA  . ASN   A 274 ? 0.52475 0.30649 0.66875 -0.02786 0.02338  0.13823  274 ASN   A CA  
2119 C  C   . ASN   A 274 ? 0.53632 0.32091 0.67466 -0.03939 0.01956  0.12301  274 ASN   A C   
2120 O  O   . ASN   A 274 ? 0.54800 0.31996 0.69130 -0.05243 0.01881  0.11772  274 ASN   A O   
2121 C  CB  . ASN   A 274 ? 0.51043 0.30907 0.65988 -0.03195 0.02476  0.15696  274 ASN   A CB  
2122 C  CG  . ASN   A 274 ? 0.57071 0.37092 0.72491 -0.02134 0.02746  0.17406  274 ASN   A CG  
2123 O  OD1 . ASN   A 274 ? 0.58762 0.36886 0.74672 -0.01303 0.02912  0.17273  274 ASN   A OD1 
2124 N  ND2 . ASN   A 274 ? 0.56728 0.39067 0.72026 -0.02164 0.02807  0.19023  274 ASN   A ND2 
2125 N  N   . GLY   A 275 ? 0.53169 0.33294 0.66056 -0.03561 0.01666  0.11619  275 GLY   A N   
2126 C  CA  . GLY   A 275 ? 0.54206 0.35089 0.66724 -0.04669 0.01226  0.10474  275 GLY   A CA  
2127 C  C   . GLY   A 275 ? 0.52835 0.36298 0.65800 -0.05372 0.01163  0.11618  275 GLY   A C   
2128 O  O   . GLY   A 275 ? 0.50157 0.35004 0.63341 -0.04914 0.01479  0.13205  275 GLY   A O   
2129 N  N   . MET   A 276 ? 0.56100 0.40307 0.69188 -0.06510 0.00746  0.10724  276 MET   A N   
2130 C  CA  . MET   A 276 ? 0.51838 0.38810 0.65407 -0.07058 0.00720  0.11586  276 MET   A CA  
2131 C  C   . MET   A 276 ? 0.56312 0.42766 0.71170 -0.08391 0.00754  0.11776  276 MET   A C   
2132 O  O   . MET   A 276 ? 0.51980 0.40619 0.67524 -0.08786 0.00925  0.12719  276 MET   A O   
2133 C  CB  . MET   A 276 ? 0.52066 0.40867 0.65066 -0.07217 0.00195  0.10650  276 MET   A CB  
2134 C  CG  . MET   A 276 ? 0.46389 0.36872 0.58272 -0.05942 0.00332  0.11165  276 MET   A CG  
2135 S  SD  . MET   A 276 ? 0.58220 0.51142 0.69422 -0.05973 -0.00144 0.10478  276 MET   A SD  
2136 C  CE  . MET   A 276 ? 0.38883 0.33964 0.51343 -0.06997 -0.00098 0.10964  276 MET   A CE  
2137 N  N   . ASN   A 277 ? 0.60046 0.43616 0.75201 -0.09072 0.00665  0.10875  277 ASN   A N   
2138 C  CA  . ASN   A 277 ? 0.58159 0.40709 0.74534 -0.10314 0.00774  0.11167  277 ASN   A CA  
2139 C  C   . ASN   A 277 ? 0.57280 0.41923 0.74481 -0.11568 0.00340  0.10827  277 ASN   A C   
2140 O  O   . ASN   A 277 ? 0.57171 0.42864 0.75617 -0.12252 0.00593  0.11865  277 ASN   A O   
2141 C  CB  . ASN   A 277 ? 0.61366 0.44095 0.78442 -0.09857 0.01443  0.13132  277 ASN   A CB  
2142 C  CG  . ASN   A 277 ? 0.67432 0.48196 0.85713 -0.11028 0.01626  0.13402  277 ASN   A CG  
2143 O  OD1 . ASN   A 277 ? 0.72680 0.50614 0.90889 -0.11679 0.01434  0.12135  277 ASN   A OD1 
2144 N  ND2 . ASN   A 277 ? 0.68716 0.50914 0.88007 -0.11351 0.02036  0.15004  277 ASN   A ND2 
2145 N  N   . GLY   A 278 ? 0.53169 0.38528 0.69753 -0.11840 -0.00328 0.09407  278 GLY   A N   
2146 C  CA  . GLY   A 278 ? 0.53480 0.40917 0.70931 -0.12939 -0.00884 0.08993  278 GLY   A CA  
2147 C  C   . GLY   A 278 ? 0.49483 0.40441 0.67466 -0.12444 -0.00732 0.10111  278 GLY   A C   
2148 O  O   . GLY   A 278 ? 0.49462 0.42382 0.68483 -0.13214 -0.01096 0.10013  278 GLY   A O   
2149 N  N   . ARG   A 279 ? 0.48502 0.40360 0.65769 -0.11163 -0.00184 0.11125  279 ARG   A N   
2150 C  CA  . ARG   A 279 ? 0.42790 0.37797 0.60197 -0.10617 0.00108  0.12009  279 ARG   A CA  
2151 C  C   . ARG   A 279 ? 0.39076 0.35077 0.55268 -0.09845 -0.00275 0.11241  279 ARG   A C   
2152 O  O   . ARG   A 279 ? 0.41495 0.35782 0.56721 -0.09666 -0.00715 0.10185  279 ARG   A O   
2153 C  CB  . ARG   A 279 ? 0.42941 0.38468 0.60140 -0.09840 0.01007  0.13640  279 ARG   A CB  
2154 C  CG  . ARG   A 279 ? 0.45408 0.40452 0.63976 -0.10677 0.01430  0.14617  279 ARG   A CG  
2155 C  CD  . ARG   A 279 ? 0.47136 0.42225 0.65207 -0.09891 0.02203  0.16175  279 ARG   A CD  
2156 N  NE  . ARG   A 279 ? 0.50986 0.43573 0.68220 -0.09236 0.02152  0.16121  279 ARG   A NE  
2157 C  CZ  . ARG   A 279 ? 0.48698 0.40426 0.65821 -0.08761 0.02627  0.17396  279 ARG   A CZ  
2158 N  NH1 . ARG   A 279 ? 0.47823 0.40867 0.65440 -0.08950 0.03204  0.18837  279 ARG   A NH1 
2159 N  NH2 . ARG   A 279 ? 0.48350 0.37917 0.64887 -0.08041 0.02536  0.17255  279 ARG   A NH2 
2160 N  N   . THR   A 280 ? 0.36885 0.35620 0.53117 -0.09394 -0.00044 0.11725  280 THR   A N   
2161 C  CA  . THR   A 280 ? 0.31786 0.31646 0.46979 -0.08718 -0.00354 0.11085  280 THR   A CA  
2162 C  C   . THR   A 280 ? 0.28523 0.30175 0.42848 -0.07641 0.00427  0.12012  280 THR   A C   
2163 O  O   . THR   A 280 ? 0.26377 0.29000 0.41043 -0.07532 0.01147  0.13062  280 THR   A O   
2164 C  CB  . THR   A 280 ? 0.30789 0.32228 0.46791 -0.09305 -0.01043 0.10285  280 THR   A CB  
2165 O  OG1 . THR   A 280 ? 0.30507 0.34100 0.47881 -0.09497 -0.00576 0.11095  280 THR   A OG1 
2166 C  CG2 . THR   A 280 ? 0.32912 0.32594 0.49257 -0.10401 -0.01942 0.09139  280 THR   A CG2 
2167 N  N   . ILE   A 281 ? 0.26544 0.28536 0.39561 -0.06892 0.00274  0.11536  281 ILE   A N   
2168 C  CA  . ILE   A 281 ? 0.23578 0.27216 0.35370 -0.05890 0.00900  0.12044  281 ILE   A CA  
2169 C  C   . ILE   A 281 ? 0.24447 0.29649 0.36030 -0.05687 0.00642  0.11261  281 ILE   A C   
2170 O  O   . ILE   A 281 ? 0.23742 0.28142 0.34881 -0.05740 -0.00025 0.10429  281 ILE   A O   
2171 C  CB  . ILE   A 281 ? 0.21481 0.23908 0.31706 -0.05044 0.00993  0.12285  281 ILE   A CB  
2172 C  CG1 . ILE   A 281 ? 0.23313 0.24137 0.33925 -0.05140 0.01232  0.13115  281 ILE   A CG1 
2173 C  CG2 . ILE   A 281 ? 0.21314 0.25538 0.29997 -0.04116 0.01466  0.12521  281 ILE   A CG2 
2174 C  CD1 . ILE   A 281 ? 0.26864 0.26714 0.36204 -0.04167 0.01288  0.13480  281 ILE   A CD1 
2175 N  N   . LEU   A 282 ? 0.23559 0.30891 0.35450 -0.05421 0.01217  0.11497  282 LEU   A N   
2176 C  CA  . LEU   A 282 ? 0.25324 0.34189 0.37231 -0.05086 0.01108  0.10788  282 LEU   A CA  
2177 C  C   . LEU   A 282 ? 0.24294 0.32733 0.37262 -0.05776 0.00039  0.09973  282 LEU   A C   
2178 O  O   . LEU   A 282 ? 0.25849 0.34425 0.38232 -0.05517 -0.00480 0.09188  282 LEU   A O   
2179 C  CB  . LEU   A 282 ? 0.19422 0.28478 0.29356 -0.04183 0.01324  0.10454  282 LEU   A CB  
2180 C  CG  . LEU   A 282 ? 0.18949 0.29005 0.27608 -0.03469 0.02292  0.10910  282 LEU   A CG  
2181 C  CD1 . LEU   A 282 ? 0.22482 0.32530 0.28955 -0.02662 0.02333  0.10436  282 LEU   A CD1 
2182 C  CD2 . LEU   A 282 ? 0.21402 0.33214 0.30949 -0.03361 0.03020  0.10919  282 LEU   A CD2 
2183 N  N   . GLY   A 283 ? 0.24711 0.32556 0.39034 -0.06671 -0.00358 0.10070  283 GLY   A N   
2184 C  CA  . GLY   A 283 ? 0.30710 0.38129 0.45728 -0.07417 -0.01474 0.09207  283 GLY   A CA  
2185 C  C   . GLY   A 283 ? 0.30481 0.35734 0.44330 -0.07732 -0.02277 0.08325  283 GLY   A C   
2186 O  O   . GLY   A 283 ? 0.34978 0.40041 0.48680 -0.08145 -0.03239 0.07379  283 GLY   A O   
2187 N  N   . SER   A 284 ? 0.29609 0.33178 0.42456 -0.07454 -0.01893 0.08586  284 SER   A N   
2188 C  CA  . SER   A 284 ? 0.29650 0.30865 0.41047 -0.07382 -0.02439 0.07502  284 SER   A CA  
2189 C  C   . SER   A 284 ? 0.31453 0.30331 0.43352 -0.07931 -0.02238 0.07887  284 SER   A C   
2190 O  O   . SER   A 284 ? 0.28280 0.27327 0.40670 -0.07679 -0.01467 0.09030  284 SER   A O   
2191 C  CB  . SER   A 284 ? 0.30242 0.31415 0.39605 -0.06014 -0.02124 0.07104  284 SER   A CB  
2192 O  OG  . SER   A 284 ? 0.31374 0.30413 0.39435 -0.05814 -0.02474 0.06062  284 SER   A OG  
2193 N  N   . ALA   A 285 ? 0.30706 0.27383 0.42164 -0.08515 -0.02870 0.06718  285 ALA   A N   
2194 C  CA  . ALA   A 285 ? 0.31683 0.25698 0.43262 -0.08735 -0.02571 0.06669  285 ALA   A CA  
2195 C  C   . ALA   A 285 ? 0.35978 0.28054 0.46143 -0.07700 -0.02272 0.06248  285 ALA   A C   
2196 O  O   . ALA   A 285 ? 0.36039 0.25506 0.46387 -0.07807 -0.02037 0.06053  285 ALA   A O   
2197 C  CB  . ALA   A 285 ? 0.33308 0.26027 0.45125 -0.09941 -0.03219 0.05425  285 ALA   A CB  
2198 N  N   . LEU   A 286 ? 0.31880 0.25280 0.40611 -0.06556 -0.02184 0.05980  286 LEU   A N   
2199 C  CA  . LEU   A 286 ? 0.37844 0.30127 0.45305 -0.05345 -0.01808 0.05670  286 LEU   A CA  
2200 C  C   . LEU   A 286 ? 0.33408 0.27712 0.40443 -0.04278 -0.01346 0.06778  286 LEU   A C   
2201 O  O   . LEU   A 286 ? 0.29205 0.25734 0.36349 -0.04362 -0.01357 0.07204  286 LEU   A O   
2202 C  CB  . LEU   A 286 ? 0.37033 0.28931 0.42895 -0.05082 -0.02231 0.04010  286 LEU   A CB  
2203 C  CG  . LEU   A 286 ? 0.39305 0.30134 0.44749 -0.06174 -0.02945 0.02555  286 LEU   A CG  
2204 C  CD1 . LEU   A 286 ? 0.42232 0.35540 0.47805 -0.06684 -0.03616 0.02585  286 LEU   A CD1 
2205 C  CD2 . LEU   A 286 ? 0.38385 0.27817 0.42094 -0.05635 -0.02893 0.01130  286 LEU   A CD2 
2206 N  N   . LEU   A 287 ? 0.33822 0.27378 0.40365 -0.03261 -0.00948 0.07170  287 LEU   A N   
2207 C  CA  . LEU   A 287 ? 0.29315 0.24770 0.35164 -0.02316 -0.00674 0.08042  287 LEU   A CA  
2208 C  C   . LEU   A 287 ? 0.26222 0.22909 0.30760 -0.01881 -0.00985 0.06892  287 LEU   A C   
2209 O  O   . LEU   A 287 ? 0.26478 0.22157 0.30355 -0.01507 -0.01115 0.05869  287 LEU   A O   
2210 C  CB  . LEU   A 287 ? 0.28555 0.22999 0.34544 -0.01418 -0.00308 0.08967  287 LEU   A CB  
2211 C  CG  . LEU   A 287 ? 0.31853 0.24796 0.39283 -0.01868 0.00028  0.10253  287 LEU   A CG  
2212 C  CD1 . LEU   A 287 ? 0.36778 0.28527 0.44480 -0.00888 0.00346  0.10940  287 LEU   A CD1 
2213 C  CD2 . LEU   A 287 ? 0.32055 0.27001 0.39693 -0.02298 0.00257  0.11439  287 LEU   A CD2 
2214 N  N   . GLU   A 288 ? 0.22236 0.21037 0.26452 -0.01914 -0.01000 0.07082  288 GLU   A N   
2215 C  CA  . GLU   A 288 ? 0.23422 0.23295 0.26660 -0.01668 -0.01295 0.06066  288 GLU   A CA  
2216 C  C   . GLU   A 288 ? 0.20113 0.20884 0.22317 -0.00748 -0.01132 0.06207  288 GLU   A C   
2217 O  O   . GLU   A 288 ? 0.17973 0.19750 0.20044 -0.00458 -0.00827 0.07208  288 GLU   A O   
2218 C  CB  . GLU   A 288 ? 0.25239 0.26759 0.28953 -0.02147 -0.01334 0.06151  288 GLU   A CB  
2219 C  CG  . GLU   A 288 ? 0.24809 0.27582 0.27629 -0.01700 -0.01437 0.05508  288 GLU   A CG  
2220 C  CD  . GLU   A 288 ? 0.29474 0.31674 0.32060 -0.01999 -0.02048 0.04411  288 GLU   A CD  
2221 O  OE1 . GLU   A 288 ? 0.32229 0.33913 0.35610 -0.02777 -0.02434 0.04248  288 GLU   A OE1 
2222 O  OE2 . GLU   A 288 ? 0.24171 0.26355 0.25723 -0.01534 -0.02176 0.03754  288 GLU   A OE2 
2223 N  N   . ASP   A 289 ? 0.20041 0.20550 0.21462 -0.00360 -0.01353 0.05243  289 ASP   A N   
2224 C  CA  . ASP   A 289 ? 0.21173 0.22568 0.21885 0.00397  -0.01271 0.05420  289 ASP   A CA  
2225 C  C   . ASP   A 289 ? 0.20366 0.22900 0.20226 0.00497  -0.01457 0.04611  289 ASP   A C   
2226 O  O   . ASP   A 289 ? 0.16531 0.19599 0.15875 0.00989  -0.01490 0.04486  289 ASP   A O   
2227 C  CB  . ASP   A 289 ? 0.18363 0.18511 0.19271 0.00957  -0.01183 0.05363  289 ASP   A CB  
2228 C  CG  . ASP   A 289 ? 0.22913 0.22243 0.23339 0.00988  -0.01280 0.04063  289 ASP   A CG  
2229 O  OD1 . ASP   A 289 ? 0.20991 0.20240 0.21011 0.00417  -0.01534 0.03267  289 ASP   A OD1 
2230 O  OD2 . ASP   A 289 ? 0.18942 0.17815 0.19459 0.01630  -0.01070 0.03954  289 ASP   A OD2 
2231 N  N   . GLU   A 290 ? 0.17298 0.20269 0.17196 0.00041  -0.01588 0.04159  290 GLU   A N   
2232 C  CA  . GLU   A 290 ? 0.16736 0.20484 0.16010 0.00150  -0.01735 0.03462  290 GLU   A CA  
2233 C  C   . GLU   A 290 ? 0.18487 0.23605 0.17693 0.00162  -0.01485 0.03683  290 GLU   A C   
2234 O  O   . GLU   A 290 ? 0.21611 0.27178 0.20695 0.00150  -0.01547 0.03153  290 GLU   A O   
2235 C  CB  . GLU   A 290 ? 0.24101 0.27183 0.23406 -0.00239 -0.02109 0.02726  290 GLU   A CB  
2236 C  CG  . GLU   A 290 ? 0.22513 0.24298 0.21314 -0.00114 -0.02187 0.02174  290 GLU   A CG  
2237 C  CD  . GLU   A 290 ? 0.25349 0.26876 0.23421 -0.00298 -0.02487 0.01362  290 GLU   A CD  
2238 O  OE1 . GLU   A 290 ? 0.23224 0.25462 0.21344 -0.00558 -0.02781 0.01300  290 GLU   A OE1 
2239 O  OE2 . GLU   A 290 ? 0.24535 0.25118 0.22023 -0.00159 -0.02374 0.00846  290 GLU   A OE2 
2240 N  N   . PHE   A 291 ? 0.18631 0.24375 0.17836 0.00224  -0.01128 0.04473  291 PHE   A N   
2241 C  CA  . PHE   A 291 ? 0.17150 0.24179 0.15789 0.00336  -0.00743 0.04530  291 PHE   A CA  
2242 C  C   . PHE   A 291 ? 0.15203 0.22522 0.13060 0.00592  -0.00659 0.04651  291 PHE   A C   
2243 O  O   . PHE   A 291 ? 0.13338 0.20466 0.11360 0.00649  -0.00636 0.05459  291 PHE   A O   
2244 C  CB  . PHE   A 291 ? 0.16612 0.24332 0.15903 0.00069  -0.00210 0.05155  291 PHE   A CB  
2245 C  CG  . PHE   A 291 ? 0.19469 0.26967 0.20160 -0.00326 -0.00302 0.05070  291 PHE   A CG  
2246 C  CD1 . PHE   A 291 ? 0.18626 0.25265 0.20267 -0.00771 -0.00549 0.05515  291 PHE   A CD1 
2247 C  CD2 . PHE   A 291 ? 0.23650 0.31812 0.24822 -0.00279 -0.00179 0.04565  291 PHE   A CD2 
2248 C  CE1 . PHE   A 291 ? 0.24044 0.30714 0.27008 -0.01292 -0.00785 0.05440  291 PHE   A CE1 
2249 C  CE2 . PHE   A 291 ? 0.21913 0.30209 0.24597 -0.00657 -0.00403 0.04646  291 PHE   A CE2 
2250 C  CZ  . PHE   A 291 ? 0.21620 0.29273 0.25132 -0.01221 -0.00766 0.05067  291 PHE   A CZ  
2251 N  N   . THR   A 292 ? 0.15288 0.22940 0.12539 0.00664  -0.00606 0.03829  292 THR   A N   
2252 C  CA  . THR   A 292 ? 0.19188 0.27106 0.15879 0.00734  -0.00660 0.03803  292 THR   A CA  
2253 C  C   . THR   A 292 ? 0.18366 0.27123 0.14452 0.00631  -0.00272 0.04188  292 THR   A C   
2254 O  O   . THR   A 292 ? 0.18471 0.27659 0.14577 0.00548  0.00182  0.04272  292 THR   A O   
2255 C  CB  . THR   A 292 ? 0.18729 0.26511 0.15084 0.00700  -0.00835 0.02844  292 THR   A CB  
2256 O  OG1 . THR   A 292 ? 0.22397 0.30522 0.18299 0.00594  -0.00535 0.02274  292 THR   A OG1 
2257 C  CG2 . THR   A 292 ? 0.19609 0.26585 0.16478 0.00768  -0.01093 0.02437  292 THR   A CG2 
2258 N  N   . PRO   A 293 ? 0.22294 0.31400 0.17810 0.00632  -0.00408 0.04475  293 PRO   A N   
2259 C  CA  . PRO   A 293 ? 0.20197 0.30045 0.14755 0.00486  -0.00046 0.04671  293 PRO   A CA  
2260 C  C   . PRO   A 293 ? 0.22779 0.32782 0.16612 0.00376  0.00322  0.03663  293 PRO   A C   
2261 O  O   . PRO   A 293 ? 0.24059 0.34492 0.17451 0.00323  0.00950  0.03745  293 PRO   A O   
2262 C  CB  . PRO   A 293 ? 0.20839 0.31020 0.14816 0.00475  -0.00479 0.04985  293 PRO   A CB  
2263 C  CG  . PRO   A 293 ? 0.21465 0.31166 0.16518 0.00724  -0.00863 0.05519  293 PRO   A CG  
2264 C  CD  . PRO   A 293 ? 0.20930 0.29883 0.16662 0.00782  -0.00868 0.04796  293 PRO   A CD  
2265 N  N   . PHE   A 294 ? 0.22870 0.32443 0.16675 0.00357  0.00040  0.02739  294 PHE   A N   
2266 C  CA  . PHE   A 294 ? 0.23592 0.33055 0.16866 0.00299  0.00420  0.01758  294 PHE   A CA  
2267 C  C   . PHE   A 294 ? 0.24102 0.33730 0.18083 0.00479  0.00986  0.01814  294 PHE   A C   
2268 O  O   . PHE   A 294 ? 0.24518 0.34447 0.18069 0.00524  0.01724  0.01470  294 PHE   A O   
2269 C  CB  . PHE   A 294 ? 0.27258 0.36112 0.20699 0.00222  -0.00026 0.00981  294 PHE   A CB  
2270 C  CG  . PHE   A 294 ? 0.36659 0.45221 0.29346 0.00104  0.00307  -0.00072 294 PHE   A CG  
2271 C  CD1 . PHE   A 294 ? 0.38042 0.46486 0.31088 0.00316  0.00868  -0.00498 294 PHE   A CD1 
2272 C  CD2 . PHE   A 294 ? 0.41220 0.49643 0.32876 -0.00202 0.00087  -0.00640 294 PHE   A CD2 
2273 C  CE1 . PHE   A 294 ? 0.39545 0.47531 0.32000 0.00292  0.01321  -0.01543 294 PHE   A CE1 
2274 C  CE2 . PHE   A 294 ? 0.43276 0.51181 0.34186 -0.00332 0.00447  -0.01706 294 PHE   A CE2 
2275 C  CZ  . PHE   A 294 ? 0.46621 0.54202 0.37953 -0.00055 0.01122  -0.02185 294 PHE   A CZ  
2276 N  N   . ASP   A 295 ? 0.20117 0.29563 0.15218 0.00583  0.00707  0.02235  295 ASP   A N   
2277 C  CA  . ASP   A 295 ? 0.20421 0.30266 0.16398 0.00697  0.01134  0.02489  295 ASP   A CA  
2278 C  C   . ASP   A 295 ? 0.23702 0.34309 0.19944 0.00643  0.01857  0.03234  295 ASP   A C   
2279 O  O   . ASP   A 295 ? 0.21785 0.32979 0.18719 0.00760  0.02604  0.03137  295 ASP   A O   
2280 C  CB  . ASP   A 295 ? 0.18345 0.27766 0.15203 0.00656  0.00554  0.02970  295 ASP   A CB  
2281 C  CG  . ASP   A 295 ? 0.21466 0.30051 0.18283 0.00703  -0.00035 0.02215  295 ASP   A CG  
2282 O  OD1 . ASP   A 295 ? 0.22630 0.31143 0.18960 0.00750  0.00086  0.01423  295 ASP   A OD1 
2283 O  OD2 . ASP   A 295 ? 0.21727 0.29591 0.19019 0.00652  -0.00519 0.02382  295 ASP   A OD2 
2284 N  N   . VAL   A 296 ? 0.18782 0.29394 0.14787 0.00492  0.01709  0.04039  296 VAL   A N   
2285 C  CA  . VAL   A 296 ? 0.22296 0.33531 0.18638 0.00365  0.02382  0.04874  296 VAL   A CA  
2286 C  C   . VAL   A 296 ? 0.23211 0.34868 0.18470 0.00423  0.03152  0.04279  296 VAL   A C   
2287 O  O   . VAL   A 296 ? 0.24879 0.37106 0.20769 0.00454  0.04024  0.04398  296 VAL   A O   
2288 C  CB  . VAL   A 296 ? 0.20210 0.31219 0.16517 0.00215  0.02040  0.05929  296 VAL   A CB  
2289 C  CG1 . VAL   A 296 ? 0.23483 0.35096 0.19952 0.00035  0.02770  0.06765  296 VAL   A CG1 
2290 C  CG2 . VAL   A 296 ? 0.18462 0.28765 0.15953 0.00129  0.01497  0.06495  296 VAL   A CG2 
2291 N  N   . VAL   A 297 ? 0.26286 0.37623 0.20006 0.00396  0.02874  0.03610  297 VAL   A N   
2292 C  CA  . VAL   A 297 ? 0.29110 0.40572 0.21442 0.00362  0.03604  0.02909  297 VAL   A CA  
2293 C  C   . VAL   A 297 ? 0.29531 0.40869 0.22378 0.00613  0.04336  0.01928  297 VAL   A C   
2294 O  O   . VAL   A 297 ? 0.33712 0.45341 0.26436 0.00712  0.05412  0.01688  297 VAL   A O   
2295 C  CB  . VAL   A 297 ? 0.27283 0.38367 0.17980 0.00174  0.02997  0.02382  297 VAL   A CB  
2296 C  CG1 . VAL   A 297 ? 0.32365 0.43320 0.21404 0.00092  0.03767  0.01469  297 VAL   A CG1 
2297 C  CG2 . VAL   A 297 ? 0.32109 0.43531 0.22482 0.00027  0.02428  0.03467  297 VAL   A CG2 
2298 N  N   . ARG   A 298 ? 0.28170 0.39060 0.21704 0.00760  0.03846  0.01368  298 ARG   A N   
2299 C  CA  . ARG   A 298 ? 0.32869 0.43642 0.27210 0.01103  0.04527  0.00539  298 ARG   A CA  
2300 C  C   . ARG   A 298 ? 0.33265 0.44918 0.29495 0.01348  0.05318  0.01194  298 ARG   A C   
2301 O  O   . ARG   A 298 ? 0.38983 0.50783 0.35727 0.01644  0.06369  0.00688  298 ARG   A O   
2302 C  CB  . ARG   A 298 ? 0.33637 0.43907 0.28573 0.01214  0.03797  0.00093  298 ARG   A CB  
2303 C  CG  . ARG   A 298 ? 0.37462 0.48075 0.34317 0.01711  0.04362  -0.00074 298 ARG   A CG  
2304 C  CD  . ARG   A 298 ? 0.41009 0.50655 0.38422 0.01827  0.03686  -0.00643 298 ARG   A CD  
2305 N  NE  . ARG   A 298 ? 0.38816 0.48151 0.37039 0.01610  0.02596  0.00080  298 ARG   A NE  
2306 C  CZ  . ARG   A 298 ? 0.29306 0.38185 0.29055 0.01742  0.02145  0.00253  298 ARG   A CZ  
2307 N  NH1 . ARG   A 298 ? 0.31104 0.39842 0.32131 0.02171  0.02627  -0.00032 298 ARG   A NH1 
2308 N  NH2 . ARG   A 298 ? 0.28524 0.37067 0.28475 0.01463  0.01210  0.00734  298 ARG   A NH2 
2309 N  N   . GLN   A 299 ? 0.30258 0.42440 0.27741 0.01192  0.04853  0.02328  299 GLN   A N   
2310 C  CA  . GLN   A 299 ? 0.28799 0.41834 0.28569 0.01287  0.05371  0.03008  299 GLN   A CA  
2311 C  C   . GLN   A 299 ? 0.33809 0.47425 0.33564 0.01120  0.06219  0.03564  299 GLN   A C   
2312 O  O   . GLN   A 299 ? 0.33006 0.47286 0.34340 0.01303  0.07045  0.03629  299 GLN   A O   
2313 C  CB  . GLN   A 299 ? 0.26975 0.40189 0.28195 0.00990  0.04500  0.03932  299 GLN   A CB  
2314 C  CG  . GLN   A 299 ? 0.23146 0.37109 0.27095 0.00985  0.04631  0.04437  299 GLN   A CG  
2315 C  CD  . GLN   A 299 ? 0.20629 0.33867 0.25626 0.00552  0.03345  0.04803  299 GLN   A CD  
2316 O  OE1 . GLN   A 299 ? 0.20156 0.33974 0.27159 0.00209  0.03130  0.05462  299 GLN   A OE1 
2317 N  NE2 . GLN   A 299 ? 0.18406 0.30415 0.21970 0.00495  0.02490  0.04355  299 GLN   A NE2 
2318 N  N   . CYS   A 300 ? 0.31115 0.44556 0.29302 0.00789  0.06011  0.04045  300 CYS   A N   
2319 C  CA  . CYS   A 300 ? 0.33951 0.47978 0.32014 0.00589  0.06825  0.04690  300 CYS   A CA  
2320 C  C   . CYS   A 300 ? 0.41003 0.54965 0.37330 0.00719  0.07840  0.03780  300 CYS   A C   
2321 O  O   . CYS   A 300 ? 0.45732 0.60271 0.41893 0.00574  0.08748  0.04200  300 CYS   A O   
2322 C  CB  . CYS   A 300 ? 0.32688 0.46565 0.30125 0.00200  0.06183  0.05812  300 CYS   A CB  
2323 S  SG  . CYS   A 300 ? 0.31445 0.45047 0.30908 -0.00082 0.05178  0.06848  300 CYS   A SG  
2324 N  N   . SER   A 301 ? 0.43943 0.57148 0.39041 0.00935  0.07786  0.02519  301 SER   A N   
2325 C  CA  . SER   A 301 ? 0.49412 0.62212 0.42815 0.01019  0.08809  0.01443  301 SER   A CA  
2326 C  C   . SER   A 301 ? 0.50502 0.62972 0.45031 0.01507  0.09626  0.00310  301 SER   A C   
2327 O  O   . SER   A 301 ? 0.49607 0.62185 0.44145 0.01683  0.11012  -0.00247 301 SER   A O   
2328 C  CB  . SER   A 301 ? 0.52714 0.64660 0.43502 0.00763  0.08053  0.00913  301 SER   A CB  
2329 O  OG  . SER   A 301 ? 0.62144 0.73314 0.51286 0.00877  0.08897  -0.00367 301 SER   A OG  
2330 N  N   . GLY   A 302 ? 0.49987 0.62025 0.45522 0.01756  0.08879  -0.00056 302 GLY   A N   
2331 C  CA  . GLY   A 302 ? 0.53299 0.65273 0.50792 0.02326  0.09541  -0.00731 302 GLY   A CA  
2332 C  C   . GLY   A 302 ? 0.55673 0.66267 0.52291 0.02617  0.09698  -0.02119 302 GLY   A C   
2333 O  O   . GLY   A 302 ? 0.57879 0.68027 0.55087 0.03047  0.10922  -0.02993 302 GLY   A O   
2334 N  N   . VAL   A 303 ? 0.58579 0.68455 0.54027 0.02379  0.08497  -0.02336 303 VAL   A N   
2335 C  CA  . VAL   A 303 ? 0.62877 0.71322 0.57313 0.02519  0.08454  -0.03595 303 VAL   A CA  
2336 C  C   . VAL   A 303 ? 0.60311 0.68602 0.57128 0.03113  0.08459  -0.03801 303 VAL   A C   
2337 O  O   . VAL   A 303 ? 0.57730 0.66970 0.56321 0.03217  0.07765  -0.02890 303 VAL   A O   
2338 C  CB  . VAL   A 303 ? 0.59628 0.67585 0.52124 0.01871  0.07084  -0.03693 303 VAL   A CB  
2339 C  CG1 . VAL   A 303 ? 0.65573 0.72150 0.57396 0.01862  0.06824  -0.04920 303 VAL   A CG1 
2340 C  CG2 . VAL   A 303 ? 0.60826 0.68985 0.51187 0.01416  0.07062  -0.03424 303 VAL   A CG2 
2341 N  N   . THR   A 304 ? 0.60100 0.67127 0.56923 0.03643  0.09166  -0.04856 304 THR   A N   
2342 C  CA  . THR   A 304 ? 0.56335 0.63015 0.55477 0.04359  0.09152  -0.05038 304 THR   A CA  
2343 C  C   . THR   A 304 ? 0.63603 0.68685 0.61668 0.03988  0.08407  -0.06067 304 THR   A C   
2344 O  O   . THR   A 304 ? 0.66716 0.71263 0.62370 0.03240  0.07819  -0.06540 304 THR   A O   
2345 C  CB  . THR   A 304 ? 0.49826 0.56893 0.50576 0.05313  0.10154  -0.05450 304 THR   A CB  
2346 O  OG1 . THR   A 304 ? 0.59597 0.65732 0.58017 0.05367  0.10862  -0.06531 304 THR   A OG1 
2347 C  CG2 . THR   A 304 ? 0.38283 0.47539 0.41106 0.05353  0.10566  -0.04596 304 THR   A CG2 
2348 N  N   . PHE   A 305 ? 0.62890 0.67116 0.63018 0.04458  0.08396  -0.06243 305 PHE   A N   
2349 C  CA  . PHE   A 305 ? 0.68525 0.71060 0.68133 0.04064  0.07797  -0.07053 305 PHE   A CA  
2350 C  C   . PHE   A 305 ? 0.66970 0.67954 0.68491 0.04814  0.08417  -0.07379 305 PHE   A C   
2351 O  O   . PHE   A 305 ? 0.66791 0.68318 0.70866 0.05619  0.08726  -0.06446 305 PHE   A O   
2352 C  CB  . PHE   A 305 ? 0.62565 0.65422 0.62537 0.03577  0.06237  -0.05928 305 PHE   A CB  
2353 C  CG  . PHE   A 305 ? 0.60695 0.65125 0.59457 0.03069  0.05553  -0.05147 305 PHE   A CG  
2354 C  CD1 . PHE   A 305 ? 0.58589 0.63192 0.54951 0.02325  0.05094  -0.05685 305 PHE   A CD1 
2355 C  CD2 . PHE   A 305 ? 0.57036 0.62786 0.57194 0.03323  0.05384  -0.03846 305 PHE   A CD2 
2356 C  CE1 . PHE   A 305 ? 0.60313 0.66255 0.55778 0.01976  0.04528  -0.04834 305 PHE   A CE1 
2357 C  CE2 . PHE   A 305 ? 0.55855 0.62762 0.55033 0.02867  0.04858  -0.03133 305 PHE   A CE2 
2358 C  CZ  . PHE   A 305 ? 0.58523 0.65473 0.55388 0.02264  0.04473  -0.03581 305 PHE   A CZ  
2359 N  N   . GLN   A 306 ? 0.67790 0.66924 0.68174 0.04496  0.08459  -0.08549 306 GLN   A N   
2360 C  CA  . GLN   A 306 ? 0.68006 0.65439 0.70114 0.05142  0.09023  -0.08861 306 GLN   A CA  
2361 C  C   . GLN   A 306 ? 0.63571 0.59022 0.65331 0.04522  0.08449  -0.09484 306 GLN   A C   
2362 O  O   . GLN   A 306 ? 0.58402 0.53635 0.61374 0.04416  0.07758  -0.08724 306 GLN   A O   
2363 C  CB  . GLN   A 306 ? 0.68772 0.65831 0.70122 0.05555  0.10120  -0.09824 306 GLN   A CB  
2364 C  CG  . GLN   A 306 ? 0.67298 0.65927 0.70505 0.06518  0.10901  -0.08987 306 GLN   A CG  
2365 C  CD  . GLN   A 306 ? 0.67728 0.65425 0.73675 0.07482  0.11489  -0.08709 306 GLN   A CD  
2366 O  OE1 . GLN   A 306 ? 0.66007 0.64749 0.74542 0.08068  0.11278  -0.07320 306 GLN   A OE1 
2367 N  NE2 . GLN   A 306 ? 0.68192 0.63977 0.73595 0.07621  0.12167  -0.09958 306 GLN   A NE2 
2368 N  N1  . A1ARW B .   ? 0.45051 0.46589 0.29417 -0.01862 -0.02582 0.01601  401 A1ARW A N1  
2369 C  C4  . A1ARW B .   ? 0.40726 0.42685 0.26932 -0.01907 -0.02483 0.03381  401 A1ARW A C4  
2370 C  C5  . A1ARW B .   ? 0.41787 0.42994 0.24233 -0.01645 -0.00798 0.00885  401 A1ARW A C5  
2371 C  C6  . A1ARW B .   ? 0.48178 0.49310 0.28857 -0.01620 0.00070  0.00582  401 A1ARW A C6  
2372 C  C7  . A1ARW B .   ? 0.47781 0.48930 0.26479 -0.01893 -0.00165 0.00640  401 A1ARW A C7  
2373 C  C8  . A1ARW B .   ? 0.50827 0.52142 0.29440 -0.02223 -0.01317 0.01051  401 A1ARW A C8  
2374 C  C10 . A1ARW B .   ? 0.45491 0.46641 0.26407 -0.01301 0.01281  0.00225  401 A1ARW A C10 
2375 C  C13 . A1ARW B .   ? 0.44483 0.46114 0.26612 -0.00705 0.03619  -0.00236 401 A1ARW A C13 
2376 C  C15 . A1ARW B .   ? 0.50521 0.51513 0.30022 -0.01047 0.02253  -0.00536 401 A1ARW A C15 
2377 C  C17 . A1ARW B .   ? 0.40764 0.41915 0.25058 -0.02253 -0.03879 -0.00335 401 A1ARW A C17 
2378 C  C20 . A1ARW B .   ? 0.41703 0.43615 0.27309 -0.01911 -0.01536 0.03197  401 A1ARW A C20 
2379 C  C1  . A1ARW B .   ? 0.37829 0.39218 0.22575 -0.01861 -0.03047 0.00856  401 A1ARW A C1  
2380 C  C11 . A1ARW B .   ? 0.42158 0.43628 0.24907 -0.01256 0.01493  0.00653  401 A1ARW A C11 
2381 C  C12 . A1ARW B .   ? 0.41409 0.43156 0.24695 -0.01034 0.02567  0.00411  401 A1ARW A C12 
2382 C  C14 . A1ARW B .   ? 0.49783 0.50994 0.29939 -0.00673 0.03469  -0.00752 401 A1ARW A C14 
2383 C  C16 . A1ARW B .   ? 0.42554 0.43865 0.26077 -0.02179 -0.03512 0.00307  401 A1ARW A C16 
2384 C  C18 . A1ARW B .   ? 0.36306 0.37420 0.22373 -0.01951 -0.03743 -0.00364 401 A1ARW A C18 
2385 C  C19 . A1ARW B .   ? 0.37051 0.38361 0.23489 -0.01588 -0.02984 0.00635  401 A1ARW A C19 
2386 C  C2  . A1ARW B .   ? 0.45132 0.46503 0.27617 -0.01902 -0.01828 0.01293  401 A1ARW A C2  
2387 C  C3  . A1ARW B .   ? 0.42414 0.44221 0.28358 -0.01822 -0.02837 0.02467  401 A1ARW A C3  
2388 C  C9  . A1ARW B .   ? 0.48344 0.49802 0.28933 -0.02208 -0.02106 0.01394  401 A1ARW A C9  
2389 N  N2  . A1ARW B .   ? 0.30054 0.31253 0.17141 -0.01591 -0.03305 0.00094  401 A1ARW A N2  
2390 O  O1  . A1ARW B .   ? 0.45930 0.47857 0.33255 -0.01730 -0.03357 0.02522  401 A1ARW A O1  
2391 CL CL1 . A1ARW B .   ? 0.50706 0.53224 0.36363 -0.01171 0.02564  0.00942  401 A1ARW A CL1 
2392 CL CL2 . A1ARW B .   ? 0.49554 0.50527 0.32559 -0.02842 -0.04547 -0.01132 401 A1ARW A CL2 
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