data_8QNE
# 
_entry.id   8QNE 
# 
_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   8QNE         pdb_00008qne 10.2210/pdb8qne/pdb 
WWPDB D_1292133578 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_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                        8QNE 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8QMX unspecified 
PDB . 8QN1 unspecified 
PDB . 8QN3 unspecified 
PDB . 8QN9 unspecified 
PDB . 8QNA unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              peter.macheroux@tugraz.at 
_pdbx_contact_author.name_first         Peter 
_pdbx_contact_author.name_last          Macheroux 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0242-454X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bijelic, A.'      1 ? 
'Macheroux, P.'    2 ? 
'Kerschbaumer, B.' 3 ? 
# 
_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                     'Crystal structures of OPR3 wildtype and variants in complex with NAD(P)H' 
_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 'Kerschbaumer, B.' 1 ? 
primary 'Bijelic, A.'      2 ? 
primary 'Macheroux, P.'    3 ? 
# 
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 '12-oxophytodienoate reductase 3' 43768.520 1   1.3.1.42 ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'           456.344   1   ?        ? ? ? 
3 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'   118.174   3   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                     96.063    1   ?        ? ? ? 
5 non-polymer nat 'PENTAETHYLENE GLYCOL'            238.278   1   ?        ? ? ? 
6 water       nat water                             18.015    361 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '12-oxophytodienoate-10,11-reductase 3,OPDA-reductase 3,LeOPR3' 
# 
_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       
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRSDKGGSEEEEARLMRTLRNAYQGTFICS
GGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRSDKGGSEEEEARLMRTLRNAYQGTFICS
GGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_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 'FLAVIN MONONUCLEOTIDE'         FMN 
3 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD 
4 'SULFATE ION'                   SO4 
5 'PENTAETHYLENE GLYCOL'          1PE 
6 water                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  MET n 
1 11  ALA n 
1 12  SER n 
1 13  SER n 
1 14  ALA n 
1 15  GLN n 
1 16  ASP n 
1 17  GLY n 
1 18  ASN n 
1 19  ASN n 
1 20  PRO n 
1 21  LEU n 
1 22  PHE n 
1 23  SER n 
1 24  PRO n 
1 25  TYR n 
1 26  LYS n 
1 27  MET n 
1 28  GLY n 
1 29  LYS n 
1 30  PHE n 
1 31  ASN n 
1 32  LEU n 
1 33  SER n 
1 34  HIS n 
1 35  ARG n 
1 36  VAL n 
1 37  VAL n 
1 38  LEU n 
1 39  ALA n 
1 40  PRO n 
1 41  MET n 
1 42  THR n 
1 43  ARG n 
1 44  CYS n 
1 45  ARG n 
1 46  ALA n 
1 47  LEU n 
1 48  ASN n 
1 49  ASN n 
1 50  ILE n 
1 51  PRO n 
1 52  GLN n 
1 53  ALA n 
1 54  ALA n 
1 55  LEU n 
1 56  GLY n 
1 57  GLU n 
1 58  TYR n 
1 59  TYR n 
1 60  GLU n 
1 61  GLN n 
1 62  ARG n 
1 63  ALA n 
1 64  THR n 
1 65  ALA n 
1 66  GLY n 
1 67  GLY n 
1 68  PHE n 
1 69  LEU n 
1 70  ILE n 
1 71  THR n 
1 72  GLU n 
1 73  GLY n 
1 74  THR n 
1 75  MET n 
1 76  ILE n 
1 77  SER n 
1 78  PRO n 
1 79  THR n 
1 80  SER n 
1 81  ALA n 
1 82  GLY n 
1 83  PHE n 
1 84  PRO n 
1 85  HIS n 
1 86  VAL n 
1 87  PRO n 
1 88  GLY n 
1 89  ILE n 
1 90  PHE n 
1 91  THR n 
1 92  LYS n 
1 93  GLU n 
1 94  GLN n 
1 95  VAL n 
1 96  ARG n 
1 97  GLU n 
1 98  TRP n 
1 99  LYS n 
1 100 LYS n 
1 101 ILE n 
1 102 VAL n 
1 103 ASP n 
1 104 VAL n 
1 105 VAL n 
1 106 HIS n 
1 107 ALA n 
1 108 LYS n 
1 109 GLY n 
1 110 ALA n 
1 111 VAL n 
1 112 ILE n 
1 113 PHE n 
1 114 CYS n 
1 115 GLN n 
1 116 LEU n 
1 117 TRP n 
1 118 HIS n 
1 119 VAL n 
1 120 GLY n 
1 121 ARG n 
1 122 ALA n 
1 123 SER n 
1 124 HIS n 
1 125 GLU n 
1 126 VAL n 
1 127 TYR n 
1 128 GLN n 
1 129 PRO n 
1 130 ALA n 
1 131 GLY n 
1 132 ALA n 
1 133 ALA n 
1 134 PRO n 
1 135 ILE n 
1 136 SER n 
1 137 SER n 
1 138 THR n 
1 139 GLU n 
1 140 LYS n 
1 141 PRO n 
1 142 ILE n 
1 143 SER n 
1 144 ASN n 
1 145 ARG n 
1 146 TRP n 
1 147 ARG n 
1 148 ILE n 
1 149 LEU n 
1 150 MET n 
1 151 PRO n 
1 152 ASP n 
1 153 GLY n 
1 154 THR n 
1 155 HIS n 
1 156 GLY n 
1 157 ILE n 
1 158 TYR n 
1 159 PRO n 
1 160 LYS n 
1 161 PRO n 
1 162 ARG n 
1 163 ALA n 
1 164 ILE n 
1 165 GLY n 
1 166 THR n 
1 167 TYR n 
1 168 GLU n 
1 169 ILE n 
1 170 SER n 
1 171 GLN n 
1 172 VAL n 
1 173 VAL n 
1 174 GLU n 
1 175 ASP n 
1 176 TYR n 
1 177 ARG n 
1 178 ARG n 
1 179 SER n 
1 180 ALA n 
1 181 LEU n 
1 182 ASN n 
1 183 ALA n 
1 184 ILE n 
1 185 GLU n 
1 186 ALA n 
1 187 GLY n 
1 188 PHE n 
1 189 ASP n 
1 190 GLY n 
1 191 ILE n 
1 192 GLU n 
1 193 ILE n 
1 194 HIS n 
1 195 GLY n 
1 196 ALA n 
1 197 HIS n 
1 198 GLY n 
1 199 TYR n 
1 200 LEU n 
1 201 ILE n 
1 202 ASP n 
1 203 GLN n 
1 204 PHE n 
1 205 LEU n 
1 206 LYS n 
1 207 ASP n 
1 208 GLY n 
1 209 ILE n 
1 210 ASN n 
1 211 ASP n 
1 212 ARG n 
1 213 THR n 
1 214 ASP n 
1 215 GLU n 
1 216 TYR n 
1 217 GLY n 
1 218 GLY n 
1 219 SER n 
1 220 LEU n 
1 221 ALA n 
1 222 ASN n 
1 223 ARG n 
1 224 CYS n 
1 225 LYS n 
1 226 PHE n 
1 227 ILE n 
1 228 THR n 
1 229 GLN n 
1 230 VAL n 
1 231 VAL n 
1 232 GLN n 
1 233 ALA n 
1 234 VAL n 
1 235 VAL n 
1 236 SER n 
1 237 ALA n 
1 238 ILE n 
1 239 GLY n 
1 240 ALA n 
1 241 ASP n 
1 242 ARG n 
1 243 VAL n 
1 244 GLY n 
1 245 VAL n 
1 246 ARG n 
1 247 VAL n 
1 248 SER n 
1 249 PRO n 
1 250 ALA n 
1 251 ILE n 
1 252 ASP n 
1 253 HIS n 
1 254 LEU n 
1 255 ASP n 
1 256 ALA n 
1 257 MET n 
1 258 ASP n 
1 259 SER n 
1 260 ASN n 
1 261 PRO n 
1 262 LEU n 
1 263 SER n 
1 264 LEU n 
1 265 GLY n 
1 266 LEU n 
1 267 ALA n 
1 268 VAL n 
1 269 VAL n 
1 270 GLU n 
1 271 ARG n 
1 272 LEU n 
1 273 ASN n 
1 274 LYS n 
1 275 ILE n 
1 276 GLN n 
1 277 LEU n 
1 278 HIS n 
1 279 SER n 
1 280 GLY n 
1 281 SER n 
1 282 LYS n 
1 283 LEU n 
1 284 ALA n 
1 285 TYR n 
1 286 LEU n 
1 287 HIS n 
1 288 VAL n 
1 289 THR n 
1 290 GLN n 
1 291 PRO n 
1 292 ARG n 
1 293 SER n 
1 294 ASP n 
1 295 LYS n 
1 296 GLY n 
1 297 GLY n 
1 298 SER n 
1 299 GLU n 
1 300 GLU n 
1 301 GLU n 
1 302 GLU n 
1 303 ALA n 
1 304 ARG n 
1 305 LEU n 
1 306 MET n 
1 307 ARG n 
1 308 THR n 
1 309 LEU n 
1 310 ARG n 
1 311 ASN n 
1 312 ALA n 
1 313 TYR n 
1 314 GLN n 
1 315 GLY n 
1 316 THR n 
1 317 PHE n 
1 318 ILE n 
1 319 CYS n 
1 320 SER n 
1 321 GLY n 
1 322 GLY n 
1 323 TYR n 
1 324 THR n 
1 325 ARG n 
1 326 GLU n 
1 327 LEU n 
1 328 GLY n 
1 329 ILE n 
1 330 GLU n 
1 331 ALA n 
1 332 VAL n 
1 333 ALA n 
1 334 GLN n 
1 335 GLY n 
1 336 ASP n 
1 337 ALA n 
1 338 ASP n 
1 339 LEU n 
1 340 VAL n 
1 341 SER n 
1 342 TYR n 
1 343 GLY n 
1 344 ARG n 
1 345 LEU n 
1 346 PHE n 
1 347 ILE n 
1 348 SER n 
1 349 ASN n 
1 350 PRO n 
1 351 ASP n 
1 352 LEU n 
1 353 VAL n 
1 354 MET n 
1 355 ARG n 
1 356 ILE n 
1 357 LYS n 
1 358 LEU n 
1 359 ASN n 
1 360 ALA n 
1 361 PRO n 
1 362 LEU n 
1 363 ASN n 
1 364 LYS n 
1 365 TYR n 
1 366 ASN n 
1 367 ARG n 
1 368 LYS n 
1 369 THR n 
1 370 PHE n 
1 371 TYR n 
1 372 THR n 
1 373 GLN n 
1 374 ASP n 
1 375 PRO n 
1 376 VAL n 
1 377 VAL n 
1 378 GLY n 
1 379 TYR n 
1 380 THR n 
1 381 ASP n 
1 382 TYR n 
1 383 PRO n 
1 384 PHE n 
1 385 LEU n 
1 386 GLN n 
1 387 GLY n 
1 388 ASN n 
1 389 GLY n 
1 390 SER n 
1 391 ASN n 
1 392 GLY n 
1 393 PRO n 
1 394 LEU n 
1 395 SER n 
1 396 ARG n 
1 397 LEU 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                   397 
_entity_src_gen.gene_src_common_name               tomato 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 OPR3 
_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      'Solanum lycopersicum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4081 
_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 
1PE non-polymer         . 'PENTAETHYLENE GLYCOL'          PEG400                     'C10 H22 O6'      238.278 
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 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE'         'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P' 456.344 
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 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL' ?                          'C6 H14 O2'       118.174 
PHE 'L-peptide linking' y PHENYLALANINE                   ?                          'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                         ?                          'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                          ?                          'C3 H7 N O3'      105.093 
SO4 non-polymer         . 'SULFATE ION'                   ?                          'O4 S -2'         96.063  
THR 'L-peptide linking' y THREONINE                       ?                          'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                      ?                          'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                        ?                          'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                          ?                          'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -8  ?   ?   ?   A . n 
A 1 2   ALA 2   -7  ?   ?   ?   A . n 
A 1 3   SER 3   -6  ?   ?   ?   A . n 
A 1 4   HIS 4   -5  ?   ?   ?   A . n 
A 1 5   HIS 5   -4  ?   ?   ?   A . n 
A 1 6   HIS 6   -3  ?   ?   ?   A . n 
A 1 7   HIS 7   -2  ?   ?   ?   A . n 
A 1 8   HIS 8   -1  ?   ?   ?   A . n 
A 1 9   HIS 9   0   ?   ?   ?   A . n 
A 1 10  MET 10  1   ?   ?   ?   A . n 
A 1 11  ALA 11  2   ?   ?   ?   A . n 
A 1 12  SER 12  3   ?   ?   ?   A . n 
A 1 13  SER 13  4   ?   ?   ?   A . n 
A 1 14  ALA 14  5   ?   ?   ?   A . n 
A 1 15  GLN 15  6   ?   ?   ?   A . n 
A 1 16  ASP 16  7   ?   ?   ?   A . n 
A 1 17  GLY 17  8   ?   ?   ?   A . n 
A 1 18  ASN 18  9   ?   ?   ?   A . n 
A 1 19  ASN 19  10  10  ASN ASN A . n 
A 1 20  PRO 20  11  11  PRO PRO A . n 
A 1 21  LEU 21  12  12  LEU LEU A . n 
A 1 22  PHE 22  13  13  PHE PHE A . n 
A 1 23  SER 23  14  14  SER SER A . n 
A 1 24  PRO 24  15  15  PRO PRO A . n 
A 1 25  TYR 25  16  16  TYR TYR A . n 
A 1 26  LYS 26  17  17  LYS LYS A . n 
A 1 27  MET 27  18  18  MET MET A . n 
A 1 28  GLY 28  19  19  GLY GLY A . n 
A 1 29  LYS 29  20  20  LYS LYS A . n 
A 1 30  PHE 30  21  21  PHE PHE A . n 
A 1 31  ASN 31  22  22  ASN ASN A . n 
A 1 32  LEU 32  23  23  LEU LEU A . n 
A 1 33  SER 33  24  24  SER SER A . n 
A 1 34  HIS 34  25  25  HIS HIS A . n 
A 1 35  ARG 35  26  26  ARG ARG A . n 
A 1 36  VAL 36  27  27  VAL VAL A . n 
A 1 37  VAL 37  28  28  VAL VAL A . n 
A 1 38  LEU 38  29  29  LEU LEU A . n 
A 1 39  ALA 39  30  30  ALA ALA A . n 
A 1 40  PRO 40  31  31  PRO PRO A . n 
A 1 41  MET 41  32  32  MET MET A . n 
A 1 42  THR 42  33  33  THR THR A . n 
A 1 43  ARG 43  34  34  ARG ARG A . n 
A 1 44  CYS 44  35  35  CYS CYS A . n 
A 1 45  ARG 45  36  36  ARG ARG A . n 
A 1 46  ALA 46  37  37  ALA ALA A . n 
A 1 47  LEU 47  38  38  LEU LEU A . n 
A 1 48  ASN 48  39  39  ASN ASN A . n 
A 1 49  ASN 49  40  40  ASN ASN A . n 
A 1 50  ILE 50  41  41  ILE ILE A . n 
A 1 51  PRO 51  42  42  PRO PRO A . n 
A 1 52  GLN 52  43  43  GLN GLN A . n 
A 1 53  ALA 53  44  44  ALA ALA A . n 
A 1 54  ALA 54  45  45  ALA ALA A . n 
A 1 55  LEU 55  46  46  LEU LEU A . n 
A 1 56  GLY 56  47  47  GLY GLY A . n 
A 1 57  GLU 57  48  48  GLU GLU A . n 
A 1 58  TYR 58  49  49  TYR TYR A . n 
A 1 59  TYR 59  50  50  TYR TYR A . n 
A 1 60  GLU 60  51  51  GLU GLU A . n 
A 1 61  GLN 61  52  52  GLN GLN A . n 
A 1 62  ARG 62  53  53  ARG ARG A . n 
A 1 63  ALA 63  54  54  ALA ALA A . n 
A 1 64  THR 64  55  55  THR THR A . n 
A 1 65  ALA 65  56  56  ALA ALA A . n 
A 1 66  GLY 66  57  57  GLY GLY A . n 
A 1 67  GLY 67  58  58  GLY GLY A . n 
A 1 68  PHE 68  59  59  PHE PHE A . n 
A 1 69  LEU 69  60  60  LEU LEU A . n 
A 1 70  ILE 70  61  61  ILE ILE A . n 
A 1 71  THR 71  62  62  THR THR A . n 
A 1 72  GLU 72  63  63  GLU GLU A . n 
A 1 73  GLY 73  64  64  GLY GLY A . n 
A 1 74  THR 74  65  65  THR THR A . n 
A 1 75  MET 75  66  66  MET MET A . n 
A 1 76  ILE 76  67  67  ILE ILE A . n 
A 1 77  SER 77  68  68  SER SER A . n 
A 1 78  PRO 78  69  69  PRO PRO A . n 
A 1 79  THR 79  70  70  THR THR A . n 
A 1 80  SER 80  71  71  SER SER A . n 
A 1 81  ALA 81  72  72  ALA ALA A . n 
A 1 82  GLY 82  73  73  GLY GLY A . n 
A 1 83  PHE 83  74  74  PHE PHE A . n 
A 1 84  PRO 84  75  75  PRO PRO A . n 
A 1 85  HIS 85  76  76  HIS HIS A . n 
A 1 86  VAL 86  77  77  VAL VAL A . n 
A 1 87  PRO 87  78  78  PRO PRO A . n 
A 1 88  GLY 88  79  79  GLY GLY A . n 
A 1 89  ILE 89  80  80  ILE ILE A . n 
A 1 90  PHE 90  81  81  PHE PHE A . n 
A 1 91  THR 91  82  82  THR THR A . n 
A 1 92  LYS 92  83  83  LYS LYS A . n 
A 1 93  GLU 93  84  84  GLU GLU A . n 
A 1 94  GLN 94  85  85  GLN GLN A . n 
A 1 95  VAL 95  86  86  VAL VAL A . n 
A 1 96  ARG 96  87  87  ARG ARG A . n 
A 1 97  GLU 97  88  88  GLU GLU A . n 
A 1 98  TRP 98  89  89  TRP TRP A . n 
A 1 99  LYS 99  90  90  LYS LYS A . n 
A 1 100 LYS 100 91  91  LYS LYS A . n 
A 1 101 ILE 101 92  92  ILE ILE A . n 
A 1 102 VAL 102 93  93  VAL VAL A . n 
A 1 103 ASP 103 94  94  ASP ASP A . n 
A 1 104 VAL 104 95  95  VAL VAL A . n 
A 1 105 VAL 105 96  96  VAL VAL A . n 
A 1 106 HIS 106 97  97  HIS HIS A . n 
A 1 107 ALA 107 98  98  ALA ALA A . n 
A 1 108 LYS 108 99  99  LYS LYS A . n 
A 1 109 GLY 109 100 100 GLY GLY A . n 
A 1 110 ALA 110 101 101 ALA ALA A . n 
A 1 111 VAL 111 102 102 VAL VAL A . n 
A 1 112 ILE 112 103 103 ILE ILE A . n 
A 1 113 PHE 113 104 104 PHE PHE A . n 
A 1 114 CYS 114 105 105 CYS CYS A . n 
A 1 115 GLN 115 106 106 GLN GLN A . n 
A 1 116 LEU 116 107 107 LEU LEU A . n 
A 1 117 TRP 117 108 108 TRP TRP A . n 
A 1 118 HIS 118 109 109 HIS HIS A . n 
A 1 119 VAL 119 110 110 VAL VAL A . n 
A 1 120 GLY 120 111 111 GLY GLY A . n 
A 1 121 ARG 121 112 112 ARG ARG A . n 
A 1 122 ALA 122 113 113 ALA ALA A . n 
A 1 123 SER 123 114 114 SER SER A . n 
A 1 124 HIS 124 115 115 HIS HIS A . n 
A 1 125 GLU 125 116 116 GLU GLU A . n 
A 1 126 VAL 126 117 117 VAL VAL A . n 
A 1 127 TYR 127 118 118 TYR TYR A . n 
A 1 128 GLN 128 119 119 GLN GLN A . n 
A 1 129 PRO 129 120 120 PRO PRO A . n 
A 1 130 ALA 130 121 121 ALA ALA A . n 
A 1 131 GLY 131 122 122 GLY GLY A . n 
A 1 132 ALA 132 123 123 ALA ALA A . n 
A 1 133 ALA 133 124 124 ALA ALA A . n 
A 1 134 PRO 134 125 125 PRO PRO A . n 
A 1 135 ILE 135 126 126 ILE ILE A . n 
A 1 136 SER 136 127 127 SER SER A . n 
A 1 137 SER 137 128 128 SER SER A . n 
A 1 138 THR 138 129 129 THR THR A . n 
A 1 139 GLU 139 130 130 GLU GLU A . n 
A 1 140 LYS 140 131 131 LYS LYS A . n 
A 1 141 PRO 141 132 132 PRO PRO A . n 
A 1 142 ILE 142 133 133 ILE ILE A . n 
A 1 143 SER 143 134 134 SER SER A . n 
A 1 144 ASN 144 135 135 ASN ASN A . n 
A 1 145 ARG 145 136 136 ARG ARG A . n 
A 1 146 TRP 146 137 137 TRP TRP A . n 
A 1 147 ARG 147 138 138 ARG ARG A . n 
A 1 148 ILE 148 139 139 ILE ILE A . n 
A 1 149 LEU 149 140 140 LEU LEU A . n 
A 1 150 MET 150 141 141 MET MET A . n 
A 1 151 PRO 151 142 142 PRO PRO A . n 
A 1 152 ASP 152 143 143 ASP ASP A . n 
A 1 153 GLY 153 144 144 GLY GLY A . n 
A 1 154 THR 154 145 145 THR THR A . n 
A 1 155 HIS 155 146 146 HIS HIS A . n 
A 1 156 GLY 156 147 147 GLY GLY A . n 
A 1 157 ILE 157 148 148 ILE ILE A . n 
A 1 158 TYR 158 149 149 TYR TYR A . n 
A 1 159 PRO 159 150 150 PRO PRO A . n 
A 1 160 LYS 160 151 151 LYS LYS A . n 
A 1 161 PRO 161 152 152 PRO PRO A . n 
A 1 162 ARG 162 153 153 ARG ARG A . n 
A 1 163 ALA 163 154 154 ALA ALA A . n 
A 1 164 ILE 164 155 155 ILE ILE A . n 
A 1 165 GLY 165 156 156 GLY GLY A . n 
A 1 166 THR 166 157 157 THR THR A . n 
A 1 167 TYR 167 158 158 TYR TYR A . n 
A 1 168 GLU 168 159 159 GLU GLU A . n 
A 1 169 ILE 169 160 160 ILE ILE A . n 
A 1 170 SER 170 161 161 SER SER A . n 
A 1 171 GLN 171 162 162 GLN GLN A . n 
A 1 172 VAL 172 163 163 VAL VAL A . n 
A 1 173 VAL 173 164 164 VAL VAL A . n 
A 1 174 GLU 174 165 165 GLU GLU A . n 
A 1 175 ASP 175 166 166 ASP ASP A . n 
A 1 176 TYR 176 167 167 TYR TYR A . n 
A 1 177 ARG 177 168 168 ARG ARG A . n 
A 1 178 ARG 178 169 169 ARG ARG A . n 
A 1 179 SER 179 170 170 SER SER A . n 
A 1 180 ALA 180 171 171 ALA ALA A . n 
A 1 181 LEU 181 172 172 LEU LEU A . n 
A 1 182 ASN 182 173 173 ASN ASN A . n 
A 1 183 ALA 183 174 174 ALA ALA A . n 
A 1 184 ILE 184 175 175 ILE ILE A . n 
A 1 185 GLU 185 176 176 GLU GLU A . n 
A 1 186 ALA 186 177 177 ALA ALA A . n 
A 1 187 GLY 187 178 178 GLY GLY A . n 
A 1 188 PHE 188 179 179 PHE PHE A . n 
A 1 189 ASP 189 180 180 ASP ASP A . n 
A 1 190 GLY 190 181 181 GLY GLY A . n 
A 1 191 ILE 191 182 182 ILE ILE A . n 
A 1 192 GLU 192 183 183 GLU GLU A . n 
A 1 193 ILE 193 184 184 ILE ILE A . n 
A 1 194 HIS 194 185 185 HIS HIS A . n 
A 1 195 GLY 195 186 186 GLY GLY A . n 
A 1 196 ALA 196 187 187 ALA ALA A . n 
A 1 197 HIS 197 188 188 HIS HIS A . n 
A 1 198 GLY 198 189 189 GLY GLY A . n 
A 1 199 TYR 199 190 190 TYR TYR A . n 
A 1 200 LEU 200 191 191 LEU LEU A . n 
A 1 201 ILE 201 192 192 ILE ILE A . n 
A 1 202 ASP 202 193 193 ASP ASP A . n 
A 1 203 GLN 203 194 194 GLN GLN A . n 
A 1 204 PHE 204 195 195 PHE PHE A . n 
A 1 205 LEU 205 196 196 LEU LEU A . n 
A 1 206 LYS 206 197 197 LYS LYS A . n 
A 1 207 ASP 207 198 198 ASP ASP A . n 
A 1 208 GLY 208 199 199 GLY GLY A . n 
A 1 209 ILE 209 200 200 ILE ILE A . n 
A 1 210 ASN 210 201 201 ASN ASN A . n 
A 1 211 ASP 211 202 202 ASP ASP A . n 
A 1 212 ARG 212 203 203 ARG ARG A . n 
A 1 213 THR 213 204 204 THR THR A . n 
A 1 214 ASP 214 205 205 ASP ASP A . n 
A 1 215 GLU 215 206 206 GLU GLU A . n 
A 1 216 TYR 216 207 207 TYR TYR A . n 
A 1 217 GLY 217 208 208 GLY GLY A . n 
A 1 218 GLY 218 209 209 GLY GLY A . n 
A 1 219 SER 219 210 210 SER SER A . n 
A 1 220 LEU 220 211 211 LEU LEU A . n 
A 1 221 ALA 221 212 212 ALA ALA A . n 
A 1 222 ASN 222 213 213 ASN ASN A . n 
A 1 223 ARG 223 214 214 ARG ARG A . n 
A 1 224 CYS 224 215 215 CYS CYS A . n 
A 1 225 LYS 225 216 216 LYS LYS A . n 
A 1 226 PHE 226 217 217 PHE PHE A . n 
A 1 227 ILE 227 218 218 ILE ILE A . n 
A 1 228 THR 228 219 219 THR THR A . n 
A 1 229 GLN 229 220 220 GLN GLN A . n 
A 1 230 VAL 230 221 221 VAL VAL A . n 
A 1 231 VAL 231 222 222 VAL VAL A . n 
A 1 232 GLN 232 223 223 GLN GLN A . n 
A 1 233 ALA 233 224 224 ALA ALA A . n 
A 1 234 VAL 234 225 225 VAL VAL A . n 
A 1 235 VAL 235 226 226 VAL VAL A . n 
A 1 236 SER 236 227 227 SER SER A . n 
A 1 237 ALA 237 228 228 ALA ALA A . n 
A 1 238 ILE 238 229 229 ILE ILE A . n 
A 1 239 GLY 239 230 230 GLY GLY A . n 
A 1 240 ALA 240 231 231 ALA ALA A . n 
A 1 241 ASP 241 232 232 ASP ASP A . n 
A 1 242 ARG 242 233 233 ARG ARG A . n 
A 1 243 VAL 243 234 234 VAL VAL A . n 
A 1 244 GLY 244 235 235 GLY GLY A . n 
A 1 245 VAL 245 236 236 VAL VAL A . n 
A 1 246 ARG 246 237 237 ARG ARG A . n 
A 1 247 VAL 247 238 238 VAL VAL A . n 
A 1 248 SER 248 239 239 SER SER A . n 
A 1 249 PRO 249 240 240 PRO PRO A . n 
A 1 250 ALA 250 241 241 ALA ALA A . n 
A 1 251 ILE 251 242 242 ILE ILE A . n 
A 1 252 ASP 252 243 243 ASP ASP A . n 
A 1 253 HIS 253 244 244 HIS HIS A . n 
A 1 254 LEU 254 245 245 LEU LEU A . n 
A 1 255 ASP 255 246 246 ASP ASP A . n 
A 1 256 ALA 256 247 247 ALA ALA A . n 
A 1 257 MET 257 248 248 MET MET A . n 
A 1 258 ASP 258 249 249 ASP ASP A . n 
A 1 259 SER 259 250 250 SER SER A . n 
A 1 260 ASN 260 251 251 ASN ASN A . n 
A 1 261 PRO 261 252 252 PRO PRO A . n 
A 1 262 LEU 262 253 253 LEU LEU A . n 
A 1 263 SER 263 254 254 SER SER A . n 
A 1 264 LEU 264 255 255 LEU LEU A . n 
A 1 265 GLY 265 256 256 GLY GLY A . n 
A 1 266 LEU 266 257 257 LEU LEU A . n 
A 1 267 ALA 267 258 258 ALA ALA A . n 
A 1 268 VAL 268 259 259 VAL VAL A . n 
A 1 269 VAL 269 260 260 VAL VAL A . n 
A 1 270 GLU 270 261 261 GLU GLU A . n 
A 1 271 ARG 271 262 262 ARG ARG A . n 
A 1 272 LEU 272 263 263 LEU LEU A . n 
A 1 273 ASN 273 264 264 ASN ASN A . n 
A 1 274 LYS 274 265 265 LYS LYS A . n 
A 1 275 ILE 275 266 266 ILE ILE A . n 
A 1 276 GLN 276 267 267 GLN GLN A . n 
A 1 277 LEU 277 268 268 LEU LEU A . n 
A 1 278 HIS 278 269 269 HIS HIS A . n 
A 1 279 SER 279 270 270 SER SER A . n 
A 1 280 GLY 280 271 271 GLY GLY A . n 
A 1 281 SER 281 272 272 SER SER A . n 
A 1 282 LYS 282 273 273 LYS LYS A . n 
A 1 283 LEU 283 274 274 LEU LEU A . n 
A 1 284 ALA 284 275 275 ALA ALA A . n 
A 1 285 TYR 285 276 276 TYR TYR A . n 
A 1 286 LEU 286 277 277 LEU LEU A . n 
A 1 287 HIS 287 278 278 HIS HIS A . n 
A 1 288 VAL 288 279 279 VAL VAL A . n 
A 1 289 THR 289 280 280 THR THR A . n 
A 1 290 GLN 290 281 281 GLN GLN A . n 
A 1 291 PRO 291 282 282 PRO PRO A . n 
A 1 292 ARG 292 283 283 ARG ARG A . n 
A 1 293 SER 293 284 284 SER SER A . n 
A 1 294 ASP 294 285 ?   ?   ?   A . n 
A 1 295 LYS 295 286 ?   ?   ?   A . n 
A 1 296 GLY 296 287 ?   ?   ?   A . n 
A 1 297 GLY 297 288 ?   ?   ?   A . n 
A 1 298 SER 298 289 290 SER SER A . n 
A 1 299 GLU 299 290 291 GLU GLU A . n 
A 1 300 GLU 300 291 292 GLU GLU A . n 
A 1 301 GLU 301 292 293 GLU GLU A . n 
A 1 302 GLU 302 293 294 GLU GLU A . n 
A 1 303 ALA 303 294 295 ALA ALA A . n 
A 1 304 ARG 304 295 296 ARG ARG A . n 
A 1 305 LEU 305 296 297 LEU LEU A . n 
A 1 306 MET 306 297 298 MET MET A . n 
A 1 307 ARG 307 298 299 ARG ARG A . n 
A 1 308 THR 308 299 300 THR THR A . n 
A 1 309 LEU 309 300 301 LEU LEU A . n 
A 1 310 ARG 310 301 302 ARG ARG A . n 
A 1 311 ASN 311 302 303 ASN ASN A . n 
A 1 312 ALA 312 303 304 ALA ALA A . n 
A 1 313 TYR 313 304 305 TYR TYR A . n 
A 1 314 GLN 314 305 306 GLN GLN A . n 
A 1 315 GLY 315 306 307 GLY GLY A . n 
A 1 316 THR 316 307 308 THR THR A . n 
A 1 317 PHE 317 308 309 PHE PHE A . n 
A 1 318 ILE 318 309 310 ILE ILE A . n 
A 1 319 CYS 319 310 311 CYS CYS A . n 
A 1 320 SER 320 311 312 SER SER A . n 
A 1 321 GLY 321 312 313 GLY GLY A . n 
A 1 322 GLY 322 313 314 GLY GLY A . n 
A 1 323 TYR 323 314 315 TYR TYR A . n 
A 1 324 THR 324 315 316 THR THR A . n 
A 1 325 ARG 325 316 317 ARG ARG A . n 
A 1 326 GLU 326 317 318 GLU GLU A . n 
A 1 327 LEU 327 318 319 LEU LEU A . n 
A 1 328 GLY 328 319 320 GLY GLY A . n 
A 1 329 ILE 329 320 321 ILE ILE A . n 
A 1 330 GLU 330 321 322 GLU GLU A . n 
A 1 331 ALA 331 322 323 ALA ALA A . n 
A 1 332 VAL 332 323 324 VAL VAL A . n 
A 1 333 ALA 333 324 325 ALA ALA A . n 
A 1 334 GLN 334 325 326 GLN GLN A . n 
A 1 335 GLY 335 326 327 GLY GLY A . n 
A 1 336 ASP 336 327 328 ASP ASP A . n 
A 1 337 ALA 337 328 329 ALA ALA A . n 
A 1 338 ASP 338 329 330 ASP ASP A . n 
A 1 339 LEU 339 330 331 LEU LEU A . n 
A 1 340 VAL 340 331 332 VAL VAL A . n 
A 1 341 SER 341 332 333 SER SER A . n 
A 1 342 TYR 342 333 334 TYR TYR A . n 
A 1 343 GLY 343 334 335 GLY GLY A . n 
A 1 344 ARG 344 335 336 ARG ARG A . n 
A 1 345 LEU 345 336 337 LEU LEU A . n 
A 1 346 PHE 346 337 338 PHE PHE A . n 
A 1 347 ILE 347 338 339 ILE ILE A . n 
A 1 348 SER 348 339 340 SER SER A . n 
A 1 349 ASN 349 340 341 ASN ASN A . n 
A 1 350 PRO 350 341 342 PRO PRO A . n 
A 1 351 ASP 351 342 343 ASP ASP A . n 
A 1 352 LEU 352 343 344 LEU LEU A . n 
A 1 353 VAL 353 344 345 VAL VAL A . n 
A 1 354 MET 354 345 346 MET MET A . n 
A 1 355 ARG 355 346 347 ARG ARG A . n 
A 1 356 ILE 356 347 348 ILE ILE A . n 
A 1 357 LYS 357 348 349 LYS LYS A . n 
A 1 358 LEU 358 349 350 LEU LEU A . n 
A 1 359 ASN 359 350 351 ASN ASN A . n 
A 1 360 ALA 360 351 352 ALA ALA A . n 
A 1 361 PRO 361 352 353 PRO PRO A . n 
A 1 362 LEU 362 353 354 LEU LEU A . n 
A 1 363 ASN 363 354 355 ASN ASN A . n 
A 1 364 LYS 364 355 356 LYS LYS A . n 
A 1 365 TYR 365 356 357 TYR TYR A . n 
A 1 366 ASN 366 357 358 ASN ASN A . n 
A 1 367 ARG 367 358 359 ARG ARG A . n 
A 1 368 LYS 368 359 360 LYS LYS A . n 
A 1 369 THR 369 360 361 THR THR A . n 
A 1 370 PHE 370 361 362 PHE PHE A . n 
A 1 371 TYR 371 362 363 TYR TYR A . n 
A 1 372 THR 372 363 364 THR THR A . n 
A 1 373 GLN 373 364 365 GLN GLN A . n 
A 1 374 ASP 374 365 366 ASP ASP A . n 
A 1 375 PRO 375 366 367 PRO PRO A . n 
A 1 376 VAL 376 367 368 VAL VAL A . n 
A 1 377 VAL 377 368 369 VAL VAL A . n 
A 1 378 GLY 378 369 370 GLY GLY A . n 
A 1 379 TYR 379 370 371 TYR TYR A . n 
A 1 380 THR 380 371 372 THR THR A . n 
A 1 381 ASP 381 372 373 ASP ASP A . n 
A 1 382 TYR 382 373 374 TYR TYR A . n 
A 1 383 PRO 383 374 375 PRO PRO A . n 
A 1 384 PHE 384 375 376 PHE PHE A . n 
A 1 385 LEU 385 376 377 LEU LEU A . n 
A 1 386 GLN 386 377 378 GLN GLN A . n 
A 1 387 GLY 387 378 ?   ?   ?   A . n 
A 1 388 ASN 388 379 ?   ?   ?   A . n 
A 1 389 GLY 389 380 ?   ?   ?   A . n 
A 1 390 SER 390 381 ?   ?   ?   A . n 
A 1 391 ASN 391 382 ?   ?   ?   A . n 
A 1 392 GLY 392 383 ?   ?   ?   A . n 
A 1 393 PRO 393 384 ?   ?   ?   A . n 
A 1 394 LEU 394 385 ?   ?   ?   A . n 
A 1 395 SER 395 386 ?   ?   ?   A . n 
A 1 396 ARG 396 387 ?   ?   ?   A . n 
A 1 397 LEU 397 388 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMN 1   400 400 FMN FMN A . 
C 3 MPD 1   401 401 MPD MPD A . 
D 3 MPD 1   402 402 MPD MPD A . 
E 3 MPD 1   403 403 MPD MPD A . 
F 4 SO4 1   404 404 SO4 SO4 A . 
G 5 1PE 1   405 405 1PE 1PE A . 
H 6 HOH 1   501 194 HOH HOH A . 
H 6 HOH 2   502 161 HOH HOH A . 
H 6 HOH 3   503 303 HOH HOH A . 
H 6 HOH 4   504 350 HOH HOH A . 
H 6 HOH 5   505 259 HOH HOH A . 
H 6 HOH 6   506 104 HOH HOH A . 
H 6 HOH 7   507 279 HOH HOH A . 
H 6 HOH 8   508 228 HOH HOH A . 
H 6 HOH 9   509 147 HOH HOH A . 
H 6 HOH 10  510 114 HOH HOH A . 
H 6 HOH 11  511 284 HOH HOH A . 
H 6 HOH 12  512 245 HOH HOH A . 
H 6 HOH 13  513 176 HOH HOH A . 
H 6 HOH 14  514 214 HOH HOH A . 
H 6 HOH 15  515 62  HOH HOH A . 
H 6 HOH 16  516 283 HOH HOH A . 
H 6 HOH 17  517 178 HOH HOH A . 
H 6 HOH 18  518 78  HOH HOH A . 
H 6 HOH 19  519 71  HOH HOH A . 
H 6 HOH 20  520 265 HOH HOH A . 
H 6 HOH 21  521 131 HOH HOH A . 
H 6 HOH 22  522 302 HOH HOH A . 
H 6 HOH 23  523 49  HOH HOH A . 
H 6 HOH 24  524 344 HOH HOH A . 
H 6 HOH 25  525 149 HOH HOH A . 
H 6 HOH 26  526 102 HOH HOH A . 
H 6 HOH 27  527 258 HOH HOH A . 
H 6 HOH 28  528 343 HOH HOH A . 
H 6 HOH 29  529 12  HOH HOH A . 
H 6 HOH 30  530 85  HOH HOH A . 
H 6 HOH 31  531 43  HOH HOH A . 
H 6 HOH 32  532 219 HOH HOH A . 
H 6 HOH 33  533 177 HOH HOH A . 
H 6 HOH 34  534 205 HOH HOH A . 
H 6 HOH 35  535 335 HOH HOH A . 
H 6 HOH 36  536 175 HOH HOH A . 
H 6 HOH 37  537 315 HOH HOH A . 
H 6 HOH 38  538 359 HOH HOH A . 
H 6 HOH 39  539 38  HOH HOH A . 
H 6 HOH 40  540 210 HOH HOH A . 
H 6 HOH 41  541 338 HOH HOH A . 
H 6 HOH 42  542 231 HOH HOH A . 
H 6 HOH 43  543 35  HOH HOH A . 
H 6 HOH 44  544 116 HOH HOH A . 
H 6 HOH 45  545 20  HOH HOH A . 
H 6 HOH 46  546 46  HOH HOH A . 
H 6 HOH 47  547 129 HOH HOH A . 
H 6 HOH 48  548 21  HOH HOH A . 
H 6 HOH 49  549 61  HOH HOH A . 
H 6 HOH 50  550 24  HOH HOH A . 
H 6 HOH 51  551 34  HOH HOH A . 
H 6 HOH 52  552 145 HOH HOH A . 
H 6 HOH 53  553 41  HOH HOH A . 
H 6 HOH 54  554 244 HOH HOH A . 
H 6 HOH 55  555 37  HOH HOH A . 
H 6 HOH 56  556 297 HOH HOH A . 
H 6 HOH 57  557 44  HOH HOH A . 
H 6 HOH 58  558 216 HOH HOH A . 
H 6 HOH 59  559 336 HOH HOH A . 
H 6 HOH 60  560 111 HOH HOH A . 
H 6 HOH 61  561 80  HOH HOH A . 
H 6 HOH 62  562 235 HOH HOH A . 
H 6 HOH 63  563 163 HOH HOH A . 
H 6 HOH 64  564 33  HOH HOH A . 
H 6 HOH 65  565 151 HOH HOH A . 
H 6 HOH 66  566 227 HOH HOH A . 
H 6 HOH 67  567 91  HOH HOH A . 
H 6 HOH 68  568 154 HOH HOH A . 
H 6 HOH 69  569 83  HOH HOH A . 
H 6 HOH 70  570 249 HOH HOH A . 
H 6 HOH 71  571 31  HOH HOH A . 
H 6 HOH 72  572 8   HOH HOH A . 
H 6 HOH 73  573 167 HOH HOH A . 
H 6 HOH 74  574 74  HOH HOH A . 
H 6 HOH 75  575 73  HOH HOH A . 
H 6 HOH 76  576 365 HOH HOH A . 
H 6 HOH 77  577 124 HOH HOH A . 
H 6 HOH 78  578 5   HOH HOH A . 
H 6 HOH 79  579 118 HOH HOH A . 
H 6 HOH 80  580 26  HOH HOH A . 
H 6 HOH 81  581 67  HOH HOH A . 
H 6 HOH 82  582 4   HOH HOH A . 
H 6 HOH 83  583 262 HOH HOH A . 
H 6 HOH 84  584 89  HOH HOH A . 
H 6 HOH 85  585 189 HOH HOH A . 
H 6 HOH 86  586 168 HOH HOH A . 
H 6 HOH 87  587 373 HOH HOH A . 
H 6 HOH 88  588 15  HOH HOH A . 
H 6 HOH 89  589 92  HOH HOH A . 
H 6 HOH 90  590 55  HOH HOH A . 
H 6 HOH 91  591 47  HOH HOH A . 
H 6 HOH 92  592 290 HOH HOH A . 
H 6 HOH 93  593 2   HOH HOH A . 
H 6 HOH 94  594 141 HOH HOH A . 
H 6 HOH 95  595 56  HOH HOH A . 
H 6 HOH 96  596 192 HOH HOH A . 
H 6 HOH 97  597 68  HOH HOH A . 
H 6 HOH 98  598 25  HOH HOH A . 
H 6 HOH 99  599 146 HOH HOH A . 
H 6 HOH 100 600 117 HOH HOH A . 
H 6 HOH 101 601 166 HOH HOH A . 
H 6 HOH 102 602 18  HOH HOH A . 
H 6 HOH 103 603 213 HOH HOH A . 
H 6 HOH 104 604 105 HOH HOH A . 
H 6 HOH 105 605 109 HOH HOH A . 
H 6 HOH 106 606 199 HOH HOH A . 
H 6 HOH 107 607 119 HOH HOH A . 
H 6 HOH 108 608 159 HOH HOH A . 
H 6 HOH 109 609 257 HOH HOH A . 
H 6 HOH 110 610 10  HOH HOH A . 
H 6 HOH 111 611 32  HOH HOH A . 
H 6 HOH 112 612 66  HOH HOH A . 
H 6 HOH 113 613 247 HOH HOH A . 
H 6 HOH 114 614 126 HOH HOH A . 
H 6 HOH 115 615 99  HOH HOH A . 
H 6 HOH 116 616 48  HOH HOH A . 
H 6 HOH 117 617 160 HOH HOH A . 
H 6 HOH 118 618 155 HOH HOH A . 
H 6 HOH 119 619 11  HOH HOH A . 
H 6 HOH 120 620 246 HOH HOH A . 
H 6 HOH 121 621 88  HOH HOH A . 
H 6 HOH 122 622 96  HOH HOH A . 
H 6 HOH 123 623 110 HOH HOH A . 
H 6 HOH 124 624 28  HOH HOH A . 
H 6 HOH 125 625 39  HOH HOH A . 
H 6 HOH 126 626 81  HOH HOH A . 
H 6 HOH 127 627 120 HOH HOH A . 
H 6 HOH 128 628 23  HOH HOH A . 
H 6 HOH 129 629 172 HOH HOH A . 
H 6 HOH 130 630 45  HOH HOH A . 
H 6 HOH 131 631 152 HOH HOH A . 
H 6 HOH 132 632 229 HOH HOH A . 
H 6 HOH 133 633 170 HOH HOH A . 
H 6 HOH 134 634 36  HOH HOH A . 
H 6 HOH 135 635 251 HOH HOH A . 
H 6 HOH 136 636 248 HOH HOH A . 
H 6 HOH 137 637 377 HOH HOH A . 
H 6 HOH 138 638 97  HOH HOH A . 
H 6 HOH 139 639 59  HOH HOH A . 
H 6 HOH 140 640 7   HOH HOH A . 
H 6 HOH 141 641 206 HOH HOH A . 
H 6 HOH 142 642 57  HOH HOH A . 
H 6 HOH 143 643 84  HOH HOH A . 
H 6 HOH 144 644 82  HOH HOH A . 
H 6 HOH 145 645 29  HOH HOH A . 
H 6 HOH 146 646 64  HOH HOH A . 
H 6 HOH 147 647 181 HOH HOH A . 
H 6 HOH 148 648 17  HOH HOH A . 
H 6 HOH 149 649 273 HOH HOH A . 
H 6 HOH 150 650 14  HOH HOH A . 
H 6 HOH 151 651 323 HOH HOH A . 
H 6 HOH 152 652 3   HOH HOH A . 
H 6 HOH 153 653 179 HOH HOH A . 
H 6 HOH 154 654 209 HOH HOH A . 
H 6 HOH 155 655 296 HOH HOH A . 
H 6 HOH 156 656 140 HOH HOH A . 
H 6 HOH 157 657 367 HOH HOH A . 
H 6 HOH 158 658 134 HOH HOH A . 
H 6 HOH 159 659 218 HOH HOH A . 
H 6 HOH 160 660 268 HOH HOH A . 
H 6 HOH 161 661 337 HOH HOH A . 
H 6 HOH 162 662 342 HOH HOH A . 
H 6 HOH 163 663 51  HOH HOH A . 
H 6 HOH 164 664 9   HOH HOH A . 
H 6 HOH 165 665 222 HOH HOH A . 
H 6 HOH 166 666 156 HOH HOH A . 
H 6 HOH 167 667 239 HOH HOH A . 
H 6 HOH 168 668 69  HOH HOH A . 
H 6 HOH 169 669 70  HOH HOH A . 
H 6 HOH 170 670 202 HOH HOH A . 
H 6 HOH 171 671 207 HOH HOH A . 
H 6 HOH 172 672 30  HOH HOH A . 
H 6 HOH 173 673 221 HOH HOH A . 
H 6 HOH 174 674 58  HOH HOH A . 
H 6 HOH 175 675 325 HOH HOH A . 
H 6 HOH 176 676 204 HOH HOH A . 
H 6 HOH 177 677 132 HOH HOH A . 
H 6 HOH 178 678 211 HOH HOH A . 
H 6 HOH 179 679 72  HOH HOH A . 
H 6 HOH 180 680 243 HOH HOH A . 
H 6 HOH 181 681 326 HOH HOH A . 
H 6 HOH 182 682 50  HOH HOH A . 
H 6 HOH 183 683 60  HOH HOH A . 
H 6 HOH 184 684 13  HOH HOH A . 
H 6 HOH 185 685 112 HOH HOH A . 
H 6 HOH 186 686 144 HOH HOH A . 
H 6 HOH 187 687 217 HOH HOH A . 
H 6 HOH 188 688 340 HOH HOH A . 
H 6 HOH 189 689 19  HOH HOH A . 
H 6 HOH 190 690 77  HOH HOH A . 
H 6 HOH 191 691 42  HOH HOH A . 
H 6 HOH 192 692 22  HOH HOH A . 
H 6 HOH 193 693 27  HOH HOH A . 
H 6 HOH 194 694 203 HOH HOH A . 
H 6 HOH 195 695 108 HOH HOH A . 
H 6 HOH 196 696 135 HOH HOH A . 
H 6 HOH 197 697 171 HOH HOH A . 
H 6 HOH 198 698 137 HOH HOH A . 
H 6 HOH 199 699 1   HOH HOH A . 
H 6 HOH 200 700 250 HOH HOH A . 
H 6 HOH 201 701 16  HOH HOH A . 
H 6 HOH 202 702 6   HOH HOH A . 
H 6 HOH 203 703 198 HOH HOH A . 
H 6 HOH 204 704 256 HOH HOH A . 
H 6 HOH 205 705 136 HOH HOH A . 
H 6 HOH 206 706 321 HOH HOH A . 
H 6 HOH 207 707 307 HOH HOH A . 
H 6 HOH 208 708 311 HOH HOH A . 
H 6 HOH 209 709 101 HOH HOH A . 
H 6 HOH 210 710 215 HOH HOH A . 
H 6 HOH 211 711 370 HOH HOH A . 
H 6 HOH 212 712 162 HOH HOH A . 
H 6 HOH 213 713 139 HOH HOH A . 
H 6 HOH 214 714 320 HOH HOH A . 
H 6 HOH 215 715 54  HOH HOH A . 
H 6 HOH 216 716 366 HOH HOH A . 
H 6 HOH 217 717 341 HOH HOH A . 
H 6 HOH 218 718 127 HOH HOH A . 
H 6 HOH 219 719 130 HOH HOH A . 
H 6 HOH 220 720 157 HOH HOH A . 
H 6 HOH 221 721 95  HOH HOH A . 
H 6 HOH 222 722 122 HOH HOH A . 
H 6 HOH 223 723 150 HOH HOH A . 
H 6 HOH 224 724 358 HOH HOH A . 
H 6 HOH 225 725 281 HOH HOH A . 
H 6 HOH 226 726 138 HOH HOH A . 
H 6 HOH 227 727 93  HOH HOH A . 
H 6 HOH 228 728 128 HOH HOH A . 
H 6 HOH 229 729 182 HOH HOH A . 
H 6 HOH 230 730 174 HOH HOH A . 
H 6 HOH 231 731 363 HOH HOH A . 
H 6 HOH 232 732 354 HOH HOH A . 
H 6 HOH 233 733 285 HOH HOH A . 
H 6 HOH 234 734 63  HOH HOH A . 
H 6 HOH 235 735 153 HOH HOH A . 
H 6 HOH 236 736 220 HOH HOH A . 
H 6 HOH 237 737 142 HOH HOH A . 
H 6 HOH 238 738 255 HOH HOH A . 
H 6 HOH 239 739 79  HOH HOH A . 
H 6 HOH 240 740 371 HOH HOH A . 
H 6 HOH 241 741 253 HOH HOH A . 
H 6 HOH 242 742 201 HOH HOH A . 
H 6 HOH 243 743 98  HOH HOH A . 
H 6 HOH 244 744 364 HOH HOH A . 
H 6 HOH 245 745 269 HOH HOH A . 
H 6 HOH 246 746 40  HOH HOH A . 
H 6 HOH 247 747 241 HOH HOH A . 
H 6 HOH 248 748 185 HOH HOH A . 
H 6 HOH 249 749 53  HOH HOH A . 
H 6 HOH 250 750 87  HOH HOH A . 
H 6 HOH 251 751 200 HOH HOH A . 
H 6 HOH 252 752 234 HOH HOH A . 
H 6 HOH 253 753 232 HOH HOH A . 
H 6 HOH 254 754 347 HOH HOH A . 
H 6 HOH 255 755 318 HOH HOH A . 
H 6 HOH 256 756 352 HOH HOH A . 
H 6 HOH 257 757 76  HOH HOH A . 
H 6 HOH 258 758 186 HOH HOH A . 
H 6 HOH 259 759 230 HOH HOH A . 
H 6 HOH 260 760 103 HOH HOH A . 
H 6 HOH 261 761 361 HOH HOH A . 
H 6 HOH 262 762 304 HOH HOH A . 
H 6 HOH 263 763 372 HOH HOH A . 
H 6 HOH 264 764 310 HOH HOH A . 
H 6 HOH 265 765 224 HOH HOH A . 
H 6 HOH 266 766 121 HOH HOH A . 
H 6 HOH 267 767 164 HOH HOH A . 
H 6 HOH 268 768 272 HOH HOH A . 
H 6 HOH 269 769 274 HOH HOH A . 
H 6 HOH 270 770 52  HOH HOH A . 
H 6 HOH 271 771 187 HOH HOH A . 
H 6 HOH 272 772 278 HOH HOH A . 
H 6 HOH 273 773 133 HOH HOH A . 
H 6 HOH 274 774 252 HOH HOH A . 
H 6 HOH 275 775 188 HOH HOH A . 
H 6 HOH 276 776 289 HOH HOH A . 
H 6 HOH 277 777 280 HOH HOH A . 
H 6 HOH 278 778 212 HOH HOH A . 
H 6 HOH 279 779 180 HOH HOH A . 
H 6 HOH 280 780 353 HOH HOH A . 
H 6 HOH 281 781 328 HOH HOH A . 
H 6 HOH 282 782 242 HOH HOH A . 
H 6 HOH 283 783 375 HOH HOH A . 
H 6 HOH 284 784 346 HOH HOH A . 
H 6 HOH 285 785 271 HOH HOH A . 
H 6 HOH 286 786 115 HOH HOH A . 
H 6 HOH 287 787 294 HOH HOH A . 
H 6 HOH 288 788 90  HOH HOH A . 
H 6 HOH 289 789 260 HOH HOH A . 
H 6 HOH 290 790 100 HOH HOH A . 
H 6 HOH 291 791 306 HOH HOH A . 
H 6 HOH 292 792 165 HOH HOH A . 
H 6 HOH 293 793 226 HOH HOH A . 
H 6 HOH 294 794 333 HOH HOH A . 
H 6 HOH 295 795 376 HOH HOH A . 
H 6 HOH 296 796 313 HOH HOH A . 
H 6 HOH 297 797 319 HOH HOH A . 
H 6 HOH 298 798 291 HOH HOH A . 
H 6 HOH 299 799 339 HOH HOH A . 
H 6 HOH 300 800 261 HOH HOH A . 
H 6 HOH 301 801 143 HOH HOH A . 
H 6 HOH 302 802 173 HOH HOH A . 
H 6 HOH 303 803 378 HOH HOH A . 
H 6 HOH 304 804 330 HOH HOH A . 
H 6 HOH 305 805 292 HOH HOH A . 
H 6 HOH 306 806 282 HOH HOH A . 
H 6 HOH 307 807 287 HOH HOH A . 
H 6 HOH 308 808 113 HOH HOH A . 
H 6 HOH 309 809 368 HOH HOH A . 
H 6 HOH 310 810 106 HOH HOH A . 
H 6 HOH 311 811 75  HOH HOH A . 
H 6 HOH 312 812 286 HOH HOH A . 
H 6 HOH 313 813 277 HOH HOH A . 
H 6 HOH 314 814 312 HOH HOH A . 
H 6 HOH 315 815 345 HOH HOH A . 
H 6 HOH 316 816 332 HOH HOH A . 
H 6 HOH 317 817 94  HOH HOH A . 
H 6 HOH 318 818 360 HOH HOH A . 
H 6 HOH 319 819 301 HOH HOH A . 
H 6 HOH 320 820 148 HOH HOH A . 
H 6 HOH 321 821 158 HOH HOH A . 
H 6 HOH 322 822 293 HOH HOH A . 
H 6 HOH 323 823 298 HOH HOH A . 
H 6 HOH 324 824 208 HOH HOH A . 
H 6 HOH 325 825 327 HOH HOH A . 
H 6 HOH 326 826 362 HOH HOH A . 
H 6 HOH 327 827 316 HOH HOH A . 
H 6 HOH 328 828 236 HOH HOH A . 
H 6 HOH 329 829 369 HOH HOH A . 
H 6 HOH 330 830 184 HOH HOH A . 
H 6 HOH 331 831 193 HOH HOH A . 
H 6 HOH 332 832 123 HOH HOH A . 
H 6 HOH 333 833 240 HOH HOH A . 
H 6 HOH 334 834 225 HOH HOH A . 
H 6 HOH 335 835 254 HOH HOH A . 
H 6 HOH 336 836 197 HOH HOH A . 
H 6 HOH 337 837 314 HOH HOH A . 
H 6 HOH 338 838 329 HOH HOH A . 
H 6 HOH 339 839 288 HOH HOH A . 
H 6 HOH 340 840 107 HOH HOH A . 
H 6 HOH 341 841 237 HOH HOH A . 
H 6 HOH 342 842 267 HOH HOH A . 
H 6 HOH 343 843 317 HOH HOH A . 
H 6 HOH 344 844 195 HOH HOH A . 
H 6 HOH 345 845 125 HOH HOH A . 
H 6 HOH 346 846 276 HOH HOH A . 
H 6 HOH 347 847 266 HOH HOH A . 
H 6 HOH 348 848 324 HOH HOH A . 
H 6 HOH 349 849 264 HOH HOH A . 
H 6 HOH 350 850 295 HOH HOH A . 
H 6 HOH 351 851 191 HOH HOH A . 
H 6 HOH 352 852 190 HOH HOH A . 
H 6 HOH 353 853 223 HOH HOH A . 
H 6 HOH 354 854 65  HOH HOH A . 
H 6 HOH 355 855 334 HOH HOH A . 
H 6 HOH 356 856 322 HOH HOH A . 
H 6 HOH 357 857 270 HOH HOH A . 
H 6 HOH 358 858 309 HOH HOH A . 
H 6 HOH 359 859 183 HOH HOH A . 
H 6 HOH 360 860 275 HOH HOH A . 
H 6 HOH 361 861 300 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 116 ? CG  ? A GLU 125 CG  
2  1 Y 1 A GLU 116 ? CD  ? A GLU 125 CD  
3  1 Y 1 A GLU 116 ? OE1 ? A GLU 125 OE1 
4  1 Y 1 A GLU 116 ? OE2 ? A GLU 125 OE2 
5  1 Y 1 A ARG 136 ? CG  ? A ARG 145 CG  
6  1 Y 1 A ARG 136 ? CD  ? A ARG 145 CD  
7  1 Y 1 A ARG 136 ? NE  ? A ARG 145 NE  
8  1 Y 1 A ARG 136 ? CZ  ? A ARG 145 CZ  
9  1 Y 1 A ARG 136 ? NH1 ? A ARG 145 NH1 
10 1 Y 1 A ARG 136 ? NH2 ? A ARG 145 NH2 
11 1 Y 1 A ASP 243 ? CG  ? A ASP 252 CG  
12 1 Y 1 A ASP 243 ? OD1 ? A ASP 252 OD1 
13 1 Y 1 A ASP 243 ? OD2 ? A ASP 252 OD2 
14 1 Y 1 A MET 248 ? CG  ? A MET 257 CG  
15 1 Y 1 A MET 248 ? SD  ? A MET 257 SD  
16 1 Y 1 A MET 248 ? CE  ? A MET 257 CE  
17 1 Y 1 A LYS 265 ? CG  ? A LYS 274 CG  
18 1 Y 1 A LYS 265 ? CD  ? A LYS 274 CD  
19 1 Y 1 A LYS 265 ? CE  ? A LYS 274 CE  
20 1 Y 1 A LYS 265 ? NZ  ? A LYS 274 NZ  
21 1 Y 1 A SER 284 ? OG  ? A SER 293 OG  
22 1 Y 1 A SER 289 ? OG  ? A SER 298 OG  
23 1 Y 1 A GLU 290 ? CG  ? A GLU 299 CG  
24 1 Y 1 A GLU 290 ? CD  ? A GLU 299 CD  
25 1 Y 1 A GLU 290 ? OE1 ? A GLU 299 OE1 
26 1 Y 1 A GLU 290 ? OE2 ? A GLU 299 OE2 
27 1 Y 1 A GLU 291 ? CG  ? A GLU 300 CG  
28 1 Y 1 A GLU 291 ? CD  ? A GLU 300 CD  
29 1 Y 1 A GLU 291 ? OE1 ? A GLU 300 OE1 
30 1 Y 1 A GLU 291 ? OE2 ? A GLU 300 OE2 
31 1 Y 1 A GLU 292 ? CG  ? A GLU 301 CG  
32 1 Y 1 A GLU 292 ? CD  ? A GLU 301 CD  
33 1 Y 1 A GLU 292 ? OE1 ? A GLU 301 OE1 
34 1 Y 1 A GLU 292 ? OE2 ? A GLU 301 OE2 
35 1 Y 1 A LYS 359 ? CG  ? A LYS 368 CG  
36 1 Y 1 A LYS 359 ? CD  ? A LYS 368 CD  
37 1 Y 1 A LYS 359 ? CE  ? A LYS 368 CE  
38 1 Y 1 A LYS 359 ? NZ  ? A LYS 368 NZ  
39 1 Y 1 A GLN 377 ? CG  ? A GLN 386 CG  
40 1 Y 1 A GLN 377 ? CD  ? A GLN 386 CD  
41 1 Y 1 A GLN 377 ? OE1 ? A GLN 386 OE1 
42 1 Y 1 A GLN 377 ? NE2 ? A GLN 386 NE2 
# 
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 ? ? ? '(dev_4761)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? '(dev_4761)' 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QNE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     87.360 
_cell.length_a_esd                 ? 
_cell.length_b                     90.100 
_cell.length_b_esd                 ? 
_cell.length_c                     49.390 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         8QNE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8QNE 
_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             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.35 
_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              6.5 
_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    '100 mM MES/Tris, 50 mM ammonium sulfate, 12% PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_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                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-30 
_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   1.03323 
_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                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA II, DESY BEAMLINE PETRA1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03323 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   PETRA1 
_diffrn_source.pdbx_synchrotron_site       'PETRA II, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QNE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               43.68 
_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                                     907508 
_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                           97.17 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.31 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.4 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             75301 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.38 
_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                                  ? 
_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                               ? 
_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                                 8QNE 
_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                            1.40 
_refine.ls_d_res_low                             43.68 
_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                     75302 
_refine.ls_number_reflns_R_free                  3766 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.17 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1598 
_refine.ls_R_factor_R_free                       0.1823 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1586 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 19.09 
_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                            0.14 
_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                       1.40 
_refine_hist.d_res_low                        43.68 
_refine_hist.number_atoms_solvent             362 
_refine_hist.number_atoms_total               3239 
_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        2801 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         76 
_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' ? 0.022  ? 2981 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.493  ? 4062 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.607 ? 433  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.112  ? 444  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.018  ? 523  ? f_plane_restr      ? ? 
# 
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' 1.40 1.42  . . 106 2015 75.00  . . . . 0.3094 . . . . . . . . . . . 0.3210 
'X-RAY DIFFRACTION' 1.42 1.44  . . 115 2191 81.00  . . . . 0.2805 . . . . . . . . . . . 0.2818 
'X-RAY DIFFRACTION' 1.44 1.46  . . 120 2277 84.00  . . . . 0.2648 . . . . . . . . . . . 0.3321 
'X-RAY DIFFRACTION' 1.46 1.48  . . 129 2443 92.00  . . . . 0.2637 . . . . . . . . . . . 0.2435 
'X-RAY DIFFRACTION' 1.48 1.50  . . 137 2605 96.00  . . . . 0.2487 . . . . . . . . . . . 0.2664 
'X-RAY DIFFRACTION' 1.50 1.52  . . 138 2630 99.00  . . . . 0.2205 . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 1.52 1.55  . . 143 2706 99.00  . . . . 0.2085 . . . . . . . . . . . 0.2569 
'X-RAY DIFFRACTION' 1.55 1.57  . . 140 2654 100.00 . . . . 0.1852 . . . . . . . . . . . 0.2156 
'X-RAY DIFFRACTION' 1.57 1.60  . . 142 2702 100.00 . . . . 0.1779 . . . . . . . . . . . 0.1935 
'X-RAY DIFFRACTION' 1.60 1.63  . . 142 2694 100.00 . . . . 0.1670 . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 1.63 1.67  . . 142 2698 100.00 . . . . 0.1637 . . . . . . . . . . . 0.1912 
'X-RAY DIFFRACTION' 1.67 1.70  . . 144 2733 100.00 . . . . 0.1603 . . . . . . . . . . . 0.2036 
'X-RAY DIFFRACTION' 1.70 1.74  . . 141 2688 100.00 . . . . 0.1596 . . . . . . . . . . . 0.1943 
'X-RAY DIFFRACTION' 1.74 1.79  . . 142 2699 100.00 . . . . 0.1600 . . . . . . . . . . . 0.1826 
'X-RAY DIFFRACTION' 1.79 1.83  . . 143 2721 100.00 . . . . 0.1618 . . . . . . . . . . . 0.2017 
'X-RAY DIFFRACTION' 1.83 1.89  . . 142 2687 100.00 . . . . 0.1683 . . . . . . . . . . . 0.2106 
'X-RAY DIFFRACTION' 1.89 1.95  . . 143 2718 100.00 . . . . 0.1605 . . . . . . . . . . . 0.1832 
'X-RAY DIFFRACTION' 1.95 2.02  . . 143 2714 100.00 . . . . 0.1547 . . . . . . . . . . . 0.1940 
'X-RAY DIFFRACTION' 2.02 2.10  . . 143 2726 100.00 . . . . 0.1557 . . . . . . . . . . . 0.1816 
'X-RAY DIFFRACTION' 2.10 2.20  . . 144 2729 100.00 . . . . 0.1546 . . . . . . . . . . . 0.1903 
'X-RAY DIFFRACTION' 2.20 2.31  . . 144 2732 100.00 . . . . 0.1550 . . . . . . . . . . . 0.1822 
'X-RAY DIFFRACTION' 2.31 2.46  . . 145 2754 100.00 . . . . 0.1567 . . . . . . . . . . . 0.1767 
'X-RAY DIFFRACTION' 2.46 2.65  . . 143 2726 100.00 . . . . 0.1677 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 2.65 2.91  . . 146 2770 100.00 . . . . 0.1584 . . . . . . . . . . . 0.1932 
'X-RAY DIFFRACTION' 2.91 3.33  . . 146 2785 100.00 . . . . 0.1529 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 3.33 4.20  . . 148 2807 100.00 . . . . 0.1360 . . . . . . . . . . . 0.1528 
'X-RAY DIFFRACTION' 4.20 43.68 . . 155 2932 99.00  . . . . 0.1470 . . . . . . . . . . . 0.1616 
# 
_struct.entry_id                     8QNE 
_struct.title                        'OPR3 variant with redesigned loop 6 (9aa)' 
_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        8QNE 
_struct_keywords.text            'Old Yellow Enzyme, ene-reductase, flavoenzyme, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    OPR3_SOLLC 
_struct_ref.pdbx_db_accession          Q9FEW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGI
FTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSP
AIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QNE 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 10 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 397 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9FEW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  396 
_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       388 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8QNE MET A 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  1  
1 8QNE ALA A 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  2  
1 8QNE SER A 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  3  
1 8QNE HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  4  
1 8QNE HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  5  
1 8QNE HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  6  
1 8QNE HIS A 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  7  
1 8QNE HIS A 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  8  
1 8QNE HIS A 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   9  
1 8QNE SER A 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 10 
1 8QNE ASP A 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 11 
1 8QNE LYS A 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 12 
1 8QNE GLY A 296 ? UNP Q9FEW9 TYR 287 'engineered mutation'   287 13 
1 8QNE ?   A ?   ? UNP Q9FEW9 GLY 288 deletion                ?   14 
1 8QNE ?   A ?   ? UNP Q9FEW9 GLN 289 deletion                ?   15 
1 8QNE ?   A ?   ? UNP Q9FEW9 THR 290 deletion                ?   16 
1 8QNE ?   A ?   ? UNP Q9FEW9 GLU 291 deletion                ?   17 
1 8QNE ?   A ?   ? UNP Q9FEW9 ALA 292 deletion                ?   18 
1 8QNE ?   A ?   ? UNP Q9FEW9 GLY 293 deletion                ?   19 
1 8QNE ?   A ?   ? UNP Q9FEW9 ARG 294 deletion                ?   20 
1 8QNE ?   A ?   ? UNP Q9FEW9 LEU 295 deletion                ?   21 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 19  ? SER A 23  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 46  ? ILE A 50  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 52  ? ALA A 63  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 91  ? ALA A 107 ? THR A 82  ALA A 98  1 ? 17 
HELX_P HELX_P5  AA5 HIS A 124 ? ALA A 132 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 165 ? ALA A 186 ? GLY A 156 ALA A 177 1 ? 22 
HELX_P HELX_P7  AA7 TYR A 199 ? LYS A 206 ? TYR A 190 LYS A 197 1 ? 8  
HELX_P HELX_P8  AA8 SER A 219 ? CYS A 224 ? SER A 210 CYS A 215 1 ? 6  
HELX_P HELX_P9  AA9 CYS A 224 ? GLY A 239 ? CYS A 215 GLY A 230 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 260 ? GLY A 280 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P11 AB2 GLU A 299 ? TYR A 313 ? GLU A 290 TYR A 304 1 ? 15 
HELX_P HELX_P12 AB3 THR A 324 ? GLN A 334 ? THR A 315 GLN A 325 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 343 ? ASN A 349 ? GLY A 334 ASN A 340 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 351 ? ASN A 359 ? ASP A 342 ASN A 350 1 ? 9  
HELX_P HELX_P15 AB6 ASN A 366 ? PHE A 370 ? ASN A 357 PHE A 361 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 25  ? MET A 27  ? TYR A 16  MET A 18  
AA1 2 PHE A 30  ? LEU A 32  ? PHE A 21  LEU A 23  
AA2 1 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA2 2 PHE A 68  ? MET A 75  ? PHE A 59  MET A 66  
AA2 3 VAL A 111 ? TRP A 117 ? VAL A 102 TRP A 108 
AA2 4 GLY A 190 ? GLY A 195 ? GLY A 181 GLY A 186 
AA2 5 VAL A 243 ? VAL A 247 ? VAL A 234 VAL A 238 
AA2 6 TYR A 285 ? THR A 289 ? TYR A 276 THR A 280 
AA2 7 PHE A 317 ? SER A 320 ? PHE A 308 SER A 311 
AA2 8 LEU A 339 ? TYR A 342 ? LEU A 330 TYR A 333 
AA2 9 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA3 1 ILE A 135 ? SER A 136 ? ILE A 126 SER A 127 
AA3 2 ARG A 162 ? ALA A 163 ? ARG A 153 ALA A 154 
AA4 1 ILE A 148 ? LEU A 149 ? ILE A 139 LEU A 140 
AA4 2 HIS A 155 ? GLY A 156 ? HIS A 146 GLY A 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 25  ? N TYR A 16  O LEU A 32  ? O LEU A 23  
AA2 1 2 N LEU A 38  ? N LEU A 29  O PHE A 68  ? O PHE A 59  
AA2 2 3 N THR A 74  ? N THR A 65  O TRP A 117 ? O TRP A 108 
AA2 3 4 N LEU A 116 ? N LEU A 107 O GLU A 192 ? O GLU A 183 
AA2 4 5 N ILE A 191 ? N ILE A 182 O GLY A 244 ? O GLY A 235 
AA2 5 6 N VAL A 245 ? N VAL A 236 O HIS A 287 ? O HIS A 278 
AA2 6 7 N LEU A 286 ? N LEU A 277 O ILE A 318 ? O ILE A 309 
AA2 7 8 N CYS A 319 ? N CYS A 310 O SER A 341 ? O SER A 332 
AA2 8 9 O VAL A 340 ? O VAL A 331 N VAL A 37  ? N VAL A 28  
AA3 1 2 N SER A 136 ? N SER A 127 O ARG A 162 ? O ARG A 153 
AA4 1 2 N ILE A 148 ? N ILE A 139 O GLY A 156 ? O GLY A 147 
# 
_pdbx_entry_details.entry_id                   8QNE 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 A ASP 232 ? ? O A HOH 501 ? ? 2.10 
2 1 O   A HOH 502 ? ? O A HOH 587 ? ? 2.11 
3 1 O   A HOH 587 ? ? O A HOH 671 ? ? 2.14 
4 1 O   A HOH 629 ? ? O A HOH 777 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NH2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ARG 
_pdbx_validate_symm_contact.auth_seq_id_1     138 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    C12 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    1PE 
_pdbx_validate_symm_contact.auth_seq_id_2     405 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_556 
_pdbx_validate_symm_contact.dist              1.80 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              180 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              180 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              180 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                124.24 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.94 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 63  ? ? -45.74  153.18 
2 1 ILE A 80  ? ? -140.05 30.31  
3 1 ALA A 121 ? ? 56.80   19.55  
4 1 SER A 239 ? ? -150.78 71.75  
5 1 ALA A 247 ? ? -110.31 68.83  
6 1 ASP A 342 ? ? -93.96  40.34  
7 1 TYR A 370 ? ? -127.28 -64.07 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 262 ? ? 0.104 'SIDE CHAIN' 
2 1 ARG A 358 ? ? 0.150 'SIDE CHAIN' 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 SER A 14 ? A 11.42 
2 1 SER A 14 ? B 11.12 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -8  ? A MET 1   
2  1 Y 1 A ALA -7  ? A ALA 2   
3  1 Y 1 A SER -6  ? A SER 3   
4  1 Y 1 A HIS -5  ? A HIS 4   
5  1 Y 1 A HIS -4  ? A HIS 5   
6  1 Y 1 A HIS -3  ? A HIS 6   
7  1 Y 1 A HIS -2  ? A HIS 7   
8  1 Y 1 A HIS -1  ? A HIS 8   
9  1 Y 1 A HIS 0   ? A HIS 9   
10 1 Y 1 A MET 1   ? A MET 10  
11 1 Y 1 A ALA 2   ? A ALA 11  
12 1 Y 1 A SER 3   ? A SER 12  
13 1 Y 1 A SER 4   ? A SER 13  
14 1 Y 1 A ALA 5   ? A ALA 14  
15 1 Y 1 A GLN 6   ? A GLN 15  
16 1 Y 1 A ASP 7   ? A ASP 16  
17 1 Y 1 A GLY 8   ? A GLY 17  
18 1 Y 1 A ASN 9   ? A ASN 18  
19 1 Y 1 A ASP 285 ? A ASP 294 
20 1 Y 1 A LYS 286 ? A LYS 295 
21 1 Y 1 A GLY 287 ? A GLY 296 
22 1 Y 1 A GLY 288 ? A GLY 297 
23 1 Y 1 A GLY 378 ? A GLY 387 
24 1 Y 1 A ASN 379 ? A ASN 388 
25 1 Y 1 A GLY 380 ? A GLY 389 
26 1 Y 1 A SER 381 ? A SER 390 
27 1 Y 1 A ASN 382 ? A ASN 391 
28 1 Y 1 A GLY 383 ? A GLY 392 
29 1 Y 1 A PRO 384 ? A PRO 393 
30 1 Y 1 A LEU 385 ? A LEU 394 
31 1 Y 1 A SER 386 ? A SER 395 
32 1 Y 1 A ARG 387 ? A ARG 396 
33 1 Y 1 A LEU 388 ? A LEU 397 
# 
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 
1PE OH2    O N N 1   
1PE C12    C N N 2   
1PE C22    C N N 3   
1PE OH3    O N N 4   
1PE C13    C N N 5   
1PE C23    C N N 6   
1PE OH4    O N N 7   
1PE C14    C N N 8   
1PE C24    C N N 9   
1PE OH5    O N N 10  
1PE C15    C N N 11  
1PE C25    C N N 12  
1PE OH6    O N N 13  
1PE C16    C N N 14  
1PE C26    C N N 15  
1PE OH7    O N N 16  
1PE HO2    H N N 17  
1PE H121   H N N 18  
1PE H122   H N N 19  
1PE H221   H N N 20  
1PE H222   H N N 21  
1PE H131   H N N 22  
1PE H132   H N N 23  
1PE H231   H N N 24  
1PE H232   H N N 25  
1PE H141   H N N 26  
1PE H142   H N N 27  
1PE H241   H N N 28  
1PE H242   H N N 29  
1PE H151   H N N 30  
1PE H152   H N N 31  
1PE H251   H N N 32  
1PE H252   H N N 33  
1PE H161   H N N 34  
1PE H162   H N N 35  
1PE H261   H N N 36  
1PE H262   H N N 37  
1PE HO7    H N N 38  
ALA N      N N N 39  
ALA CA     C N S 40  
ALA C      C N N 41  
ALA O      O N N 42  
ALA CB     C N N 43  
ALA OXT    O N N 44  
ALA H      H N N 45  
ALA H2     H N N 46  
ALA HA     H N N 47  
ALA HB1    H N N 48  
ALA HB2    H N N 49  
ALA HB3    H N N 50  
ALA HXT    H N N 51  
ARG N      N N N 52  
ARG CA     C N S 53  
ARG C      C N N 54  
ARG O      O N N 55  
ARG CB     C N N 56  
ARG CG     C N N 57  
ARG CD     C N N 58  
ARG NE     N N N 59  
ARG CZ     C N N 60  
ARG NH1    N N N 61  
ARG NH2    N N N 62  
ARG OXT    O N N 63  
ARG H      H N N 64  
ARG H2     H N N 65  
ARG HA     H N N 66  
ARG HB2    H N N 67  
ARG HB3    H N N 68  
ARG HG2    H N N 69  
ARG HG3    H N N 70  
ARG HD2    H N N 71  
ARG HD3    H N N 72  
ARG HE     H N N 73  
ARG HH11   H N N 74  
ARG HH12   H N N 75  
ARG HH21   H N N 76  
ARG HH22   H N N 77  
ARG HXT    H N N 78  
ASN N      N N N 79  
ASN CA     C N S 80  
ASN C      C N N 81  
ASN O      O N N 82  
ASN CB     C N N 83  
ASN CG     C N N 84  
ASN OD1    O N N 85  
ASN ND2    N N N 86  
ASN OXT    O N N 87  
ASN H      H N N 88  
ASN H2     H N N 89  
ASN HA     H N N 90  
ASN HB2    H N N 91  
ASN HB3    H N N 92  
ASN HD21   H N N 93  
ASN HD22   H N N 94  
ASN HXT    H N N 95  
ASP N      N N N 96  
ASP CA     C N S 97  
ASP C      C N N 98  
ASP O      O N N 99  
ASP CB     C N N 100 
ASP CG     C N N 101 
ASP OD1    O N N 102 
ASP OD2    O N N 103 
ASP OXT    O N N 104 
ASP H      H N N 105 
ASP H2     H N N 106 
ASP HA     H N N 107 
ASP HB2    H N N 108 
ASP HB3    H N N 109 
ASP HD2    H N N 110 
ASP HXT    H N N 111 
CYS N      N N N 112 
CYS CA     C N R 113 
CYS C      C N N 114 
CYS O      O N N 115 
CYS CB     C N N 116 
CYS SG     S N N 117 
CYS OXT    O N N 118 
CYS H      H N N 119 
CYS H2     H N N 120 
CYS HA     H N N 121 
CYS HB2    H N N 122 
CYS HB3    H N N 123 
CYS HG     H N N 124 
CYS HXT    H N N 125 
FMN N1     N N N 126 
FMN C2     C N N 127 
FMN O2     O N N 128 
FMN N3     N N N 129 
FMN C4     C N N 130 
FMN O4     O N N 131 
FMN C4A    C N N 132 
FMN N5     N N N 133 
FMN C5A    C Y N 134 
FMN C6     C Y N 135 
FMN C7     C Y N 136 
FMN C7M    C N N 137 
FMN C8     C Y N 138 
FMN C8M    C N N 139 
FMN C9     C Y N 140 
FMN C9A    C Y N 141 
FMN N10    N N N 142 
FMN C10    C N N 143 
FMN "C1'"  C N N 144 
FMN "C2'"  C N S 145 
FMN "O2'"  O N N 146 
FMN "C3'"  C N S 147 
FMN "O3'"  O N N 148 
FMN "C4'"  C N R 149 
FMN "O4'"  O N N 150 
FMN "C5'"  C N N 151 
FMN "O5'"  O N N 152 
FMN P      P N N 153 
FMN O1P    O N N 154 
FMN O2P    O N N 155 
FMN O3P    O N N 156 
FMN HN3    H N N 157 
FMN H6     H N N 158 
FMN HM71   H N N 159 
FMN HM72   H N N 160 
FMN HM73   H N N 161 
FMN HM81   H N N 162 
FMN HM82   H N N 163 
FMN HM83   H N N 164 
FMN H9     H N N 165 
FMN "H1'1" H N N 166 
FMN "H1'2" H N N 167 
FMN "H2'"  H N N 168 
FMN "HO2'" H N N 169 
FMN "H3'"  H N N 170 
FMN "HO3'" H N N 171 
FMN "H4'"  H N N 172 
FMN "HO4'" H N N 173 
FMN "H5'1" H N N 174 
FMN "H5'2" H N N 175 
FMN HOP2   H N N 176 
FMN HOP3   H N N 177 
GLN N      N N N 178 
GLN CA     C N S 179 
GLN C      C N N 180 
GLN O      O N N 181 
GLN CB     C N N 182 
GLN CG     C N N 183 
GLN CD     C N N 184 
GLN OE1    O N N 185 
GLN NE2    N N N 186 
GLN OXT    O N N 187 
GLN H      H N N 188 
GLN H2     H N N 189 
GLN HA     H N N 190 
GLN HB2    H N N 191 
GLN HB3    H N N 192 
GLN HG2    H N N 193 
GLN HG3    H N N 194 
GLN HE21   H N N 195 
GLN HE22   H N N 196 
GLN HXT    H N N 197 
GLU N      N N N 198 
GLU CA     C N S 199 
GLU C      C N N 200 
GLU O      O N N 201 
GLU CB     C N N 202 
GLU CG     C N N 203 
GLU CD     C N N 204 
GLU OE1    O N N 205 
GLU OE2    O N N 206 
GLU OXT    O N N 207 
GLU H      H N N 208 
GLU H2     H N N 209 
GLU HA     H N N 210 
GLU HB2    H N N 211 
GLU HB3    H N N 212 
GLU HG2    H N N 213 
GLU HG3    H N N 214 
GLU HE2    H N N 215 
GLU HXT    H N N 216 
GLY N      N N N 217 
GLY CA     C N N 218 
GLY C      C N N 219 
GLY O      O N N 220 
GLY OXT    O N N 221 
GLY H      H N N 222 
GLY H2     H N N 223 
GLY HA2    H N N 224 
GLY HA3    H N N 225 
GLY HXT    H N N 226 
HIS N      N N N 227 
HIS CA     C N S 228 
HIS C      C N N 229 
HIS O      O N N 230 
HIS CB     C N N 231 
HIS CG     C Y N 232 
HIS ND1    N Y N 233 
HIS CD2    C Y N 234 
HIS CE1    C Y N 235 
HIS NE2    N Y N 236 
HIS OXT    O N N 237 
HIS H      H N N 238 
HIS H2     H N N 239 
HIS HA     H N N 240 
HIS HB2    H N N 241 
HIS HB3    H N N 242 
HIS HD1    H N N 243 
HIS HD2    H N N 244 
HIS HE1    H N N 245 
HIS HE2    H N N 246 
HIS HXT    H N N 247 
HOH O      O N N 248 
HOH H1     H N N 249 
HOH H2     H N N 250 
ILE N      N N N 251 
ILE CA     C N S 252 
ILE C      C N N 253 
ILE O      O N N 254 
ILE CB     C N S 255 
ILE CG1    C N N 256 
ILE CG2    C N N 257 
ILE CD1    C N N 258 
ILE OXT    O N N 259 
ILE H      H N N 260 
ILE H2     H N N 261 
ILE HA     H N N 262 
ILE HB     H N N 263 
ILE HG12   H N N 264 
ILE HG13   H N N 265 
ILE HG21   H N N 266 
ILE HG22   H N N 267 
ILE HG23   H N N 268 
ILE HD11   H N N 269 
ILE HD12   H N N 270 
ILE HD13   H N N 271 
ILE HXT    H N N 272 
LEU N      N N N 273 
LEU CA     C N S 274 
LEU C      C N N 275 
LEU O      O N N 276 
LEU CB     C N N 277 
LEU CG     C N N 278 
LEU CD1    C N N 279 
LEU CD2    C N N 280 
LEU OXT    O N N 281 
LEU H      H N N 282 
LEU H2     H N N 283 
LEU HA     H N N 284 
LEU HB2    H N N 285 
LEU HB3    H N N 286 
LEU HG     H N N 287 
LEU HD11   H N N 288 
LEU HD12   H N N 289 
LEU HD13   H N N 290 
LEU HD21   H N N 291 
LEU HD22   H N N 292 
LEU HD23   H N N 293 
LEU HXT    H N N 294 
LYS N      N N N 295 
LYS CA     C N S 296 
LYS C      C N N 297 
LYS O      O N N 298 
LYS CB     C N N 299 
LYS CG     C N N 300 
LYS CD     C N N 301 
LYS CE     C N N 302 
LYS NZ     N N N 303 
LYS OXT    O N N 304 
LYS H      H N N 305 
LYS H2     H N N 306 
LYS HA     H N N 307 
LYS HB2    H N N 308 
LYS HB3    H N N 309 
LYS HG2    H N N 310 
LYS HG3    H N N 311 
LYS HD2    H N N 312 
LYS HD3    H N N 313 
LYS HE2    H N N 314 
LYS HE3    H N N 315 
LYS HZ1    H N N 316 
LYS HZ2    H N N 317 
LYS HZ3    H N N 318 
LYS HXT    H N N 319 
MET N      N N N 320 
MET CA     C N S 321 
MET C      C N N 322 
MET O      O N N 323 
MET CB     C N N 324 
MET CG     C N N 325 
MET SD     S N N 326 
MET CE     C N N 327 
MET OXT    O N N 328 
MET H      H N N 329 
MET H2     H N N 330 
MET HA     H N N 331 
MET HB2    H N N 332 
MET HB3    H N N 333 
MET HG2    H N N 334 
MET HG3    H N N 335 
MET HE1    H N N 336 
MET HE2    H N N 337 
MET HE3    H N N 338 
MET HXT    H N N 339 
MPD C1     C N N 340 
MPD C2     C N N 341 
MPD O2     O N N 342 
MPD CM     C N N 343 
MPD C3     C N N 344 
MPD C4     C N S 345 
MPD O4     O N N 346 
MPD C5     C N N 347 
MPD H11    H N N 348 
MPD H12    H N N 349 
MPD H13    H N N 350 
MPD HO2    H N N 351 
MPD HM1    H N N 352 
MPD HM2    H N N 353 
MPD HM3    H N N 354 
MPD H31    H N N 355 
MPD H32    H N N 356 
MPD H4     H N N 357 
MPD HO4    H N N 358 
MPD H51    H N N 359 
MPD H52    H N N 360 
MPD H53    H N N 361 
PHE N      N N N 362 
PHE CA     C N S 363 
PHE C      C N N 364 
PHE O      O N N 365 
PHE CB     C N N 366 
PHE CG     C Y N 367 
PHE CD1    C Y N 368 
PHE CD2    C Y N 369 
PHE CE1    C Y N 370 
PHE CE2    C Y N 371 
PHE CZ     C Y N 372 
PHE OXT    O N N 373 
PHE H      H N N 374 
PHE H2     H N N 375 
PHE HA     H N N 376 
PHE HB2    H N N 377 
PHE HB3    H N N 378 
PHE HD1    H N N 379 
PHE HD2    H N N 380 
PHE HE1    H N N 381 
PHE HE2    H N N 382 
PHE HZ     H N N 383 
PHE HXT    H N N 384 
PRO N      N N N 385 
PRO CA     C N S 386 
PRO C      C N N 387 
PRO O      O N N 388 
PRO CB     C N N 389 
PRO CG     C N N 390 
PRO CD     C N N 391 
PRO OXT    O N N 392 
PRO H      H N N 393 
PRO HA     H N N 394 
PRO HB2    H N N 395 
PRO HB3    H N N 396 
PRO HG2    H N N 397 
PRO HG3    H N N 398 
PRO HD2    H N N 399 
PRO HD3    H N N 400 
PRO HXT    H N N 401 
SER N      N N N 402 
SER CA     C N S 403 
SER C      C N N 404 
SER O      O N N 405 
SER CB     C N N 406 
SER OG     O N N 407 
SER OXT    O N N 408 
SER H      H N N 409 
SER H2     H N N 410 
SER HA     H N N 411 
SER HB2    H N N 412 
SER HB3    H N N 413 
SER HG     H N N 414 
SER HXT    H N N 415 
SO4 S      S N N 416 
SO4 O1     O N N 417 
SO4 O2     O N N 418 
SO4 O3     O N N 419 
SO4 O4     O N N 420 
THR N      N N N 421 
THR CA     C N S 422 
THR C      C N N 423 
THR O      O N N 424 
THR CB     C N R 425 
THR OG1    O N N 426 
THR CG2    C N N 427 
THR OXT    O N N 428 
THR H      H N N 429 
THR H2     H N N 430 
THR HA     H N N 431 
THR HB     H N N 432 
THR HG1    H N N 433 
THR HG21   H N N 434 
THR HG22   H N N 435 
THR HG23   H N N 436 
THR HXT    H N N 437 
TRP N      N N N 438 
TRP CA     C N S 439 
TRP C      C N N 440 
TRP O      O N N 441 
TRP CB     C N N 442 
TRP CG     C Y N 443 
TRP CD1    C Y N 444 
TRP CD2    C Y N 445 
TRP NE1    N Y N 446 
TRP CE2    C Y N 447 
TRP CE3    C Y N 448 
TRP CZ2    C Y N 449 
TRP CZ3    C Y N 450 
TRP CH2    C Y N 451 
TRP OXT    O N N 452 
TRP H      H N N 453 
TRP H2     H N N 454 
TRP HA     H N N 455 
TRP HB2    H N N 456 
TRP HB3    H N N 457 
TRP HD1    H N N 458 
TRP HE1    H N N 459 
TRP HE3    H N N 460 
TRP HZ2    H N N 461 
TRP HZ3    H N N 462 
TRP HH2    H N N 463 
TRP HXT    H N N 464 
TYR N      N N N 465 
TYR CA     C N S 466 
TYR C      C N N 467 
TYR O      O N N 468 
TYR CB     C N N 469 
TYR CG     C Y N 470 
TYR CD1    C Y N 471 
TYR CD2    C Y N 472 
TYR CE1    C Y N 473 
TYR CE2    C Y N 474 
TYR CZ     C Y N 475 
TYR OH     O N N 476 
TYR OXT    O N N 477 
TYR H      H N N 478 
TYR H2     H N N 479 
TYR HA     H N N 480 
TYR HB2    H N N 481 
TYR HB3    H N N 482 
TYR HD1    H N N 483 
TYR HD2    H N N 484 
TYR HE1    H N N 485 
TYR HE2    H N N 486 
TYR HH     H N N 487 
TYR HXT    H N N 488 
VAL N      N N N 489 
VAL CA     C N S 490 
VAL C      C N N 491 
VAL O      O N N 492 
VAL CB     C N N 493 
VAL CG1    C N N 494 
VAL CG2    C N N 495 
VAL OXT    O N N 496 
VAL H      H N N 497 
VAL H2     H N N 498 
VAL HA     H N N 499 
VAL HB     H N N 500 
VAL HG11   H N N 501 
VAL HG12   H N N 502 
VAL HG13   H N N 503 
VAL HG21   H N N 504 
VAL HG22   H N N 505 
VAL HG23   H N N 506 
VAL HXT    H N N 507 
# 
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 
1PE OH2   C12    sing N N 1   
1PE OH2   HO2    sing N N 2   
1PE C12   C22    sing N N 3   
1PE C12   H121   sing N N 4   
1PE C12   H122   sing N N 5   
1PE C22   OH3    sing N N 6   
1PE C22   H221   sing N N 7   
1PE C22   H222   sing N N 8   
1PE OH3   C23    sing N N 9   
1PE C13   C23    sing N N 10  
1PE C13   OH4    sing N N 11  
1PE C13   H131   sing N N 12  
1PE C13   H132   sing N N 13  
1PE C23   H231   sing N N 14  
1PE C23   H232   sing N N 15  
1PE OH4   C24    sing N N 16  
1PE C14   C24    sing N N 17  
1PE C14   OH5    sing N N 18  
1PE C14   H141   sing N N 19  
1PE C14   H142   sing N N 20  
1PE C24   H241   sing N N 21  
1PE C24   H242   sing N N 22  
1PE OH5   C25    sing N N 23  
1PE C15   C25    sing N N 24  
1PE C15   OH6    sing N N 25  
1PE C15   H151   sing N N 26  
1PE C15   H152   sing N N 27  
1PE C25   H251   sing N N 28  
1PE C25   H252   sing N N 29  
1PE OH6   C26    sing N N 30  
1PE C16   C26    sing N N 31  
1PE C16   OH7    sing N N 32  
1PE C16   H161   sing N N 33  
1PE C16   H162   sing N N 34  
1PE C26   H261   sing N N 35  
1PE C26   H262   sing N N 36  
1PE OH7   HO7    sing N N 37  
ALA N     CA     sing N N 38  
ALA N     H      sing N N 39  
ALA N     H2     sing N N 40  
ALA CA    C      sing N N 41  
ALA CA    CB     sing N N 42  
ALA CA    HA     sing N N 43  
ALA C     O      doub N N 44  
ALA C     OXT    sing N N 45  
ALA CB    HB1    sing N N 46  
ALA CB    HB2    sing N N 47  
ALA CB    HB3    sing N N 48  
ALA OXT   HXT    sing N N 49  
ARG N     CA     sing N N 50  
ARG N     H      sing N N 51  
ARG N     H2     sing N N 52  
ARG CA    C      sing N N 53  
ARG CA    CB     sing N N 54  
ARG CA    HA     sing N N 55  
ARG C     O      doub N N 56  
ARG C     OXT    sing N N 57  
ARG CB    CG     sing N N 58  
ARG CB    HB2    sing N N 59  
ARG CB    HB3    sing N N 60  
ARG CG    CD     sing N N 61  
ARG CG    HG2    sing N N 62  
ARG CG    HG3    sing N N 63  
ARG CD    NE     sing N N 64  
ARG CD    HD2    sing N N 65  
ARG CD    HD3    sing N N 66  
ARG NE    CZ     sing N N 67  
ARG NE    HE     sing N N 68  
ARG CZ    NH1    sing N N 69  
ARG CZ    NH2    doub N N 70  
ARG NH1   HH11   sing N N 71  
ARG NH1   HH12   sing N N 72  
ARG NH2   HH21   sing N N 73  
ARG NH2   HH22   sing N N 74  
ARG OXT   HXT    sing N N 75  
ASN N     CA     sing N N 76  
ASN N     H      sing N N 77  
ASN N     H2     sing N N 78  
ASN CA    C      sing N N 79  
ASN CA    CB     sing N N 80  
ASN CA    HA     sing N N 81  
ASN C     O      doub N N 82  
ASN C     OXT    sing N N 83  
ASN CB    CG     sing N N 84  
ASN CB    HB2    sing N N 85  
ASN CB    HB3    sing N N 86  
ASN CG    OD1    doub N N 87  
ASN CG    ND2    sing N N 88  
ASN ND2   HD21   sing N N 89  
ASN ND2   HD22   sing N N 90  
ASN OXT   HXT    sing N N 91  
ASP N     CA     sing N N 92  
ASP N     H      sing N N 93  
ASP N     H2     sing N N 94  
ASP CA    C      sing N N 95  
ASP CA    CB     sing N N 96  
ASP CA    HA     sing N N 97  
ASP C     O      doub N N 98  
ASP C     OXT    sing N N 99  
ASP CB    CG     sing N N 100 
ASP CB    HB2    sing N N 101 
ASP CB    HB3    sing N N 102 
ASP CG    OD1    doub N N 103 
ASP CG    OD2    sing N N 104 
ASP OD2   HD2    sing N N 105 
ASP OXT   HXT    sing N N 106 
CYS N     CA     sing N N 107 
CYS N     H      sing N N 108 
CYS N     H2     sing N N 109 
CYS CA    C      sing N N 110 
CYS CA    CB     sing N N 111 
CYS CA    HA     sing N N 112 
CYS C     O      doub N N 113 
CYS C     OXT    sing N N 114 
CYS CB    SG     sing N N 115 
CYS CB    HB2    sing N N 116 
CYS CB    HB3    sing N N 117 
CYS SG    HG     sing N N 118 
CYS OXT   HXT    sing N N 119 
FMN N1    C2     sing N N 120 
FMN N1    C10    doub N N 121 
FMN C2    O2     doub N N 122 
FMN C2    N3     sing N N 123 
FMN N3    C4     sing N N 124 
FMN N3    HN3    sing N N 125 
FMN C4    O4     doub N N 126 
FMN C4    C4A    sing N N 127 
FMN C4A   N5     doub N N 128 
FMN C4A   C10    sing N N 129 
FMN N5    C5A    sing N N 130 
FMN C5A   C6     doub Y N 131 
FMN C5A   C9A    sing Y N 132 
FMN C6    C7     sing Y N 133 
FMN C6    H6     sing N N 134 
FMN C7    C7M    sing N N 135 
FMN C7    C8     doub Y N 136 
FMN C7M   HM71   sing N N 137 
FMN C7M   HM72   sing N N 138 
FMN C7M   HM73   sing N N 139 
FMN C8    C8M    sing N N 140 
FMN C8    C9     sing Y N 141 
FMN C8M   HM81   sing N N 142 
FMN C8M   HM82   sing N N 143 
FMN C8M   HM83   sing N N 144 
FMN C9    C9A    doub Y N 145 
FMN C9    H9     sing N N 146 
FMN C9A   N10    sing N N 147 
FMN N10   C10    sing N N 148 
FMN N10   "C1'"  sing N N 149 
FMN "C1'" "C2'"  sing N N 150 
FMN "C1'" "H1'1" sing N N 151 
FMN "C1'" "H1'2" sing N N 152 
FMN "C2'" "O2'"  sing N N 153 
FMN "C2'" "C3'"  sing N N 154 
FMN "C2'" "H2'"  sing N N 155 
FMN "O2'" "HO2'" sing N N 156 
FMN "C3'" "O3'"  sing N N 157 
FMN "C3'" "C4'"  sing N N 158 
FMN "C3'" "H3'"  sing N N 159 
FMN "O3'" "HO3'" sing N N 160 
FMN "C4'" "O4'"  sing N N 161 
FMN "C4'" "C5'"  sing N N 162 
FMN "C4'" "H4'"  sing N N 163 
FMN "O4'" "HO4'" sing N N 164 
FMN "C5'" "O5'"  sing N N 165 
FMN "C5'" "H5'1" sing N N 166 
FMN "C5'" "H5'2" sing N N 167 
FMN "O5'" P      sing N N 168 
FMN P     O1P    doub N N 169 
FMN P     O2P    sing N N 170 
FMN P     O3P    sing N N 171 
FMN O2P   HOP2   sing N N 172 
FMN O3P   HOP3   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
MPD C1    C2     sing N N 328 
MPD C1    H11    sing N N 329 
MPD C1    H12    sing N N 330 
MPD C1    H13    sing N N 331 
MPD C2    O2     sing N N 332 
MPD C2    CM     sing N N 333 
MPD C2    C3     sing N N 334 
MPD O2    HO2    sing N N 335 
MPD CM    HM1    sing N N 336 
MPD CM    HM2    sing N N 337 
MPD CM    HM3    sing N N 338 
MPD C3    C4     sing N N 339 
MPD C3    H31    sing N N 340 
MPD C3    H32    sing N N 341 
MPD C4    O4     sing N N 342 
MPD C4    C5     sing N N 343 
MPD C4    H4     sing N N 344 
MPD O4    HO4    sing N N 345 
MPD C5    H51    sing N N 346 
MPD C5    H52    sing N N 347 
MPD C5    H53    sing N N 348 
PHE N     CA     sing N N 349 
PHE N     H      sing N N 350 
PHE N     H2     sing N N 351 
PHE CA    C      sing N N 352 
PHE CA    CB     sing N N 353 
PHE CA    HA     sing N N 354 
PHE C     O      doub N N 355 
PHE C     OXT    sing N N 356 
PHE CB    CG     sing N N 357 
PHE CB    HB2    sing N N 358 
PHE CB    HB3    sing N N 359 
PHE CG    CD1    doub Y N 360 
PHE CG    CD2    sing Y N 361 
PHE CD1   CE1    sing Y N 362 
PHE CD1   HD1    sing N N 363 
PHE CD2   CE2    doub Y N 364 
PHE CD2   HD2    sing N N 365 
PHE CE1   CZ     doub Y N 366 
PHE CE1   HE1    sing N N 367 
PHE CE2   CZ     sing Y N 368 
PHE CE2   HE2    sing N N 369 
PHE CZ    HZ     sing N N 370 
PHE OXT   HXT    sing N N 371 
PRO N     CA     sing N N 372 
PRO N     CD     sing N N 373 
PRO N     H      sing N N 374 
PRO CA    C      sing N N 375 
PRO CA    CB     sing N N 376 
PRO CA    HA     sing N N 377 
PRO C     O      doub N N 378 
PRO C     OXT    sing N N 379 
PRO CB    CG     sing N N 380 
PRO CB    HB2    sing N N 381 
PRO CB    HB3    sing N N 382 
PRO CG    CD     sing N N 383 
PRO CG    HG2    sing N N 384 
PRO CG    HG3    sing N N 385 
PRO CD    HD2    sing N N 386 
PRO CD    HD3    sing N N 387 
PRO OXT   HXT    sing N N 388 
SER N     CA     sing N N 389 
SER N     H      sing N N 390 
SER N     H2     sing N N 391 
SER CA    C      sing N N 392 
SER CA    CB     sing N N 393 
SER CA    HA     sing N N 394 
SER C     O      doub N N 395 
SER C     OXT    sing N N 396 
SER CB    OG     sing N N 397 
SER CB    HB2    sing N N 398 
SER CB    HB3    sing N N 399 
SER OG    HG     sing N N 400 
SER OXT   HXT    sing N N 401 
SO4 S     O1     doub N N 402 
SO4 S     O2     doub N N 403 
SO4 S     O3     sing N N 404 
SO4 S     O4     sing N N 405 
THR N     CA     sing N N 406 
THR N     H      sing N N 407 
THR N     H2     sing N N 408 
THR CA    C      sing N N 409 
THR CA    CB     sing N N 410 
THR CA    HA     sing N N 411 
THR C     O      doub N N 412 
THR C     OXT    sing N N 413 
THR CB    OG1    sing N N 414 
THR CB    CG2    sing N N 415 
THR CB    HB     sing N N 416 
THR OG1   HG1    sing N N 417 
THR CG2   HG21   sing N N 418 
THR CG2   HG22   sing N N 419 
THR CG2   HG23   sing N N 420 
THR OXT   HXT    sing N N 421 
TRP N     CA     sing N N 422 
TRP N     H      sing N N 423 
TRP N     H2     sing N N 424 
TRP CA    C      sing N N 425 
TRP CA    CB     sing N N 426 
TRP CA    HA     sing N N 427 
TRP C     O      doub N N 428 
TRP C     OXT    sing N N 429 
TRP CB    CG     sing N N 430 
TRP CB    HB2    sing N N 431 
TRP CB    HB3    sing N N 432 
TRP CG    CD1    doub Y N 433 
TRP CG    CD2    sing Y N 434 
TRP CD1   NE1    sing Y N 435 
TRP CD1   HD1    sing N N 436 
TRP CD2   CE2    doub Y N 437 
TRP CD2   CE3    sing Y N 438 
TRP NE1   CE2    sing Y N 439 
TRP NE1   HE1    sing N N 440 
TRP CE2   CZ2    sing Y N 441 
TRP CE3   CZ3    doub Y N 442 
TRP CE3   HE3    sing N N 443 
TRP CZ2   CH2    doub Y N 444 
TRP CZ2   HZ2    sing N N 445 
TRP CZ3   CH2    sing Y N 446 
TRP CZ3   HZ3    sing N N 447 
TRP CH2   HH2    sing N N 448 
TRP OXT   HXT    sing N N 449 
TYR N     CA     sing N N 450 
TYR N     H      sing N N 451 
TYR N     H2     sing N N 452 
TYR CA    C      sing N N 453 
TYR CA    CB     sing N N 454 
TYR CA    HA     sing N N 455 
TYR C     O      doub N N 456 
TYR C     OXT    sing N N 457 
TYR CB    CG     sing N N 458 
TYR CB    HB2    sing N N 459 
TYR CB    HB3    sing N N 460 
TYR CG    CD1    doub Y N 461 
TYR CG    CD2    sing Y N 462 
TYR CD1   CE1    sing Y N 463 
TYR CD1   HD1    sing N N 464 
TYR CD2   CE2    doub Y N 465 
TYR CD2   HD2    sing N N 466 
TYR CE1   CZ     doub Y N 467 
TYR CE1   HE1    sing N N 468 
TYR CE2   CZ     sing Y N 469 
TYR CE2   HE2    sing N N 470 
TYR CZ    OH     sing N N 471 
TYR OH    HH     sing N N 472 
TYR OXT   HXT    sing N N 473 
VAL N     CA     sing N N 474 
VAL N     H      sing N N 475 
VAL N     H2     sing N N 476 
VAL CA    C      sing N N 477 
VAL CA    CB     sing N N 478 
VAL CA    HA     sing N N 479 
VAL C     O      doub N N 480 
VAL C     OXT    sing N N 481 
VAL CB    CG1    sing N N 482 
VAL CB    CG2    sing N N 483 
VAL CB    HB     sing N N 484 
VAL CG1   HG11   sing N N 485 
VAL CG1   HG12   sing N N 486 
VAL CG1   HG13   sing N N 487 
VAL CG2   HG21   sing N N 488 
VAL CG2   HG22   sing N N 489 
VAL CG2   HG23   sing N N 490 
VAL OXT   HXT    sing N N 491 
# 
_pdbx_audit_support.funding_organization   'Austrian Science Fund' 
_pdbx_audit_support.country                Austria 
_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   2hs6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QNE 
_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]   0.011447 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011099 
_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]   0.020247 
_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 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ASN A 1 19  ? 36.609 9.916  0.738  1.00 36.89 ? 10  ASN A N     1 
ATOM   2    C CA    . ASN A 1 19  ? 36.204 10.495 2.029  1.00 30.18 ? 10  ASN A CA    1 
ATOM   3    C C     . ASN A 1 19  ? 34.747 10.119 2.313  1.00 25.82 ? 10  ASN A C     1 
ATOM   4    O O     . ASN A 1 19  ? 33.844 10.560 1.604  1.00 27.32 ? 10  ASN A O     1 
ATOM   5    C CB    . ASN A 1 19  ? 36.350 12.012 1.967  1.00 28.95 ? 10  ASN A CB    1 
ATOM   6    C CG    . ASN A 1 19  ? 36.125 12.679 3.318  1.00 26.58 ? 10  ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 19  ? 35.423 12.142 4.173  1.00 30.21 ? 10  ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 19  ? 36.718 13.830 3.512  1.00 31.74 ? 10  ASN A ND2   1 
ATOM   9    N N     . PRO A 1 20  ? 34.503 9.254  3.310  1.00 27.84 ? 11  PRO A N     1 
ATOM   10   C CA    . PRO A 1 20  ? 33.126 8.820  3.562  1.00 26.36 ? 11  PRO A CA    1 
ATOM   11   C C     . PRO A 1 20  ? 32.241 9.921  4.104  1.00 23.25 ? 11  PRO A C     1 
ATOM   12   O O     . PRO A 1 20  ? 31.021 9.755  4.058  1.00 24.22 ? 11  PRO A O     1 
ATOM   13   C CB    . PRO A 1 20  ? 33.284 7.709  4.613  1.00 28.09 ? 11  PRO A CB    1 
ATOM   14   C CG    . PRO A 1 20  ? 34.500 8.091  5.345  1.00 26.69 ? 11  PRO A CG    1 
ATOM   15   C CD    . PRO A 1 20  ? 35.442 8.718  4.311  1.00 31.60 ? 11  PRO A CD    1 
ATOM   16   N N     . LEU A 1 21  ? 32.799 11.040 4.581  1.00 24.45 ? 12  LEU A N     1 
ATOM   17   C CA    . LEU A 1 21  ? 31.903 12.135 4.923  1.00 23.63 ? 12  LEU A CA    1 
ATOM   18   C C     . LEU A 1 21  ? 31.200 12.691 3.710  1.00 24.63 ? 12  LEU A C     1 
ATOM   19   O O     . LEU A 1 21  ? 30.251 13.453 3.873  1.00 22.99 ? 12  LEU A O     1 
ATOM   20   C CB    . LEU A 1 21  ? 32.656 13.274 5.578  1.00 23.44 ? 12  LEU A CB    1 
ATOM   21   C CG    . LEU A 1 21  ? 33.118 12.908 6.970  1.00 22.95 ? 12  LEU A CG    1 
ATOM   22   C CD1   . LEU A 1 21  ? 34.020 13.999 7.460  1.00 26.02 ? 12  LEU A CD1   1 
ATOM   23   C CD2   . LEU A 1 21  ? 31.858 12.725 7.854  1.00 25.21 ? 12  LEU A CD2   1 
ATOM   24   N N     . PHE A 1 22  ? 31.651 12.374 2.494  1.00 22.54 ? 13  PHE A N     1 
ATOM   25   C CA    . PHE A 1 22  ? 31.033 12.896 1.278  1.00 22.07 ? 13  PHE A CA    1 
ATOM   26   C C     . PHE A 1 22  ? 30.254 11.830 0.544  1.00 27.27 ? 13  PHE A C     1 
ATOM   27   O O     . PHE A 1 22  ? 29.922 11.992 -0.630 1.00 28.45 ? 13  PHE A O     1 
ATOM   28   C CB    . PHE A 1 22  ? 32.027 13.692 0.396  1.00 21.34 ? 13  PHE A CB    1 
ATOM   29   C CG    . PHE A 1 22  ? 32.426 14.947 1.057  1.00 24.13 ? 13  PHE A CG    1 
ATOM   30   C CD1   . PHE A 1 22  ? 33.448 14.943 1.966  1.00 26.62 ? 13  PHE A CD1   1 
ATOM   31   C CD2   . PHE A 1 22  ? 31.641 16.074 0.936  1.00 27.35 ? 13  PHE A CD2   1 
ATOM   32   C CE1   . PHE A 1 22  ? 33.753 16.088 2.704  1.00 27.29 ? 13  PHE A CE1   1 
ATOM   33   C CE2   . PHE A 1 22  ? 31.930 17.230 1.674  1.00 27.11 ? 13  PHE A CE2   1 
ATOM   34   C CZ    . PHE A 1 22  ? 33.003 17.222 2.563  1.00 27.02 ? 13  PHE A CZ    1 
ATOM   35   N N     A SER A 1 23  ? 29.848 10.796 1.283  0.50 26.15 ? 14  SER A N     1 
ATOM   36   N N     B SER A 1 23  ? 29.847 10.798 1.283  0.50 26.21 ? 14  SER A N     1 
ATOM   37   C CA    A SER A 1 23  ? 28.998 9.748  0.679  0.50 26.27 ? 14  SER A CA    1 
ATOM   38   C CA    B SER A 1 23  ? 29.001 9.745  0.685  0.50 26.40 ? 14  SER A CA    1 
ATOM   39   C C     A SER A 1 23  ? 27.556 10.144 0.990  0.50 28.06 ? 14  SER A C     1 
ATOM   40   C C     B SER A 1 23  ? 27.557 10.146 0.990  0.50 27.73 ? 14  SER A C     1 
ATOM   41   O O     A SER A 1 23  ? 27.342 10.724 2.067  0.50 25.02 ? 14  SER A O     1 
ATOM   42   O O     B SER A 1 23  ? 27.340 10.722 2.068  0.50 26.39 ? 14  SER A O     1 
ATOM   43   C CB    A SER A 1 23  ? 29.308 8.392  1.245  0.50 30.52 ? 14  SER A CB    1 
ATOM   44   C CB    B SER A 1 23  ? 29.316 8.408  1.293  0.50 27.48 ? 14  SER A CB    1 
ATOM   45   O OG    A SER A 1 23  ? 29.040 8.354  2.634  0.50 28.20 ? 14  SER A OG    1 
ATOM   46   O OG    B SER A 1 23  ? 28.140 7.637  1.469  0.50 26.76 ? 14  SER A OG    1 
ATOM   47   N N     . PRO A 1 24  ? 26.684 10.242 -0.032 1.00 22.54 ? 15  PRO A N     1 
ATOM   48   C CA    . PRO A 1 24  ? 25.323 10.659 0.202  1.00 25.99 ? 15  PRO A CA    1 
ATOM   49   C C     . PRO A 1 24  ? 24.591 9.822  1.262  1.00 24.41 ? 15  PRO A C     1 
ATOM   50   O O     . PRO A 1 24  ? 24.910 8.686  1.461  1.00 25.42 ? 15  PRO A O     1 
ATOM   51   C CB    . PRO A 1 24  ? 24.686 10.500 -1.181 1.00 31.69 ? 15  PRO A CB    1 
ATOM   52   C CG    . PRO A 1 24  ? 25.540 9.466  -1.868 1.00 38.33 ? 15  PRO A CG    1 
ATOM   53   C CD    . PRO A 1 24  ? 26.941 9.759  -1.385 1.00 32.13 ? 15  PRO A CD    1 
ATOM   54   N N     . TYR A 1 25  ? 23.621 10.451 1.915  1.00 23.88 ? 16  TYR A N     1 
ATOM   55   C CA    . TYR A 1 25  ? 22.859 9.763  2.977  1.00 21.98 ? 16  TYR A CA    1 
ATOM   56   C C     . TYR A 1 25  ? 21.386 10.158 2.910  1.00 22.64 ? 16  TYR A C     1 
ATOM   57   O O     . TYR A 1 25  ? 21.093 11.336 2.791  1.00 23.96 ? 16  TYR A O     1 
ATOM   58   C CB    . TYR A 1 25  ? 23.409 10.095 4.367  1.00 24.24 ? 16  TYR A CB    1 
ATOM   59   C CG    . TYR A 1 25  ? 22.766 9.262  5.440  1.00 21.44 ? 16  TYR A CG    1 
ATOM   60   C CD1   . TYR A 1 25  ? 23.098 7.929  5.588  1.00 21.96 ? 16  TYR A CD1   1 
ATOM   61   C CD2   . TYR A 1 25  ? 21.783 9.786  6.257  1.00 22.51 ? 16  TYR A CD2   1 
ATOM   62   C CE1   . TYR A 1 25  ? 22.494 7.140  6.548  1.00 22.27 ? 16  TYR A CE1   1 
ATOM   63   C CE2   . TYR A 1 25  ? 21.165 9.010  7.219  1.00 22.79 ? 16  TYR A CE2   1 
ATOM   64   C CZ    . TYR A 1 25  ? 21.521 7.682  7.363  1.00 21.05 ? 16  TYR A CZ    1 
ATOM   65   O OH    . TYR A 1 25  ? 20.922 6.907  8.314  1.00 23.62 ? 16  TYR A OH    1 
ATOM   66   N N     . LYS A 1 26  ? 20.503 9.172  3.018  1.00 21.68 ? 17  LYS A N     1 
ATOM   67   C CA    . LYS A 1 26  ? 19.050 9.443  3.037  1.00 22.69 ? 17  LYS A CA    1 
ATOM   68   C C     . LYS A 1 26  ? 18.562 9.550  4.482  1.00 26.07 ? 17  LYS A C     1 
ATOM   69   O O     . LYS A 1 26  ? 18.424 8.518  5.118  1.00 28.48 ? 17  LYS A O     1 
ATOM   70   C CB    . LYS A 1 26  ? 18.283 8.336  2.316  1.00 28.00 ? 17  LYS A CB    1 
ATOM   71   C CG    . LYS A 1 26  ? 16.846 8.695  1.973  1.00 36.81 ? 17  LYS A CG    1 
ATOM   72   C CD    . LYS A 1 26  ? 16.271 7.908  0.820  1.00 52.20 ? 17  LYS A CD    1 
ATOM   73   C CE    . LYS A 1 26  ? 14.992 8.515  0.283  1.00 49.72 ? 17  LYS A CE    1 
ATOM   74   N NZ    . LYS A 1 26  ? 14.913 9.969  0.553  1.00 50.71 ? 17  LYS A NZ    1 
ATOM   75   N N     . MET A 1 27  ? 18.313 10.683 4.876  1.00 23.29 ? 18  MET A N     1 
ATOM   76   C CA    . MET A 1 27  ? 17.829 10.912 6.253  1.00 23.84 ? 18  MET A CA    1 
ATOM   77   C C     . MET A 1 27  ? 16.314 11.058 6.161  1.00 27.92 ? 18  MET A C     1 
ATOM   78   O O     . MET A 1 27  ? 15.825 12.180 6.184  1.00 29.48 ? 18  MET A O     1 
ATOM   79   C CB    . MET A 1 27  ? 18.471 12.150 6.882  1.00 24.42 ? 18  MET A CB    1 
ATOM   80   C CG    . MET A 1 27  ? 17.847 12.572 8.203  1.00 27.32 ? 18  MET A CG    1 
ATOM   81   S SD    . MET A 1 27  ? 18.682 13.986 8.946  1.00 27.82 ? 18  MET A SD    1 
ATOM   82   C CE    . MET A 1 27  ? 17.824 15.342 8.150  1.00 26.08 ? 18  MET A CE    1 
ATOM   83   N N     . GLY A 1 28  ? 15.687 9.884  5.969  1.00 28.70 ? 19  GLY A N     1 
ATOM   84   C CA    . GLY A 1 28  ? 14.236 9.814  5.779  1.00 31.90 ? 19  GLY A CA    1 
ATOM   85   C C     . GLY A 1 28  ? 13.877 10.401 4.441  1.00 38.58 ? 19  GLY A C     1 
ATOM   86   O O     . GLY A 1 28  ? 14.355 9.913  3.430  1.00 35.16 ? 19  GLY A O     1 
ATOM   87   N N     . LYS A 1 29  ? 13.103 11.465 4.470  1.00 39.30 ? 20  LYS A N     1 
ATOM   88   C CA    . LYS A 1 29  ? 12.673 12.070 3.197  1.00 32.82 ? 20  LYS A CA    1 
ATOM   89   C C     . LYS A 1 29  ? 13.755 13.012 2.681  1.00 33.90 ? 20  LYS A C     1 
ATOM   90   O O     . LYS A 1 29  ? 13.597 13.506 1.574  1.00 33.79 ? 20  LYS A O     1 
ATOM   91   C CB    . LYS A 1 29  ? 11.360 12.827 3.388  1.00 49.66 ? 20  LYS A CB    1 
ATOM   92   C CG    . LYS A 1 29  ? 11.353 13.902 4.460  1.00 48.55 ? 20  LYS A CG    1 
ATOM   93   C CD    . LYS A 1 29  ? 10.158 14.816 4.334  1.00 46.37 ? 20  LYS A CD    1 
ATOM   94   C CE    . LYS A 1 29  ? 9.019  14.171 3.576  1.00 62.30 ? 20  LYS A CE    1 
ATOM   95   N NZ    . LYS A 1 29  ? 8.293  15.142 2.724  1.00 67.72 ? 20  LYS A NZ    1 
ATOM   96   N N     . PHE A 1 30  ? 14.826 13.202 3.441  1.00 24.13 ? 21  PHE A N     1 
ATOM   97   C CA    . PHE A 1 30  ? 15.787 14.206 3.027  1.00 21.70 ? 21  PHE A CA    1 
ATOM   98   C C     . PHE A 1 30  ? 17.004 13.539 2.422  1.00 23.29 ? 21  PHE A C     1 
ATOM   99   O O     . PHE A 1 30  ? 17.661 12.722 3.065  1.00 27.26 ? 21  PHE A O     1 
ATOM   100  C CB    . PHE A 1 30  ? 16.192 15.073 4.230  1.00 24.67 ? 21  PHE A CB    1 
ATOM   101  C CG    . PHE A 1 30  ? 15.029 15.677 4.925  1.00 22.88 ? 21  PHE A CG    1 
ATOM   102  C CD1   . PHE A 1 30  ? 14.325 16.692 4.317  1.00 22.08 ? 21  PHE A CD1   1 
ATOM   103  C CD2   . PHE A 1 30  ? 14.578 15.199 6.153  1.00 27.43 ? 21  PHE A CD2   1 
ATOM   104  C CE1   . PHE A 1 30  ? 13.197 17.250 4.920  1.00 24.24 ? 21  PHE A CE1   1 
ATOM   105  C CE2   . PHE A 1 30  ? 13.471 15.770 6.760  1.00 25.99 ? 21  PHE A CE2   1 
ATOM   106  C CZ    . PHE A 1 30  ? 12.784 16.768 6.155  1.00 28.25 ? 21  PHE A CZ    1 
ATOM   107  N N     . ASN A 1 31  ? 17.326 13.911 1.200  1.00 21.95 ? 22  ASN A N     1 
ATOM   108  C CA    . ASN A 1 31  ? 18.507 13.368 0.540  1.00 21.64 ? 22  ASN A CA    1 
ATOM   109  C C     . ASN A 1 31  ? 19.694 14.283 0.795  1.00 23.81 ? 22  ASN A C     1 
ATOM   110  O O     . ASN A 1 31  ? 19.792 15.362 0.206  1.00 29.28 ? 22  ASN A O     1 
ATOM   111  C CB    . ASN A 1 31  ? 18.243 13.266 -0.958 1.00 23.77 ? 22  ASN A CB    1 
ATOM   112  C CG    . ASN A 1 31  ? 17.031 12.389 -1.238 1.00 30.55 ? 22  ASN A CG    1 
ATOM   113  O OD1   . ASN A 1 31  ? 17.100 11.170 -1.027 1.00 32.84 ? 22  ASN A OD1   1 
ATOM   114  N ND2   . ASN A 1 31  ? 15.929 12.994 -1.754 1.00 30.65 ? 22  ASN A ND2   1 
ATOM   115  N N     . LEU A 1 32  ? 20.589 13.876 1.700  1.00 20.42 ? 23  LEU A N     1 
ATOM   116  C CA    . LEU A 1 32  ? 21.765 14.677 2.017  1.00 22.08 ? 23  LEU A CA    1 
ATOM   117  C C     . LEU A 1 32  ? 22.934 14.324 1.114  1.00 20.54 ? 23  LEU A C     1 
ATOM   118  O O     . LEU A 1 32  ? 23.125 13.167 0.765  1.00 22.19 ? 23  LEU A O     1 
ATOM   119  C CB    . LEU A 1 32  ? 22.174 14.461 3.476  1.00 20.52 ? 23  LEU A CB    1 
ATOM   120  C CG    . LEU A 1 32  ? 21.095 14.804 4.503  1.00 20.00 ? 23  LEU A CG    1 
ATOM   121  C CD1   . LEU A 1 32  ? 21.606 14.553 5.990  1.00 21.60 ? 23  LEU A CD1   1 
ATOM   122  C CD2   . LEU A 1 32  ? 20.610 16.232 4.315  1.00 22.96 ? 23  LEU A CD2   1 
ATOM   123  N N     A SER A 1 33  ? 23.730 15.326 0.736  0.50 21.36 ? 24  SER A N     1 
ATOM   124  N N     B SER A 1 33  ? 23.724 15.342 0.748  0.50 21.35 ? 24  SER A N     1 
ATOM   125  C CA    A SER A 1 33  ? 24.869 15.028 -0.129 0.50 22.12 ? 24  SER A CA    1 
ATOM   126  C CA    B SER A 1 33  ? 24.876 15.161 -0.135 0.50 21.75 ? 24  SER A CA    1 
ATOM   127  C C     A SER A 1 33  ? 26.126 14.693 0.642  0.50 22.96 ? 24  SER A C     1 
ATOM   128  C C     B SER A 1 33  ? 26.168 14.878 0.612  0.50 22.56 ? 24  SER A C     1 
ATOM   129  O O     A SER A 1 33  ? 27.074 14.145 0.066  0.50 23.19 ? 24  SER A O     1 
ATOM   130  O O     B SER A 1 33  ? 27.184 14.542 -0.007 0.50 21.07 ? 24  SER A O     1 
ATOM   131  C CB    A SER A 1 33  ? 25.230 16.209 -1.014 0.50 21.47 ? 24  SER A CB    1 
ATOM   132  C CB    B SER A 1 33  ? 25.109 16.406 -0.986 0.50 22.77 ? 24  SER A CB    1 
ATOM   133  O OG    A SER A 1 33  ? 25.327 17.379 -0.230 0.50 22.18 ? 24  SER A OG    1 
ATOM   134  O OG    B SER A 1 33  ? 24.006 16.692 -1.829 0.50 26.78 ? 24  SER A OG    1 
ATOM   135  N N     . HIS A 1 34  ? 26.168 15.029 1.926  1.00 19.76 ? 25  HIS A N     1 
ATOM   136  C CA    . HIS A 1 34  ? 27.360 14.795 2.702  1.00 19.88 ? 25  HIS A CA    1 
ATOM   137  C C     . HIS A 1 34  ? 26.901 14.755 4.146  1.00 21.13 ? 25  HIS A C     1 
ATOM   138  O O     . HIS A 1 34  ? 25.746 15.055 4.451  1.00 20.00 ? 25  HIS A O     1 
ATOM   139  C CB    . HIS A 1 34  ? 28.433 15.863 2.490  1.00 19.69 ? 25  HIS A CB    1 
ATOM   140  C CG    . HIS A 1 34  ? 27.986 17.224 2.907  1.00 18.77 ? 25  HIS A CG    1 
ATOM   141  N ND1   . HIS A 1 34  ? 27.928 17.607 4.241  1.00 18.82 ? 25  HIS A ND1   1 
ATOM   142  C CD2   . HIS A 1 34  ? 27.536 18.270 2.177  1.00 19.70 ? 25  HIS A CD2   1 
ATOM   143  C CE1   . HIS A 1 34  ? 27.478 18.856 4.294  1.00 20.49 ? 25  HIS A CE1   1 
ATOM   144  N NE2   . HIS A 1 34  ? 27.227 19.277 3.052  1.00 19.92 ? 25  HIS A NE2   1 
ATOM   145  N N     . ARG A 1 35  ? 27.826 14.369 5.006  1.00 18.25 ? 26  ARG A N     1 
ATOM   146  C CA    . ARG A 1 35  ? 27.486 13.959 6.362  1.00 19.03 ? 26  ARG A CA    1 
ATOM   147  C C     . ARG A 1 35  ? 27.964 14.921 7.410  1.00 19.79 ? 26  ARG A C     1 
ATOM   148  O O     . ARG A 1 35  ? 27.949 14.566 8.610  1.00 18.93 ? 26  ARG A O     1 
ATOM   149  C CB    . ARG A 1 35  ? 28.019 12.573 6.634  1.00 19.16 ? 26  ARG A CB    1 
ATOM   150  C CG    . ARG A 1 35  ? 27.355 11.593 5.640  1.00 24.24 ? 26  ARG A CG    1 
ATOM   151  C CD    . ARG A 1 35  ? 28.064 10.335 5.631  1.00 31.47 ? 26  ARG A CD    1 
ATOM   152  N NE    . ARG A 1 35  ? 27.438 9.427  4.681  1.00 23.25 ? 26  ARG A NE    1 
ATOM   153  C CZ    . ARG A 1 35  ? 26.917 8.255  5.005  1.00 23.82 ? 26  ARG A CZ    1 
ATOM   154  N NH1   . ARG A 1 35  ? 26.682 7.924  6.275  1.00 21.51 ? 26  ARG A NH1   1 
ATOM   155  N NH2   . ARG A 1 35  ? 26.669 7.373  4.028  1.00 24.90 ? 26  ARG A NH2   1 
ATOM   156  N N     . VAL A 1 36  ? 28.398 16.120 7.003  1.00 18.65 ? 27  VAL A N     1 
ATOM   157  C CA    . VAL A 1 36  ? 28.879 17.143 7.926  1.00 18.86 ? 27  VAL A CA    1 
ATOM   158  C C     . VAL A 1 36  ? 27.689 18.010 8.299  1.00 19.33 ? 27  VAL A C     1 
ATOM   159  O O     . VAL A 1 36  ? 27.133 18.695 7.452  1.00 19.74 ? 27  VAL A O     1 
ATOM   160  C CB    . VAL A 1 36  ? 29.984 17.986 7.258  1.00 17.99 ? 27  VAL A CB    1 
ATOM   161  C CG1   . VAL A 1 36  ? 30.486 19.155 8.182  1.00 19.87 ? 27  VAL A CG1   1 
ATOM   162  C CG2   . VAL A 1 36  ? 31.145 17.096 6.809  1.00 23.17 ? 27  VAL A CG2   1 
ATOM   163  N N     . VAL A 1 37  ? 27.322 18.023 9.578  1.00 16.88 ? 28  VAL A N     1 
ATOM   164  C CA    . VAL A 1 37  ? 26.128 18.701 10.074 1.00 16.10 ? 28  VAL A CA    1 
ATOM   165  C C     . VAL A 1 37  ? 26.544 19.873 10.937 1.00 16.00 ? 28  VAL A C     1 
ATOM   166  O O     . VAL A 1 37  ? 27.514 19.778 11.711 1.00 17.10 ? 28  VAL A O     1 
ATOM   167  C CB    . VAL A 1 37  ? 25.334 17.671 10.915 1.00 15.33 ? 28  VAL A CB    1 
ATOM   168  C CG1   . VAL A 1 37  ? 24.124 18.305 11.533 1.00 17.23 ? 28  VAL A CG1   1 
ATOM   169  C CG2   . VAL A 1 37  ? 24.890 16.469 10.036 1.00 17.93 ? 28  VAL A CG2   1 
ATOM   170  N N     . LEU A 1 38  ? 25.816 20.982 10.828 1.00 15.63 ? 29  LEU A N     1 
ATOM   171  C CA    . LEU A 1 38  ? 26.014 22.130 11.719 1.00 15.01 ? 29  LEU A CA    1 
ATOM   172  C C     . LEU A 1 38  ? 25.292 21.793 13.028 1.00 16.96 ? 29  LEU A C     1 
ATOM   173  O O     . LEU A 1 38  ? 24.055 21.653 13.075 1.00 16.51 ? 29  LEU A O     1 
ATOM   174  C CB    . LEU A 1 38  ? 25.438 23.404 11.074 1.00 15.50 ? 29  LEU A CB    1 
ATOM   175  C CG    . LEU A 1 38  ? 25.341 24.596 12.070 1.00 16.24 ? 29  LEU A CG    1 
ATOM   176  C CD1   . LEU A 1 38  ? 26.704 25.070 12.479 1.00 17.72 ? 29  LEU A CD1   1 
ATOM   177  C CD2   . LEU A 1 38  ? 24.618 25.763 11.406 1.00 18.63 ? 29  LEU A CD2   1 
ATOM   178  N N     . ALA A 1 39  ? 26.063 21.600 14.113 1.00 16.64 ? 30  ALA A N     1 
ATOM   179  C CA    . ALA A 1 39  ? 25.465 21.376 15.421 1.00 15.81 ? 30  ALA A CA    1 
ATOM   180  C C     . ALA A 1 39  ? 24.719 22.619 15.911 1.00 15.34 ? 30  ALA A C     1 
ATOM   181  O O     . ALA A 1 39  ? 25.113 23.737 15.593 1.00 15.98 ? 30  ALA A O     1 
ATOM   182  C CB    . ALA A 1 39  ? 26.557 21.019 16.425 1.00 17.16 ? 30  ALA A CB    1 
ATOM   183  N N     . PRO A 1 40  ? 23.692 22.437 16.729 1.00 15.14 ? 31  PRO A N     1 
ATOM   184  C CA    . PRO A 1 40  ? 22.934 23.574 17.270 1.00 14.89 ? 31  PRO A CA    1 
ATOM   185  C C     . PRO A 1 40  ? 23.817 24.370 18.224 1.00 14.47 ? 31  PRO A C     1 
ATOM   186  O O     . PRO A 1 40  ? 24.418 23.824 19.166 1.00 16.37 ? 31  PRO A O     1 
ATOM   187  C CB    . PRO A 1 40  ? 21.783 22.897 18.024 1.00 15.99 ? 31  PRO A CB    1 
ATOM   188  C CG    . PRO A 1 40  ? 22.344 21.513 18.379 1.00 16.22 ? 31  PRO A CG    1 
ATOM   189  C CD    . PRO A 1 40  ? 23.176 21.127 17.185 1.00 16.15 ? 31  PRO A CD    1 
ATOM   190  N N     . MET A 1 41  ? 23.891 25.673 17.999 1.00 15.22 ? 32  MET A N     1 
ATOM   191  C CA    . MET A 1 41  ? 24.684 26.553 18.869 1.00 15.51 ? 32  MET A CA    1 
ATOM   192  C C     . MET A 1 41  ? 24.021 27.858 19.200 1.00 15.68 ? 32  MET A C     1 
ATOM   193  O O     . MET A 1 41  ? 23.867 28.704 18.319 1.00 16.75 ? 32  MET A O     1 
ATOM   194  C CB    . MET A 1 41  ? 26.098 26.831 18.331 1.00 16.30 ? 32  MET A CB    1 
ATOM   195  C CG    . MET A 1 41  ? 27.014 25.595 18.306 1.00 15.91 ? 32  MET A CG    1 
ATOM   196  S SD    . MET A 1 41  ? 28.573 25.972 17.517 1.00 18.57 ? 32  MET A SD    1 
ATOM   197  C CE    . MET A 1 41  ? 27.964 26.087 15.777 1.00 18.19 ? 32  MET A CE    1 
ATOM   198  N N     . THR A 1 42  ? 23.788 28.042 20.501 1.00 16.37 ? 33  THR A N     1 
ATOM   199  C CA    . THR A 1 42  ? 23.359 29.344 21.046 1.00 16.14 ? 33  THR A CA    1 
ATOM   200  C C     . THR A 1 42  ? 24.452 30.375 20.846 1.00 18.30 ? 33  THR A C     1 
ATOM   201  O O     . THR A 1 42  ? 25.612 30.153 21.226 1.00 17.44 ? 33  THR A O     1 
ATOM   202  C CB    . THR A 1 42  ? 23.136 29.128 22.536 1.00 16.38 ? 33  THR A CB    1 
ATOM   203  O OG1   . THR A 1 42  ? 21.984 28.298 22.699 1.00 17.87 ? 33  THR A OG1   1 
ATOM   204  C CG2   . THR A 1 42  ? 22.904 30.450 23.285 1.00 17.48 ? 33  THR A CG2   1 
ATOM   205  N N     . ARG A 1 43  ? 24.088 31.480 20.195 1.00 16.04 ? 34  ARG A N     1 
ATOM   206  C CA    . ARG A 1 43  ? 25.038 32.552 19.940 1.00 16.56 ? 34  ARG A CA    1 
ATOM   207  C C     . ARG A 1 43  ? 24.549 33.904 20.450 1.00 16.97 ? 34  ARG A C     1 
ATOM   208  O O     . ARG A 1 43  ? 25.338 34.853 20.472 1.00 17.75 ? 34  ARG A O     1 
ATOM   209  C CB    . ARG A 1 43  ? 25.376 32.686 18.450 1.00 17.23 ? 34  ARG A CB    1 
ATOM   210  C CG    . ARG A 1 43  ? 25.812 31.367 17.839 1.00 18.04 ? 34  ARG A CG    1 
ATOM   211  C CD    . ARG A 1 43  ? 27.154 30.826 18.365 1.00 18.34 ? 34  ARG A CD    1 
ATOM   212  N NE    . ARG A 1 43  ? 28.188 31.865 18.400 1.00 16.97 ? 34  ARG A NE    1 
ATOM   213  C CZ    . ARG A 1 43  ? 28.908 32.255 17.350 1.00 17.52 ? 34  ARG A CZ    1 
ATOM   214  N NH1   . ARG A 1 43  ? 28.764 31.696 16.143 1.00 16.40 ? 34  ARG A NH1   1 
ATOM   215  N NH2   . ARG A 1 43  ? 29.823 33.229 17.515 1.00 18.78 ? 34  ARG A NH2   1 
ATOM   216  N N     . CYS A 1 44  ? 23.296 34.018 20.855 1.00 17.02 ? 35  CYS A N     1 
ATOM   217  C CA    . CYS A 1 44  ? 22.771 35.217 21.536 1.00 17.39 ? 35  CYS A CA    1 
ATOM   218  C C     . CYS A 1 44  ? 22.804 36.472 20.662 1.00 20.26 ? 35  CYS A C     1 
ATOM   219  O O     . CYS A 1 44  ? 22.930 37.593 21.195 1.00 18.85 ? 35  CYS A O     1 
ATOM   220  C CB    . CYS A 1 44  ? 23.523 35.483 22.830 1.00 17.49 ? 35  CYS A CB    1 
ATOM   221  S SG    . CYS A 1 44  ? 23.687 34.041 23.914 1.00 18.75 ? 35  CYS A SG    1 
ATOM   222  N N     . ARG A 1 45  ? 22.592 36.338 19.351 1.00 16.96 ? 36  ARG A N     1 
ATOM   223  C CA    . ARG A 1 45  ? 22.384 37.508 18.483 1.00 15.94 ? 36  ARG A CA    1 
ATOM   224  C C     . ARG A 1 45  ? 20.931 37.779 18.171 1.00 17.98 ? 36  ARG A C     1 
ATOM   225  O O     . ARG A 1 45  ? 20.656 38.806 17.506 1.00 18.45 ? 36  ARG A O     1 
ATOM   226  C CB    . ARG A 1 45  ? 23.162 37.274 17.179 1.00 16.84 ? 36  ARG A CB    1 
ATOM   227  C CG    . ARG A 1 45  ? 24.603 37.840 17.183 1.00 18.78 ? 36  ARG A CG    1 
ATOM   228  C CD    . ARG A 1 45  ? 25.518 36.987 18.052 1.00 19.26 ? 36  ARG A CD    1 
ATOM   229  N NE    . ARG A 1 45  ? 26.890 37.436 17.915 1.00 18.93 ? 36  ARG A NE    1 
ATOM   230  C CZ    . ARG A 1 45  ? 27.908 36.818 18.483 1.00 17.45 ? 36  ARG A CZ    1 
ATOM   231  N NH1   . ARG A 1 45  ? 27.719 35.706 19.209 1.00 17.17 ? 36  ARG A NH1   1 
ATOM   232  N NH2   . ARG A 1 45  ? 29.144 37.263 18.257 1.00 19.93 ? 36  ARG A NH2   1 
ATOM   233  N N     . ALA A 1 46  ? 19.990 36.978 18.691 1.00 17.50 ? 37  ALA A N     1 
ATOM   234  C CA    . ALA A 1 46  ? 18.553 37.138 18.380 1.00 18.01 ? 37  ALA A CA    1 
ATOM   235  C C     . ALA A 1 46  ? 17.960 38.137 19.371 1.00 17.66 ? 37  ALA A C     1 
ATOM   236  O O     . ALA A 1 46  ? 17.228 37.786 20.306 1.00 18.05 ? 37  ALA A O     1 
ATOM   237  C CB    . ALA A 1 46  ? 17.834 35.786 18.416 1.00 16.57 ? 37  ALA A CB    1 
ATOM   238  N N     . LEU A 1 47  ? 18.240 39.416 19.119 1.00 17.37 ? 38  LEU A N     1 
ATOM   239  C CA    . LEU A 1 47  ? 17.887 40.437 20.123 1.00 20.35 ? 38  LEU A CA    1 
ATOM   240  C C     . LEU A 1 47  ? 16.392 40.410 20.478 1.00 19.28 ? 38  LEU A C     1 
ATOM   241  O O     . LEU A 1 47  ? 15.526 40.295 19.596 1.00 19.68 ? 38  LEU A O     1 
ATOM   242  C CB    . LEU A 1 47  ? 18.279 41.830 19.617 1.00 21.15 ? 38  LEU A CB    1 
ATOM   243  C CG    . LEU A 1 47  ? 19.756 41.965 19.246 1.00 20.74 ? 38  LEU A CG    1 
ATOM   244  C CD1   . LEU A 1 47  ? 20.071 43.422 18.866 1.00 22.32 ? 38  LEU A CD1   1 
ATOM   245  C CD2   . LEU A 1 47  ? 20.680 41.515 20.395 1.00 20.12 ? 38  LEU A CD2   1 
ATOM   246  N N     . ASN A 1 48  ? 16.096 40.446 21.773 1.00 19.75 ? 39  ASN A N     1 
ATOM   247  C CA    . ASN A 1 48  ? 14.717 40.422 22.300 1.00 21.51 ? 39  ASN A CA    1 
ATOM   248  C C     . ASN A 1 48  ? 13.963 39.168 21.869 1.00 21.21 ? 39  ASN A C     1 
ATOM   249  O O     . ASN A 1 48  ? 12.730 39.150 21.738 1.00 21.80 ? 39  ASN A O     1 
ATOM   250  C CB    . ASN A 1 48  ? 13.921 41.681 21.965 1.00 24.23 ? 39  ASN A CB    1 
ATOM   251  C CG    . ASN A 1 48  ? 14.578 42.928 22.500 1.00 27.23 ? 39  ASN A CG    1 
ATOM   252  O OD1   . ASN A 1 48  ? 14.998 43.017 23.660 1.00 30.96 ? 39  ASN A OD1   1 
ATOM   253  N ND2   . ASN A 1 48  ? 14.692 43.840 21.668 1.00 23.76 ? 39  ASN A ND2   1 
ATOM   254  N N     . ASN A 1 49  ? 14.726 38.111 21.634 1.00 17.96 ? 40  ASN A N     1 
ATOM   255  C CA    . ASN A 1 49  ? 14.193 36.798 21.265 1.00 18.82 ? 40  ASN A CA    1 
ATOM   256  C C     . ASN A 1 49  ? 13.610 36.758 19.860 1.00 18.98 ? 40  ASN A C     1 
ATOM   257  O O     . ASN A 1 49  ? 12.868 35.798 19.530 1.00 19.52 ? 40  ASN A O     1 
ATOM   258  C CB    . ASN A 1 49  ? 13.195 36.242 22.295 1.00 18.13 ? 40  ASN A CB    1 
ATOM   259  C CG    . ASN A 1 49  ? 13.658 36.387 23.730 1.00 18.20 ? 40  ASN A CG    1 
ATOM   260  O OD1   . ASN A 1 49  ? 12.954 36.970 24.579 1.00 23.93 ? 40  ASN A OD1   1 
ATOM   261  N ND2   . ASN A 1 49  ? 14.807 35.834 24.041 1.00 20.31 ? 40  ASN A ND2   1 
ATOM   262  N N     . ILE A 1 50  ? 13.900 37.755 19.043 1.00 18.23 ? 41  ILE A N     1 
ATOM   263  C CA    . ILE A 1 50  ? 13.397 37.815 17.680 1.00 18.66 ? 41  ILE A CA    1 
ATOM   264  C C     . ILE A 1 50  ? 14.557 37.465 16.760 1.00 19.79 ? 41  ILE A C     1 
ATOM   265  O O     . ILE A 1 50  ? 15.631 38.068 16.865 1.00 20.21 ? 41  ILE A O     1 
ATOM   266  C CB    . ILE A 1 50  ? 12.834 39.212 17.341 1.00 21.82 ? 41  ILE A CB    1 
ATOM   267  C CG1   . ILE A 1 50  ? 11.613 39.514 18.187 1.00 24.96 ? 41  ILE A CG1   1 
ATOM   268  C CG2   . ILE A 1 50  ? 12.404 39.241 15.846 1.00 24.62 ? 41  ILE A CG2   1 
ATOM   269  C CD1   . ILE A 1 50  ? 11.497 41.004 18.514 1.00 40.24 ? 41  ILE A CD1   1 
ATOM   270  N N     . PRO A 1 51  ? 14.423 36.475 15.879 1.00 18.31 ? 42  PRO A N     1 
ATOM   271  C CA    . PRO A 1 51  ? 15.469 36.245 14.902 1.00 17.84 ? 42  PRO A CA    1 
ATOM   272  C C     . PRO A 1 51  ? 15.741 37.539 14.147 1.00 23.00 ? 42  PRO A C     1 
ATOM   273  O O     . PRO A 1 51  ? 14.826 38.316 13.812 1.00 25.28 ? 42  PRO A O     1 
ATOM   274  C CB    . PRO A 1 51  ? 14.872 35.169 13.988 1.00 21.86 ? 42  PRO A CB    1 
ATOM   275  C CG    . PRO A 1 51  ? 13.813 34.530 14.798 1.00 20.28 ? 42  PRO A CG    1 
ATOM   276  C CD    . PRO A 1 51  ? 13.266 35.596 15.706 1.00 20.69 ? 42  PRO A CD    1 
ATOM   277  N N     . GLN A 1 52  ? 17.017 37.784 13.929 1.00 19.53 ? 43  GLN A N     1 
ATOM   278  C CA    . GLN A 1 52  ? 17.497 39.009 13.298 1.00 20.09 ? 43  GLN A CA    1 
ATOM   279  C C     . GLN A 1 52  ? 18.134 38.690 11.951 1.00 21.14 ? 43  GLN A C     1 
ATOM   280  O O     . GLN A 1 52  ? 18.519 37.565 11.654 1.00 21.59 ? 43  GLN A O     1 
ATOM   281  C CB    . GLN A 1 52  ? 18.502 39.751 14.221 1.00 24.75 ? 43  GLN A CB    1 
ATOM   282  C CG    . GLN A 1 52  ? 17.966 40.087 15.598 1.00 23.52 ? 43  GLN A CG    1 
ATOM   283  C CD    . GLN A 1 52  ? 16.898 41.155 15.601 1.00 24.10 ? 43  GLN A CD    1 
ATOM   284  O OE1   . GLN A 1 52  ? 16.920 42.031 14.720 1.00 31.86 ? 43  GLN A OE1   1 
ATOM   285  N NE2   . GLN A 1 52  ? 15.988 41.127 16.550 1.00 24.55 ? 43  GLN A NE2   1 
ATOM   286  N N     . ALA A 1 53  ? 18.280 39.731 11.119 1.00 22.27 ? 44  ALA A N     1 
ATOM   287  C CA    . ALA A 1 53  ? 18.966 39.585 9.839  1.00 21.34 ? 44  ALA A CA    1 
ATOM   288  C C     . ALA A 1 53  ? 20.342 38.937 9.969  1.00 21.21 ? 44  ALA A C     1 
ATOM   289  O O     . ALA A 1 53  ? 20.770 38.201 9.071  1.00 24.29 ? 44  ALA A O     1 
ATOM   290  C CB    . ALA A 1 53  ? 19.110 40.975 9.185  1.00 27.17 ? 44  ALA A CB    1 
ATOM   291  N N     . ALA A 1 54  ? 21.080 39.256 11.047 1.00 22.73 ? 45  ALA A N     1 
ATOM   292  C CA    . ALA A 1 54  ? 22.395 38.653 11.239 1.00 21.44 ? 45  ALA A CA    1 
ATOM   293  C C     . ALA A 1 54  ? 22.322 37.128 11.239 1.00 18.52 ? 45  ALA A C     1 
ATOM   294  O O     . ALA A 1 54  ? 23.230 36.473 10.739 1.00 21.26 ? 45  ALA A O     1 
ATOM   295  C CB    . ALA A 1 54  ? 23.024 39.136 12.552 1.00 24.85 ? 45  ALA A CB    1 
ATOM   296  N N     . LEU A 1 55  ? 21.262 36.551 11.842 1.00 19.35 ? 46  LEU A N     1 
ATOM   297  C CA    . LEU A 1 55  ? 21.143 35.084 11.831 1.00 19.41 ? 46  LEU A CA    1 
ATOM   298  C C     . LEU A 1 55  ? 21.004 34.589 10.401 1.00 18.39 ? 46  LEU A C     1 
ATOM   299  O O     . LEU A 1 55  ? 21.531 33.554 10.039 1.00 19.70 ? 46  LEU A O     1 
ATOM   300  C CB    . LEU A 1 55  ? 19.918 34.644 12.627 1.00 19.97 ? 46  LEU A CB    1 
ATOM   301  C CG    . LEU A 1 55  ? 20.096 34.471 14.128 1.00 17.27 ? 46  LEU A CG    1 
ATOM   302  C CD1   . LEU A 1 55  ? 20.439 35.814 14.747 1.00 18.59 ? 46  LEU A CD1   1 
ATOM   303  C CD2   . LEU A 1 55  ? 18.879 33.827 14.728 1.00 19.43 ? 46  LEU A CD2   1 
ATOM   304  N N     . GLY A 1 56  ? 20.256 35.323 9.574  1.00 19.85 ? 47  GLY A N     1 
ATOM   305  C CA    . GLY A 1 56  ? 20.180 34.946 8.160  1.00 20.69 ? 47  GLY A CA    1 
ATOM   306  C C     . GLY A 1 56  ? 21.545 34.877 7.488  1.00 19.58 ? 47  GLY A C     1 
ATOM   307  O O     . GLY A 1 56  ? 21.861 33.919 6.762  1.00 21.33 ? 47  GLY A O     1 
ATOM   308  N N     . GLU A 1 57  ? 22.380 35.903 7.712  1.00 19.43 ? 48  GLU A N     1 
ATOM   309  C CA    . GLU A 1 57  ? 23.689 35.888 7.081  1.00 19.74 ? 48  GLU A CA    1 
ATOM   310  C C     . GLU A 1 57  ? 24.541 34.732 7.636  1.00 18.48 ? 48  GLU A C     1 
ATOM   311  O O     . GLU A 1 57  ? 25.230 34.032 6.892  1.00 20.24 ? 48  GLU A O     1 
ATOM   312  C CB    . GLU A 1 57  ? 24.370 37.243 7.327  1.00 22.27 ? 48  GLU A CB    1 
ATOM   313  C CG    . GLU A 1 57  ? 25.842 37.254 6.854  1.00 29.91 ? 48  GLU A CG    1 
ATOM   314  C CD    . GLU A 1 57  ? 26.502 38.632 6.849  1.00 63.85 ? 48  GLU A CD    1 
ATOM   315  O OE1   . GLU A 1 57  ? 25.994 39.549 7.520  1.00 72.54 ? 48  GLU A OE1   1 
ATOM   316  O OE2   . GLU A 1 57  ? 27.550 38.785 6.173  1.00 61.70 ? 48  GLU A OE2   1 
ATOM   317  N N     . TYR A 1 58  ? 24.450 34.500 8.946  1.00 18.48 ? 49  TYR A N     1 
ATOM   318  C CA    . TYR A 1 58  ? 25.248 33.449 9.582  1.00 19.02 ? 49  TYR A CA    1 
ATOM   319  C C     . TYR A 1 58  ? 24.883 32.062 9.076  1.00 17.40 ? 49  TYR A C     1 
ATOM   320  O O     . TYR A 1 58  ? 25.754 31.275 8.728  1.00 17.26 ? 49  TYR A O     1 
ATOM   321  C CB    . TYR A 1 58  ? 24.987 33.537 11.078 1.00 18.57 ? 49  TYR A CB    1 
ATOM   322  C CG    . TYR A 1 58  ? 25.517 32.417 11.941 1.00 18.86 ? 49  TYR A CG    1 
ATOM   323  C CD1   . TYR A 1 58  ? 26.851 32.399 12.333 1.00 19.15 ? 49  TYR A CD1   1 
ATOM   324  C CD2   . TYR A 1 58  ? 24.660 31.439 12.408 1.00 20.00 ? 49  TYR A CD2   1 
ATOM   325  C CE1   . TYR A 1 58  ? 27.321 31.425 13.181 1.00 18.52 ? 49  TYR A CE1   1 
ATOM   326  C CE2   . TYR A 1 58  ? 25.114 30.438 13.284 1.00 19.39 ? 49  TYR A CE2   1 
ATOM   327  C CZ    . TYR A 1 58  ? 26.443 30.485 13.660 1.00 20.81 ? 49  TYR A CZ    1 
ATOM   328  O OH    . TYR A 1 58  ? 26.871 29.550 14.596 1.00 21.48 ? 49  TYR A OH    1 
ATOM   329  N N     . TYR A 1 59  ? 23.587 31.737 9.033  1.00 16.57 ? 50  TYR A N     1 
ATOM   330  C CA    . TYR A 1 59  ? 23.204 30.410 8.530  1.00 17.35 ? 50  TYR A CA    1 
ATOM   331  C C     . TYR A 1 59  ? 23.422 30.257 7.020  1.00 18.11 ? 50  TYR A C     1 
ATOM   332  O O     . TYR A 1 59  ? 23.869 29.208 6.557  1.00 20.41 ? 50  TYR A O     1 
ATOM   333  C CB    . TYR A 1 59  ? 21.772 30.075 8.926  1.00 17.65 ? 50  TYR A CB    1 
ATOM   334  C CG    . TYR A 1 59  ? 21.571 29.806 10.417 1.00 17.71 ? 50  TYR A CG    1 
ATOM   335  C CD1   . TYR A 1 59  ? 22.098 28.668 10.980 1.00 17.56 ? 50  TYR A CD1   1 
ATOM   336  C CD2   . TYR A 1 59  ? 20.881 30.696 11.189 1.00 17.93 ? 50  TYR A CD2   1 
ATOM   337  C CE1   . TYR A 1 59  ? 21.929 28.424 12.346 1.00 18.11 ? 50  TYR A CE1   1 
ATOM   338  C CE2   . TYR A 1 59  ? 20.689 30.473 12.548 1.00 19.07 ? 50  TYR A CE2   1 
ATOM   339  C CZ    . TYR A 1 59  ? 21.225 29.324 13.103 1.00 16.62 ? 50  TYR A CZ    1 
ATOM   340  O OH    . TYR A 1 59  ? 21.037 29.083 14.452 1.00 19.05 ? 50  TYR A OH    1 
ATOM   341  N N     . GLU A 1 60  ? 23.161 31.336 6.261  1.00 19.62 ? 51  GLU A N     1 
ATOM   342  C CA    . GLU A 1 60  ? 23.441 31.297 4.821  1.00 19.08 ? 51  GLU A CA    1 
ATOM   343  C C     . GLU A 1 60  ? 24.918 31.022 4.546  1.00 19.68 ? 51  GLU A C     1 
ATOM   344  O O     . GLU A 1 60  ? 25.249 30.227 3.648  1.00 21.51 ? 51  GLU A O     1 
ATOM   345  C CB    . GLU A 1 60  ? 22.996 32.623 4.189  1.00 21.23 ? 51  GLU A CB    1 
ATOM   346  C CG    . GLU A 1 60  ? 23.090 32.594 2.646  1.00 21.81 ? 51  GLU A CG    1 
ATOM   347  C CD    . GLU A 1 60  ? 22.826 33.969 2.029  1.00 34.49 ? 51  GLU A CD    1 
ATOM   348  O OE1   . GLU A 1 60  ? 23.399 34.965 2.518  1.00 45.04 ? 51  GLU A OE1   1 
ATOM   349  O OE2   . GLU A 1 60  ? 22.056 34.055 1.036  1.00 43.37 ? 51  GLU A OE2   1 
ATOM   350  N N     . GLN A 1 61  ? 25.834 31.619 5.354  1.00 18.59 ? 52  GLN A N     1 
ATOM   351  C CA    . GLN A 1 61  ? 27.254 31.391 5.124  1.00 18.65 ? 52  GLN A CA    1 
ATOM   352  C C     . GLN A 1 61  ? 27.624 29.933 5.270  1.00 18.75 ? 52  GLN A C     1 
ATOM   353  O O     . GLN A 1 61  ? 28.531 29.448 4.604  1.00 21.02 ? 52  GLN A O     1 
ATOM   354  C CB    . GLN A 1 61  ? 28.112 32.139 6.148  1.00 17.16 ? 52  GLN A CB    1 
ATOM   355  C CG    . GLN A 1 61  ? 28.200 33.664 5.905  1.00 19.93 ? 52  GLN A CG    1 
ATOM   356  C CD    . GLN A 1 61  ? 29.078 34.393 6.894  1.00 23.50 ? 52  GLN A CD    1 
ATOM   357  O OE1   . GLN A 1 61  ? 29.339 33.918 8.005  1.00 22.23 ? 52  GLN A OE1   1 
ATOM   358  N NE2   . GLN A 1 61  ? 29.550 35.578 6.501  1.00 26.85 ? 52  GLN A NE2   1 
ATOM   359  N N     . ARG A 1 62  ? 26.929 29.216 6.167  1.00 19.45 ? 53  ARG A N     1 
ATOM   360  C CA    . ARG A 1 62  ? 27.288 27.854 6.494  1.00 18.67 ? 53  ARG A CA    1 
ATOM   361  C C     . ARG A 1 62  ? 26.506 26.806 5.711  1.00 18.32 ? 53  ARG A C     1 
ATOM   362  O O     . ARG A 1 62  ? 26.939 25.646 5.651  1.00 20.69 ? 53  ARG A O     1 
ATOM   363  C CB    . ARG A 1 62  ? 27.113 27.669 8.005  1.00 18.97 ? 53  ARG A CB    1 
ATOM   364  C CG    . ARG A 1 62  ? 28.228 28.421 8.741  1.00 18.55 ? 53  ARG A CG    1 
ATOM   365  C CD    . ARG A 1 62  ? 27.877 28.875 10.177 1.00 18.63 ? 53  ARG A CD    1 
ATOM   366  N NE    . ARG A 1 62  ? 29.035 29.586 10.711 1.00 20.49 ? 53  ARG A NE    1 
ATOM   367  C CZ    . ARG A 1 62  ? 29.406 30.787 10.288 1.00 20.50 ? 53  ARG A CZ    1 
ATOM   368  N NH1   . ARG A 1 62  ? 28.621 31.515 9.500  1.00 18.46 ? 53  ARG A NH1   1 
ATOM   369  N NH2   . ARG A 1 62  ? 30.577 31.284 10.678 1.00 20.38 ? 53  ARG A NH2   1 
ATOM   370  N N     . ALA A 1 63  ? 25.402 27.207 5.086  1.00 19.12 ? 54  ALA A N     1 
ATOM   371  C CA    . ALA A 1 63  ? 24.589 26.305 4.287  1.00 20.16 ? 54  ALA A CA    1 
ATOM   372  C C     . ALA A 1 63  ? 25.310 25.848 3.025  1.00 18.57 ? 54  ALA A C     1 
ATOM   373  O O     . ALA A 1 63  ? 26.047 26.609 2.381  1.00 21.67 ? 54  ALA A O     1 
ATOM   374  C CB    . ALA A 1 63  ? 23.314 27.055 3.874  1.00 19.95 ? 54  ALA A CB    1 
ATOM   375  N N     . THR A 1 64  ? 25.108 24.574 2.710  1.00 18.90 ? 55  THR A N     1 
ATOM   376  C CA    . THR A 1 64  ? 25.644 23.977 1.496  1.00 18.41 ? 55  THR A CA    1 
ATOM   377  C C     . THR A 1 64  ? 24.541 23.151 0.846  1.00 21.78 ? 55  THR A C     1 
ATOM   378  O O     . THR A 1 64  ? 23.596 22.698 1.501  1.00 21.20 ? 55  THR A O     1 
ATOM   379  C CB    . THR A 1 64  ? 26.824 23.056 1.767  1.00 21.97 ? 55  THR A CB    1 
ATOM   380  O OG1   . THR A 1 64  ? 26.451 22.058 2.757  1.00 21.32 ? 55  THR A OG1   1 
ATOM   381  C CG2   . THR A 1 64  ? 27.985 23.846 2.302  1.00 22.65 ? 55  THR A CG2   1 
ATOM   382  N N     . ALA A 1 65  ? 24.664 22.945 -0.471 1.00 20.28 ? 56  ALA A N     1 
ATOM   383  C CA    . ALA A 1 65  ? 23.713 22.118 -1.195 1.00 20.48 ? 56  ALA A CA    1 
ATOM   384  C C     . ALA A 1 65  ? 23.709 20.695 -0.668 1.00 21.90 ? 56  ALA A C     1 
ATOM   385  O O     . ALA A 1 65  ? 24.739 20.004 -0.690 1.00 25.99 ? 56  ALA A O     1 
ATOM   386  C CB    . ALA A 1 65  ? 24.123 22.131 -2.670 1.00 23.80 ? 56  ALA A CB    1 
ATOM   387  N N     . GLY A 1 66  ? 22.547 20.264 -0.199 1.00 19.57 ? 57  GLY A N     1 
ATOM   388  C CA    . GLY A 1 66  ? 22.436 18.942 0.369  1.00 22.26 ? 57  GLY A CA    1 
ATOM   389  C C     . GLY A 1 66  ? 23.042 18.805 1.750  1.00 20.74 ? 57  GLY A C     1 
ATOM   390  O O     . GLY A 1 66  ? 23.213 17.679 2.193  1.00 21.27 ? 57  GLY A O     1 
ATOM   391  N N     . GLY A 1 67  ? 23.391 19.908 2.418  1.00 19.41 ? 58  GLY A N     1 
ATOM   392  C CA    . GLY A 1 67  ? 23.890 19.831 3.778  1.00 19.19 ? 58  GLY A CA    1 
ATOM   393  C C     . GLY A 1 67  ? 22.790 20.042 4.791  1.00 19.06 ? 58  GLY A C     1 
ATOM   394  O O     . GLY A 1 67  ? 21.847 20.765 4.551  1.00 21.17 ? 58  GLY A O     1 
ATOM   395  N N     . PHE A 1 68  ? 22.970 19.453 5.966  1.00 18.07 ? 59  PHE A N     1 
ATOM   396  C CA    . PHE A 1 68  ? 21.997 19.570 7.055  1.00 18.36 ? 59  PHE A CA    1 
ATOM   397  C C     . PHE A 1 68  ? 22.481 20.555 8.126  1.00 16.01 ? 59  PHE A C     1 
ATOM   398  O O     . PHE A 1 68  ? 23.636 20.476 8.594  1.00 17.58 ? 59  PHE A O     1 
ATOM   399  C CB    . PHE A 1 68  ? 21.764 18.171 7.644  1.00 16.20 ? 59  PHE A CB    1 
ATOM   400  C CG    . PHE A 1 68  ? 20.767 18.132 8.783  1.00 16.96 ? 59  PHE A CG    1 
ATOM   401  C CD1   . PHE A 1 68  ? 19.626 18.927 8.771  1.00 18.12 ? 59  PHE A CD1   1 
ATOM   402  C CD2   . PHE A 1 68  ? 20.949 17.238 9.840  1.00 18.36 ? 59  PHE A CD2   1 
ATOM   403  C CE1   . PHE A 1 68  ? 18.704 18.878 9.785  1.00 19.92 ? 59  PHE A CE1   1 
ATOM   404  C CE2   . PHE A 1 68  ? 20.046 17.224 10.915 1.00 17.93 ? 59  PHE A CE2   1 
ATOM   405  C CZ    . PHE A 1 68  ? 18.923 17.996 10.879 1.00 17.27 ? 59  PHE A CZ    1 
ATOM   406  N N     . LEU A 1 69  ? 21.606 21.483 8.500  1.00 16.70 ? 60  LEU A N     1 
ATOM   407  C CA    . LEU A 1 69  ? 21.889 22.474 9.552  1.00 17.10 ? 60  LEU A CA    1 
ATOM   408  C C     . LEU A 1 69  ? 20.862 22.304 10.667 1.00 16.99 ? 60  LEU A C     1 
ATOM   409  O O     . LEU A 1 69  ? 19.658 22.148 10.406 1.00 16.90 ? 60  LEU A O     1 
ATOM   410  C CB    . LEU A 1 69  ? 21.707 23.932 9.008  1.00 19.35 ? 60  LEU A CB    1 
ATOM   411  C CG    . LEU A 1 69  ? 22.513 24.312 7.780  1.00 22.26 ? 60  LEU A CG    1 
ATOM   412  C CD1   . LEU A 1 69  ? 22.192 25.791 7.444  1.00 26.81 ? 60  LEU A CD1   1 
ATOM   413  C CD2   . LEU A 1 69  ? 23.953 24.175 8.009  1.00 23.94 ? 60  LEU A CD2   1 
ATOM   414  N N     . ILE A 1 70  ? 21.285 22.486 11.927 1.00 15.25 ? 61  ILE A N     1 
ATOM   415  C CA    . ILE A 1 70  ? 20.359 22.551 13.041 1.00 15.75 ? 61  ILE A CA    1 
ATOM   416  C C     . ILE A 1 70  ? 20.574 23.927 13.663 1.00 16.12 ? 61  ILE A C     1 
ATOM   417  O O     . ILE A 1 70  ? 21.731 24.324 13.895 1.00 17.28 ? 61  ILE A O     1 
ATOM   418  C CB    . ILE A 1 70  ? 20.677 21.431 14.048 1.00 15.09 ? 61  ILE A CB    1 
ATOM   419  C CG1   . ILE A 1 70  ? 20.652 20.033 13.362 1.00 16.29 ? 61  ILE A CG1   1 
ATOM   420  C CG2   . ILE A 1 70  ? 19.672 21.477 15.162 1.00 16.12 ? 61  ILE A CG2   1 
ATOM   421  C CD1   . ILE A 1 70  ? 21.362 18.959 14.204 1.00 17.51 ? 61  ILE A CD1   1 
ATOM   422  N N     . THR A 1 71  ? 19.487 24.641 13.946 1.00 15.77 ? 62  THR A N     1 
ATOM   423  C CA    . THR A 1 71  ? 19.640 25.971 14.544 1.00 15.18 ? 62  THR A CA    1 
ATOM   424  C C     . THR A 1 71  ? 20.061 25.900 16.001 1.00 15.60 ? 62  THR A C     1 
ATOM   425  O O     . THR A 1 71  ? 19.905 24.874 16.694 1.00 16.40 ? 62  THR A O     1 
ATOM   426  C CB    . THR A 1 71  ? 18.328 26.777 14.547 1.00 16.14 ? 62  THR A CB    1 
ATOM   427  O OG1   . THR A 1 71  ? 17.371 26.201 15.462 1.00 17.16 ? 62  THR A OG1   1 
ATOM   428  C CG2   . THR A 1 71  ? 17.697 26.877 13.126 1.00 18.24 ? 62  THR A CG2   1 
ATOM   429  N N     . GLU A 1 72  ? 20.525 27.065 16.473 1.00 16.38 ? 63  GLU A N     1 
ATOM   430  C CA    . GLU A 1 72  ? 20.604 27.329 17.901 1.00 16.36 ? 63  GLU A CA    1 
ATOM   431  C C     . GLU A 1 72  ? 19.317 26.908 18.604 1.00 16.53 ? 63  GLU A C     1 
ATOM   432  O O     . GLU A 1 72  ? 18.206 26.957 18.049 1.00 16.72 ? 63  GLU A O     1 
ATOM   433  C CB    . GLU A 1 72  ? 20.810 28.828 18.109 1.00 17.52 ? 63  GLU A CB    1 
ATOM   434  C CG    . GLU A 1 72  ? 19.678 29.711 17.571 1.00 18.34 ? 63  GLU A CG    1 
ATOM   435  C CD    . GLU A 1 72  ? 20.209 31.052 17.018 1.00 21.59 ? 63  GLU A CD    1 
ATOM   436  O OE1   . GLU A 1 72  ? 20.620 31.134 15.825 1.00 21.80 ? 63  GLU A OE1   1 
ATOM   437  O OE2   . GLU A 1 72  ? 20.253 32.049 17.807 1.00 20.80 ? 63  GLU A OE2   1 
ATOM   438  N N     . GLY A 1 73  ? 19.433 26.572 19.892 1.00 15.33 ? 64  GLY A N     1 
ATOM   439  C CA    . GLY A 1 73  ? 18.238 26.292 20.667 1.00 16.56 ? 64  GLY A CA    1 
ATOM   440  C C     . GLY A 1 73  ? 17.282 27.479 20.657 1.00 15.81 ? 64  GLY A C     1 
ATOM   441  O O     . GLY A 1 73  ? 17.687 28.630 20.771 1.00 17.28 ? 64  GLY A O     1 
ATOM   442  N N     . THR A 1 74  ? 15.999 27.173 20.495 1.00 16.00 ? 65  THR A N     1 
ATOM   443  C CA    . THR A 1 74  ? 14.962 28.172 20.270 1.00 15.89 ? 65  THR A CA    1 
ATOM   444  C C     . THR A 1 74  ? 13.873 27.987 21.306 1.00 15.70 ? 65  THR A C     1 
ATOM   445  O O     . THR A 1 74  ? 13.404 26.862 21.539 1.00 15.85 ? 65  THR A O     1 
ATOM   446  C CB    . THR A 1 74  ? 14.448 27.980 18.830 1.00 16.15 ? 65  THR A CB    1 
ATOM   447  O OG1   . THR A 1 74  ? 15.511 28.279 17.929 1.00 17.80 ? 65  THR A OG1   1 
ATOM   448  C CG2   . THR A 1 74  ? 13.345 28.950 18.522 1.00 18.24 ? 65  THR A CG2   1 
ATOM   449  N N     . MET A 1 75  ? 13.463 29.087 21.932 1.00 15.71 ? 66  MET A N     1 
ATOM   450  C CA    . MET A 1 75  ? 12.430 29.012 22.956 1.00 16.69 ? 66  MET A CA    1 
ATOM   451  C C     . MET A 1 75  ? 11.078 28.505 22.488 1.00 15.66 ? 66  MET A C     1 
ATOM   452  O O     . MET A 1 75  ? 10.581 28.874 21.423 1.00 18.29 ? 66  MET A O     1 
ATOM   453  C CB    . MET A 1 75  ? 12.219 30.342 23.747 1.00 20.27 ? 66  MET A CB    1 
ATOM   454  C CG    . MET A 1 75  ? 13.443 31.190 24.007 1.00 17.19 ? 66  MET A CG    1 
ATOM   455  S SD    . MET A 1 75  ? 13.060 32.897 24.368 1.00 19.48 ? 66  MET A SD    1 
ATOM   456  C CE    . MET A 1 75  ? 11.885 32.806 25.718 1.00 22.52 ? 66  MET A CE    1 
ATOM   457  N N     . ILE A 1 76  ? 10.461 27.700 23.336 1.00 16.04 ? 67  ILE A N     1 
ATOM   458  C CA    . ILE A 1 76  ? 9.124  27.164 23.079 1.00 17.50 ? 67  ILE A CA    1 
ATOM   459  C C     . ILE A 1 76  ? 8.045  27.899 23.842 1.00 17.86 ? 67  ILE A C     1 
ATOM   460  O O     . ILE A 1 76  ? 6.847  27.635 23.617 1.00 19.13 ? 67  ILE A O     1 
ATOM   461  C CB    . ILE A 1 76  ? 9.014  25.652 23.401 1.00 17.72 ? 67  ILE A CB    1 
ATOM   462  C CG1   . ILE A 1 76  ? 9.266  25.386 24.905 1.00 17.67 ? 67  ILE A CG1   1 
ATOM   463  C CG2   . ILE A 1 76  ? 9.971  24.853 22.532 1.00 20.05 ? 67  ILE A CG2   1 
ATOM   464  C CD1   . ILE A 1 76  ? 8.913  23.936 25.322 1.00 18.69 ? 67  ILE A CD1   1 
ATOM   465  N N     . SER A 1 77  ? 8.415  28.824 24.710 1.00 19.08 ? 68  SER A N     1 
ATOM   466  C CA    . SER A 1 77  ? 7.460  29.528 25.551 1.00 20.33 ? 68  SER A CA    1 
ATOM   467  C C     . SER A 1 77  ? 8.165  30.664 26.262 1.00 20.51 ? 68  SER A C     1 
ATOM   468  O O     . SER A 1 77  ? 9.406  30.722 26.295 1.00 19.60 ? 68  SER A O     1 
ATOM   469  C CB    . SER A 1 77  ? 6.873  28.589 26.581 1.00 21.81 ? 68  SER A CB    1 
ATOM   470  O OG    . SER A 1 77  ? 7.862  28.375 27.595 1.00 23.07 ? 68  SER A OG    1 
ATOM   471  N N     . PRO A 1 78  ? 7.428  31.585 26.885 1.00 21.16 ? 69  PRO A N     1 
ATOM   472  C CA    . PRO A 1 78  ? 8.100  32.711 27.563 1.00 21.13 ? 69  PRO A CA    1 
ATOM   473  C C     . PRO A 1 78  ? 8.936  32.302 28.756 1.00 21.93 ? 69  PRO A C     1 
ATOM   474  O O     . PRO A 1 78  ? 9.752  33.121 29.182 1.00 24.81 ? 69  PRO A O     1 
ATOM   475  C CB    . PRO A 1 78  ? 6.933  33.623 27.999 1.00 28.10 ? 69  PRO A CB    1 
ATOM   476  C CG    . PRO A 1 78  ? 5.800  33.268 27.048 1.00 22.84 ? 69  PRO A CG    1 
ATOM   477  C CD    . PRO A 1 78  ? 5.976  31.793 26.696 1.00 21.70 ? 69  PRO A CD    1 
ATOM   478  N N     . THR A 1 79  ? 8.772  31.090 29.296 1.00 23.00 ? 70  THR A N     1 
ATOM   479  C CA    . THR A 1 79  ? 9.518  30.649 30.482 1.00 23.09 ? 70  THR A CA    1 
ATOM   480  C C     . THR A 1 79  ? 10.694 29.750 30.131 1.00 21.18 ? 70  THR A C     1 
ATOM   481  O O     . THR A 1 79  ? 11.382 29.232 31.040 1.00 22.34 ? 70  THR A O     1 
ATOM   482  C CB    . THR A 1 79  ? 8.605  29.895 31.451 1.00 28.08 ? 70  THR A CB    1 
ATOM   483  O OG1   . THR A 1 79  ? 8.172  28.660 30.823 1.00 34.43 ? 70  THR A OG1   1 
ATOM   484  C CG2   . THR A 1 79  ? 7.425  30.791 31.918 1.00 40.47 ? 70  THR A CG2   1 
ATOM   485  N N     A SER A 1 80  ? 10.984 29.572 28.846 0.50 18.33 ? 71  SER A N     1 
ATOM   486  N N     B SER A 1 80  ? 10.964 29.550 28.818 0.50 18.29 ? 71  SER A N     1 
ATOM   487  C CA    A SER A 1 80  ? 11.914 28.535 28.441 0.50 19.00 ? 71  SER A CA    1 
ATOM   488  C CA    B SER A 1 80  ? 11.930 28.562 28.336 0.50 18.85 ? 71  SER A CA    1 
ATOM   489  C C     A SER A 1 80  ? 13.358 28.996 28.301 0.50 18.65 ? 71  SER A C     1 
ATOM   490  C C     B SER A 1 80  ? 13.373 28.999 28.364 0.50 18.62 ? 71  SER A C     1 
ATOM   491  O O     A SER A 1 80  ? 14.206 28.149 27.950 0.50 18.00 ? 71  SER A O     1 
ATOM   492  O O     B SER A 1 80  ? 14.230 28.133 28.136 0.50 18.18 ? 71  SER A O     1 
ATOM   493  C CB    A SER A 1 80  ? 11.440 27.931 27.121 0.50 20.91 ? 71  SER A CB    1 
ATOM   494  C CB    B SER A 1 80  ? 11.691 28.141 26.872 0.50 19.79 ? 71  SER A CB    1 
ATOM   495  O OG    A SER A 1 80  ? 11.472 28.936 26.148 0.50 16.08 ? 71  SER A OG    1 
ATOM   496  O OG    B SER A 1 80  ? 10.375 27.742 26.650 0.50 27.14 ? 71  SER A OG    1 
ATOM   497  N N     . ALA A 1 81  ? 13.676 30.290 28.520 1.00 18.24 ? 72  ALA A N     1 
ATOM   498  C CA    . ALA A 1 81  ? 15.020 30.809 28.255 1.00 18.54 ? 72  ALA A CA    1 
ATOM   499  C C     . ALA A 1 81  ? 15.879 30.903 29.507 1.00 18.25 ? 72  ALA A C     1 
ATOM   500  O O     . ALA A 1 81  ? 15.405 31.183 30.604 1.00 18.66 ? 72  ALA A O     1 
ATOM   501  C CB    . ALA A 1 81  ? 15.014 32.210 27.619 1.00 19.55 ? 72  ALA A CB    1 
ATOM   502  N N     . GLY A 1 82  ? 17.159 30.702 29.279 1.00 18.65 ? 73  GLY A N     1 
ATOM   503  C CA    . GLY A 1 82  ? 18.170 30.908 30.314 1.00 20.68 ? 73  GLY A CA    1 
ATOM   504  C C     . GLY A 1 82  ? 19.454 31.498 29.784 1.00 18.02 ? 73  GLY A C     1 
ATOM   505  O O     . GLY A 1 82  ? 20.509 31.376 30.425 1.00 18.86 ? 73  GLY A O     1 
ATOM   506  N N     . PHE A 1 83  ? 19.378 32.161 28.634 1.00 17.65 ? 74  PHE A N     1 
ATOM   507  C CA    . PHE A 1 83  ? 20.470 32.882 28.002 1.00 17.73 ? 74  PHE A CA    1 
ATOM   508  C C     . PHE A 1 83  ? 19.853 34.143 27.434 1.00 18.57 ? 74  PHE A C     1 
ATOM   509  O O     . PHE A 1 83  ? 18.660 34.166 27.114 1.00 19.12 ? 74  PHE A O     1 
ATOM   510  C CB    . PHE A 1 83  ? 21.096 32.102 26.828 1.00 16.19 ? 74  PHE A CB    1 
ATOM   511  C CG    . PHE A 1 83  ? 22.208 31.152 27.225 1.00 18.73 ? 74  PHE A CG    1 
ATOM   512  C CD1   . PHE A 1 83  ? 21.901 29.921 27.817 1.00 18.94 ? 74  PHE A CD1   1 
ATOM   513  C CD2   . PHE A 1 83  ? 23.550 31.476 26.995 1.00 18.71 ? 74  PHE A CD2   1 
ATOM   514  C CE1   . PHE A 1 83  ? 22.921 29.030 28.197 1.00 18.82 ? 74  PHE A CE1   1 
ATOM   515  C CE2   . PHE A 1 83  ? 24.562 30.595 27.351 1.00 19.94 ? 74  PHE A CE2   1 
ATOM   516  C CZ    . PHE A 1 83  ? 24.237 29.363 27.963 1.00 18.64 ? 74  PHE A CZ    1 
ATOM   517  N N     . PRO A 1 84  ? 20.650 35.176 27.235 1.00 17.92 ? 75  PRO A N     1 
ATOM   518  C CA    . PRO A 1 84  ? 20.121 36.427 26.680 1.00 18.79 ? 75  PRO A CA    1 
ATOM   519  C C     . PRO A 1 84  ? 20.024 36.327 25.172 1.00 16.86 ? 75  PRO A C     1 
ATOM   520  O O     . PRO A 1 84  ? 20.879 35.720 24.521 1.00 17.84 ? 75  PRO A O     1 
ATOM   521  C CB    . PRO A 1 84  ? 21.216 37.445 27.042 1.00 21.34 ? 75  PRO A CB    1 
ATOM   522  C CG    . PRO A 1 84  ? 22.516 36.625 27.052 1.00 18.32 ? 75  PRO A CG    1 
ATOM   523  C CD    . PRO A 1 84  ? 22.086 35.231 27.588 1.00 17.09 ? 75  PRO A CD    1 
ATOM   524  N N     . HIS A 1 85  ? 18.974 36.953 24.614 1.00 19.54 ? 76  HIS A N     1 
ATOM   525  C CA    . HIS A 1 85  ? 18.892 37.145 23.165 1.00 19.42 ? 76  HIS A CA    1 
ATOM   526  C C     . HIS A 1 85  ? 18.955 35.846 22.388 1.00 16.89 ? 76  HIS A C     1 
ATOM   527  O O     . HIS A 1 85  ? 19.598 35.794 21.336 1.00 17.78 ? 76  HIS A O     1 
ATOM   528  C CB    . HIS A 1 85  ? 19.912 38.182 22.712 1.00 20.62 ? 76  HIS A CB    1 
ATOM   529  C CG    . HIS A 1 85  ? 19.816 39.442 23.503 1.00 22.30 ? 76  HIS A CG    1 
ATOM   530  N ND1   . HIS A 1 85  ? 18.624 40.125 23.582 1.00 23.27 ? 76  HIS A ND1   1 
ATOM   531  C CD2   . HIS A 1 85  ? 20.691 40.078 24.311 1.00 27.39 ? 76  HIS A CD2   1 
ATOM   532  C CE1   . HIS A 1 85  ? 18.786 41.165 24.399 1.00 27.74 ? 76  HIS A CE1   1 
ATOM   533  N NE2   . HIS A 1 85  ? 20.029 41.146 24.846 1.00 25.86 ? 76  HIS A NE2   1 
ATOM   534  N N     . VAL A 1 86  ? 18.263 34.856 22.930 1.00 16.91 ? 77  VAL A N     1 
ATOM   535  C CA    . VAL A 1 86  ? 18.055 33.602 22.170 1.00 18.42 ? 77  VAL A CA    1 
ATOM   536  C C     . VAL A 1 86  ? 16.735 33.708 21.410 1.00 17.94 ? 77  VAL A C     1 
ATOM   537  O O     . VAL A 1 86  ? 15.758 34.254 21.936 1.00 17.66 ? 77  VAL A O     1 
ATOM   538  C CB    . VAL A 1 86  ? 18.124 32.377 23.076 1.00 20.51 ? 77  VAL A CB    1 
ATOM   539  C CG1   . VAL A 1 86  ? 19.536 32.321 23.704 1.00 22.09 ? 77  VAL A CG1   1 
ATOM   540  C CG2   . VAL A 1 86  ? 17.039 32.424 24.141 1.00 19.97 ? 77  VAL A CG2   1 
ATOM   541  N N     . PRO A 1 87  ? 16.609 33.141 20.229 1.00 16.51 ? 78  PRO A N     1 
ATOM   542  C CA    . PRO A 1 87  ? 15.343 33.281 19.489 1.00 17.24 ? 78  PRO A CA    1 
ATOM   543  C C     . PRO A 1 87  ? 14.270 32.414 20.091 1.00 17.49 ? 78  PRO A C     1 
ATOM   544  O O     . PRO A 1 87  ? 14.548 31.376 20.709 1.00 17.68 ? 78  PRO A O     1 
ATOM   545  C CB    . PRO A 1 87  ? 15.705 32.793 18.091 1.00 17.38 ? 78  PRO A CB    1 
ATOM   546  C CG    . PRO A 1 87  ? 16.833 31.782 18.301 1.00 17.45 ? 78  PRO A CG    1 
ATOM   547  C CD    . PRO A 1 87  ? 17.612 32.344 19.507 1.00 15.89 ? 78  PRO A CD    1 
ATOM   548  N N     . GLY A 1 88  ? 13.011 32.831 19.930 1.00 18.37 ? 79  GLY A N     1 
ATOM   549  C CA    . GLY A 1 88  ? 11.855 32.000 20.176 1.00 17.72 ? 79  GLY A CA    1 
ATOM   550  C C     . GLY A 1 88  ? 11.176 31.602 18.875 1.00 16.68 ? 79  GLY A C     1 
ATOM   551  O O     . GLY A 1 88  ? 11.480 32.093 17.789 1.00 17.62 ? 79  GLY A O     1 
ATOM   552  N N     . ILE A 1 89  ? 10.241 30.684 19.030 1.00 16.79 ? 80  ILE A N     1 
ATOM   553  C CA    . ILE A 1 89  ? 9.379  30.311 17.902 1.00 19.68 ? 80  ILE A CA    1 
ATOM   554  C C     . ILE A 1 89  ? 7.958  30.118 18.418 1.00 20.82 ? 80  ILE A C     1 
ATOM   555  O O     . ILE A 1 89  ? 7.173  29.349 17.840 1.00 21.63 ? 80  ILE A O     1 
ATOM   556  C CB    . ILE A 1 89  ? 9.969  29.164 17.046 1.00 17.89 ? 80  ILE A CB    1 
ATOM   557  C CG1   . ILE A 1 89  ? 9.324  29.143 15.632 1.00 23.34 ? 80  ILE A CG1   1 
ATOM   558  C CG2   . ILE A 1 89  ? 9.907  27.787 17.761 1.00 20.17 ? 80  ILE A CG2   1 
ATOM   559  C CD1   . ILE A 1 89  ? 10.180 28.447 14.630 1.00 25.86 ? 80  ILE A CD1   1 
ATOM   560  N N     . PHE A 1 90  ? 7.598  30.844 19.456 1.00 19.99 ? 81  PHE A N     1 
ATOM   561  C CA    . PHE A 1 90  ? 6.282  30.727 20.053 1.00 22.98 ? 81  PHE A CA    1 
ATOM   562  C C     . PHE A 1 90  ? 5.350  31.869 19.684 1.00 20.61 ? 81  PHE A C     1 
ATOM   563  O O     . PHE A 1 90  ? 4.173  31.797 20.045 1.00 28.65 ? 81  PHE A O     1 
ATOM   564  C CB    . PHE A 1 90  ? 6.365  30.526 21.599 1.00 23.28 ? 81  PHE A CB    1 
ATOM   565  C CG    . PHE A 1 90  ? 7.094  31.625 22.322 1.00 23.04 ? 81  PHE A CG    1 
ATOM   566  C CD1   . PHE A 1 90  ? 8.478  31.586 22.457 1.00 21.40 ? 81  PHE A CD1   1 
ATOM   567  C CD2   . PHE A 1 90  ? 6.396  32.727 22.831 1.00 23.41 ? 81  PHE A CD2   1 
ATOM   568  C CE1   . PHE A 1 90  ? 9.163  32.600 23.130 1.00 19.85 ? 81  PHE A CE1   1 
ATOM   569  C CE2   . PHE A 1 90  ? 7.041  33.725 23.476 1.00 23.06 ? 81  PHE A CE2   1 
ATOM   570  C CZ    . PHE A 1 90  ? 8.438  33.701 23.609 1.00 24.35 ? 81  PHE A CZ    1 
ATOM   571  N N     . THR A 1 91  ? 5.826  32.900 18.983 1.00 21.08 ? 82  THR A N     1 
ATOM   572  C CA    . THR A 1 91  ? 4.996  34.035 18.563 1.00 22.80 ? 82  THR A CA    1 
ATOM   573  C C     . THR A 1 91  ? 4.987  34.084 17.050 1.00 27.98 ? 82  THR A C     1 
ATOM   574  O O     . THR A 1 91  ? 5.911  33.611 16.383 1.00 24.41 ? 82  THR A O     1 
ATOM   575  C CB    . THR A 1 91  ? 5.483  35.394 19.086 1.00 26.32 ? 82  THR A CB    1 
ATOM   576  O OG1   . THR A 1 91  ? 6.680  35.797 18.412 1.00 23.98 ? 82  THR A OG1   1 
ATOM   577  C CG2   . THR A 1 91  ? 5.693  35.404 20.616 1.00 27.87 ? 82  THR A CG2   1 
ATOM   578  N N     . LYS A 1 92  ? 3.924  34.689 16.513 1.00 27.13 ? 83  LYS A N     1 
ATOM   579  C CA    . LYS A 1 92  ? 3.825  34.798 15.065 1.00 31.46 ? 83  LYS A CA    1 
ATOM   580  C C     . LYS A 1 92  ? 4.847  35.774 14.501 1.00 24.24 ? 83  LYS A C     1 
ATOM   581  O O     . LYS A 1 92  ? 5.355  35.548 13.403 1.00 25.81 ? 83  LYS A O     1 
ATOM   582  C CB    . LYS A 1 92  ? 2.380  35.104 14.647 1.00 33.60 ? 83  LYS A CB    1 
ATOM   583  C CG    . LYS A 1 92  ? 1.397  33.955 14.987 1.00 40.91 ? 83  LYS A CG    1 
ATOM   584  C CD    . LYS A 1 92  ? 1.786  32.578 14.354 1.00 41.46 ? 83  LYS A CD    1 
ATOM   585  C CE    . LYS A 1 92  ? 0.748  31.501 14.742 1.00 48.32 ? 83  LYS A CE    1 
ATOM   586  N NZ    . LYS A 1 92  ? 1.012  30.088 14.265 1.00 42.09 ? 83  LYS A NZ    1 
ATOM   587  N N     . GLU A 1 93  ? 5.234  36.800 15.251 1.00 24.71 ? 84  GLU A N     1 
ATOM   588  C CA    . GLU A 1 93  ? 6.364  37.650 14.854 1.00 24.57 ? 84  GLU A CA    1 
ATOM   589  C C     . GLU A 1 93  ? 7.666  36.852 14.720 1.00 22.63 ? 84  GLU A C     1 
ATOM   590  O O     . GLU A 1 93  ? 8.412  36.997 13.741 1.00 23.49 ? 84  GLU A O     1 
ATOM   591  C CB    . GLU A 1 93  ? 6.543  38.769 15.874 1.00 29.50 ? 84  GLU A CB    1 
ATOM   592  C CG    . GLU A 1 93  ? 7.707  39.656 15.562 1.00 30.62 ? 84  GLU A CG    1 
ATOM   593  C CD    . GLU A 1 93  ? 7.951  40.705 16.643 1.00 38.70 ? 84  GLU A CD    1 
ATOM   594  O OE1   . GLU A 1 93  ? 7.593  40.461 17.825 1.00 40.64 ? 84  GLU A OE1   1 
ATOM   595  O OE2   . GLU A 1 93  ? 8.495  41.777 16.304 1.00 40.52 ? 84  GLU A OE2   1 
ATOM   596  N N     . GLN A 1 94  ? 7.931  35.940 15.664 1.00 21.98 ? 85  GLN A N     1 
ATOM   597  C CA    . GLN A 1 94  ? 9.116  35.114 15.518 1.00 22.81 ? 85  GLN A CA    1 
ATOM   598  C C     . GLN A 1 94  ? 9.047  34.235 14.280 1.00 19.64 ? 85  GLN A C     1 
ATOM   599  O O     . GLN A 1 94  ? 10.065 34.060 13.589 1.00 20.45 ? 85  GLN A O     1 
ATOM   600  C CB    . GLN A 1 94  ? 9.295  34.273 16.777 1.00 20.25 ? 85  GLN A CB    1 
ATOM   601  C CG    . GLN A 1 94  ? 9.693  35.138 17.989 1.00 20.32 ? 85  GLN A CG    1 
ATOM   602  C CD    . GLN A 1 94  ? 9.356  34.469 19.299 1.00 19.23 ? 85  GLN A CD    1 
ATOM   603  O OE1   . GLN A 1 94  ? 8.723  33.413 19.344 1.00 18.97 ? 85  GLN A OE1   1 
ATOM   604  N NE2   . GLN A 1 94  ? 9.779  35.064 20.398 1.00 23.20 ? 85  GLN A NE2   1 
ATOM   605  N N     . VAL A 1 95  ? 7.866  33.639 14.006 1.00 19.12 ? 86  VAL A N     1 
ATOM   606  C CA    . VAL A 1 95  ? 7.686  32.801 12.807 1.00 18.83 ? 86  VAL A CA    1 
ATOM   607  C C     . VAL A 1 95  ? 7.985  33.590 11.547 1.00 18.71 ? 86  VAL A C     1 
ATOM   608  O O     . VAL A 1 95  ? 8.699  33.126 10.654 1.00 21.82 ? 86  VAL A O     1 
ATOM   609  C CB    . VAL A 1 95  ? 6.258  32.219 12.763 1.00 22.85 ? 86  VAL A CB    1 
ATOM   610  C CG1   . VAL A 1 95  ? 5.951  31.507 11.419 1.00 23.96 ? 86  VAL A CG1   1 
ATOM   611  C CG2   . VAL A 1 95  ? 6.056  31.219 13.917 1.00 23.21 ? 86  VAL A CG2   1 
ATOM   612  N N     . ARG A 1 96  ? 7.446  34.818 11.472 1.00 20.81 ? 87  ARG A N     1 
ATOM   613  C CA    . ARG A 1 96  ? 7.683  35.642 10.289 1.00 23.63 ? 87  ARG A CA    1 
ATOM   614  C C     . ARG A 1 96  ? 9.163  35.885 10.068 1.00 22.07 ? 87  ARG A C     1 
ATOM   615  O O     . ARG A 1 96  ? 9.647  35.850 8.927  1.00 21.92 ? 87  ARG A O     1 
ATOM   616  C CB    . ARG A 1 96  ? 6.956  36.979 10.456 1.00 26.89 ? 87  ARG A CB    1 
ATOM   617  C CG    . ARG A 1 96  ? 5.465  36.864 10.266 1.00 43.01 ? 87  ARG A CG    1 
ATOM   618  C CD    . ARG A 1 96  ? 4.862  38.224 9.990  1.00 45.63 ? 87  ARG A CD    1 
ATOM   619  N NE    . ARG A 1 96  ? 5.046  39.135 11.117 1.00 39.16 ? 87  ARG A NE    1 
ATOM   620  C CZ    . ARG A 1 96  ? 4.268  39.169 12.192 1.00 38.05 ? 87  ARG A CZ    1 
ATOM   621  N NH1   . ARG A 1 96  ? 3.233  38.346 12.327 1.00 43.35 ? 87  ARG A NH1   1 
ATOM   622  N NH2   . ARG A 1 96  ? 4.534  40.050 13.154 1.00 39.54 ? 87  ARG A NH2   1 
ATOM   623  N N     . GLU A 1 97  ? 9.909  36.166 11.149 1.00 19.03 ? 88  GLU A N     1 
ATOM   624  C CA    . GLU A 1 97  ? 11.321 36.464 10.950 1.00 18.64 ? 88  GLU A CA    1 
ATOM   625  C C     . GLU A 1 97  ? 12.132 35.202 10.667 1.00 19.61 ? 88  GLU A C     1 
ATOM   626  O O     . GLU A 1 97  ? 13.074 35.228 9.874  1.00 20.36 ? 88  GLU A O     1 
ATOM   627  C CB    . GLU A 1 97  ? 11.891 37.197 12.186 1.00 20.51 ? 88  GLU A CB    1 
ATOM   628  C CG    . GLU A 1 97  ? 11.235 38.595 12.389 1.00 24.77 ? 88  GLU A CG    1 
ATOM   629  C CD    . GLU A 1 97  ? 11.171 39.376 11.081 1.00 30.02 ? 88  GLU A CD    1 
ATOM   630  O OE1   . GLU A 1 97  ? 10.046 39.702 10.640 1.00 39.57 ? 88  GLU A OE1   1 
ATOM   631  O OE2   . GLU A 1 97  ? 12.245 39.690 10.496 1.00 31.67 ? 88  GLU A OE2   1 
ATOM   632  N N     . TRP A 1 98  ? 11.759 34.080 11.295 1.00 19.07 ? 89  TRP A N     1 
ATOM   633  C CA    . TRP A 1 98  ? 12.454 32.832 10.952 1.00 19.39 ? 89  TRP A CA    1 
ATOM   634  C C     . TRP A 1 98  ? 12.276 32.471 9.488  1.00 18.59 ? 89  TRP A C     1 
ATOM   635  O O     . TRP A 1 98  ? 13.179 31.886 8.891  1.00 20.60 ? 89  TRP A O     1 
ATOM   636  C CB    . TRP A 1 98  ? 11.910 31.677 11.797 1.00 17.65 ? 89  TRP A CB    1 
ATOM   637  C CG    . TRP A 1 98  ? 12.577 31.469 13.123 1.00 19.02 ? 89  TRP A CG    1 
ATOM   638  C CD1   . TRP A 1 98  ? 11.963 31.511 14.337 1.00 17.99 ? 89  TRP A CD1   1 
ATOM   639  C CD2   . TRP A 1 98  ? 13.941 31.122 13.347 1.00 16.94 ? 89  TRP A CD2   1 
ATOM   640  N NE1   . TRP A 1 98  ? 12.881 31.175 15.348 1.00 18.23 ? 89  TRP A NE1   1 
ATOM   641  C CE2   . TRP A 1 98  ? 14.094 30.961 14.746 1.00 16.13 ? 89  TRP A CE2   1 
ATOM   642  C CE3   . TRP A 1 98  ? 15.055 30.961 12.514 1.00 17.47 ? 89  TRP A CE3   1 
ATOM   643  C CZ2   . TRP A 1 98  ? 15.324 30.560 15.321 1.00 16.64 ? 89  TRP A CZ2   1 
ATOM   644  C CZ3   . TRP A 1 98  ? 16.291 30.583 13.096 1.00 16.96 ? 89  TRP A CZ3   1 
ATOM   645  C CH2   . TRP A 1 98  ? 16.407 30.423 14.502 1.00 17.32 ? 89  TRP A CH2   1 
ATOM   646  N N     . LYS A 1 99  ? 11.086 32.725 8.920  1.00 21.08 ? 90  LYS A N     1 
ATOM   647  C CA    . LYS A 1 99  ? 10.823 32.372 7.532  1.00 19.53 ? 90  LYS A CA    1 
ATOM   648  C C     . LYS A 1 99  ? 11.852 32.984 6.614  1.00 19.52 ? 90  LYS A C     1 
ATOM   649  O O     . LYS A 1 99  ? 12.293 32.338 5.664  1.00 20.75 ? 90  LYS A O     1 
ATOM   650  C CB    . LYS A 1 99  ? 9.413  32.848 7.148  1.00 23.48 ? 90  LYS A CB    1 
ATOM   651  C CG    . LYS A 1 99  ? 8.990  32.383 5.762  1.00 34.54 ? 90  LYS A CG    1 
ATOM   652  C CD    . LYS A 1 99  ? 7.529  32.697 5.508  1.00 47.65 ? 90  LYS A CD    1 
ATOM   653  C CE    . LYS A 1 99  ? 7.077  32.035 4.208  1.00 64.08 ? 90  LYS A CE    1 
ATOM   654  N NZ    . LYS A 1 99  ? 8.046  32.362 3.090  1.00 54.94 ? 90  LYS A NZ    1 
ATOM   655  N N     . LYS A 1 100 ? 12.289 34.222 6.918  1.00 22.28 ? 91  LYS A N     1 
ATOM   656  C CA    . LYS A 1 100 ? 13.276 34.886 6.067  1.00 21.15 ? 91  LYS A CA    1 
ATOM   657  C C     . LYS A 1 100 ? 14.621 34.180 6.127  1.00 23.81 ? 91  LYS A C     1 
ATOM   658  O O     . LYS A 1 100 ? 15.331 34.099 5.121  1.00 24.90 ? 91  LYS A O     1 
ATOM   659  C CB    . LYS A 1 100 ? 13.406 36.360 6.456  1.00 23.81 ? 91  LYS A CB    1 
ATOM   660  C CG    . LYS A 1 100 ? 12.067 37.073 6.378  1.00 27.53 ? 91  LYS A CG    1 
ATOM   661  C CD    . LYS A 1 100 ? 11.898 38.146 7.425  1.00 45.92 ? 91  LYS A CD    1 
ATOM   662  C CE    . LYS A 1 100 ? 11.340 39.412 6.860  1.00 43.45 ? 91  LYS A CE    1 
ATOM   663  N NZ    . LYS A 1 100 ? 11.659 40.566 7.753  1.00 48.54 ? 91  LYS A NZ    1 
ATOM   664  N N     . ILE A 1 101 ? 14.956 33.611 7.297  1.00 20.85 ? 92  ILE A N     1 
ATOM   665  C CA    . ILE A 1 101 ? 16.207 32.876 7.468  1.00 21.11 ? 92  ILE A CA    1 
ATOM   666  C C     . ILE A 1 101 ? 16.126 31.525 6.782  1.00 19.79 ? 92  ILE A C     1 
ATOM   667  O O     . ILE A 1 101 ? 17.055 31.107 6.062  1.00 20.57 ? 92  ILE A O     1 
ATOM   668  C CB    . ILE A 1 101 ? 16.494 32.740 8.981  1.00 20.06 ? 92  ILE A CB    1 
ATOM   669  C CG1   . ILE A 1 101 ? 16.777 34.128 9.537  1.00 22.33 ? 92  ILE A CG1   1 
ATOM   670  C CG2   . ILE A 1 101 ? 17.643 31.767 9.209  1.00 23.35 ? 92  ILE A CG2   1 
ATOM   671  C CD1   . ILE A 1 101 ? 16.552 34.145 11.028 1.00 21.99 ? 92  ILE A CD1   1 
ATOM   672  N N     . VAL A 1 102 ? 14.991 30.834 6.952  1.00 20.21 ? 93  VAL A N     1 
ATOM   673  C CA    . VAL A 1 102 ? 14.831 29.520 6.325  1.00 20.05 ? 93  VAL A CA    1 
ATOM   674  C C     . VAL A 1 102 ? 14.879 29.672 4.809  1.00 19.96 ? 93  VAL A C     1 
ATOM   675  O O     . VAL A 1 102 ? 15.475 28.839 4.110  1.00 20.70 ? 93  VAL A O     1 
ATOM   676  C CB    . VAL A 1 102 ? 13.510 28.893 6.784  1.00 21.35 ? 93  VAL A CB    1 
ATOM   677  C CG1   . VAL A 1 102 ? 13.223 27.625 6.012  1.00 23.12 ? 93  VAL A CG1   1 
ATOM   678  C CG2   . VAL A 1 102 ? 13.580 28.556 8.281  1.00 21.09 ? 93  VAL A CG2   1 
ATOM   679  N N     . ASP A 1 103 ? 14.340 30.782 4.296  1.00 22.89 ? 94  ASP A N     1 
ATOM   680  C CA    . ASP A 1 103 ? 14.293 30.922 2.836  1.00 20.99 ? 94  ASP A CA    1 
ATOM   681  C C     . ASP A 1 103 ? 15.693 31.054 2.257  1.00 20.43 ? 94  ASP A C     1 
ATOM   682  O O     . ASP A 1 103 ? 16.001 30.473 1.201  1.00 23.40 ? 94  ASP A O     1 
ATOM   683  C CB    . ASP A 1 103 ? 13.452 32.143 2.498  1.00 24.97 ? 94  ASP A CB    1 
ATOM   684  C CG    . ASP A 1 103 ? 11.952 31.836 2.519  1.00 36.11 ? 94  ASP A CG    1 
ATOM   685  O OD1   . ASP A 1 103 ? 11.595 30.651 2.762  1.00 33.45 ? 94  ASP A OD1   1 
ATOM   686  O OD2   . ASP A 1 103 ? 11.146 32.806 2.412  1.00 41.17 ? 94  ASP A OD2   1 
ATOM   687  N N     . VAL A 1 104 ? 16.570 31.841 2.898  1.00 21.26 ? 95  VAL A N     1 
ATOM   688  C CA    . VAL A 1 104 ? 17.924 31.968 2.364  1.00 20.14 ? 95  VAL A CA    1 
ATOM   689  C C     . VAL A 1 104 ? 18.724 30.666 2.470  1.00 22.04 ? 95  VAL A C     1 
ATOM   690  O O     . VAL A 1 104 ? 19.622 30.398 1.644  1.00 23.39 ? 95  VAL A O     1 
ATOM   691  C CB    . VAL A 1 104 ? 18.710 33.182 2.894  1.00 21.81 ? 95  VAL A CB    1 
ATOM   692  C CG1   . VAL A 1 104 ? 17.951 34.470 2.632  1.00 27.92 ? 95  VAL A CG1   1 
ATOM   693  C CG2   . VAL A 1 104 ? 19.024 33.074 4.399  1.00 24.59 ? 95  VAL A CG2   1 
ATOM   694  N N     . VAL A 1 105 ? 18.451 29.840 3.493  1.00 20.28 ? 96  VAL A N     1 
ATOM   695  C CA    . VAL A 1 105 ? 19.129 28.549 3.602  1.00 18.89 ? 96  VAL A CA    1 
ATOM   696  C C     . VAL A 1 105 ? 18.633 27.589 2.521  1.00 18.75 ? 96  VAL A C     1 
ATOM   697  O O     . VAL A 1 105 ? 19.417 26.858 1.899  1.00 19.67 ? 96  VAL A O     1 
ATOM   698  C CB    . VAL A 1 105 ? 18.924 28.003 5.038  1.00 20.71 ? 96  VAL A CB    1 
ATOM   699  C CG1   . VAL A 1 105 ? 19.363 26.558 5.186  1.00 23.05 ? 96  VAL A CG1   1 
ATOM   700  C CG2   . VAL A 1 105 ? 19.754 28.902 6.010  1.00 22.02 ? 96  VAL A CG2   1 
ATOM   701  N N     . HIS A 1 106 ? 17.326 27.577 2.303  1.00 19.74 ? 97  HIS A N     1 
ATOM   702  C CA    . HIS A 1 106 ? 16.799 26.696 1.266  1.00 20.12 ? 97  HIS A CA    1 
ATOM   703  C C     . HIS A 1 106 ? 17.216 27.168 -0.110 1.00 22.97 ? 97  HIS A C     1 
ATOM   704  O O     . HIS A 1 106 ? 17.318 26.342 -1.014 1.00 21.91 ? 97  HIS A O     1 
ATOM   705  C CB    . HIS A 1 106 ? 15.295 26.696 1.363  1.00 20.86 ? 97  HIS A CB    1 
ATOM   706  C CG    . HIS A 1 106 ? 14.775 25.811 2.437  1.00 20.61 ? 97  HIS A CG    1 
ATOM   707  N ND1   . HIS A 1 106 ? 13.483 25.868 2.891  1.00 25.06 ? 97  HIS A ND1   1 
ATOM   708  C CD2   . HIS A 1 106 ? 15.384 24.820 3.132  1.00 21.21 ? 97  HIS A CD2   1 
ATOM   709  C CE1   . HIS A 1 106 ? 13.311 24.958 3.841  1.00 23.86 ? 97  HIS A CE1   1 
ATOM   710  N NE2   . HIS A 1 106 ? 14.444 24.287 3.975  1.00 22.07 ? 97  HIS A NE2   1 
ATOM   711  N N     . ALA A 1 107 ? 17.485 28.457 -0.282 1.00 20.44 ? 98  ALA A N     1 
ATOM   712  C CA    . ALA A 1 107 ? 17.955 28.877 -1.600 1.00 21.19 ? 98  ALA A CA    1 
ATOM   713  C C     . ALA A 1 107 ? 19.306 28.268 -1.929 1.00 22.87 ? 98  ALA A C     1 
ATOM   714  O O     . ALA A 1 107 ? 19.676 28.197 -3.114 1.00 27.44 ? 98  ALA A O     1 
ATOM   715  C CB    . ALA A 1 107 ? 18.053 30.390 -1.624 1.00 22.42 ? 98  ALA A CB    1 
ATOM   716  N N     . LYS A 1 108 ? 20.074 27.838 -0.934 1.00 22.81 ? 99  LYS A N     1 
ATOM   717  C CA    . LYS A 1 108 ? 21.320 27.169 -1.195 1.00 24.35 ? 99  LYS A CA    1 
ATOM   718  C C     . LYS A 1 108 ? 21.177 25.663 -1.257 1.00 19.94 ? 99  LYS A C     1 
ATOM   719  O O     . LYS A 1 108 ? 22.191 25.015 -1.486 1.00 27.46 ? 99  LYS A O     1 
ATOM   720  C CB    . LYS A 1 108 ? 22.390 27.590 -0.210 1.00 26.87 ? 99  LYS A CB    1 
ATOM   721  C CG    . LYS A 1 108 ? 22.754 29.050 -0.403 1.00 40.77 ? 99  LYS A CG    1 
ATOM   722  C CD    . LYS A 1 108 ? 23.893 29.488 0.460  1.00 36.12 ? 99  LYS A CD    1 
ATOM   723  C CE    . LYS A 1 108 ? 25.198 28.849 0.067  1.00 39.42 ? 99  LYS A CE    1 
ATOM   724  N NZ    . LYS A 1 108 ? 26.281 29.374 0.973  1.00 34.93 ? 99  LYS A NZ    1 
ATOM   725  N N     . GLY A 1 109 ? 19.957 25.124 -1.131 1.00 20.44 ? 100 GLY A N     1 
ATOM   726  C CA    . GLY A 1 109 ? 19.729 23.689 -1.199 1.00 21.47 ? 100 GLY A CA    1 
ATOM   727  C C     . GLY A 1 109 ? 20.014 22.938 0.089  1.00 20.30 ? 100 GLY A C     1 
ATOM   728  O O     . GLY A 1 109 ? 20.185 21.716 0.049  1.00 22.11 ? 100 GLY A O     1 
ATOM   729  N N     . ALA A 1 110 ? 20.097 23.638 1.217  1.00 19.74 ? 101 ALA A N     1 
ATOM   730  C CA    . ALA A 1 110 ? 20.360 22.967 2.479  1.00 19.76 ? 101 ALA A CA    1 
ATOM   731  C C     . ALA A 1 110 ? 19.051 22.575 3.149  1.00 20.78 ? 101 ALA A C     1 
ATOM   732  O O     . ALA A 1 110 ? 17.983 23.078 2.835  1.00 22.63 ? 101 ALA A O     1 
ATOM   733  C CB    . ALA A 1 110 ? 21.180 23.884 3.396  1.00 22.06 ? 101 ALA A CB    1 
ATOM   734  N N     . VAL A 1 111 ? 19.144 21.605 4.083  1.00 18.62 ? 102 VAL A N     1 
ATOM   735  C CA    . VAL A 1 111 ? 18.026 21.185 4.922  1.00 16.68 ? 102 VAL A CA    1 
ATOM   736  C C     . VAL A 1 111 ? 18.245 21.784 6.300  1.00 17.81 ? 102 VAL A C     1 
ATOM   737  O O     . VAL A 1 111 ? 19.379 21.796 6.774  1.00 19.38 ? 102 VAL A O     1 
ATOM   738  C CB    . VAL A 1 111 ? 17.977 19.653 5.009  1.00 17.74 ? 102 VAL A CB    1 
ATOM   739  C CG1   . VAL A 1 111 ? 16.913 19.205 5.978  1.00 19.13 ? 102 VAL A CG1   1 
ATOM   740  C CG2   . VAL A 1 111 ? 17.726 19.072 3.599  1.00 22.13 ? 102 VAL A CG2   1 
ATOM   741  N N     . ILE A 1 112 ? 17.197 22.292 6.935  1.00 17.28 ? 103 ILE A N     1 
ATOM   742  C CA    . ILE A 1 112 ? 17.407 22.962 8.227  1.00 16.20 ? 103 ILE A CA    1 
ATOM   743  C C     . ILE A 1 112 ? 16.324 22.560 9.203  1.00 16.94 ? 103 ILE A C     1 
ATOM   744  O O     . ILE A 1 112 ? 15.131 22.626 8.898  1.00 17.08 ? 103 ILE A O     1 
ATOM   745  C CB    . ILE A 1 112 ? 17.598 24.483 8.085  1.00 16.62 ? 103 ILE A CB    1 
ATOM   746  C CG1   . ILE A 1 112 ? 17.807 25.143 9.451  1.00 17.67 ? 103 ILE A CG1   1 
ATOM   747  C CG2   . ILE A 1 112 ? 16.385 25.120 7.375  1.00 19.87 ? 103 ILE A CG2   1 
ATOM   748  C CD1   . ILE A 1 112 ? 18.319 26.622 9.297  1.00 21.69 ? 103 ILE A CD1   1 
ATOM   749  N N     . PHE A 1 113 ? 16.734 22.146 10.403 1.00 16.76 ? 104 PHE A N     1 
ATOM   750  C CA    . PHE A 1 113 ? 15.816 21.869 11.502 1.00 15.76 ? 104 PHE A CA    1 
ATOM   751  C C     . PHE A 1 113 ? 15.976 22.925 12.588 1.00 16.27 ? 104 PHE A C     1 
ATOM   752  O O     . PHE A 1 113 ? 17.090 23.373 12.846 1.00 17.74 ? 104 PHE A O     1 
ATOM   753  C CB    . PHE A 1 113 ? 16.174 20.512 12.128 1.00 16.35 ? 104 PHE A CB    1 
ATOM   754  C CG    . PHE A 1 113 ? 15.556 19.286 11.457 1.00 15.40 ? 104 PHE A CG    1 
ATOM   755  C CD1   . PHE A 1 113 ? 15.270 19.250 10.060 1.00 17.66 ? 104 PHE A CD1   1 
ATOM   756  C CD2   . PHE A 1 113 ? 15.341 18.153 12.208 1.00 18.14 ? 104 PHE A CD2   1 
ATOM   757  C CE1   . PHE A 1 113 ? 14.681 18.109 9.491  1.00 18.05 ? 104 PHE A CE1   1 
ATOM   758  C CE2   . PHE A 1 113 ? 14.811 16.975 11.633 1.00 19.36 ? 104 PHE A CE2   1 
ATOM   759  C CZ    . PHE A 1 113 ? 14.482 16.939 10.256 1.00 17.33 ? 104 PHE A CZ    1 
ATOM   760  N N     . CYS A 1 114 ? 14.888 23.262 13.255 1.00 15.75 ? 105 CYS A N     1 
ATOM   761  C CA    . CYS A 1 114 ? 14.914 24.171 14.377 1.00 15.44 ? 105 CYS A CA    1 
ATOM   762  C C     . CYS A 1 114 ? 15.005 23.374 15.665 1.00 16.38 ? 105 CYS A C     1 
ATOM   763  O O     . CYS A 1 114 ? 14.144 22.531 15.907 1.00 16.35 ? 105 CYS A O     1 
ATOM   764  C CB    . CYS A 1 114 ? 13.604 24.957 14.387 1.00 16.56 ? 105 CYS A CB    1 
ATOM   765  S SG    . CYS A 1 114 ? 13.488 26.169 15.760 1.00 18.76 ? 105 CYS A SG    1 
ATOM   766  N N     . GLN A 1 115 ? 15.987 23.695 16.539 1.00 15.56 ? 106 GLN A N     1 
ATOM   767  C CA    . GLN A 1 115 ? 16.078 22.992 17.816 1.00 15.68 ? 106 GLN A CA    1 
ATOM   768  C C     . GLN A 1 115 ? 15.166 23.659 18.832 1.00 15.14 ? 106 GLN A C     1 
ATOM   769  O O     . GLN A 1 115 ? 15.294 24.881 19.095 1.00 17.06 ? 106 GLN A O     1 
ATOM   770  C CB    . GLN A 1 115 ? 17.514 23.012 18.333 1.00 15.33 ? 106 GLN A CB    1 
ATOM   771  C CG    . GLN A 1 115 ? 17.574 22.189 19.651 1.00 17.41 ? 106 GLN A CG    1 
ATOM   772  C CD    . GLN A 1 115 ? 18.883 22.297 20.381 1.00 15.19 ? 106 GLN A CD    1 
ATOM   773  O OE1   . GLN A 1 115 ? 19.221 23.362 20.919 1.00 16.55 ? 106 GLN A OE1   1 
ATOM   774  N NE2   . GLN A 1 115 ? 19.588 21.177 20.463 1.00 15.79 ? 106 GLN A NE2   1 
ATOM   775  N N     . LEU A 1 116 ? 14.271 22.869 19.447 1.00 14.17 ? 107 LEU A N     1 
ATOM   776  C CA    . LEU A 1 116 ? 13.315 23.406 20.427 1.00 16.26 ? 107 LEU A CA    1 
ATOM   777  C C     . LEU A 1 116 ? 13.897 23.210 21.823 1.00 15.18 ? 107 LEU A C     1 
ATOM   778  O O     . LEU A 1 116 ? 14.161 22.058 22.213 1.00 15.88 ? 107 LEU A O     1 
ATOM   779  C CB    . LEU A 1 116 ? 11.961 22.693 20.326 1.00 15.87 ? 107 LEU A CB    1 
ATOM   780  C CG    . LEU A 1 116 ? 11.278 22.737 18.922 1.00 16.50 ? 107 LEU A CG    1 
ATOM   781  C CD1   . LEU A 1 116 ? 9.917  22.094 19.048 1.00 19.47 ? 107 LEU A CD1   1 
ATOM   782  C CD2   . LEU A 1 116 ? 11.157 24.182 18.472 1.00 17.95 ? 107 LEU A CD2   1 
ATOM   783  N N     . TRP A 1 117 ? 14.012 24.295 22.584 1.00 16.74 ? 108 TRP A N     1 
ATOM   784  C CA    . TRP A 1 117 ? 14.831 24.285 23.807 1.00 17.41 ? 108 TRP A CA    1 
ATOM   785  C C     . TRP A 1 117 ? 14.067 24.888 24.967 1.00 16.29 ? 108 TRP A C     1 
ATOM   786  O O     . TRP A 1 117 ? 13.695 26.078 24.906 1.00 18.04 ? 108 TRP A O     1 
ATOM   787  C CB    . TRP A 1 117 ? 16.065 25.158 23.573 1.00 17.03 ? 108 TRP A CB    1 
ATOM   788  C CG    . TRP A 1 117 ? 17.134 25.188 24.664 1.00 15.66 ? 108 TRP A CG    1 
ATOM   789  C CD1   . TRP A 1 117 ? 17.384 24.233 25.624 1.00 16.92 ? 108 TRP A CD1   1 
ATOM   790  C CD2   . TRP A 1 117 ? 18.135 26.187 24.775 1.00 17.78 ? 108 TRP A CD2   1 
ATOM   791  N NE1   . TRP A 1 117 ? 18.502 24.623 26.341 1.00 17.47 ? 108 TRP A NE1   1 
ATOM   792  C CE2   . TRP A 1 117 ? 18.970 25.811 25.847 1.00 16.73 ? 108 TRP A CE2   1 
ATOM   793  C CE3   . TRP A 1 117 ? 18.373 27.415 24.131 1.00 17.20 ? 108 TRP A CE3   1 
ATOM   794  C CZ2   . TRP A 1 117 ? 20.057 26.600 26.229 1.00 20.18 ? 108 TRP A CZ2   1 
ATOM   795  C CZ3   . TRP A 1 117 ? 19.490 28.184 24.496 1.00 19.40 ? 108 TRP A CZ3   1 
ATOM   796  C CH2   . TRP A 1 117 ? 20.303 27.776 25.537 1.00 18.86 ? 108 TRP A CH2   1 
ATOM   797  N N     . HIS A 1 118 ? 13.941 24.133 26.060 1.00 15.93 ? 109 HIS A N     1 
ATOM   798  C CA    . HIS A 1 118 ? 13.492 24.659 27.335 1.00 16.99 ? 109 HIS A CA    1 
ATOM   799  C C     . HIS A 1 118 ? 14.585 24.366 28.364 1.00 14.99 ? 109 HIS A C     1 
ATOM   800  O O     . HIS A 1 118 ? 14.989 23.201 28.552 1.00 15.83 ? 109 HIS A O     1 
ATOM   801  C CB    . HIS A 1 118 ? 12.161 24.008 27.729 1.00 16.36 ? 109 HIS A CB    1 
ATOM   802  C CG    . HIS A 1 118 ? 11.472 24.732 28.838 1.00 16.83 ? 109 HIS A CG    1 
ATOM   803  N ND1   . HIS A 1 118 ? 12.071 25.024 30.044 1.00 17.85 ? 109 HIS A ND1   1 
ATOM   804  C CD2   . HIS A 1 118 ? 10.232 25.276 28.886 1.00 19.02 ? 109 HIS A CD2   1 
ATOM   805  C CE1   . HIS A 1 118 ? 11.219 25.691 30.812 1.00 17.99 ? 109 HIS A CE1   1 
ATOM   806  N NE2   . HIS A 1 118 ? 10.088 25.854 30.130 1.00 19.11 ? 109 HIS A NE2   1 
ATOM   807  N N     . VAL A 1 119 ? 15.046 25.426 29.049 1.00 15.22 ? 110 VAL A N     1 
ATOM   808  C CA    . VAL A 1 119 ? 16.158 25.274 30.001 1.00 15.53 ? 110 VAL A CA    1 
ATOM   809  C C     . VAL A 1 119 ? 15.771 24.772 31.379 1.00 17.85 ? 110 VAL A C     1 
ATOM   810  O O     . VAL A 1 119 ? 16.674 24.420 32.147 1.00 15.80 ? 110 VAL A O     1 
ATOM   811  C CB    . VAL A 1 119 ? 16.888 26.608 30.229 1.00 16.29 ? 110 VAL A CB    1 
ATOM   812  C CG1   . VAL A 1 119 ? 17.491 27.113 28.914 1.00 16.99 ? 110 VAL A CG1   1 
ATOM   813  C CG2   . VAL A 1 119 ? 15.973 27.678 30.858 1.00 17.20 ? 110 VAL A CG2   1 
ATOM   814  N N     . GLY A 1 120 ? 14.482 24.692 31.695 1.00 16.39 ? 111 GLY A N     1 
ATOM   815  C CA    . GLY A 1 120 ? 14.046 24.340 33.045 1.00 17.15 ? 111 GLY A CA    1 
ATOM   816  C C     . GLY A 1 120 ? 14.722 25.193 34.110 1.00 16.47 ? 111 GLY A C     1 
ATOM   817  O O     . GLY A 1 120 ? 14.707 26.419 34.053 1.00 17.62 ? 111 GLY A O     1 
ATOM   818  N N     . ARG A 1 121 ? 15.355 24.518 35.079 1.00 16.97 ? 112 ARG A N     1 
ATOM   819  C CA    . ARG A 1 121 ? 15.934 25.224 36.225 1.00 17.08 ? 112 ARG A CA    1 
ATOM   820  C C     . ARG A 1 121 ? 17.180 26.013 35.883 1.00 18.11 ? 112 ARG A C     1 
ATOM   821  O O     . ARG A 1 121 ? 17.646 26.778 36.731 1.00 18.44 ? 112 ARG A O     1 
ATOM   822  C CB    . ARG A 1 121 ? 16.224 24.243 37.366 1.00 17.12 ? 112 ARG A CB    1 
ATOM   823  C CG    . ARG A 1 121 ? 17.429 23.369 37.139 1.00 15.50 ? 112 ARG A CG    1 
ATOM   824  C CD    . ARG A 1 121 ? 17.599 22.372 38.322 1.00 18.57 ? 112 ARG A CD    1 
ATOM   825  N NE    . ARG A 1 121 ? 18.752 21.535 38.106 1.00 17.24 ? 112 ARG A NE    1 
ATOM   826  C CZ    . ARG A 1 121 ? 19.348 20.834 39.064 1.00 17.19 ? 112 ARG A CZ    1 
ATOM   827  N NH1   . ARG A 1 121 ? 18.840 20.792 40.286 1.00 18.95 ? 112 ARG A NH1   1 
ATOM   828  N NH2   . ARG A 1 121 ? 20.454 20.178 38.772 1.00 20.00 ? 112 ARG A NH2   1 
ATOM   829  N N     . ALA A 1 122 ? 17.710 25.906 34.675 1.00 16.27 ? 113 ALA A N     1 
ATOM   830  C CA    . ALA A 1 122 ? 18.941 26.600 34.306 1.00 15.76 ? 113 ALA A CA    1 
ATOM   831  C C     . ALA A 1 122 ? 18.600 27.975 33.769 1.00 17.52 ? 113 ALA A C     1 
ATOM   832  O O     . ALA A 1 122 ? 18.754 28.287 32.580 1.00 18.49 ? 113 ALA A O     1 
ATOM   833  C CB    . ALA A 1 122 ? 19.721 25.812 33.267 1.00 17.97 ? 113 ALA A CB    1 
ATOM   834  N N     . SER A 1 123 ? 18.030 28.766 34.656 1.00 19.17 ? 114 SER A N     1 
ATOM   835  C CA    . SER A 1 123 ? 17.575 30.093 34.281 1.00 17.09 ? 114 SER A CA    1 
ATOM   836  C C     . SER A 1 123 ? 17.751 30.993 35.487 1.00 19.12 ? 114 SER A C     1 
ATOM   837  O O     . SER A 1 123 ? 18.438 30.608 36.437 1.00 20.18 ? 114 SER A O     1 
ATOM   838  C CB    . SER A 1 123 ? 16.104 30.066 33.831 1.00 19.54 ? 114 SER A CB    1 
ATOM   839  O OG    . SER A 1 123 ? 15.727 31.317 33.248 1.00 18.25 ? 114 SER A OG    1 
ATOM   840  N N     . HIS A 1 124 ? 17.165 32.194 35.421 1.00 19.18 ? 115 HIS A N     1 
ATOM   841  C CA    . HIS A 1 124 ? 17.323 33.206 36.473 1.00 18.45 ? 115 HIS A CA    1 
ATOM   842  C C     . HIS A 1 124 ? 16.122 34.111 36.370 1.00 23.04 ? 115 HIS A C     1 
ATOM   843  O O     . HIS A 1 124 ? 15.501 34.220 35.310 1.00 20.27 ? 115 HIS A O     1 
ATOM   844  C CB    . HIS A 1 124 ? 18.599 33.996 36.200 1.00 20.51 ? 115 HIS A CB    1 
ATOM   845  C CG    . HIS A 1 124 ? 19.034 34.932 37.270 1.00 20.14 ? 115 HIS A CG    1 
ATOM   846  N ND1   . HIS A 1 124 ? 18.489 36.182 37.407 1.00 24.42 ? 115 HIS A ND1   1 
ATOM   847  C CD2   . HIS A 1 124 ? 20.021 34.826 38.190 1.00 22.69 ? 115 HIS A CD2   1 
ATOM   848  C CE1   . HIS A 1 124 ? 19.073 36.784 38.438 1.00 24.88 ? 115 HIS A CE1   1 
ATOM   849  N NE2   . HIS A 1 124 ? 20.018 35.994 38.917 1.00 25.52 ? 115 HIS A NE2   1 
ATOM   850  N N     . GLU A 1 125 ? 15.842 34.829 37.462 1.00 24.63 ? 116 GLU A N     1 
ATOM   851  C CA    . GLU A 1 125 ? 14.723 35.763 37.435 1.00 28.22 ? 116 GLU A CA    1 
ATOM   852  C C     . GLU A 1 125 ? 14.820 36.754 36.268 1.00 21.52 ? 116 GLU A C     1 
ATOM   853  O O     . GLU A 1 125 ? 13.794 37.158 35.697 1.00 25.33 ? 116 GLU A O     1 
ATOM   854  C CB    . GLU A 1 125 ? 14.666 36.522 38.773 1.00 28.73 ? 116 GLU A CB    1 
ATOM   855  N N     . VAL A 1 126 ? 16.033 37.183 35.922 1.00 21.22 ? 117 VAL A N     1 
ATOM   856  C CA    . VAL A 1 126 ? 16.186 38.169 34.865 1.00 21.67 ? 117 VAL A CA    1 
ATOM   857  C C     . VAL A 1 126 ? 15.649 37.656 33.521 1.00 19.20 ? 117 VAL A C     1 
ATOM   858  O O     . VAL A 1 126 ? 15.344 38.451 32.632 1.00 24.40 ? 117 VAL A O     1 
ATOM   859  C CB    . VAL A 1 126 ? 17.645 38.647 34.728 1.00 23.12 ? 117 VAL A CB    1 
ATOM   860  C CG1   . VAL A 1 126 ? 18.572 37.548 34.085 1.00 23.96 ? 117 VAL A CG1   1 
ATOM   861  C CG2   . VAL A 1 126 ? 17.753 39.985 33.932 1.00 28.23 ? 117 VAL A CG2   1 
ATOM   862  N N     . TYR A 1 127 ? 15.558 36.328 33.363 1.00 20.24 ? 118 TYR A N     1 
ATOM   863  C CA    . TYR A 1 127 ? 15.112 35.732 32.107 1.00 20.20 ? 118 TYR A CA    1 
ATOM   864  C C     . TYR A 1 127 ? 13.676 35.273 32.166 1.00 21.58 ? 118 TYR A C     1 
ATOM   865  O O     . TYR A 1 127 ? 13.165 34.771 31.154 1.00 23.91 ? 118 TYR A O     1 
ATOM   866  C CB    . TYR A 1 127 ? 15.992 34.505 31.773 1.00 18.88 ? 118 TYR A CB    1 
ATOM   867  C CG    . TYR A 1 127 ? 17.394 34.873 31.462 1.00 16.10 ? 118 TYR A CG    1 
ATOM   868  C CD1   . TYR A 1 127 ? 17.690 35.840 30.473 1.00 17.20 ? 118 TYR A CD1   1 
ATOM   869  C CD2   . TYR A 1 127 ? 18.435 34.317 32.136 1.00 16.68 ? 118 TYR A CD2   1 
ATOM   870  C CE1   . TYR A 1 127 ? 18.982 36.175 30.180 1.00 19.18 ? 118 TYR A CE1   1 
ATOM   871  C CE2   . TYR A 1 127 ? 19.763 34.680 31.853 1.00 17.79 ? 118 TYR A CE2   1 
ATOM   872  C CZ    . TYR A 1 127 ? 20.019 35.648 30.886 1.00 18.12 ? 118 TYR A CZ    1 
ATOM   873  O OH    . TYR A 1 127 ? 21.326 35.983 30.600 1.00 20.75 ? 118 TYR A OH    1 
ATOM   874  N N     . GLN A 1 128 ? 12.992 35.416 33.320 1.00 22.13 ? 119 GLN A N     1 
ATOM   875  C CA    . GLN A 1 128 ? 11.663 34.876 33.504 1.00 21.54 ? 119 GLN A CA    1 
ATOM   876  C C     . GLN A 1 128 ? 10.609 35.983 33.527 1.00 25.71 ? 119 GLN A C     1 
ATOM   877  O O     . GLN A 1 128 ? 10.853 37.056 34.081 1.00 27.85 ? 119 GLN A O     1 
ATOM   878  C CB    . GLN A 1 128 ? 11.571 34.076 34.816 1.00 24.12 ? 119 GLN A CB    1 
ATOM   879  C CG    . GLN A 1 128 ? 12.378 32.783 34.789 1.00 21.15 ? 119 GLN A CG    1 
ATOM   880  C CD    . GLN A 1 128 ? 11.832 31.828 33.746 1.00 25.15 ? 119 GLN A CD    1 
ATOM   881  O OE1   . GLN A 1 128 ? 10.629 31.673 33.609 1.00 26.64 ? 119 GLN A OE1   1 
ATOM   882  N NE2   . GLN A 1 128 ? 12.714 31.183 33.031 1.00 20.13 ? 119 GLN A NE2   1 
ATOM   883  N N     . PRO A 1 129 ? 9.429  35.732 32.968 1.00 27.60 ? 120 PRO A N     1 
ATOM   884  C CA    . PRO A 1 129 ? 8.350  36.734 33.043 1.00 34.16 ? 120 PRO A CA    1 
ATOM   885  C C     . PRO A 1 129 ? 8.023  37.013 34.492 1.00 30.23 ? 120 PRO A C     1 
ATOM   886  O O     . PRO A 1 129 ? 7.928  36.094 35.305 1.00 31.30 ? 120 PRO A O     1 
ATOM   887  C CB    . PRO A 1 129 ? 7.165  36.034 32.377 1.00 31.97 ? 120 PRO A CB    1 
ATOM   888  C CG    . PRO A 1 129 ? 7.748  34.890 31.614 1.00 37.87 ? 120 PRO A CG    1 
ATOM   889  C CD    . PRO A 1 129 ? 8.980  34.472 32.343 1.00 32.24 ? 120 PRO A CD    1 
ATOM   890  N N     . ALA A 1 130 ? 7.827  38.294 34.799 1.00 31.06 ? 121 ALA A N     1 
ATOM   891  C CA    . ALA A 1 130 ? 7.514  38.736 36.151 1.00 32.29 ? 121 ALA A CA    1 
ATOM   892  C C     . ALA A 1 130 ? 8.563  38.307 37.164 1.00 31.96 ? 121 ALA A C     1 
ATOM   893  O O     . ALA A 1 130 ? 8.288  38.287 38.364 1.00 34.32 ? 121 ALA A O     1 
ATOM   894  C CB    . ALA A 1 130 ? 6.121  38.273 36.579 1.00 37.09 ? 121 ALA A CB    1 
ATOM   895  N N     . GLY A 1 131 ? 9.769  37.971 36.700 1.00 28.70 ? 122 GLY A N     1 
ATOM   896  C CA    . GLY A 1 131 ? 10.811 37.488 37.589 1.00 28.91 ? 122 GLY A CA    1 
ATOM   897  C C     . GLY A 1 131 ? 10.416 36.261 38.399 1.00 33.63 ? 122 GLY A C     1 
ATOM   898  O O     . GLY A 1 131 ? 10.901 36.092 39.519 1.00 33.43 ? 122 GLY A O     1 
ATOM   899  N N     . ALA A 1 132 ? 9.545  35.408 37.863 1.00 26.88 ? 123 ALA A N     1 
ATOM   900  C CA    . ALA A 1 132 ? 9.131  34.199 38.563 1.00 31.57 ? 123 ALA A CA    1 
ATOM   901  C C     . ALA A 1 132 ? 10.256 33.178 38.585 1.00 29.26 ? 123 ALA A C     1 
ATOM   902  O O     . ALA A 1 132 ? 11.204 33.238 37.802 1.00 27.53 ? 123 ALA A O     1 
ATOM   903  C CB    . ALA A 1 132 ? 7.980  33.540 37.815 1.00 30.60 ? 123 ALA A CB    1 
ATOM   904  N N     . ALA A 1 133 ? 10.119 32.206 39.486 1.00 25.14 ? 124 ALA A N     1 
ATOM   905  C CA    . ALA A 1 133 ? 11.079 31.118 39.555 1.00 22.69 ? 124 ALA A CA    1 
ATOM   906  C C     . ALA A 1 133 ? 11.028 30.263 38.281 1.00 23.82 ? 124 ALA A C     1 
ATOM   907  O O     . ALA A 1 133 ? 9.946  29.952 37.775 1.00 24.92 ? 124 ALA A O     1 
ATOM   908  C CB    . ALA A 1 133 ? 10.741 30.229 40.748 1.00 25.47 ? 124 ALA A CB    1 
ATOM   909  N N     . PRO A 1 134 ? 12.185 29.832 37.784 1.00 20.43 ? 125 PRO A N     1 
ATOM   910  C CA    . PRO A 1 134 ? 12.225 28.807 36.700 1.00 19.31 ? 125 PRO A CA    1 
ATOM   911  C C     . PRO A 1 134 ? 11.515 27.534 37.120 1.00 22.35 ? 125 PRO A C     1 
ATOM   912  O O     . PRO A 1 134 ? 11.386 27.230 38.303 1.00 21.30 ? 125 PRO A O     1 
ATOM   913  C CB    . PRO A 1 134 ? 13.724 28.521 36.538 1.00 22.93 ? 125 PRO A CB    1 
ATOM   914  C CG    . PRO A 1 134 ? 14.463 29.631 37.270 1.00 27.28 ? 125 PRO A CG    1 
ATOM   915  C CD    . PRO A 1 134 ? 13.511 30.106 38.341 1.00 22.90 ? 125 PRO A CD    1 
ATOM   916  N N     . ILE A 1 135 ? 11.088 26.745 36.141 1.00 19.01 ? 126 ILE A N     1 
ATOM   917  C CA    . ILE A 1 135 ? 10.383 25.494 36.435 1.00 18.67 ? 126 ILE A CA    1 
ATOM   918  C C     . ILE A 1 135 ? 11.310 24.306 36.250 1.00 18.89 ? 126 ILE A C     1 
ATOM   919  O O     . ILE A 1 135 ? 12.267 24.351 35.460 1.00 19.82 ? 126 ILE A O     1 
ATOM   920  C CB    . ILE A 1 135 ? 9.152  25.317 35.524 1.00 21.28 ? 126 ILE A CB    1 
ATOM   921  C CG1   . ILE A 1 135 ? 9.532  25.290 34.044 1.00 21.50 ? 126 ILE A CG1   1 
ATOM   922  C CG2   . ILE A 1 135 ? 8.094  26.357 35.830 1.00 22.38 ? 126 ILE A CG2   1 
ATOM   923  C CD1   . ILE A 1 135 ? 8.540  24.457 33.216 1.00 28.38 ? 126 ILE A CD1   1 
ATOM   924  N N     . SER A 1 136 ? 10.994 23.209 36.938 1.00 18.56 ? 127 SER A N     1 
ATOM   925  C CA    . SER A 1 136 ? 11.821 22.016 36.814 1.00 18.67 ? 127 SER A CA    1 
ATOM   926  C C     . SER A 1 136 ? 11.060 20.784 37.269 1.00 18.69 ? 127 SER A C     1 
ATOM   927  O O     . SER A 1 136 ? 9.926  20.867 37.755 1.00 18.63 ? 127 SER A O     1 
ATOM   928  C CB    . SER A 1 136 ? 13.121 22.201 37.599 1.00 19.91 ? 127 SER A CB    1 
ATOM   929  O OG    . SER A 1 136 ? 14.047 21.146 37.386 1.00 20.88 ? 127 SER A OG    1 
ATOM   930  N N     . SER A 1 137 ? 11.744 19.638 37.195 1.00 18.81 ? 128 SER A N     1 
ATOM   931  C CA    . SER A 1 137 ? 11.244 18.415 37.817 1.00 18.37 ? 128 SER A CA    1 
ATOM   932  C C     . SER A 1 137 ? 11.333 18.490 39.319 1.00 19.68 ? 128 SER A C     1 
ATOM   933  O O     . SER A 1 137 ? 10.547 17.826 40.003 1.00 19.46 ? 128 SER A O     1 
ATOM   934  C CB    . SER A 1 137 ? 12.064 17.229 37.336 1.00 20.23 ? 128 SER A CB    1 
ATOM   935  O OG    . SER A 1 137 ? 13.441 17.473 37.697 1.00 17.86 ? 128 SER A OG    1 
ATOM   936  N N     . THR A 1 138 ? 12.234 19.333 39.837 1.00 19.96 ? 129 THR A N     1 
ATOM   937  C CA    . THR A 1 138 ? 12.664 19.328 41.233 1.00 19.35 ? 129 THR A CA    1 
ATOM   938  C C     . THR A 1 138 ? 12.581 20.752 41.759 1.00 22.45 ? 129 THR A C     1 
ATOM   939  O O     . THR A 1 138 ? 12.495 21.698 40.976 1.00 21.26 ? 129 THR A O     1 
ATOM   940  C CB    . THR A 1 138 ? 14.126 18.852 41.243 1.00 23.76 ? 129 THR A CB    1 
ATOM   941  O OG1   . THR A 1 138 ? 14.569 18.774 42.593 1.00 23.22 ? 129 THR A OG1   1 
ATOM   942  C CG2   . THR A 1 138 ? 15.092 19.770 40.445 1.00 22.82 ? 129 THR A CG2   1 
ATOM   943  N N     . GLU A 1 139 ? 12.601 20.897 43.088 1.00 21.74 ? 130 GLU A N     1 
ATOM   944  C CA    . GLU A 1 139 ? 12.755 22.211 43.725 1.00 21.29 ? 130 GLU A CA    1 
ATOM   945  C C     . GLU A 1 139 ? 14.197 22.531 44.082 1.00 24.63 ? 130 GLU A C     1 
ATOM   946  O O     . GLU A 1 139 ? 14.465 23.602 44.649 1.00 26.73 ? 130 GLU A O     1 
ATOM   947  C CB    . GLU A 1 139 ? 11.885 22.318 44.993 1.00 27.42 ? 130 GLU A CB    1 
ATOM   948  C CG    . GLU A 1 139 ? 10.542 21.693 44.918 1.00 43.94 ? 130 GLU A CG    1 
ATOM   949  C CD    . GLU A 1 139 ? 9.735  22.032 46.140 1.00 67.61 ? 130 GLU A CD    1 
ATOM   950  O OE1   . GLU A 1 139 ? 10.316 22.688 47.037 1.00 67.89 ? 130 GLU A OE1   1 
ATOM   951  O OE2   . GLU A 1 139 ? 8.539  21.659 46.200 1.00 77.07 ? 130 GLU A OE2   1 
ATOM   952  N N     . LYS A 1 140 ? 15.133 21.667 43.741 1.00 21.29 ? 131 LYS A N     1 
ATOM   953  C CA    . LYS A 1 140 ? 16.523 21.914 44.103 1.00 23.05 ? 131 LYS A CA    1 
ATOM   954  C C     . LYS A 1 140 ? 17.208 22.768 43.037 1.00 21.50 ? 131 LYS A C     1 
ATOM   955  O O     . LYS A 1 140 ? 17.051 22.506 41.830 1.00 20.70 ? 131 LYS A O     1 
ATOM   956  C CB    . LYS A 1 140 ? 17.247 20.597 44.189 1.00 24.12 ? 131 LYS A CB    1 
ATOM   957  C CG    . LYS A 1 140 ? 16.679 19.651 45.304 1.00 24.41 ? 131 LYS A CG    1 
ATOM   958  C CD    . LYS A 1 140 ? 16.670 20.372 46.689 1.00 35.94 ? 131 LYS A CD    1 
ATOM   959  C CE    . LYS A 1 140 ? 16.695 19.360 47.851 1.00 40.73 ? 131 LYS A CE    1 
ATOM   960  N NZ    . LYS A 1 140 ? 17.560 19.830 49.029 1.00 43.30 ? 131 LYS A NZ    1 
ATOM   961  N N     . PRO A 1 141 ? 18.018 23.743 43.433 1.00 20.09 ? 132 PRO A N     1 
ATOM   962  C CA    . PRO A 1 141 ? 18.780 24.542 42.469 1.00 20.83 ? 132 PRO A CA    1 
ATOM   963  C C     . PRO A 1 141 ? 19.988 23.792 41.960 1.00 19.87 ? 132 PRO A C     1 
ATOM   964  O O     . PRO A 1 141 ? 20.495 22.877 42.594 1.00 21.38 ? 132 PRO A O     1 
ATOM   965  C CB    . PRO A 1 141 ? 19.248 25.737 43.304 1.00 19.57 ? 132 PRO A CB    1 
ATOM   966  C CG    . PRO A 1 141 ? 19.351 25.190 44.721 1.00 24.66 ? 132 PRO A CG    1 
ATOM   967  C CD    . PRO A 1 141 ? 18.192 24.215 44.836 1.00 22.43 ? 132 PRO A CD    1 
ATOM   968  N N     . ILE A 1 142 ? 20.454 24.206 40.755 1.00 18.62 ? 133 ILE A N     1 
ATOM   969  C CA    . ILE A 1 142 ? 21.802 23.865 40.326 1.00 17.97 ? 133 ILE A CA    1 
ATOM   970  C C     . ILE A 1 142 ? 22.727 24.445 41.408 1.00 20.71 ? 133 ILE A C     1 
ATOM   971  O O     . ILE A 1 142 ? 22.475 25.543 41.922 1.00 21.27 ? 133 ILE A O     1 
ATOM   972  C CB    . ILE A 1 142 ? 22.064 24.508 38.945 1.00 19.09 ? 133 ILE A CB    1 
ATOM   973  C CG1   . ILE A 1 142 ? 21.161 23.856 37.882 1.00 18.80 ? 133 ILE A CG1   1 
ATOM   974  C CG2   . ILE A 1 142 ? 23.530 24.373 38.552 1.00 20.16 ? 133 ILE A CG2   1 
ATOM   975  C CD1   . ILE A 1 142 ? 21.002 24.774 36.663 1.00 20.51 ? 133 ILE A CD1   1 
ATOM   976  N N     . SER A 1 143 ? 23.757 23.696 41.775 1.00 21.36 ? 134 SER A N     1 
ATOM   977  C CA    . SER A 1 143 ? 24.616 24.193 42.848 1.00 22.43 ? 134 SER A CA    1 
ATOM   978  C C     . SER A 1 143 ? 25.525 25.328 42.371 1.00 25.38 ? 134 SER A C     1 
ATOM   979  O O     . SER A 1 143 ? 25.690 25.596 41.159 1.00 23.58 ? 134 SER A O     1 
ATOM   980  C CB    . SER A 1 143 ? 25.492 23.071 43.372 1.00 24.09 ? 134 SER A CB    1 
ATOM   981  O OG    . SER A 1 143 ? 26.453 22.696 42.421 1.00 26.17 ? 134 SER A OG    1 
ATOM   982  N N     . ASN A 1 144 ? 26.187 25.987 43.345 1.00 26.78 ? 135 ASN A N     1 
ATOM   983  C CA    . ASN A 1 144 ? 27.045 27.118 42.972 1.00 26.55 ? 135 ASN A CA    1 
ATOM   984  C C     . ASN A 1 144 ? 28.382 26.676 42.380 1.00 27.14 ? 135 ASN A C     1 
ATOM   985  O O     . ASN A 1 144 ? 29.215 27.537 42.088 1.00 32.29 ? 135 ASN A O     1 
ATOM   986  C CB    . ASN A 1 144 ? 27.220 28.173 44.069 1.00 35.68 ? 135 ASN A CB    1 
ATOM   987  C CG    . ASN A 1 144 ? 27.621 27.581 45.366 1.00 43.22 ? 135 ASN A CG    1 
ATOM   988  O OD1   . ASN A 1 144 ? 28.303 26.553 45.395 1.00 47.82 ? 135 ASN A OD1   1 
ATOM   989  N ND2   . ASN A 1 144 ? 27.260 28.249 46.461 1.00 45.52 ? 135 ASN A ND2   1 
ATOM   990  N N     . ARG A 1 145 ? 28.563 25.390 42.108 1.00 26.04 ? 136 ARG A N     1 
ATOM   991  C CA    . ARG A 1 145 ? 29.601 24.924 41.191 1.00 26.66 ? 136 ARG A CA    1 
ATOM   992  C C     . ARG A 1 145 ? 29.436 25.487 39.774 1.00 28.79 ? 136 ARG A C     1 
ATOM   993  O O     . ARG A 1 145 ? 30.397 25.490 38.999 1.00 30.54 ? 136 ARG A O     1 
ATOM   994  C CB    . ARG A 1 145 ? 29.549 23.388 41.118 1.00 34.68 ? 136 ARG A CB    1 
ATOM   995  N N     . TRP A 1 146 ? 28.236 25.926 39.406 1.00 24.61 ? 137 TRP A N     1 
ATOM   996  C CA    . TRP A 1 146 ? 27.958 26.432 38.064 1.00 21.90 ? 137 TRP A CA    1 
ATOM   997  C C     . TRP A 1 146 ? 27.379 27.827 38.196 1.00 21.85 ? 137 TRP A C     1 
ATOM   998  O O     . TRP A 1 146 ? 26.780 28.146 39.201 1.00 23.47 ? 137 TRP A O     1 
ATOM   999  C CB    . TRP A 1 146 ? 26.876 25.578 37.400 1.00 23.53 ? 137 TRP A CB    1 
ATOM   1000 C CG    . TRP A 1 146 ? 27.267 24.132 37.335 1.00 24.18 ? 137 TRP A CG    1 
ATOM   1001 C CD1   . TRP A 1 146 ? 26.999 23.183 38.278 1.00 25.06 ? 137 TRP A CD1   1 
ATOM   1002 C CD2   . TRP A 1 146 ? 27.969 23.480 36.272 1.00 23.30 ? 137 TRP A CD2   1 
ATOM   1003 N NE1   . TRP A 1 146 ? 27.515 21.974 37.863 1.00 25.29 ? 137 TRP A NE1   1 
ATOM   1004 C CE2   . TRP A 1 146 ? 28.129 22.127 36.650 1.00 26.64 ? 137 TRP A CE2   1 
ATOM   1005 C CE3   . TRP A 1 146 ? 28.473 23.904 35.033 1.00 24.57 ? 137 TRP A CE3   1 
ATOM   1006 C CZ2   . TRP A 1 146 ? 28.770 21.189 35.831 1.00 28.00 ? 137 TRP A CZ2   1 
ATOM   1007 C CZ3   . TRP A 1 146 ? 29.126 22.974 34.227 1.00 27.90 ? 137 TRP A CZ3   1 
ATOM   1008 C CH2   . TRP A 1 146 ? 29.276 21.634 34.639 1.00 29.65 ? 137 TRP A CH2   1 
ATOM   1009 N N     . ARG A 1 147 ? 27.557 28.675 37.166 1.00 23.01 ? 138 ARG A N     1 
ATOM   1010 C CA    . ARG A 1 147 ? 27.106 30.062 37.233 1.00 24.14 ? 138 ARG A CA    1 
ATOM   1011 C C     . ARG A 1 147 ? 26.437 30.355 35.905 1.00 22.13 ? 138 ARG A C     1 
ATOM   1012 O O     . ARG A 1 147 ? 26.872 29.845 34.891 1.00 25.40 ? 138 ARG A O     1 
ATOM   1013 C CB    . ARG A 1 147 ? 28.314 31.012 37.314 1.00 27.70 ? 138 ARG A CB    1 
ATOM   1014 C CG    . ARG A 1 147 ? 29.061 30.927 38.608 1.00 35.14 ? 138 ARG A CG    1 
ATOM   1015 C CD    . ARG A 1 147 ? 28.205 31.335 39.748 1.00 36.64 ? 138 ARG A CD    1 
ATOM   1016 N NE    . ARG A 1 147 ? 28.650 30.725 41.001 1.00 56.97 ? 138 ARG A NE    1 
ATOM   1017 C CZ    . ARG A 1 147 ? 29.372 31.352 41.919 1.00 57.05 ? 138 ARG A CZ    1 
ATOM   1018 N NH1   . ARG A 1 147 ? 29.763 32.608 41.750 1.00 56.38 ? 138 ARG A NH1   1 
ATOM   1019 N NH2   . ARG A 1 147 ? 29.699 30.712 43.040 1.00 69.39 ? 138 ARG A NH2   1 
ATOM   1020 N N     . ILE A 1 148 ? 25.408 31.195 35.926 1.00 20.36 ? 139 ILE A N     1 
ATOM   1021 C CA    . ILE A 1 148 ? 24.642 31.528 34.693 1.00 19.37 ? 139 ILE A CA    1 
ATOM   1022 C C     . ILE A 1 148 ? 25.158 32.832 34.071 1.00 18.27 ? 139 ILE A C     1 
ATOM   1023 O O     . ILE A 1 148 ? 25.477 33.764 34.792 1.00 20.59 ? 139 ILE A O     1 
ATOM   1024 C CB    . ILE A 1 148 ? 23.126 31.588 34.976 1.00 17.58 ? 139 ILE A CB    1 
ATOM   1025 C CG1   . ILE A 1 148 ? 22.315 31.693 33.685 1.00 18.88 ? 139 ILE A CG1   1 
ATOM   1026 C CG2   . ILE A 1 148 ? 22.778 32.703 35.950 1.00 23.96 ? 139 ILE A CG2   1 
ATOM   1027 C CD1   . ILE A 1 148 ? 20.832 31.675 33.899 1.00 21.69 ? 139 ILE A CD1   1 
ATOM   1028 N N     . LEU A 1 149 ? 25.251 32.841 32.754 1.00 18.92 ? 140 LEU A N     1 
ATOM   1029 C CA    . LEU A 1 149 ? 25.626 34.092 32.057 1.00 18.23 ? 140 LEU A CA    1 
ATOM   1030 C C     . LEU A 1 149 ? 24.448 35.061 32.143 1.00 19.07 ? 140 LEU A C     1 
ATOM   1031 O O     . LEU A 1 149 ? 23.346 34.696 31.753 1.00 19.91 ? 140 LEU A O     1 
ATOM   1032 C CB    . LEU A 1 149 ? 25.987 33.765 30.607 1.00 18.26 ? 140 LEU A CB    1 
ATOM   1033 C CG    . LEU A 1 149 ? 26.296 34.967 29.718 1.00 18.62 ? 140 LEU A CG    1 
ATOM   1034 C CD1   . LEU A 1 149 ? 27.574 35.656 30.166 1.00 22.53 ? 140 LEU A CD1   1 
ATOM   1035 C CD2   . LEU A 1 149 ? 26.398 34.541 28.263 1.00 24.06 ? 140 LEU A CD2   1 
ATOM   1036 N N     . MET A 1 150 ? 24.634 36.234 32.573 1.00 19.15 ? 141 MET A N     1 
ATOM   1037 C CA    . MET A 1 150 ? 23.684 37.325 32.850 1.00 19.77 ? 141 MET A CA    1 
ATOM   1038 C C     . MET A 1 150 ? 23.608 38.251 31.630 1.00 19.85 ? 141 MET A C     1 
ATOM   1039 O O     . MET A 1 150 ? 24.491 38.209 30.787 1.00 19.05 ? 141 MET A O     1 
ATOM   1040 C CB    . MET A 1 150 ? 24.097 38.108 34.097 1.00 21.62 ? 141 MET A CB    1 
ATOM   1041 C CG    . MET A 1 150 ? 24.008 37.313 35.389 1.00 23.00 ? 141 MET A CG    1 
ATOM   1042 S SD    . MET A 1 150 ? 22.342 36.717 35.728 1.00 23.80 ? 141 MET A SD    1 
ATOM   1043 C CE    . MET A 1 150 ? 21.572 38.207 36.358 1.00 29.45 ? 141 MET A CE    1 
ATOM   1044 N N     . PRO A 1 151 ? 22.645 38.976 31.302 1.00 18.47 ? 142 PRO A N     1 
ATOM   1045 C CA    . PRO A 1 151 ? 22.594 39.852 30.139 1.00 20.04 ? 142 PRO A CA    1 
ATOM   1046 C C     . PRO A 1 151 ? 23.728 40.896 30.100 1.00 21.33 ? 142 PRO A C     1 
ATOM   1047 O O     . PRO A 1 151 ? 24.082 41.302 29.032 1.00 22.95 ? 142 PRO A O     1 
ATOM   1048 C CB    . PRO A 1 151 ? 21.199 40.475 30.279 1.00 23.85 ? 142 PRO A CB    1 
ATOM   1049 C CG    . PRO A 1 151 ? 20.404 39.485 31.074 1.00 23.87 ? 142 PRO A CG    1 
ATOM   1050 C CD    . PRO A 1 151 ? 21.404 38.960 32.073 1.00 20.68 ? 142 PRO A CD    1 
ATOM   1051 N N     . ASP A 1 152 ? 24.276 41.277 31.254 1.00 20.68 ? 143 ASP A N     1 
ATOM   1052 C CA    . ASP A 1 152 ? 25.370 42.246 31.245 1.00 21.22 ? 143 ASP A CA    1 
ATOM   1053 C C     . ASP A 1 152 ? 26.736 41.618 31.057 1.00 21.34 ? 143 ASP A C     1 
ATOM   1054 O O     . ASP A 1 152 ? 27.752 42.317 31.194 1.00 24.76 ? 143 ASP A O     1 
ATOM   1055 C CB    . ASP A 1 152 ? 25.415 43.148 32.488 1.00 22.26 ? 143 ASP A CB    1 
ATOM   1056 C CG    . ASP A 1 152 ? 25.388 42.383 33.795 1.00 29.26 ? 143 ASP A CG    1 
ATOM   1057 O OD1   . ASP A 1 152 ? 25.849 41.238 33.804 1.00 24.20 ? 143 ASP A OD1   1 
ATOM   1058 O OD2   . ASP A 1 152 ? 25.157 43.020 34.869 1.00 27.98 ? 143 ASP A OD2   1 
ATOM   1059 N N     . GLY A 1 153 ? 26.810 40.289 30.863 1.00 21.09 ? 144 GLY A N     1 
ATOM   1060 C CA    . GLY A 1 153 ? 28.102 39.649 30.710 1.00 23.88 ? 144 GLY A CA    1 
ATOM   1061 C C     . GLY A 1 153 ? 28.734 39.141 31.991 1.00 22.98 ? 144 GLY A C     1 
ATOM   1062 O O     . GLY A 1 153 ? 29.796 38.505 31.927 1.00 30.57 ? 144 GLY A O     1 
ATOM   1063 N N     . THR A 1 154 ? 28.145 39.431 33.148 1.00 22.54 ? 145 THR A N     1 
ATOM   1064 C CA    . THR A 1 154 ? 28.606 38.845 34.396 1.00 23.44 ? 145 THR A CA    1 
ATOM   1065 C C     . THR A 1 154 ? 28.038 37.434 34.560 1.00 22.10 ? 145 THR A C     1 
ATOM   1066 O O     . THR A 1 154 ? 27.214 36.948 33.774 1.00 21.45 ? 145 THR A O     1 
ATOM   1067 C CB    . THR A 1 154 ? 28.202 39.684 35.606 1.00 23.26 ? 145 THR A CB    1 
ATOM   1068 O OG1   . THR A 1 154 ? 26.773 39.722 35.764 1.00 24.53 ? 145 THR A OG1   1 
ATOM   1069 C CG2   . THR A 1 154 ? 28.732 41.153 35.487 1.00 31.06 ? 145 THR A CG2   1 
ATOM   1070 N N     . HIS A 1 155 ? 28.412 36.812 35.675 1.00 22.62 ? 146 HIS A N     1 
ATOM   1071 C CA    . HIS A 1 155 ? 27.964 35.452 35.965 1.00 22.93 ? 146 HIS A CA    1 
ATOM   1072 C C     . HIS A 1 155 ? 27.169 35.469 37.244 1.00 26.08 ? 146 HIS A C     1 
ATOM   1073 O O     . HIS A 1 155 ? 27.629 35.995 38.261 1.00 31.54 ? 146 HIS A O     1 
ATOM   1074 C CB    . HIS A 1 155 ? 29.129 34.470 35.999 1.00 22.89 ? 146 HIS A CB    1 
ATOM   1075 C CG    . HIS A 1 155 ? 29.663 34.198 34.641 1.00 27.96 ? 146 HIS A CG    1 
ATOM   1076 N ND1   . HIS A 1 155 ? 30.500 35.070 33.984 1.00 38.96 ? 146 HIS A ND1   1 
ATOM   1077 C CD2   . HIS A 1 155 ? 29.340 33.238 33.741 1.00 39.41 ? 146 HIS A CD2   1 
ATOM   1078 C CE1   . HIS A 1 155 ? 30.742 34.611 32.769 1.00 42.64 ? 146 HIS A CE1   1 
ATOM   1079 N NE2   . HIS A 1 155 ? 30.041 33.507 32.592 1.00 41.32 ? 146 HIS A NE2   1 
ATOM   1080 N N     . GLY A 1 156 ? 25.957 34.926 37.183 1.00 19.56 ? 147 GLY A N     1 
ATOM   1081 C CA    . GLY A 1 156 ? 25.021 34.960 38.274 1.00 18.84 ? 147 GLY A CA    1 
ATOM   1082 C C     . GLY A 1 156 ? 24.831 33.591 38.909 1.00 18.50 ? 147 GLY A C     1 
ATOM   1083 O O     . GLY A 1 156 ? 25.401 32.583 38.504 1.00 22.05 ? 147 GLY A O     1 
ATOM   1084 N N     . ILE A 1 157 ? 23.981 33.614 39.924 1.00 21.02 ? 148 ILE A N     1 
ATOM   1085 C CA    . ILE A 1 157 ? 23.703 32.421 40.732 1.00 23.16 ? 148 ILE A CA    1 
ATOM   1086 C C     . ILE A 1 157 ? 22.387 31.821 40.284 1.00 20.36 ? 148 ILE A C     1 
ATOM   1087 O O     . ILE A 1 157 ? 21.365 32.509 40.210 1.00 21.02 ? 148 ILE A O     1 
ATOM   1088 C CB    . ILE A 1 157 ? 23.604 32.820 42.211 1.00 23.70 ? 148 ILE A CB    1 
ATOM   1089 C CG1   . ILE A 1 157 ? 24.924 33.421 42.712 1.00 28.25 ? 148 ILE A CG1   1 
ATOM   1090 C CG2   . ILE A 1 157 ? 23.230 31.614 43.062 1.00 23.99 ? 148 ILE A CG2   1 
ATOM   1091 C CD1   . ILE A 1 157 ? 26.135 32.674 42.303 1.00 37.11 ? 148 ILE A CD1   1 
ATOM   1092 N N     . TYR A 1 158 ? 22.381 30.509 40.013 1.00 19.24 ? 149 TYR A N     1 
ATOM   1093 C CA    . TYR A 1 158 ? 21.112 29.884 39.655 1.00 21.93 ? 149 TYR A CA    1 
ATOM   1094 C C     . TYR A 1 158 ? 20.189 29.854 40.869 1.00 22.69 ? 149 TYR A C     1 
ATOM   1095 O O     . TYR A 1 158 ? 20.611 29.428 41.944 1.00 21.66 ? 149 TYR A O     1 
ATOM   1096 C CB    . TYR A 1 158 ? 21.362 28.440 39.232 1.00 19.82 ? 149 TYR A CB    1 
ATOM   1097 C CG    . TYR A 1 158 ? 21.998 28.303 37.860 1.00 17.58 ? 149 TYR A CG    1 
ATOM   1098 C CD1   . TYR A 1 158 ? 21.242 28.531 36.686 1.00 18.32 ? 149 TYR A CD1   1 
ATOM   1099 C CD2   . TYR A 1 158 ? 23.332 27.972 37.734 1.00 17.88 ? 149 TYR A CD2   1 
ATOM   1100 C CE1   . TYR A 1 158 ? 21.857 28.385 35.441 1.00 18.08 ? 149 TYR A CE1   1 
ATOM   1101 C CE2   . TYR A 1 158 ? 23.949 27.824 36.513 1.00 20.58 ? 149 TYR A CE2   1 
ATOM   1102 C CZ    . TYR A 1 158 ? 23.195 28.024 35.373 1.00 19.76 ? 149 TYR A CZ    1 
ATOM   1103 O OH    . TYR A 1 158 ? 23.873 27.902 34.148 1.00 23.57 ? 149 TYR A OH    1 
ATOM   1104 N N     . PRO A 1 159 ? 18.929 30.211 40.718 1.00 21.24 ? 150 PRO A N     1 
ATOM   1105 C CA    . PRO A 1 159 ? 17.976 30.217 41.829 1.00 22.22 ? 150 PRO A CA    1 
ATOM   1106 C C     . PRO A 1 159 ? 17.299 28.868 42.023 1.00 22.74 ? 150 PRO A C     1 
ATOM   1107 O O     . PRO A 1 159 ? 17.446 27.932 41.227 1.00 21.95 ? 150 PRO A O     1 
ATOM   1108 C CB    . PRO A 1 159 ? 16.930 31.235 41.350 1.00 25.05 ? 150 PRO A CB    1 
ATOM   1109 C CG    . PRO A 1 159 ? 16.902 30.986 39.825 1.00 22.93 ? 150 PRO A CG    1 
ATOM   1110 C CD    . PRO A 1 159 ? 18.324 30.706 39.469 1.00 23.42 ? 150 PRO A CD    1 
ATOM   1111 N N     . LYS A 1 160 ? 16.551 28.791 43.110 1.00 22.93 ? 151 LYS A N     1 
ATOM   1112 C CA    . LYS A 1 160 ? 15.704 27.645 43.370 1.00 21.27 ? 151 LYS A CA    1 
ATOM   1113 C C     . LYS A 1 160 ? 14.579 27.591 42.341 1.00 21.86 ? 151 LYS A C     1 
ATOM   1114 O O     . LYS A 1 160 ? 13.850 28.565 42.176 1.00 23.86 ? 151 LYS A O     1 
ATOM   1115 C CB    . LYS A 1 160 ? 15.077 27.834 44.776 1.00 28.67 ? 151 LYS A CB    1 
ATOM   1116 C CG    . LYS A 1 160 ? 14.483 26.568 45.337 1.00 31.18 ? 151 LYS A CG    1 
ATOM   1117 C CD    . LYS A 1 160 ? 13.647 26.904 46.601 1.00 27.15 ? 151 LYS A CD    1 
ATOM   1118 C CE    . LYS A 1 160 ? 12.379 27.650 46.160 1.00 40.75 ? 151 LYS A CE    1 
ATOM   1119 N NZ    . LYS A 1 160 ? 11.500 26.766 45.263 1.00 46.73 ? 151 LYS A NZ    1 
ATOM   1120 N N     . PRO A 1 161 ? 14.394 26.463 41.662 1.00 20.81 ? 152 PRO A N     1 
ATOM   1121 C CA    . PRO A 1 161 ? 13.269 26.345 40.729 1.00 18.97 ? 152 PRO A CA    1 
ATOM   1122 C C     . PRO A 1 161 ? 12.015 25.900 41.468 1.00 20.54 ? 152 PRO A C     1 
ATOM   1123 O O     . PRO A 1 161 ? 12.047 25.512 42.646 1.00 23.06 ? 152 PRO A O     1 
ATOM   1124 C CB    . PRO A 1 161 ? 13.745 25.231 39.774 1.00 21.28 ? 152 PRO A CB    1 
ATOM   1125 C CG    . PRO A 1 161 ? 14.504 24.298 40.694 1.00 19.93 ? 152 PRO A CG    1 
ATOM   1126 C CD    . PRO A 1 161 ? 15.225 25.243 41.682 1.00 20.00 ? 152 PRO A CD    1 
ATOM   1127 N N     . ARG A 1 162 ? 10.916 25.918 40.745 1.00 21.26 ? 153 ARG A N     1 
ATOM   1128 C CA    . ARG A 1 162 ? 9.629  25.412 41.224 1.00 23.00 ? 153 ARG A CA    1 
ATOM   1129 C C     . ARG A 1 162 ? 9.366  24.056 40.563 1.00 21.95 ? 153 ARG A C     1 
ATOM   1130 O O     . ARG A 1 162 ? 9.417  23.939 39.331 1.00 21.56 ? 153 ARG A O     1 
ATOM   1131 C CB    . ARG A 1 162 ? 8.552  26.416 40.805 1.00 27.73 ? 153 ARG A CB    1 
ATOM   1132 C CG    . ARG A 1 162 ? 7.130  26.057 41.174 1.00 32.56 ? 153 ARG A CG    1 
ATOM   1133 C CD    . ARG A 1 162 ? 6.137  27.220 40.889 1.00 26.41 ? 153 ARG A CD    1 
ATOM   1134 N NE    . ARG A 1 162 ? 6.057  27.626 39.485 1.00 29.19 ? 153 ARG A NE    1 
ATOM   1135 C CZ    . ARG A 1 162 ? 5.353  26.982 38.556 1.00 31.60 ? 153 ARG A CZ    1 
ATOM   1136 N NH1   . ARG A 1 162 ? 4.678  25.875 38.851 1.00 31.24 ? 153 ARG A NH1   1 
ATOM   1137 N NH2   . ARG A 1 162 ? 5.307  27.470 37.320 1.00 29.97 ? 153 ARG A NH2   1 
ATOM   1138 N N     . ALA A 1 163 ? 9.107  23.032 41.357 1.00 22.32 ? 154 ALA A N     1 
ATOM   1139 C CA    . ALA A 1 163 ? 8.808  21.719 40.796 1.00 21.40 ? 154 ALA A CA    1 
ATOM   1140 C C     . ALA A 1 163 ? 7.365  21.681 40.313 1.00 25.03 ? 154 ALA A C     1 
ATOM   1141 O O     . ALA A 1 163 ? 6.439  22.005 41.069 1.00 30.23 ? 154 ALA A O     1 
ATOM   1142 C CB    . ALA A 1 163 ? 9.046  20.627 41.831 1.00 22.80 ? 154 ALA A CB    1 
ATOM   1143 N N     . ILE A 1 164 ? 7.174  21.323 39.067 1.00 20.24 ? 155 ILE A N     1 
ATOM   1144 C CA    . ILE A 1 164 ? 5.858  21.415 38.440 1.00 20.49 ? 155 ILE A CA    1 
ATOM   1145 C C     . ILE A 1 164 ? 5.047  20.142 38.625 1.00 19.99 ? 155 ILE A C     1 
ATOM   1146 O O     . ILE A 1 164 ? 5.578  19.040 38.696 1.00 21.54 ? 155 ILE A O     1 
ATOM   1147 C CB    . ILE A 1 164 ? 6.011  21.765 36.955 1.00 19.64 ? 155 ILE A CB    1 
ATOM   1148 C CG1   . ILE A 1 164 ? 6.864  20.744 36.190 1.00 22.25 ? 155 ILE A CG1   1 
ATOM   1149 C CG2   . ILE A 1 164 ? 6.622  23.177 36.826 1.00 23.83 ? 155 ILE A CG2   1 
ATOM   1150 C CD1   . ILE A 1 164 ? 6.804  21.015 34.656 1.00 22.98 ? 155 ILE A CD1   1 
ATOM   1151 N N     . GLY A 1 165 ? 3.726  20.302 38.694 1.00 20.53 ? 156 GLY A N     1 
ATOM   1152 C CA    . GLY A 1 165 ? 2.798  19.181 38.704 1.00 19.98 ? 156 GLY A CA    1 
ATOM   1153 C C     . GLY A 1 165 ? 2.578  18.603 37.336 1.00 20.66 ? 156 GLY A C     1 
ATOM   1154 O O     . GLY A 1 165 ? 3.104  19.106 36.335 1.00 19.19 ? 156 GLY A O     1 
ATOM   1155 N N     . THR A 1 166 ? 1.808  17.499 37.282 1.00 18.72 ? 157 THR A N     1 
ATOM   1156 C CA    . THR A 1 166 ? 1.670  16.789 36.015 1.00 18.62 ? 157 THR A CA    1 
ATOM   1157 C C     . THR A 1 166 ? 0.803  17.539 35.007 1.00 18.30 ? 157 THR A C     1 
ATOM   1158 O O     . THR A 1 166 ? 1.010  17.408 33.802 1.00 19.38 ? 157 THR A O     1 
ATOM   1159 C CB    . THR A 1 166 ? 1.208  15.333 36.190 1.00 18.46 ? 157 THR A CB    1 
ATOM   1160 O OG1   . THR A 1 166 ? -0.126 15.350 36.707 1.00 20.95 ? 157 THR A OG1   1 
ATOM   1161 C CG2   . THR A 1 166 ? 2.123  14.655 37.199 1.00 20.54 ? 157 THR A CG2   1 
ATOM   1162 N N     . TYR A 1 167 ? -0.204 18.291 35.469 1.00 19.26 ? 158 TYR A N     1 
ATOM   1163 C CA    . TYR A 1 167 ? -0.907 19.162 34.521 1.00 18.66 ? 158 TYR A CA    1 
ATOM   1164 C C     . TYR A 1 167 ? 0.074  20.130 33.878 1.00 17.35 ? 158 TYR A C     1 
ATOM   1165 O O     . TYR A 1 167 ? 0.088  20.291 32.646 1.00 18.62 ? 158 TYR A O     1 
ATOM   1166 C CB    . TYR A 1 167 ? -2.026 19.931 35.242 1.00 18.93 ? 158 TYR A CB    1 
ATOM   1167 C CG    . TYR A 1 167 ? -2.546 21.119 34.404 1.00 18.42 ? 158 TYR A CG    1 
ATOM   1168 C CD1   . TYR A 1 167 ? -3.218 20.902 33.211 1.00 20.03 ? 158 TYR A CD1   1 
ATOM   1169 C CD2   . TYR A 1 167 ? -2.297 22.461 34.803 1.00 19.53 ? 158 TYR A CD2   1 
ATOM   1170 C CE1   . TYR A 1 167 ? -3.652 21.988 32.454 1.00 22.16 ? 158 TYR A CE1   1 
ATOM   1171 C CE2   . TYR A 1 167 ? -2.766 23.549 34.038 1.00 21.73 ? 158 TYR A CE2   1 
ATOM   1172 C CZ    . TYR A 1 167 ? -3.427 23.260 32.899 1.00 21.17 ? 158 TYR A CZ    1 
ATOM   1173 O OH    . TYR A 1 167 ? -3.858 24.359 32.157 1.00 24.43 ? 158 TYR A OH    1 
ATOM   1174 N N     . GLU A 1 168 ? 0.914  20.787 34.686 1.00 18.53 ? 159 GLU A N     1 
ATOM   1175 C CA    . GLU A 1 168 ? 1.894  21.724 34.108 1.00 19.40 ? 159 GLU A CA    1 
ATOM   1176 C C     . GLU A 1 168 ? 2.864  21.018 33.144 1.00 21.07 ? 159 GLU A C     1 
ATOM   1177 O O     . GLU A 1 168 ? 3.183  21.559 32.071 1.00 18.63 ? 159 GLU A O     1 
ATOM   1178 C CB    . GLU A 1 168 ? 2.719  22.395 35.182 1.00 20.14 ? 159 GLU A CB    1 
ATOM   1179 C CG    . GLU A 1 168 ? 3.393  23.605 34.564 1.00 24.17 ? 159 GLU A CG    1 
ATOM   1180 C CD    . GLU A 1 168 ? 3.784  24.636 35.620 1.00 36.93 ? 159 GLU A CD    1 
ATOM   1181 O OE1   . GLU A 1 168 ? 3.209  24.571 36.732 1.00 31.96 ? 159 GLU A OE1   1 
ATOM   1182 O OE2   . GLU A 1 168 ? 4.557  25.594 35.286 1.00 30.88 ? 159 GLU A OE2   1 
ATOM   1183 N N     . ILE A 1 169 ? 3.320  19.795 33.491 1.00 18.35 ? 160 ILE A N     1 
ATOM   1184 C CA    . ILE A 1 169 ? 4.090  18.996 32.540 1.00 17.10 ? 160 ILE A CA    1 
ATOM   1185 C C     . ILE A 1 169 ? 3.351  18.887 31.211 1.00 18.62 ? 160 ILE A C     1 
ATOM   1186 O O     . ILE A 1 169 ? 3.939  19.086 30.134 1.00 18.63 ? 160 ILE A O     1 
ATOM   1187 C CB    . ILE A 1 169 ? 4.389  17.612 33.149 1.00 19.29 ? 160 ILE A CB    1 
ATOM   1188 C CG1   . ILE A 1 169 ? 5.431  17.767 34.250 1.00 20.97 ? 160 ILE A CG1   1 
ATOM   1189 C CG2   . ILE A 1 169 ? 4.871  16.697 32.045 1.00 23.25 ? 160 ILE A CG2   1 
ATOM   1190 C CD1   . ILE A 1 169 ? 5.586  16.402 35.063 1.00 19.79 ? 160 ILE A CD1   1 
ATOM   1191 N N     . SER A 1 170 ? 2.057  18.528 31.254 1.00 18.33 ? 161 SER A N     1 
ATOM   1192 C CA    . SER A 1 170 ? 1.317  18.357 30.006 1.00 18.03 ? 161 SER A CA    1 
ATOM   1193 C C     . SER A 1 170 ? 1.243  19.661 29.221 1.00 20.18 ? 161 SER A C     1 
ATOM   1194 O O     . SER A 1 170 ? 1.163  19.638 27.988 1.00 19.70 ? 161 SER A O     1 
ATOM   1195 C CB    . SER A 1 170 ? -0.067 17.758 30.268 1.00 19.41 ? 161 SER A CB    1 
ATOM   1196 O OG    . SER A 1 170 ? -0.985 18.715 30.762 1.00 21.02 ? 161 SER A OG    1 
ATOM   1197 N N     . GLN A 1 171 ? 1.253  20.792 29.913 1.00 18.96 ? 162 GLN A N     1 
ATOM   1198 C CA    . GLN A 1 171 ? 1.189  22.058 29.186 1.00 19.19 ? 162 GLN A CA    1 
ATOM   1199 C C     . GLN A 1 171 ? 2.531  22.415 28.576 1.00 20.09 ? 162 GLN A C     1 
ATOM   1200 O O     . GLN A 1 171 ? 2.569  23.028 27.500 1.00 19.38 ? 162 GLN A O     1 
ATOM   1201 C CB    . GLN A 1 171 ? 0.717  23.150 30.130 1.00 19.66 ? 162 GLN A CB    1 
ATOM   1202 C CG    . GLN A 1 171 ? -0.749 22.922 30.611 1.00 22.89 ? 162 GLN A CG    1 
ATOM   1203 C CD    . GLN A 1 171 ? -1.710 22.552 29.522 1.00 27.71 ? 162 GLN A CD    1 
ATOM   1204 O OE1   . GLN A 1 171 ? -2.046 21.374 29.294 1.00 33.00 ? 162 GLN A OE1   1 
ATOM   1205 N NE2   . GLN A 1 171 ? -2.159 23.582 28.799 1.00 31.44 ? 162 GLN A NE2   1 
ATOM   1206 N N     . VAL A 1 172 ? 3.635  22.010 29.216 1.00 18.19 ? 163 VAL A N     1 
ATOM   1207 C CA    . VAL A 1 172 ? 4.936  22.153 28.572 1.00 19.94 ? 163 VAL A CA    1 
ATOM   1208 C C     . VAL A 1 172 ? 4.983  21.288 27.321 1.00 19.44 ? 163 VAL A C     1 
ATOM   1209 O O     . VAL A 1 172 ? 5.516  21.703 26.284 1.00 17.55 ? 163 VAL A O     1 
ATOM   1210 C CB    . VAL A 1 172 ? 6.066  21.816 29.568 1.00 18.92 ? 163 VAL A CB    1 
ATOM   1211 C CG1   . VAL A 1 172 ? 7.397  21.973 28.818 1.00 21.63 ? 163 VAL A CG1   1 
ATOM   1212 C CG2   . VAL A 1 172 ? 6.018  22.780 30.794 1.00 20.05 ? 163 VAL A CG2   1 
ATOM   1213 N N     . VAL A 1 173 ? 4.440  20.074 27.400 1.00 18.20 ? 164 VAL A N     1 
ATOM   1214 C CA    . VAL A 1 173 ? 4.370  19.248 26.203 1.00 18.91 ? 164 VAL A CA    1 
ATOM   1215 C C     . VAL A 1 173 ? 3.618  19.975 25.102 1.00 18.68 ? 164 VAL A C     1 
ATOM   1216 O O     . VAL A 1 173 ? 4.023  19.947 23.934 1.00 17.82 ? 164 VAL A O     1 
ATOM   1217 C CB    . VAL A 1 173 ? 3.738  17.880 26.512 1.00 18.67 ? 164 VAL A CB    1 
ATOM   1218 C CG1   . VAL A 1 173 ? 3.482  17.075 25.218 1.00 20.74 ? 164 VAL A CG1   1 
ATOM   1219 C CG2   . VAL A 1 173 ? 4.665  17.054 27.432 1.00 20.87 ? 164 VAL A CG2   1 
ATOM   1220 N N     . GLU A 1 174 ? 2.516  20.654 25.452 1.00 20.03 ? 165 GLU A N     1 
ATOM   1221 C CA    . GLU A 1 174 ? 1.772  21.341 24.417 1.00 21.24 ? 165 GLU A CA    1 
ATOM   1222 C C     . GLU A 1 174 ? 2.544  22.545 23.885 1.00 20.62 ? 165 GLU A C     1 
ATOM   1223 O O     . GLU A 1 174 ? 2.437  22.870 22.692 1.00 21.65 ? 165 GLU A O     1 
ATOM   1224 C CB    . GLU A 1 174 ? 0.388  21.691 24.937 1.00 22.47 ? 165 GLU A CB    1 
ATOM   1225 C CG    . GLU A 1 174 ? -0.283 22.666 24.050 1.00 39.43 ? 165 GLU A CG    1 
ATOM   1226 C CD    . GLU A 1 174 ? -0.990 21.946 22.910 1.00 61.23 ? 165 GLU A CD    1 
ATOM   1227 O OE1   . GLU A 1 174 ? -1.107 20.671 22.962 1.00 35.03 ? 165 GLU A OE1   1 
ATOM   1228 O OE2   . GLU A 1 174 ? -1.381 22.667 21.948 1.00 50.74 ? 165 GLU A OE2   1 
ATOM   1229 N N     . ASP A 1 175 ? 3.421  23.123 24.693 1.00 18.90 ? 166 ASP A N     1 
ATOM   1230 C CA    . ASP A 1 175 ? 4.316  24.153 24.148 1.00 18.43 ? 166 ASP A CA    1 
ATOM   1231 C C     . ASP A 1 175 ? 5.271  23.615 23.083 1.00 17.58 ? 166 ASP A C     1 
ATOM   1232 O O     . ASP A 1 175 ? 5.538  24.299 22.075 1.00 18.25 ? 166 ASP A O     1 
ATOM   1233 C CB    . ASP A 1 175 ? 5.089  24.947 25.203 1.00 20.04 ? 166 ASP A CB    1 
ATOM   1234 C CG    . ASP A 1 175 ? 4.168  25.647 26.188 1.00 24.46 ? 166 ASP A CG    1 
ATOM   1235 O OD1   . ASP A 1 175 ? 3.259  26.340 25.708 1.00 26.94 ? 166 ASP A OD1   1 
ATOM   1236 O OD2   . ASP A 1 175 ? 4.541  25.791 27.387 1.00 25.80 ? 166 ASP A OD2   1 
ATOM   1237 N N     . TYR A 1 176 ? 5.841  22.431 23.312 1.00 17.80 ? 167 TYR A N     1 
ATOM   1238 C CA    . TYR A 1 176 ? 6.646  21.807 22.279 1.00 17.12 ? 167 TYR A CA    1 
ATOM   1239 C C     . TYR A 1 176 ? 5.824  21.572 21.033 1.00 17.37 ? 167 TYR A C     1 
ATOM   1240 O O     . TYR A 1 176 ? 6.322  21.800 19.931 1.00 18.13 ? 167 TYR A O     1 
ATOM   1241 C CB    . TYR A 1 176 ? 7.210  20.480 22.755 1.00 19.11 ? 167 TYR A CB    1 
ATOM   1242 C CG    . TYR A 1 176 ? 8.445  20.576 23.667 1.00 17.59 ? 167 TYR A CG    1 
ATOM   1243 C CD1   . TYR A 1 176 ? 9.710  20.830 23.129 1.00 16.48 ? 167 TYR A CD1   1 
ATOM   1244 C CD2   . TYR A 1 176 ? 8.329  20.421 25.033 1.00 16.44 ? 167 TYR A CD2   1 
ATOM   1245 C CE1   . TYR A 1 176 ? 10.852 20.902 23.958 1.00 16.49 ? 167 TYR A CE1   1 
ATOM   1246 C CE2   . TYR A 1 176 ? 9.447  20.490 25.889 1.00 16.25 ? 167 TYR A CE2   1 
ATOM   1247 C CZ    . TYR A 1 176 ? 10.679 20.730 25.328 1.00 17.70 ? 167 TYR A CZ    1 
ATOM   1248 O OH    . TYR A 1 176 ? 11.794 20.782 26.170 1.00 17.94 ? 167 TYR A OH    1 
ATOM   1249 N N     . ARG A 1 177 ? 4.591  21.051 21.200 1.00 18.73 ? 168 ARG A N     1 
ATOM   1250 C CA    . ARG A 1 177 ? 3.744  20.760 20.031 1.00 19.32 ? 168 ARG A CA    1 
ATOM   1251 C C     . ARG A 1 177 ? 3.445  22.019 19.231 1.00 17.86 ? 168 ARG A C     1 
ATOM   1252 O O     . ARG A 1 177 ? 3.578  22.017 17.993 1.00 20.34 ? 168 ARG A O     1 
ATOM   1253 C CB    . ARG A 1 177 ? 2.436  20.123 20.500 1.00 21.10 ? 168 ARG A CB    1 
ATOM   1254 C CG    . ARG A 1 177 ? 1.573  19.627 19.339 1.00 23.04 ? 168 ARG A CG    1 
ATOM   1255 C CD    . ARG A 1 177 ? 0.131  19.247 19.837 1.00 28.48 ? 168 ARG A CD    1 
ATOM   1256 N NE    . ARG A 1 177 ? -0.857 19.522 18.798 1.00 57.23 ? 168 ARG A NE    1 
ATOM   1257 C CZ    . ARG A 1 177 ? -1.517 20.665 18.654 1.00 47.39 ? 168 ARG A CZ    1 
ATOM   1258 N NH1   . ARG A 1 177 ? -1.391 21.654 19.521 1.00 44.50 ? 168 ARG A NH1   1 
ATOM   1259 N NH2   . ARG A 1 177 ? -2.343 20.812 17.621 1.00 69.07 ? 168 ARG A NH2   1 
ATOM   1260 N N     . ARG A 1 178 ? 3.055  23.079 19.925 1.00 18.96 ? 169 ARG A N     1 
ATOM   1261 C CA    . ARG A 1 178 ? 2.758  24.330 19.220 1.00 18.73 ? 169 ARG A CA    1 
ATOM   1262 C C     . ARG A 1 178 ? 3.990  24.892 18.519 1.00 21.77 ? 169 ARG A C     1 
ATOM   1263 O O     . ARG A 1 178 ? 3.901  25.413 17.396 1.00 21.64 ? 169 ARG A O     1 
ATOM   1264 C CB    . ARG A 1 178 ? 2.203  25.354 20.202 1.00 22.82 ? 169 ARG A CB    1 
ATOM   1265 C CG    . ARG A 1 178 ? 0.889  24.933 20.859 1.00 34.58 ? 169 ARG A CG    1 
ATOM   1266 C CD    . ARG A 1 178 ? 0.377  26.107 21.727 1.00 56.21 ? 169 ARG A CD    1 
ATOM   1267 N NE    . ARG A 1 178 ? -1.029 25.995 22.104 1.00 69.58 ? 169 ARG A NE    1 
ATOM   1268 C CZ    . ARG A 1 178 ? -1.454 25.760 23.341 1.00 70.91 ? 169 ARG A CZ    1 
ATOM   1269 N NH1   . ARG A 1 178 ? -0.616 25.732 24.369 1.00 56.97 ? 169 ARG A NH1   1 
ATOM   1270 N NH2   . ARG A 1 178 ? -2.756 25.584 23.560 1.00 72.71 ? 169 ARG A NH2   1 
ATOM   1271 N N     . SER A 1 179 ? 5.155  24.824 19.187 1.00 20.58 ? 170 SER A N     1 
ATOM   1272 C CA    . SER A 1 179 ? 6.358  25.354 18.579 1.00 17.39 ? 170 SER A CA    1 
ATOM   1273 C C     . SER A 1 179 ? 6.783  24.523 17.392 1.00 18.54 ? 170 SER A C     1 
ATOM   1274 O O     . SER A 1 179 ? 7.328  25.073 16.436 1.00 18.93 ? 170 SER A O     1 
ATOM   1275 C CB    . SER A 1 179 ? 7.503  25.416 19.615 1.00 21.71 ? 170 SER A CB    1 
ATOM   1276 O OG    . SER A 1 179 ? 7.160  26.345 20.628 1.00 22.74 ? 170 SER A OG    1 
ATOM   1277 N N     . ALA A 1 180 ? 6.563  23.206 17.421 1.00 18.86 ? 171 ALA A N     1 
ATOM   1278 C CA    . ALA A 1 180 ? 6.859  22.378 16.248 1.00 18.22 ? 171 ALA A CA    1 
ATOM   1279 C C     . ALA A 1 180 ? 5.991  22.803 15.072 1.00 18.34 ? 171 ALA A C     1 
ATOM   1280 O O     . ALA A 1 180 ? 6.479  22.885 13.932 1.00 19.97 ? 171 ALA A O     1 
ATOM   1281 C CB    . ALA A 1 180 ? 6.663  20.894 16.551 1.00 19.21 ? 171 ALA A CB    1 
ATOM   1282 N N     . LEU A 1 181 ? 4.711  23.039 15.337 1.00 19.10 ? 172 LEU A N     1 
ATOM   1283 C CA    . LEU A 1 181 ? 3.833  23.455 14.237 1.00 19.12 ? 172 LEU A CA    1 
ATOM   1284 C C     . LEU A 1 181 ? 4.259  24.824 13.724 1.00 18.92 ? 172 LEU A C     1 
ATOM   1285 O O     . LEU A 1 181 ? 4.265  25.055 12.496 1.00 20.10 ? 172 LEU A O     1 
ATOM   1286 C CB    . LEU A 1 181 ? 2.397  23.489 14.734 1.00 20.14 ? 172 LEU A CB    1 
ATOM   1287 C CG    . LEU A 1 181 ? 1.795  22.109 14.916 1.00 21.62 ? 172 LEU A CG    1 
ATOM   1288 C CD1   . LEU A 1 181 ? 0.510  22.243 15.720 1.00 25.27 ? 172 LEU A CD1   1 
ATOM   1289 C CD2   . LEU A 1 181 ? 1.515  21.437 13.566 1.00 26.00 ? 172 LEU A CD2   1 
ATOM   1290 N N     . ASN A 1 182 ? 4.695  25.715 14.640 1.00 18.85 ? 173 ASN A N     1 
ATOM   1291 C CA    . ASN A 1 182 ? 5.196  27.019 14.215 1.00 17.94 ? 173 ASN A CA    1 
ATOM   1292 C C     . ASN A 1 182 ? 6.456  26.884 13.367 1.00 19.87 ? 173 ASN A C     1 
ATOM   1293 O O     . ASN A 1 182 ? 6.663  27.643 12.406 1.00 19.81 ? 173 ASN A O     1 
ATOM   1294 C CB    . ASN A 1 182 ? 5.484  27.878 15.435 1.00 21.53 ? 173 ASN A CB    1 
ATOM   1295 C CG    . ASN A 1 182 ? 4.232  28.437 16.061 1.00 26.80 ? 173 ASN A CG    1 
ATOM   1296 O OD1   . ASN A 1 182 ? 3.133  28.363 15.494 1.00 27.59 ? 173 ASN A OD1   1 
ATOM   1297 N ND2   . ASN A 1 182 ? 4.392  29.047 17.215 1.00 26.62 ? 173 ASN A ND2   1 
ATOM   1298 N N     . ALA A 1 183 ? 7.331  25.916 13.700 1.00 17.90 ? 174 ALA A N     1 
ATOM   1299 C CA    . ALA A 1 183 ? 8.523  25.757 12.897 1.00 16.97 ? 174 ALA A CA    1 
ATOM   1300 C C     . ALA A 1 183 ? 8.186  25.326 11.480 1.00 18.32 ? 174 ALA A C     1 
ATOM   1301 O O     . ALA A 1 183 ? 8.775  25.832 10.523 1.00 18.74 ? 174 ALA A O     1 
ATOM   1302 C CB    . ALA A 1 183 ? 9.463  24.724 13.555 1.00 17.54 ? 174 ALA A CB    1 
ATOM   1303 N N     . ILE A 1 184 ? 7.259  24.375 11.344 1.00 17.94 ? 175 ILE A N     1 
ATOM   1304 C CA    . ILE A 1 184 ? 6.798  23.998 9.999  1.00 20.31 ? 175 ILE A CA    1 
ATOM   1305 C C     . ILE A 1 184 ? 6.192  25.207 9.282  1.00 22.76 ? 175 ILE A C     1 
ATOM   1306 O O     . ILE A 1 184 ? 6.446  25.404 8.090  1.00 21.39 ? 175 ILE A O     1 
ATOM   1307 C CB    . ILE A 1 184 ? 5.801  22.838 10.130 1.00 21.31 ? 175 ILE A CB    1 
ATOM   1308 C CG1   . ILE A 1 184 ? 6.482  21.583 10.672 1.00 23.52 ? 175 ILE A CG1   1 
ATOM   1309 C CG2   . ILE A 1 184 ? 5.116  22.548 8.758  1.00 24.75 ? 175 ILE A CG2   1 
ATOM   1310 C CD1   . ILE A 1 184 ? 7.717  21.149 9.921  1.00 27.11 ? 175 ILE A CD1   1 
ATOM   1311 N N     . GLU A 1 185 ? 5.417  26.032 9.994  1.00 20.53 ? 176 GLU A N     1 
ATOM   1312 C CA    . GLU A 1 185 ? 4.832  27.237 9.377  1.00 21.65 ? 176 GLU A CA    1 
ATOM   1313 C C     . GLU A 1 185 ? 5.914  28.181 8.832  1.00 25.61 ? 176 GLU A C     1 
ATOM   1314 O O     . GLU A 1 185 ? 5.747  28.802 7.770  1.00 25.72 ? 176 GLU A O     1 
ATOM   1315 C CB    . GLU A 1 185 ? 3.936  27.965 10.390 1.00 23.23 ? 176 GLU A CB    1 
ATOM   1316 C CG    . GLU A 1 185 ? 3.238  29.190 9.767  1.00 26.68 ? 176 GLU A CG    1 
ATOM   1317 C CD    . GLU A 1 185 ? 2.360  29.937 10.734 1.00 39.56 ? 176 GLU A CD    1 
ATOM   1318 O OE1   . GLU A 1 185 ? 1.960  29.334 11.757 1.00 42.42 ? 176 GLU A OE1   1 
ATOM   1319 O OE2   . GLU A 1 185 ? 2.041  31.118 10.441 1.00 40.45 ? 176 GLU A OE2   1 
ATOM   1320 N N     . ALA A 1 186 ? 7.050  28.298 9.520  1.00 19.75 ? 177 ALA A N     1 
ATOM   1321 C CA    . ALA A 1 186 ? 8.149  29.124 9.049  1.00 19.41 ? 177 ALA A CA    1 
ATOM   1322 C C     . ALA A 1 186 ? 8.929  28.488 7.939  1.00 19.96 ? 177 ALA A C     1 
ATOM   1323 O O     . ALA A 1 186 ? 9.814  29.148 7.367  1.00 23.13 ? 177 ALA A O     1 
ATOM   1324 C CB    . ALA A 1 186 ? 9.108  29.415 10.212 1.00 20.39 ? 177 ALA A CB    1 
ATOM   1325 N N     . GLY A 1 187 ? 8.605  27.246 7.590  1.00 20.05 ? 178 GLY A N     1 
ATOM   1326 C CA    . GLY A 1 187 ? 9.251  26.570 6.508  1.00 19.52 ? 178 GLY A CA    1 
ATOM   1327 C C     . GLY A 1 187 ? 10.353 25.611 6.896  1.00 17.42 ? 178 GLY A C     1 
ATOM   1328 O O     . GLY A 1 187 ? 10.958 24.988 6.025  1.00 20.46 ? 178 GLY A O     1 
ATOM   1329 N N     . PHE A 1 188 ? 10.667 25.508 8.189  1.00 17.30 ? 179 PHE A N     1 
ATOM   1330 C CA    . PHE A 1 188 ? 11.699 24.534 8.550  1.00 17.55 ? 179 PHE A CA    1 
ATOM   1331 C C     . PHE A 1 188 ? 11.365 23.145 8.049  1.00 17.13 ? 179 PHE A C     1 
ATOM   1332 O O     . PHE A 1 188 ? 10.202 22.736 8.005  1.00 19.52 ? 179 PHE A O     1 
ATOM   1333 C CB    . PHE A 1 188 ? 11.828 24.442 10.085 1.00 18.88 ? 179 PHE A CB    1 
ATOM   1334 C CG    . PHE A 1 188 ? 12.609 25.570 10.702 1.00 17.16 ? 179 PHE A CG    1 
ATOM   1335 C CD1   . PHE A 1 188 ? 13.978 25.551 10.652 1.00 17.38 ? 179 PHE A CD1   1 
ATOM   1336 C CD2   . PHE A 1 188 ? 11.951 26.640 11.301 1.00 16.82 ? 179 PHE A CD2   1 
ATOM   1337 C CE1   . PHE A 1 188 ? 14.705 26.613 11.194 1.00 18.30 ? 179 PHE A CE1   1 
ATOM   1338 C CE2   . PHE A 1 188 ? 12.684 27.690 11.876 1.00 16.87 ? 179 PHE A CE2   1 
ATOM   1339 C CZ    . PHE A 1 188 ? 14.070 27.641 11.815 1.00 17.37 ? 179 PHE A CZ    1 
ATOM   1340 N N     . ASP A 1 189 ? 12.422 22.377 7.775  1.00 16.61 ? 180 ASP A N     1 
ATOM   1341 C CA    . ASP A 1 189 ? 12.215 20.998 7.359  1.00 17.85 ? 180 ASP A CA    1 
ATOM   1342 C C     . ASP A 1 189 ? 11.797 20.096 8.504  1.00 19.75 ? 180 ASP A C     1 
ATOM   1343 O O     . ASP A 1 189 ? 11.194 19.024 8.283  1.00 19.18 ? 180 ASP A O     1 
ATOM   1344 C CB    . ASP A 1 189 ? 13.385 20.424 6.604  1.00 19.23 ? 180 ASP A CB    1 
ATOM   1345 C CG    . ASP A 1 189 ? 13.763 21.309 5.454  1.00 22.16 ? 180 ASP A CG    1 
ATOM   1346 O OD1   . ASP A 1 189 ? 13.200 21.025 4.407  1.00 26.41 ? 180 ASP A OD1   1 
ATOM   1347 O OD2   . ASP A 1 189 ? 14.740 22.095 5.460  1.00 19.90 ? 180 ASP A OD2   1 
ATOM   1348 N N     . GLY A 1 190 ? 12.123 20.493 9.730  1.00 18.86 ? 181 GLY A N     1 
ATOM   1349 C CA    . GLY A 1 190 ? 11.802 19.686 10.870 1.00 18.72 ? 181 GLY A CA    1 
ATOM   1350 C C     . GLY A 1 190 ? 12.305 20.380 12.107 1.00 16.65 ? 181 GLY A C     1 
ATOM   1351 O O     . GLY A 1 190 ? 12.707 21.537 12.065 1.00 16.77 ? 181 GLY A O     1 
ATOM   1352 N N     . ILE A 1 191 ? 12.207 19.647 13.204 1.00 16.11 ? 182 ILE A N     1 
ATOM   1353 C CA    . ILE A 1 191 ? 12.632 20.158 14.508 1.00 15.35 ? 182 ILE A CA    1 
ATOM   1354 C C     . ILE A 1 191 ? 13.495 19.122 15.197 1.00 15.13 ? 182 ILE A C     1 
ATOM   1355 O O     . ILE A 1 191 ? 13.390 17.928 14.951 1.00 16.28 ? 182 ILE A O     1 
ATOM   1356 C CB    . ILE A 1 191 ? 11.467 20.578 15.445 1.00 15.87 ? 182 ILE A CB    1 
ATOM   1357 C CG1   . ILE A 1 191 ? 10.550 19.403 15.862 1.00 16.66 ? 182 ILE A CG1   1 
ATOM   1358 C CG2   . ILE A 1 191 ? 10.649 21.681 14.708 1.00 17.02 ? 182 ILE A CG2   1 
ATOM   1359 C CD1   . ILE A 1 191 ? 11.054 18.691 17.150 1.00 18.26 ? 182 ILE A CD1   1 
ATOM   1360 N N     . GLU A 1 192 ? 14.325 19.598 16.140 1.00 15.81 ? 183 GLU A N     1 
ATOM   1361 C CA    . GLU A 1 192 ? 15.097 18.723 17.012 1.00 15.95 ? 183 GLU A CA    1 
ATOM   1362 C C     . GLU A 1 192 ? 14.676 19.016 18.444 1.00 15.65 ? 183 GLU A C     1 
ATOM   1363 O O     . GLU A 1 192 ? 14.635 20.160 18.877 1.00 16.06 ? 183 GLU A O     1 
ATOM   1364 C CB    . GLU A 1 192 ? 16.601 19.022 16.884 1.00 16.21 ? 183 GLU A CB    1 
ATOM   1365 C CG    . GLU A 1 192 ? 17.441 18.133 17.854 1.00 17.57 ? 183 GLU A CG    1 
ATOM   1366 C CD    . GLU A 1 192 ? 18.917 18.302 17.654 1.00 17.32 ? 183 GLU A CD    1 
ATOM   1367 O OE1   . GLU A 1 192 ? 19.479 17.610 16.788 1.00 17.12 ? 183 GLU A OE1   1 
ATOM   1368 O OE2   . GLU A 1 192 ? 19.549 19.102 18.368 1.00 19.11 ? 183 GLU A OE2   1 
ATOM   1369 N N     . ILE A 1 193 ? 14.387 17.981 19.204 1.00 15.34 ? 184 ILE A N     1 
ATOM   1370 C CA    . ILE A 1 193 ? 14.085 18.145 20.631 1.00 15.76 ? 184 ILE A CA    1 
ATOM   1371 C C     . ILE A 1 193 ? 15.404 18.225 21.408 1.00 15.90 ? 184 ILE A C     1 
ATOM   1372 O O     . ILE A 1 193 ? 16.193 17.265 21.370 1.00 17.29 ? 184 ILE A O     1 
ATOM   1373 C CB    . ILE A 1 193 ? 13.224 16.971 21.124 1.00 15.64 ? 184 ILE A CB    1 
ATOM   1374 C CG1   . ILE A 1 193 ? 11.834 16.955 20.414 1.00 16.53 ? 184 ILE A CG1   1 
ATOM   1375 C CG2   . ILE A 1 193 ? 13.125 16.990 22.666 1.00 17.80 ? 184 ILE A CG2   1 
ATOM   1376 C CD1   . ILE A 1 193 ? 11.024 18.232 20.693 1.00 18.04 ? 184 ILE A CD1   1 
ATOM   1377 N N     . HIS A 1 194 ? 15.640 19.346 22.111 1.00 15.48 ? 185 HIS A N     1 
ATOM   1378 C CA    . HIS A 1 194 ? 16.851 19.436 22.949 1.00 14.45 ? 185 HIS A CA    1 
ATOM   1379 C C     . HIS A 1 194 ? 16.585 18.733 24.279 1.00 15.60 ? 185 HIS A C     1 
ATOM   1380 O O     . HIS A 1 194 ? 15.952 19.284 25.168 1.00 17.04 ? 185 HIS A O     1 
ATOM   1381 C CB    . HIS A 1 194 ? 17.269 20.891 23.058 1.00 15.36 ? 185 HIS A CB    1 
ATOM   1382 C CG    . HIS A 1 194 ? 18.460 21.133 23.906 1.00 15.06 ? 185 HIS A CG    1 
ATOM   1383 N ND1   . HIS A 1 194 ? 19.204 20.115 24.506 1.00 16.56 ? 185 HIS A ND1   1 
ATOM   1384 C CD2   . HIS A 1 194 ? 19.219 22.248 23.956 1.00 16.85 ? 185 HIS A CD2   1 
ATOM   1385 C CE1   . HIS A 1 194 ? 20.295 20.667 25.033 1.00 17.89 ? 185 HIS A CE1   1 
ATOM   1386 N NE2   . HIS A 1 194 ? 20.330 21.957 24.711 1.00 18.61 ? 185 HIS A NE2   1 
ATOM   1387 N N     . GLY A 1 195 ? 17.015 17.498 24.368 1.00 15.31 ? 186 GLY A N     1 
ATOM   1388 C CA    . GLY A 1 195 ? 16.852 16.707 25.590 1.00 15.84 ? 186 GLY A CA    1 
ATOM   1389 C C     . GLY A 1 195 ? 18.181 16.462 26.290 1.00 15.85 ? 186 GLY A C     1 
ATOM   1390 O O     . GLY A 1 195 ? 18.315 15.453 26.989 1.00 18.22 ? 186 GLY A O     1 
ATOM   1391 N N     . ALA A 1 196 ? 19.139 17.352 26.131 1.00 16.55 ? 187 ALA A N     1 
ATOM   1392 C CA    . ALA A 1 196 ? 20.513 17.141 26.561 1.00 18.23 ? 187 ALA A CA    1 
ATOM   1393 C C     . ALA A 1 196 ? 20.928 18.208 27.582 1.00 16.39 ? 187 ALA A C     1 
ATOM   1394 O O     . ALA A 1 196 ? 20.178 19.148 27.920 1.00 17.08 ? 187 ALA A O     1 
ATOM   1395 C CB    . ALA A 1 196 ? 21.437 17.162 25.341 1.00 18.69 ? 187 ALA A CB    1 
ATOM   1396 N N     . HIS A 1 197 ? 22.157 18.020 28.100 1.00 17.59 ? 188 HIS A N     1 
ATOM   1397 C CA    . HIS A 1 197 ? 22.959 19.090 28.741 1.00 17.09 ? 188 HIS A CA    1 
ATOM   1398 C C     . HIS A 1 197 ? 22.350 19.675 30.014 1.00 19.50 ? 188 HIS A C     1 
ATOM   1399 O O     . HIS A 1 197 ? 22.591 20.837 30.337 1.00 19.36 ? 188 HIS A O     1 
ATOM   1400 C CB    . HIS A 1 197 ? 23.347 20.199 27.759 1.00 18.69 ? 188 HIS A CB    1 
ATOM   1401 C CG    . HIS A 1 197 ? 24.010 19.697 26.535 1.00 16.55 ? 188 HIS A CG    1 
ATOM   1402 N ND1   . HIS A 1 197 ? 23.900 20.346 25.327 1.00 20.94 ? 188 HIS A ND1   1 
ATOM   1403 C CD2   . HIS A 1 197 ? 24.704 18.555 26.303 1.00 23.92 ? 188 HIS A CD2   1 
ATOM   1404 C CE1   . HIS A 1 197 ? 24.568 19.671 24.410 1.00 23.56 ? 188 HIS A CE1   1 
ATOM   1405 N NE2   . HIS A 1 197 ? 25.075 18.582 24.976 1.00 25.44 ? 188 HIS A NE2   1 
ATOM   1406 N N     . GLY A 1 198 ? 21.574 18.898 30.736 1.00 18.54 ? 189 GLY A N     1 
ATOM   1407 C CA    . GLY A 1 198 ? 21.073 19.371 32.031 1.00 16.49 ? 189 GLY A CA    1 
ATOM   1408 C C     . GLY A 1 198 ? 19.908 20.323 31.964 1.00 16.94 ? 189 GLY A C     1 
ATOM   1409 O O     . GLY A 1 198 ? 19.579 20.944 32.985 1.00 16.92 ? 189 GLY A O     1 
ATOM   1410 N N     . TYR A 1 199 ? 19.248 20.468 30.779 1.00 15.79 ? 190 TYR A N     1 
ATOM   1411 C CA    . TYR A 1 199 ? 18.122 21.375 30.626 1.00 15.96 ? 190 TYR A CA    1 
ATOM   1412 C C     . TYR A 1 199 ? 16.845 20.613 30.987 1.00 16.80 ? 190 TYR A C     1 
ATOM   1413 O O     . TYR A 1 199 ? 16.932 19.589 31.663 1.00 15.80 ? 190 TYR A O     1 
ATOM   1414 C CB    . TYR A 1 199 ? 18.163 22.018 29.241 1.00 16.19 ? 190 TYR A CB    1 
ATOM   1415 C CG    . TYR A 1 199 ? 19.380 22.897 29.083 1.00 16.74 ? 190 TYR A CG    1 
ATOM   1416 C CD1   . TYR A 1 199 ? 19.555 24.027 29.895 1.00 17.34 ? 190 TYR A CD1   1 
ATOM   1417 C CD2   . TYR A 1 199 ? 20.382 22.585 28.197 1.00 17.04 ? 190 TYR A CD2   1 
ATOM   1418 C CE1   . TYR A 1 199 ? 20.700 24.831 29.775 1.00 16.55 ? 190 TYR A CE1   1 
ATOM   1419 C CE2   . TYR A 1 199 ? 21.509 23.373 28.070 1.00 18.81 ? 190 TYR A CE2   1 
ATOM   1420 C CZ    . TYR A 1 199 ? 21.633 24.532 28.842 1.00 18.49 ? 190 TYR A CZ    1 
ATOM   1421 O OH    . TYR A 1 199 ? 22.743 25.362 28.760 1.00 22.73 ? 190 TYR A OH    1 
ATOM   1422 N N     . LEU A 1 200 ? 15.649 21.131 30.644 1.00 15.87 ? 191 LEU A N     1 
ATOM   1423 C CA    . LEU A 1 200 ? 14.438 20.640 31.301 1.00 15.80 ? 191 LEU A CA    1 
ATOM   1424 C C     . LEU A 1 200 ? 14.248 19.149 31.138 1.00 15.81 ? 191 LEU A C     1 
ATOM   1425 O O     . LEU A 1 200 ? 13.958 18.429 32.118 1.00 16.54 ? 191 LEU A O     1 
ATOM   1426 C CB    . LEU A 1 200 ? 13.238 21.409 30.753 1.00 16.13 ? 191 LEU A CB    1 
ATOM   1427 C CG    . LEU A 1 200 ? 11.924 20.957 31.397 1.00 16.88 ? 191 LEU A CG    1 
ATOM   1428 C CD1   . LEU A 1 200 ? 11.844 21.277 32.870 1.00 19.52 ? 191 LEU A CD1   1 
ATOM   1429 C CD2   . LEU A 1 200 ? 10.689 21.573 30.718 1.00 18.15 ? 191 LEU A CD2   1 
ATOM   1430 N N     . ILE A 1 201 ? 14.337 18.659 29.905 1.00 15.35 ? 192 ILE A N     1 
ATOM   1431 C CA    . ILE A 1 201 ? 14.135 17.222 29.688 1.00 16.71 ? 192 ILE A CA    1 
ATOM   1432 C C     . ILE A 1 201 ? 15.152 16.402 30.489 1.00 16.04 ? 192 ILE A C     1 
ATOM   1433 O O     . ILE A 1 201 ? 14.792 15.372 31.117 1.00 15.47 ? 192 ILE A O     1 
ATOM   1434 C CB    . ILE A 1 201 ? 14.147 16.884 28.184 1.00 16.52 ? 192 ILE A CB    1 
ATOM   1435 C CG1   . ILE A 1 201 ? 12.869 17.462 27.544 1.00 17.69 ? 192 ILE A CG1   1 
ATOM   1436 C CG2   . ILE A 1 201 ? 14.260 15.357 27.994 1.00 17.68 ? 192 ILE A CG2   1 
ATOM   1437 C CD1   . ILE A 1 201 ? 12.898 17.498 26.021 1.00 17.55 ? 192 ILE A CD1   1 
ATOM   1438 N N     . ASP A 1 202 ? 16.432 16.808 30.449 1.00 16.61 ? 193 ASP A N     1 
ATOM   1439 C CA    . ASP A 1 202 ? 17.462 16.095 31.221 1.00 16.42 ? 193 ASP A CA    1 
ATOM   1440 C C     . ASP A 1 202 ? 17.231 16.171 32.721 1.00 18.10 ? 193 ASP A C     1 
ATOM   1441 O O     . ASP A 1 202 ? 17.621 15.257 33.446 1.00 19.38 ? 193 ASP A O     1 
ATOM   1442 C CB    . ASP A 1 202 ? 18.808 16.650 30.795 1.00 20.10 ? 193 ASP A CB    1 
ATOM   1443 C CG    . ASP A 1 202 ? 19.933 15.641 30.870 1.00 21.01 ? 193 ASP A CG    1 
ATOM   1444 O OD1   . ASP A 1 202 ? 19.755 14.459 30.524 1.00 23.20 ? 193 ASP A OD1   1 
ATOM   1445 O OD2   . ASP A 1 202 ? 21.060 16.112 31.202 1.00 22.35 ? 193 ASP A OD2   1 
ATOM   1446 N N     . GLN A 1 203 ? 16.572 17.234 33.210 1.00 15.62 ? 194 GLN A N     1 
ATOM   1447 C CA    . GLN A 1 203 ? 16.208 17.311 34.634 1.00 14.72 ? 194 GLN A CA    1 
ATOM   1448 C C     . GLN A 1 203 ? 15.188 16.252 35.016 1.00 16.20 ? 194 GLN A C     1 
ATOM   1449 O O     . GLN A 1 203 ? 15.058 15.917 36.211 1.00 18.06 ? 194 GLN A O     1 
ATOM   1450 C CB    . GLN A 1 203 ? 15.693 18.711 34.978 1.00 16.68 ? 194 GLN A CB    1 
ATOM   1451 C CG    . GLN A 1 203 ? 16.811 19.778 34.860 1.00 15.78 ? 194 GLN A CG    1 
ATOM   1452 C CD    . GLN A 1 203 ? 16.302 21.160 34.510 1.00 15.26 ? 194 GLN A CD    1 
ATOM   1453 O OE1   . GLN A 1 203 ? 15.230 21.565 34.946 1.00 17.05 ? 194 GLN A OE1   1 
ATOM   1454 N NE2   . GLN A 1 203 ? 17.102 21.907 33.792 1.00 16.10 ? 194 GLN A NE2   1 
ATOM   1455 N N     . PHE A 1 204 ? 14.411 15.754 34.048 1.00 15.71 ? 195 PHE A N     1 
ATOM   1456 C CA    . PHE A 1 204 ? 13.564 14.606 34.323 1.00 17.10 ? 195 PHE A CA    1 
ATOM   1457 C C     . PHE A 1 204 ? 14.306 13.279 34.115 1.00 16.13 ? 195 PHE A C     1 
ATOM   1458 O O     . PHE A 1 204 ? 14.087 12.326 34.864 1.00 17.41 ? 195 PHE A O     1 
ATOM   1459 C CB    . PHE A 1 204 ? 12.296 14.627 33.444 1.00 16.56 ? 195 PHE A CB    1 
ATOM   1460 C CG    . PHE A 1 204 ? 11.200 15.575 33.930 1.00 16.64 ? 195 PHE A CG    1 
ATOM   1461 C CD1   . PHE A 1 204 ? 11.242 16.942 33.593 1.00 17.81 ? 195 PHE A CD1   1 
ATOM   1462 C CD2   . PHE A 1 204 ? 10.204 15.133 34.763 1.00 15.14 ? 195 PHE A CD2   1 
ATOM   1463 C CE1   . PHE A 1 204 ? 10.252 17.802 34.087 1.00 18.52 ? 195 PHE A CE1   1 
ATOM   1464 C CE2   . PHE A 1 204 ? 9.222  15.943 35.261 1.00 17.69 ? 195 PHE A CE2   1 
ATOM   1465 C CZ    . PHE A 1 204 ? 9.243  17.310 34.959 1.00 18.33 ? 195 PHE A CZ    1 
ATOM   1466 N N     . LEU A 1 205 ? 15.164 13.195 33.102 1.00 15.33 ? 196 LEU A N     1 
ATOM   1467 C CA    . LEU A 1 205 ? 15.858 11.936 32.828 1.00 16.79 ? 196 LEU A CA    1 
ATOM   1468 C C     . LEU A 1 205 ? 16.842 11.528 33.924 1.00 18.49 ? 196 LEU A C     1 
ATOM   1469 O O     . LEU A 1 205 ? 16.939 10.321 34.244 1.00 19.10 ? 196 LEU A O     1 
ATOM   1470 C CB    . LEU A 1 205 ? 16.658 12.103 31.552 1.00 17.34 ? 196 LEU A CB    1 
ATOM   1471 C CG    . LEU A 1 205 ? 15.827 12.149 30.288 1.00 17.78 ? 196 LEU A CG    1 
ATOM   1472 C CD1   . LEU A 1 205 ? 16.723 12.486 29.078 1.00 19.88 ? 196 LEU A CD1   1 
ATOM   1473 C CD2   . LEU A 1 205 ? 15.049 10.858 30.012 1.00 18.79 ? 196 LEU A CD2   1 
ATOM   1474 N N     . LYS A 1 206 ? 17.630 12.473 34.440 1.00 18.41 ? 197 LYS A N     1 
ATOM   1475 C CA    . LYS A 1 206 ? 18.792 12.139 35.262 1.00 16.14 ? 197 LYS A CA    1 
ATOM   1476 C C     . LYS A 1 206 ? 18.402 11.876 36.702 1.00 19.43 ? 197 LYS A C     1 
ATOM   1477 O O     . LYS A 1 206 ? 17.781 12.735 37.332 1.00 17.98 ? 197 LYS A O     1 
ATOM   1478 C CB    . LYS A 1 206 ? 19.798 13.292 35.217 1.00 18.58 ? 197 LYS A CB    1 
ATOM   1479 C CG    . LYS A 1 206 ? 20.377 13.568 33.788 1.00 21.03 ? 197 LYS A CG    1 
ATOM   1480 C CD    . LYS A 1 206 ? 21.351 12.472 33.411 1.00 20.88 ? 197 LYS A CD    1 
ATOM   1481 C CE    . LYS A 1 206 ? 21.857 12.558 31.946 1.00 21.03 ? 197 LYS A CE    1 
ATOM   1482 N NZ    . LYS A 1 206 ? 22.730 13.737 31.789 1.00 24.51 ? 197 LYS A NZ    1 
ATOM   1483 N N     . ASP A 1 207 ? 18.812 10.710 37.233 1.00 19.50 ? 198 ASP A N     1 
ATOM   1484 C CA    . ASP A 1 207 ? 18.485 10.425 38.631 1.00 21.28 ? 198 ASP A CA    1 
ATOM   1485 C C     . ASP A 1 207 ? 19.265 11.288 39.616 1.00 22.78 ? 198 ASP A C     1 
ATOM   1486 O O     . ASP A 1 207 ? 18.836 11.394 40.778 1.00 25.14 ? 198 ASP A O     1 
ATOM   1487 C CB    . ASP A 1 207 ? 18.520 8.918  38.950 1.00 22.30 ? 198 ASP A CB    1 
ATOM   1488 C CG    . ASP A 1 207 ? 19.900 8.322  38.941 1.00 24.84 ? 198 ASP A CG    1 
ATOM   1489 O OD1   . ASP A 1 207 ? 20.917 9.015  38.746 1.00 25.78 ? 198 ASP A OD1   1 
ATOM   1490 O OD2   . ASP A 1 207 ? 19.990 7.054  39.067 1.00 29.01 ? 198 ASP A OD2   1 
ATOM   1491 N N     . GLY A 1 208 ? 20.303 11.999 39.170 1.00 19.19 ? 199 GLY A N     1 
ATOM   1492 C CA    . GLY A 1 208 ? 20.943 12.975 40.040 1.00 22.84 ? 199 GLY A CA    1 
ATOM   1493 C C     . GLY A 1 208 ? 20.167 14.264 40.206 1.00 26.41 ? 199 GLY A C     1 
ATOM   1494 O O     . GLY A 1 208 ? 20.565 15.108 41.012 1.00 27.59 ? 199 GLY A O     1 
ATOM   1495 N N     . ILE A 1 209 ? 19.107 14.477 39.424 1.00 20.27 ? 200 ILE A N     1 
ATOM   1496 C CA    . ILE A 1 209 ? 18.270 15.672 39.506 1.00 19.71 ? 200 ILE A CA    1 
ATOM   1497 C C     . ILE A 1 209 ? 16.843 15.321 39.895 1.00 19.84 ? 200 ILE A C     1 
ATOM   1498 O O     . ILE A 1 209 ? 16.244 15.956 40.779 1.00 22.84 ? 200 ILE A O     1 
ATOM   1499 C CB    . ILE A 1 209 ? 18.273 16.436 38.183 1.00 18.55 ? 200 ILE A CB    1 
ATOM   1500 C CG1   . ILE A 1 209 ? 19.681 16.841 37.745 1.00 22.10 ? 200 ILE A CG1   1 
ATOM   1501 C CG2   . ILE A 1 209 ? 17.339 17.662 38.274 1.00 22.43 ? 200 ILE A CG2   1 
ATOM   1502 C CD1   . ILE A 1 209 ? 19.680 17.502 36.341 1.00 21.37 ? 200 ILE A CD1   1 
ATOM   1503 N N     . ASN A 1 210 ? 16.278 14.283 39.258 1.00 18.47 ? 201 ASN A N     1 
ATOM   1504 C CA    . ASN A 1 210 ? 14.867 13.991 39.426 1.00 18.60 ? 201 ASN A CA    1 
ATOM   1505 C C     . ASN A 1 210 ? 14.692 13.275 40.750 1.00 21.16 ? 201 ASN A C     1 
ATOM   1506 O O     . ASN A 1 210 ? 14.990 12.091 40.861 1.00 23.35 ? 201 ASN A O     1 
ATOM   1507 C CB    . ASN A 1 210 ? 14.394 13.131 38.253 1.00 17.75 ? 201 ASN A CB    1 
ATOM   1508 C CG    . ASN A 1 210 ? 12.909 12.862 38.292 1.00 18.31 ? 201 ASN A CG    1 
ATOM   1509 O OD1   . ASN A 1 210 ? 12.265 12.922 39.349 1.00 20.87 ? 201 ASN A OD1   1 
ATOM   1510 N ND2   . ASN A 1 210 ? 12.335 12.558 37.124 1.00 18.34 ? 201 ASN A ND2   1 
ATOM   1511 N N     . ASP A 1 211 ? 14.207 14.028 41.738 1.00 21.56 ? 202 ASP A N     1 
ATOM   1512 C CA    . ASP A 1 211 ? 13.826 13.523 43.049 1.00 22.07 ? 202 ASP A CA    1 
ATOM   1513 C C     . ASP A 1 211 ? 12.316 13.386 43.226 1.00 27.70 ? 202 ASP A C     1 
ATOM   1514 O O     . ASP A 1 211 ? 11.831 13.401 44.368 1.00 27.88 ? 202 ASP A O     1 
ATOM   1515 C CB    . ASP A 1 211 ? 14.459 14.386 44.178 1.00 20.02 ? 202 ASP A CB    1 
ATOM   1516 C CG    . ASP A 1 211 ? 13.977 15.838 44.171 1.00 28.65 ? 202 ASP A CG    1 
ATOM   1517 O OD1   . ASP A 1 211 ? 13.266 16.273 43.217 1.00 24.39 ? 202 ASP A OD1   1 
ATOM   1518 O OD2   . ASP A 1 211 ? 14.309 16.598 45.141 1.00 27.95 ? 202 ASP A OD2   1 
ATOM   1519 N N     . ARG A 1 212 ? 11.558 13.246 42.134 1.00 22.49 ? 203 ARG A N     1 
ATOM   1520 C CA    . ARG A 1 212 ? 10.107 13.191 42.272 1.00 21.19 ? 203 ARG A CA    1 
ATOM   1521 C C     . ARG A 1 212 ? 9.666  11.845 42.822 1.00 22.16 ? 203 ARG A C     1 
ATOM   1522 O O     . ARG A 1 212 ? 10.299 10.826 42.583 1.00 22.74 ? 203 ARG A O     1 
ATOM   1523 C CB    . ARG A 1 212 ? 9.435  13.387 40.912 1.00 21.70 ? 203 ARG A CB    1 
ATOM   1524 C CG    . ARG A 1 212 ? 9.764  14.718 40.266 1.00 19.56 ? 203 ARG A CG    1 
ATOM   1525 C CD    . ARG A 1 212 ? 9.129  14.726 38.903 1.00 19.43 ? 203 ARG A CD    1 
ATOM   1526 N NE    . ARG A 1 212 ? 7.684  14.958 38.960 1.00 19.29 ? 203 ARG A NE    1 
ATOM   1527 C CZ    . ARG A 1 212 ? 7.108  16.147 38.893 1.00 19.13 ? 203 ARG A CZ    1 
ATOM   1528 N NH1   . ARG A 1 212 ? 7.828  17.280 38.828 1.00 19.29 ? 203 ARG A NH1   1 
ATOM   1529 N NH2   . ARG A 1 212 ? 5.768  16.224 38.867 1.00 21.46 ? 203 ARG A NH2   1 
ATOM   1530 N N     . THR A 1 213 ? 8.533  11.848 43.535 1.00 27.05 ? 204 THR A N     1 
ATOM   1531 C CA    . THR A 1 213 ? 7.918  10.622 44.040 1.00 23.90 ? 204 THR A CA    1 
ATOM   1532 C C     . THR A 1 213 ? 6.587  10.327 43.363 1.00 32.90 ? 204 THR A C     1 
ATOM   1533 O O     . THR A 1 213 ? 5.846  9.446  43.816 1.00 31.19 ? 204 THR A O     1 
ATOM   1534 C CB    . THR A 1 213 ? 7.780  10.670 45.576 1.00 31.10 ? 204 THR A CB    1 
ATOM   1535 O OG1   . THR A 1 213 ? 7.074  11.848 45.957 1.00 34.71 ? 204 THR A OG1   1 
ATOM   1536 C CG2   . THR A 1 213 ? 9.174  10.707 46.212 1.00 32.75 ? 204 THR A CG2   1 
ATOM   1537 N N     . ASP A 1 214 ? 6.272  11.016 42.273 1.00 23.12 ? 205 ASP A N     1 
ATOM   1538 C CA    . ASP A 1 214 ? 5.059  10.730 41.525 1.00 21.36 ? 205 ASP A CA    1 
ATOM   1539 C C     . ASP A 1 214 ? 5.423  9.866  40.314 1.00 23.12 ? 205 ASP A C     1 
ATOM   1540 O O     . ASP A 1 214 ? 6.509  9.272  40.260 1.00 23.83 ? 205 ASP A O     1 
ATOM   1541 C CB    . ASP A 1 214 ? 4.298  12.022 41.171 1.00 21.06 ? 205 ASP A CB    1 
ATOM   1542 C CG    . ASP A 1 214 ? 5.040  12.899 40.162 1.00 22.92 ? 205 ASP A CG    1 
ATOM   1543 O OD1   . ASP A 1 214 ? 6.196  12.606 39.770 1.00 21.93 ? 205 ASP A OD1   1 
ATOM   1544 O OD2   . ASP A 1 214 ? 4.445  13.939 39.785 1.00 21.50 ? 205 ASP A OD2   1 
ATOM   1545 N N     . GLU A 1 215 ? 4.549  9.828  39.312 1.00 20.96 ? 206 GLU A N     1 
ATOM   1546 C CA    . GLU A 1 215 ? 4.749  8.926  38.193 1.00 23.08 ? 206 GLU A CA    1 
ATOM   1547 C C     . GLU A 1 215 ? 5.782  9.428  37.193 1.00 21.75 ? 206 GLU A C     1 
ATOM   1548 O O     . GLU A 1 215 ? 6.068  8.753  36.200 1.00 21.89 ? 206 GLU A O     1 
ATOM   1549 C CB    . GLU A 1 215 ? 3.414  8.604  37.514 1.00 24.59 ? 206 GLU A CB    1 
ATOM   1550 C CG    . GLU A 1 215 ? 2.803  9.705  36.665 1.00 24.99 ? 206 GLU A CG    1 
ATOM   1551 C CD    . GLU A 1 215 ? 1.863  10.626 37.419 1.00 28.63 ? 206 GLU A CD    1 
ATOM   1552 O OE1   . GLU A 1 215 ? 1.970  10.757 38.674 1.00 28.85 ? 206 GLU A OE1   1 
ATOM   1553 O OE2   . GLU A 1 215 ? 1.050  11.257 36.692 1.00 32.37 ? 206 GLU A OE2   1 
ATOM   1554 N N     . TYR A 1 216 ? 6.382  10.600 37.446 1.00 19.85 ? 207 TYR A N     1 
ATOM   1555 C CA    . TYR A 1 216 ? 7.458  11.056 36.586 1.00 21.00 ? 207 TYR A CA    1 
ATOM   1556 C C     . TYR A 1 216 ? 8.811  10.912 37.268 1.00 22.31 ? 207 TYR A C     1 
ATOM   1557 O O     . TYR A 1 216 ? 9.794  11.409 36.733 1.00 22.38 ? 207 TYR A O     1 
ATOM   1558 C CB    . TYR A 1 216 ? 7.227  12.527 36.189 1.00 18.78 ? 207 TYR A CB    1 
ATOM   1559 C CG    . TYR A 1 216 ? 6.154  12.675 35.162 1.00 18.44 ? 207 TYR A CG    1 
ATOM   1560 C CD1   . TYR A 1 216 ? 4.808  12.702 35.539 1.00 21.61 ? 207 TYR A CD1   1 
ATOM   1561 C CD2   . TYR A 1 216 ? 6.479  12.854 33.808 1.00 18.10 ? 207 TYR A CD2   1 
ATOM   1562 C CE1   . TYR A 1 216 ? 3.787  12.854 34.538 1.00 22.04 ? 207 TYR A CE1   1 
ATOM   1563 C CE2   . TYR A 1 216 ? 5.490  13.018 32.838 1.00 19.85 ? 207 TYR A CE2   1 
ATOM   1564 C CZ    . TYR A 1 216 ? 4.148  13.004 33.210 1.00 21.72 ? 207 TYR A CZ    1 
ATOM   1565 O OH    . TYR A 1 216 ? 3.167  13.150 32.249 1.00 22.99 ? 207 TYR A OH    1 
ATOM   1566 N N     . GLY A 1 217 ? 8.886  10.221 38.417 1.00 19.92 ? 208 GLY A N     1 
ATOM   1567 C CA    . GLY A 1 217 ? 10.147 10.048 39.109 1.00 23.41 ? 208 GLY A CA    1 
ATOM   1568 C C     . GLY A 1 217 ? 10.349 8.606  39.531 1.00 20.94 ? 208 GLY A C     1 
ATOM   1569 O O     . GLY A 1 217 ? 9.437  7.821  39.501 1.00 24.03 ? 208 GLY A O     1 
ATOM   1570 N N     . GLY A 1 218 ? 11.585 8.305  39.926 1.00 22.52 ? 209 GLY A N     1 
ATOM   1571 C CA    . GLY A 1 218 ? 11.929 6.987  40.460 1.00 23.31 ? 209 GLY A CA    1 
ATOM   1572 C C     . GLY A 1 218 ? 12.490 6.097  39.384 1.00 22.67 ? 209 GLY A C     1 
ATOM   1573 O O     . GLY A 1 218 ? 13.668 6.205  38.982 1.00 24.66 ? 209 GLY A O     1 
ATOM   1574 N N     . SER A 1 219 ? 11.634 5.210  38.892 1.00 23.16 ? 210 SER A N     1 
ATOM   1575 C CA    . SER A 1 219 ? 12.106 4.194  37.975 1.00 23.82 ? 210 SER A CA    1 
ATOM   1576 C C     . SER A 1 219 ? 12.555 4.815  36.647 1.00 25.08 ? 210 SER A C     1 
ATOM   1577 O O     . SER A 1 219 ? 12.218 5.977  36.314 1.00 21.98 ? 210 SER A O     1 
ATOM   1578 C CB    . SER A 1 219 ? 11.000 3.182  37.684 1.00 24.15 ? 210 SER A CB    1 
ATOM   1579 O OG    . SER A 1 219 ? 9.923  3.850  37.019 1.00 23.26 ? 210 SER A OG    1 
ATOM   1580 N N     . LEU A 1 220 ? 13.328 4.049  35.876 1.00 24.60 ? 211 LEU A N     1 
ATOM   1581 C CA    . LEU A 1 220 ? 13.701 4.474  34.519 1.00 21.71 ? 211 LEU A CA    1 
ATOM   1582 C C     . LEU A 1 220 ? 12.486 4.790  33.680 1.00 25.23 ? 211 LEU A C     1 
ATOM   1583 O O     . LEU A 1 220 ? 12.473 5.796  32.952 1.00 21.93 ? 211 LEU A O     1 
ATOM   1584 C CB    . LEU A 1 220 ? 14.468 3.363  33.781 1.00 23.55 ? 211 LEU A CB    1 
ATOM   1585 C CG    . LEU A 1 220 ? 15.948 3.331  34.046 1.00 27.83 ? 211 LEU A CG    1 
ATOM   1586 C CD1   . LEU A 1 220 ? 16.553 2.016  33.506 1.00 29.78 ? 211 LEU A CD1   1 
ATOM   1587 C CD2   . LEU A 1 220 ? 16.592 4.598  33.466 1.00 26.37 ? 211 LEU A CD2   1 
ATOM   1588 N N     . ALA A 1 221 ? 11.448 3.953  33.767 1.00 21.35 ? 212 ALA A N     1 
ATOM   1589 C CA    . ALA A 1 221 ? 10.250 4.176  32.975 1.00 24.30 ? 212 ALA A CA    1 
ATOM   1590 C C     . ALA A 1 221 ? 9.643  5.504  33.331 1.00 22.90 ? 212 ALA A C     1 
ATOM   1591 O O     . ALA A 1 221 ? 9.260  6.285  32.445 1.00 22.12 ? 212 ALA A O     1 
ATOM   1592 C CB    . ALA A 1 221 ? 9.235  3.041  33.211 1.00 26.38 ? 212 ALA A CB    1 
ATOM   1593 N N     . ASN A 1 222 ? 9.570  5.789  34.633 1.00 20.02 ? 213 ASN A N     1 
ATOM   1594 C CA    . ASN A 1 222 ? 8.982  7.051  35.046 1.00 19.32 ? 213 ASN A CA    1 
ATOM   1595 C C     . ASN A 1 222 ? 9.841  8.222  34.596 1.00 21.32 ? 213 ASN A C     1 
ATOM   1596 O O     . ASN A 1 222 ? 9.304  9.232  34.127 1.00 19.17 ? 213 ASN A O     1 
ATOM   1597 C CB    . ASN A 1 222 ? 8.757  7.080  36.550 1.00 20.71 ? 213 ASN A CB    1 
ATOM   1598 C CG    . ASN A 1 222 ? 7.585  6.192  36.979 1.00 20.73 ? 213 ASN A CG    1 
ATOM   1599 O OD1   . ASN A 1 222 ? 6.926  5.609  36.139 1.00 25.09 ? 213 ASN A OD1   1 
ATOM   1600 N ND2   . ASN A 1 222 ? 7.288  6.182  38.277 1.00 22.32 ? 213 ASN A ND2   1 
ATOM   1601 N N     . ARG A 1 223 ? 11.162 8.138  34.763 1.00 19.21 ? 214 ARG A N     1 
ATOM   1602 C CA    . ARG A 1 223 ? 12.016 9.271  34.385 1.00 18.40 ? 214 ARG A CA    1 
ATOM   1603 C C     . ARG A 1 223 ? 12.010 9.497  32.870 1.00 17.94 ? 214 ARG A C     1 
ATOM   1604 O O     . ARG A 1 223 ? 12.249 10.637 32.428 1.00 18.42 ? 214 ARG A O     1 
ATOM   1605 C CB    . ARG A 1 223 ? 13.451 9.035  34.865 1.00 18.01 ? 214 ARG A CB    1 
ATOM   1606 C CG    . ARG A 1 223 ? 13.570 9.045  36.352 1.00 20.04 ? 214 ARG A CG    1 
ATOM   1607 C CD    . ARG A 1 223 ? 15.038 9.034  36.842 1.00 23.06 ? 214 ARG A CD    1 
ATOM   1608 N NE    . ARG A 1 223 ? 15.460 7.627  36.925 1.00 33.40 ? 214 ARG A NE    1 
ATOM   1609 C CZ    . ARG A 1 223 ? 16.574 7.121  36.425 1.00 31.15 ? 214 ARG A CZ    1 
ATOM   1610 N NH1   . ARG A 1 223 ? 17.351 7.804  35.594 1.00 31.60 ? 214 ARG A NH1   1 
ATOM   1611 N NH2   . ARG A 1 223 ? 16.939 5.904  36.794 1.00 32.65 ? 214 ARG A NH2   1 
ATOM   1612 N N     . CYS A 1 224 ? 11.712 8.493  32.049 1.00 18.28 ? 215 CYS A N     1 
ATOM   1613 C CA    . CYS A 1 224 ? 11.618 8.643  30.602 1.00 17.47 ? 215 CYS A CA    1 
ATOM   1614 C C     . CYS A 1 224 ? 10.250 9.077  30.134 1.00 17.84 ? 215 CYS A C     1 
ATOM   1615 O O     . CYS A 1 224 ? 10.083 9.300  28.936 1.00 18.68 ? 215 CYS A O     1 
ATOM   1616 C CB    . CYS A 1 224 ? 11.979 7.324  29.886 1.00 19.21 ? 215 CYS A CB    1 
ATOM   1617 S SG    . CYS A 1 224 ? 13.745 6.906  30.048 1.00 22.90 ? 215 CYS A SG    1 
ATOM   1618 N N     . LYS A 1 225 ? 9.269  9.193  31.028 1.00 18.24 ? 216 LYS A N     1 
ATOM   1619 C CA    . LYS A 1 225 ? 7.916  9.554  30.575 1.00 18.80 ? 216 LYS A CA    1 
ATOM   1620 C C     . LYS A 1 225 ? 7.907  10.914 29.920 1.00 18.54 ? 216 LYS A C     1 
ATOM   1621 O O     . LYS A 1 225 ? 7.278  11.090 28.876 1.00 18.98 ? 216 LYS A O     1 
ATOM   1622 C CB    . LYS A 1 225 ? 6.938  9.631  31.740 1.00 20.28 ? 216 LYS A CB    1 
ATOM   1623 C CG    . LYS A 1 225 ? 6.099  8.403  32.005 1.00 35.51 ? 216 LYS A CG    1 
ATOM   1624 C CD    . LYS A 1 225 ? 4.984  8.788  33.020 1.00 35.35 ? 216 LYS A CD    1 
ATOM   1625 C CE    . LYS A 1 225 ? 4.167  7.544  33.331 1.00 38.92 ? 216 LYS A CE    1 
ATOM   1626 N NZ    . LYS A 1 225 ? 4.704  6.852  34.541 1.00 31.33 ? 216 LYS A NZ    1 
ATOM   1627 N N     . PHE A 1 226 ? 8.601  11.897 30.489 1.00 16.22 ? 217 PHE A N     1 
ATOM   1628 C CA    . PHE A 1 226 ? 8.524  13.260 29.928 1.00 18.07 ? 217 PHE A CA    1 
ATOM   1629 C C     . PHE A 1 226 ? 9.070  13.322 28.500 1.00 17.68 ? 217 PHE A C     1 
ATOM   1630 O O     . PHE A 1 226 ? 8.393  13.824 27.588 1.00 18.74 ? 217 PHE A O     1 
ATOM   1631 C CB    . PHE A 1 226 ? 9.227  14.264 30.856 1.00 18.17 ? 217 PHE A CB    1 
ATOM   1632 C CG    . PHE A 1 226 ? 9.084  15.729 30.398 1.00 17.31 ? 217 PHE A CG    1 
ATOM   1633 C CD1   . PHE A 1 226 ? 7.835  16.270 30.059 1.00 20.85 ? 217 PHE A CD1   1 
ATOM   1634 C CD2   . PHE A 1 226 ? 10.200 16.498 30.181 1.00 20.31 ? 217 PHE A CD2   1 
ATOM   1635 C CE1   . PHE A 1 226 ? 7.707  17.631 29.644 1.00 22.82 ? 217 PHE A CE1   1 
ATOM   1636 C CE2   . PHE A 1 226 ? 10.088 17.822 29.764 1.00 20.09 ? 217 PHE A CE2   1 
ATOM   1637 C CZ    . PHE A 1 226 ? 8.833  18.382 29.496 1.00 20.69 ? 217 PHE A CZ    1 
ATOM   1638 N N     . ILE A 1 227 ? 10.277 12.779 28.254 1.00 17.65 ? 218 ILE A N     1 
ATOM   1639 C CA    . ILE A 1 227 ? 10.811 12.828 26.896 1.00 18.48 ? 218 ILE A CA    1 
ATOM   1640 C C     . ILE A 1 227 ? 9.905  12.043 25.952 1.00 17.36 ? 218 ILE A C     1 
ATOM   1641 O O     . ILE A 1 227 ? 9.702  12.456 24.799 1.00 18.01 ? 218 ILE A O     1 
ATOM   1642 C CB    . ILE A 1 227 ? 12.288 12.380 26.835 1.00 18.24 ? 218 ILE A CB    1 
ATOM   1643 C CG1   . ILE A 1 227 ? 12.874 12.824 25.479 1.00 17.67 ? 218 ILE A CG1   1 
ATOM   1644 C CG2   . ILE A 1 227 ? 12.440 10.847 27.031 1.00 18.33 ? 218 ILE A CG2   1 
ATOM   1645 C CD1   . ILE A 1 227 ? 14.366 12.522 25.344 1.00 20.32 ? 218 ILE A CD1   1 
ATOM   1646 N N     . THR A 1 228 ? 9.349  10.912 26.421 1.00 17.63 ? 219 THR A N     1 
ATOM   1647 C CA    . THR A 1 228 ? 8.495  10.139 25.522 1.00 19.20 ? 219 THR A CA    1 
ATOM   1648 C C     . THR A 1 228 ? 7.279  10.966 25.133 1.00 17.98 ? 219 THR A C     1 
ATOM   1649 O O     . THR A 1 228 ? 6.865  10.965 23.960 1.00 19.12 ? 219 THR A O     1 
ATOM   1650 C CB    . THR A 1 228 ? 8.036  8.877  26.229 1.00 20.07 ? 219 THR A CB    1 
ATOM   1651 O OG1   . THR A 1 228 ? 9.185  8.083  26.641 1.00 21.20 ? 219 THR A OG1   1 
ATOM   1652 C CG2   . THR A 1 228 ? 7.179  8.033  25.291 1.00 21.58 ? 219 THR A CG2   1 
ATOM   1653 N N     . GLN A 1 229 ? 6.676  11.648 26.103 1.00 17.52 ? 220 GLN A N     1 
ATOM   1654 C CA    . GLN A 1 229 ? 5.477  12.445 25.802 1.00 18.72 ? 220 GLN A CA    1 
ATOM   1655 C C     . GLN A 1 229 ? 5.787  13.663 24.927 1.00 19.00 ? 220 GLN A C     1 
ATOM   1656 O O     . GLN A 1 229 ? 4.968  14.031 24.068 1.00 18.83 ? 220 GLN A O     1 
ATOM   1657 C CB    . GLN A 1 229 ? 4.824  12.914 27.109 1.00 18.57 ? 220 GLN A CB    1 
ATOM   1658 C CG    . GLN A 1 229 ? 4.230  11.723 27.839 1.00 20.00 ? 220 GLN A CG    1 
ATOM   1659 C CD    . GLN A 1 229 ? 3.777  12.034 29.248 1.00 24.27 ? 220 GLN A CD    1 
ATOM   1660 O OE1   . GLN A 1 229 ? 3.917  13.111 29.748 1.00 23.36 ? 220 GLN A OE1   1 
ATOM   1661 N NE2   . GLN A 1 229 ? 3.324  10.989 29.926 1.00 29.52 ? 220 GLN A NE2   1 
ATOM   1662 N N     . VAL A 1 230 ? 6.955  14.280 25.089 1.00 17.35 ? 221 VAL A N     1 
ATOM   1663 C CA    . VAL A 1 230 ? 7.338  15.395 24.239 1.00 15.99 ? 221 VAL A CA    1 
ATOM   1664 C C     . VAL A 1 230 ? 7.508  14.913 22.812 1.00 17.73 ? 221 VAL A C     1 
ATOM   1665 O O     . VAL A 1 230 ? 6.966  15.516 21.873 1.00 17.98 ? 221 VAL A O     1 
ATOM   1666 C CB    . VAL A 1 230 ? 8.642  16.009 24.761 1.00 15.74 ? 221 VAL A CB    1 
ATOM   1667 C CG1   . VAL A 1 230 ? 9.205  17.008 23.733 1.00 17.41 ? 221 VAL A CG1   1 
ATOM   1668 C CG2   . VAL A 1 230 ? 8.390  16.781 26.083 1.00 18.38 ? 221 VAL A CG2   1 
ATOM   1669 N N     . VAL A 1 231 ? 8.265  13.814 22.631 1.00 18.14 ? 222 VAL A N     1 
ATOM   1670 C CA    . VAL A 1 231 ? 8.544  13.304 21.294 1.00 17.63 ? 222 VAL A CA    1 
ATOM   1671 C C     . VAL A 1 231 ? 7.255  12.820 20.649 1.00 19.75 ? 222 VAL A C     1 
ATOM   1672 O O     . VAL A 1 231 ? 7.001  13.148 19.481 1.00 19.83 ? 222 VAL A O     1 
ATOM   1673 C CB    . VAL A 1 231 ? 9.620  12.186 21.344 1.00 17.49 ? 222 VAL A CB    1 
ATOM   1674 C CG1   . VAL A 1 231 ? 9.788  11.566 19.946 1.00 22.45 ? 222 VAL A CG1   1 
ATOM   1675 C CG2   . VAL A 1 231 ? 10.967 12.815 21.794 1.00 18.82 ? 222 VAL A CG2   1 
ATOM   1676 N N     . GLN A 1 232 ? 6.388  12.121 21.415 1.00 18.26 ? 223 GLN A N     1 
ATOM   1677 C CA    . GLN A 1 232 ? 5.131  11.653 20.806 1.00 21.19 ? 223 GLN A CA    1 
ATOM   1678 C C     . GLN A 1 232 ? 4.280  12.837 20.357 1.00 20.14 ? 223 GLN A C     1 
ATOM   1679 O O     . GLN A 1 232 ? 3.636  12.781 19.293 1.00 21.91 ? 223 GLN A O     1 
ATOM   1680 C CB    . GLN A 1 232 ? 4.305  10.869 21.825 1.00 22.08 ? 223 GLN A CB    1 
ATOM   1681 C CG    . GLN A 1 232 ? 3.034  10.211 21.241 1.00 34.38 ? 223 GLN A CG    1 
ATOM   1682 C CD    . GLN A 1 232 ? 3.273  9.436  19.936 1.00 36.55 ? 223 GLN A CD    1 
ATOM   1683 O OE1   . GLN A 1 232 ? 3.837  8.336  19.985 1.00 35.70 ? 223 GLN A OE1   1 
ATOM   1684 N NE2   . GLN A 1 232 ? 2.866  10.005 18.769 1.00 30.83 ? 223 GLN A NE2   1 
ATOM   1685 N N     . ALA A 1 233 ? 4.239  13.921 21.141 1.00 18.71 ? 224 ALA A N     1 
ATOM   1686 C CA    . ALA A 1 233 ? 3.409  15.077 20.785 1.00 19.85 ? 224 ALA A CA    1 
ATOM   1687 C C     . ALA A 1 233 ? 3.887  15.712 19.494 1.00 23.71 ? 224 ALA A C     1 
ATOM   1688 O O     . ALA A 1 233 ? 3.084  16.011 18.597 1.00 21.73 ? 224 ALA A O     1 
ATOM   1689 C CB    . ALA A 1 233 ? 3.371  16.125 21.901 1.00 20.60 ? 224 ALA A CB    1 
ATOM   1690 N N     . VAL A 1 234 ? 5.195  15.897 19.341 1.00 18.66 ? 225 VAL A N     1 
ATOM   1691 C CA    . VAL A 1 234 ? 5.682  16.509 18.114 1.00 18.81 ? 225 VAL A CA    1 
ATOM   1692 C C     . VAL A 1 234 ? 5.543  15.563 16.926 1.00 19.92 ? 225 VAL A C     1 
ATOM   1693 O O     . VAL A 1 234 ? 5.306  16.026 15.790 1.00 20.35 ? 225 VAL A O     1 
ATOM   1694 C CB    . VAL A 1 234 ? 7.096  17.126 18.268 1.00 19.64 ? 225 VAL A CB    1 
ATOM   1695 C CG1   . VAL A 1 234 ? 7.094  18.244 19.314 1.00 22.04 ? 225 VAL A CG1   1 
ATOM   1696 C CG2   . VAL A 1 234 ? 8.151  16.086 18.579 1.00 23.94 ? 225 VAL A CG2   1 
ATOM   1697 N N     . VAL A 1 235 ? 5.760  14.256 17.139 1.00 17.98 ? 226 VAL A N     1 
ATOM   1698 C CA    . VAL A 1 235 ? 5.545  13.255 16.078 1.00 17.29 ? 226 VAL A CA    1 
ATOM   1699 C C     . VAL A 1 235 ? 4.102  13.323 15.583 1.00 20.96 ? 226 VAL A C     1 
ATOM   1700 O O     . VAL A 1 235 ? 3.842  13.352 14.378 1.00 22.68 ? 226 VAL A O     1 
ATOM   1701 C CB    . VAL A 1 235 ? 5.915  11.853 16.588 1.00 22.41 ? 226 VAL A CB    1 
ATOM   1702 C CG1   . VAL A 1 235 ? 5.304  10.762 15.664 1.00 24.37 ? 226 VAL A CG1   1 
ATOM   1703 C CG2   . VAL A 1 235 ? 7.427  11.707 16.658 1.00 22.49 ? 226 VAL A CG2   1 
ATOM   1704 N N     . SER A 1 236 ? 3.152  13.371 16.499 1.00 22.40 ? 227 SER A N     1 
ATOM   1705 C CA    . SER A 1 236 ? 1.752  13.447 16.089 1.00 26.19 ? 227 SER A CA    1 
ATOM   1706 C C     . SER A 1 236 ? 1.463  14.741 15.333 1.00 25.71 ? 227 SER A C     1 
ATOM   1707 O O     . SER A 1 236 ? 0.626  14.758 14.410 1.00 28.20 ? 227 SER A O     1 
ATOM   1708 C CB    . SER A 1 236 ? 0.844  13.357 17.308 1.00 27.80 ? 227 SER A CB    1 
ATOM   1709 O OG    . SER A 1 236 ? 0.895  12.059 17.877 1.00 36.43 ? 227 SER A OG    1 
ATOM   1710 N N     . ALA A 1 237 ? 2.143  15.826 15.682 1.00 23.26 ? 228 ALA A N     1 
ATOM   1711 C CA    . ALA A 1 237 ? 1.808  17.116 15.073 1.00 23.32 ? 228 ALA A CA    1 
ATOM   1712 C C     . ALA A 1 237 ? 2.419  17.289 13.692 1.00 24.19 ? 228 ALA A C     1 
ATOM   1713 O O     . ALA A 1 237 ? 1.774  17.872 12.805 1.00 23.77 ? 228 ALA A O     1 
ATOM   1714 C CB    . ALA A 1 237 ? 2.227  18.283 15.981 1.00 22.81 ? 228 ALA A CB    1 
ATOM   1715 N N     . ILE A 1 238 ? 3.650  16.813 13.477 1.00 21.16 ? 229 ILE A N     1 
ATOM   1716 C CA    . ILE A 1 238 ? 4.392  17.139 12.259 1.00 19.93 ? 229 ILE A CA    1 
ATOM   1717 C C     . ILE A 1 238 ? 4.923  15.920 11.517 1.00 19.11 ? 229 ILE A C     1 
ATOM   1718 O O     . ILE A 1 238 ? 5.442  16.069 10.397 1.00 20.76 ? 229 ILE A O     1 
ATOM   1719 C CB    . ILE A 1 238 ? 5.497  18.194 12.493 1.00 20.30 ? 229 ILE A CB    1 
ATOM   1720 C CG1   . ILE A 1 238 ? 6.717  17.612 13.232 1.00 20.65 ? 229 ILE A CG1   1 
ATOM   1721 C CG2   . ILE A 1 238 ? 4.950  19.455 13.192 1.00 20.32 ? 229 ILE A CG2   1 
ATOM   1722 C CD1   . ILE A 1 238 ? 7.909  18.592 13.217 1.00 21.85 ? 229 ILE A CD1   1 
ATOM   1723 N N     . GLY A 1 239 ? 4.805  14.726 12.115 1.00 20.16 ? 230 GLY A N     1 
ATOM   1724 C CA    . GLY A 1 239 ? 5.291  13.505 11.491 1.00 21.72 ? 230 GLY A CA    1 
ATOM   1725 C C     . GLY A 1 239 ? 6.672  13.104 11.981 1.00 21.77 ? 230 GLY A C     1 
ATOM   1726 O O     . GLY A 1 239 ? 7.560  13.959 12.115 1.00 20.39 ? 230 GLY A O     1 
ATOM   1727 N N     . ALA A 1 240 ? 6.878  11.814 12.223 1.00 20.63 ? 231 ALA A N     1 
ATOM   1728 C CA    . ALA A 1 240 ? 8.144  11.393 12.824 1.00 18.08 ? 231 ALA A CA    1 
ATOM   1729 C C     . ALA A 1 240 ? 9.340  11.760 11.966 1.00 17.44 ? 231 ALA A C     1 
ATOM   1730 O O     . ALA A 1 240 ? 10.424 12.049 12.521 1.00 19.08 ? 231 ALA A O     1 
ATOM   1731 C CB    . ALA A 1 240 ? 8.138  9.881  13.098 1.00 21.03 ? 231 ALA A CB    1 
ATOM   1732 N N     . ASP A 1 241 ? 9.215  11.734 10.629 1.00 19.45 ? 232 ASP A N     1 
ATOM   1733 C CA    . ASP A 1 241 ? 10.397 11.923 9.808  1.00 18.36 ? 232 ASP A CA    1 
ATOM   1734 C C     . ASP A 1 241 ? 10.892 13.379 9.836  1.00 20.71 ? 232 ASP A C     1 
ATOM   1735 O O     . ASP A 1 241 ? 11.921 13.687 9.231  1.00 21.52 ? 232 ASP A O     1 
ATOM   1736 C CB    . ASP A 1 241 ? 10.019 11.600 8.355  1.00 22.63 ? 232 ASP A CB    1 
ATOM   1737 C CG    . ASP A 1 241 ? 8.768  12.344 7.912  1.00 29.48 ? 232 ASP A CG    1 
ATOM   1738 O OD1   . ASP A 1 241 ? 7.715  12.236 8.570  1.00 55.15 ? 232 ASP A OD1   1 
ATOM   1739 O OD2   . ASP A 1 241 ? 8.840  13.047 6.901  1.00 60.11 ? 232 ASP A OD2   1 
ATOM   1740 N N     . ARG A 1 242 ? 10.159 14.270 10.501 1.00 19.15 ? 233 ARG A N     1 
ATOM   1741 C CA    . ARG A 1 242 ? 10.545 15.668 10.674 1.00 18.12 ? 233 ARG A CA    1 
ATOM   1742 C C     . ARG A 1 242 ? 10.981 15.939 12.103 1.00 18.57 ? 233 ARG A C     1 
ATOM   1743 O O     . ARG A 1 242 ? 11.113 17.108 12.477 1.00 18.18 ? 233 ARG A O     1 
ATOM   1744 C CB    . ARG A 1 242 ? 9.404  16.616 10.293 1.00 19.59 ? 233 ARG A CB    1 
ATOM   1745 C CG    . ARG A 1 242 ? 9.101  16.562 8.773  1.00 19.81 ? 233 ARG A CG    1 
ATOM   1746 C CD    . ARG A 1 242 ? 8.082  17.617 8.409  1.00 23.94 ? 233 ARG A CD    1 
ATOM   1747 N NE    . ARG A 1 242 ? 7.682  17.478 7.006  1.00 29.11 ? 233 ARG A NE    1 
ATOM   1748 C CZ    . ARG A 1 242 ? 8.282  18.024 5.944  1.00 43.73 ? 233 ARG A CZ    1 
ATOM   1749 N NH1   . ARG A 1 242 ? 9.406  18.724 6.044  1.00 25.73 ? 233 ARG A NH1   1 
ATOM   1750 N NH2   . ARG A 1 242 ? 7.718  17.894 4.740  1.00 36.08 ? 233 ARG A NH2   1 
ATOM   1751 N N     . VAL A 1 243 ? 11.261 14.889 12.880 1.00 18.66 ? 234 VAL A N     1 
ATOM   1752 C CA    . VAL A 1 243 ? 11.600 15.062 14.312 1.00 17.72 ? 234 VAL A CA    1 
ATOM   1753 C C     . VAL A 1 243 ? 12.927 14.394 14.563 1.00 15.94 ? 234 VAL A C     1 
ATOM   1754 O O     . VAL A 1 243 ? 13.050 13.181 14.361 1.00 17.53 ? 234 VAL A O     1 
ATOM   1755 C CB    . VAL A 1 243 ? 10.523 14.463 15.217 1.00 17.09 ? 234 VAL A CB    1 
ATOM   1756 C CG1   . VAL A 1 243 ? 10.961 14.544 16.701 1.00 18.16 ? 234 VAL A CG1   1 
ATOM   1757 C CG2   . VAL A 1 243 ? 9.223  15.232 14.974 1.00 19.27 ? 234 VAL A CG2   1 
ATOM   1758 N N     . GLY A 1 244 ? 13.917 15.159 15.063 1.00 16.68 ? 235 GLY A N     1 
ATOM   1759 C CA    . GLY A 1 244 ? 15.145 14.581 15.616 1.00 18.12 ? 235 GLY A CA    1 
ATOM   1760 C C     . GLY A 1 244 ? 15.133 14.735 17.131 1.00 15.61 ? 235 GLY A C     1 
ATOM   1761 O O     . GLY A 1 244 ? 14.408 15.602 17.667 1.00 16.92 ? 235 GLY A O     1 
ATOM   1762 N N     . VAL A 1 245 ? 15.906 13.889 17.837 1.00 15.59 ? 236 VAL A N     1 
ATOM   1763 C CA    . VAL A 1 245 ? 15.967 13.931 19.297 1.00 15.98 ? 236 VAL A CA    1 
ATOM   1764 C C     . VAL A 1 245 ? 17.425 13.974 19.723 1.00 16.14 ? 236 VAL A C     1 
ATOM   1765 O O     . VAL A 1 245 ? 18.219 13.138 19.284 1.00 17.15 ? 236 VAL A O     1 
ATOM   1766 C CB    . VAL A 1 245 ? 15.274 12.690 19.904 1.00 17.51 ? 236 VAL A CB    1 
ATOM   1767 C CG1   . VAL A 1 245 ? 15.279 12.751 21.441 1.00 19.71 ? 236 VAL A CG1   1 
ATOM   1768 C CG2   . VAL A 1 245 ? 13.801 12.585 19.380 1.00 18.45 ? 236 VAL A CG2   1 
ATOM   1769 N N     . ARG A 1 246 ? 17.774 14.924 20.601 1.00 15.44 ? 237 ARG A N     1 
ATOM   1770 C CA    . ARG A 1 246 ? 19.157 15.051 21.082 1.00 17.86 ? 237 ARG A CA    1 
ATOM   1771 C C     . ARG A 1 246 ? 19.218 14.762 22.569 1.00 16.71 ? 237 ARG A C     1 
ATOM   1772 O O     . ARG A 1 246 ? 18.448 15.343 23.333 1.00 17.18 ? 237 ARG A O     1 
ATOM   1773 C CB    . ARG A 1 246 ? 19.700 16.462 20.812 1.00 17.03 ? 237 ARG A CB    1 
ATOM   1774 C CG    . ARG A 1 246 ? 21.220 16.508 21.018 1.00 18.78 ? 237 ARG A CG    1 
ATOM   1775 C CD    . ARG A 1 246 ? 21.791 17.860 20.604 1.00 17.70 ? 237 ARG A CD    1 
ATOM   1776 N NE    . ARG A 1 246 ? 23.111 17.702 19.994 1.00 19.23 ? 237 ARG A NE    1 
ATOM   1777 C CZ    . ARG A 1 246 ? 24.109 18.569 20.089 1.00 17.76 ? 237 ARG A CZ    1 
ATOM   1778 N NH1   . ARG A 1 246 ? 24.053 19.620 20.887 1.00 18.19 ? 237 ARG A NH1   1 
ATOM   1779 N NH2   . ARG A 1 246 ? 25.204 18.379 19.350 1.00 19.44 ? 237 ARG A NH2   1 
ATOM   1780 N N     . VAL A 1 247 ? 20.153 13.893 22.977 1.00 16.25 ? 238 VAL A N     1 
ATOM   1781 C CA    . VAL A 1 247 ? 20.330 13.586 24.404 1.00 16.42 ? 238 VAL A CA    1 
ATOM   1782 C C     . VAL A 1 247 ? 21.816 13.465 24.676 1.00 15.64 ? 238 VAL A C     1 
ATOM   1783 O O     . VAL A 1 247 ? 22.638 13.452 23.780 1.00 17.01 ? 238 VAL A O     1 
ATOM   1784 C CB    . VAL A 1 247 ? 19.626 12.274 24.821 1.00 16.53 ? 238 VAL A CB    1 
ATOM   1785 C CG1   . VAL A 1 247 ? 18.101 12.456 24.770 1.00 19.01 ? 238 VAL A CG1   1 
ATOM   1786 C CG2   . VAL A 1 247 ? 20.073 11.088 23.968 1.00 18.95 ? 238 VAL A CG2   1 
ATOM   1787 N N     . SER A 1 248 ? 22.148 13.429 25.971 1.00 16.76 ? 239 SER A N     1 
ATOM   1788 C CA    . SER A 1 248 ? 23.544 13.354 26.413 1.00 18.04 ? 239 SER A CA    1 
ATOM   1789 C C     . SER A 1 248 ? 23.603 12.627 27.750 1.00 16.65 ? 239 SER A C     1 
ATOM   1790 O O     . SER A 1 248 ? 23.888 13.226 28.791 1.00 18.79 ? 239 SER A O     1 
ATOM   1791 C CB    . SER A 1 248 ? 24.143 14.761 26.538 1.00 17.36 ? 239 SER A CB    1 
ATOM   1792 O OG    . SER A 1 248 ? 23.458 15.562 27.491 1.00 17.72 ? 239 SER A OG    1 
ATOM   1793 N N     . PRO A 1 249 ? 23.377 11.313 27.752 1.00 17.53 ? 240 PRO A N     1 
ATOM   1794 C CA    . PRO A 1 249 ? 23.316 10.584 29.026 1.00 18.53 ? 240 PRO A CA    1 
ATOM   1795 C C     . PRO A 1 249 ? 24.597 10.607 29.799 1.00 21.01 ? 240 PRO A C     1 
ATOM   1796 O O     . PRO A 1 249 ? 24.557 10.468 31.026 1.00 21.14 ? 240 PRO A O     1 
ATOM   1797 C CB    . PRO A 1 249 ? 22.935 9.150  28.607 1.00 20.86 ? 240 PRO A CB    1 
ATOM   1798 C CG    . PRO A 1 249 ? 23.208 9.065  27.150 1.00 18.83 ? 240 PRO A CG    1 
ATOM   1799 C CD    . PRO A 1 249 ? 23.049 10.482 26.606 1.00 17.11 ? 240 PRO A CD    1 
ATOM   1800 N N     . ALA A 1 250 ? 25.737 10.774 29.152 1.00 19.50 ? 241 ALA A N     1 
ATOM   1801 C CA    . ALA A 1 250 ? 27.027 10.711 29.812 1.00 22.43 ? 241 ALA A CA    1 
ATOM   1802 C C     . ALA A 1 250 ? 27.638 12.085 30.019 1.00 23.38 ? 241 ALA A C     1 
ATOM   1803 O O     . ALA A 1 250 ? 28.807 12.176 30.411 1.00 28.48 ? 241 ALA A O     1 
ATOM   1804 C CB    . ALA A 1 250 ? 27.985 9.851  28.974 1.00 26.41 ? 241 ALA A CB    1 
ATOM   1805 N N     . ILE A 1 251 ? 26.907 13.182 29.759 1.00 20.07 ? 242 ILE A N     1 
ATOM   1806 C CA    . ILE A 1 251 ? 27.396 14.529 30.099 1.00 22.38 ? 242 ILE A CA    1 
ATOM   1807 C C     . ILE A 1 251 ? 26.736 14.980 31.398 1.00 22.20 ? 242 ILE A C     1 
ATOM   1808 O O     . ILE A 1 251 ? 25.507 14.867 31.541 1.00 25.16 ? 242 ILE A O     1 
ATOM   1809 C CB    . ILE A 1 251 ? 27.113 15.518 28.958 1.00 21.44 ? 242 ILE A CB    1 
ATOM   1810 C CG1   . ILE A 1 251 ? 27.975 15.102 27.763 1.00 23.07 ? 242 ILE A CG1   1 
ATOM   1811 C CG2   . ILE A 1 251 ? 27.412 16.953 29.409 1.00 22.46 ? 242 ILE A CG2   1 
ATOM   1812 C CD1   . ILE A 1 251 ? 28.022 16.073 26.583 1.00 28.32 ? 242 ILE A CD1   1 
ATOM   1813 N N     . ASP A 1 252 ? 27.532 15.532 32.347 1.00 22.83 ? 243 ASP A N     1 
ATOM   1814 C CA    . ASP A 1 252 ? 27.037 15.929 33.681 1.00 22.96 ? 243 ASP A CA    1 
ATOM   1815 C C     . ASP A 1 252 ? 26.867 17.435 33.895 1.00 31.26 ? 243 ASP A C     1 
ATOM   1816 O O     . ASP A 1 252 ? 26.828 17.892 35.058 1.00 35.72 ? 243 ASP A O     1 
ATOM   1817 C CB    . ASP A 1 252 ? 27.935 15.369 34.793 1.00 28.69 ? 243 ASP A CB    1 
ATOM   1818 N N     . HIS A 1 253 ? 26.628 18.178 32.814 1.00 24.06 ? 244 HIS A N     1 
ATOM   1819 C CA    . HIS A 1 253 ? 26.568 19.641 32.812 1.00 26.48 ? 244 HIS A CA    1 
ATOM   1820 C C     . HIS A 1 253 ? 25.447 20.104 33.735 1.00 24.24 ? 244 HIS A C     1 
ATOM   1821 O O     . HIS A 1 253 ? 24.360 19.526 33.732 1.00 22.38 ? 244 HIS A O     1 
ATOM   1822 C CB    . HIS A 1 253 ? 26.269 20.026 31.346 1.00 23.47 ? 244 HIS A CB    1 
ATOM   1823 C CG    . HIS A 1 253 ? 26.267 21.496 31.081 1.00 25.27 ? 244 HIS A CG    1 
ATOM   1824 N ND1   . HIS A 1 253 ? 25.157 22.204 30.648 1.00 26.80 ? 244 HIS A ND1   1 
ATOM   1825 C CD2   . HIS A 1 253 ? 27.260 22.395 31.230 1.00 29.52 ? 244 HIS A CD2   1 
ATOM   1826 C CE1   . HIS A 1 253 ? 25.488 23.477 30.510 1.00 28.97 ? 244 HIS A CE1   1 
ATOM   1827 N NE2   . HIS A 1 253 ? 26.750 23.621 30.874 1.00 29.16 ? 244 HIS A NE2   1 
ATOM   1828 N N     . LEU A 1 254 ? 25.698 21.148 34.564 1.00 21.83 ? 245 LEU A N     1 
ATOM   1829 C CA    . LEU A 1 254 ? 24.649 21.697 35.418 1.00 20.11 ? 245 LEU A CA    1 
ATOM   1830 C C     . LEU A 1 254 ? 24.103 20.656 36.411 1.00 20.26 ? 245 LEU A C     1 
ATOM   1831 O O     . LEU A 1 254 ? 22.913 20.610 36.703 1.00 20.44 ? 245 LEU A O     1 
ATOM   1832 C CB    . LEU A 1 254 ? 23.511 22.346 34.610 1.00 20.60 ? 245 LEU A CB    1 
ATOM   1833 C CG    . LEU A 1 254 ? 23.995 23.346 33.581 1.00 19.15 ? 245 LEU A CG    1 
ATOM   1834 C CD1   . LEU A 1 254 ? 22.744 23.870 32.801 1.00 22.10 ? 245 LEU A CD1   1 
ATOM   1835 C CD2   . LEU A 1 254 ? 24.673 24.540 34.312 1.00 23.35 ? 245 LEU A CD2   1 
ATOM   1836 N N     . ASP A 1 255 ? 24.995 19.834 36.963 1.00 20.01 ? 246 ASP A N     1 
ATOM   1837 C CA    . ASP A 1 255 ? 24.663 18.870 38.024 1.00 21.03 ? 246 ASP A CA    1 
ATOM   1838 C C     . ASP A 1 255 ? 23.698 17.810 37.496 1.00 24.25 ? 246 ASP A C     1 
ATOM   1839 O O     . ASP A 1 255 ? 22.799 17.391 38.222 1.00 31.73 ? 246 ASP A O     1 
ATOM   1840 C CB    . ASP A 1 255 ? 24.112 19.522 39.315 1.00 25.01 ? 246 ASP A CB    1 
ATOM   1841 C CG    . ASP A 1 255 ? 25.159 20.349 40.068 1.00 22.39 ? 246 ASP A CG    1 
ATOM   1842 O OD1   . ASP A 1 255 ? 24.772 21.183 40.908 1.00 26.90 ? 246 ASP A OD1   1 
ATOM   1843 O OD2   . ASP A 1 255 ? 26.376 20.180 39.790 1.00 26.77 ? 246 ASP A OD2   1 
ATOM   1844 N N     . ALA A 1 256 ? 23.895 17.359 36.253 1.00 21.23 ? 247 ALA A N     1 
ATOM   1845 C CA    . ALA A 1 256 ? 23.003 16.405 35.610 1.00 21.35 ? 247 ALA A CA    1 
ATOM   1846 C C     . ALA A 1 256 ? 23.688 15.058 35.450 1.00 24.93 ? 247 ALA A C     1 
ATOM   1847 O O     . ALA A 1 256 ? 23.917 14.570 34.348 1.00 26.37 ? 247 ALA A O     1 
ATOM   1848 C CB    . ALA A 1 256 ? 22.624 16.943 34.228 1.00 23.87 ? 247 ALA A CB    1 
ATOM   1849 N N     . MET A 1 257 ? 23.917 14.401 36.550 1.00 22.83 ? 248 MET A N     1 
ATOM   1850 C CA    . MET A 1 257 ? 24.544 13.085 36.506 1.00 21.73 ? 248 MET A CA    1 
ATOM   1851 C C     . MET A 1 257 ? 23.466 12.012 36.622 1.00 20.13 ? 248 MET A C     1 
ATOM   1852 O O     . MET A 1 257 ? 22.452 12.216 37.285 1.00 22.98 ? 248 MET A O     1 
ATOM   1853 C CB    . MET A 1 257 ? 25.522 12.948 37.671 1.00 30.04 ? 248 MET A CB    1 
ATOM   1854 N N     . ASP A 1 258 ? 23.692 10.852 35.970 1.00 22.70 ? 249 ASP A N     1 
ATOM   1855 C CA    . ASP A 1 258 ? 22.915 9.655  36.244 1.00 22.50 ? 249 ASP A CA    1 
ATOM   1856 C C     . ASP A 1 258 ? 23.818 8.586  36.867 1.00 24.78 ? 249 ASP A C     1 
ATOM   1857 O O     . ASP A 1 258 ? 24.990 8.457  36.482 1.00 26.22 ? 249 ASP A O     1 
ATOM   1858 C CB    . ASP A 1 258 ? 22.295 9.061  34.979 1.00 24.74 ? 249 ASP A CB    1 
ATOM   1859 C CG    . ASP A 1 258 ? 21.108 8.156  35.293 1.00 30.12 ? 249 ASP A CG    1 
ATOM   1860 O OD1   . ASP A 1 258 ? 20.016 8.655  35.667 1.00 25.07 ? 249 ASP A OD1   1 
ATOM   1861 O OD2   . ASP A 1 258 ? 21.296 6.898  35.327 1.00 27.69 ? 249 ASP A OD2   1 
ATOM   1862 N N     . SER A 1 259 ? 23.236 7.789  37.767 1.00 22.31 ? 250 SER A N     1 
ATOM   1863 C CA    . SER A 1 259 ? 23.978 6.679  38.364 1.00 23.63 ? 250 SER A CA    1 
ATOM   1864 C C     . SER A 1 259 ? 24.343 5.602  37.345 1.00 28.00 ? 250 SER A C     1 
ATOM   1865 O O     . SER A 1 259 ? 25.242 4.807  37.610 1.00 27.40 ? 250 SER A O     1 
ATOM   1866 C CB    . SER A 1 259 ? 23.164 6.062  39.485 1.00 26.88 ? 250 SER A CB    1 
ATOM   1867 O OG    . SER A 1 259 ? 22.008 5.447  38.956 1.00 28.58 ? 250 SER A OG    1 
ATOM   1868 N N     . ASN A 1 260 ? 23.660 5.508  36.204 1.00 24.59 ? 251 ASN A N     1 
ATOM   1869 C CA    . ASN A 1 260 ? 23.954 4.470  35.209 1.00 21.53 ? 251 ASN A CA    1 
ATOM   1870 C C     . ASN A 1 260 ? 23.694 5.061  33.834 1.00 22.56 ? 251 ASN A C     1 
ATOM   1871 O O     . ASN A 1 260 ? 22.644 4.810  33.231 1.00 23.51 ? 251 ASN A O     1 
ATOM   1872 C CB    . ASN A 1 260 ? 23.105 3.219  35.422 1.00 24.77 ? 251 ASN A CB    1 
ATOM   1873 C CG    . ASN A 1 260 ? 23.582 2.068  34.608 1.00 26.54 ? 251 ASN A CG    1 
ATOM   1874 O OD1   . ASN A 1 260 ? 24.262 2.225  33.606 1.00 26.62 ? 251 ASN A OD1   1 
ATOM   1875 N ND2   . ASN A 1 260 ? 23.257 0.851  35.080 1.00 31.45 ? 251 ASN A ND2   1 
ATOM   1876 N N     . PRO A 1 261 ? 24.631 5.860  33.309 1.00 21.21 ? 252 PRO A N     1 
ATOM   1877 C CA    . PRO A 1 261 ? 24.369 6.569  32.046 1.00 21.24 ? 252 PRO A CA    1 
ATOM   1878 C C     . PRO A 1 261 ? 24.027 5.658  30.898 1.00 19.62 ? 252 PRO A C     1 
ATOM   1879 O O     . PRO A 1 261 ? 23.150 5.988  30.079 1.00 18.34 ? 252 PRO A O     1 
ATOM   1880 C CB    . PRO A 1 261 ? 25.682 7.326  31.771 1.00 24.28 ? 252 PRO A CB    1 
ATOM   1881 C CG    . PRO A 1 261 ? 26.231 7.598  33.163 1.00 23.21 ? 252 PRO A CG    1 
ATOM   1882 C CD    . PRO A 1 261 ? 25.898 6.301  33.923 1.00 23.11 ? 252 PRO A CD    1 
ATOM   1883 N N     . LEU A 1 262 ? 24.721 4.531  30.748 1.00 21.73 ? 253 LEU A N     1 
ATOM   1884 C CA    . LEU A 1 262 ? 24.398 3.641  29.629 1.00 19.17 ? 253 LEU A CA    1 
ATOM   1885 C C     . LEU A 1 262 ? 22.974 3.112  29.739 1.00 18.93 ? 253 LEU A C     1 
ATOM   1886 O O     . LEU A 1 262 ? 22.235 3.125  28.763 1.00 18.61 ? 253 LEU A O     1 
ATOM   1887 C CB    . LEU A 1 262 ? 25.418 2.503  29.496 1.00 20.45 ? 253 LEU A CB    1 
ATOM   1888 C CG    . LEU A 1 262 ? 25.044 1.564  28.333 1.00 23.00 ? 253 LEU A CG    1 
ATOM   1889 C CD1   . LEU A 1 262 ? 24.950 2.188  26.917 1.00 23.48 ? 253 LEU A CD1   1 
ATOM   1890 C CD2   . LEU A 1 262 ? 26.066 0.410  28.336 1.00 25.24 ? 253 LEU A CD2   1 
ATOM   1891 N N     A SER A 1 263 ? 22.580 2.663  30.929 0.50 20.12 ? 254 SER A N     1 
ATOM   1892 N N     B SER A 1 263 ? 22.552 2.671  30.934 0.50 20.11 ? 254 SER A N     1 
ATOM   1893 C CA    A SER A 1 263 ? 21.225 2.165  31.105 0.50 18.64 ? 254 SER A CA    1 
ATOM   1894 C CA    B SER A 1 263 ? 21.186 2.161  31.078 0.50 18.64 ? 254 SER A CA    1 
ATOM   1895 C C     A SER A 1 263 ? 20.196 3.254  30.803 0.50 19.41 ? 254 SER A C     1 
ATOM   1896 C C     B SER A 1 263 ? 20.157 3.259  30.830 0.50 19.37 ? 254 SER A C     1 
ATOM   1897 O O     A SER A 1 263 ? 19.183 2.985  30.150 0.50 18.85 ? 254 SER A O     1 
ATOM   1898 O O     B SER A 1 263 ? 19.083 2.994  30.283 0.50 18.71 ? 254 SER A O     1 
ATOM   1899 C CB    A SER A 1 263 ? 21.065 1.613  32.519 0.50 19.55 ? 254 SER A CB    1 
ATOM   1900 C CB    B SER A 1 263 ? 20.964 1.544  32.463 0.50 19.33 ? 254 SER A CB    1 
ATOM   1901 O OG    A SER A 1 263 ? 19.792 1.079  32.669 0.50 18.81 ? 254 SER A OG    1 
ATOM   1902 O OG    B SER A 1 263 ? 21.537 0.264  32.528 0.50 22.32 ? 254 SER A OG    1 
ATOM   1903 N N     . LEU A 1 264 ? 20.455 4.490  31.236 1.00 19.52 ? 255 LEU A N     1 
ATOM   1904 C CA    . LEU A 1 264 ? 19.521 5.564  30.959 1.00 18.20 ? 255 LEU A CA    1 
ATOM   1905 C C     . LEU A 1 264 ? 19.442 5.799  29.457 1.00 18.12 ? 255 LEU A C     1 
ATOM   1906 O O     . LEU A 1 264 ? 18.355 5.925  28.888 1.00 18.43 ? 255 LEU A O     1 
ATOM   1907 C CB    . LEU A 1 264 ? 19.978 6.833  31.664 1.00 19.60 ? 255 LEU A CB    1 
ATOM   1908 C CG    . LEU A 1 264 ? 19.201 8.083  31.235 1.00 16.63 ? 255 LEU A CG    1 
ATOM   1909 C CD1   . LEU A 1 264 ? 17.724 7.908  31.651 1.00 21.26 ? 255 LEU A CD1   1 
ATOM   1910 C CD2   . LEU A 1 264 ? 19.847 9.295  31.928 1.00 19.95 ? 255 LEU A CD2   1 
ATOM   1911 N N     . GLY A 1 265 ? 20.589 5.871  28.790 1.00 18.12 ? 256 GLY A N     1 
ATOM   1912 C CA    . GLY A 1 265 ? 20.584 6.032  27.345 1.00 17.63 ? 256 GLY A CA    1 
ATOM   1913 C C     . GLY A 1 265 ? 19.798 4.935  26.647 1.00 17.51 ? 256 GLY A C     1 
ATOM   1914 O O     . GLY A 1 265 ? 19.031 5.194  25.695 1.00 17.18 ? 256 GLY A O     1 
ATOM   1915 N N     . LEU A 1 266 ? 20.023 3.683  27.074 1.00 16.95 ? 257 LEU A N     1 
ATOM   1916 C CA    . LEU A 1 266 ? 19.323 2.568  26.426 1.00 17.07 ? 257 LEU A CA    1 
ATOM   1917 C C     . LEU A 1 266 ? 17.833 2.639  26.704 1.00 18.11 ? 257 LEU A C     1 
ATOM   1918 O O     . LEU A 1 266 ? 17.045 2.254  25.833 1.00 18.99 ? 257 LEU A O     1 
ATOM   1919 C CB    . LEU A 1 266 ? 19.901 1.220  26.859 1.00 17.87 ? 257 LEU A CB    1 
ATOM   1920 C CG    . LEU A 1 266 ? 21.305 0.943  26.321 1.00 19.46 ? 257 LEU A CG    1 
ATOM   1921 C CD1   . LEU A 1 266 ? 21.759 -0.396 26.960 1.00 19.97 ? 257 LEU A CD1   1 
ATOM   1922 C CD2   . LEU A 1 266 ? 21.319 0.831  24.835 1.00 21.28 ? 257 LEU A CD2   1 
ATOM   1923 N N     . ALA A 1 267 ? 17.420 3.126  27.872 1.00 17.54 ? 258 ALA A N     1 
ATOM   1924 C CA    . ALA A 1 267 ? 15.990 3.248  28.122 1.00 17.50 ? 258 ALA A CA    1 
ATOM   1925 C C     . ALA A 1 267 ? 15.362 4.319  27.220 1.00 17.58 ? 258 ALA A C     1 
ATOM   1926 O O     . ALA A 1 267 ? 14.243 4.126  26.713 1.00 19.99 ? 258 ALA A O     1 
ATOM   1927 C CB    . ALA A 1 267 ? 15.730 3.565  29.600 1.00 19.14 ? 258 ALA A CB    1 
ATOM   1928 N N     . VAL A 1 268 ? 16.066 5.441  27.004 1.00 17.35 ? 259 VAL A N     1 
ATOM   1929 C CA    . VAL A 1 268 ? 15.566 6.434  26.060 1.00 18.13 ? 259 VAL A CA    1 
ATOM   1930 C C     . VAL A 1 268 ? 15.451 5.833  24.672 1.00 18.42 ? 259 VAL A C     1 
ATOM   1931 O O     . VAL A 1 268 ? 14.448 6.017  23.971 1.00 18.68 ? 259 VAL A O     1 
ATOM   1932 C CB    . VAL A 1 268 ? 16.496 7.642  26.054 1.00 18.87 ? 259 VAL A CB    1 
ATOM   1933 C CG1   . VAL A 1 268 ? 16.014 8.610  24.960 1.00 17.95 ? 259 VAL A CG1   1 
ATOM   1934 C CG2   . VAL A 1 268 ? 16.398 8.351  27.434 1.00 20.32 ? 259 VAL A CG2   1 
ATOM   1935 N N     . VAL A 1 269 ? 16.494 5.136  24.235 1.00 17.15 ? 260 VAL A N     1 
ATOM   1936 C CA    . VAL A 1 269 ? 16.490 4.557  22.890 1.00 16.93 ? 260 VAL A CA    1 
ATOM   1937 C C     . VAL A 1 269 ? 15.324 3.587  22.731 1.00 18.35 ? 260 VAL A C     1 
ATOM   1938 O O     . VAL A 1 269 ? 14.652 3.586  21.690 1.00 19.45 ? 260 VAL A O     1 
ATOM   1939 C CB    . VAL A 1 269 ? 17.844 3.862  22.624 1.00 19.00 ? 260 VAL A CB    1 
ATOM   1940 C CG1   . VAL A 1 269 ? 17.755 2.957  21.392 1.00 21.34 ? 260 VAL A CG1   1 
ATOM   1941 C CG2   . VAL A 1 269 ? 18.964 4.865  22.481 1.00 20.18 ? 260 VAL A CG2   1 
ATOM   1942 N N     . GLU A 1 270 ? 15.060 2.748  23.749 1.00 19.18 ? 261 GLU A N     1 
ATOM   1943 C CA    . GLU A 1 270 ? 13.918 1.847  23.641 1.00 20.79 ? 261 GLU A CA    1 
ATOM   1944 C C     . GLU A 1 270 ? 12.605 2.613  23.476 1.00 21.13 ? 261 GLU A C     1 
ATOM   1945 O O     . GLU A 1 270 ? 11.755 2.184  22.679 1.00 21.80 ? 261 GLU A O     1 
ATOM   1946 C CB    . GLU A 1 270 ? 13.870 0.947  24.873 1.00 25.04 ? 261 GLU A CB    1 
ATOM   1947 C CG    . GLU A 1 270 ? 12.719 -0.112 24.825 1.00 29.44 ? 261 GLU A CG    1 
ATOM   1948 C CD    . GLU A 1 270 ? 11.352 0.333  25.318 1.00 57.40 ? 261 GLU A CD    1 
ATOM   1949 O OE1   . GLU A 1 270 ? 11.259 1.335  26.051 1.00 61.86 ? 261 GLU A OE1   1 
ATOM   1950 O OE2   . GLU A 1 270 ? 10.350 -0.361 24.999 1.00 63.46 ? 261 GLU A OE2   1 
ATOM   1951 N N     . ARG A 1 271 ? 12.446 3.709  24.213 1.00 20.17 ? 262 ARG A N     1 
ATOM   1952 C CA    . ARG A 1 271 ? 11.243 4.570  24.000 1.00 22.17 ? 262 ARG A CA    1 
ATOM   1953 C C     . ARG A 1 271 ? 11.065 5.157  22.559 1.00 19.62 ? 262 ARG A C     1 
ATOM   1954 O O     . ARG A 1 271 ? 9.983  5.235  21.851 1.00 22.18 ? 262 ARG A O     1 
ATOM   1955 C CB    . ARG A 1 271 ? 11.217 5.741  24.990 1.00 20.75 ? 262 ARG A CB    1 
ATOM   1956 C CG    . ARG A 1 271 ? 11.301 5.360  26.460 1.00 29.29 ? 262 ARG A CG    1 
ATOM   1957 C CD    . ARG A 1 271 ? 10.244 4.375  26.909 1.00 31.66 ? 262 ARG A CD    1 
ATOM   1958 N NE    . ARG A 1 271 ? 8.906  4.814  26.556 1.00 41.57 ? 262 ARG A NE    1 
ATOM   1959 C CZ    . ARG A 1 271 ? 7.894  3.993  26.303 1.00 55.19 ? 262 ARG A CZ    1 
ATOM   1960 N NH1   . ARG A 1 271 ? 8.130  2.740  25.954 1.00 40.77 ? 262 ARG A NH1   1 
ATOM   1961 N NH2   . ARG A 1 271 ? 6.651  4.427  26.405 1.00 39.02 ? 262 ARG A NH2   1 
ATOM   1962 N N     . LEU A 1 272 ? 12.230 5.549  22.021 1.00 17.73 ? 263 LEU A N     1 
ATOM   1963 C CA    . LEU A 1 272 ? 12.197 6.058  20.653 1.00 17.90 ? 263 LEU A CA    1 
ATOM   1964 C C     . LEU A 1 272 ? 11.857 4.944  19.668 1.00 18.16 ? 263 LEU A C     1 
ATOM   1965 O O     . LEU A 1 272 ? 11.068 5.162  18.722 1.00 18.04 ? 263 LEU A O     1 
ATOM   1966 C CB    . LEU A 1 272 ? 13.546 6.726  20.296 1.00 18.37 ? 263 LEU A CB    1 
ATOM   1967 C CG    . LEU A 1 272 ? 14.008 7.875  21.219 1.00 18.82 ? 263 LEU A CG    1 
ATOM   1968 C CD1   . LEU A 1 272 ? 15.340 8.429  20.721 1.00 20.81 ? 263 LEU A CD1   1 
ATOM   1969 C CD2   . LEU A 1 272 ? 12.924 8.961  21.255 1.00 20.25 ? 263 LEU A CD2   1 
ATOM   1970 N N     . ASN A 1 273 ? 12.458 3.759  19.840 1.00 18.54 ? 264 ASN A N     1 
ATOM   1971 C CA    . ASN A 1 273 ? 12.099 2.635  18.976 1.00 19.44 ? 264 ASN A CA    1 
ATOM   1972 C C     . ASN A 1 273 ? 10.616 2.329  19.090 1.00 20.94 ? 264 ASN A C     1 
ATOM   1973 O O     . ASN A 1 273 ? 9.970  2.061  18.077 1.00 21.26 ? 264 ASN A O     1 
ATOM   1974 C CB    . ASN A 1 273 ? 12.912 1.399  19.353 1.00 18.46 ? 264 ASN A CB    1 
ATOM   1975 C CG    . ASN A 1 273 ? 14.359 1.470  18.925 1.00 18.08 ? 264 ASN A CG    1 
ATOM   1976 O OD1   . ASN A 1 273 ? 14.781 2.331  18.160 1.00 20.03 ? 264 ASN A OD1   1 
ATOM   1977 N ND2   . ASN A 1 273 ? 15.166 0.593  19.492 1.00 18.97 ? 264 ASN A ND2   1 
ATOM   1978 N N     . LYS A 1 274 ? 10.068 2.386  20.300 1.00 19.23 ? 265 LYS A N     1 
ATOM   1979 C CA    . LYS A 1 274 ? 8.644  2.118  20.510 1.00 20.70 ? 265 LYS A CA    1 
ATOM   1980 C C     . LYS A 1 274 ? 7.771  3.181  19.848 1.00 20.86 ? 265 LYS A C     1 
ATOM   1981 O O     . LYS A 1 274 ? 6.758  2.847  19.231 1.00 23.83 ? 265 LYS A O     1 
ATOM   1982 C CB    . LYS A 1 274 ? 8.331  1.997  22.009 1.00 25.06 ? 265 LYS A CB    1 
ATOM   1983 N N     . ILE A 1 275 ? 8.134  4.469  19.939 1.00 20.08 ? 266 ILE A N     1 
ATOM   1984 C CA    . ILE A 1 275 ? 7.362  5.504  19.265 1.00 20.91 ? 266 ILE A CA    1 
ATOM   1985 C C     . ILE A 1 275 ? 7.343  5.248  17.773 1.00 24.09 ? 266 ILE A C     1 
ATOM   1986 O O     . ILE A 1 275 ? 6.318  5.461  17.109 1.00 26.25 ? 266 ILE A O     1 
ATOM   1987 C CB    . ILE A 1 275 ? 7.967  6.890  19.593 1.00 20.63 ? 266 ILE A CB    1 
ATOM   1988 C CG1   . ILE A 1 275 ? 7.659  7.259  21.047 1.00 21.70 ? 266 ILE A CG1   1 
ATOM   1989 C CG2   . ILE A 1 275 ? 7.416  7.942  18.635 1.00 24.47 ? 266 ILE A CG2   1 
ATOM   1990 C CD1   . ILE A 1 275 ? 8.445  8.494  21.513 1.00 22.04 ? 266 ILE A CD1   1 
ATOM   1991 N N     . GLN A 1 276 ? 8.486  4.850  17.220 1.00 20.25 ? 267 GLN A N     1 
ATOM   1992 C CA    . GLN A 1 276 ? 8.566  4.564  15.776 1.00 20.85 ? 267 GLN A CA    1 
ATOM   1993 C C     . GLN A 1 276 ? 7.653  3.412  15.395 1.00 25.01 ? 267 GLN A C     1 
ATOM   1994 O O     . GLN A 1 276 ? 6.925  3.496  14.400 1.00 25.20 ? 267 GLN A O     1 
ATOM   1995 C CB    . GLN A 1 276 ? 10.001 4.255  15.345 1.00 20.40 ? 267 GLN A CB    1 
ATOM   1996 C CG    . GLN A 1 276 ? 10.876 5.484  15.517 1.00 21.34 ? 267 GLN A CG    1 
ATOM   1997 C CD    . GLN A 1 276 ? 12.287 5.305  15.093 1.00 21.49 ? 267 GLN A CD    1 
ATOM   1998 O OE1   . GLN A 1 276 ? 12.963 6.280  14.840 1.00 20.94 ? 267 GLN A OE1   1 
ATOM   1999 N NE2   . GLN A 1 276 ? 12.788 4.085  15.041 1.00 20.40 ? 267 GLN A NE2   1 
ATOM   2000 N N     . LEU A 1 277 ? 7.691  2.323  16.159 1.00 22.38 ? 268 LEU A N     1 
ATOM   2001 C CA    . LEU A 1 277 ? 6.843  1.172  15.823 1.00 26.41 ? 268 LEU A CA    1 
ATOM   2002 C C     . LEU A 1 277 ? 5.373  1.529  15.949 1.00 31.45 ? 268 LEU A C     1 
ATOM   2003 O O     . LEU A 1 277 ? 4.555  1.117  15.120 1.00 36.63 ? 268 LEU A O     1 
ATOM   2004 C CB    . LEU A 1 277 ? 7.186  0.012  16.736 1.00 26.64 ? 268 LEU A CB    1 
ATOM   2005 C CG    . LEU A 1 277 ? 8.570  -0.543 16.440 1.00 31.28 ? 268 LEU A CG    1 
ATOM   2006 C CD1   . LEU A 1 277 ? 9.030  -1.492 17.547 1.00 37.29 ? 268 LEU A CD1   1 
ATOM   2007 C CD2   . LEU A 1 277 ? 8.624  -1.203 15.050 1.00 37.36 ? 268 LEU A CD2   1 
ATOM   2008 N N     . HIS A 1 278 ? 5.013  2.310  16.958 1.00 29.32 ? 269 HIS A N     1 
ATOM   2009 C CA    . HIS A 1 278 ? 3.611  2.693  17.123 1.00 34.41 ? 269 HIS A CA    1 
ATOM   2010 C C     . HIS A 1 278 ? 3.139  3.632  16.013 1.00 40.90 ? 269 HIS A C     1 
ATOM   2011 O O     . HIS A 1 278 ? 1.989  3.547  15.575 1.00 50.21 ? 269 HIS A O     1 
ATOM   2012 C CB    . HIS A 1 278 ? 3.406  3.331  18.498 1.00 34.61 ? 269 HIS A CB    1 
ATOM   2013 C CG    . HIS A 1 278 ? 2.008  3.795  18.747 1.00 57.31 ? 269 HIS A CG    1 
ATOM   2014 N ND1   . HIS A 1 278 ? 1.569  5.055  18.393 1.00 56.97 ? 269 HIS A ND1   1 
ATOM   2015 C CD2   . HIS A 1 278 ? 0.946  3.167  19.305 1.00 60.04 ? 269 HIS A CD2   1 
ATOM   2016 C CE1   . HIS A 1 278 ? 0.299  5.187  18.735 1.00 61.68 ? 269 HIS A CE1   1 
ATOM   2017 N NE2   . HIS A 1 278 ? -0.103 4.055  19.289 1.00 71.84 ? 269 HIS A NE2   1 
ATOM   2018 N N     A SER A 1 279 ? 4.007  4.544  15.556 0.50 32.47 ? 270 SER A N     1 
ATOM   2019 N N     B SER A 1 279 ? 4.000  4.525  15.545 0.50 32.45 ? 270 SER A N     1 
ATOM   2020 C CA    A SER A 1 279 ? 3.640  5.546  14.560 0.50 31.05 ? 270 SER A CA    1 
ATOM   2021 C CA    B SER A 1 279 ? 3.607  5.517  14.558 0.50 31.06 ? 270 SER A CA    1 
ATOM   2022 C C     A SER A 1 279 ? 3.777  5.038  13.129 0.50 35.75 ? 270 SER A C     1 
ATOM   2023 C C     B SER A 1 279 ? 3.723  5.007  13.130 0.50 35.74 ? 270 SER A C     1 
ATOM   2024 O O     A SER A 1 279 ? 3.359  5.736  12.194 0.50 42.07 ? 270 SER A O     1 
ATOM   2025 O O     B SER A 1 279 ? 3.245  5.674  12.203 0.50 42.02 ? 270 SER A O     1 
ATOM   2026 C CB    A SER A 1 279 ? 4.483  6.834  14.717 0.50 36.74 ? 270 SER A CB    1 
ATOM   2027 C CB    B SER A 1 279 ? 4.496  6.746  14.712 0.50 36.82 ? 270 SER A CB    1 
ATOM   2028 O OG    A SER A 1 279 ? 4.371  7.439  16.002 0.50 31.36 ? 270 SER A OG    1 
ATOM   2029 O OG    B SER A 1 279 ? 5.820  6.369  14.389 0.50 30.80 ? 270 SER A OG    1 
ATOM   2030 N N     . GLY A 1 280 ? 4.344  3.851  12.938 1.00 32.11 ? 271 GLY A N     1 
ATOM   2031 C CA    . GLY A 1 280 ? 4.638  3.346  11.612 1.00 40.68 ? 271 GLY A CA    1 
ATOM   2032 C C     . GLY A 1 280 ? 5.676  4.129  10.832 1.00 33.31 ? 271 GLY A C     1 
ATOM   2033 O O     . GLY A 1 280 ? 5.662  4.091  9.605  1.00 36.61 ? 271 GLY A O     1 
ATOM   2034 N N     A SER A 1 281 ? 6.602  4.797  11.508 0.50 32.16 ? 272 SER A N     1 
ATOM   2035 N N     B SER A 1 281 ? 6.566  4.882  11.501 0.50 32.18 ? 272 SER A N     1 
ATOM   2036 C CA    A SER A 1 281 ? 7.539  5.641  10.792 0.50 32.75 ? 272 SER A CA    1 
ATOM   2037 C CA    B SER A 1 281 ? 7.492  5.762  10.787 0.50 32.91 ? 272 SER A CA    1 
ATOM   2038 C C     A SER A 1 281 ? 8.786  5.763  11.647 0.50 27.74 ? 272 SER A C     1 
ATOM   2039 C C     B SER A 1 281 ? 8.693  6.122  11.661 0.50 23.12 ? 272 SER A C     1 
ATOM   2040 O O     A SER A 1 281 ? 8.772  5.428  12.827 0.50 31.89 ? 272 SER A O     1 
ATOM   2041 O O     B SER A 1 281 ? 8.549  6.316  12.866 0.50 27.57 ? 272 SER A O     1 
ATOM   2042 C CB    A SER A 1 281 ? 6.939  7.028  10.565 0.50 34.84 ? 272 SER A CB    1 
ATOM   2043 C CB    B SER A 1 281 ? 6.821  7.068  10.339 0.50 35.21 ? 272 SER A CB    1 
ATOM   2044 O OG    A SER A 1 281 ? 6.228  7.409  11.724 0.50 31.18 ? 272 SER A OG    1 
ATOM   2045 O OG    B SER A 1 281 ? 7.725  7.860  9.577  0.50 42.08 ? 272 SER A OG    1 
ATOM   2046 N N     . LYS A 1 282 ? 9.862  6.229  11.036 1.00 25.37 ? 273 LYS A N     1 
ATOM   2047 C CA    . LYS A 1 282 ? 11.099 6.491  11.760 1.00 23.65 ? 273 LYS A CA    1 
ATOM   2048 C C     . LYS A 1 282 ? 11.250 7.982  11.998 1.00 22.54 ? 273 LYS A C     1 
ATOM   2049 O O     . LYS A 1 282 ? 10.810 8.809  11.195 1.00 23.42 ? 273 LYS A O     1 
ATOM   2050 C CB    . LYS A 1 282 ? 12.323 5.982  11.004 1.00 26.81 ? 273 LYS A CB    1 
ATOM   2051 C CG    . LYS A 1 282 ? 12.348 4.390  11.026 1.00 33.08 ? 273 LYS A CG    1 
ATOM   2052 C CD    . LYS A 1 282 ? 13.741 3.796  10.977 1.00 41.51 ? 273 LYS A CD    1 
ATOM   2053 C CE    . LYS A 1 282 ? 13.793 2.282  11.324 1.00 39.39 ? 273 LYS A CE    1 
ATOM   2054 N NZ    . LYS A 1 282 ? 12.516 1.526  11.211 1.00 53.86 ? 273 LYS A NZ    1 
ATOM   2055 N N     . LEU A 1 283 ? 11.808 8.310  13.152 1.00 18.66 ? 274 LEU A N     1 
ATOM   2056 C CA    . LEU A 1 283 ? 12.280 9.673  13.411 1.00 17.26 ? 274 LEU A CA    1 
ATOM   2057 C C     . LEU A 1 283 ? 13.328 10.058 12.387 1.00 18.26 ? 274 LEU A C     1 
ATOM   2058 O O     . LEU A 1 283 ? 13.948 9.227  11.729 1.00 20.15 ? 274 LEU A O     1 
ATOM   2059 C CB    . LEU A 1 283 ? 12.914 9.717  14.806 1.00 18.45 ? 274 LEU A CB    1 
ATOM   2060 C CG    . LEU A 1 283 ? 11.899 9.429  15.918 1.00 19.11 ? 274 LEU A CG    1 
ATOM   2061 C CD1   . LEU A 1 283 ? 12.607 9.053  17.274 1.00 23.23 ? 274 LEU A CD1   1 
ATOM   2062 C CD2   . LEU A 1 283 ? 10.923 10.614 16.135 1.00 20.47 ? 274 LEU A CD2   1 
ATOM   2063 N N     . ALA A 1 284 ? 13.568 11.363 12.265 1.00 18.28 ? 275 ALA A N     1 
ATOM   2064 C CA    . ALA A 1 284 ? 14.658 11.754 11.392 1.00 16.54 ? 275 ALA A CA    1 
ATOM   2065 C C     . ALA A 1 284 ? 15.997 11.223 11.909 1.00 17.65 ? 275 ALA A C     1 
ATOM   2066 O O     . ALA A 1 284 ? 16.865 10.847 11.114 1.00 18.90 ? 275 ALA A O     1 
ATOM   2067 C CB    . ALA A 1 284 ? 14.731 13.294 11.338 1.00 21.23 ? 275 ALA A CB    1 
ATOM   2068 N N     . TYR A 1 285 ? 16.231 11.306 13.233 1.00 17.88 ? 276 TYR A N     1 
ATOM   2069 C CA    . TYR A 1 285 ? 17.484 10.808 13.791 1.00 18.16 ? 276 TYR A CA    1 
ATOM   2070 C C     . TYR A 1 285 ? 17.454 10.859 15.310 1.00 15.61 ? 276 TYR A C     1 
ATOM   2071 O O     . TYR A 1 285 ? 16.630 11.560 15.920 1.00 16.93 ? 276 TYR A O     1 
ATOM   2072 C CB    . TYR A 1 285 ? 18.701 11.619 13.305 1.00 17.26 ? 276 TYR A CB    1 
ATOM   2073 C CG    . TYR A 1 285 ? 18.586 13.087 13.618 1.00 15.74 ? 276 TYR A CG    1 
ATOM   2074 C CD1   . TYR A 1 285 ? 18.899 13.605 14.898 1.00 16.82 ? 276 TYR A CD1   1 
ATOM   2075 C CD2   . TYR A 1 285 ? 18.054 13.963 12.671 1.00 17.41 ? 276 TYR A CD2   1 
ATOM   2076 C CE1   . TYR A 1 285 ? 18.768 14.968 15.167 1.00 16.71 ? 276 TYR A CE1   1 
ATOM   2077 C CE2   . TYR A 1 285 ? 17.905 15.325 12.953 1.00 17.70 ? 276 TYR A CE2   1 
ATOM   2078 C CZ    . TYR A 1 285 ? 18.257 15.806 14.202 1.00 16.94 ? 276 TYR A CZ    1 
ATOM   2079 O OH    . TYR A 1 285 ? 18.119 17.175 14.480 1.00 19.02 ? 276 TYR A OH    1 
ATOM   2080 N N     . LEU A 1 286 ? 18.425 10.159 15.895 1.00 15.55 ? 277 LEU A N     1 
ATOM   2081 C CA    . LEU A 1 286 ? 18.883 10.342 17.277 1.00 14.95 ? 277 LEU A CA    1 
ATOM   2082 C C     . LEU A 1 286 ? 20.263 10.991 17.254 1.00 16.93 ? 277 LEU A C     1 
ATOM   2083 O O     . LEU A 1 286 ? 21.151 10.589 16.496 1.00 16.62 ? 277 LEU A O     1 
ATOM   2084 C CB    . LEU A 1 286 ? 18.999 8.962  17.939 1.00 15.95 ? 277 LEU A CB    1 
ATOM   2085 C CG    . LEU A 1 286 ? 19.678 8.926  19.322 1.00 16.06 ? 277 LEU A CG    1 
ATOM   2086 C CD1   . LEU A 1 286 ? 18.902 9.668  20.364 1.00 18.83 ? 277 LEU A CD1   1 
ATOM   2087 C CD2   . LEU A 1 286 ? 19.830 7.424  19.761 1.00 17.84 ? 277 LEU A CD2   1 
ATOM   2088 N N     . HIS A 1 287 ? 20.437 12.030 18.076 1.00 14.78 ? 278 HIS A N     1 
ATOM   2089 C CA    . HIS A 1 287 ? 21.657 12.832 18.059 1.00 15.78 ? 278 HIS A CA    1 
ATOM   2090 C C     . HIS A 1 287 ? 22.204 12.774 19.466 1.00 17.92 ? 278 HIS A C     1 
ATOM   2091 O O     . HIS A 1 287 ? 21.499 13.122 20.425 1.00 16.75 ? 278 HIS A O     1 
ATOM   2092 C CB    . HIS A 1 287 ? 21.257 14.281 17.674 1.00 16.20 ? 278 HIS A CB    1 
ATOM   2093 C CG    . HIS A 1 287 ? 22.370 15.262 17.427 1.00 16.54 ? 278 HIS A CG    1 
ATOM   2094 N ND1   . HIS A 1 287 ? 22.058 16.538 17.017 1.00 17.27 ? 278 HIS A ND1   1 
ATOM   2095 C CD2   . HIS A 1 287 ? 23.719 15.198 17.488 1.00 16.78 ? 278 HIS A CD2   1 
ATOM   2096 C CE1   . HIS A 1 287 ? 23.181 17.208 16.780 1.00 17.49 ? 278 HIS A CE1   1 
ATOM   2097 N NE2   . HIS A 1 287 ? 24.208 16.433 17.089 1.00 16.86 ? 278 HIS A NE2   1 
ATOM   2098 N N     . VAL A 1 288 ? 23.421 12.252 19.638 1.00 16.42 ? 279 VAL A N     1 
ATOM   2099 C CA    . VAL A 1 288 ? 24.005 12.121 20.990 1.00 16.86 ? 279 VAL A CA    1 
ATOM   2100 C C     . VAL A 1 288 ? 25.306 12.911 21.058 1.00 16.18 ? 279 VAL A C     1 
ATOM   2101 O O     . VAL A 1 288 ? 26.177 12.748 20.185 1.00 18.12 ? 279 VAL A O     1 
ATOM   2102 C CB    . VAL A 1 288 ? 24.204 10.636 21.382 1.00 16.92 ? 279 VAL A CB    1 
ATOM   2103 C CG1   . VAL A 1 288 ? 24.778 10.554 22.804 1.00 19.45 ? 279 VAL A CG1   1 
ATOM   2104 C CG2   . VAL A 1 288 ? 22.862 9.892  21.302 1.00 18.66 ? 279 VAL A CG2   1 
ATOM   2105 N N     . THR A 1 289 ? 25.482 13.696 22.136 1.00 16.89 ? 280 THR A N     1 
ATOM   2106 C CA    . THR A 1 289 ? 26.752 14.375 22.355 1.00 17.22 ? 280 THR A CA    1 
ATOM   2107 C C     . THR A 1 289 ? 27.530 13.658 23.439 1.00 20.27 ? 280 THR A C     1 
ATOM   2108 O O     . THR A 1 289 ? 26.962 13.326 24.511 1.00 21.47 ? 280 THR A O     1 
ATOM   2109 C CB    . THR A 1 289 ? 26.593 15.837 22.827 1.00 22.95 ? 280 THR A CB    1 
ATOM   2110 O OG1   . THR A 1 289 ? 25.849 15.907 24.037 1.00 27.17 ? 280 THR A OG1   1 
ATOM   2111 C CG2   . THR A 1 289 ? 25.800 16.560 21.900 1.00 24.55 ? 280 THR A CG2   1 
ATOM   2112 N N     . GLN A 1 290 ? 28.748 13.382 23.157 1.00 19.95 ? 281 GLN A N     1 
ATOM   2113 C CA    . GLN A 1 290 ? 29.634 12.680 24.083 1.00 21.41 ? 281 GLN A CA    1 
ATOM   2114 C C     . GLN A 1 290 ? 30.550 13.641 24.825 1.00 23.34 ? 281 GLN A C     1 
ATOM   2115 O O     . GLN A 1 290 ? 30.945 14.699 24.314 1.00 24.35 ? 281 GLN A O     1 
ATOM   2116 C CB    . GLN A 1 290 ? 30.487 11.646 23.345 1.00 20.37 ? 281 GLN A CB    1 
ATOM   2117 C CG    . GLN A 1 290 ? 31.531 12.245 22.427 1.00 21.83 ? 281 GLN A CG    1 
ATOM   2118 C CD    . GLN A 1 290 ? 32.411 11.146 21.819 1.00 27.42 ? 281 GLN A CD    1 
ATOM   2119 O OE1   . GLN A 1 290 ? 32.074 10.547 20.812 1.00 34.24 ? 281 GLN A OE1   1 
ATOM   2120 N NE2   . GLN A 1 290 ? 33.539 10.873 22.470 1.00 31.26 ? 281 GLN A NE2   1 
ATOM   2121 N N     . PRO A 1 291 ? 30.912 13.271 26.045 1.00 25.69 ? 282 PRO A N     1 
ATOM   2122 C CA    . PRO A 1 291 ? 31.984 13.972 26.727 1.00 29.18 ? 282 PRO A CA    1 
ATOM   2123 C C     . PRO A 1 291 ? 33.286 13.525 26.070 1.00 31.69 ? 282 PRO A C     1 
ATOM   2124 O O     . PRO A 1 291 ? 33.360 12.483 25.405 1.00 34.07 ? 282 PRO A O     1 
ATOM   2125 C CB    . PRO A 1 291 ? 31.869 13.428 28.162 1.00 29.56 ? 282 PRO A CB    1 
ATOM   2126 C CG    . PRO A 1 291 ? 31.470 11.983 27.932 1.00 30.87 ? 282 PRO A CG    1 
ATOM   2127 C CD    . PRO A 1 291 ? 30.465 12.067 26.772 1.00 26.60 ? 282 PRO A CD    1 
ATOM   2128 N N     . ARG A 1 292 ? 34.305 14.355 26.232 1.00 32.79 ? 283 ARG A N     1 
ATOM   2129 C CA    . ARG A 1 292 ? 35.688 14.044 25.878 1.00 32.61 ? 283 ARG A CA    1 
ATOM   2130 C C     . ARG A 1 292 ? 36.497 14.179 27.163 1.00 42.39 ? 283 ARG A C     1 
ATOM   2131 O O     . ARG A 1 292 ? 36.967 15.271 27.479 1.00 42.22 ? 283 ARG A O     1 
ATOM   2132 C CB    . ARG A 1 292 ? 36.175 15.075 24.858 1.00 33.28 ? 283 ARG A CB    1 
ATOM   2133 C CG    . ARG A 1 292 ? 35.469 14.924 23.535 1.00 28.77 ? 283 ARG A CG    1 
ATOM   2134 C CD    . ARG A 1 292 ? 36.059 13.724 22.763 1.00 29.06 ? 283 ARG A CD    1 
ATOM   2135 N NE    . ARG A 1 292 ? 35.408 13.609 21.462 1.00 26.94 ? 283 ARG A NE    1 
ATOM   2136 C CZ    . ARG A 1 292 ? 35.655 12.695 20.540 1.00 27.04 ? 283 ARG A CZ    1 
ATOM   2137 N NH1   . ARG A 1 292 ? 36.627 11.795 20.682 1.00 29.12 ? 283 ARG A NH1   1 
ATOM   2138 N NH2   . ARG A 1 292 ? 34.876 12.636 19.468 1.00 23.93 ? 283 ARG A NH2   1 
ATOM   2139 N N     . SER A 1 293 ? 36.670 13.081 27.896 1.00 45.94 ? 284 SER A N     1 
ATOM   2140 C CA    . SER A 1 293 ? 37.441 13.117 29.148 1.00 58.95 ? 284 SER A CA    1 
ATOM   2141 C C     . SER A 1 293 ? 38.942 12.904 28.922 1.00 49.92 ? 284 SER A C     1 
ATOM   2142 O O     . SER A 1 293 ? 39.407 12.812 27.779 1.00 58.05 ? 284 SER A O     1 
ATOM   2143 C CB    . SER A 1 293 ? 36.904 12.087 30.151 1.00 49.15 ? 284 SER A CB    1 
ATOM   2144 N N     . SER A 1 298 ? 39.758 6.789  28.933 1.00 60.05 ? 289 SER A N     1 
ATOM   2145 C CA    . SER A 1 298 ? 38.535 7.529  28.635 1.00 58.87 ? 289 SER A CA    1 
ATOM   2146 C C     . SER A 1 298 ? 38.062 7.281  27.213 1.00 49.69 ? 289 SER A C     1 
ATOM   2147 O O     . SER A 1 298 ? 36.880 7.013  27.003 1.00 44.77 ? 289 SER A O     1 
ATOM   2148 C CB    . SER A 1 298 ? 38.699 9.049  28.869 1.00 46.64 ? 289 SER A CB    1 
ATOM   2149 N N     . GLU A 1 299 ? 38.965 7.364  26.232 1.00 43.38 ? 290 GLU A N     1 
ATOM   2150 C CA    . GLU A 1 299 ? 38.509 7.367  24.844 1.00 44.64 ? 290 GLU A CA    1 
ATOM   2151 C C     . GLU A 1 299 ? 37.769 6.082  24.504 1.00 37.89 ? 290 GLU A C     1 
ATOM   2152 O O     . GLU A 1 299 ? 36.716 6.116  23.855 1.00 32.92 ? 290 GLU A O     1 
ATOM   2153 C CB    . GLU A 1 299 ? 39.665 7.622  23.869 1.00 47.59 ? 290 GLU A CB    1 
ATOM   2154 N N     . GLU A 1 300 ? 38.300 4.933  24.927 1.00 35.27 ? 291 GLU A N     1 
ATOM   2155 C CA    . GLU A 1 300 ? 37.666 3.685  24.531 1.00 29.43 ? 291 GLU A CA    1 
ATOM   2156 C C     . GLU A 1 300 ? 36.314 3.501  25.221 1.00 27.59 ? 291 GLU A C     1 
ATOM   2157 O O     . GLU A 1 300 ? 35.355 3.047  24.585 1.00 28.49 ? 291 GLU A O     1 
ATOM   2158 C CB    . GLU A 1 300 ? 38.597 2.492  24.795 1.00 35.75 ? 291 GLU A CB    1 
ATOM   2159 N N     . GLU A 1 301 ? 36.222 3.848  26.508 1.00 31.52 ? 292 GLU A N     1 
ATOM   2160 C CA    . GLU A 1 301 ? 34.950 3.740  27.217 1.00 29.94 ? 292 GLU A CA    1 
ATOM   2161 C C     . GLU A 1 301 ? 33.911 4.710  26.652 1.00 30.80 ? 292 GLU A C     1 
ATOM   2162 O O     . GLU A 1 301 ? 32.758 4.329  26.438 1.00 28.11 ? 292 GLU A O     1 
ATOM   2163 C CB    . GLU A 1 301 ? 35.164 3.972  28.712 1.00 39.72 ? 292 GLU A CB    1 
ATOM   2164 N N     . GLU A 1 302 ? 34.293 5.962  26.394 1.00 27.32 ? 293 GLU A N     1 
ATOM   2165 C CA    . GLU A 1 302 ? 33.326 6.886  25.781 1.00 27.36 ? 293 GLU A CA    1 
ATOM   2166 C C     . GLU A 1 302 ? 32.871 6.394  24.417 1.00 24.60 ? 293 GLU A C     1 
ATOM   2167 O O     . GLU A 1 302 ? 31.682 6.487  24.074 1.00 24.55 ? 293 GLU A O     1 
ATOM   2168 C CB    . GLU A 1 302 ? 33.894 8.308  25.626 1.00 34.95 ? 293 GLU A CB    1 
ATOM   2169 C CG    . GLU A 1 302 ? 34.637 8.819  26.817 1.00 45.76 ? 293 GLU A CG    1 
ATOM   2170 C CD    . GLU A 1 302 ? 35.338 10.153 26.550 1.00 58.82 ? 293 GLU A CD    1 
ATOM   2171 O OE1   . GLU A 1 302 ? 35.962 10.320 25.459 1.00 50.52 ? 293 GLU A OE1   1 
ATOM   2172 O OE2   . GLU A 1 302 ? 35.292 11.006 27.459 1.00 45.19 ? 293 GLU A OE2   1 
ATOM   2173 N N     . ALA A 1 303 ? 33.801 5.893  23.604 1.00 23.92 ? 294 ALA A N     1 
ATOM   2174 C CA    . ALA A 1 303 ? 33.412 5.405  22.305 1.00 21.01 ? 294 ALA A CA    1 
ATOM   2175 C C     . ALA A 1 303 ? 32.469 4.221  22.432 1.00 22.64 ? 294 ALA A C     1 
ATOM   2176 O O     . ALA A 1 303 ? 31.532 4.073  21.627 1.00 23.95 ? 294 ALA A O     1 
ATOM   2177 C CB    . ALA A 1 303 ? 34.635 5.016  21.461 1.00 26.39 ? 294 ALA A CB    1 
ATOM   2178 N N     . ARG A 1 304 ? 32.733 3.332  23.420 1.00 22.41 ? 295 ARG A N     1 
ATOM   2179 C CA    . ARG A 1 304 ? 31.922 2.138  23.516 1.00 22.68 ? 295 ARG A CA    1 
ATOM   2180 C C     . ARG A 1 304 ? 30.500 2.480  23.891 1.00 19.29 ? 295 ARG A C     1 
ATOM   2181 O O     . ARG A 1 304 ? 29.559 1.908  23.329 1.00 21.11 ? 295 ARG A O     1 
ATOM   2182 C CB    . ARG A 1 304 ? 32.529 1.186  24.542 1.00 27.27 ? 295 ARG A CB    1 
ATOM   2183 C CG    . ARG A 1 304 ? 31.699 -0.068 24.686 1.00 24.87 ? 295 ARG A CG    1 
ATOM   2184 C CD    . ARG A 1 304 ? 32.378 -1.095 25.619 1.00 26.33 ? 295 ARG A CD    1 
ATOM   2185 N NE    . ARG A 1 304 ? 32.434 -0.595 26.972 1.00 34.60 ? 295 ARG A NE    1 
ATOM   2186 C CZ    . ARG A 1 304 ? 33.108 -1.198 27.943 1.00 51.43 ? 295 ARG A CZ    1 
ATOM   2187 N NH1   . ARG A 1 304 ? 33.806 -2.296 27.709 1.00 47.92 ? 295 ARG A NH1   1 
ATOM   2188 N NH2   . ARG A 1 304 ? 33.067 -0.695 29.174 1.00 44.66 ? 295 ARG A NH2   1 
ATOM   2189 N N     . LEU A 1 305 ? 30.330 3.478  24.749 1.00 21.29 ? 296 LEU A N     1 
ATOM   2190 C CA    . LEU A 1 305 ? 28.991 3.897  25.125 1.00 21.87 ? 296 LEU A CA    1 
ATOM   2191 C C     . LEU A 1 305 ? 28.245 4.453  23.917 1.00 20.96 ? 296 LEU A C     1 
ATOM   2192 O O     . LEU A 1 305 ? 27.082 4.094  23.665 1.00 20.97 ? 296 LEU A O     1 
ATOM   2193 C CB    . LEU A 1 305 ? 29.079 4.908  26.281 1.00 23.39 ? 296 LEU A CB    1 
ATOM   2194 C CG    . LEU A 1 305 ? 27.818 5.079  27.091 1.00 27.73 ? 296 LEU A CG    1 
ATOM   2195 C CD1   . LEU A 1 305 ? 28.197 5.711  28.448 1.00 29.94 ? 296 LEU A CD1   1 
ATOM   2196 C CD2   . LEU A 1 305 ? 26.927 5.967  26.353 1.00 29.81 ? 296 LEU A CD2   1 
ATOM   2197 N N     . MET A 1 306 ? 28.910 5.312  23.137 1.00 19.17 ? 297 MET A N     1 
ATOM   2198 C CA    . MET A 1 306 ? 28.291 5.804  21.909 1.00 18.33 ? 297 MET A CA    1 
ATOM   2199 C C     . MET A 1 306 ? 27.855 4.712  20.968 1.00 21.03 ? 297 MET A C     1 
ATOM   2200 O O     . MET A 1 306 ? 26.743 4.740  20.415 1.00 20.82 ? 297 MET A O     1 
ATOM   2201 C CB    . MET A 1 306 ? 29.093 6.901  21.199 1.00 21.35 ? 297 MET A CB    1 
ATOM   2202 C CG    . MET A 1 306 ? 29.413 8.086  22.100 1.00 22.82 ? 297 MET A CG    1 
ATOM   2203 S SD    . MET A 1 306 ? 27.914 9.156  21.918 1.00 22.59 ? 297 MET A SD    1 
ATOM   2204 C CE    . MET A 1 306 ? 28.293 9.990  20.369 1.00 21.89 ? 297 MET A CE    1 
ATOM   2205 N N     . ARG A 1 307 ? 28.730 3.734  20.747 1.00 20.72 ? 298 ARG A N     1 
ATOM   2206 C CA    . ARG A 1 307 ? 28.423 2.661  19.819 1.00 21.63 ? 298 ARG A CA    1 
ATOM   2207 C C     . ARG A 1 307 ? 27.277 1.798  20.334 1.00 17.10 ? 298 ARG A C     1 
ATOM   2208 O O     . ARG A 1 307 ? 26.463 1.320  19.542 1.00 19.02 ? 298 ARG A O     1 
ATOM   2209 C CB    . ARG A 1 307 ? 29.696 1.856  19.573 1.00 25.19 ? 298 ARG A CB    1 
ATOM   2210 C CG    . ARG A 1 307 ? 29.564 0.873  18.451 1.00 28.17 ? 298 ARG A CG    1 
ATOM   2211 C CD    . ARG A 1 307 ? 29.036 1.568  17.191 1.00 33.87 ? 298 ARG A CD    1 
ATOM   2212 N NE    . ARG A 1 307 ? 28.581 0.631  16.175 1.00 39.22 ? 298 ARG A NE    1 
ATOM   2213 C CZ    . ARG A 1 307 ? 29.293 0.225  15.133 1.00 30.96 ? 298 ARG A CZ    1 
ATOM   2214 N NH1   . ARG A 1 307 ? 30.495 0.712  14.881 1.00 35.47 ? 298 ARG A NH1   1 
ATOM   2215 N NH2   . ARG A 1 307 ? 28.768 -0.673 14.309 1.00 44.15 ? 298 ARG A NH2   1 
ATOM   2216 N N     . THR A 1 308 ? 27.192 1.633  21.662 1.00 19.69 ? 299 THR A N     1 
ATOM   2217 C CA    . THR A 1 308 ? 26.126 0.831  22.234 1.00 18.92 ? 299 THR A CA    1 
ATOM   2218 C C     . THR A 1 308 ? 24.767 1.501  22.043 1.00 18.03 ? 299 THR A C     1 
ATOM   2219 O O     . THR A 1 308 ? 23.798 0.847  21.631 1.00 19.24 ? 299 THR A O     1 
ATOM   2220 C CB    . THR A 1 308 ? 26.418 0.596  23.712 1.00 20.44 ? 299 THR A CB    1 
ATOM   2221 O OG1   . THR A 1 308 ? 27.714 -0.034 23.852 1.00 22.83 ? 299 THR A OG1   1 
ATOM   2222 C CG2   . THR A 1 308 ? 25.379 -0.317 24.331 1.00 21.03 ? 299 THR A CG2   1 
ATOM   2223 N N     . LEU A 1 309 ? 24.698 2.830  22.233 1.00 18.15 ? 300 LEU A N     1 
ATOM   2224 C CA    . LEU A 1 309 ? 23.457 3.541  21.945 1.00 19.12 ? 300 LEU A CA    1 
ATOM   2225 C C     . LEU A 1 309 ? 23.119 3.478  20.467 1.00 16.28 ? 300 LEU A C     1 
ATOM   2226 O O     . LEU A 1 309 ? 21.968 3.231  20.085 1.00 18.75 ? 300 LEU A O     1 
ATOM   2227 C CB    . LEU A 1 309 ? 23.598 5.010  22.380 1.00 18.74 ? 300 LEU A CB    1 
ATOM   2228 C CG    . LEU A 1 309 ? 23.866 5.213  23.858 1.00 18.78 ? 300 LEU A CG    1 
ATOM   2229 C CD1   . LEU A 1 309 ? 24.081 6.737  24.205 1.00 21.60 ? 300 LEU A CD1   1 
ATOM   2230 C CD2   . LEU A 1 309 ? 22.752 4.566  24.705 1.00 20.79 ? 300 LEU A CD2   1 
ATOM   2231 N N     . ARG A 1 310 ? 24.117 3.697  19.596 1.00 17.46 ? 301 ARG A N     1 
ATOM   2232 C CA    . ARG A 1 310 ? 23.878 3.642  18.156 1.00 16.28 ? 301 ARG A CA    1 
ATOM   2233 C C     . ARG A 1 310 ? 23.345 2.268  17.747 1.00 17.60 ? 301 ARG A C     1 
ATOM   2234 O O     . ARG A 1 310 ? 22.338 2.155  17.033 1.00 18.23 ? 301 ARG A O     1 
ATOM   2235 C CB    . ARG A 1 310 ? 25.193 3.936  17.419 1.00 19.24 ? 301 ARG A CB    1 
ATOM   2236 C CG    . ARG A 1 310 ? 25.091 4.142  15.899 1.00 19.89 ? 301 ARG A CG    1 
ATOM   2237 C CD    . ARG A 1 310 ? 25.034 2.801  15.132 1.00 19.05 ? 301 ARG A CD    1 
ATOM   2238 N NE    . ARG A 1 310 ? 25.603 2.987  13.794 1.00 20.96 ? 301 ARG A NE    1 
ATOM   2239 C CZ    . ARG A 1 310 ? 24.995 3.687  12.831 1.00 21.01 ? 301 ARG A CZ    1 
ATOM   2240 N NH1   . ARG A 1 310 ? 23.757 4.135  12.976 1.00 21.11 ? 301 ARG A NH1   1 
ATOM   2241 N NH2   . ARG A 1 310 ? 25.675 4.014  11.723 1.00 23.90 ? 301 ARG A NH2   1 
ATOM   2242 N N     . ASN A 1 311 ? 23.992 1.201  18.234 1.00 18.06 ? 302 ASN A N     1 
ATOM   2243 C CA    . ASN A 1 311 ? 23.548 -0.134 17.831 1.00 20.38 ? 302 ASN A CA    1 
ATOM   2244 C C     . ASN A 1 311 ? 22.154 -0.468 18.354 1.00 18.72 ? 302 ASN A C     1 
ATOM   2245 O O     . ASN A 1 311 ? 21.447 -1.316 17.768 1.00 20.17 ? 302 ASN A O     1 
ATOM   2246 C CB    . ASN A 1 311 ? 24.521 -1.172 18.379 1.00 21.13 ? 302 ASN A CB    1 
ATOM   2247 C CG    . ASN A 1 311 ? 25.817 -1.218 17.634 1.00 26.20 ? 302 ASN A CG    1 
ATOM   2248 O OD1   . ASN A 1 311 ? 25.994 -0.621 16.570 1.00 26.82 ? 302 ASN A OD1   1 
ATOM   2249 N ND2   . ASN A 1 311 ? 26.763 -1.947 18.210 1.00 25.56 ? 302 ASN A ND2   1 
ATOM   2250 N N     . ALA A 1 312 ? 21.731 0.166  19.449 1.00 17.75 ? 303 ALA A N     1 
ATOM   2251 C CA    . ALA A 1 312 ? 20.423 -0.088 20.033 1.00 18.70 ? 303 ALA A CA    1 
ATOM   2252 C C     . ALA A 1 312 ? 19.298 0.635  19.305 1.00 16.93 ? 303 ALA A C     1 
ATOM   2253 O O     . ALA A 1 312 ? 18.129 0.243  19.471 1.00 18.24 ? 303 ALA A O     1 
ATOM   2254 C CB    . ALA A 1 312 ? 20.432 0.341  21.516 1.00 17.32 ? 303 ALA A CB    1 
ATOM   2255 N N     . TYR A 1 313 ? 19.610 1.708  18.549 1.00 17.02 ? 304 TYR A N     1 
ATOM   2256 C CA    . TYR A 1 313 ? 18.589 2.579  17.979 1.00 17.20 ? 304 TYR A CA    1 
ATOM   2257 C C     . TYR A 1 313 ? 18.265 2.165  16.542 1.00 16.86 ? 304 TYR A C     1 
ATOM   2258 O O     . TYR A 1 313 ? 19.167 2.020  15.707 1.00 18.80 ? 304 TYR A O     1 
ATOM   2259 C CB    . TYR A 1 313 ? 19.084 4.045  18.035 1.00 16.42 ? 304 TYR A CB    1 
ATOM   2260 C CG    . TYR A 1 313 ? 18.128 4.959  17.311 1.00 16.28 ? 304 TYR A CG    1 
ATOM   2261 C CD1   . TYR A 1 313 ? 16.773 4.980  17.652 1.00 17.22 ? 304 TYR A CD1   1 
ATOM   2262 C CD2   . TYR A 1 313 ? 18.549 5.773  16.256 1.00 14.80 ? 304 TYR A CD2   1 
ATOM   2263 C CE1   . TYR A 1 313 ? 15.844 5.725  16.951 1.00 17.99 ? 304 TYR A CE1   1 
ATOM   2264 C CE2   . TYR A 1 313 ? 17.611 6.542  15.554 1.00 16.99 ? 304 TYR A CE2   1 
ATOM   2265 C CZ    . TYR A 1 313 ? 16.300 6.502  15.904 1.00 17.94 ? 304 TYR A CZ    1 
ATOM   2266 O OH    . TYR A 1 313 ? 15.404 7.221  15.137 1.00 19.01 ? 304 TYR A OH    1 
ATOM   2267 N N     . GLN A 1 314 ? 16.964 2.023  16.256 1.00 17.62 ? 305 GLN A N     1 
ATOM   2268 C CA    . GLN A 1 314 ? 16.520 1.641  14.904 1.00 18.53 ? 305 GLN A CA    1 
ATOM   2269 C C     . GLN A 1 314 ? 16.406 2.906  14.067 1.00 19.64 ? 305 GLN A C     1 
ATOM   2270 O O     . GLN A 1 314 ? 15.317 3.427  13.815 1.00 23.84 ? 305 GLN A O     1 
ATOM   2271 C CB    . GLN A 1 314 ? 15.169 0.946  14.944 1.00 21.12 ? 305 GLN A CB    1 
ATOM   2272 C CG    . GLN A 1 314 ? 15.223 -0.402 15.707 1.00 21.53 ? 305 GLN A CG    1 
ATOM   2273 C CD    . GLN A 1 314 ? 13.880 -1.069 15.802 1.00 21.76 ? 305 GLN A CD    1 
ATOM   2274 O OE1   . GLN A 1 314 ? 12.983 -0.821 14.971 1.00 25.04 ? 305 GLN A OE1   1 
ATOM   2275 N NE2   . GLN A 1 314 ? 13.728 -1.920 16.826 1.00 26.27 ? 305 GLN A NE2   1 
ATOM   2276 N N     . GLY A 1 315 ? 17.549 3.427  13.652 1.00 19.09 ? 306 GLY A N     1 
ATOM   2277 C CA    . GLY A 1 315 ? 17.496 4.572  12.752 1.00 19.53 ? 306 GLY A CA    1 
ATOM   2278 C C     . GLY A 1 315 ? 18.836 5.308  12.657 1.00 17.43 ? 306 GLY A C     1 
ATOM   2279 O O     . GLY A 1 315 ? 19.892 4.764  12.941 1.00 18.86 ? 306 GLY A O     1 
ATOM   2280 N N     . THR A 1 316 ? 18.751 6.541  12.180 1.00 18.07 ? 307 THR A N     1 
ATOM   2281 C CA    . THR A 1 316 ? 19.917 7.376  11.858 1.00 17.58 ? 307 THR A CA    1 
ATOM   2282 C C     . THR A 1 316 ? 20.513 7.961  13.124 1.00 18.06 ? 307 THR A C     1 
ATOM   2283 O O     . THR A 1 316 ? 19.777 8.394  14.018 1.00 17.72 ? 307 THR A O     1 
ATOM   2284 C CB    . THR A 1 316 ? 19.464 8.544  10.992 1.00 18.37 ? 307 THR A CB    1 
ATOM   2285 O OG1   . THR A 1 316 ? 19.002 8.024  9.747  1.00 21.26 ? 307 THR A OG1   1 
ATOM   2286 C CG2   . THR A 1 316 ? 20.602 9.564  10.727 1.00 18.11 ? 307 THR A CG2   1 
ATOM   2287 N N     . PHE A 1 317 ? 21.831 7.898  13.234 1.00 17.49 ? 308 PHE A N     1 
ATOM   2288 C CA    . PHE A 1 317 ? 22.567 8.331  14.422 1.00 17.24 ? 308 PHE A CA    1 
ATOM   2289 C C     . PHE A 1 317 ? 23.513 9.449  14.055 1.00 16.78 ? 308 PHE A C     1 
ATOM   2290 O O     . PHE A 1 317 ? 24.351 9.304  13.163 1.00 17.52 ? 308 PHE A O     1 
ATOM   2291 C CB    . PHE A 1 317 ? 23.317 7.117  15.018 1.00 18.04 ? 308 PHE A CB    1 
ATOM   2292 C CG    . PHE A 1 317 ? 23.907 7.366  16.378 1.00 17.27 ? 308 PHE A CG    1 
ATOM   2293 C CD1   . PHE A 1 317 ? 23.112 7.186  17.520 1.00 17.35 ? 308 PHE A CD1   1 
ATOM   2294 C CD2   . PHE A 1 317 ? 25.237 7.716  16.535 1.00 17.15 ? 308 PHE A CD2   1 
ATOM   2295 C CE1   . PHE A 1 317 ? 23.672 7.375  18.815 1.00 18.14 ? 308 PHE A CE1   1 
ATOM   2296 C CE2   . PHE A 1 317 ? 25.805 7.891  17.815 1.00 19.48 ? 308 PHE A CE2   1 
ATOM   2297 C CZ    . PHE A 1 317 ? 24.985 7.729  18.954 1.00 18.17 ? 308 PHE A CZ    1 
ATOM   2298 N N     . ILE A 1 318 ? 23.388 10.588 14.758 1.00 17.32 ? 309 ILE A N     1 
ATOM   2299 C CA    . ILE A 1 318 ? 24.319 11.710 14.630 1.00 16.69 ? 309 ILE A CA    1 
ATOM   2300 C C     . ILE A 1 318 ? 25.188 11.774 15.877 1.00 16.62 ? 309 ILE A C     1 
ATOM   2301 O O     . ILE A 1 318 ? 24.662 11.851 16.989 1.00 18.06 ? 309 ILE A O     1 
ATOM   2302 C CB    . ILE A 1 318 ? 23.568 13.048 14.446 1.00 16.75 ? 309 ILE A CB    1 
ATOM   2303 C CG1   . ILE A 1 318 ? 22.450 12.882 13.401 1.00 15.88 ? 309 ILE A CG1   1 
ATOM   2304 C CG2   . ILE A 1 318 ? 24.548 14.179 14.154 1.00 17.13 ? 309 ILE A CG2   1 
ATOM   2305 C CD1   . ILE A 1 318 ? 21.806 14.272 12.997 1.00 20.07 ? 309 ILE A CD1   1 
ATOM   2306 N N     . CYS A 1 319 ? 26.520 11.740 15.698 1.00 17.01 ? 310 CYS A N     1 
ATOM   2307 C CA    . CYS A 1 319 ? 27.386 11.839 16.873 1.00 18.59 ? 310 CYS A CA    1 
ATOM   2308 C C     . CYS A 1 319 ? 27.893 13.288 16.941 1.00 20.94 ? 310 CYS A C     1 
ATOM   2309 O O     . CYS A 1 319 ? 28.016 13.981 15.915 1.00 19.92 ? 310 CYS A O     1 
ATOM   2310 C CB    . CYS A 1 319 ? 28.674 11.003 16.814 1.00 19.65 ? 310 CYS A CB    1 
ATOM   2311 S SG    . CYS A 1 319 ? 29.551 11.028 15.223 1.00 22.97 ? 310 CYS A SG    1 
ATOM   2312 N N     . SER A 1 320 ? 28.292 13.733 18.139 1.00 18.20 ? 311 SER A N     1 
ATOM   2313 C CA    . SER A 1 320 ? 28.760 15.097 18.324 1.00 17.41 ? 311 SER A CA    1 
ATOM   2314 C C     . SER A 1 320 ? 29.620 15.139 19.568 1.00 17.42 ? 311 SER A C     1 
ATOM   2315 O O     . SER A 1 320 ? 29.455 14.301 20.467 1.00 19.82 ? 311 SER A O     1 
ATOM   2316 C CB    . SER A 1 320 ? 27.555 16.028 18.569 1.00 19.80 ? 311 SER A CB    1 
ATOM   2317 O OG    . SER A 1 320 ? 27.917 17.391 18.370 1.00 22.90 ? 311 SER A OG    1 
ATOM   2318 N N     . GLY A 1 321 ? 30.487 16.160 19.646 1.00 18.31 ? 312 GLY A N     1 
ATOM   2319 C CA    . GLY A 1 321 ? 31.293 16.437 20.828 1.00 19.11 ? 312 GLY A CA    1 
ATOM   2320 C C     . GLY A 1 321 ? 32.761 16.191 20.541 1.00 21.68 ? 312 GLY A C     1 
ATOM   2321 O O     . GLY A 1 321 ? 33.215 15.046 20.591 1.00 21.83 ? 312 GLY A O     1 
ATOM   2322 N N     . GLY A 1 322 ? 33.494 17.275 20.250 1.00 19.21 ? 313 GLY A N     1 
ATOM   2323 C CA    . GLY A 1 322 ? 34.919 17.129 20.035 1.00 20.91 ? 313 GLY A CA    1 
ATOM   2324 C C     . GLY A 1 322 ? 35.357 16.552 18.720 1.00 23.03 ? 313 GLY A C     1 
ATOM   2325 O O     . GLY A 1 322 ? 36.528 16.164 18.612 1.00 24.48 ? 313 GLY A O     1 
ATOM   2326 N N     . TYR A 1 323 ? 34.473 16.478 17.722 1.00 21.62 ? 314 TYR A N     1 
ATOM   2327 C CA    . TYR A 1 323 ? 34.858 15.881 16.448 1.00 21.75 ? 314 TYR A CA    1 
ATOM   2328 C C     . TYR A 1 323 ? 35.790 16.800 15.656 1.00 23.90 ? 314 TYR A C     1 
ATOM   2329 O O     . TYR A 1 323 ? 35.775 18.036 15.764 1.00 24.38 ? 314 TYR A O     1 
ATOM   2330 C CB    . TYR A 1 323 ? 33.643 15.367 15.618 1.00 22.24 ? 314 TYR A CB    1 
ATOM   2331 C CG    . TYR A 1 323 ? 33.146 14.045 16.194 1.00 22.33 ? 314 TYR A CG    1 
ATOM   2332 C CD1   . TYR A 1 323 ? 32.274 14.048 17.280 1.00 22.34 ? 314 TYR A CD1   1 
ATOM   2333 C CD2   . TYR A 1 323 ? 33.622 12.796 15.752 1.00 22.70 ? 314 TYR A CD2   1 
ATOM   2334 C CE1   . TYR A 1 323 ? 31.853 12.880 17.905 1.00 22.97 ? 314 TYR A CE1   1 
ATOM   2335 C CE2   . TYR A 1 323 ? 33.175 11.627 16.351 1.00 24.06 ? 314 TYR A CE2   1 
ATOM   2336 C CZ    . TYR A 1 323 ? 32.319 11.671 17.444 1.00 25.24 ? 314 TYR A CZ    1 
ATOM   2337 O OH    . TYR A 1 323 ? 31.907 10.494 18.078 1.00 25.42 ? 314 TYR A OH    1 
ATOM   2338 N N     . THR A 1 324 ? 36.661 16.163 14.924 1.00 23.91 ? 315 THR A N     1 
ATOM   2339 C CA    . THR A 1 324 ? 37.567 16.832 13.990 1.00 21.67 ? 315 THR A CA    1 
ATOM   2340 C C     . THR A 1 324 ? 37.346 16.198 12.635 1.00 26.04 ? 315 THR A C     1 
ATOM   2341 O O     . THR A 1 324 ? 36.541 15.282 12.474 1.00 24.82 ? 315 THR A O     1 
ATOM   2342 C CB    . THR A 1 324 ? 39.011 16.605 14.418 1.00 25.59 ? 315 THR A CB    1 
ATOM   2343 O OG1   . THR A 1 324 ? 39.263 15.188 14.396 1.00 26.27 ? 315 THR A OG1   1 
ATOM   2344 C CG2   . THR A 1 324 ? 39.265 17.158 15.825 1.00 27.34 ? 315 THR A CG2   1 
ATOM   2345 N N     . ARG A 1 325 ? 38.094 16.662 11.642 1.00 26.18 ? 316 ARG A N     1 
ATOM   2346 C CA    . ARG A 1 325 ? 37.983 16.024 10.341 1.00 23.98 ? 316 ARG A CA    1 
ATOM   2347 C C     . ARG A 1 325 ? 38.283 14.525 10.429 1.00 21.57 ? 316 ARG A C     1 
ATOM   2348 O O     . ARG A 1 325 ? 37.513 13.674 9.955  1.00 23.08 ? 316 ARG A O     1 
ATOM   2349 C CB    . ARG A 1 325 ? 38.935 16.689 9.342  1.00 23.96 ? 316 ARG A CB    1 
ATOM   2350 C CG    . ARG A 1 325 ? 38.946 15.962 7.987  1.00 25.22 ? 316 ARG A CG    1 
ATOM   2351 C CD    . ARG A 1 325 ? 39.794 16.749 7.007  1.00 24.94 ? 316 ARG A CD    1 
ATOM   2352 N NE    . ARG A 1 325 ? 39.626 16.227 5.648  1.00 26.44 ? 316 ARG A NE    1 
ATOM   2353 C CZ    . ARG A 1 325 ? 40.295 15.185 5.154  1.00 26.26 ? 316 ARG A CZ    1 
ATOM   2354 N NH1   . ARG A 1 325 ? 41.163 14.504 5.897  1.00 28.82 ? 316 ARG A NH1   1 
ATOM   2355 N NH2   . ARG A 1 325 ? 40.072 14.809 3.896  1.00 31.50 ? 316 ARG A NH2   1 
ATOM   2356 N N     . GLU A 1 326 ? 39.415 14.185 11.038 1.00 23.99 ? 317 GLU A N     1 
ATOM   2357 C CA    . GLU A 1 326 ? 39.838 12.786 11.118 1.00 25.93 ? 317 GLU A CA    1 
ATOM   2358 C C     . GLU A 1 326 ? 38.897 11.958 11.975 1.00 23.92 ? 317 GLU A C     1 
ATOM   2359 O O     . GLU A 1 326 ? 38.580 10.819 11.607 1.00 24.09 ? 317 GLU A O     1 
ATOM   2360 C CB    . GLU A 1 326 ? 41.269 12.744 11.664 1.00 32.31 ? 317 GLU A CB    1 
ATOM   2361 C CG    . GLU A 1 326 ? 42.298 13.337 10.684 1.00 44.73 ? 317 GLU A CG    1 
ATOM   2362 C CD    . GLU A 1 326 ? 42.158 14.860 10.463 1.00 59.64 ? 317 GLU A CD    1 
ATOM   2363 O OE1   . GLU A 1 326 ? 41.904 15.651 11.448 1.00 37.56 ? 317 GLU A OE1   1 
ATOM   2364 O OE2   . GLU A 1 326 ? 42.291 15.232 9.254  1.00 42.98 ? 317 GLU A OE2   1 
ATOM   2365 N N     . LEU A 1 327 ? 38.446 12.497 13.119 1.00 21.94 ? 318 LEU A N     1 
ATOM   2366 C CA    . LEU A 1 327 ? 37.539 11.719 13.963 1.00 23.20 ? 318 LEU A CA    1 
ATOM   2367 C C     . LEU A 1 327 ? 36.186 11.524 13.295 1.00 22.77 ? 318 LEU A C     1 
ATOM   2368 O O     . LEU A 1 327 ? 35.552 10.477 13.455 1.00 22.81 ? 318 LEU A O     1 
ATOM   2369 C CB    . LEU A 1 327 ? 37.371 12.383 15.332 1.00 24.53 ? 318 LEU A CB    1 
ATOM   2370 C CG    . LEU A 1 327 ? 38.594 12.382 16.256 1.00 25.61 ? 318 LEU A CG    1 
ATOM   2371 C CD1   . LEU A 1 327 ? 38.341 13.271 17.459 1.00 25.77 ? 318 LEU A CD1   1 
ATOM   2372 C CD2   . LEU A 1 327 ? 38.951 10.925 16.677 1.00 28.68 ? 318 LEU A CD2   1 
ATOM   2373 N N     . GLY A 1 328 ? 35.730 12.501 12.517 1.00 20.53 ? 319 GLY A N     1 
ATOM   2374 C CA    . GLY A 1 328 ? 34.468 12.317 11.818 1.00 21.71 ? 319 GLY A CA    1 
ATOM   2375 C C     . GLY A 1 328 ? 34.573 11.319 10.683 1.00 21.43 ? 319 GLY A C     1 
ATOM   2376 O O     . GLY A 1 328 ? 33.660 10.514 10.453 1.00 22.81 ? 319 GLY A O     1 
ATOM   2377 N N     . ILE A 1 329 ? 35.681 11.369 9.936  1.00 24.05 ? 320 ILE A N     1 
ATOM   2378 C CA    . ILE A 1 329 ? 35.909 10.349 8.921  1.00 24.39 ? 320 ILE A CA    1 
ATOM   2379 C C     . ILE A 1 329 ? 35.887 8.952  9.538  1.00 23.51 ? 320 ILE A C     1 
ATOM   2380 O O     . ILE A 1 329 ? 35.221 8.045  9.036  1.00 24.43 ? 320 ILE A O     1 
ATOM   2381 C CB    . ILE A 1 329 ? 37.233 10.617 8.185  1.00 24.20 ? 320 ILE A CB    1 
ATOM   2382 C CG1   . ILE A 1 329 ? 37.102 11.822 7.255  1.00 25.24 ? 320 ILE A CG1   1 
ATOM   2383 C CG2   . ILE A 1 329 ? 37.687 9.392  7.394  1.00 25.42 ? 320 ILE A CG2   1 
ATOM   2384 C CD1   . ILE A 1 329 ? 38.499 12.263 6.643  1.00 25.68 ? 320 ILE A CD1   1 
ATOM   2385 N N     . GLU A 1 330 ? 36.612 8.774  10.633 1.00 24.94 ? 321 GLU A N     1 
ATOM   2386 C CA    . GLU A 1 330 ? 36.666 7.485  11.324 1.00 26.06 ? 321 GLU A CA    1 
ATOM   2387 C C     . GLU A 1 330 ? 35.279 7.040  11.777 1.00 27.39 ? 321 GLU A C     1 
ATOM   2388 O O     . GLU A 1 330 ? 34.901 5.869  11.616 1.00 26.14 ? 321 GLU A O     1 
ATOM   2389 C CB    . GLU A 1 330 ? 37.606 7.653  12.517 1.00 26.92 ? 321 GLU A CB    1 
ATOM   2390 C CG    . GLU A 1 330 ? 38.286 6.440  13.036 1.00 57.15 ? 321 GLU A CG    1 
ATOM   2391 C CD    . GLU A 1 330 ? 38.504 6.413  14.575 1.00 76.63 ? 321 GLU A CD    1 
ATOM   2392 O OE1   . GLU A 1 330 ? 38.092 7.353  15.310 1.00 64.52 ? 321 GLU A OE1   1 
ATOM   2393 O OE2   . GLU A 1 330 ? 39.086 5.407  15.054 1.00 72.69 ? 321 GLU A OE2   1 
ATOM   2394 N N     . ALA A 1 331 ? 34.489 7.962  12.348 1.00 24.99 ? 322 ALA A N     1 
ATOM   2395 C CA    . ALA A 1 331 ? 33.172 7.571  12.850 1.00 23.39 ? 322 ALA A CA    1 
ATOM   2396 C C     . ALA A 1 331 ? 32.287 7.026  11.745 1.00 24.42 ? 322 ALA A C     1 
ATOM   2397 O O     . ALA A 1 331 ? 31.569 6.034  11.956 1.00 24.11 ? 322 ALA A O     1 
ATOM   2398 C CB    . ALA A 1 331 ? 32.487 8.772  13.499 1.00 23.97 ? 322 ALA A CB    1 
ATOM   2399 N N     . VAL A 1 332 ? 32.297 7.665  10.558 1.00 23.43 ? 323 VAL A N     1 
ATOM   2400 C CA    . VAL A 1 332 ? 31.443 7.184  9.484  1.00 22.05 ? 323 VAL A CA    1 
ATOM   2401 C C     . VAL A 1 332 ? 32.013 5.911  8.882  1.00 22.31 ? 323 VAL A C     1 
ATOM   2402 O O     . VAL A 1 332 ? 31.278 4.947  8.648  1.00 24.44 ? 323 VAL A O     1 
ATOM   2403 C CB    . VAL A 1 332 ? 31.209 8.257  8.413  1.00 24.82 ? 323 VAL A CB    1 
ATOM   2404 C CG1   . VAL A 1 332 ? 30.467 7.677  7.230  1.00 25.96 ? 323 VAL A CG1   1 
ATOM   2405 C CG2   . VAL A 1 332 ? 30.437 9.460  9.030  1.00 24.37 ? 323 VAL A CG2   1 
ATOM   2406 N N     . ALA A 1 333 ? 33.322 5.880  8.675  1.00 23.55 ? 324 ALA A N     1 
ATOM   2407 C CA    . ALA A 1 333 ? 33.957 4.737  8.025  1.00 25.60 ? 324 ALA A CA    1 
ATOM   2408 C C     . ALA A 1 333 ? 33.793 3.490  8.859  1.00 26.37 ? 324 ALA A C     1 
ATOM   2409 O O     . ALA A 1 333 ? 33.607 2.401  8.303  1.00 27.01 ? 324 ALA A O     1 
ATOM   2410 C CB    . ALA A 1 333 ? 35.436 5.029  7.817  1.00 28.85 ? 324 ALA A CB    1 
ATOM   2411 N N     . GLN A 1 334 ? 33.828 3.621  10.187 1.00 23.94 ? 325 GLN A N     1 
ATOM   2412 C CA    . GLN A 1 334 ? 33.658 2.457  11.072 1.00 26.97 ? 325 GLN A CA    1 
ATOM   2413 C C     . GLN A 1 334 ? 32.225 2.100  11.403 1.00 29.87 ? 325 GLN A C     1 
ATOM   2414 O O     . GLN A 1 334 ? 32.009 1.123  12.142 1.00 30.22 ? 325 GLN A O     1 
ATOM   2415 C CB    . GLN A 1 334 ? 34.477 2.523  12.346 1.00 29.01 ? 325 GLN A CB    1 
ATOM   2416 C CG    . GLN A 1 334 ? 35.941 2.678  12.159 1.00 33.70 ? 325 GLN A CG    1 
ATOM   2417 C CD    . GLN A 1 334 ? 36.629 3.355  13.287 1.00 59.27 ? 325 GLN A CD    1 
ATOM   2418 O OE1   . GLN A 1 334 ? 36.140 3.353  14.422 1.00 66.28 ? 325 GLN A OE1   1 
ATOM   2419 N NE2   . GLN A 1 334 ? 37.886 3.688  13.055 1.00 62.20 ? 325 GLN A NE2   1 
ATOM   2420 N N     . GLY A 1 335 ? 31.264 2.842  10.885 1.00 27.41 ? 326 GLY A N     1 
ATOM   2421 C CA    . GLY A 1 335 ? 29.881 2.546  11.116 1.00 27.14 ? 326 GLY A CA    1 
ATOM   2422 C C     . GLY A 1 335 ? 29.385 3.036  12.448 1.00 23.50 ? 326 GLY A C     1 
ATOM   2423 O O     . GLY A 1 335 ? 28.287 2.627  12.860 1.00 26.86 ? 326 GLY A O     1 
ATOM   2424 N N     . ASP A 1 336 ? 30.183 3.848  13.156 1.00 23.65 ? 327 ASP A N     1 
ATOM   2425 C CA    . ASP A 1 336 ? 29.842 4.323  14.493 1.00 21.43 ? 327 ASP A CA    1 
ATOM   2426 C C     . ASP A 1 336 ? 28.756 5.393  14.437 1.00 22.84 ? 327 ASP A C     1 
ATOM   2427 O O     . ASP A 1 336 ? 28.084 5.632  15.443 1.00 24.19 ? 327 ASP A O     1 
ATOM   2428 C CB    . ASP A 1 336 ? 31.076 4.910  15.200 1.00 25.06 ? 327 ASP A CB    1 
ATOM   2429 C CG    . ASP A 1 336 ? 32.183 3.874  15.434 1.00 38.26 ? 327 ASP A CG    1 
ATOM   2430 O OD1   . ASP A 1 336 ? 31.866 2.690  15.638 1.00 35.23 ? 327 ASP A OD1   1 
ATOM   2431 O OD2   . ASP A 1 336 ? 33.363 4.267  15.429 1.00 39.44 ? 327 ASP A OD2   1 
ATOM   2432 N N     . ALA A 1 337 ? 28.592 6.055  13.286 1.00 21.80 ? 328 ALA A N     1 
ATOM   2433 C CA    . ALA A 1 337 ? 27.596 7.105  13.162 1.00 19.93 ? 328 ALA A CA    1 
ATOM   2434 C C     . ALA A 1 337 ? 27.252 7.229  11.700 1.00 18.76 ? 328 ALA A C     1 
ATOM   2435 O O     . ALA A 1 337 ? 28.064 6.900  10.819 1.00 21.63 ? 328 ALA A O     1 
ATOM   2436 C CB    . ALA A 1 337 ? 28.136 8.452  13.672 1.00 22.66 ? 328 ALA A CB    1 
ATOM   2437 N N     . ASP A 1 338 ? 26.060 7.761  11.432 1.00 18.76 ? 329 ASP A N     1 
ATOM   2438 C CA    . ASP A 1 338 ? 25.730 8.078  10.048 1.00 18.67 ? 329 ASP A CA    1 
ATOM   2439 C C     . ASP A 1 338 ? 26.058 9.511  9.669  1.00 19.08 ? 329 ASP A C     1 
ATOM   2440 O O     . ASP A 1 338 ? 26.398 9.794  8.504  1.00 19.96 ? 329 ASP A O     1 
ATOM   2441 C CB    . ASP A 1 338 ? 24.248 7.856  9.811  1.00 18.93 ? 329 ASP A CB    1 
ATOM   2442 C CG    . ASP A 1 338 ? 23.827 6.472  10.263 1.00 20.02 ? 329 ASP A CG    1 
ATOM   2443 O OD1   . ASP A 1 338 ? 24.312 5.505  9.612  1.00 22.29 ? 329 ASP A OD1   1 
ATOM   2444 O OD2   . ASP A 1 338 ? 23.063 6.292  11.248 1.00 19.36 ? 329 ASP A OD2   1 
ATOM   2445 N N     . LEU A 1 339 ? 25.935 10.434 10.610 1.00 18.05 ? 330 LEU A N     1 
ATOM   2446 C CA    . LEU A 1 339 ? 26.216 11.847 10.387 1.00 17.35 ? 330 LEU A CA    1 
ATOM   2447 C C     . LEU A 1 339 ? 27.052 12.327 11.564 1.00 18.24 ? 330 LEU A C     1 
ATOM   2448 O O     . LEU A 1 339 ? 26.953 11.770 12.658 1.00 18.06 ? 330 LEU A O     1 
ATOM   2449 C CB    . LEU A 1 339 ? 24.911 12.681 10.276 1.00 18.93 ? 330 LEU A CB    1 
ATOM   2450 C CG    . LEU A 1 339 ? 23.888 12.216 9.231  1.00 18.63 ? 330 LEU A CG    1 
ATOM   2451 C CD1   . LEU A 1 339 ? 22.527 12.887 9.346  1.00 19.93 ? 330 LEU A CD1   1 
ATOM   2452 C CD2   . LEU A 1 339 ? 24.434 12.517 7.851  1.00 21.78 ? 330 LEU A CD2   1 
ATOM   2453 N N     . VAL A 1 340 ? 27.855 13.383 11.338 1.00 17.99 ? 331 VAL A N     1 
ATOM   2454 C CA    . VAL A 1 340 ? 28.742 13.945 12.358 1.00 16.74 ? 331 VAL A CA    1 
ATOM   2455 C C     . VAL A 1 340 ? 28.421 15.424 12.448 1.00 16.76 ? 331 VAL A C     1 
ATOM   2456 O O     . VAL A 1 340 ? 28.526 16.134 11.441 1.00 17.37 ? 331 VAL A O     1 
ATOM   2457 C CB    . VAL A 1 340 ? 30.215 13.766 11.983 1.00 19.47 ? 331 VAL A CB    1 
ATOM   2458 C CG1   . VAL A 1 340 ? 31.071 14.245 13.104 1.00 20.09 ? 331 VAL A CG1   1 
ATOM   2459 C CG2   . VAL A 1 340 ? 30.538 12.258 11.742 1.00 19.36 ? 331 VAL A CG2   1 
ATOM   2460 N N     . SER A 1 341 ? 28.056 15.897 13.643 1.00 16.40 ? 332 SER A N     1 
ATOM   2461 C CA    . SER A 1 341 ? 27.810 17.326 13.787 1.00 15.49 ? 332 SER A CA    1 
ATOM   2462 C C     . SER A 1 341 ? 29.029 17.987 14.410 1.00 17.84 ? 332 SER A C     1 
ATOM   2463 O O     . SER A 1 341 ? 29.708 17.430 15.272 1.00 18.85 ? 332 SER A O     1 
ATOM   2464 C CB    . SER A 1 341 ? 26.503 17.653 14.565 1.00 16.90 ? 332 SER A CB    1 
ATOM   2465 O OG    . SER A 1 341 ? 26.610 17.326 15.946 1.00 19.16 ? 332 SER A OG    1 
ATOM   2466 N N     . TYR A 1 342 ? 29.277 19.208 13.977 1.00 16.76 ? 333 TYR A N     1 
ATOM   2467 C CA    . TYR A 1 342 ? 30.385 20.038 14.421 1.00 18.15 ? 333 TYR A CA    1 
ATOM   2468 C C     . TYR A 1 342 ? 29.803 21.349 14.928 1.00 16.58 ? 333 TYR A C     1 
ATOM   2469 O O     . TYR A 1 342 ? 29.009 21.997 14.239 1.00 17.45 ? 333 TYR A O     1 
ATOM   2470 C CB    . TYR A 1 342 ? 31.300 20.354 13.210 1.00 17.71 ? 333 TYR A CB    1 
ATOM   2471 C CG    . TYR A 1 342 ? 32.049 19.146 12.705 1.00 18.15 ? 333 TYR A CG    1 
ATOM   2472 C CD1   . TYR A 1 342 ? 31.480 18.311 11.739 1.00 19.11 ? 333 TYR A CD1   1 
ATOM   2473 C CD2   . TYR A 1 342 ? 33.308 18.854 13.192 1.00 19.19 ? 333 TYR A CD2   1 
ATOM   2474 C CE1   . TYR A 1 342 ? 32.171 17.202 11.240 1.00 19.37 ? 333 TYR A CE1   1 
ATOM   2475 C CE2   . TYR A 1 342 ? 34.000 17.734 12.721 1.00 19.00 ? 333 TYR A CE2   1 
ATOM   2476 C CZ    . TYR A 1 342 ? 33.432 16.946 11.751 1.00 19.20 ? 333 TYR A CZ    1 
ATOM   2477 O OH    . TYR A 1 342 ? 34.083 15.824 11.254 1.00 22.23 ? 333 TYR A OH    1 
ATOM   2478 N N     . GLY A 1 343 ? 30.278 21.782 16.090 1.00 16.98 ? 334 GLY A N     1 
ATOM   2479 C CA    . GLY A 1 343 ? 29.898 23.040 16.688 1.00 17.17 ? 334 GLY A CA    1 
ATOM   2480 C C     . GLY A 1 343 ? 31.003 24.055 16.490 1.00 18.41 ? 334 GLY A C     1 
ATOM   2481 O O     . GLY A 1 343 ? 30.954 24.874 15.561 1.00 18.27 ? 334 GLY A O     1 
ATOM   2482 N N     . ARG A 1 344 ? 31.976 24.084 17.404 1.00 17.77 ? 335 ARG A N     1 
ATOM   2483 C CA    . ARG A 1 344 ? 32.940 25.174 17.435 1.00 17.33 ? 335 ARG A CA    1 
ATOM   2484 C C     . ARG A 1 344 ? 33.682 25.349 16.114 1.00 16.07 ? 335 ARG A C     1 
ATOM   2485 O O     . ARG A 1 344 ? 33.904 26.498 15.730 1.00 17.02 ? 335 ARG A O     1 
ATOM   2486 C CB    . ARG A 1 344 ? 33.910 24.952 18.591 1.00 18.22 ? 335 ARG A CB    1 
ATOM   2487 C CG    . ARG A 1 344 ? 33.229 25.186 19.920 1.00 19.39 ? 335 ARG A CG    1 
ATOM   2488 C CD    . ARG A 1 344 ? 34.093 24.776 21.115 1.00 20.16 ? 335 ARG A CD    1 
ATOM   2489 N NE    . ARG A 1 344 ? 34.213 23.323 21.112 1.00 20.81 ? 335 ARG A NE    1 
ATOM   2490 C CZ    . ARG A 1 344 ? 35.169 22.681 21.757 1.00 24.08 ? 335 ARG A CZ    1 
ATOM   2491 N NH1   . ARG A 1 344 ? 36.014 23.341 22.558 1.00 26.01 ? 335 ARG A NH1   1 
ATOM   2492 N NH2   . ARG A 1 344 ? 35.304 21.377 21.570 1.00 25.25 ? 335 ARG A NH2   1 
ATOM   2493 N N     . LEU A 1 345 ? 34.070 24.268 15.425 1.00 16.74 ? 336 LEU A N     1 
ATOM   2494 C CA    . LEU A 1 345 ? 34.728 24.457 14.134 1.00 18.04 ? 336 LEU A CA    1 
ATOM   2495 C C     . LEU A 1 345 ? 33.824 25.155 13.141 1.00 17.76 ? 336 LEU A C     1 
ATOM   2496 O O     . LEU A 1 345 ? 34.320 25.860 12.258 1.00 18.22 ? 336 LEU A O     1 
ATOM   2497 C CB    . LEU A 1 345 ? 35.245 23.145 13.550 1.00 17.28 ? 336 LEU A CB    1 
ATOM   2498 C CG    . LEU A 1 345 ? 36.506 22.661 14.292 1.00 19.36 ? 336 LEU A CG    1 
ATOM   2499 C CD1   . LEU A 1 345 ? 36.771 21.203 13.916 1.00 21.48 ? 336 LEU A CD1   1 
ATOM   2500 C CD2   . LEU A 1 345 ? 37.725 23.571 13.977 1.00 20.72 ? 336 LEU A CD2   1 
ATOM   2501 N N     . PHE A 1 346 ? 32.503 24.999 13.260 1.00 17.88 ? 337 PHE A N     1 
ATOM   2502 C CA    . PHE A 1 346 ? 31.629 25.711 12.329 1.00 18.20 ? 337 PHE A CA    1 
ATOM   2503 C C     . PHE A 1 346 ? 31.473 27.175 12.703 1.00 17.34 ? 337 PHE A C     1 
ATOM   2504 O O     . PHE A 1 346 ? 31.089 27.993 11.843 1.00 19.64 ? 337 PHE A O     1 
ATOM   2505 C CB    . PHE A 1 346 ? 30.253 25.028 12.328 1.00 20.68 ? 337 PHE A CB    1 
ATOM   2506 C CG    . PHE A 1 346 ? 29.830 24.455 11.001 1.00 16.38 ? 337 PHE A CG    1 
ATOM   2507 C CD1   . PHE A 1 346 ? 29.870 25.227 9.854  1.00 17.91 ? 337 PHE A CD1   1 
ATOM   2508 C CD2   . PHE A 1 346 ? 29.372 23.136 10.883 1.00 17.93 ? 337 PHE A CD2   1 
ATOM   2509 C CE1   . PHE A 1 346 ? 29.421 24.711 8.643  1.00 18.86 ? 337 PHE A CE1   1 
ATOM   2510 C CE2   . PHE A 1 346 ? 28.910 22.662 9.661  1.00 18.90 ? 337 PHE A CE2   1 
ATOM   2511 C CZ    . PHE A 1 346 ? 28.949 23.439 8.555  1.00 18.61 ? 337 PHE A CZ    1 
ATOM   2512 N N     . ILE A 1 347 ? 31.726 27.540 13.957 1.00 17.55 ? 338 ILE A N     1 
ATOM   2513 C CA    . ILE A 1 347 ? 31.706 28.951 14.335 1.00 17.93 ? 338 ILE A CA    1 
ATOM   2514 C C     . ILE A 1 347 ? 32.737 29.701 13.510 1.00 18.58 ? 338 ILE A C     1 
ATOM   2515 O O     . ILE A 1 347 ? 32.447 30.751 12.920 1.00 18.49 ? 338 ILE A O     1 
ATOM   2516 C CB    . ILE A 1 347 ? 31.960 29.131 15.854 1.00 16.91 ? 338 ILE A CB    1 
ATOM   2517 C CG1   . ILE A 1 347 ? 30.732 28.653 16.629 1.00 17.16 ? 338 ILE A CG1   1 
ATOM   2518 C CG2   . ILE A 1 347 ? 32.374 30.634 16.184 1.00 18.63 ? 338 ILE A CG2   1 
ATOM   2519 C CD1   . ILE A 1 347 ? 30.962 28.678 18.127 1.00 23.57 ? 338 ILE A CD1   1 
ATOM   2520 N N     . SER A 1 348 ? 33.945 29.144 13.419 1.00 17.39 ? 339 SER A N     1 
ATOM   2521 C CA    . SER A 1 348 ? 35.057 29.894 12.832 1.00 19.42 ? 339 SER A CA    1 
ATOM   2522 C C     . SER A 1 348 ? 35.380 29.517 11.397 1.00 21.01 ? 339 SER A C     1 
ATOM   2523 O O     . SER A 1 348 ? 36.275 30.111 10.777 1.00 21.97 ? 339 SER A O     1 
ATOM   2524 C CB    . SER A 1 348 ? 36.318 29.759 13.693 1.00 20.45 ? 339 SER A CB    1 
ATOM   2525 O OG    . SER A 1 348 ? 36.603 28.368 13.881 1.00 18.94 ? 339 SER A OG    1 
ATOM   2526 N N     . ASN A 1 349 ? 34.711 28.509 10.846 1.00 18.11 ? 340 ASN A N     1 
ATOM   2527 C CA    . ASN A 1 349 ? 34.942 28.097 9.473  1.00 18.26 ? 340 ASN A CA    1 
ATOM   2528 C C     . ASN A 1 349 ? 33.586 28.029 8.829  1.00 20.37 ? 340 ASN A C     1 
ATOM   2529 O O     . ASN A 1 349 ? 32.949 26.963 8.835  1.00 19.91 ? 340 ASN A O     1 
ATOM   2530 C CB    . ASN A 1 349 ? 35.617 26.740 9.423  1.00 19.84 ? 340 ASN A CB    1 
ATOM   2531 C CG    . ASN A 1 349 ? 36.974 26.765 10.093 1.00 19.86 ? 340 ASN A CG    1 
ATOM   2532 O OD1   . ASN A 1 349 ? 37.975 27.074 9.437  1.00 20.57 ? 340 ASN A OD1   1 
ATOM   2533 N ND2   . ASN A 1 349 ? 37.028 26.429 11.365 1.00 19.30 ? 340 ASN A ND2   1 
ATOM   2534 N N     . PRO A 1 350 ? 33.126 29.121 8.238  1.00 19.44 ? 341 PRO A N     1 
ATOM   2535 C CA    . PRO A 1 350 ? 31.784 29.085 7.647  1.00 18.25 ? 341 PRO A CA    1 
ATOM   2536 C C     . PRO A 1 350 ? 31.713 28.068 6.536  1.00 19.95 ? 341 PRO A C     1 
ATOM   2537 O O     . PRO A 1 350 ? 30.680 27.409 6.345  1.00 21.45 ? 341 PRO A O     1 
ATOM   2538 C CB    . PRO A 1 350 ? 31.587 30.523 7.128  1.00 21.39 ? 341 PRO A CB    1 
ATOM   2539 C CG    . PRO A 1 350 ? 33.023 31.054 6.910  1.00 19.99 ? 341 PRO A CG    1 
ATOM   2540 C CD    . PRO A 1 350 ? 33.830 30.417 8.047  1.00 19.99 ? 341 PRO A CD    1 
ATOM   2541 N N     . ASP A 1 351 ? 32.809 27.893 5.816  1.00 19.99 ? 342 ASP A N     1 
ATOM   2542 C CA    . ASP A 1 351 ? 32.957 26.867 4.791  1.00 20.25 ? 342 ASP A CA    1 
ATOM   2543 C C     . ASP A 1 351 ? 33.595 25.590 5.310  1.00 21.44 ? 342 ASP A C     1 
ATOM   2544 O O     . ASP A 1 351 ? 34.407 24.927 4.642  1.00 21.73 ? 342 ASP A O     1 
ATOM   2545 C CB    . ASP A 1 351 ? 33.706 27.426 3.571  1.00 21.61 ? 342 ASP A CB    1 
ATOM   2546 C CG    . ASP A 1 351 ? 35.024 28.098 3.912  1.00 25.36 ? 342 ASP A CG    1 
ATOM   2547 O OD1   . ASP A 1 351 ? 35.395 28.278 5.103  1.00 23.65 ? 342 ASP A OD1   1 
ATOM   2548 O OD2   . ASP A 1 351 ? 35.715 28.459 2.920  1.00 28.30 ? 342 ASP A OD2   1 
ATOM   2549 N N     . LEU A 1 352 ? 33.206 25.185 6.520  1.00 19.11 ? 343 LEU A N     1 
ATOM   2550 C CA    . LEU A 1 352 ? 33.768 23.960 7.094  1.00 19.37 ? 343 LEU A CA    1 
ATOM   2551 C C     . LEU A 1 352 ? 33.607 22.772 6.161  1.00 19.91 ? 343 LEU A C     1 
ATOM   2552 O O     . LEU A 1 352 ? 34.494 21.931 6.079  1.00 21.06 ? 343 LEU A O     1 
ATOM   2553 C CB    . LEU A 1 352 ? 33.090 23.653 8.431  1.00 19.31 ? 343 LEU A CB    1 
ATOM   2554 C CG    . LEU A 1 352 ? 33.658 22.417 9.156  1.00 18.18 ? 343 LEU A CG    1 
ATOM   2555 C CD1   . LEU A 1 352 ? 35.177 22.578 9.479  1.00 21.42 ? 343 LEU A CD1   1 
ATOM   2556 C CD2   . LEU A 1 352 ? 32.877 22.130 10.445 1.00 20.42 ? 343 LEU A CD2   1 
ATOM   2557 N N     . VAL A 1 353 ? 32.455 22.648 5.492  1.00 19.95 ? 344 VAL A N     1 
ATOM   2558 C CA    . VAL A 1 353 ? 32.240 21.486 4.632  1.00 19.31 ? 344 VAL A CA    1 
ATOM   2559 C C     . VAL A 1 353 ? 33.301 21.427 3.547  1.00 20.13 ? 344 VAL A C     1 
ATOM   2560 O O     . VAL A 1 353 ? 33.930 20.384 3.330  1.00 20.83 ? 344 VAL A O     1 
ATOM   2561 C CB    . VAL A 1 353 ? 30.836 21.534 4.018  1.00 20.38 ? 344 VAL A CB    1 
ATOM   2562 C CG1   . VAL A 1 353 ? 30.612 20.322 3.126  1.00 24.56 ? 344 VAL A CG1   1 
ATOM   2563 C CG2   . VAL A 1 353 ? 29.783 21.536 5.119  1.00 21.96 ? 344 VAL A CG2   1 
ATOM   2564 N N     . MET A 1 354 ? 33.508 22.563 2.858  1.00 21.24 ? 345 MET A N     1 
ATOM   2565 C CA    . MET A 1 354 ? 34.499 22.600 1.781  1.00 22.25 ? 345 MET A CA    1 
ATOM   2566 C C     . MET A 1 354 ? 35.905 22.384 2.326  1.00 22.84 ? 345 MET A C     1 
ATOM   2567 O O     . MET A 1 354 ? 36.706 21.667 1.713  1.00 23.44 ? 345 MET A O     1 
ATOM   2568 C CB    . MET A 1 354 ? 34.443 23.986 1.163  1.00 25.07 ? 345 MET A CB    1 
ATOM   2569 C CG    . MET A 1 354 ? 35.282 24.207 -0.070 1.00 31.98 ? 345 MET A CG    1 
ATOM   2570 S SD    . MET A 1 354 ? 35.164 23.026 -1.454 1.00 55.36 ? 345 MET A SD    1 
ATOM   2571 C CE    . MET A 1 354 ? 33.466 22.392 -1.372 1.00 51.42 ? 345 MET A CE    1 
ATOM   2572 N N     . ARG A 1 355 ? 36.225 22.965 3.504  1.00 20.43 ? 346 ARG A N     1 
ATOM   2573 C CA    . ARG A 1 355 ? 37.551 22.746 4.058  1.00 22.79 ? 346 ARG A CA    1 
ATOM   2574 C C     . ARG A 1 355 ? 37.777 21.275 4.361  1.00 23.63 ? 346 ARG A C     1 
ATOM   2575 O O     . ARG A 1 355 ? 38.872 20.737 4.143  1.00 24.64 ? 346 ARG A O     1 
ATOM   2576 C CB    . ARG A 1 355 ? 37.740 23.574 5.327  1.00 20.65 ? 346 ARG A CB    1 
ATOM   2577 C CG    . ARG A 1 355 ? 37.733 25.072 5.019  1.00 22.65 ? 346 ARG A CG    1 
ATOM   2578 C CD    . ARG A 1 355 ? 38.058 25.889 6.260  1.00 22.55 ? 346 ARG A CD    1 
ATOM   2579 N NE    . ARG A 1 355 ? 37.795 27.311 6.063  1.00 23.67 ? 346 ARG A NE    1 
ATOM   2580 C CZ    . ARG A 1 355 ? 38.693 28.257 6.303  1.00 26.14 ? 346 ARG A CZ    1 
ATOM   2581 N NH1   . ARG A 1 355 ? 39.896 27.960 6.755  1.00 25.09 ? 346 ARG A NH1   1 
ATOM   2582 N NH2   . ARG A 1 355 ? 38.355 29.529 6.133  1.00 25.81 ? 346 ARG A NH2   1 
ATOM   2583 N N     . ILE A 1 356 ? 36.755 20.596 4.890  1.00 20.20 ? 347 ILE A N     1 
ATOM   2584 C CA    . ILE A 1 356 ? 36.869 19.165 5.152  1.00 23.11 ? 347 ILE A CA    1 
ATOM   2585 C C     . ILE A 1 356 ? 37.043 18.394 3.850  1.00 24.85 ? 347 ILE A C     1 
ATOM   2586 O O     . ILE A 1 356 ? 37.870 17.468 3.756  1.00 26.31 ? 347 ILE A O     1 
ATOM   2587 C CB    . ILE A 1 356 ? 35.655 18.699 5.985  1.00 22.21 ? 347 ILE A CB    1 
ATOM   2588 C CG1   . ILE A 1 356 ? 35.816 19.218 7.427  1.00 23.44 ? 347 ILE A CG1   1 
ATOM   2589 C CG2   . ILE A 1 356 ? 35.451 17.133 5.948  1.00 26.13 ? 347 ILE A CG2   1 
ATOM   2590 C CD1   . ILE A 1 356 ? 34.645 18.805 8.319  1.00 24.33 ? 347 ILE A CD1   1 
ATOM   2591 N N     . LYS A 1 357 ? 36.269 18.758 2.822  1.00 24.62 ? 348 LYS A N     1 
ATOM   2592 C CA    . LYS A 1 357 ? 36.413 18.085 1.532  1.00 26.69 ? 348 LYS A CA    1 
ATOM   2593 C C     . LYS A 1 357 ? 37.826 18.237 0.964  1.00 25.98 ? 348 LYS A C     1 
ATOM   2594 O O     . LYS A 1 357 ? 38.419 17.257 0.482  1.00 28.55 ? 348 LYS A O     1 
ATOM   2595 C CB    . LYS A 1 357 ? 35.361 18.629 0.566  1.00 25.21 ? 348 LYS A CB    1 
ATOM   2596 C CG    . LYS A 1 357 ? 35.449 18.083 -0.882 1.00 28.81 ? 348 LYS A CG    1 
ATOM   2597 C CD    . LYS A 1 357 ? 34.882 16.724 -0.977 1.00 38.32 ? 348 LYS A CD    1 
ATOM   2598 C CE    . LYS A 1 357 ? 34.567 16.326 -2.438 1.00 48.33 ? 348 LYS A CE    1 
ATOM   2599 N NZ    . LYS A 1 357 ? 33.624 17.298 -3.075 1.00 59.62 ? 348 LYS A NZ    1 
ATOM   2600 N N     . LEU A 1 358 ? 38.390 19.437 1.037  1.00 25.19 ? 349 LEU A N     1 
ATOM   2601 C CA    . LEU A 1 358 ? 39.714 19.696 0.478  1.00 27.46 ? 349 LEU A CA    1 
ATOM   2602 C C     . LEU A 1 358 ? 40.860 19.375 1.439  1.00 27.42 ? 349 LEU A C     1 
ATOM   2603 O O     . LEU A 1 358 ? 42.029 19.472 1.046  1.00 28.76 ? 349 LEU A O     1 
ATOM   2604 C CB    . LEU A 1 358 ? 39.809 21.171 0.069  1.00 27.10 ? 349 LEU A CB    1 
ATOM   2605 C CG    . LEU A 1 358 ? 38.791 21.694 -0.941 1.00 30.11 ? 349 LEU A CG    1 
ATOM   2606 C CD1   . LEU A 1 358 ? 38.983 23.218 -1.104 1.00 31.71 ? 349 LEU A CD1   1 
ATOM   2607 C CD2   . LEU A 1 358 ? 38.976 20.956 -2.271 1.00 36.59 ? 349 LEU A CD2   1 
ATOM   2608 N N     . ASN A 1 359 ? 40.576 18.994 2.696  1.00 25.14 ? 350 ASN A N     1 
ATOM   2609 C CA    . ASN A 1 359 ? 41.608 18.913 3.745  1.00 24.88 ? 350 ASN A CA    1 
ATOM   2610 C C     . ASN A 1 359 ? 42.405 20.216 3.853  1.00 26.54 ? 350 ASN A C     1 
ATOM   2611 O O     . ASN A 1 359 ? 43.630 20.209 4.000  1.00 28.36 ? 350 ASN A O     1 
ATOM   2612 C CB    . ASN A 1 359 ? 42.514 17.691 3.585  1.00 27.77 ? 350 ASN A CB    1 
ATOM   2613 C CG    . ASN A 1 359 ? 43.208 17.331 4.882  1.00 31.45 ? 350 ASN A CG    1 
ATOM   2614 O OD1   . ASN A 1 359 ? 42.805 17.783 5.957  1.00 29.76 ? 350 ASN A OD1   1 
ATOM   2615 N ND2   . ASN A 1 359 ? 44.257 16.519 4.797  1.00 36.88 ? 350 ASN A ND2   1 
ATOM   2616 N N     . ALA A 1 360 ? 41.705 21.336 3.793  1.00 24.31 ? 351 ALA A N     1 
ATOM   2617 C CA    . ALA A 1 360 ? 42.313 22.644 3.955  1.00 26.21 ? 351 ALA A CA    1 
ATOM   2618 C C     . ALA A 1 360 ? 42.440 22.948 5.440  1.00 25.97 ? 351 ALA A C     1 
ATOM   2619 O O     . ALA A 1 360 ? 41.600 22.528 6.238  1.00 26.10 ? 351 ALA A O     1 
ATOM   2620 C CB    . ALA A 1 360 ? 41.437 23.706 3.308  1.00 24.64 ? 351 ALA A CB    1 
ATOM   2621 N N     . PRO A 1 361 ? 43.469 23.685 5.852  1.00 26.73 ? 352 PRO A N     1 
ATOM   2622 C CA    . PRO A 1 361 ? 43.600 24.009 7.284  1.00 27.50 ? 352 PRO A CA    1 
ATOM   2623 C C     . PRO A 1 361 ? 42.379 24.731 7.824  1.00 23.34 ? 352 PRO A C     1 
ATOM   2624 O O     . PRO A 1 361 ? 41.792 25.580 7.161  1.00 25.78 ? 352 PRO A O     1 
ATOM   2625 C CB    . PRO A 1 361 ? 44.861 24.871 7.339  1.00 34.69 ? 352 PRO A CB    1 
ATOM   2626 C CG    . PRO A 1 361 ? 45.677 24.376 6.090  1.00 37.86 ? 352 PRO A CG    1 
ATOM   2627 C CD    . PRO A 1 361 ? 44.618 24.155 5.044  1.00 31.84 ? 352 PRO A CD    1 
ATOM   2628 N N     . LEU A 1 362 ? 42.005 24.390 9.056  1.00 21.75 ? 353 LEU A N     1 
ATOM   2629 C CA    . LEU A 1 362 ? 40.875 25.010 9.731  1.00 19.07 ? 353 LEU A CA    1 
ATOM   2630 C C     . LEU A 1 362 ? 41.334 26.201 10.566 1.00 19.66 ? 353 LEU A C     1 
ATOM   2631 O O     . LEU A 1 362 ? 42.432 26.197 11.132 1.00 20.41 ? 353 LEU A O     1 
ATOM   2632 C CB    . LEU A 1 362 ? 40.183 23.978 10.632 1.00 21.25 ? 353 LEU A CB    1 
ATOM   2633 C CG    . LEU A 1 362 ? 39.749 22.736 9.874  1.00 21.30 ? 353 LEU A CG    1 
ATOM   2634 C CD1   . LEU A 1 362 ? 38.986 21.809 10.832 1.00 25.00 ? 353 LEU A CD1   1 
ATOM   2635 C CD2   . LEU A 1 362 ? 38.880 23.050 8.680  1.00 23.38 ? 353 LEU A CD2   1 
ATOM   2636 N N     . ASN A 1 363 ? 40.474 27.221 10.692 1.00 18.99 ? 354 ASN A N     1 
ATOM   2637 C CA    . ASN A 1 363 ? 40.810 28.433 11.423 1.00 20.42 ? 354 ASN A CA    1 
ATOM   2638 C C     . ASN A 1 363 ? 40.277 28.350 12.847 1.00 20.12 ? 354 ASN A C     1 
ATOM   2639 O O     . ASN A 1 363 ? 39.229 27.741 13.094 1.00 20.63 ? 354 ASN A O     1 
ATOM   2640 C CB    . ASN A 1 363 ? 40.223 29.675 10.733 1.00 19.53 ? 354 ASN A CB    1 
ATOM   2641 C CG    . ASN A 1 363 ? 40.976 30.027 9.481  1.00 23.56 ? 354 ASN A CG    1 
ATOM   2642 O OD1   . ASN A 1 363 ? 42.094 29.576 9.253  1.00 26.66 ? 354 ASN A OD1   1 
ATOM   2643 N ND2   . ASN A 1 363 ? 40.339 30.822 8.622  1.00 26.72 ? 354 ASN A ND2   1 
ATOM   2644 N N     . LYS A 1 364 ? 41.019 28.918 13.805 1.00 18.88 ? 355 LYS A N     1 
ATOM   2645 C CA    . LYS A 1 364 ? 40.624 28.875 15.205 1.00 21.57 ? 355 LYS A CA    1 
ATOM   2646 C C     . LYS A 1 364 ? 39.355 29.685 15.469 1.00 20.37 ? 355 LYS A C     1 
ATOM   2647 O O     . LYS A 1 364 ? 39.026 30.637 14.738 1.00 20.43 ? 355 LYS A O     1 
ATOM   2648 C CB    . LYS A 1 364 ? 41.752 29.361 16.114 1.00 20.20 ? 355 LYS A CB    1 
ATOM   2649 C CG    . LYS A 1 364 ? 42.173 30.770 15.788 1.00 22.71 ? 355 LYS A CG    1 
ATOM   2650 C CD    . LYS A 1 364 ? 43.243 31.236 16.824 1.00 26.02 ? 355 LYS A CD    1 
ATOM   2651 C CE    . LYS A 1 364 ? 42.643 31.552 18.125 1.00 27.64 ? 355 LYS A CE    1 
ATOM   2652 N NZ    . LYS A 1 364 ? 43.707 32.143 19.030 1.00 35.27 ? 355 LYS A NZ    1 
ATOM   2653 N N     . TYR A 1 365 ? 38.676 29.337 16.548 1.00 19.40 ? 356 TYR A N     1 
ATOM   2654 C CA    . TYR A 1 365 ? 37.516 30.087 17.031 1.00 20.34 ? 356 TYR A CA    1 
ATOM   2655 C C     . TYR A 1 365 ? 37.883 30.897 18.270 1.00 24.00 ? 356 TYR A C     1 
ATOM   2656 O O     . TYR A 1 365 ? 38.769 30.518 19.052 1.00 24.36 ? 356 TYR A O     1 
ATOM   2657 C CB    . TYR A 1 365 ? 36.350 29.143 17.346 1.00 22.22 ? 356 TYR A CB    1 
ATOM   2658 C CG    . TYR A 1 365 ? 36.761 27.799 17.982 1.00 21.17 ? 356 TYR A CG    1 
ATOM   2659 C CD1   . TYR A 1 365 ? 36.994 27.688 19.385 1.00 26.69 ? 356 TYR A CD1   1 
ATOM   2660 C CD2   . TYR A 1 365 ? 36.898 26.633 17.220 1.00 21.11 ? 356 TYR A CD2   1 
ATOM   2661 C CE1   . TYR A 1 365 ? 37.354 26.477 19.957 1.00 22.74 ? 356 TYR A CE1   1 
ATOM   2662 C CE2   . TYR A 1 365 ? 37.271 25.388 17.800 1.00 21.69 ? 356 TYR A CE2   1 
ATOM   2663 C CZ    . TYR A 1 365 ? 37.485 25.319 19.172 1.00 20.68 ? 356 TYR A CZ    1 
ATOM   2664 O OH    . TYR A 1 365 ? 37.862 24.077 19.710 1.00 24.58 ? 356 TYR A OH    1 
ATOM   2665 N N     . ASN A 1 366 ? 37.160 32.001 18.440 1.00 22.16 ? 357 ASN A N     1 
ATOM   2666 C CA    . ASN A 1 366 ? 37.415 32.941 19.559 1.00 22.60 ? 357 ASN A CA    1 
ATOM   2667 C C     . ASN A 1 366 ? 36.269 32.822 20.557 1.00 26.05 ? 357 ASN A C     1 
ATOM   2668 O O     . ASN A 1 366 ? 35.199 33.377 20.310 1.00 21.80 ? 357 ASN A O     1 
ATOM   2669 C CB    . ASN A 1 366 ? 37.590 34.362 19.031 1.00 25.33 ? 357 ASN A CB    1 
ATOM   2670 C CG    . ASN A 1 366 ? 38.554 34.434 17.866 1.00 31.01 ? 357 ASN A CG    1 
ATOM   2671 O OD1   . ASN A 1 366 ? 38.231 34.980 16.817 1.00 43.78 ? 357 ASN A OD1   1 
ATOM   2672 N ND2   . ASN A 1 366 ? 39.744 33.888 18.042 1.00 42.59 ? 357 ASN A ND2   1 
ATOM   2673 N N     . ARG A 1 367 ? 36.525 32.154 21.667 1.00 29.17 ? 358 ARG A N     1 
ATOM   2674 C CA    . ARG A 1 367 ? 35.474 31.879 22.666 1.00 22.10 ? 358 ARG A CA    1 
ATOM   2675 C C     . ARG A 1 367 ? 34.870 33.170 23.216 1.00 22.85 ? 358 ARG A C     1 
ATOM   2676 O O     . ARG A 1 367 ? 33.714 33.156 23.599 1.00 22.65 ? 358 ARG A O     1 
ATOM   2677 C CB    . ARG A 1 367 ? 36.123 31.033 23.761 1.00 29.05 ? 358 ARG A CB    1 
ATOM   2678 C CG    . ARG A 1 367 ? 37.020 29.937 23.202 1.00 39.57 ? 358 ARG A CG    1 
ATOM   2679 C CD    . ARG A 1 367 ? 38.071 29.429 24.169 1.00 52.73 ? 358 ARG A CD    1 
ATOM   2680 N NE    . ARG A 1 367 ? 39.377 30.008 23.894 1.00 70.66 ? 358 ARG A NE    1 
ATOM   2681 C CZ    . ARG A 1 367 ? 40.391 30.016 24.751 1.00 69.40 ? 358 ARG A CZ    1 
ATOM   2682 N NH1   . ARG A 1 367 ? 40.527 29.029 25.616 1.00 49.54 ? 358 ARG A NH1   1 
ATOM   2683 N NH2   . ARG A 1 367 ? 41.260 31.013 24.741 1.00 54.63 ? 358 ARG A NH2   1 
ATOM   2684 N N     . LYS A 1 368 ? 35.665 34.230 23.263 1.00 22.83 ? 359 LYS A N     1 
ATOM   2685 C CA    . LYS A 1 368 ? 35.157 35.458 23.874 1.00 21.59 ? 359 LYS A CA    1 
ATOM   2686 C C     . LYS A 1 368 ? 33.948 36.008 23.116 1.00 22.97 ? 359 LYS A C     1 
ATOM   2687 O O     . LYS A 1 368 ? 33.147 36.733 23.721 1.00 23.12 ? 359 LYS A O     1 
ATOM   2688 C CB    . LYS A 1 368 ? 36.233 36.551 23.882 1.00 27.11 ? 359 LYS A CB    1 
ATOM   2689 N N     . THR A 1 369 ? 33.765 35.654 21.827 1.00 19.96 ? 360 THR A N     1 
ATOM   2690 C CA    . THR A 1 369 ? 32.608 36.172 21.102 1.00 21.13 ? 360 THR A CA    1 
ATOM   2691 C C     . THR A 1 369 ? 31.580 35.083 20.796 1.00 20.51 ? 360 THR A C     1 
ATOM   2692 O O     . THR A 1 369 ? 30.740 35.256 19.910 1.00 19.87 ? 360 THR A O     1 
ATOM   2693 C CB    . THR A 1 369 ? 33.054 36.907 19.848 1.00 18.83 ? 360 THR A CB    1 
ATOM   2694 O OG1   . THR A 1 369 ? 33.943 36.081 19.097 1.00 21.67 ? 360 THR A OG1   1 
ATOM   2695 C CG2   . THR A 1 369 ? 33.798 38.207 20.227 1.00 22.19 ? 360 THR A CG2   1 
ATOM   2696 N N     . PHE A 1 370 ? 31.594 33.989 21.556 1.00 18.53 ? 361 PHE A N     1 
ATOM   2697 C CA    . PHE A 1 370 ? 30.563 32.975 21.352 1.00 16.84 ? 361 PHE A CA    1 
ATOM   2698 C C     . PHE A 1 370 ? 29.177 33.512 21.664 1.00 17.19 ? 361 PHE A C     1 
ATOM   2699 O O     . PHE A 1 370 ? 28.200 33.199 20.942 1.00 17.64 ? 361 PHE A O     1 
ATOM   2700 C CB    . PHE A 1 370 ? 30.835 31.762 22.265 1.00 17.81 ? 361 PHE A CB    1 
ATOM   2701 C CG    . PHE A 1 370 ? 31.902 30.820 21.752 1.00 18.65 ? 361 PHE A CG    1 
ATOM   2702 C CD1   . PHE A 1 370 ? 32.640 31.062 20.601 1.00 19.78 ? 361 PHE A CD1   1 
ATOM   2703 C CD2   . PHE A 1 370 ? 32.189 29.678 22.497 1.00 20.36 ? 361 PHE A CD2   1 
ATOM   2704 C CE1   . PHE A 1 370 ? 33.623 30.183 20.162 1.00 21.35 ? 361 PHE A CE1   1 
ATOM   2705 C CE2   . PHE A 1 370 ? 33.192 28.769 22.032 1.00 20.20 ? 361 PHE A CE2   1 
ATOM   2706 C CZ    . PHE A 1 370 ? 33.893 29.041 20.888 1.00 19.57 ? 361 PHE A CZ    1 
ATOM   2707 N N     . TYR A 1 371 ? 29.037 34.327 22.728 1.00 18.46 ? 362 TYR A N     1 
ATOM   2708 C CA    . TYR A 1 371 ? 27.755 34.707 23.302 1.00 17.89 ? 362 TYR A CA    1 
ATOM   2709 C C     . TYR A 1 371 ? 27.531 36.230 23.352 1.00 17.22 ? 362 TYR A C     1 
ATOM   2710 O O     . TYR A 1 371 ? 26.603 36.662 24.045 1.00 21.06 ? 362 TYR A O     1 
ATOM   2711 C CB    . TYR A 1 371 ? 27.515 34.108 24.691 1.00 19.54 ? 362 TYR A CB    1 
ATOM   2712 C CG    . TYR A 1 371 ? 27.741 32.603 24.765 1.00 19.82 ? 362 TYR A CG    1 
ATOM   2713 C CD1   . TYR A 1 371 ? 26.915 31.714 24.137 1.00 20.01 ? 362 TYR A CD1   1 
ATOM   2714 C CD2   . TYR A 1 371 ? 28.793 32.109 25.499 1.00 21.72 ? 362 TYR A CD2   1 
ATOM   2715 C CE1   . TYR A 1 371 ? 27.105 30.351 24.248 1.00 22.34 ? 362 TYR A CE1   1 
ATOM   2716 C CE2   . TYR A 1 371 ? 29.026 30.750 25.578 1.00 21.45 ? 362 TYR A CE2   1 
ATOM   2717 C CZ    . TYR A 1 371 ? 28.156 29.899 24.967 1.00 20.70 ? 362 TYR A CZ    1 
ATOM   2718 O OH    . TYR A 1 371 ? 28.351 28.526 25.087 1.00 23.32 ? 362 TYR A OH    1 
ATOM   2719 N N     . THR A 1 372 ? 28.299 36.979 22.608 1.00 19.86 ? 363 THR A N     1 
ATOM   2720 C CA    . THR A 1 372 ? 28.130 38.440 22.593 1.00 21.35 ? 363 THR A CA    1 
ATOM   2721 C C     . THR A 1 372 ? 26.989 38.801 21.632 1.00 22.87 ? 363 THR A C     1 
ATOM   2722 O O     . THR A 1 372 ? 26.461 37.947 20.913 1.00 22.56 ? 363 THR A O     1 
ATOM   2723 C CB    . THR A 1 372 ? 29.466 39.063 22.183 1.00 21.91 ? 363 THR A CB    1 
ATOM   2724 O OG1   . THR A 1 372 ? 30.064 38.350 21.077 1.00 23.49 ? 363 THR A OG1   1 
ATOM   2725 C CG2   . THR A 1 372 ? 30.434 39.031 23.372 1.00 22.38 ? 363 THR A CG2   1 
ATOM   2726 N N     . GLN A 1 373 ? 26.590 40.089 21.605 1.00 21.71 ? 364 GLN A N     1 
ATOM   2727 C CA    . GLN A 1 373 ? 25.412 40.506 20.833 1.00 22.38 ? 364 GLN A CA    1 
ATOM   2728 C C     . GLN A 1 373 ? 25.753 41.154 19.501 1.00 22.46 ? 364 GLN A C     1 
ATOM   2729 O O     . GLN A 1 373 ? 24.833 41.433 18.712 1.00 22.37 ? 364 GLN A O     1 
ATOM   2730 C CB    . GLN A 1 373 ? 24.510 41.454 21.650 1.00 20.65 ? 364 GLN A CB    1 
ATOM   2731 C CG    . GLN A 1 373 ? 23.623 40.720 22.639 1.00 21.15 ? 364 GLN A CG    1 
ATOM   2732 C CD    . GLN A 1 373 ? 24.465 39.934 23.621 1.00 24.42 ? 364 GLN A CD    1 
ATOM   2733 O OE1   . GLN A 1 373 ? 25.158 40.524 24.497 1.00 23.36 ? 364 GLN A OE1   1 
ATOM   2734 N NE2   . GLN A 1 373 ? 24.447 38.604 23.482 1.00 22.69 ? 364 GLN A NE2   1 
ATOM   2735 N N     . ASP A 1 374 ? 27.015 41.320 19.188 1.00 21.28 ? 365 ASP A N     1 
ATOM   2736 C CA    . ASP A 1 374 ? 27.375 42.024 17.970 1.00 21.41 ? 365 ASP A CA    1 
ATOM   2737 C C     . ASP A 1 374 ? 26.913 41.231 16.738 1.00 21.93 ? 365 ASP A C     1 
ATOM   2738 O O     . ASP A 1 374 ? 27.135 40.011 16.656 1.00 21.40 ? 365 ASP A O     1 
ATOM   2739 C CB    . ASP A 1 374 ? 28.885 42.275 17.906 1.00 25.02 ? 365 ASP A CB    1 
ATOM   2740 C CG    . ASP A 1 374 ? 29.237 43.354 16.900 1.00 31.24 ? 365 ASP A CG    1 
ATOM   2741 O OD1   . ASP A 1 374 ? 29.242 43.082 15.709 1.00 23.47 ? 365 ASP A OD1   1 
ATOM   2742 O OD2   . ASP A 1 374 ? 29.523 44.520 17.289 1.00 31.39 ? 365 ASP A OD2   1 
ATOM   2743 N N     . PRO A 1 375 ? 26.271 41.867 15.761 1.00 21.92 ? 366 PRO A N     1 
ATOM   2744 C CA    . PRO A 1 375 ? 25.727 41.103 14.637 1.00 22.28 ? 366 PRO A CA    1 
ATOM   2745 C C     . PRO A 1 375 ? 26.796 40.626 13.682 1.00 22.65 ? 366 PRO A C     1 
ATOM   2746 O O     . PRO A 1 375 ? 26.521 39.806 12.783 1.00 25.33 ? 366 PRO A O     1 
ATOM   2747 C CB    . PRO A 1 375 ? 24.767 42.097 13.957 1.00 22.60 ? 366 PRO A CB    1 
ATOM   2748 C CG    . PRO A 1 375 ? 25.309 43.485 14.375 1.00 21.42 ? 366 PRO A CG    1 
ATOM   2749 C CD    . PRO A 1 375 ? 25.857 43.293 15.781 1.00 21.37 ? 366 PRO A CD    1 
ATOM   2750 N N     . VAL A 1 376 ? 28.005 41.169 13.778 1.00 21.10 ? 367 VAL A N     1 
ATOM   2751 C CA    . VAL A 1 376 ? 29.085 40.843 12.864 1.00 20.99 ? 367 VAL A CA    1 
ATOM   2752 C C     . VAL A 1 376 ? 30.271 40.206 13.592 1.00 22.72 ? 367 VAL A C     1 
ATOM   2753 O O     . VAL A 1 376 ? 30.734 39.125 13.226 1.00 22.07 ? 367 VAL A O     1 
ATOM   2754 C CB    . VAL A 1 376 ? 29.543 42.086 12.063 1.00 25.19 ? 367 VAL A CB    1 
ATOM   2755 C CG1   . VAL A 1 376 ? 30.701 41.752 11.200 1.00 25.06 ? 367 VAL A CG1   1 
ATOM   2756 C CG2   . VAL A 1 376 ? 28.389 42.578 11.188 1.00 25.68 ? 367 VAL A CG2   1 
ATOM   2757 N N     . VAL A 1 377 ? 30.775 40.870 14.627 1.00 23.42 ? 368 VAL A N     1 
ATOM   2758 C CA    . VAL A 1 377 ? 32.077 40.512 15.188 1.00 23.00 ? 368 VAL A CA    1 
ATOM   2759 C C     . VAL A 1 377 ? 32.017 39.147 15.884 1.00 21.14 ? 368 VAL A C     1 
ATOM   2760 O O     . VAL A 1 377 ? 31.237 38.946 16.817 1.00 21.79 ? 368 VAL A O     1 
ATOM   2761 C CB    . VAL A 1 377 ? 32.581 41.631 16.116 1.00 21.58 ? 368 VAL A CB    1 
ATOM   2762 C CG1   . VAL A 1 377 ? 33.855 41.167 16.829 1.00 25.46 ? 368 VAL A CG1   1 
ATOM   2763 C CG2   . VAL A 1 377 ? 32.876 42.895 15.304 1.00 24.59 ? 368 VAL A CG2   1 
ATOM   2764 N N     . GLY A 1 378 ? 32.889 38.237 15.461 1.00 21.03 ? 369 GLY A N     1 
ATOM   2765 C CA    . GLY A 1 378 ? 32.898 36.858 15.949 1.00 20.71 ? 369 GLY A CA    1 
ATOM   2766 C C     . GLY A 1 378 ? 31.671 36.078 15.549 1.00 21.55 ? 369 GLY A C     1 
ATOM   2767 O O     . GLY A 1 378 ? 31.384 35.042 16.162 1.00 20.60 ? 369 GLY A O     1 
ATOM   2768 N N     . TYR A 1 379 ? 30.920 36.560 14.557 1.00 20.09 ? 370 TYR A N     1 
ATOM   2769 C CA    . TYR A 1 379 ? 29.674 35.907 14.157 1.00 19.34 ? 370 TYR A CA    1 
ATOM   2770 C C     . TYR A 1 379 ? 29.684 35.639 12.664 1.00 19.04 ? 370 TYR A C     1 
ATOM   2771 O O     . TYR A 1 379 ? 29.676 34.483 12.192 1.00 19.55 ? 370 TYR A O     1 
ATOM   2772 C CB    . TYR A 1 379 ? 28.457 36.740 14.595 1.00 19.98 ? 370 TYR A CB    1 
ATOM   2773 C CG    . TYR A 1 379 ? 27.100 36.052 14.550 1.00 19.11 ? 370 TYR A CG    1 
ATOM   2774 C CD1   . TYR A 1 379 ? 26.903 34.782 15.173 1.00 19.03 ? 370 TYR A CD1   1 
ATOM   2775 C CD2   . TYR A 1 379 ? 26.037 36.608 13.845 1.00 19.52 ? 370 TYR A CD2   1 
ATOM   2776 C CE1   . TYR A 1 379 ? 25.650 34.140 15.100 1.00 18.99 ? 370 TYR A CE1   1 
ATOM   2777 C CE2   . TYR A 1 379 ? 24.778 36.000 13.837 1.00 21.22 ? 370 TYR A CE2   1 
ATOM   2778 C CZ    . TYR A 1 379 ? 24.623 34.772 14.440 1.00 20.21 ? 370 TYR A CZ    1 
ATOM   2779 O OH    . TYR A 1 379 ? 23.432 34.126 14.401 1.00 23.32 ? 370 TYR A OH    1 
ATOM   2780 N N     . THR A 1 380 ? 29.716 36.727 11.872 1.00 18.91 ? 371 THR A N     1 
ATOM   2781 C CA    . THR A 1 380 ? 29.735 36.579 10.421 1.00 20.75 ? 371 THR A CA    1 
ATOM   2782 C C     . THR A 1 380 ? 31.028 37.048 9.779  1.00 20.67 ? 371 THR A C     1 
ATOM   2783 O O     . THR A 1 380 ? 31.148 36.992 8.547  1.00 21.84 ? 371 THR A O     1 
ATOM   2784 C CB    . THR A 1 380 ? 28.557 37.297 9.777  1.00 22.08 ? 371 THR A CB    1 
ATOM   2785 O OG1   . THR A 1 380 ? 28.602 38.694 10.121 1.00 22.39 ? 371 THR A OG1   1 
ATOM   2786 C CG2   . THR A 1 380 ? 27.265 36.704 10.233 1.00 24.90 ? 371 THR A CG2   1 
ATOM   2787 N N     . ASP A 1 381 ? 32.008 37.466 10.587 1.00 20.90 ? 372 ASP A N     1 
ATOM   2788 C CA    . ASP A 1 381 ? 33.258 37.964 10.015 1.00 23.06 ? 372 ASP A CA    1 
ATOM   2789 C C     . ASP A 1 381 ? 34.411 36.973 10.024 1.00 27.28 ? 372 ASP A C     1 
ATOM   2790 O O     . ASP A 1 381 ? 35.544 37.374 9.749  1.00 27.45 ? 372 ASP A O     1 
ATOM   2791 C CB    . ASP A 1 381 ? 33.672 39.305 10.637 1.00 25.40 ? 372 ASP A CB    1 
ATOM   2792 C CG    . ASP A 1 381 ? 33.987 39.198 12.105 1.00 29.38 ? 372 ASP A CG    1 
ATOM   2793 O OD1   . ASP A 1 381 ? 33.792 38.103 12.696 1.00 27.41 ? 372 ASP A OD1   1 
ATOM   2794 O OD2   . ASP A 1 381 ? 34.420 40.209 12.711 1.00 30.36 ? 372 ASP A OD2   1 
ATOM   2795 N N     . TYR A 1 382 ? 34.174 35.692 10.318 1.00 20.55 ? 373 TYR A N     1 
ATOM   2796 C CA    . TYR A 1 382 ? 35.216 34.701 10.074 1.00 21.17 ? 373 TYR A CA    1 
ATOM   2797 C C     . TYR A 1 382 ? 35.291 34.448 8.577  1.00 24.01 ? 373 TYR A C     1 
ATOM   2798 O O     . TYR A 1 382 ? 34.262 34.156 7.935  1.00 25.35 ? 373 TYR A O     1 
ATOM   2799 C CB    . TYR A 1 382 ? 34.851 33.382 10.769 1.00 19.05 ? 373 TYR A CB    1 
ATOM   2800 C CG    . TYR A 1 382 ? 35.006 33.385 12.266 1.00 19.73 ? 373 TYR A CG    1 
ATOM   2801 C CD1   . TYR A 1 382 ? 36.262 33.185 12.873 1.00 20.62 ? 373 TYR A CD1   1 
ATOM   2802 C CD2   . TYR A 1 382 ? 33.907 33.556 13.092 1.00 18.66 ? 373 TYR A CD2   1 
ATOM   2803 C CE1   . TYR A 1 382 ? 36.395 33.146 14.268 1.00 22.64 ? 373 TYR A CE1   1 
ATOM   2804 C CE2   . TYR A 1 382 ? 34.001 33.521 14.488 1.00 19.76 ? 373 TYR A CE2   1 
ATOM   2805 C CZ    . TYR A 1 382 ? 35.270 33.283 15.073 1.00 19.18 ? 373 TYR A CZ    1 
ATOM   2806 O OH    . TYR A 1 382 ? 35.330 33.160 16.396 1.00 21.98 ? 373 TYR A OH    1 
ATOM   2807 N N     . PRO A 1 383 ? 36.464 34.572 7.965  1.00 24.24 ? 374 PRO A N     1 
ATOM   2808 C CA    . PRO A 1 383 ? 36.536 34.470 6.511  1.00 25.49 ? 374 PRO A CA    1 
ATOM   2809 C C     . PRO A 1 383 ? 36.384 33.069 5.966  1.00 25.42 ? 374 PRO A C     1 
ATOM   2810 O O     . PRO A 1 383 ? 36.615 32.055 6.633  1.00 22.48 ? 374 PRO A O     1 
ATOM   2811 C CB    . PRO A 1 383 ? 37.935 35.008 6.178  1.00 27.48 ? 374 PRO A CB    1 
ATOM   2812 C CG    . PRO A 1 383 ? 38.715 34.739 7.441  1.00 31.03 ? 374 PRO A CG    1 
ATOM   2813 C CD    . PRO A 1 383 ? 37.735 35.022 8.559  1.00 25.79 ? 374 PRO A CD    1 
ATOM   2814 N N     . PHE A 1 384 ? 35.976 33.032 4.709  1.00 26.75 ? 375 PHE A N     1 
ATOM   2815 C CA    . PHE A 1 384 ? 36.035 31.851 3.861  1.00 27.12 ? 375 PHE A CA    1 
ATOM   2816 C C     . PHE A 1 384 ? 37.474 31.611 3.409  1.00 27.62 ? 375 PHE A C     1 
ATOM   2817 O O     . PHE A 1 384 ? 38.343 32.496 3.521  1.00 29.53 ? 375 PHE A O     1 
ATOM   2818 C CB    . PHE A 1 384 ? 35.135 32.050 2.634  1.00 24.35 ? 375 PHE A CB    1 
ATOM   2819 C CG    . PHE A 1 384 ? 33.675 32.057 2.973  1.00 29.22 ? 375 PHE A CG    1 
ATOM   2820 C CD1   . PHE A 1 384 ? 33.065 33.200 3.483  1.00 27.95 ? 375 PHE A CD1   1 
ATOM   2821 C CD2   . PHE A 1 384 ? 32.928 30.897 2.830  1.00 25.38 ? 375 PHE A CD2   1 
ATOM   2822 C CE1   . PHE A 1 384 ? 31.720 33.170 3.833  1.00 27.11 ? 375 PHE A CE1   1 
ATOM   2823 C CE2   . PHE A 1 384 ? 31.569 30.881 3.182  1.00 27.66 ? 375 PHE A CE2   1 
ATOM   2824 C CZ    . PHE A 1 384 ? 30.993 32.001 3.686  1.00 23.79 ? 375 PHE A CZ    1 
ATOM   2825 N N     . LEU A 1 385 ? 37.738 30.404 2.925  1.00 27.49 ? 376 LEU A N     1 
ATOM   2826 C CA    . LEU A 1 385 ? 39.027 30.140 2.286  1.00 28.93 ? 376 LEU A CA    1 
ATOM   2827 C C     . LEU A 1 385 ? 39.306 31.191 1.219  1.00 37.45 ? 376 LEU A C     1 
ATOM   2828 O O     . LEU A 1 385 ? 38.399 31.630 0.510  1.00 35.17 ? 376 LEU A O     1 
ATOM   2829 C CB    . LEU A 1 385 ? 39.030 28.773 1.618  1.00 32.12 ? 376 LEU A CB    1 
ATOM   2830 C CG    . LEU A 1 385 ? 39.125 27.502 2.448  1.00 36.83 ? 376 LEU A CG    1 
ATOM   2831 C CD1   . LEU A 1 385 ? 38.816 26.285 1.565  1.00 32.45 ? 376 LEU A CD1   1 
ATOM   2832 C CD2   . LEU A 1 385 ? 40.530 27.410 3.038  1.00 39.08 ? 376 LEU A CD2   1 
ATOM   2833 N N     . GLN A 1 386 ? 40.574 31.571 1.092  1.00 43.24 ? 377 GLN A N     1 
ATOM   2834 C CA    . GLN A 1 386 ? 40.964 32.619 0.147  1.00 42.34 ? 377 GLN A CA    1 
ATOM   2835 C C     . GLN A 1 386 ? 40.539 32.298 -1.285 1.00 43.49 ? 377 GLN A C     1 
ATOM   2836 O O     . GLN A 1 386 ? 40.610 31.145 -1.725 1.00 41.35 ? 377 GLN A O     1 
ATOM   2837 C CB    . GLN A 1 386 ? 42.479 32.839 0.213  1.00 45.86 ? 377 GLN A CB    1 
HETATM 2838 N N1    . FMN B 2 .   ? 23.977 22.298 22.097 1.00 15.03 ? 400 FMN A N1    1 
HETATM 2839 C C2    . FMN B 2 .   ? 22.610 22.280 21.998 1.00 15.66 ? 400 FMN A C2    1 
HETATM 2840 O O2    . FMN B 2 .   ? 22.005 21.195 21.937 1.00 16.25 ? 400 FMN A O2    1 
HETATM 2841 N N3    . FMN B 2 .   ? 21.920 23.450 21.841 1.00 15.61 ? 400 FMN A N3    1 
HETATM 2842 C C4    . FMN B 2 .   ? 22.553 24.686 21.897 1.00 15.69 ? 400 FMN A C4    1 
HETATM 2843 O O4    . FMN B 2 .   ? 21.869 25.724 21.765 1.00 17.52 ? 400 FMN A O4    1 
HETATM 2844 C C4A   . FMN B 2 .   ? 23.955 24.718 22.053 1.00 17.37 ? 400 FMN A C4A   1 
HETATM 2845 N N5    . FMN B 2 .   ? 24.647 25.897 22.099 1.00 18.14 ? 400 FMN A N5    1 
HETATM 2846 C C5A   . FMN B 2 .   ? 26.041 25.890 21.999 1.00 16.96 ? 400 FMN A C5A   1 
HETATM 2847 C C6    . FMN B 2 .   ? 26.691 27.124 21.976 1.00 16.86 ? 400 FMN A C6    1 
HETATM 2848 C C7    . FMN B 2 .   ? 28.052 27.132 21.855 1.00 16.39 ? 400 FMN A C7    1 
HETATM 2849 C C7M   . FMN B 2 .   ? 28.761 28.475 21.823 1.00 18.95 ? 400 FMN A C7M   1 
HETATM 2850 C C8    . FMN B 2 .   ? 28.746 25.938 21.850 1.00 18.10 ? 400 FMN A C8    1 
HETATM 2851 C C8M   . FMN B 2 .   ? 30.262 25.943 21.841 1.00 23.06 ? 400 FMN A C8M   1 
HETATM 2852 C C9    . FMN B 2 .   ? 28.076 24.715 21.913 1.00 17.46 ? 400 FMN A C9    1 
HETATM 2853 C C9A   . FMN B 2 .   ? 26.718 24.680 22.017 1.00 14.62 ? 400 FMN A C9A   1 
HETATM 2854 N N10   . FMN B 2 .   ? 26.033 23.499 22.071 1.00 16.77 ? 400 FMN A N10   1 
HETATM 2855 C C10   . FMN B 2 .   ? 24.642 23.500 22.038 1.00 16.22 ? 400 FMN A C10   1 
HETATM 2856 C "C1'" . FMN B 2 .   ? 26.720 22.177 21.976 1.00 15.26 ? 400 FMN A "C1'" 1 
HETATM 2857 C "C2'" . FMN B 2 .   ? 26.985 21.904 20.494 1.00 16.70 ? 400 FMN A "C2'" 1 
HETATM 2858 O "O2'" . FMN B 2 .   ? 25.789 21.613 19.765 1.00 16.15 ? 400 FMN A "O2'" 1 
HETATM 2859 C "C3'" . FMN B 2 .   ? 27.873 20.712 20.173 1.00 15.53 ? 400 FMN A "C3'" 1 
HETATM 2860 O "O3'" . FMN B 2 .   ? 27.350 19.554 20.826 1.00 17.67 ? 400 FMN A "O3'" 1 
HETATM 2861 C "C4'" . FMN B 2 .   ? 29.305 20.842 20.577 1.00 18.52 ? 400 FMN A "C4'" 1 
HETATM 2862 O "O4'" . FMN B 2 .   ? 29.732 22.188 20.215 1.00 20.27 ? 400 FMN A "O4'" 1 
HETATM 2863 C "C5'" . FMN B 2 .   ? 30.013 19.766 19.740 1.00 19.29 ? 400 FMN A "C5'" 1 
HETATM 2864 O "O5'" . FMN B 2 .   ? 31.366 19.805 20.068 1.00 20.22 ? 400 FMN A "O5'" 1 
HETATM 2865 P P     . FMN B 2 .   ? 32.406 20.608 19.137 1.00 18.62 ? 400 FMN A P     1 
HETATM 2866 O O1P   . FMN B 2 .   ? 32.242 22.058 19.423 1.00 18.26 ? 400 FMN A O1P   1 
HETATM 2867 O O2P   . FMN B 2 .   ? 32.056 20.262 17.712 1.00 18.21 ? 400 FMN A O2P   1 
HETATM 2868 O O3P   . FMN B 2 .   ? 33.770 20.073 19.614 1.00 21.62 ? 400 FMN A O3P   1 
HETATM 2869 C C1    . MPD C 3 .   ? 25.982 26.614 27.317 0.81 40.45 ? 401 MPD A C1    1 
HETATM 2870 C C2    . MPD C 3 .   ? 25.257 25.828 26.240 0.81 27.22 ? 401 MPD A C2    1 
HETATM 2871 O O2    . MPD C 3 .   ? 24.495 24.793 26.877 0.81 25.23 ? 401 MPD A O2    1 
HETATM 2872 C CM    . MPD C 3 .   ? 24.292 26.709 25.465 0.81 26.53 ? 401 MPD A CM    1 
HETATM 2873 C C3    . MPD C 3 .   ? 26.271 25.148 25.322 0.81 33.96 ? 401 MPD A C3    1 
HETATM 2874 C C4    . MPD C 3 .   ? 27.395 24.629 26.171 0.81 46.22 ? 401 MPD A C4    1 
HETATM 2875 O O4    . MPD C 3 .   ? 27.096 23.298 26.571 0.81 48.54 ? 401 MPD A O4    1 
HETATM 2876 C C5    . MPD C 3 .   ? 28.722 24.669 25.476 0.81 38.10 ? 401 MPD A C5    1 
HETATM 2877 C C1    . MPD D 3 .   ? 6.596  14.297 43.272 1.00 34.34 ? 402 MPD A C1    1 
HETATM 2878 C C2    . MPD D 3 .   ? 6.820  15.489 44.209 1.00 54.77 ? 402 MPD A C2    1 
HETATM 2879 O O2    . MPD D 3 .   ? 8.119  15.265 44.746 1.00 65.19 ? 402 MPD A O2    1 
HETATM 2880 C CM    . MPD D 3 .   ? 5.797  15.421 45.348 1.00 59.00 ? 402 MPD A CM    1 
HETATM 2881 C C3    . MPD D 3 .   ? 6.796  16.866 43.488 1.00 53.25 ? 402 MPD A C3    1 
HETATM 2882 C C4    . MPD D 3 .   ? 5.502  17.410 42.865 1.00 46.76 ? 402 MPD A C4    1 
HETATM 2883 O O4    . MPD D 3 .   ? 4.581  17.811 43.875 1.00 48.86 ? 402 MPD A O4    1 
HETATM 2884 C C5    . MPD D 3 .   ? 5.764  18.620 41.979 1.00 45.36 ? 402 MPD A C5    1 
HETATM 2885 C C1    . MPD E 3 .   ? 31.353 22.633 23.359 1.00 34.90 ? 403 MPD A C1    1 
HETATM 2886 C C2    . MPD E 3 .   ? 32.088 21.756 24.387 1.00 59.10 ? 403 MPD A C2    1 
HETATM 2887 O O2    . MPD E 3 .   ? 31.178 21.552 25.465 1.00 55.00 ? 403 MPD A O2    1 
HETATM 2888 C CM    . MPD E 3 .   ? 33.325 22.508 24.899 1.00 54.40 ? 403 MPD A CM    1 
HETATM 2889 C C3    . MPD E 3 .   ? 32.469 20.402 23.741 1.00 44.76 ? 403 MPD A C3    1 
HETATM 2890 C C4    . MPD E 3 .   ? 33.309 19.444 24.586 1.00 61.13 ? 403 MPD A C4    1 
HETATM 2891 O O4    . MPD E 3 .   ? 32.482 18.973 25.649 1.00 64.21 ? 403 MPD A O4    1 
HETATM 2892 C C5    . MPD E 3 .   ? 33.860 18.272 23.774 1.00 43.21 ? 403 MPD A C5    1 
HETATM 2893 S S     . SO4 F 4 .   ? 40.008 33.530 22.485 1.00 78.74 ? 404 SO4 A S     1 
HETATM 2894 O O1    . SO4 F 4 .   ? 40.921 33.973 21.472 1.00 57.80 ? 404 SO4 A O1    1 
HETATM 2895 O O2    . SO4 F 4 .   ? 39.708 32.139 22.286 1.00 49.19 ? 404 SO4 A O2    1 
HETATM 2896 O O3    . SO4 F 4 .   ? 38.796 34.302 22.415 1.00 48.94 ? 404 SO4 A O3    1 
HETATM 2897 O O4    . SO4 F 4 .   ? 40.606 33.706 23.776 1.00 75.90 ? 404 SO4 A O4    1 
HETATM 2898 O OH2   . 1PE G 5 .   ? 27.945 31.623 -4.186 1.00 57.23 ? 405 1PE A OH2   1 
HETATM 2899 C C12   . 1PE G 5 .   ? 29.132 31.033 -4.673 1.00 70.65 ? 405 1PE A C12   1 
HETATM 2900 C C22   . 1PE G 5 .   ? 29.672 29.994 -3.746 1.00 61.24 ? 405 1PE A C22   1 
HETATM 2901 O OH3   . 1PE G 5 .   ? 30.253 30.610 -2.603 1.00 68.61 ? 405 1PE A OH3   1 
HETATM 2902 C C13   . 1PE G 5 .   ? 29.288 32.134 -1.049 1.00 54.61 ? 405 1PE A C13   1 
HETATM 2903 C C23   . 1PE G 5 .   ? 29.351 30.712 -1.507 1.00 65.57 ? 405 1PE A C23   1 
HETATM 2904 O OH4   . 1PE G 5 .   ? 30.035 32.299 0.153  1.00 68.23 ? 405 1PE A OH4   1 
HETATM 2905 C C14   . 1PE G 5 .   ? 32.311 31.760 -0.293 1.00 52.40 ? 405 1PE A C14   1 
HETATM 2906 C C24   . 1PE G 5 .   ? 31.322 32.859 -0.074 1.00 38.43 ? 405 1PE A C24   1 
HETATM 2907 O OH5   . 1PE G 5 .   ? 33.310 32.167 -1.217 1.00 67.22 ? 405 1PE A OH5   1 
HETATM 2908 C C15   . 1PE G 5 .   ? 35.524 32.948 -0.757 1.00 50.30 ? 405 1PE A C15   1 
HETATM 2909 C C25   . 1PE G 5 .   ? 34.064 33.280 -0.760 1.00 54.26 ? 405 1PE A C25   1 
HETATM 2910 O OH6   . 1PE G 5 .   ? 35.807 31.967 -1.747 1.00 70.27 ? 405 1PE A OH6   1 
HETATM 2911 C C16   . 1PE G 5 .   ? 35.670 29.635 -2.192 1.00 57.43 ? 405 1PE A C16   1 
HETATM 2912 C C26   . 1PE G 5 .   ? 36.066 30.677 -1.205 1.00 49.69 ? 405 1PE A C26   1 
HETATM 2913 O OH7   . 1PE G 5 .   ? 34.355 29.167 -1.968 1.00 64.46 ? 405 1PE A OH7   1 
HETATM 2914 O O     . HOH H 6 .   ? 6.853  10.405 9.138  1.00 35.85 ? 501 HOH A O     1 
HETATM 2915 O O     . HOH H 6 .   ? 7.507  26.565 31.114 1.00 32.79 ? 502 HOH A O     1 
HETATM 2916 O O     . HOH H 6 .   ? 14.123 44.161 19.431 1.00 50.75 ? 503 HOH A O     1 
HETATM 2917 O O     . HOH H 6 .   ? 9.868  0.501  27.804 1.00 42.96 ? 504 HOH A O     1 
HETATM 2918 O O     . HOH H 6 .   ? 14.548 39.405 11.193 1.00 41.16 ? 505 HOH A O     1 
HETATM 2919 O O     . HOH H 6 .   ? 23.423 28.155 31.753 1.00 28.37 ? 506 HOH A O     1 
HETATM 2920 O O     . HOH H 6 .   ? 43.143 17.472 8.690  1.00 41.85 ? 507 HOH A O     1 
HETATM 2921 O O     . HOH H 6 .   ? 12.359 36.691 27.027 1.00 40.71 ? 508 HOH A O     1 
HETATM 2922 O O     . HOH H 6 .   ? 10.424 29.495 4.695  1.00 34.88 ? 509 HOH A O     1 
HETATM 2923 O O     . HOH H 6 .   ? 20.165 30.099 -4.739 1.00 30.72 ? 510 HOH A O     1 
HETATM 2924 O O     . HOH H 6 .   ? 30.614 27.547 25.740 1.00 45.81 ? 511 HOH A O     1 
HETATM 2925 O O     . HOH H 6 .   ? -2.094 26.070 31.451 1.00 44.05 ? 512 HOH A O     1 
HETATM 2926 O O     . HOH H 6 .   ? 38.694 16.187 19.974 1.00 39.58 ? 513 HOH A O     1 
HETATM 2927 O O     . HOH H 6 .   ? 26.063 39.113 38.153 1.00 41.11 ? 514 HOH A O     1 
HETATM 2928 O O     . HOH H 6 .   ? 30.846 40.083 19.333 1.00 26.23 ? 515 HOH A O     1 
HETATM 2929 O O     . HOH H 6 .   ? 14.187 23.601 47.215 1.00 37.45 ? 516 HOH A O     1 
HETATM 2930 O O     . HOH H 6 .   ? 21.773 2.875  38.975 1.00 40.58 ? 517 HOH A O     1 
HETATM 2931 O O     . HOH H 6 .   ? 20.695 32.243 -0.210 1.00 30.62 ? 518 HOH A O     1 
HETATM 2932 O O     . HOH H 6 .   ? 2.685  22.986 38.709 1.00 26.49 ? 519 HOH A O     1 
HETATM 2933 O O     . HOH H 6 .   ? 33.199 37.943 26.009 1.00 47.48 ? 520 HOH A O     1 
HETATM 2934 O O     . HOH H 6 .   ? 13.893 21.630 1.984  1.00 34.01 ? 521 HOH A O     1 
HETATM 2935 O O     . HOH H 6 .   ? 5.716  3.316  36.080 1.00 43.61 ? 522 HOH A O     1 
HETATM 2936 O O     . HOH H 6 .   ? -0.844 12.946 37.399 1.00 25.74 ? 523 HOH A O     1 
HETATM 2937 O O     . HOH H 6 .   ? 2.033  36.423 11.038 1.00 52.64 ? 524 HOH A O     1 
HETATM 2938 O O     . HOH H 6 .   ? 34.793 28.159 0.407  1.00 36.69 ? 525 HOH A O     1 
HETATM 2939 O O     . HOH H 6 .   ? 19.689 4.968  36.072 1.00 35.69 ? 526 HOH A O     1 
HETATM 2940 O O     . HOH H 6 .   ? 19.438 10.075 -0.536 1.00 46.07 ? 527 HOH A O     1 
HETATM 2941 O O     . HOH H 6 .   ? 36.558 40.572 14.204 1.00 42.41 ? 528 HOH A O     1 
HETATM 2942 O O     . HOH H 6 .   ? 33.237 33.670 17.910 1.00 21.67 ? 529 HOH A O     1 
HETATM 2943 O O     . HOH H 6 .   ? 31.829 45.795 17.260 1.00 28.81 ? 530 HOH A O     1 
HETATM 2944 O O     . HOH H 6 .   ? 23.195 31.665 15.634 1.00 24.29 ? 531 HOH A O     1 
HETATM 2945 O O     . HOH H 6 .   ? 11.827 35.326 2.795  1.00 39.22 ? 532 HOH A O     1 
HETATM 2946 O O     . HOH H 6 .   ? 38.279 14.784 1.393  1.00 36.89 ? 533 HOH A O     1 
HETATM 2947 O O     . HOH H 6 .   ? 16.352 4.089  38.620 1.00 37.82 ? 534 HOH A O     1 
HETATM 2948 O O     . HOH H 6 .   ? 25.886 6.488  0.369  1.00 44.73 ? 535 HOH A O     1 
HETATM 2949 O O     . HOH H 6 .   ? 28.803 27.673 2.663  1.00 37.52 ? 536 HOH A O     1 
HETATM 2950 O O     . HOH H 6 .   ? 30.943 37.455 29.786 1.00 46.51 ? 537 HOH A O     1 
HETATM 2951 O O     . HOH H 6 .   ? 27.186 13.262 -2.431 1.00 43.04 ? 538 HOH A O     1 
HETATM 2952 O O     . HOH H 6 .   ? 24.552 43.004 25.221 1.00 25.19 ? 539 HOH A O     1 
HETATM 2953 O O     . HOH H 6 .   ? 41.560 14.404 15.470 1.00 37.10 ? 540 HOH A O     1 
HETATM 2954 O O     . HOH H 6 .   ? 23.651 16.215 30.199 1.00 29.10 ? 541 HOH A O     1 
HETATM 2955 O O     . HOH H 6 .   ? 3.390  25.664 29.781 1.00 39.17 ? 542 HOH A O     1 
HETATM 2956 O O     . HOH H 6 .   ? 22.913 28.072 42.619 1.00 23.72 ? 543 HOH A O     1 
HETATM 2957 O O     . HOH H 6 .   ? 2.144  14.539 40.977 1.00 31.51 ? 544 HOH A O     1 
HETATM 2958 O O     . HOH H 6 .   ? 26.095 22.990 5.223  1.00 21.99 ? 545 HOH A O     1 
HETATM 2959 O O     . HOH H 6 .   ? 37.670 31.724 9.054  1.00 25.68 ? 546 HOH A O     1 
HETATM 2960 O O     . HOH H 6 .   ? 7.498  29.795 38.930 1.00 34.58 ? 547 HOH A O     1 
HETATM 2961 O O     . HOH H 6 .   ? 20.136 13.674 28.007 1.00 19.54 ? 548 HOH A O     1 
HETATM 2962 O O     . HOH H 6 .   ? 28.429 4.897  9.099  1.00 28.34 ? 549 HOH A O     1 
HETATM 2963 O O     . HOH H 6 .   ? 24.490 28.587 15.728 1.00 19.69 ? 550 HOH A O     1 
HETATM 2964 O O     . HOH H 6 .   ? 15.423 28.555 25.611 1.00 21.15 ? 551 HOH A O     1 
HETATM 2965 O O     . HOH H 6 .   ? 7.818  2.213  37.128 1.00 32.04 ? 552 HOH A O     1 
HETATM 2966 O O     . HOH H 6 .   ? 16.696 9.187  9.029  1.00 23.43 ? 553 HOH A O     1 
HETATM 2967 O O     . HOH H 6 .   ? 2.921  5.195  35.645 1.00 45.56 ? 554 HOH A O     1 
HETATM 2968 O O     . HOH H 6 .   ? 20.934 28.645 31.074 1.00 24.25 ? 555 HOH A O     1 
HETATM 2969 O O     . HOH H 6 .   ? 31.844 2.228  27.821 1.00 46.02 ? 556 HOH A O     1 
HETATM 2970 O O     . HOH H 6 .   ? 35.701 20.132 17.761 1.00 22.82 ? 557 HOH A O     1 
HETATM 2971 O O     . HOH H 6 .   ? 32.861 31.396 25.434 1.00 48.12 ? 558 HOH A O     1 
HETATM 2972 O O     . HOH H 6 .   ? 34.117 2.068  5.691  1.00 51.21 ? 559 HOH A O     1 
HETATM 2973 O O     . HOH H 6 .   ? 25.675 39.982 10.243 1.00 32.33 ? 560 HOH A O     1 
HETATM 2974 O O     . HOH H 6 .   ? 16.300 15.830 46.774 1.00 29.48 ? 561 HOH A O     1 
HETATM 2975 O O     . HOH H 6 .   ? 22.585 20.673 42.386 1.00 41.92 ? 562 HOH A O     1 
HETATM 2976 O O     . HOH H 6 .   ? 15.558 7.388  40.485 1.00 34.16 ? 563 HOH A O     1 
HETATM 2977 O O     . HOH H 6 .   ? 21.142 32.054 20.345 1.00 19.84 ? 564 HOH A O     1 
HETATM 2978 O O     . HOH H 6 .   ? 22.978 3.189  9.299  1.00 36.46 ? 565 HOH A O     1 
HETATM 2979 O O     . HOH H 6 .   ? 21.399 16.035 -1.946 1.00 37.16 ? 566 HOH A O     1 
HETATM 2980 O O     . HOH H 6 .   ? 17.042 17.427 42.888 1.00 30.27 ? 567 HOH A O     1 
HETATM 2981 O O     . HOH H 6 .   ? 0.014  18.341 23.729 1.00 37.13 ? 568 HOH A O     1 
HETATM 2982 O O     . HOH H 6 .   ? 8.922  30.302 35.188 1.00 32.68 ? 569 HOH A O     1 
HETATM 2983 O O     . HOH H 6 .   ? 26.019 40.044 27.015 1.00 37.03 ? 570 HOH A O     1 
HETATM 2984 O O     . HOH H 6 .   ? 7.016  26.002 28.579 1.00 23.90 ? 571 HOH A O     1 
HETATM 2985 O O     . HOH H 6 .   ? 22.034 34.072 17.576 1.00 19.46 ? 572 HOH A O     1 
HETATM 2986 O O     . HOH H 6 .   ? 34.450 42.686 11.622 1.00 33.63 ? 573 HOH A O     1 
HETATM 2987 O O     . HOH H 6 .   ? 20.440 0.007  14.419 1.00 31.68 ? 574 HOH A O     1 
HETATM 2988 O O     . HOH H 6 .   ? 13.668 31.136 43.006 1.00 29.27 ? 575 HOH A O     1 
HETATM 2989 O O     . HOH H 6 .   ? 9.853  42.009 13.971 1.00 49.03 ? 576 HOH A O     1 
HETATM 2990 O O     . HOH H 6 .   ? 15.618 38.786 29.957 1.00 33.59 ? 577 HOH A O     1 
HETATM 2991 O O     . HOH H 6 .   ? 14.126 21.289 24.886 1.00 18.07 ? 578 HOH A O     1 
HETATM 2992 O O     . HOH H 6 .   ? 14.068 9.624  40.220 1.00 32.24 ? 579 HOH A O     1 
HETATM 2993 O O     . HOH H 6 .   ? 44.123 24.210 11.877 1.00 21.29 ? 580 HOH A O     1 
HETATM 2994 O O     . HOH H 6 .   ? 25.898 5.378  7.413  1.00 25.21 ? 581 HOH A O     1 
HETATM 2995 O O     . HOH H 6 .   ? 31.632 17.601 17.384 1.00 19.75 ? 582 HOH A O     1 
HETATM 2996 O O     . HOH H 6 .   ? 27.702 8.459  36.360 1.00 42.46 ? 583 HOH A O     1 
HETATM 2997 O O     . HOH H 6 .   ? 13.396 11.860 7.868  1.00 30.73 ? 584 HOH A O     1 
HETATM 2998 O O     . HOH H 6 .   ? 14.440 46.521 22.034 1.00 32.47 ? 585 HOH A O     1 
HETATM 2999 O O     . HOH H 6 .   ? 40.756 29.261 20.417 1.00 33.19 ? 586 HOH A O     1 
HETATM 3000 O O     . HOH H 6 .   ? 5.676  27.605 31.045 1.00 41.26 ? 587 HOH A O     1 
HETATM 3001 O O     . HOH H 6 .   ? 12.301 32.420 29.818 1.00 21.64 ? 588 HOH A O     1 
HETATM 3002 O O     . HOH H 6 .   ? 0.216  12.428 39.920 1.00 32.70 ? 589 HOH A O     1 
HETATM 3003 O O     . HOH H 6 .   ? 35.842 8.819  15.771 1.00 26.26 ? 590 HOH A O     1 
HETATM 3004 O O     . HOH H 6 .   ? 23.019 32.425 30.270 1.00 22.97 ? 591 HOH A O     1 
HETATM 3005 O O     . HOH H 6 .   ? 11.821 34.607 41.611 1.00 40.11 ? 592 HOH A O     1 
HETATM 3006 O O     . HOH H 6 .   ? 20.052 29.810 21.438 1.00 17.17 ? 593 HOH A O     1 
HETATM 3007 O O     . HOH H 6 .   ? 26.661 27.255 34.064 1.00 30.10 ? 594 HOH A O     1 
HETATM 3008 O O     . HOH H 6 .   ? 10.666 16.952 42.745 1.00 25.99 ? 595 HOH A O     1 
HETATM 3009 O O     . HOH H 6 .   ? 0.112  10.243 34.339 1.00 34.80 ? 596 HOH A O     1 
HETATM 3010 O O     . HOH H 6 .   ? -5.944 23.764 30.501 1.00 31.27 ? 597 HOH A O     1 
HETATM 3011 O O     . HOH H 6 .   ? 18.595 26.214 39.444 1.00 19.69 ? 598 HOH A O     1 
HETATM 3012 O O     . HOH H 6 .   ? 16.353 23.817 -1.394 1.00 33.52 ? 599 HOH A O     1 
HETATM 3013 O O     . HOH H 6 .   ? 14.207 29.588 -0.657 1.00 30.55 ? 600 HOH A O     1 
HETATM 3014 O O     . HOH H 6 .   ? 20.404 38.869 6.447  1.00 33.36 ? 601 HOH A O     1 
HETATM 3015 O O     . HOH H 6 .   ? 33.823 21.496 16.028 1.00 19.23 ? 602 HOH A O     1 
HETATM 3016 O O     . HOH H 6 .   ? 21.439 11.834 -0.928 1.00 34.90 ? 603 HOH A O     1 
HETATM 3017 O O     . HOH H 6 .   ? 39.366 24.108 21.999 1.00 32.65 ? 604 HOH A O     1 
HETATM 3018 O O     . HOH H 6 .   ? 16.275 22.076 0.940  1.00 28.49 ? 605 HOH A O     1 
HETATM 3019 O O     . HOH H 6 .   ? 11.658 27.947 2.316  1.00 33.99 ? 606 HOH A O     1 
HETATM 3020 O O     . HOH H 6 .   ? 35.760 36.582 13.853 1.00 31.87 ? 607 HOH A O     1 
HETATM 3021 O O     . HOH H 6 .   ? 30.310 44.940 13.993 1.00 35.62 ? 608 HOH A O     1 
HETATM 3022 O O     . HOH H 6 .   ? 38.802 35.010 2.513  1.00 43.54 ? 609 HOH A O     1 
HETATM 3023 O O     . HOH H 6 .   ? 25.971 21.172 7.169  1.00 19.51 ? 610 HOH A O     1 
HETATM 3024 O O     . HOH H 6 .   ? 16.108 7.684  12.455 1.00 22.32 ? 611 HOH A O     1 
HETATM 3025 O O     . HOH H 6 .   ? 12.861 18.934 45.294 1.00 27.83 ? 612 HOH A O     1 
HETATM 3026 O O     . HOH H 6 .   ? 28.067 18.719 37.373 1.00 45.07 ? 613 HOH A O     1 
HETATM 3027 O O     . HOH H 6 .   ? 10.597 20.227 3.992  1.00 34.57 ? 614 HOH A O     1 
HETATM 3028 O O     . HOH H 6 .   ? 24.814 26.433 30.234 1.00 29.53 ? 615 HOH A O     1 
HETATM 3029 O O     . HOH H 6 .   ? 40.949 20.007 7.158  1.00 26.61 ? 616 HOH A O     1 
HETATM 3030 O O     . HOH H 6 .   ? 2.127  19.124 10.367 1.00 38.94 ? 617 HOH A O     1 
HETATM 3031 O O     . HOH H 6 .   ? -0.886 18.615 12.919 1.00 34.52 ? 618 HOH A O     1 
HETATM 3032 O O     . HOH H 6 .   ? 12.193 12.572 30.452 1.00 19.91 ? 619 HOH A O     1 
HETATM 3033 O O     . HOH H 6 .   ? 12.291 39.357 34.946 1.00 41.22 ? 620 HOH A O     1 
HETATM 3034 O O     . HOH H 6 .   ? 19.581 33.963 41.748 1.00 31.68 ? 621 HOH A O     1 
HETATM 3035 O O     . HOH H 6 .   ? 11.519 1.408  15.715 1.00 26.60 ? 622 HOH A O     1 
HETATM 3036 O O     . HOH H 6 .   ? 7.901  38.134 19.298 1.00 31.06 ? 623 HOH A O     1 
HETATM 3037 O O     . HOH H 6 .   ? 29.957 25.010 5.161  1.00 21.98 ? 624 HOH A O     1 
HETATM 3038 O O     . HOH H 6 .   ? 40.324 32.538 13.190 1.00 23.25 ? 625 HOH A O     1 
HETATM 3039 O O     . HOH H 6 .   ? 8.224  36.617 6.672  1.00 29.45 ? 626 HOH A O     1 
HETATM 3040 O O     . HOH H 6 .   ? 7.966  23.420 6.496  1.00 29.93 ? 627 HOH A O     1 
HETATM 3041 O O     . HOH H 6 .   ? 44.517 28.228 9.502  1.00 23.71 ? 628 HOH A O     1 
HETATM 3042 O O     . HOH H 6 .   ? 17.399 0.025  24.200 1.00 32.30 ? 629 HOH A O     1 
HETATM 3043 O O     . HOH H 6 .   ? 31.760 33.789 9.378  1.00 22.42 ? 630 HOH A O     1 
HETATM 3044 O O     . HOH H 6 .   ? 25.473 30.368 46.177 1.00 38.10 ? 631 HOH A O     1 
HETATM 3045 O O     . HOH H 6 .   ? 13.594 -0.947 12.254 1.00 47.75 ? 632 HOH A O     1 
HETATM 3046 O O     . HOH H 6 .   ? 17.166 -1.278 21.600 1.00 33.10 ? 633 HOH A O     1 
HETATM 3047 O O     . HOH H 6 .   ? -3.569 17.791 31.256 1.00 23.12 ? 634 HOH A O     1 
HETATM 3048 O O     . HOH H 6 .   ? 1.561  27.169 13.524 1.00 40.86 ? 635 HOH A O     1 
HETATM 3049 O O     . HOH H 6 .   ? 0.919  25.328 26.840 1.00 36.30 ? 636 HOH A O     1 
HETATM 3050 O O     . HOH H 6 .   ? 12.639 2.403  28.228 1.00 31.19 ? 637 HOH A O     1 
HETATM 3051 O O     . HOH H 6 .   ? 31.108 8.178  16.740 1.00 33.03 ? 638 HOH A O     1 
HETATM 3052 O O     . HOH H 6 .   ? -0.088 17.674 26.448 1.00 26.35 ? 639 HOH A O     1 
HETATM 3053 O O     . HOH H 6 .   ? 20.351 21.124 35.662 1.00 18.85 ? 640 HOH A O     1 
HETATM 3054 O O     . HOH H 6 .   ? 19.245 5.848  5.098  1.00 41.24 ? 641 HOH A O     1 
HETATM 3055 O O     . HOH H 6 .   ? 27.935 19.055 23.512 1.00 27.17 ? 642 HOH A O     1 
HETATM 3056 O O     . HOH H 6 .   ? 19.804 -0.906 30.674 1.00 29.56 ? 643 HOH A O     1 
HETATM 3057 O O     . HOH H 6 .   ? 2.188  24.186 10.839 1.00 29.07 ? 644 HOH A O     1 
HETATM 3058 O O     . HOH H 6 .   ? 26.262 11.326 26.335 1.00 21.88 ? 645 HOH A O     1 
HETATM 3059 O O     . HOH H 6 .   ? 24.850 30.544 31.210 1.00 24.63 ? 646 HOH A O     1 
HETATM 3060 O O     . HOH H 6 .   ? 42.377 30.963 3.146  1.00 42.71 ? 647 HOH A O     1 
HETATM 3061 O O     . HOH H 6 .   ? 23.483 -1.923 21.903 1.00 22.15 ? 648 HOH A O     1 
HETATM 3062 O O     . HOH H 6 .   ? 24.703 -1.182 33.802 1.00 43.10 ? 649 HOH A O     1 
HETATM 3063 O O     . HOH H 6 .   ? 23.642 26.052 15.014 1.00 18.74 ? 650 HOH A O     1 
HETATM 3064 O O     . HOH H 6 .   ? 23.517 41.180 36.209 1.00 43.05 ? 651 HOH A O     1 
HETATM 3065 O O     . HOH H 6 .   ? 30.427 32.458 14.013 1.00 18.61 ? 652 HOH A O     1 
HETATM 3066 O O     . HOH H 6 .   ? 8.562  5.775  29.773 1.00 33.93 ? 653 HOH A O     1 
HETATM 3067 O O     . HOH H 6 .   ? 12.956 9.990  42.942 1.00 38.63 ? 654 HOH A O     1 
HETATM 3068 O O     . HOH H 6 .   ? 37.945 38.565 10.598 1.00 48.81 ? 655 HOH A O     1 
HETATM 3069 O O     . HOH H 6 .   ? 29.311 6.259  17.895 1.00 33.44 ? 656 HOH A O     1 
HETATM 3070 O O     . HOH H 6 .   ? 21.390 -3.334 15.808 1.00 31.97 ? 657 HOH A O     1 
HETATM 3071 O O     . HOH H 6 .   ? 25.420 11.321 33.566 1.00 31.31 ? 658 HOH A O     1 
HETATM 3072 O O     . HOH H 6 .   ? 17.863 42.529 12.114 1.00 37.99 ? 659 HOH A O     1 
HETATM 3073 O O     . HOH H 6 .   ? 4.069  28.096 23.538 1.00 39.84 ? 660 HOH A O     1 
HETATM 3074 O O     . HOH H 6 .   ? 23.062 23.025 25.076 1.00 19.90 ? 661 HOH A O     1 
HETATM 3075 O O     . HOH H 6 .   ? 35.910 37.378 17.547 1.00 32.96 ? 662 HOH A O     1 
HETATM 3076 O O     . HOH H 6 .   ? 24.751 29.223 40.841 1.00 25.47 ? 663 HOH A O     1 
HETATM 3077 O O     . HOH H 6 .   ? 21.706 4.036  14.977 1.00 21.04 ? 664 HOH A O     1 
HETATM 3078 O O     . HOH H 6 .   ? 17.915 5.749  40.469 1.00 33.64 ? 665 HOH A O     1 
HETATM 3079 O O     . HOH H 6 .   ? 29.215 45.158 20.024 1.00 32.84 ? 666 HOH A O     1 
HETATM 3080 O O     . HOH H 6 .   ? 20.902 3.034  10.946 1.00 39.75 ? 667 HOH A O     1 
HETATM 3081 O O     . HOH H 6 .   ? 2.226  13.465 24.464 1.00 25.62 ? 668 HOH A O     1 
HETATM 3082 O O     . HOH H 6 .   ? 16.768 34.431 40.106 1.00 27.47 ? 669 HOH A O     1 
HETATM 3083 O O     . HOH H 6 .   ? 7.581  7.093  41.717 1.00 34.51 ? 670 HOH A O     1 
HETATM 3084 O O     . HOH H 6 .   ? 5.257  26.201 32.609 1.00 38.05 ? 671 HOH A O     1 
HETATM 3085 O O     . HOH H 6 .   ? 31.000 35.177 24.728 1.00 25.21 ? 672 HOH A O     1 
HETATM 3086 O O     . HOH H 6 .   ? 35.715 1.471  22.253 1.00 37.63 ? 673 HOH A O     1 
HETATM 3087 O O     . HOH H 6 .   ? 22.510 40.837 16.805 1.00 23.82 ? 674 HOH A O     1 
HETATM 3088 O O     . HOH H 6 .   ? 9.680  24.033 3.678  1.00 47.61 ? 675 HOH A O     1 
HETATM 3089 O O     . HOH H 6 .   ? 17.936 0.404  30.108 1.00 32.22 ? 676 HOH A O     1 
HETATM 3090 O O     . HOH H 6 .   ? 33.086 36.393 6.561  1.00 37.34 ? 677 HOH A O     1 
HETATM 3091 O O     . HOH H 6 .   ? 13.008 12.109 46.609 1.00 35.66 ? 678 HOH A O     1 
HETATM 3092 O O     . HOH H 6 .   ? 1.862  15.044 29.365 1.00 27.24 ? 679 HOH A O     1 
HETATM 3093 O O     . HOH H 6 .   ? 32.400 28.470 -0.019 1.00 47.60 ? 680 HOH A O     1 
HETATM 3094 O O     . HOH H 6 .   ? 11.897 38.264 41.070 1.00 47.88 ? 681 HOH A O     1 
HETATM 3095 O O     . HOH H 6 .   ? 22.533 42.034 26.756 1.00 22.49 ? 682 HOH A O     1 
HETATM 3096 O O     . HOH H 6 .   ? 14.368 35.858 28.809 1.00 26.52 ? 683 HOH A O     1 
HETATM 3097 O O     . HOH H 6 .   ? 24.978 17.293 6.213  1.00 19.47 ? 684 HOH A O     1 
HETATM 3098 O O     . HOH H 6 .   ? 31.560 5.051  18.944 1.00 30.87 ? 685 HOH A O     1 
HETATM 3099 O O     . HOH H 6 .   ? 4.357  23.958 40.955 1.00 35.62 ? 686 HOH A O     1 
HETATM 3100 O O     . HOH H 6 .   ? 33.823 6.987  16.180 1.00 35.58 ? 687 HOH A O     1 
HETATM 3101 O O     . HOH H 6 .   ? 29.842 39.994 7.889  1.00 41.71 ? 688 HOH A O     1 
HETATM 3102 O O     . HOH H 6 .   ? 12.163 27.585 33.415 1.00 19.95 ? 689 HOH A O     1 
HETATM 3103 O O     . HOH H 6 .   ? 27.382 37.720 26.599 1.00 27.04 ? 690 HOH A O     1 
HETATM 3104 O O     . HOH H 6 .   ? 17.041 38.203 26.336 1.00 22.10 ? 691 HOH A O     1 
HETATM 3105 O O     . HOH H 6 .   ? 16.195 35.617 26.826 1.00 20.29 ? 692 HOH A O     1 
HETATM 3106 O O     . HOH H 6 .   ? 15.267 20.459 27.702 1.00 19.72 ? 693 HOH A O     1 
HETATM 3107 O O     . HOH H 6 .   ? 42.503 29.643 6.407  1.00 39.18 ? 694 HOH A O     1 
HETATM 3108 O O     . HOH H 6 .   ? 35.611 10.046 18.456 1.00 29.78 ? 695 HOH A O     1 
HETATM 3109 O O     . HOH H 6 .   ? 40.211 18.582 11.974 1.00 32.09 ? 696 HOH A O     1 
HETATM 3110 O O     . HOH H 6 .   ? 10.213 37.697 24.080 1.00 40.09 ? 697 HOH A O     1 
HETATM 3111 O O     . HOH H 6 .   ? 15.065 37.304 10.032 1.00 31.62 ? 698 HOH A O     1 
HETATM 3112 O O     . HOH H 6 .   ? 17.373 18.774 28.462 1.00 18.27 ? 699 HOH A O     1 
HETATM 3113 O O     . HOH H 6 .   ? 40.346 9.372  9.849  1.00 44.49 ? 700 HOH A O     1 
HETATM 3114 O O     . HOH H 6 .   ? 17.750 29.704 26.631 1.00 18.66 ? 701 HOH A O     1 
HETATM 3115 O O     . HOH H 6 .   ? 9.767  11.925 33.178 1.00 18.87 ? 702 HOH A O     1 
HETATM 3116 O O     . HOH H 6 .   ? 10.151 37.986 21.136 1.00 33.66 ? 703 HOH A O     1 
HETATM 3117 O O     . HOH H 6 .   ? 5.799  14.586 7.937  1.00 37.67 ? 704 HOH A O     1 
HETATM 3118 O O     . HOH H 6 .   ? 9.969  35.778 28.046 1.00 35.98 ? 705 HOH A O     1 
HETATM 3119 O O     . HOH H 6 .   ? 24.418 -0.877 14.150 1.00 47.05 ? 706 HOH A O     1 
HETATM 3120 O O     . HOH H 6 .   ? 30.193 17.497 24.105 1.00 38.97 ? 707 HOH A O     1 
HETATM 3121 O O     . HOH H 6 .   ? 11.590 -2.320 12.900 1.00 49.55 ? 708 HOH A O     1 
HETATM 3122 O O     . HOH H 6 .   ? 4.711  9.886  11.949 1.00 30.07 ? 709 HOH A O     1 
HETATM 3123 O O     . HOH H 6 .   ? 11.798 12.081 -0.225 1.00 42.08 ? 710 HOH A O     1 
HETATM 3124 O O     . HOH H 6 .   ? 8.104  23.659 44.023 1.00 38.65 ? 711 HOH A O     1 
HETATM 3125 O O     . HOH H 6 .   ? 3.578  37.993 17.335 1.00 34.43 ? 712 HOH A O     1 
HETATM 3126 O O     . HOH H 6 .   ? 14.409 35.844 2.971  1.00 31.93 ? 713 HOH A O     1 
HETATM 3127 O O     . HOH H 6 .   ? 27.559 20.354 -1.364 1.00 43.78 ? 714 HOH A O     1 
HETATM 3128 O O     . HOH H 6 .   ? 11.378 1.230  34.833 1.00 25.17 ? 715 HOH A O     1 
HETATM 3129 O O     . HOH H 6 .   ? 36.260 38.887 7.348  1.00 52.45 ? 716 HOH A O     1 
HETATM 3130 O O     . HOH H 6 .   ? 15.103 44.317 14.501 1.00 52.69 ? 717 HOH A O     1 
HETATM 3131 O O     . HOH H 6 .   ? 21.088 18.998 41.378 1.00 33.79 ? 718 HOH A O     1 
HETATM 3132 O O     . HOH H 6 .   ? 14.410 1.666  37.202 1.00 32.66 ? 719 HOH A O     1 
HETATM 3133 O O     . HOH H 6 .   ? 27.943 42.099 23.280 1.00 34.24 ? 720 HOH A O     1 
HETATM 3134 O O     . HOH H 6 .   ? 4.571  18.401 8.822  1.00 33.12 ? 721 HOH A O     1 
HETATM 3135 O O     . HOH H 6 .   ? 40.255 31.741 5.705  1.00 35.80 ? 722 HOH A O     1 
HETATM 3136 O O     . HOH H 6 .   ? 1.133  10.516 31.849 1.00 36.38 ? 723 HOH A O     1 
HETATM 3137 O O     . HOH H 6 .   ? 3.534  28.507 27.963 1.00 44.28 ? 724 HOH A O     1 
HETATM 3138 O O     . HOH H 6 .   ? 28.206 26.496 48.643 1.00 48.02 ? 725 HOH A O     1 
HETATM 3139 O O     . HOH H 6 .   ? 30.822 37.841 37.045 1.00 37.25 ? 726 HOH A O     1 
HETATM 3140 O O     . HOH H 6 .   ? 21.399 6.361  2.798  1.00 31.01 ? 727 HOH A O     1 
HETATM 3141 O O     . HOH H 6 .   ? 30.240 8.456  25.747 1.00 27.76 ? 728 HOH A O     1 
HETATM 3142 O O     . HOH H 6 .   ? 9.263  4.596  40.561 1.00 33.95 ? 729 HOH A O     1 
HETATM 3143 O O     . HOH H 6 .   ? 27.344 3.815  31.928 1.00 31.94 ? 730 HOH A O     1 
HETATM 3144 O O     . HOH H 6 .   ? 20.065 20.482 -2.645 1.00 47.83 ? 731 HOH A O     1 
HETATM 3145 O O     . HOH H 6 .   ? 21.265 0.828  37.277 1.00 36.09 ? 732 HOH A O     1 
HETATM 3146 O O     . HOH H 6 .   ? 13.323 41.506 25.586 1.00 39.83 ? 733 HOH A O     1 
HETATM 3147 O O     . HOH H 6 .   ? 15.902 31.215 44.696 1.00 27.18 ? 734 HOH A O     1 
HETATM 3148 O O     . HOH H 6 .   ? 1.215  26.358 16.556 1.00 34.36 ? 735 HOH A O     1 
HETATM 3149 O O     . HOH H 6 .   ? 28.063 -2.364 22.043 1.00 35.94 ? 736 HOH A O     1 
HETATM 3150 O O     . HOH H 6 .   ? 24.396 25.963 -3.239 1.00 31.50 ? 737 HOH A O     1 
HETATM 3151 O O     . HOH H 6 .   ? -0.077 12.131 20.686 1.00 45.94 ? 738 HOH A O     1 
HETATM 3152 O O     . HOH H 6 .   ? 35.823 35.635 3.266  1.00 33.00 ? 739 HOH A O     1 
HETATM 3153 O O     . HOH H 6 .   ? 30.020 -0.737 22.033 1.00 47.28 ? 740 HOH A O     1 
HETATM 3154 O O     . HOH H 6 .   ? 36.005 8.697  22.537 1.00 42.76 ? 741 HOH A O     1 
HETATM 3155 O O     . HOH H 6 .   ? 15.928 16.291 0.057  1.00 33.78 ? 742 HOH A O     1 
HETATM 3156 O O     . HOH H 6 .   ? 26.772 24.703 -1.671 1.00 31.53 ? 743 HOH A O     1 
HETATM 3157 O O     . HOH H 6 .   ? 28.606 36.510 3.812  1.00 43.38 ? 744 HOH A O     1 
HETATM 3158 O O     . HOH H 6 .   ? 0.187  16.105 19.370 1.00 42.39 ? 745 HOH A O     1 
HETATM 3159 O O     . HOH H 6 .   ? 31.445 24.742 2.839  1.00 24.66 ? 746 HOH A O     1 
HETATM 3160 O O     . HOH H 6 .   ? 4.719  5.218  39.492 1.00 40.48 ? 747 HOH A O     1 
HETATM 3161 O O     . HOH H 6 .   ? 34.220 8.519  20.269 1.00 36.18 ? 748 HOH A O     1 
HETATM 3162 O O     . HOH H 6 .   ? 20.817 41.884 12.484 1.00 25.74 ? 749 HOH A O     1 
HETATM 3163 O O     . HOH H 6 .   ? 1.863  35.696 18.458 1.00 35.51 ? 750 HOH A O     1 
HETATM 3164 O O     . HOH H 6 .   ? 29.814 27.883 35.339 1.00 37.71 ? 751 HOH A O     1 
HETATM 3165 O O     . HOH H 6 .   ? 3.737  34.393 11.134 1.00 40.25 ? 752 HOH A O     1 
HETATM 3166 O O     . HOH H 6 .   ? 23.239 10.265 40.211 1.00 35.20 ? 753 HOH A O     1 
HETATM 3167 O O     . HOH H 6 .   ? 0.878  7.478  12.707 1.00 52.12 ? 754 HOH A O     1 
HETATM 3168 O O     . HOH H 6 .   ? 10.375 5.438  8.164  1.00 44.40 ? 755 HOH A O     1 
HETATM 3169 O O     . HOH H 6 .   ? 19.331 2.021  35.508 1.00 34.96 ? 756 HOH A O     1 
HETATM 3170 O O     . HOH H 6 .   ? 43.297 21.950 10.325 1.00 28.15 ? 757 HOH A O     1 
HETATM 3171 O O     . HOH H 6 .   ? 6.380  6.509  28.605 1.00 36.90 ? 758 HOH A O     1 
HETATM 3172 O O     . HOH H 6 .   ? 29.711 -2.313 17.558 1.00 36.73 ? 759 HOH A O     1 
HETATM 3173 O O     . HOH H 6 .   ? 22.660 36.280 40.640 1.00 30.73 ? 760 HOH A O     1 
HETATM 3174 O O     . HOH H 6 .   ? 7.665  31.768 41.264 1.00 53.72 ? 761 HOH A O     1 
HETATM 3175 O O     . HOH H 6 .   ? 25.240 4.735  4.679  1.00 40.36 ? 762 HOH A O     1 
HETATM 3176 O O     . HOH H 6 .   ? 38.256 9.286  19.976 1.00 45.39 ? 763 HOH A O     1 
HETATM 3177 O O     . HOH H 6 .   ? 11.683 -4.213 16.736 1.00 40.47 ? 764 HOH A O     1 
HETATM 3178 O O     . HOH H 6 .   ? 30.513 15.498 31.594 1.00 42.52 ? 765 HOH A O     1 
HETATM 3179 O O     . HOH H 6 .   ? 4.008  7.417  22.935 1.00 34.05 ? 766 HOH A O     1 
HETATM 3180 O O     . HOH H 6 .   ? 17.577 36.032 6.022  1.00 33.39 ? 767 HOH A O     1 
HETATM 3181 O O     . HOH H 6 .   ? 32.300 33.367 26.347 1.00 39.51 ? 768 HOH A O     1 
HETATM 3182 O O     . HOH H 6 .   ? 35.840 26.221 23.733 1.00 35.11 ? 769 HOH A O     1 
HETATM 3183 O O     . HOH H 6 .   ? 25.771 -3.119 20.927 1.00 23.69 ? 770 HOH A O     1 
HETATM 3184 O O     . HOH H 6 .   ? 12.775 9.258  8.809  1.00 30.94 ? 771 HOH A O     1 
HETATM 3185 O O     . HOH H 6 .   ? 3.233  24.693 31.890 1.00 40.07 ? 772 HOH A O     1 
HETATM 3186 O O     . HOH H 6 .   ? 43.178 28.619 27.248 1.00 33.48 ? 773 HOH A O     1 
HETATM 3187 O O     . HOH H 6 .   ? 13.770 -2.073 20.391 1.00 37.82 ? 774 HOH A O     1 
HETATM 3188 O O     . HOH H 6 .   ? -1.062 16.754 17.232 1.00 40.03 ? 775 HOH A O     1 
HETATM 3189 O O     . HOH H 6 .   ? 44.066 34.349 21.858 1.00 42.10 ? 776 HOH A O     1 
HETATM 3190 O O     . HOH H 6 .   ? 17.106 -0.961 26.115 1.00 44.37 ? 777 HOH A O     1 
HETATM 3191 O O     . HOH H 6 .   ? 6.331  29.784 35.293 1.00 41.93 ? 778 HOH A O     1 
HETATM 3192 O O     . HOH H 6 .   ? 41.056 34.380 15.088 1.00 32.85 ? 779 HOH A O     1 
HETATM 3193 O O     . HOH H 6 .   ? 15.376 40.367 25.643 1.00 38.03 ? 780 HOH A O     1 
HETATM 3194 O O     . HOH H 6 .   ? 38.321 19.980 21.210 1.00 45.53 ? 781 HOH A O     1 
HETATM 3195 O O     . HOH H 6 .   ? 5.253  29.928 29.729 1.00 38.43 ? 782 HOH A O     1 
HETATM 3196 O O     . HOH H 6 .   ? 1.645  7.959  33.663 1.00 54.56 ? 783 HOH A O     1 
HETATM 3197 O O     . HOH H 6 .   ? 4.204  8.328  28.034 1.00 51.65 ? 784 HOH A O     1 
HETATM 3198 O O     . HOH H 6 .   ? 19.291 1.120  11.881 1.00 45.74 ? 785 HOH A O     1 
HETATM 3199 O O     . HOH H 6 .   ? 44.092 31.132 26.666 1.00 34.45 ? 786 HOH A O     1 
HETATM 3200 O O     . HOH H 6 .   ? 16.686 0.739  11.699 1.00 44.22 ? 787 HOH A O     1 
HETATM 3201 O O     . HOH H 6 .   ? 22.642 -2.496 34.346 1.00 28.92 ? 788 HOH A O     1 
HETATM 3202 O O     . HOH H 6 .   ? 15.991 33.444 -0.702 1.00 41.02 ? 789 HOH A O     1 
HETATM 3203 O O     . HOH H 6 .   ? 3.844  9.265  24.648 1.00 31.76 ? 790 HOH A O     1 
HETATM 3204 O O     . HOH H 6 .   ? 29.298 31.798 29.587 1.00 52.45 ? 791 HOH A O     1 
HETATM 3205 O O     . HOH H 6 .   ? 39.374 33.351 10.904 1.00 33.14 ? 792 HOH A O     1 
HETATM 3206 O O     . HOH H 6 .   ? 14.657 7.636  8.635  1.00 38.62 ? 793 HOH A O     1 
HETATM 3207 O O     . HOH H 6 .   ? 27.519 41.714 27.684 1.00 44.32 ? 794 HOH A O     1 
HETATM 3208 O O     . HOH H 6 .   ? 36.428 38.520 15.132 1.00 51.53 ? 795 HOH A O     1 
HETATM 3209 O O     . HOH H 6 .   ? 23.680 0.946  11.280 1.00 47.19 ? 796 HOH A O     1 
HETATM 3210 O O     . HOH H 6 .   ? 11.342 23.466 1.238  1.00 46.81 ? 797 HOH A O     1 
HETATM 3211 O O     . HOH H 6 .   ? 7.817  2.635  39.717 1.00 42.02 ? 798 HOH A O     1 
HETATM 3212 O O     . HOH H 6 .   ? 29.571 42.701 21.398 1.00 47.91 ? 799 HOH A O     1 
HETATM 3213 O O     . HOH H 6 .   ? 38.038 40.569 12.266 1.00 47.75 ? 800 HOH A O     1 
HETATM 3214 O O     . HOH H 6 .   ? 27.091 44.532 21.058 1.00 35.08 ? 801 HOH A O     1 
HETATM 3215 O O     . HOH H 6 .   ? 33.589 1.246  20.273 1.00 37.86 ? 802 HOH A O     1 
HETATM 3216 O O     . HOH H 6 .   ? 11.524 2.683  30.227 1.00 36.85 ? 803 HOH A O     1 
HETATM 3217 O O     . HOH H 6 .   ? 22.519 0.593  13.531 1.00 48.14 ? 804 HOH A O     1 
HETATM 3218 O O     . HOH H 6 .   ? 2.234  25.046 8.153  1.00 39.89 ? 805 HOH A O     1 
HETATM 3219 O O     . HOH H 6 .   ? 10.241 18.423 44.936 1.00 37.72 ? 806 HOH A O     1 
HETATM 3220 O O     . HOH H 6 .   ? 11.906 28.179 -0.139 1.00 47.18 ? 807 HOH A O     1 
HETATM 3221 O O     . HOH H 6 .   ? 40.782 26.988 22.013 1.00 34.29 ? 808 HOH A O     1 
HETATM 3222 O O     . HOH H 6 .   ? 15.560 5.902  10.142 1.00 41.68 ? 809 HOH A O     1 
HETATM 3223 O O     . HOH H 6 .   ? 9.176  0.244  35.888 1.00 29.40 ? 810 HOH A O     1 
HETATM 3224 O O     . HOH H 6 .   ? 27.851 9.599  25.066 1.00 27.12 ? 811 HOH A O     1 
HETATM 3225 O O     . HOH H 6 .   ? 18.176 16.213 45.289 1.00 43.06 ? 812 HOH A O     1 
HETATM 3226 O O     . HOH H 6 .   ? 33.672 6.561  18.561 1.00 43.09 ? 813 HOH A O     1 
HETATM 3227 O O     . HOH H 6 .   ? -1.293 24.935 17.414 1.00 50.17 ? 814 HOH A O     1 
HETATM 3228 O O     . HOH H 6 .   ? 9.932  33.544 43.174 1.00 45.67 ? 815 HOH A O     1 
HETATM 3229 O O     . HOH H 6 .   ? 5.031  33.718 8.568  1.00 44.02 ? 816 HOH A O     1 
HETATM 3230 O O     . HOH H 6 .   ? 23.502 28.395 45.218 1.00 27.21 ? 817 HOH A O     1 
HETATM 3231 O O     . HOH H 6 .   ? 6.239  21.524 5.433  1.00 44.96 ? 818 HOH A O     1 
HETATM 3232 O O     . HOH H 6 .   ? 24.762 42.538 9.870  1.00 47.60 ? 819 HOH A O     1 
HETATM 3233 O O     . HOH H 6 .   ? 16.944 37.728 7.895  1.00 33.33 ? 820 HOH A O     1 
HETATM 3234 O O     . HOH H 6 .   ? 44.578 30.051 22.638 1.00 32.26 ? 821 HOH A O     1 
HETATM 3235 O O     . HOH H 6 .   ? 3.905  30.252 24.548 1.00 40.66 ? 822 HOH A O     1 
HETATM 3236 O O     . HOH H 6 .   ? 13.823 32.961 40.969 1.00 35.68 ? 823 HOH A O     1 
HETATM 3237 O O     . HOH H 6 .   ? 14.495 31.458 -2.463 1.00 34.23 ? 824 HOH A O     1 
HETATM 3238 O O     . HOH H 6 .   ? 28.122 10.958 34.248 1.00 43.82 ? 825 HOH A O     1 
HETATM 3239 O O     . HOH H 6 .   ? 0.200  25.342 11.947 1.00 52.50 ? 826 HOH A O     1 
HETATM 3240 O O     . HOH H 6 .   ? 11.088 8.066  7.098  1.00 44.41 ? 827 HOH A O     1 
HETATM 3241 O O     . HOH H 6 .   ? 21.873 31.732 -2.718 1.00 48.62 ? 828 HOH A O     1 
HETATM 3242 O O     . HOH H 6 .   ? 29.111 41.680 25.352 1.00 46.44 ? 829 HOH A O     1 
HETATM 3243 O O     . HOH H 6 .   ? 31.045 7.948  28.195 1.00 34.90 ? 830 HOH A O     1 
HETATM 3244 O O     . HOH H 6 .   ? 18.571 33.797 -1.322 1.00 35.22 ? 831 HOH A O     1 
HETATM 3245 O O     . HOH H 6 .   ? 33.439 44.327 18.861 1.00 37.32 ? 832 HOH A O     1 
HETATM 3246 O O     . HOH H 6 .   ? 30.732 33.901 28.443 1.00 43.64 ? 833 HOH A O     1 
HETATM 3247 O O     . HOH H 6 .   ? 9.540  36.354 4.058  1.00 39.76 ? 834 HOH A O     1 
HETATM 3248 O O     . HOH H 6 .   ? 14.731 47.136 19.005 1.00 42.30 ? 835 HOH A O     1 
HETATM 3249 O O     . HOH H 6 .   ? 41.784 19.631 9.654  1.00 32.27 ? 836 HOH A O     1 
HETATM 3250 O O     . HOH H 6 .   ? 11.649 31.208 44.694 1.00 46.05 ? 837 HOH A O     1 
HETATM 3251 O O     . HOH H 6 .   ? 34.702 36.962 27.700 1.00 50.87 ? 838 HOH A O     1 
HETATM 3252 O O     . HOH H 6 .   ? 19.805 36.975 4.450  1.00 43.66 ? 839 HOH A O     1 
HETATM 3253 O O     . HOH H 6 .   ? 29.805 36.592 26.973 1.00 34.30 ? 840 HOH A O     1 
HETATM 3254 O O     . HOH H 6 .   ? 22.399 43.393 11.047 1.00 42.56 ? 841 HOH A O     1 
HETATM 3255 O O     . HOH H 6 .   ? 27.438 30.297 29.992 1.00 40.96 ? 842 HOH A O     1 
HETATM 3256 O O     . HOH H 6 .   ? 7.526  39.397 6.927  1.00 48.65 ? 843 HOH A O     1 
HETATM 3257 O O     . HOH H 6 .   ? 19.016 32.736 44.340 1.00 38.46 ? 844 HOH A O     1 
HETATM 3258 O O     . HOH H 6 .   ? 17.145 1.455  37.158 1.00 33.79 ? 845 HOH A O     1 
HETATM 3259 O O     . HOH H 6 .   ? 32.547 41.986 20.145 1.00 35.11 ? 846 HOH A O     1 
HETATM 3260 O O     . HOH H 6 .   ? 34.643 35.851 1.018  1.00 45.44 ? 847 HOH A O     1 
HETATM 3261 O O     . HOH H 6 .   ? 32.541 25.856 24.924 1.00 43.55 ? 848 HOH A O     1 
HETATM 3262 O O     . HOH H 6 .   ? 8.499  36.552 25.706 1.00 44.79 ? 849 HOH A O     1 
HETATM 3263 O O     . HOH H 6 .   ? 5.524  35.561 6.829  1.00 47.00 ? 850 HOH A O     1 
HETATM 3264 O O     . HOH H 6 .   ? 1.682  10.905 25.128 1.00 33.38 ? 851 HOH A O     1 
HETATM 3265 O O     . HOH H 6 .   ? 15.149 35.527 0.382  1.00 37.95 ? 852 HOH A O     1 
HETATM 3266 O O     . HOH H 6 .   ? 13.087 0.755  39.565 1.00 40.67 ? 853 HOH A O     1 
HETATM 3267 O O     . HOH H 6 .   ? 17.924 39.192 28.666 1.00 24.47 ? 854 HOH A O     1 
HETATM 3268 O O     . HOH H 6 .   ? 32.371 -1.017 20.761 1.00 50.67 ? 855 HOH A O     1 
HETATM 3269 O O     . HOH H 6 .   ? 18.680 41.007 5.580  1.00 43.70 ? 856 HOH A O     1 
HETATM 3270 O O     . HOH H 6 .   ? 1.454  21.928 9.774  1.00 38.02 ? 857 HOH A O     1 
HETATM 3271 O O     . HOH H 6 .   ? 16.518 39.969 6.381  1.00 46.09 ? 858 HOH A O     1 
HETATM 3272 O O     . HOH H 6 .   ? 35.994 44.715 15.575 1.00 40.05 ? 859 HOH A O     1 
HETATM 3273 O O     . HOH H 6 .   ? 25.837 44.907 10.177 1.00 37.78 ? 860 HOH A O     1 
HETATM 3274 O O     . HOH H 6 .   ? 28.036 44.802 8.413  1.00 44.23 ? 861 HOH A O     1 
# 
